pmid	termid	comment
PMID:10022828	GO:0110085	establishment, but not maintenance, of ring localization requires F-actin (assayed using latrunculin A)
PMID:10022828	GO:0110085	establishment, but not maintenance, of ring localization requires F-actin (assayed using latrunculin A)
PMID:10022921	FYPO:0003775	(comment: assayed using Tf1 transposon plasmid construct)
PMID:10022921	FYPO:0003773	(comment: assayed using Tf1 transposon Gag and IN)
PMID:10022921	FYPO:0003772	(comment: assayed using Tf1 transposon)
PMID:10022921	FYPO:0003774	(comment: assayed using Tf1 transposon)
PMID:10022921	FYPO:0000593	(comment: assayed using Tf1 transposon plasmid construct)
PMID:10087262	PBO:0093772	data not shown
PMID:10087262	FYPO:0002061	mok1-664􏰌pck2 was synthetically lethal at 30􏰊C, a temperature at which either single mutant could grew (Fig. 10b)
PMID:10087262	FYPO:0002060	Synthetic lethality was not observed between mok1- 664 and 􏰌pck1, consistent with our previous result showing that pck2􏰇 plays the major role (Toda et al., 1993)
PMID:10087262	FYPO:0007293	mok1-664􏰌pck2 was synthetically lethal at 30􏰊C, a temperature at which either single mutant could grew (Fig. 10b)
PMID:10087262	PBO:0099872	(Fig. 1c)
PMID:10087262	GO:0016020	These results suggested that Mok1 is an stable integral membrane protein, which is consistent with the presence of several transmembrane domains (Fig. 2 a).
PMID:10087262	PBO:0105980	more than threefold over compared with wild-type cells (344%)
PMID:10087262	PBO:0105979	translocation of actin from one end t the other (also fig7)
PMID:10087262	PBO:0105978	The other was observed as pairs of divided cells associated side-by-side (12%), the cell wall of which appeared fragile and often lysed upon division.
PMID:10087262	GO:0032178	combined localization and membrane fraction
PMID:10087262	GO:0031520	combined localization and membrane fraction
PMID:10087262	FYPO:0002060	pck2delta rescues ags1 ox defect, we cant do this genetic interaction type in new interface
PMID:10087262	FYPO:0006802	(Fig. 1a) 'delocalized actin'
PMID:10091325	GO:0004371	(comment: activated_by CHEBI:29108 | activated_by CHEBI:18420 | inhibited_by CHEBI:16761)
PMID:10207075	FYPO:0003606	In contrast to the point mutation, the rec8::ura4 strain showed no shortening of prophase in three independent time courses (data not shown). Shortening of the prophase in the point mutation strain may indicate a role of Rec8p in meiosis regulation. Alternative explanations, like shortening of prophase by an additional mutation, were not excluded.
PMID:10226032	PBO:0098010	(comment: mcs6 requires mcs2 for CTD kinase activity but not cyclin-dependent kinase activating kinase activity. mcs2 does not cycle throughout the cell cycle.)
PMID:10226032	PBO:0098011	(comment: Csk1 activated both the monomeric and the Mcs2-bound forms of Mcs6)
PMID:10226032	PBO:0098012	Surprisingly, Csk1 also activated Cdc2 in complexes with either Cdc13 or Cig2 cyclins.
PMID:10364209	FYPO:0001357	DNS
PMID:10364209	MOD:00046	(Fig. 1B)
PMID:10364209	MOD:00046	(Fig. 1B)
PMID:10364209	FYPO:0001357	DNS
PMID:10364209	PBO:0096439	The same level of Myo2p co-immunoprecipitated with mutant Cdc4p as with wild-type Cdc4p (Fig. 5A).
PMID:10366596	FYPO:0004086	(comment: in zygotic nucleus)
PMID:10381387	PBO:0094917	(comment: it doesn't say old, but it is...)
PMID:10381387	PBO:0094917	(comment: it doesn't say old, but it is...)
PMID:10388806	PBO:0026408	(comment: Val: moved down from FYPO:0001429, its a fully penetrant inviable phenotype (anucleate))
PMID:10388806	FYPO:0001430	(comment: CHECK cdc18delta::p[nmt*.cdc18+-LEU2])
PMID:10388806	FYPO:0001428	(comment: CHECK cdc18delta::p[nmt*.cdc18+-LEU2])
PMID:10392445	FYPO:0000474	conditions under which pat1-114 alone induces meiosis & sporulation
PMID:10398679	GO:0038066	(comment: CHECK is response to heat/response to denatured protein)
PMID:10398680	FYPO:0006174	(Figure 3)
PMID:10398680	FYPO:0003788	(Fig. 1a)
PMID:10398680	FYPO:0003241	(Figure 1F,7B) (comment: All of these required passage through G1 - i.e. second mitosis)
PMID:10398680	FYPO:0006190	(Figure 1A,B) (comment: All of these required passage through G1 - i.e. second mitosis)
PMID:10398680	FYPO:0002060	(Figure 8a)
PMID:10398680	FYPO:0002061	(Figure 8a)
PMID:10398680	FYPO:0002061	(Figure 8a)
PMID:10398680	FYPO:0007914	suggesting that sister centromeres were separated in the metaphase-arrested cells.
PMID:10398680	PBO:0103286	(Figure 6) Conversely, the mis6-302 strain integrated with the Mis12-HA gene was used.
PMID:10398680	PBO:0103285	(Figure 6) Hence, mis6-HA could interact with the centromere in the absence of functional Mis12.
PMID:10398680	FYPO:0007914	(Figure 3) (comment: before phase 3 extension)
PMID:10398680	FYPO:0006190	(Figure 2)
PMID:10398680	FYPO:0006715	(Figure 1A,B) (comment: All of these required passage through G1 - i.e. second mitosis)
PMID:10398680	FYPO:0004308	(Fig. 6D): Mis12 is thus required for maintaining the inner centromere structure.
PMID:10398680	GO:0000939	These results showed that Mis12 was localized at centromeres throughout the cell cycle
PMID:10398680	FYPO:0001042	(Figure 4)
PMID:10398680	FYPO:0007304	(Figure 3)
PMID:10428959	PBO:0096484	(comment: vw: sty1-atf1 pathway)
PMID:10428959	FYPO:0002060	DNS
PMID:10428959	PBO:0096482	(Figure 3) (comemnt: vw severity 23.4 micron)
PMID:10428959	PBO:0096482	(Figure 3) (comemnt: vw: severity 20.2 micron)
PMID:10428959	GO:0010971	(Figure 3)
PMID:10428959	GO:0010971	(Figure 3)
PMID:10428959	GO:0031139	(Table 2)
PMID:10428959	FYPO:0001214	(Figure 3b)
PMID:10428959	PBO:0096487	(Figure 5)
PMID:10428959	FYPO:0004481	(Figure 3b)
PMID:10428959	PBO:0096485	(comment: vw: sty1-atf1 pathway)
PMID:10428959	PBO:0096486	(Figure 5)
PMID:10428959	PBO:0022884	(Figure 2C) (comemnt: vw: not by sty1)
PMID:10428959	GO:0005515	(Figure 1,2)
PMID:10428959	PBO:0096488	(Figure 6)
PMID:10428959	PBO:0096489	(Figure 6B)
PMID:10428959	PBO:0096490	(Figure 7)
PMID:10428959	PBO:0096491	(Figure 7)
PMID:10428959	PBO:0096492	(Figure 7)
PMID:10428959	GO:0005515	(Figure 1,2)
PMID:10428959	GO:0038066	(Table 2)
PMID:10430583	PBO:0093619	(comment: same as rad51delta alone)
PMID:10430583	PBO:0093619	(comment: same as rad51delta alone)
PMID:10459013	GO:0044732	(comment: present throughout mitotic cell cycle)
PMID:10462529	FYPO:0006822	(Fig. 7)
PMID:10462529	FYPO:0000951	(Fig. 7)
PMID:10462529	FYPO:0002085	(Fig. 5)
PMID:10462529	FYPO:0006038	(Figure 4a)
PMID:10462529	FYPO:0002085	(Fig. 3)
PMID:10462529	FYPO:0002061	(Fig. 3)
PMID:10462529	FYPO:0002061	(Fig. 2)
PMID:10462529	GO:0002183	(Fig. 2)
PMID:10462529	FYPO:0006037	(Fig. 1)
PMID:10462529	PBO:0094621	(comment: CHECK extension, of cdc25) Figure 7b
PMID:10462529	FYPO:0006036	(Fig. 1)
PMID:10462529	FYPO:0001122	(Fig. 6)
PMID:10462529	PBO:0101461	(Fig. 6)
PMID:10462529	FYPO:0003503	(Fig. 5)
PMID:10462529	FYPO:0003503	(Fig. 5)
PMID:10462529	PBO:0101462	(Fig. 5)
PMID:10462529	FYPO:0001490	(Fig. 2)
PMID:10462529	FYPO:0002061	(Fig. 2)
PMID:10462529	FYPO:0006038	(Fig. 3)
PMID:10462529	PBO:0101463	(Fig. 6)
PMID:10473641	FYPO:0004539	(comment: CHECK broken)
PMID:10521402	PBO:0096558	(Fig. 6C)
PMID:10521402	PBO:0096550	(Fig. 1A) rad1 is required for meiotic DNA replication checkpoint
PMID:10521402	FYPO:0006763	(Fig. 1B) cds1 is required for meiotic DNA replication checkpoint
PMID:10521402	PBO:0096551	(Fig. 1B)
PMID:10521402	PBO:0096551	(Fig. 1B)
PMID:10521402	PBO:0096550	(Fig. 1B) (comment: CHECK double cds1delta chk1 delta has same phenotype as single cds1delta/cds1 delta)
PMID:10521402	PBO:0096552	(Fig. 2A, 2B)
PMID:10521402	PBO:0096552	(Fig. 2A, 2B)
PMID:10521402	PBO:0096552	Data not shown. kinetics same as pat1ts rad1delta diploid
PMID:10521402	PBO:0096552	Data not shown. kinetics same as pat1ts rad1delta diploid
PMID:10521402	PBO:0096552	Data not shown. kinetics same as pat1ts rad1delta diploid
PMID:10521402	PBO:0096553	Data not shown prophase arrest with horsetail nuclear morphology see fig3A for pat1ts control
PMID:10521402	PBO:0096553	Data not shown prophase arrest with horsetail nuclear morphology see fig3A for pat1ts control
PMID:10521402	PBO:0021428	(Fig. 3B) data not shown
PMID:10521402	PBO:0021428	(Fig. 3B) data not shown
PMID:10521402	FYPO:0000734	(Fig. 3B)
PMID:10521402	FYPO:0004929	(Fig. 3B)
PMID:10521402	FYPO:0001733	(Fig. 3B)
PMID:10521402	GO:0072441	(Fig. 4)
PMID:10521402	PBO:0096554	(Fig. 4) (comment: CHECK present during meiotic DNA replication checkpoint arrest)
PMID:10521402	PBO:0096555	(Fig. 5A) (comment: see control in Fig4A)
PMID:10521402	PBO:0096556	(Fig. 5B) (comment: see Fig4B for control)
PMID:10521402	PBO:0096555	(Fig. 5A) (comment: see control in Fig4A)
PMID:10521402	PBO:0096557	(Fig. 5A) (comment: see Fig4A for control)
PMID:10521402	PBO:0096557	(Fig. 5A) (comment: see Fig4A for control)
PMID:10521402	PBO:0096550	Data not shown when rad1 is deleted checkpoint is not activated and cells attempt meiotic nuclear divisions see also Fig1, 2, 3B
PMID:10521402	PBO:0096559	(Fig. 6A, 6D) meiotic cells unable to inhibit CDK1 activity in response to activation of the meiotic DNA replication checkpoint, arrest at metaphase of Meiosis I and do not undergo nuclear division
PMID:10523629	PBO:0095532	(Figure 1a)
PMID:10523629	PBO:0100796	(Figure 1a)
PMID:10523629	PBO:0095532	(Figure 1a)
PMID:10523629	PBO:0100796	(Figure 1a)
PMID:10523629	PBO:0095532	(Figure 1a)
PMID:10523629	PBO:0095532	(Figure 1a)
PMID:10523629	PBO:0095532	(Figure 1a)
PMID:10523629	PBO:0095532	(Figure 1a)
PMID:10523629	PBO:0100796	(Figure 1a)
PMID:10523629	PBO:0095532	(Figure 1a)
PMID:10523629	PBO:0100798	(Fig. 2a)
PMID:10523629	PBO:0100796	(Figure 1a)
PMID:10523629	PBO:0094734	(Fig. 2a)
PMID:10523629	PBO:0095532	(Figure 1a)
PMID:10523629	PBO:0095532	(Figure 1a)
PMID:10523629	PBO:0038186	(Fig. 4)
PMID:10523629	PBO:0100799	(Fig. 3C)
PMID:10523629	PBO:0093616	(Fig. 4)
PMID:10523629	PBO:0100803	(Fig. 5G)
PMID:10523629	PBO:0100802	(Fig. 5C)
PMID:10523629	PBO:0100801	(Fig. 5J)
PMID:10523629	PBO:0095532	(Figure 1a)
PMID:10526233	FYPO:0003166	(comment: (it basically the same as cut except the nucleus is not bisected))
PMID:10526233	FYPO:0003166	(comment: (it basically the same as cut except the nucleus is not bisected))
PMID:10545452	PBO:0094637	Microtubule staining confirmed that the drc1-191 cells were arrested in interphase since cells blocked predominantly either with interphase arrays of microtubules or with a postanaphase array of microtubules (Figure 3A, 4 hr).
PMID:10545452	FYPO:0001368	(comment: i.e next round of replication)
PMID:10545452	FYPO:0004629	(comment: i.e next round of replication)
PMID:10545452	FYPO:0001234	The drc1-191 rng2-D5 and drc1-191 cdc4-8 double mutants grew extremely poorly a
PMID:10545452	FYPO:0002060	The drc1-191 mutation was found to be recessive, since cells of the genotype drc1Δ/drc1- 191 resembled wild-type cells and were capable of colony formation under conditions in which the drc1-191 mutant was unable to form colonies (data not shown).
PMID:10545452	FYPO:0002061	The drc1-191 mutation was found to be recessive, since cells of the genotype drc1Δ/drc1- 191 resembled wild-type cells and were capable of colony formation under conditions in which the drc1-191 mutant was unable to form colonies (data not shown).
PMID:10545452	FYPO:0003931	(Figure 1, 4) hr
PMID:10545452	FYPO:0001006	(Figure 1, 8) hr
PMID:10545452	FYPO:0002061	The drc1-191 myo2-E1 double mutant was unable to form colonies at 24􏰌, a temperature at which both parental strains were capable of colony formation (data not shown).
PMID:10545452	FYPO:0003710	(Figure 1, 0) hr
PMID:10545452	FYPO:0001495	The drc1-191 rng2-D5 and drc1-191 cdc4-8 double mutants grew extremely poorly and showed cytokinesis defects at 24􏰌, a temperature at which rng2-D5 and cdc4-8 single mutants grew healthily and resembled wild-type cells in morphology (Figure 7).
PMID:10545452	PBO:0094638	Upon prolonged incubation at the restrictive temperature (Figure 2, 8 hr), cells assumed a variety of shapes and 􏰍20% of cells were found to contain four nuclei with actomyosin rings, whereas the rest of the cells (80%) still contained only two interphase nuclei and detectable
PMID:10545452	FYPO:0002061	The drc1-191 myo2-E1 double mutant was unable to form colonies at 24􏰌, a temperature at which both parental strains were capable of colony formation (data not shown).
PMID:10545452	PBO:0094639	Upon prolonged incubation at the restrictive temperature (Figure 2, 8 hr), cells assumed a variety of shapes and 􏰍20% of cells were found to contain four nuclei with actomyosin rings, whereas the rest of the cells (80%) still contained only two interphase nuclei and detectable
PMID:10545452	PBO:0094640	Upon prolonged incubation at the restrictive temperature (Figure 2, 8 hr), cells assumed a variety of shapes and 􏰍20% of cells were found to contain four nuclei with actomyosin rings, whereas the rest of the cells (80%) still contained only two interphase nuclei and detectable
PMID:10545452	FYPO:0007541	The drc1-191 rng2-D5 and drc1-191 cdc4-8 double mutants grew extremely poorly and showed cytokinesis defects at 24􏰌, a temperature at which rng2-D5 and cdc4-8 single mutants grew healthily and resembled wild-type cells in morphology (Figure 7). In both double mutant combinations (drc1-191 cdc4-8 and drc1-191 rng2- D5) highly elongated cells with multiple nuclei were seen frequently.
PMID:10545452	PBO:0094641	Upon prolonged incubation at the restrictive temperature (Figure 2, 8 hr), cells assumed a variety of shapes and 􏰍20% of cells were found to contain four nuclei with actomyosin rings, whereas the rest of the cells (80%) still contained only two interphase nuclei and detectable
PMID:10545452	FYPO:0000026	capable of germination and establishing polarized growth, but were incapable of performing cytokinesis and did not maintain polarity (Figure 6B).
PMID:10545452	FYPO:0000579	capable of germination and establishing polarized growth, but were incapable of performing cytokinesis and did not maintain polarity (Figure 6B).
PMID:10545452	PBO:0109007	At the drc1-191 arrest point all binucleate cells were found to have Cdc7p staining localized at one SPB. Merged images of chromosomal staining with DAPI and Cdc7p staining with HA antibodies is shown in Figure 4. The drc1-191 mutant, therefore, arrests at a point in the cell cycle where the septum-promoting Cdc7p is located on one SPB.
PMID:10545452	FYPO:0000272	capable of germination and establishing polarized growth, but were incapable of performing cytokinesis and did not maintain polarity (Figure 6B).
PMID:10545452	FYPO:0004691	Germinated drc1::ura4 spores were capable of polarity establishment (shown with arrows in Figure 6C), but appeared to be incapable of polarity maintenance, causing them to become spherical and highly enlarged (Figure 6C).
PMID:10545452	PBO:0109008	Interestingly, unlike the drc1-191 mutant, drc1::ura4 underwent multiple nuclear division cycles causing arrested cells to accumulate up to 32 nuclei.
PMID:10545452	FYPO:0001234	The drc1-191 rng2-D5 and drc1-191 cdc4-8 double mutants grew extremely poorly a
PMID:10547441	FYPO:0003889	(comment: CHECK this should be decreased thickness at old end during veg growth)
PMID:10567589	FYPO:0001122	The profile of pmt3􏰗 cells showed a decrease of the number of cells with 2C DNA content and an increase in the number of cells with a DNA content greater or less than 2C DNA content (at times 􏰔2 and 0 h in Fig. 3C)
PMID:10567589	FYPO:0001929	(Fig. 3c)
PMID:10567589	PBO:0093769	(Fig. 2d)
PMID:10567589	PBO:0096816	(Fig. 2d)
PMID:10567589	FYPO:0003241	The profile of pmt3􏰗 cells showed a decrease of the number of cells with 2C DNA content and an increase in the number of cells with a DNA content greater or less than 2C DNA content (at times 􏰔2 and 0 h in Fig. 3C)
PMID:10574765	PBO:0096824	(Figure 3) (comment: normal at non-growing end)
PMID:10574765	PBO:0096820	(Figure 4) (comment: Ral3/cor-CGFP fusion is expressed from pMral3/cor-C)
PMID:10574765	PBO:0109946	"(comment: vw: jacky suggested ""protein localisation to the lateral plasma membrane"" but will keep as parent Figures 1, S1 and S2. Cor-C GFP is probably episomal but it is not clear)"
PMID:10574765	PBO:0096817	(Figure 2b) (comment: Boundary of non growing cell end maintained)
PMID:10574765	PBO:0096818	(Figure 2c) (comment: Boundary of the non growing cell end not maintained)
PMID:10574765	PBO:0096819	(Figure 3) (comment: F actin is absent from non growing end)
PMID:10574765	PBO:0096822	(Figure 4) (comment: Ral3/cor-CGFP fusion is expressed from pMral3/cor-C)
PMID:10574765	PBO:0096824	(Figure 3) (comment: normal at non-growing end)
PMID:10574765	PBO:0096817	(Figure 2a) (comment: Boundary of non growing cell end maintained)
PMID:10574765	PBO:0096821	(Figure 4) (comment: Ral3/cor-CGFP fusion is expressed from pMral3/cor-C)
PMID:10581266	FYPO:0002061	(Fig. 9) (comment: high overexpression is lethal)
PMID:10581266	FYPO:0001493	(Fig. 9)
PMID:10581266	FYPO:0002177	(Fig. 6)
PMID:10581266	FYPO:0002025	(Fig. 6)
PMID:10581266	FYPO:0003439	(Fig. 4)
PMID:10581266	FYPO:0002729	(Fig. 6)
PMID:10588638	FYPO:0004372	inferred from Chk1 phosphorylation phenotypes
PMID:10588653	FYPO:0001357	DNS
PMID:10588653	PBO:0097633	(Figure 8) The most striking difference between wild-type Arp2p and Arp2-E316K was the failure to coimmunoprecipitate labeled Arp3p with Arp2-E316K
PMID:10588653	FYPO:0001324	(Figure 8B & C) These results clearly establish that the mutant Arp2-E316K protein turns over more rapidly than wild-type Arp2 protein
PMID:10588653	PBO:0097632	(Figure 8A). Arp2-E316K mutant protein had a reduced affinity for ATP compared with wild type Arp2p
PMID:10588653	PBO:0097632	(Figure 8A). T12A protein was also labeled by the ATP analogue, but to a much lesser degree than wild-type Arp2p
PMID:10588653	GO:0005524	(Fig. 8A) After UV irradiation, we found that both wild-type Arp2p and Arp3p were labeled by 8-azido-[a-32P]ATP, indicating that these actin-related proteins bind ATP as predicted
PMID:10588653	GO:0005524	(Fig. 8A) After UV irradiation, we found that both wild-type Arp2p and Arp3p were labeled by 8-azido-[a-32P]ATP, indicating that these actin-related proteins bind ATP as predicted
PMID:10588653	PBO:0097631	(Figure 6D)
PMID:10588653	PBO:0097630	(Figure 6)
PMID:10588653	GO:0005885	(Fig 6)
PMID:10588653	GO:0005885	(Fig 6)
PMID:10588653	FYPO:0001324	suggesting that the mutant protein is likely less stable than the wild-type Arp2 protein (Figure 6B), a hypothesis confirmed below (see Figure 8C).
PMID:10588653	GO:0005885	(Fig 6)
PMID:10588653	GO:0005885	(Fig 6)
PMID:10588653	GO:0005885	(Fig 6)
PMID:10588653	FYPO:0006116	In arp2-1 mutant cells grown at the restrictive temperature, the protein was not detected in patches. Rather, it appeared to be diffusely distributed throughout the cytoplasm (Figure 4C).
PMID:10588653	PBO:0097629	(Figure 4)
PMID:10588653	PBO:0018339	(Figure 4)
PMID:10588653	GO:0030479	(Figure 4)
PMID:10588653	FYPO:0002060	(Fig 3) (comment: CHECK synthetic rescue of cdc3)
PMID:10588653	FYPO:0002061	(Fig 3)
PMID:10588653	FYPO:0002061	(Fig 3)
PMID:10588653	FYPO:0002061	(DNS) In all tetrads, the viable colonies were Arp21 Ura2, indicating that arp21 is an essential gene
PMID:10588653	PBO:0095676	(Figure 1C)
PMID:10588653	PBO:0035605	(Figure 1) after 8 hours, medial region of the cells continued to accumulate excess cell wall material
PMID:10588653	FYPO:0000650	(Figure 1)
PMID:10588653	PBO:0035615	DNS
PMID:10588653	FYPO:0001367	DNS
PMID:10591634	PBO:0101467	(comment: IPI and IMP evidence)
PMID:10593886	GO:0004674	(comment: CHECK only in vitro data evidence)
PMID:10641037	FYPO:0007915	Because the same distribution pattern was observed when nmt-GFP-13g6 was expressedin the klp3 null allele (Figure 3B), we conclude that ER distribution is not affected by the disruption of klp3 in Fission yeast.
PMID:10641037	FYPO:0002060	DNS
PMID:10641037	FYPO:0002060	(Figure 2)
PMID:10641037	FYPO:0007912	(Figure 3b)
PMID:10651902	PBO:0099872	(Fig. 6)
PMID:10651902	GO:0005515	(comment: Rho1 GTP bound form) (comment: pck2 HR1 domain)
PMID:10651902	PBO:0105063	(comment: Rho1 appears to have a dual role in stabilizing and localizing Pck proteins)
PMID:10651902	PBO:0019176	(Fig. 6)
PMID:10683155	GO:0000785	constant level throughout cell cycle
PMID:10683155	FYPO:0000229	cut if exposed to radiation during S phase, but not if exposed during G2
PMID:10698951	FYPO:0002061	(comment: temperature restrictive for cdc27-P11 alone)
PMID:10698951	FYPO:0002060	(comment: temperature restrictive for cdc27-P11 alone)
PMID:10712506	PBO:0104977	from materials and methods
PMID:10712506	PBO:0095855	from materials and methods
PMID:10712506	FYPO:0001719	from materials and methods
PMID:10712506	PBO:0104977	from materials and methods
PMID:10718196	FYPO:0000337	DNS
PMID:10725227	PBO:0107277	(Fig. 1B) (comment: there is a small G1 peak which get slightly bigger but they also cells arrested in G1 by -N, when refed and shifted to the restrictive temp cannot enter S phase but this is data not shown)
PMID:10725227	PBO:0107289	(Fig. 9)
PMID:10725227	PBO:0107288	(Fig. 10B)
PMID:10725227	PBO:0107287	(Fig. 10A)
PMID:10725227	PBO:0107286	(Fig. 9)
PMID:10725227	FYPO:0001355	(Fig. 7 B) (comment: over expression of cig2+ cDNAI partially suppresses the rescue of cdc21-M68 by ded1-1D5)
PMID:10725227	PBO:0097954	(Fig. 1B)
PMID:10725227	PBO:0097954	(Fig. 1B) (comment: G1)
PMID:10725227	FYPO:0002060	(Table 2)
PMID:10725227	FYPO:0002060	(Table 2)
PMID:10725227	FYPO:0002060	(Table 2)
PMID:10725227	FYPO:0002060	(Fig. 2B)
PMID:10725227	FYPO:0002060	(Fig. 2B)
PMID:10725227	FYPO:0002060	(Fig. 2B)
PMID:10725227	FYPO:0002061	(Fig. 2C)
PMID:10725227	FYPO:0002061	(Fig. 2C)
PMID:10725227	FYPO:0002060	(Fig. 2B)
PMID:10725227	FYPO:0002060	(Fig. 2D) (comment: the semi permissive temperature 34.5C for ded1-D5 allows it to suppress cdc19-P1)
PMID:10725227	PBO:0107278	(Fig. 3A)
PMID:10725227	PBO:0107279	(Fig. 3A)
PMID:10725227	PBO:0107278	(Fig. 3B)
PMID:10725227	PBO:0107279	(Fig. 3B)
PMID:10725227	GO:0005737	(Fig. 4B)
PMID:10725227	PBO:0107280	(Fig. 5A) (comment: 35S)
PMID:10725227	PBO:0105174	(Fig. 5B) (comment: 35S)
PMID:10725227	PBO:0107281	(Fig. 5B) (comment: 35S)
PMID:10725227	PBO:0107282	(Fig. 6) (comment: total protein translation not affected)
PMID:10725227	PBO:0107283	(Fig. 6) (comment: total protein translation not affected)
PMID:10725227	PBO:0107284	(Fig. 7C, D) (comment: The protein and mRNA levels are compared to cDNA-I which is also expressed from medium strength nmt1 promoter ON)
PMID:10725227	FYPO:0002061	(Fig. 7B)
PMID:10725227	FYPO:0002061	(Fig. 7 B) (comment: over expression of cig2+ cDNAII suppresses the rescue of cdc21-M68 by ded1-1D5)
PMID:10733588	FYPO:0001840	Table2
PMID:10733588	FYPO:0001840	Table2
PMID:10733588	FYPO:0001420	(Fig. 3D) and data not shown
PMID:10748059	GO:0044750	(comment: CHECK inhibited_by(CHEBI:48828))
PMID:10749926	PBO:0106370	(Fig. 6)
PMID:10749926	FYPO:0000229	(Figure 4) (comment: spindle is still present, normally disassembled by cytokinesis)
PMID:10749926	FYPO:0002061	(Figure 1B)
PMID:10749926	FYPO:0000228	(Figure 4)
PMID:10749926	FYPO:0000620	(Figure 1B)
PMID:10749926	PBO:0106371	(Fig. 6)
PMID:10757807	PBO:0093580	(comment: same as cdc27-P11 alone)
PMID:10757807	PBO:0093580	(comment: same as rqh1delta alone)
PMID:10757807	PBO:0093580	(comment: same as cds1delta alone)
PMID:10766248	PBO:0095955	((comment: severity correlates positively with overexpression level)
PMID:10766248	PBO:0095955	(comment: cdc18+ low level overexpression)
PMID:10766248	PBO:0095955	(comment: severity correlates positively with overexpression level, and different isolates with same construct integrated show different Cdc18 level)
PMID:10769212	FYPO:0002061	inviable at 37 degrees; some growth at 34 degrees
PMID:10769212	FYPO:0002060	(comment: temperature restrictive for cdc4-8 alone)
PMID:10769212	GO:0110085	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:10769212	PBO:0094469	(comment: temperature restrictive for cdc4-8 alone)
PMID:10769212	FYPO:0003389	(comment: temperature restrictive for cdc4-8 alone)
PMID:10769212	FYPO:0004652	(comment: temperature restrictive for cdc4-8 alone)
PMID:10769212	FYPO:0002061	inviable at 34 or 37 degrees
PMID:10769212	FYPO:0002061	inviable at 37 degrees; some growth at 34 degrees
PMID:10769212	PBO:0023726	(comment: early mitosis; independent of F-actin (assayed using Latrunculin A))
PMID:10770926	GO:0003697	(comment: CHECK activated by ATP)
PMID:10770926	GO:0003697	(comment: CHECK activated by ATP)
PMID:10770926	GO:0003697	(comment: CHECK activated by ATP)
PMID:10775265	PBO:0095730	(Figure 4; Table I)
PMID:10775265	PBO:0095730	(Figure 4; Table I)
PMID:10775265	PBO:0097839	(Figure 4; Table I)
PMID:10775265	PBO:0095730	GFP±Sid1p signal was not observed at SPBs in these cells although faint nuclear signal was observed (Figure 7A). This suggests that some aspect of completion of mitosis is required in order for Sid1p to localize.
PMID:10775265	PBO:0097843	Afterashifttorestrictivetemperaturefor50min to inactivate Cdc2p, cells could now be observed that were septating without undergoing anaphase (Figure 7E and F, see arrows). At this point, 96% (68/71) of cells displaying Sid1p signal at the SPB were septating without having undergone anaphase (Figure 7E and F, see arrows
PMID:10775265	PBO:0095730	(Figure 4; Table I)
PMID:10775265	PBO:0095730	(Figure 4; Table I)
PMID:10775265	PBO:0097835	(Fig. 3c)
PMID:10775265	PBO:0097836	(Fig. 3d)
PMID:10775265	PBO:0097839	(Figure 4; Table I)
PMID:10775265	PBO:0097839	(Figure 4; Table I)
PMID:10775265	PBO:0095730	(Figure 4; Table I)
PMID:10775265	PBO:0095730	(Figure 4; Table I)
PMID:10775265	PBO:0097834	I inferred new because it's asymmetric and we know sin is new
PMID:10775265	PBO:0095731	Cdc7p cannot localize to the SPB(s) in cdc11 (Figure 4; Table I)
PMID:10775265	FYPO:0005055	After shift to restrictive temperature, cdc16-116 cells display two phenotypes termed type I and type II cells (Minet et al., 1979; Cerutti and Simanis, 1999). Type I cells have two nuclei and make multiple septa. Type II cells have a single nucleus and a septa. It has been proposed that the type II cells immediately septate again after division because they inherit the SPB that contains active Spg1p (Cerutti and Simanis, 1999). In support of this hypothesis, Sid1p was present at the SPB in type II cells (Figure 3A; see arrow).
PMID:10775265	FYPO:0003501	After shift to restrictive temperature, cdc16-116 cells display two phenotypes termed type I and type II cells (Minet et al., 1979; Cerutti and Simanis, 1999). Type I cells have two nuclei and make multiple septa. Type II cells have a single nucleus and a septa. It has been proposed that the type II cells immediately septate again after division because they inherit the SPB that contains active Spg1p (Cerutti and Simanis, 1999). In support of this hypothesis, Sid1p was present at the SPB in type II cells (Figure 3A; see arrow).
PMID:10775265	FYPO:0001493	(comment: dns)
PMID:10775265	PBO:0021078	I inferred new because it's asymmetric and we know sin is new
PMID:10775265	PBO:0097834	I inferred new because it's asymmetric and we know sin is new
PMID:10775265	PBO:0097839	(Figure 4; Table I)
PMID:10775265	PBO:0097839	(Figure 4; Table I)
PMID:10779336	FYPO:0002060	(Figure 2B)
PMID:10779336	FYPO:0001490	(Figure 1A) (comment:increased size?)
PMID:10779336	FYPO:0000158	(Figure 1B)
PMID:10779336	FYPO:0001387	(Figure 1A)
PMID:10779336	FYPO:0000141	(Figure 2B)
PMID:10779336	FYPO:0000620	(Figure 2B)
PMID:10779336	FYPO:0003165	(Figure 2B)
PMID:10779336	FYPO:0000141	(Figure 2)
PMID:10779336	FYPO:0000268	(Figure 3A)
PMID:10779336	FYPO:0000089	(Figure 3B)
PMID:10779336	FYPO:0000089	(Figure 3B)
PMID:10779336	FYPO:0000095	(Figure 3B)
PMID:10779336	FYPO:0001689	(Figure 3B)
PMID:10779336	FYPO:0002553	(Figure 3B)
PMID:10779336	FYPO:0002092	(Figure 4C)
PMID:10779336	FYPO:0001128	(comment: CHECK 5.6%)
PMID:10779336	FYPO:0002061	(Fig. 8)
PMID:10792724	GO:0004185	(comment: CHECK residue=S200)
PMID:10799520	PBO:0104248	Examination of these cells following 12 h of growth in thiamine-containing medium also showed that most cells (59%) contained Byr4 at all SPBs (Table II). In contrast to sid3-106 mutants, though, the amount of Byr4 localized to SPBs in cells depleted of Spg1 using the conditional promoter was greatly reduced (data not shown)
PMID:10799520	PBO:0018634	Spg1-HAH localized to SPBs throughout the cell cycle (Fig. 1B, second column) (8). Byr4 colocalized with Spg1-HAH during interphase (Fig. 1B, 1), but was absent from SPBs in metaphase (Fig. 1B, 2) and early anaphase
PMID:10799520	PBO:0019671	Later in anaphase, Byr4 colocalized with one SPB (Fig. 1B, 4). Byr4 colocalized with one or both SPBs in binucleate cells with septa (Fig. 1B, 5 and 6). In the vast majority of cells, Byr4 localized to SPBs that did not contain Cdc7 (Fig. 1C, 1, 4, and 5).
PMID:10799520	PBO:0104241	(comment: CHECK is this the right term?)
PMID:10799520	FYPO:0001222	(comment: CHECK combine, other binucleates should unde new term)
PMID:10799520	PBO:0104243	This analysis of microtubule structures confirmed that mononucleate cells with Cdc7 localized to SPBs were in interphase and suggested that Byr4 was required to prevent septation during interphase.
PMID:10799520	PBO:0104244	(Figure 2E) These results show that Byr4 is required to prevent septation in G1 cells.
PMID:10799520	PBO:0104245	A corresponding decrease in the fraction of cells with Spg1 localized to SPBs occurred and reached 7% at 16 h (Fig. 3)
PMID:10799520	PBO:0104247	As expected, most sid3-106 mutant cells (71%) contained four or more nuclei showing that there was insufficient Spg1 function in these cells for septation.
PMID:10799520	PBO:0104248	Examination of these cells following 12 h of growth in thiamine-containing medium also showed that most cells (59%) contained Byr4 at all SPBs (Table II). In contrast to sid3-106 mutants, though, the amount of Byr4 localized to SPBs in cells depleted of Spg1 using the conditional promoter was greatly reduced (data not shown)
PMID:10799520	PBO:0104249	Western analysis showed that the reduction in Byr4 localization to SPBs in cells depleted of Spg1 was not due to reduced Byr4 protein amounts (data not shown).
PMID:10799520	PBO:0104249	Western analysis showed that this decrease was not due to reduced Byr4 amounts
PMID:10799520	PBO:0023023	Cdc7-HA was not localized to SPBs during interphase (Fig. 1C, 1),, localized to both SPBs in metaphase and early anaphase cells (Fig. 1C, 2 and 3), and localized to one SPB in late mitotic cells (Fig. 1C, 4 - 6) (8).
PMID:10799520	PBO:0022584	Cdc7-HA was not localized to SPBs during interphase (Fig. 1C, 1)
PMID:10805744	PBO:0094458	(comment: not shown it is ser/thr kinase activity)
PMID:10805744	PBO:0093825	(comment: same as cdc2delta alone)
PMID:10805785	PBO:0095723	(Fig. 1c)
PMID:10805785	PBO:0095723	(Fig. 1c)
PMID:10805785	PBO:0095723	(Fig. 1c)
PMID:10805785	PBO:0095723	(Fig. 1c)
PMID:10805785	PBO:0094918	(Fig. 2)
PMID:10805785	PBO:0095723	(Fig. 1c)
PMID:10805785	PBO:0095723	(Fig. 1c)
PMID:10805785	PBO:0095723	(Fig. 1c)
PMID:10805785	PBO:0095723	(Fig. 1c)
PMID:10837231	FYPO:0002061	To examine the function of Mob1p in vivo, we deleted the mob1 gene (see Supplementary material) and found that it was essential for growth.
PMID:10837231	PBO:0094642	These results support the model that Mob1p, like Sid2p, functions downstream in the sid pathway. Consistent with this hypothesis, we found that Cdc7p localizes normally to the SPB in a mob1-1 temperature-sensitive mutant (Figure 4f). I
PMID:10837231	PBO:0116854	SPB was unaffected in sid1, sid2, spg1 and cdc14 mutants (Figure 4a and data not shown), but was severely affected in sid4, cdc7 and cdc11 mutants.
PMID:10837231	PBO:0116854	SPB was unaffected in sid1, sid2, spg1 and cdc14 mutants (Figure 4a and data not shown), but was severely affected in sid4, cdc7 and cdc11 mutants.
PMID:10837231	PBO:0116853	GFP-Mob1p localization to the SPB was unaffected in sid1, sid2, spg1 and cdc14 mutants (Figure 4a and data not shown)
PMID:10837231	PBO:0116853	GFP-Mob1p localization to the SPB was unaffected in sid1, sid2, spg1 and cdc14 mutants (Figure 4a and data not shown)
PMID:10837231	PBO:0116852	In all of the sid mutants, sid1, sid2, spg1, sid4 cdc7,cdc11 and cdc14, GFP-Mob1p could not localize to themedial region (Figure 4a-c and data not shown)
PMID:10837231	PBO:0116852	In all of the sid mutants, sid1, sid2, spg1, sid4 cdc7,cdc11 and cdc14, GFP-Mob1p could not localize to themedial region (Figure 4a-c and data not shown)
PMID:10837231	PBO:0116852	In all of the sid mutants, sid1, sid2, spg1, sid4 cdc7,cdc11 and cdc14, GFP-Mob1p could not localize to themedial region (Figure 4a-c and data not shown) (vw cdc15-140 in Figure legend must be a typo)
PMID:10837231	GO:0044732	The nuclear-associated spotlike localization of Mob1p suggested that it was a component of the SPB. To confirm SPB localization, we fixed and stained cells expressing GFP-Mob1p with an antitubulin antibody. GFP-Mob1p was localized at the ends of the mitotic spindle in cells undergoing mitosis, consistent with its localization to the SPB (Figure 3m).
PMID:10837231	PBO:0018611	These results are consistent with Mob1p localizing to the cell division site at, or just before, the initiation of septum formation, and then leaving the division site before cell separation. T
PMID:10837231	FYPO:0003702	Examination of microtubules showed that mob1-1 cells form normal mitotic spindles (Figure 2f,g), and interphase arrays of microtubules. Thus, unlike S. cerevisiae mob1 mutants, S. pombe mob1 mutants do not have defects in mitotic exit, but are specifically defective in cytokinesis
PMID:10837231	FYPO:0001294	Staining for the myosin light chain Cdc4p and actin revealed mob1-1 cells formed normal actomyosin rings and medially placed patches (Figure 2c-e).
PMID:10837231	FYPO:0001368	Staining for the myosin light chain Cdc4p and actin revealed mob1-1 cells formed normal actomyosin rings and medially placed patches (Figure 2c-e).
PMID:10837231	FYPO:0002024	After shifting to the restrictive temperature, mob1-1 cells failed to perform cytokinesis, became multinucleate, and did not form septa(Figure 2a-b).
PMID:10837231	GO:0004674	suggesting that Mob1-associated kinase activity is probably due to Sid2p.
PMID:10837231	FYPO:0001382	Kinase activity was associated with 13Myc-Mob1p prepared from wild-type cells, but Mob1p-associated kinase activity was reduced in sid2-250 cells (Figure 1c).
PMID:10837231	GO:0034973	We tested for an interaction between Mob1p and Sid2p using the yeast two-hybrid system. Sid2p and Mob1p specifically interacted with each other but not with control proteins (Figure 1a) Western blotting with anti-Myc antibodies detected Sid2p-13Myc as two bands that co-immunoprecipitated with GFP-Mob1p (Figure 1b).
PMID:10837231	GO:0034973	We tested for an interaction between Mob1p and Sid2p using the yeast two-hybrid system. Sid2p and Mob1p specifically interacted with each other but not with control proteins (Figure 1a)
PMID:10850973	GO:0008441	(comment: CHECK activated_by(CHEBI:18420)| activated_by(CHEBI:29103)| inhibited_by(CHEBI:48607)| inhibited_by(CHEBI:26710))
PMID:10852821	PBO:0094465	(Fig. 6)
PMID:10852821	FYPO:0001368	(Fig. 8)
PMID:10852821	PBO:0094468	(Fig. 8) (comment: myo2 clumped in nodes instead of ring)
PMID:10852821	FYPO:0004736	(Fig. 9) (comment: mainrtenance)
PMID:10852821	FYPO:0000161	(Fig. 3B)
PMID:10852821	FYPO:0000161	(Fig. 3B)
PMID:10852821	PBO:0094464	(Fig. 6)
PMID:10852821	PBO:0094465	(Fig. 6)
PMID:10852821	PBO:0094464	(Fig. 6)
PMID:10852821	PBO:0094469	(Fig. 8)
PMID:10852821	FYPO:0001368	(Fig. 8)
PMID:10852821	PBO:0094468	(Fig. 8) (comment: myo2 clumped in nodes instead of ring)
PMID:10852821	FYPO:0007127	(Fig. 9)
PMID:10852821	PBO:0094464	(Fig. 6)
PMID:10852821	PBO:0094469	(Fig. 8)
PMID:10852821	PBO:0094466	(Fig. 7A)
PMID:10852821	PBO:0094464	(Fig. 6)
PMID:10852821	PBO:0094467	(Fig. 7A) (comment: depends on actin)
PMID:10852821	FYPO:0002050	(Fig. 3B)
PMID:10852821	FYPO:0002050	(Fig. 3B)
PMID:10864871	FYPO:0000284	(comment: 2nd division)
PMID:10871341	FYPO:0002044	(Fig. 1)
PMID:10871341	FYPO:0000474	(Fig. 1)
PMID:10871341	PBO:0095590	(Fig. 1)
PMID:10871341	FYPO:0002044	(Fig. 1)
PMID:10879493	FYPO:0000081	(comment: 2M glucose = 36% w/v = A LOT, so it is osmolarity rather than glucose itself I guess)
PMID:10879493	FYPO:0000081	(comment: 2M glucose = 36% w/v = A LOT, so it is osmolarity rather than glucose itself I guess)
PMID:10886372	FYPO:0002059	(comment: don't know veg or spore)
PMID:10905343	PBO:0098816	(comment: total alpha tubulin level reduced but not known whether from nda2 or atb2 or both)
PMID:10905343	PBO:0098815	(comment: total alpha tubulin level reduced but not known whether from nda3 or atb2 or both)
PMID:10921876	PBO:0105402	(comment: APC-Ste9 dependent protein destruction/11365/) I didn't do a phenotype for this because they don't show a WT scanario. I used the ubiquitin-dependent term becasuethis is whet they were testing as we already know that this decgradation is APC/protiesome dependnet. I know its a bit of a stretch)
PMID:10921876	GO:1905785	(comment: APC-SLP1)
PMID:10921876	PBO:0096939	(Fig. 3) (comment: cdc25-22 block and release)
PMID:10921876	PBO:0105406	(Fig. 3) (comment: cdc25-22 block and release)
PMID:10921876	PBO:0105405	(Fig. 3) ((comment: CHECK cdc25-22 block and release)
PMID:10921876	PBO:0105409	(Fig. 1a)
PMID:10921876	PBO:0100981	(Fig. 1a)
PMID:10921876	FYPO:0001425	(Fig. 1b)
PMID:10921876	PBO:0105404	(Fig. 3) ((comment: CHECK cdc25-22 block and release)
PMID:10921876	PBO:0105405	(Fig. 3) (comment: CHECK cdc25-22 block and release)
PMID:10921876	PBO:0105404	(Fig. 3) (comment: CHECK cdc25-22 block and release)
PMID:10921876	PBO:0105403	(comment: APC-Ste9 dependent protein destruction/11365/) I didn't do a phenotype for this because they don't show a WT scanario. I used the ubiquitin-dependent term becasuethis is whet they were testing as we already know that this decgradation is APC/protiesome dependnet. I know its a bit of a stretch)
PMID:10921878	PBO:0103561	during mitotic G2 arrest
PMID:10930468	PBO:0104482	DNES1-mid1p had a clear defect in nuclear export- in contrast to wild-type mid1p, which exits the nucleus during mitosis, it remained in the nucleus throughout the cell cycle, although some faint rings were occasionally seen (Figure 6, A-B).
PMID:10930468	PBO:0104483	inferred from Nuclear export of mid1p was sensitive to leptomycin B (LMB), a drug that blocks the nuclear export factor crm1p (see Figure 8; Nishi et al., 1994; Kudo et al.; 1999), showing that the nuclear export of mid1p is crm1 dependent.
PMID:10930468	PBO:0104484	no NLS*-mid1p was detectable in the nucleus when expressed under the control of mid1 promoter (
PMID:10930468	PBO:0104486	DNES1-mid1p had a clear defect in nuclear export- in contrast to wild-type mid1p, which exits the nucleus during mitosis, it remained in the nucleus throughout the cell cycle, although some faint rings were occasionally seen (Figure 6, A-B).
PMID:10930468	PBO:0104479	Cells carrying pREP41Xmid1 exhibited a striking phenotype: they formed bulges near the cell center (Figure 1B). Medial bulges were exhibited in 40% of the cells 20 h after removal of thiamine (Figure 1C middle). Cells were longer than normal, suggestive of a cell cycle delay in interphase (Figure 1B)
PMID:10930468	PBO:0104481	DNES1-mid1p had a clear defect in nuclear export- in contrast to wild-type mid1p, which exits the nucleus during mitosis, it remained in the nucleus throughout the cell cycle, although some faint rings were occasionally seen (Figure 6, A-B).
PMID:10930468	PBO:0109149	DNES1-mid1p had a clear defect in nuclear export- in contrast to wild-type mid1p, which exits the nucleus during mitosis, it remained in the nucleus throughout the cell cycle, although some faint rings were occasionally seen (Figure 6, A-B).
PMID:10930468	PBO:0109148	DNES1-mid1p had a clear defect in nuclear export- in contrast to wild-type mid1p, which exits the nucleus during mitosis, it remained in the nucleus throughout the cell cycle, although some faint rings were occasionally seen (Figure 6, A-B).
PMID:10930468	PBO:0104485	localized in an identical manner to wild-type mid1p (Figure 9A) and was fully functional (Figure 7 and Table 2).
PMID:10930468	FYPO:0008074	noNLS*-mid1p was detectable in the nucleus when expressed under the control of mid1 promoter (
PMID:10930468	FYPO:0001234	and the generation time of the population was increased approximately two-fold (Figure 1C top).
PMID:10930468	PBO:0104480	DNES2-mid1p had a weaker, but demonstrable nuclear export defect: it retained some weak cortical staining and weak rings in addition to nuclear staining (Figure 6C), but
PMID:10930468	PBO:0109150	DNES2-mid1p had a weaker, but demonstrable nuclear export defect: it retained some weak cortical staining and weak rings in addition to nuclear staining (Figure 6C), but
PMID:10930468	FYPO:0006638	(comment: CHECK diffuse cytoplsmic throughout the cell cycle)
PMID:10930468	PBO:0104487	(comment: CHECK diffuse cytoplsmic throughout the cell cycle)
PMID:10930468	FYPO:0002070	No defects in nuclear positioning were apparent, as nuclei were positioned properly at the middle of the cell or in the bulge region (see Figure 2). Mid1p localization in these
PMID:10947840	FYPO:0002060	We found, on the other hand, that the ts phenotype of mis3-224 was suppressed by dis2-11, a cs mutation with greatly reduced type 1 protein phosphatase (PP1) activity and the inability to exit from mitosis (Ohkura et al. 1989).
PMID:10947840	FYPO:0002060	We found, on the other hand, that the ts phenotype of mis3-224 was suppressed by dis2-11, a cs mutation with greatly reduced type 1 protein phosphatase (PP1) activity and the inability to exit from mitosis (Ohkura et al. 1989).
PMID:10947840	FYPO:0002061	In addition to the interaction between Mis3 and Wee1, it was found that the double mutants mis3 cdc25 and mis3 cdc13 were able to form colonies at 268C, but not at 308C (Fig. 6A).
PMID:10947840	FYPO:0002061	In addition to the interaction between Mis3 and Wee1, it was found that the double mutants mis3 cdc25 and mis3 cdc13 were able to form colonies at 268C, but not at 308C (Fig. 6A).
PMID:10947840	FYPO:0002061	In addition to the interaction between Mis3 and Wee1, it was found that the double mutants mis3 cdc25 and mis3 cdc13 were able to form colonies at 268C, but not at 308C (Fig. 6A).
PMID:10947840	FYPO:0004481	they ceased to increase in number after two divisions (Fig. 1A, open triangles). The growth arrest phenotype of mis3-224 (Fig. 1C) was distinct from that of typical cdc mutants, as its cell length increase was insigni®cant (1.3-fold) after 8h at 36 8C. mis3-224 at 36 8C was unable to increase in cell length because the levels of protein and RNA ceased to increase (B, ®lled and open triangles, respectively).
PMID:10947840	FYPO:0007136	they ceased to increase in number after two divisions (Fig. 1A, open triangles). The growth arrest phenotype of mis3-224 (Fig. 1C) was distinct from that of typical cdc mutants, as its cell length increase was insigni®cant (1.3-fold) after 8h at 36 8C. mis3-224 at 36 8C was unable to increase in cell length because the levels of protein and RNA ceased to increase (B, ®lled and open triangles, respectively).
PMID:10947840	FYPO:0008218	These results showed that cells lacking functional Mis3 could not promote cell growth upon the release to complete medium and remained in the G1/S phase.
PMID:10947840	FYPO:0000088	it was moderately sensitive at 308C (Fig. 5A, top): mutant failed to produce colonies in the presence of 8 mM HU at 30 8C, a semi-restrictive temperature.
PMID:10947840	PBO:0112273	At 36 8C in mis3-224, the level of Mik1 increased to a peak after 4h, but then strikingly decreased to a low level (E).
PMID:10947840	PBO:0112789	At 36 8C in mis3-224, the level of Mik1 increased to a peak after 4h, but then strikingly decreased to a low level (E).
PMID:10947840	FYPO:0002061	Tetrad dissection indicated that the mis3-224 dsk1 null double mutant failed to grow at any temperature.
PMID:10947840	FYPO:0002061	Tetrad dissection indicated that the mis3-224 dsk1 null double mutant failed to grow at any temperature.
PMID:10947840	FYPO:0002061	In addition to the interaction between Mis3 and Wee1, it was found that the double mutants mis3 cdc25 and mis3 cdc13 were able to form colonies at 268C, but not at 308C (Fig. 6A).
PMID:10950958	FYPO:0001406	Microscopic observation revealed that some mutant cells have a thick septum that was brightly stained with Calcofluor and was hardly seen in wild-type cells (Fig. 8A).
PMID:10950958	FYPO:0002061	Tetrad analysis of the heterozygous diploid showed two viable (UraΔ) and two inviable spores (Fig. 3D), indicating that the its3Δ gene is essential for cell growth.
PMID:10950958	FYPO:0006625	(comment: CHECK NOT PLASMA MEMBRANE) As shown in Fig. 5B, its3-1 mutant cells contained about 10% of the amount of PI(4,5)P2 found in wild-type cells, indicating that the mutation caused a significant decrease in PI(4)P5K activity of Its3.
PMID:10950958	FYPO:0000994	Interestingly, the level of PI(4)P was significantly higher than that of the wild-type cells.
PMID:10950958	FYPO:0006626	(comment: CHECK NOT PLASMA MEMBRANE)
PMID:10950958	FYPO:0000790	In wild-type cells, a shift from 27 to 33 °C caused a transient heat-induced disorganization of actin patches
PMID:10950958	FYPO:0008042	On the other hand, in the its3-1 mutant cells, actin patches were partially polarized at 27 °C, and the polarization was completely lost upon temperature upshift or FK506 treatment (Fig. 7A).
PMID:10950958	FYPO:0002061	As shown in Fig. 1A, its3-1 mutant cells could not grow at 33 °C, 36 °C, or in the YPD plate containing FK506, whereas wild-type cells grew normally.
PMID:10950958	FYPO:0000650	In addition, its3-1 mutant had a septation index approximately twice that seen in wild-type cells at the permissive temperature.
PMID:10950958	GO:0005886	GFP-Its3 localized to the plasma membrane at all stages of the cell cycle (Fig. 9A).
PMID:10950958	GO:0032153	GFP-Its3 localized to the plasma membrane at all stages of the cell cycle (Fig. 9A).
PMID:10950958	PBO:0095430	As shown in Fig. 9B, the GFP-Its3-1 mutant protein (GFP-mIts3) was no longer localized to the plasma membrane and instead...
PMID:10950958	FYPO:0000086	As shown in Fig. 1A, its3-1 mutant cells could not grow at 33 °C, 36 °C, or in the YPD plate containing FK506, whereas wild-type cells grew normally.
PMID:10950958	PBO:0109009	PI(4)5K activity kinase: As shown in Fig. 1A, its3-1 mutant cells could not grow at 33 °C, 36 °C, or in the YPD plate containing FK506, whereas wild-type cells grew normally.
PMID:10950958	PBO:0095429	Purified GST fusion proteins were subjected to in vitro kinase reaction as described under “Experimental Procedures.” Fig. 6 shows that mutant Its3 tagged with GST had detectable but reduced PI(4)5K activity compared with the wild-type.
PMID:10950958	FYPO:0002061	􏰇ppb1 (􏰇CN in Fig. 2) mutant. As expected, no double mutant was obtained, indicating that its3 mutation and calcineurin deletion was synthetically lethal.
PMID:10950958	FYPO:0002061	􏰇ppb1 (􏰇CN in Fig. 2) mutant. As expected, no double mutant was obtained, indicating that its3 mutation and calcineurin deletion was synthetically lethal.
PMID:10954610	PBO:0099392	steady-state labeling assay; stability increases in wt but not mutant upon UV exposure
PMID:10954610	PBO:0099391	transcription run-on assay
PMID:10954610	PBO:0099391	transcription run-on assay
PMID:10954610	PBO:0099392	steady-state labeling assay; stability increases in wt but not sty1delta upon UV exposure
PMID:10970777	PBO:0096414	(comment: decreased)
PMID:10970777	GO:0004081	(comment: there is another unknown gene with this activity)
PMID:10978278	PBO:0097277	(comment: beta tubulin specific pathway)
PMID:11007487	GO:0031122	"""We conclude that tip1p is required for the correct organization of the microtubule cytoskeleton and for the proper localization of the tea1p marker to the cell ends"""
PMID:11007487	PBO:0018345	(Fig. 4A, 3G)
PMID:11007487	PBO:0038059	(Fig. 4F) However, tip1p was observed at the tips of the astral microtubules that emanated from the cytoplasmic face of the nuclear-located spindle pole body during anaphase and at the tips of the microtubules generated from the central region of postmitotic cells (Figures 4F).
PMID:11007487	PBO:0098917	(Fig. 4)
PMID:11007487	PBO:0038055	(Fig. 3D)
PMID:11007487	PBO:0038056	(Fig. 3F) (comment: (methanol fixation))
PMID:11007487	PBO:0098918	(Fig. 6) (comment: (live cell imaging) GFP-tubulin expressed from nmt1 promoter on multi copy plasmid)
PMID:11007487	FYPO:0005799	(Fig. 6) (comment: (live cell imaging) GFP-tubulin expressed from nmt1 promoter on multi copy plasmid)
PMID:11007487	PBO:0037211	(Figures 4C, 4G)
PMID:11007487	PBO:0037218	(Fig. 3I)
PMID:11007487	PBO:0098915	(Fig. 3K) (comment: (methanol fixation))
PMID:11007487	FYPO:0001400	(Fig. 3K) (comment: (methanol fixation))
PMID:11007487	PBO:0098920	(Fig. 3C)
PMID:11007487	GO:0008017	(Figure 4H) (comment: CHECK in vitro)
PMID:11007487	FYPO:0001018	(Fig. 1B)
PMID:11007487	PBO:0098916	( data for these cells not shown)
PMID:11007487	PBO:0098922	(Figure 4I)
PMID:11007487	PBO:0098921	(Figure 4I) (comment: I'm not sure if we knew it was the plus end then, but we do now ;))
PMID:11007487	GO:0030010	"""These phenotypes establish that tip1p is required to properly position the growth zones at the antipodes of the cells."""
PMID:11007487	FYPO:0001399	data not shown
PMID:11007487	FYPO:0004700	(Fig. 1) (comment: tip1 expressed from pREP3X)
PMID:11007487	FYPO:0000224	(Fig. 1) (comment: tip1 expressed from pREP3X)
PMID:11007487	FYPO:0000015	(Fig. 1) (comment: tip1 expressed from pREP3X)
PMID:11007487	FYPO:0000014	(Fig. 1) (comment: tip1 expressed from pREP3X. I've used this term as it is the nearest to schmoozing which is the term they use in the paper. To be honest I think tapered is better as they don't know that the cells are shmooing)
PMID:11007487	PBO:0038053	(Fig. 3B)
PMID:11007487	PBO:0098915	(Fig. 3H) ((comment: methanol fixation))
PMID:11007487	PBO:0098919	(Fig. 3) (comment: (methanol fixation))
PMID:11007487	FYPO:0001366	(Fig. 3I) (comment: (Formaldehyde fixation))
PMID:11014802	GO:0010515	(comment: maybe not shown strongly in this paper but I'm trying to get the git genes annotated to this term because pka1 phosphorylates rst2 which excludes rst2 from the nucleus. rst2 when in the nucleus activates ste11 transcription.)
PMID:11014802	GO:0010515	(comment: maybe not shown strongly in this paper but I'm trying to get the git genes annotated to this term because pka1 phosphorylates rst2 which excludes rst2 from the nucleus. rst2 when in the nucleus activates ste11 transcription.)
PMID:11017199	PBO:0099479	structure
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	PBO:0037208	(Fig. 4)
PMID:11018050	FYPO:0005809	Data was not shown.
PMID:11018050	PBO:0098938	(Fig. 2D)
PMID:11018050	FYPO:0002760	(Fig. 3)
PMID:11018050	PBO:0037206	(Fig. 2B)
PMID:11018050	PBO:0095634	(comment: forms microcolonies)
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002060	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002060	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	PBO:0037209	(Fig. 2G)
PMID:11018050	PBO:0022298	(Fig. 5)
PMID:11018050	PBO:0037211	(Fig. 5)
PMID:11018050	FYPO:0002060	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	PBO:0037212	(Fig. 6) cell tip localisation increased compared to exponentially growing cells
PMID:11018050	PBO:0098939	(Fig. 8, 5) Tea2 is not completely delocalised but is has a more extended distribution along the microtubules
PMID:11018050	PBO:0098940	(Fig. 8) (comment: vw: I made this 'along micriotubule because we know its microtubule dept)
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	PBO:0018421	(Fig. 6)
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media.
PMID:11018050	PBO:0098941	(Fig. 8c)
PMID:11018050	FYPO:0002060	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002060	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002060	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002060	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media.
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media.
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002060	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002060	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11018050	PBO:0037209	(Fig. 2)
PMID:11018050	FYPO:0002058	growth assayed on agar plates at different temperature and media
PMID:11027257	FYPO:0002061	(comment: higher temp, restrictive for spp2-8 alone)
PMID:11027257	PBO:0019630	(comment: mixed population)
PMID:11027257	PBO:0023027	(comment: mixed population)
PMID:11027257	FYPO:0002061	(comment: temp semi-permissive for spp2-8 alone)
PMID:11027257	FYPO:0002061	(comment: temp semi-permissive for spp2-8 alone)
PMID:11027257	FYPO:0002060	(comment: temp semi-permissive for spp2-8 alone)
PMID:11027257	FYPO:0006822	(comment: higher temp, restrictive for spp2-8 alone)
PMID:11027257	FYPO:0000062	(comment: higher temp, restrictive for spp2-8 alone)
PMID:11027257	FYPO:0002061	(comment: temp semi-permissive for spp2-8 alone)
PMID:11027257	FYPO:0002061	(comment: temp semi-permissive for spp2-8 alone)
PMID:11027257	FYPO:0002061	(comment: temp semi-permissive for spp2-8 alone)
PMID:11027257	FYPO:0002061	(comment: temp semi-permissive for spp2-8 alone)
PMID:11027257	FYPO:0002061	(comment: temp semi-permissive for spp2-8 alone)
PMID:11027257	FYPO:0002061	(comment: temp semi-permissive for spp2-9 alone)
PMID:11027257	FYPO:0002061	(comment: temp semi-permissive for spp2-9 alone)
PMID:11027257	FYPO:0002060	(comment: temp semi-permissive for spp2-9 alone)
PMID:11027257	FYPO:0002061	(comment: higher temp, restrictive for spp2-9 alone)
PMID:11027257	FYPO:0006822	(comment: higher temp, restrictive for spp2-9 alone)
PMID:11027257	FYPO:0000062	(comment: higher temp, restrictive for spp2-9 alone)
PMID:11027257	FYPO:0002061	(comment: temp semi-permissive for spp2-9 alone)
PMID:11027257	FYPO:0002061	(comment: temp semi-permissive for spp2-9 alone)
PMID:11027257	FYPO:0002061	(comment: temp semi-permissive for spp2-9 alone)
PMID:11027257	FYPO:0002061	(comment: temp semi-permissive for spp2-9 alone)
PMID:11027257	FYPO:0002061	(comment: temp semi-permissive for spp2-9 alone)
PMID:11027257	FYPO:0002061	(comment: temp semi-permissive for spp2-8 alone)
PMID:11027257	FYPO:0002061	(comment: temp semi-permissive for spp2-9 alone)
PMID:11027263	FYPO:0001355	(comment: temp. restrictive for hsk1-1312 alone; fudged a bit because assayed at 32)
PMID:11027263	FYPO:0004672	(comment: same as hsk1-1312 alone)
PMID:11030618	PBO:0093615	(Fig. 6)
PMID:11030618	FYPO:0001690	(Fig. 6)
PMID:11030618	FYPO:0001690	(Fig. 6)
PMID:11030618	FYPO:0001690	(Fig. 6)
PMID:11030618	PBO:0093614	(Fig. 6)
PMID:11030618	FYPO:0006602	(Fig. 2A)
PMID:11030618	FYPO:0006602	(Fig. 2A)
PMID:11030618	FYPO:0006603	(Fig. 4)
PMID:11030618	FYPO:0006603	(Fig. 4)
PMID:11030618	FYPO:0008230	(Fig. 5)
PMID:11030618	FYPO:0006603	(Fig. 5)
PMID:11030618	GO:0011000	If RTS1 function in imprinting and sporulation had been affected because of top1p deficiency, an increase in imprinting and sporulation would be expected. However, no increase was observed, showing that top1p was not involved in termination of replication.
PMID:11030618	FYPO:0001234	a swi1-111, Dtop1 double mutant revealed a decreased growth rate, suggesting a swi1 and top1 interaction.
PMID:11030618	FYPO:0001234	a swi1-111, Dtop1 double mutant revealed a decreased growth rate, suggesting a swi1 and top1 interaction.
PMID:11030618	FYPO:0001234	A similar slow growth phenotype was also observed for a Dtop1, swi3 double mutant (JZ454) when compared to a swi3 mutant strain (E157).
PMID:11030618	FYPO:0001234	A similar slow growth phenotype was also observed for a Dtop1, swi3 double mutant (JZ454) when compared to a swi3 mutant strain (E157).
PMID:11030618	PBO:0093613	(Fig. 6)
PMID:11030618	GO:0011000	the swi1p and swi3p proteins, necessary for imprinting, were shown to pause the replication fork at the site of imprinting.
PMID:11030618	GO:0011000	the swi1p and swi3p proteins, necessary for imprinting, were shown to pause the replication fork at the site of imprinting.
PMID:11030618	FYPO:0001690	(Fig. 6)
PMID:11030618	FYPO:0001690	(Fig. 6)
PMID:11069657	FYPO:0000175	(comment: they form parts that fail to mature)
PMID:11069779	FYPO:0002061	(comment: CHECK **SYNTHETIC LETHAL)
PMID:11069779	FYPO:0001524	(comment: CONDITION toxic aa-analog)
PMID:11071923	FYPO:0007317	(comment: global translation, not a specific gene)
PMID:11076964	GO:0030479	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:11080156	FYPO:0003165	(comment: after passage through G1)
PMID:11080156	FYPO:0004537	(comment: CHECK SAC- fypo/issues/2310)
PMID:11080156	PBO:0033364	(comment: with cut at second division)
PMID:11080156	PBO:0033364	(comment: with cut)
PMID:11084332	PBO:0102589	(comment: CHECK during G1 arrest ) fig4C right hand panel
PMID:11084332	FYPO:0000833	(comment: total ubiquitinated)
PMID:11084332	PBO:0102590	(comment: ubiquitinated)
PMID:11084332	PBO:0097048	(comment: ubiquitinated)
PMID:11084332	PBO:0102585	(comment: CHECK during anaphase)
PMID:11084332	PBO:0102586	(comment: CHECK delayed during anaphase)
PMID:11084332	PBO:0102587	(comment: total protein in proteasome mutant)
PMID:11084332	PBO:0102587	(comment: total protein in proteasome mutant)
PMID:11084332	PBO:0102588	(comment: CHECK during G1 arrest ) fig4C right hand panel
PMID:11102508	PBO:0033981	(comment: WT 0.5%)
PMID:11112691	PBO:0099929	Whereas Myo51 overproduction resulted in elongated cells with wispy, misoriented septal material (Fig. 4A)
PMID:11112691	PBO:0112862	cells overproducing Myo52 were less elongated and branched due to the failure of septa to properly cleave (Fig. 4B).
PMID:11112691	PBO:0020227	Myo52 formed a cap at the growing tips (Fig. 5C,D).
PMID:11112691	PBO:0018339	Myo52 formed a cap at the growing tips (Fig. 5C,D).
PMID:11112691	FYPO:0001357	Myo51 were indistinguishable from an isogenic wild-type strain (Fig. 2A,B).
PMID:11112691	PBO:0095634	myo52∆ cells showed extremely slow growth at 36°C (Fig. 2C).
PMID:11112691	PBO:0018339	Myo51 appears to be a component of the CAR.
PMID:11112691	FYPO:0000801	Loss of cell shape in myo52∆ was accompanied by the depolarisation of the actin cytoskeleton whereas no change in actin organisation could be detected in myo51∆ (Fig. 3A).
PMID:11112691	PBO:0112863	Mok1 was delocalised in myo52∆ (Fig. 8C)
PMID:11112691	FYPO:0001234	At this temperature myo52∆ cells grew more slowly (Fig. 2B) and had an altered morphology, being shorter and
PMID:11112691	FYPO:0000024	At this temperature myo52∆ cells grew more slowly (Fig. 2B) and had an altered morphology, being shorter and
PMID:11112691	PBO:0112861	(Fig. 3B). The double mutant myo52∆ cps8− was extremely sick even at the permissive temperature and formed only micro colonies consisting of severely deformed cells.
PMID:11112691	FYPO:0000650	septation index of 20%, twice that of wild type (Fig. 2A).
PMID:11112691	FYPO:0000032	(comment: Figure missing from pdf, so I could not be more precise myo51∆ cps8− cells were viable at 25°C but had marked cytokinetic defects) (Fig. 3B).
PMID:11134033	GO:0005737	(Fig. 2)
PMID:11134033	FYPO:0003302	(Figure 1b)
PMID:11134033	FYPO:0000337	(Figure 1b)
PMID:11134033	PBO:0037397	(Figure 1b) (I)
PMID:11134033	PBO:0096454	(Figure 1b) (I)
PMID:11134033	PBO:0037399	(Figure 1C)
PMID:11134033	FYPO:0002946	(Figure 1a)
PMID:11134033	FYPO:0002060	(data not shown)
PMID:11134033	PBO:0037400	indicated by decreased polysome to monosome ratio
PMID:11160827	PBO:0092751	present throughout mitotic cell cycle
PMID:11179424	PBO:0103795	(comment: residue not determined experimentally, but probably Y173)
PMID:11226171	FYPO:0000267	(comment: same sensitivity as rhp54delta alone)
PMID:11226171	FYPO:0000267	(comment: same sensitivity as rhp54delta alone)
PMID:11231017	FYPO:0001234	(Fig. 1)
PMID:11231017	FYPO:0000106	(Fig. 1)
PMID:11231572	GO:0110085	(comment: dependent on F-actin, assayed using Latrunculin A)
PMID:11231572	GO:0030479	(comment: dependent on F-actin, assayed using Latrunculin A)
PMID:11238401	GO:0010515	comment: maybe not shown strongly in this paper but I'm trying to get the git genes annotated to this term because pka1 phosphorylates rst2 which excludes rst2 from the nucleus. rst2 when in the nucleus activates ste11 transcription.)
PMID:11238401	GO:0010515	(comment: maybe not shown strongly in this paper but I'm trying to get the git genes annotated to this term because pka1 phosphorylates rst2 which excludes rst2 from the nucleus. rst2 when in the nucleus activates ste11 transcription.)
PMID:11242054	PBO:0111086	whereas the Clr4-G341D strain shows loss of localization from the nuclear periphery and accumulation of more diffuse staining over the nucleolus (Fig. 4c).
PMID:11242054	PBO:0119827	(comment: The fission yeast S. pombe has an HP1 homologue Swi6, which contains a chromo domain that is closely related to those of HP1 family members.) (Figure 4a) shows that the Swi6 chromo domain is able to bind H3 peptide methylated at Lys 9, whereas its chromo-shadow domain has no methyl-binding activity.
PMID:11242054	FYPO:0007334	loss of association of Swi6 with centromeres should result in expression of a normally silent marker gene embedded in centromeric chromatin. Figure 4e shows that this is indeed the case. On indicator plates, wild-type strains silence the centromeric ade6+ marker, which results in red, repressed colonies13; however, in strains lacking Clr4 (D) or strains defective in Clr4 methylase activity (G341D), this ade6+ gene is clearly expressed, resulting in the formation of white colonies.
PMID:11242054	FYPO:0007334	loss of association of Swi6 with centromeres should result in expression of a normally silent marker gene embedded in centromeric chromatin. Figure 4e shows that this is indeed the case. On indicator plates, wild-type strains silence the centromeric ade6+ marker, which results in red, repressed colonies13; however, in strains lacking Clr4 (D) or strains defective in Clr4 methylase activity (G341D), this ade6+ gene is clearly expressed, resulting in the formation of white colonies.
PMID:11248251	PBO:0117238	We propose that the two proteins are part of a mitochondrial (prokaryotic) type monooxygenase that hydroxylates the methyl group of heme O. Accordingly, the third component of this pathway is ferredoxin (adrenodoxin) dehydrogenase encoded by ARH1 which has been localized in mitochondria of S. cerevisiae [13]. As depicted in Fig. 3, the function of Cox15p would be analogous to that of P450 in other three component monooxygenases [14].
PMID:11248251	FYPO:0008143	The two exceptions were the cox10 and cox15 mutants, both of which lacked heme A. In agreement with earlier results the cox10 mutant also had no heme O [4]. This was not true of the cox15 mutant which had a very low but detectable amount of heme O (Fig. 1).
PMID:11248251	FYPO:0008143	The two exceptions were the cox10 and cox15 mutants, both of which lacked heme A. In agreement with earlier results the cox10 mutant also had no heme O [4].
PMID:11248251	GO:0005759	These results further indicate that the C-terminal end of Cox15p, together with Yah1p, is located in the matrix compartment. Yah1p fused to Cox15p is therefore in the same compartment as the native protein (Fig. 5B).
PMID:11248251	PBO:0110543	This was not true of the cox15 mutant which had a very low but detectable amount of heme O (Fig. 1).
PMID:11248251	FYPO:0008144	In agreement with earlier results the cox10 mutant also had no heme O [4]. This was not true of the cox15 mutant which had a very low but detectable amount of heme O (Fig. 1).
PMID:11250892	GO:0072686	(Figure 1C)
PMID:11250892	PBO:0108091	(Fig. 1)
PMID:11250892	PBO:0108093	(Fig. 7)
PMID:11250892	PBO:0108092	(Figure 3)
PMID:11252721	FYPO:0002061	(comment: facs and author comment about growth)
PMID:11260263	PBO:0093595	(comment: CONDITION 0.75 M)
PMID:11260263	FYPO:0002021	(Fig. 2B)
PMID:11260263	FYPO:0000708	(Fig. 2B)
PMID:11260263	FYPO:0002061	(comment: CONDITION 0.75 M)
PMID:11263963	PBO:0094278	(Fig. 3D)
PMID:11263963	FYPO:0001492	(Fig. 3A)
PMID:11263963	GO:0005886	(Fig. 1B)
PMID:11263963	PBO:0112460	(Fig. 4)
PMID:11263963	PBO:0112429	(Fig. 4)
PMID:11263963	FYPO:0002459	(Fig. 3A)
PMID:11263963	FYPO:0002459	(Fig. 3A)
PMID:11263963	GO:0032956	This hypersensitivity to LatB of mutants of either Drkp1 or Dpck2 indicates that both Rkp1 and Pck2 are required for stable filamentous actin network.
PMID:11263963	FYPO:0000648	(Fig. 3A)
PMID:11263963	PBO:0112461	As shown in Fig. 5, growth of the cells expressing human RACK1 was not seriously affected by the presence of LatB indicating human RACK1 is a functional homolog of Rkp1.
PMID:11263963	FYPO:0001357	(Fig. 3B and D)
PMID:11263963	FYPO:0001357	(Fig. 3B and D)
PMID:11263963	FYPO:0001355	(Fig. 3B and D)
PMID:11263963	PBO:0094276	(Fig. 3D)
PMID:11263963	GO:0032956	This hypersensitivity to LatB of mutants of either Drkp1 or Dpck2 indicates that both Rkp1 and Pck2 are required for stable filamentous actin network.
PMID:11263963	FYPO:0000961	(Fig. 3D)
PMID:11263963	FYPO:0000961	(Fig. 3D)
PMID:11263963	PBO:0093596	(Fig. 3D)
PMID:11263963	PBO:0112460	(Fig. 4)
PMID:11263963	PBO:0093596	(Fig. 3D)
PMID:11263963	PBO:0094279	(Fig. 3D)
PMID:11271422	PBO:0097505	(Fig. 2B)
PMID:11271422	FYPO:0002060	(Fig. 3A)
PMID:11271422	FYPO:0002060	(Fig. 3A)
PMID:11271422	PBO:0112773	(Fig. 1A)
PMID:11271422	FYPO:0005369	(Fig. 3A)
PMID:11271422	PBO:0104247	(Fig. 1A)
PMID:11271422	PBO:0097505	(Fig. 2A)
PMID:11271422	PBO:0112774	Microscopy revealed occasional cells with an aberrant septum or with multiple nuclei Fig. 2A
PMID:11271422	PBO:0107432	(Fig. 2A)
PMID:11271422	PBO:0038207	(Fig. 2A)
PMID:11271422	FYPO:0002049	(Fig. 2B)
PMID:11271422	FYPO:0001315	(Fig. 2B)
PMID:11271422	PBO:0112775	(Fig. 1A)
PMID:11271422	PBO:0097505	(Fig. 2B)
PMID:11279037	FYPO:0002061	(comment: CHECK taf73 does not substitute for taf5)
PMID:11294895	PBO:0018421	(comment: localization requires F-actin -assayed using latrunculin A)
PMID:11294895	PBO:0100352	(comment: localization requires F-actin -assayed using latrunculin A)
PMID:11294895	PBO:0019716	(comment: localization requires F-actin -assayed using latrunculin A)
PMID:11294907	PBO:0095174	(comment: dependent on actin cytoskeleton (assayed using Latrunculin A))
PMID:11294907	PBO:0095173	(comment: dependent on actin cytoskeleton (assayed using Latrunculin A))
PMID:11294907	GO:0110085	(comment: dependent on actin cytoskeleton (assayed using Latrunculin A))
PMID:11294907	PBO:0018972	(comment: dependent on actin cytoskeleton (assayed using Latrunculin A))
PMID:11313455	GO:0003682	(comment: increased during response to DNA damage by MMS or ionizing radiation; dissociates during response to HU)
PMID:11313465	PBO:0106865	(comment: Rad3 phosphorylates T11 in response to hydroxyurea treatment)
PMID:11313465	PBO:0106867	(comment: CHECK phosphorylates Cds1)
PMID:11313465	PBO:0106866	(comment: CHECK cellular response to hydroxyurea)
PMID:11331883	FYPO:0005648	(Fig. 2c and Table 1)
PMID:11331883	PBO:0098558	In contrast, Rec8 disappeared completely in Dbub1 anaphase I cells. Rec8 was not observed in any of the >100 late-anaphase cells examined and was obviously never detected in early MII cells
PMID:11331883	PBO:0098557	In contrast, Rec8 disappeared completely in Dbub1 anaphase I cells. Rec8 was not observed in any of the >100 late-anaphase cells examined and was obviously never detected in early MII cells
PMID:11331883	PBO:0098556	Consistently, Rec8 localization was indistinguishable from wild-type from early meiosis and until metaphase I (Fig. 3). Rec8 first appeared in the centromeric regions of cells before conjugation (Fig. 3, G1 cells) and its distribution was further extended throughout chromatin during the horse-tail stage and until metaphase I. Therefore, Rec8 is properly localized and co-orientation still occurs in the absence of Bub1, indicating that the occurrence of equational segregation in Dbub1 cells may be due to a defect in functional fusion of sister kinetochores rather than to defective co-orientation of sister centromeres.
PMID:11331883	PBO:0109723	Table1 Together, these results rule out the possibility that equational segregation in the absence of Bub1 is due to loss of sister-chromatid cohesion before attachment of kinetochores to microtubules.
PMID:11331883	PBO:0109722	Table1 Interestingly, sister chromatids do not segregate randomly in the absence of Rec8 but rather segregate equationally10 (Table 1), implying that cohesion must be preserved between sister centromeres to give them a mitotic-like, back-to-back orientation
PMID:11331883	PBO:0109721	Table1
PMID:11331883	GO:1990813	The most straightforward interpretation is that Bub1 is required to maintain sister-chromatid cohesion at anaphase I by preventing the removal of Rec8 from centromeric regions.
PMID:11350031	PBO:0098377	(comment: all taf1 introns affected)
PMID:11359920	PBO:0032998	(comment: CONDITION 30 degrees)
PMID:11359920	PBO:0032997	(comment: CONDITION 30 degrees)
PMID:11359920	PBO:0032994	(comment: CONDITION 30 degrees)
PMID:11359920	FYPO:0001430	(comment: CONDITION 30 degrees)
PMID:11359920	PBO:0097498	(comment: CONDITION 30 degrees)
PMID:11359920	PBO:0032993	(comment: CONDITION 30 degrees)
PMID:11359920	PBO:0097500	(comment: CONDITION 30 degrees)
PMID:11359920	PBO:0097499	(comment: CONDITION 30 degrees)
PMID:11359920	FYPO:0001933	(comment: CONDITION 30 degrees)
PMID:11359920	PBO:0094206	(comment: CONDITION 30 degrees)
PMID:11359928	PBO:0095312	(Fig. 3a)
PMID:11359928	PBO:0019203	(Fig. 8)
PMID:11359928	PBO:0106453	(Figure 4A)
PMID:11359928	PBO:0019203	(Fig. 2c)
PMID:11359928	PBO:0106452	(Fig. 2c)
PMID:11359928	PBO:0106454	(Figure 4A)
PMID:11369198	PBO:0036768	(Figure 5b)
PMID:11369198	FYPO:0004236	(Figure 5b)
PMID:11369198	FYPO:0002061	data not shown
PMID:11369198	PBO:0022298	Movie 1A
PMID:11369198	PBO:0023853	(Fig. 2B)
PMID:11369198	PBO:0018845	(Fig. 2B)
PMID:11369198	PBO:0097445	(Figure 5b)
PMID:11384993	PBO:0101549	(comment: a significant reduction in kinase activity, 40% of Sid1)
PMID:11384993	PBO:0101548	(comment: barely above background for vector alone and Sid1C) (Fig. 2B)
PMID:11387218	PBO:0095886	punctate in wild type, diffuse throughout nucleus in mutant
PMID:11387325	PBO:0111636	The key findings were that the S. pombe guanylyltransferase bound equally well to the CTD Ser5-PO4 peptide and the Ser2-PO4/Ser5-PO4 peptide. Slightly less than one-fifth of the input protein was retained on the beads in both cases
PMID:11387325	PBO:0111635	The novel finding was that the recombinant S. pombe RNA triphosphatase by itself bound specifically to CTD peptides phosphorylated on Ser-5 and not to the unphosphorylated peptide or the Ser2-PO4 peptide (Fig. 3B).
PMID:11387325	PBO:0111636	The key findings were that the S. pombe guanylyltransferase bound equally well to the CTD Ser5-PO4 peptide and the Ser2-PO4/Ser5-PO4 peptide. Slightly less than one-fifth of the input protein was retained on the beads in both cases
PMID:11387325	PBO:0111612	To gauge the role of the non-reiterated protein segment, we constructed an AD-Rpb1(1516 -1752) fusion clone and tested it in a directed two-hybrid assay paired with BD-Pce1 and BD- Pct1. We found that the Rpb1 interaction with both capping enzymes persisted when the AD fusion contained little more than the CTD repeats per se.
PMID:11387325	PBO:0111613	To gauge the role of the non-reiterated protein segment, we constructed an AD-Rpb1(1516 -1752) fusion clone and tested it in a directed two-hybrid assay paired with BD-Pce1 and BD- Pct1. We found that the Rpb1 interaction with both capping enzymes persisted when the AD fusion contained little more than the CTD repeats per se.
PMID:11389847	PBO:0114389	(Fig. 5A)
PMID:11389847	PBO:0114389	(Fig. 2)
PMID:11389847	FYPO:0006279	(Fig. 5A)
PMID:11389847	FYPO:0006279	(Fig. 5A)
PMID:11389847	FYPO:0006279	(Fig. 5A)
PMID:11405625	PBO:0019133	(comment: CHECK high penetrance = large fraction of cells)
PMID:11414703	FYPO:0002059	One of the diploid clones (C1) was allowed to sporulate and ;100 of the haploids obtained were tested for resistance to G418. We found no resistants, which implicates that spSNW1 is an essential gene in S. pombe.
PMID:11432827	FYPO:0000416	(comment: cut2 levels were reduced in alp14 mutant)
PMID:11432827	FYPO:0004318	(comment: Question could be required for, or upstream spindle checkpoint, but it could cause a problem which preceds the point where it is possible to activate the checkpoint?BUT...alp14 and mad2 in same pathway and overexpression of mad2 cannot resuce defect of double/single mutant)
PMID:11432827	PBO:0033178	(Figure 4B)
PMID:11432827	PBO:0093562	(Figure 4A)
PMID:11432827	FYPO:0001491	(Figure 2C)
PMID:11432827	FYPO:0002060	(Figure 2C)
PMID:11432827	FYPO:0004317	(Figure 1A)
PMID:11432827	FYPO:0000131	(Figure 1A)
PMID:11432827	FYPO:0000324	(Figure 3F)
PMID:11432827	FYPO:0003165	(Figure 3B)
PMID:11432827	FYPO:0002061	(Figure 3A) (comment: rapid loss of viability)
PMID:11432827	FYPO:0002061	(Table 1)
PMID:11432827	FYPO:0000141	(Figure 1A)
PMID:11432827	GO:0000940	(comment: dependent on mitotic spindle)
PMID:11432827	FYPO:0001574	(Figure 1A)
PMID:11432827	FYPO:0000276	(Figure 1C)
PMID:11432827	FYPO:0001734	(Figure 1C)
PMID:11432827	FYPO:0006196	(Figure 1C)
PMID:11448769	PBO:0019801	(comment vw: sid2 phenotype indicates that Clp1 localization is independent of SIN)
PMID:11460168	PBO:0112762	(Fig. 3B)
PMID:11460168	PBO:0112427	Importantly, we found that synchronized Datf1 cells completely failed to arrest nuclear division in the presence of Lat B (Fig. 4d)
PMID:11460168	FYPO:0009019	(Fig. 4D)
PMID:11460168	PBO:0112765	(Fig. 4B)
PMID:11460168	PBO:0112430	(Fig. 4F)
PMID:11460168	FYPO:0001357	(Fig. 4A)
PMID:11460168	PBO:0112429	(Fig. 4A)
PMID:11460168	FYPO:0006660	(Fig. 4E)
PMID:11460168	PBO:0112763	(Fig. 3B)
PMID:11460168	PBO:0112762	(Fig. 3B)
PMID:11460168	PBO:0112764	(Fig. 4B)
PMID:11460168	FYPO:0000620	Cells that lack Mad2 arrest in metaphase in the presence of Lat B (Fig. 3a)
PMID:11460168	FYPO:0009019	(Fig. 2D)
PMID:11460168	PBO:0112427	We found that a rad21-45 mutant was unable to arrest in the presence of Lat B. Fig. 2B and C
PMID:11460168	PBO:0112426	(Fig. 2C)
PMID:11460168	PBO:0116865	(Fig. 2B)
PMID:11460168	PBO:0112424	(Fig. 1E and F)
PMID:11493649	GO:0051446	(comment: CHECK positive regulation of meiotic cell cycle exit)
PMID:11493649	GO:0051447	(comment: CHECK negative regulation of meiotic exit)
PMID:11509236	FYPO:0000426	After 15 min, vacuoles were visible in all three strains, and this observation demonstrates that, as in budding yeast [8, 9], endocytosis does not require a functional type V myosin.
PMID:11509236	FYPO:0002792	vacuoles in myo52Δ were smaller (0.21 ± 0.14 μm). (Figure 1)
PMID:11509236	FYPO:0000426	After 15 min, vacuoles were visible in all three strains, and this observation demonstrates that, as in budding yeast [8, 9], endocytosis does not require a functional type V myosin.
PMID:11514435	PBO:0098118	(Fig. 6)
PMID:11514435	PBO:0098115	(Figure 5D)
PMID:11514435	PBO:0098116	(Figure 5E) (comment: to membrane)
PMID:11514435	GO:0052712	(Figure 7b) (comment: heterologous complementation)
PMID:11514435	FYPO:0005485	(Figure 7b)
PMID:11514435	FYPO:0005485	(Figure 7b)
PMID:11514435	GO:0005886	(Figure 4D,5)
PMID:11514435	GO:0071944	(Figure 5)
PMID:11514435	GO:0016020	(Figure 4D)
PMID:11514435	PBO:0098114	(Figure 1, 3B; Table 2)
PMID:11514435	FYPO:0001489	(Figure 2a)
PMID:11514435	FYPO:0002061	(Figure 2a)
PMID:11514435	FYPO:0002061	(Figure 2a)
PMID:11514435	FYPO:0002627	(Figure 1)
PMID:11514435	GO:0052714	(Figure 7D) (comment: assayed reaction products)
PMID:11514435	GO:0046513	(comment: from MF)
PMID:11514435	GO:0046521	(comment: from MF)
PMID:11514435	PBO:0098117	(Fig. 6)
PMID:11514435	PBO:0098115	(Figure 5E)
PMID:11514435	PBO:0098113	(Figure 1, 3B; Table 2)
PMID:11514436	PBO:0094971	(comment: asymetric localization is normal)
PMID:11514436	FYPO:0002061	(Figure 3a)
PMID:11514436	FYPO:0002024	(Figure 3b)
PMID:11514436	FYPO:0002061	(Figure 3a)
PMID:11514436	FYPO:0002024	(Figure 3b)
PMID:11514436	FYPO:0002024	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0006023	(Figure 2b)
PMID:11514436	FYPO:0002024	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	(comment: SID PHENOTYPE) (Figure 2B).
PMID:11514436	FYPO:0001357	(Figure 1C, lane 8
PMID:11514436	FYPO:0002024	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002151	Thefact that out of almost 200 tetrads analyzed, not a single ura spore survived confirmed that spg1 is essential for vegetative growth, and this essential function cannot be bypassed by inactivating par1 and par2 by deletion.
PMID:11514436	PBO:0105022	(comment: dns)
PMID:11514436	PBO:0113871	(Figure 4a)
PMID:11514436	FYPO:0001120	(Figure 4a)
PMID:11514436	FYPO:0002061	(Figure 3a)
PMID:11514436	FYPO:0002061	(Figure 2A).
PMID:11514436	FYPO:0002024	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	Table 2, par1/2 does not supress sin phenotype
PMID:11553781	PBO:0103159	(comment: vw: changed from response to chemical to part of DNA damage checkpoint signalling)
PMID:11553781	PBO:0103157	Rad3 phosphorylates S345 in response to DNA damage caused by ionizing radiation
PMID:11554922	FYPO:0000188	(comment: evidence: immunoblot using antibody that recognizes thymine dimers)
PMID:11598020	GO:0005721	(Fig. 4a)
PMID:11598020	PBO:0106461	(Fig. 4a)
PMID:11598020	PBO:0106460	(Fig. 4a)
PMID:11598020	GO:0005634	(Fig. 4a)
PMID:11598020	GO:0005721	(Fig. 4a)
PMID:11600706	GO:0005515	(Fig. 2B)
PMID:11600706	PBO:0111729	(comment: vw: in vitro purification system)
PMID:11600706	PBO:0111728	(comment: vw: in vitro purification system)
PMID:11600706	PBO:0111727	(comment: vw: in vitro purification system)
PMID:11600706	FYPO:0002778	(Figure 1C)
PMID:11600706	FYPO:0005934	(Figure 1C)
PMID:11600706	MOD:01149	(Figure 3B)
PMID:11600706	GO:0005515	(Fig. 2B)
PMID:11606752	PBO:0098344	(comment: CHECK level of mutant cdc18deltaCDK1-5 protein)
PMID:1165770	PBO:0093712	(comment: CHECK cdc9-50 is the original name for wee1-50 allele. It was changed in subsequent publications to wee1 because of its phenotype and there is now no cdc9 gene)
PMID:1165770	PBO:0093712	(Table 1)
PMID:1165770	PBO:0102251	(Figure 3)
PMID:1165770	PBO:0102250	Table 1, Figure 2
PMID:1165770	PBO:0102252	(Table 1)
PMID:1165770	PBO:0102253	(Table 1)
PMID:11676915	PBO:0095732	(Figure 6)
PMID:11676915	PBO:0095733	(Figure 6)
PMID:11676915	PBO:0095725	(comment: scaffold, platform)
PMID:11676915	PBO:0095726	(comment: scaffold, platform)
PMID:11676915	PBO:0095727	(comment: scaffold, platform)
PMID:11676915	PBO:0095721	(Figure 6)
PMID:11676915	PBO:0095728	(Figure 6)
PMID:11676915	PBO:0018634	(Figure 3b)
PMID:11676915	PBO:0018346	(Figure 3b)
PMID:11676915	PBO:0095723	(Fig. 5a)
PMID:11676915	PBO:0094089	(Fig. 5c)
PMID:11676915	FYPO:0000941	dns
PMID:11676915	PBO:0095724	(comment: scaffold, platform)
PMID:11676915	PBO:0094918	(Figure 6)
PMID:11676915	PBO:0095731	(Figure 6)
PMID:11676915	PBO:0095718	(Fig. 1a)
PMID:11676915	FYPO:0002912	(Fig. 1a)
PMID:11676915	FYPO:0001368	(Fig. 1a)
PMID:11676915	PBO:0095729	(Figure 6)
PMID:11676915	PBO:0095730	(Figure 6)
PMID:11676924	GO:0140445	(comment: colocalizes with this region and taz1, abnormal localization in taz1-delta, and physically associates with taz1)
PMID:11676924	GO:0000723	(comment: same_pathway)
PMID:11683390	PBO:0037409	(Fig. 2A b-c, 5) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	PBO:0037148	(Fig. 2A b-c, 5) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	PBO:0037408	(Fig. 2A b-c, 5) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	PBO:0018634	(Fig. 2A b-c, 5D) (comment: pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	PBO:0023023	(Fig. 2A b-c, 5D) (comment: pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	PBO:0037404	(Fig. 2A, 2B, 4C) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF)) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	PBO:0021746	(Fig. 2A, 2B, 4C) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF)) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	PBO:0021499	(Fig. 2A, 2B, 4C) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF)) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	PBO:0037406	(Fig. 2A, 2B, 4C) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF)) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	PBO:0018712	(Fig. 2A, 2B, 4C) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF)) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	PBO:0037405	(Fig. 2A, 2B, 4C) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF)) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	PBO:0037407	(Fig. 2A, 2B, 4C) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF)) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	PBO:0019070	(Fig. 2A) (comment: pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF))
PMID:11683390	PBO:0022133	(Fig. 2A) (comment: pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF))
PMID:11683390	PBO:0106307	(Fig. 7)
PMID:11683390	PBO:0106306	(Fig. 7)
PMID:11683390	PBO:0037426	(Fig. 7)
PMID:11683390	PBO:0037423	(Fig. 8)
PMID:11683390	GO:0000776	cdc2 is localised at the centromeres during horse tail movement. Fig 9 shows that cdc2YFP is associated with cen1GFP
PMID:11683390	PBO:0037421	(Fig. 7) (comment: do not actually say it is associated with SPB just SPB region, i.e. telomere-SPB- centromere bouquet cluster)
PMID:11683390	PBO:0106305	(Fig. 6) Cdc13YFP and Cdc2YFP remain associated with spindle, SPB. Cdc13 is not degraded by defective proteasome. Rpt1 is called Mts2 in this paper
PMID:11683390	PBO:0106305	(Fig. 6) Cdc13YFP and Cdc2YFP remain associated with spindle, SPB. Cdc13 is not recognised by defective APC
PMID:11683390	PBO:0106305	(Fig. 6) Cdc2YFP and non-degradable Cdc13YFP remain associated with spindle, SPB.Cdc13 degradation is abolished rather than delayed
PMID:11683390	PBO:0037419	(Fig. 6)
PMID:11683390	PBO:0106300	(Figure 4A) (comment: Cdc13YFP expressed from integrated pREP45.) Decreased nuclear import of cdc2YFP compared to cdc13delta cig1delta mutant
PMID:11683390	PBO:0106301	(Figure 4B) (comment: Cdc13YFP expressed from integrated pREP45)
PMID:11683390	PBO:0106304	Data not shown. (comment: Cdc2 does not go prematurely to the SPB in a cut12 mutant (this is the stf1-1 mutant))
PMID:11683390	PBO:0106301	(Figure 4A) (comment: Cdc13YFP expressed from integrated pREP45.)
PMID:11683390	PBO:0106300	(Figure 4A) (comment: Cdc13YFP expressed from integrated pREP45)
PMID:11683390	PBO:0106299	(Figure 4A)
PMID:11683390	PBO:0037412	(Fig. 2C) (comment: pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	PBO:0021007	(Fig. 2A, 3, 5D) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	PBO:0037411	(Fig. 2A, 3, 5D) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	PBO:0021007	(Fig. 2A, 3, 5D) (comment: pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	PBO:0037411	(Fig. 2A, 3, 5D) (comment: pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	PBO:0021770	(Fig. 2A, 2B) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	PBO:0018999	(Fig. 2A) (comment: pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF))
PMID:11683390	PBO:0018677	(Fig. 2A) (comment: pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF))
PMID:11683390	PBO:0037148	(Fig. 2A b-c, 5D) (comment: pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	PBO:0037410	(Fig. 2A, 2B) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	PBO:0018999	(Fig. 2A, 2B) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	PBO:0022133	(Fig. 2A, 2B) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	PBO:0019070	(Fig. 2A, 2B) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	PBO:0024116	(Fig. 2A, 2B) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	PBO:0023023	(Fig. 2A b-c, 5) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11685532	GO:0000776	(comment: mitotic, in meiosis it is only n the kinetochore during meitoic division(metaphase/anaphase) not during prophase)
PMID:11694585	GO:0051015	(comment: assayed using purified rabbit skeletal muscle F-actin)
PMID:11694585	FYPO:0002437	(comment: temperature permissive for cdc4-8)
PMID:11694585	FYPO:0003315	(comment: temperature restrictive for cdc4-8)
PMID:11694585	PBO:0019147	(comment: various abnormal shapes)
PMID:11694585	FYPO:0002061	(comment: CONDITION 30 degrees C)
PMID:11694585	FYPO:0002023	(comment: CONDITION 27 degrees C)
PMID:11694585	FYPO:0004257	(comment: CONDITION 27 degrees C)
PMID:11694585	PBO:0019147	(comment: various abnormal shapes)
PMID:11694585	FYPO:0002061	(comment: CONDITION 30 degrees C)
PMID:11694585	GO:0030479	(comment: dependent on actin cytoskeleton (assayed using Latrunculin A))
PMID:11694585	GO:0032153	(comment: dependent on actin cytoskeleton (assayed using Latrunculin A))
PMID:11694585	GO:0051017	in vitro bundling, detected by microscopy; Figure 2
PMID:11694585	FYPO:0004257	(comment: CONDITION 27 degrees C)
PMID:11696322	FYPO:0003315	(Figure 3b-g)
PMID:11696322	FYPO:0001368	(Figure 3f,g)
PMID:11696322	PBO:0104462	(Figure 3b-g,i)
PMID:11696322	FYPO:0002021	(Figure 3b-g,i)
PMID:11696322	FYPO:0002401	(Figure 4, table 1)
PMID:11696322	FYPO:0003225	(Table 1)
PMID:11696322	FYPO:0003193	(Table 1)
PMID:11696322	PBO:0018345	(Figure 5a)
PMID:11696322	PBO:0022665	(Figure 5b,c)
PMID:11696322	PBO:0104463	(Figure 5e)
PMID:11696322	FYPO:0001367	(Figure 3f,g)
PMID:11696322	FYPO:0001234	data not shown
PMID:11696322	FYPO:0000016	(Figure 3)
PMID:11719193	GO:0008821	(comment: magneisum activated_by CHEBI:18420)
PMID:11737264	FYPO:0005103	(comment: population is viable but sick; can't tell which individual cells are viable)
PMID:11737264	FYPO:0007436	(comment: population is viable but sick, and the elongated multiseptate cells are probably dead)
PMID:11737264	PBO:0019176	(comment: population grows well, but very small cells look lysed)
PMID:11737264	FYPO:0000021	(comment: population is viable but sick; can't tell which individual cells are viable)
PMID:11737264	FYPO:0000647	(comment: population is viable but sick; can't tell which individual cells are viable, but very small cells look lysed)
PMID:11737264	PBO:0019176	(comment: population is viable, but very small cells look lysed)
PMID:11739790	FYPO:0004511	(Figure 4B and D)
PMID:11739790	PBO:0105588	(comment: arrested)
PMID:11739790	PBO:0105588	(comment: arrested)
PMID:11739790	PBO:0105588	(comment: arrested)
PMID:11739790	FYPO:0004511	(Figure 4B and D)
PMID:11739790	FYPO:0002060	(Figure 2, Table 2)
PMID:11777938	FYPO:0005322	(Figure 2)
PMID:11777938	FYPO:0000620	(comment: CHECK NORMAL LENGTH)
PMID:11780129	PBO:0112302	Psc3 localization was strikingly disrupted in the swi6∆ strain at both loci (Fig. 1b).
PMID:11780129	PBO:0112305	(Fig. 2a, b).
PMID:11780129	PBO:0112558	psc3-1T also displays the lagging-chromosome phenotype and mis-segregated the mini-chromosome Ch16 (ref. 17) at a higher rate than the wild type, mimicking the swi6∆ phenotype (Fig. 2a, b).
PMID:11780129	PBO:0112306	(Fig. 2a, b).
PMID:11780129	PBO:0112307	we found that cohesin mutants (psc3-1T, psc3-2T, psc3-4T and rad21-K1) produced switching-defective colonies at a rate nearly 100-fold that of the wild type (Fig. 3a,b).
PMID:11780129	GO:0005721	Interestingly, we found that Psc3 is enriched at the heterochromatic locations containing Swi6, such as the silent mating-type locus and the centromeric repeats (Fig. 1b, c, wild type).
PMID:11780129	FYPO:0002360	We consistently observed that psc3-4T and the other psc3 mutant alleles had no detectable effect on the silencing of a marker gene inserted at either centromeric (otr1R::ura4+) repeats or in the silent mating-type (Kint2::ura4+) region (see Supplementary Information).
PMID:11780129	FYPO:0002336	We consistently observed that psc3-4T and the other psc3 mutant alleles had no detectable effect on the silencing of a marker gene inserted at either centromeric (otr1R::ura4+) repeats or in the silent mating-type (Kint2::ura4+) region (see Supplementary Information).
PMID:11780129	PBO:0112301	Psc3 localization was strikingly disrupted in the swi6∆ strain at both loci (Fig. 1b).
PMID:11780129	GO:0031934	Interestingly, we found that Psc3 is enriched at the heterochromatic locations containing Swi6, such as the silent mating-type locus and the centromeric repeats (Fig. 1b, c, wild type).
PMID:11780129	GO:0031934	Interestingly, we found that Psc3 is enriched at the heterochromatic locations containing Swi6, such as the silent mating-type locus and the centromeric repeats (Fig. 1b, c, wild type).
PMID:11780129	FYPO:0000228	(Figure 2b)
PMID:11780129	PBO:0120506	shown), and the association with otr and KR was much reduced (Fig. 1d).
PMID:11780129	PBO:0112301	Psc3 localization was strikingly disrupted in the swi6∆ strain at both loci (Fig. 1b).
PMID:11780129	PBO:0112302	Psc3 localization was strikingly disrupted in the swi6∆ strain at both loci (Fig. 1b).
PMID:11780129	PBO:0112307	we found that cohesin mutants (psc3-1T, psc3-2T, psc3-4T and rad21-K1) produced switching-defective colonies at a rate nearly 100-fold that of the wild type (Fig. 2a,b).
PMID:11780129	PBO:0112559	psc3-1T also displays the lagging-chromosome phenotype and mis-segregated the mini-chromosome Ch16 (ref. 17) at a higher rate than the wild type, mimicking the swi6∆ phenotype (Fig. 2a, b).
PMID:11780129	GO:0005721	Interestingly, we found that Psc3 is enriched at the heterochromatic locations containing Swi6, such as the silent mating-type locus and the centromeric repeats (Fig. 1b, c, wild type).
PMID:11780129	PBO:0110924	However, this mutation did not affect Swi6 localization at otr and KR (Fig. 1e).
PMID:11780129	PBO:0112307	we found that cohesin mutants (psc3-1T, psc3-2T, psc3-4T and rad21-K1) produced switching-defective colonies at a rate nearly 100-fold that of the wild type (Fig. 2a,b).
PMID:11780129	FYPO:0000228	Moreover, the psc3+-GFP swi6∆ cells showed increased mini-chromosome loss and exhibited a high incidence of lagging chromosome and other chromosome segregation abnormalities (Fig. 2c)
PMID:11780129	PBO:0112308	(Fig. 3b, data not shown)
PMID:11780129	PBO:0112307	we found that cohesin mutants (psc3-1T, psc3-2T, psc3-4T and rad21-K1) produced switching-defective colonies at a rate nearly 100-fold that of the wild type (Fig. 3a,b).
PMID:11781565	PBO:0106293	(Fig. 4D)
PMID:11781565	PBO:0106294	(Fig 4E)
PMID:11781565	PBO:0106278	(Fig. 1B)
PMID:11781565	FYPO:0002061	(Fig. 5) res1+ is unable to rescue the pat1-114 mutant at low levels of over expression
PMID:11781565	PBO:0106291	(Fig. 2B)
PMID:11781565	PBO:0106290	(Fig. 2B)
PMID:11781565	PBO:0106289	(Fig. 2B)
PMID:11781565	PBO:0106288	(Fig. 2B)
PMID:11781565	PBO:0106286	(Fig. 1C) 5 fold increase in HU compared to no HU. res1 and lacZ fusion on episomal plasmids
PMID:11781565	PBO:0106287	(Fig. 1C) no increase in presence of HU compared to no HU when all MCB elements are removed. res1 and lacZ fusion on episomal plasmids
PMID:11781565	PBO:0106286	(Fig. 1C) Shows 5 fold increase in presence of HU compared to no HU. res1 and lacZ fusion on episomal plasmids
PMID:11781565	PBO:0106285	Data not shown 20 fold increase in response to res1 oe. res1 and lacZ fusion on episomal plasmids
PMID:11781565	PBO:0106284	data not shown 8 fold increase in response to res1 oe. res1 and lacZ fusion on episomal plasmids
PMID:11781565	PBO:0106283	(Fig. 1B)
PMID:11781565	PBO:0106282	(Fig. 1B)
PMID:11781565	PBO:0106281	(Fig. 1B)
PMID:11781565	PBO:0106280	(Fig. 1B)
PMID:11781565	PBO:0106279	(Fig. 1B)
PMID:11781565	PBO:0106278	(Fig. 1B)
PMID:11781565	PBO:0106277	(Fig. 1B)
PMID:11781565	FYPO:0006762	(Fig. 2B)
PMID:11781565	PBO:0109006	(Fig. 2B)
PMID:11781565	PBO:0096413	(Fig. 7B) res1S130A prevents the normal down regulation of MBF dependent transcription by res1+
PMID:11781565	PBO:0096409	(Fig. 7B) res1S130A prevents the normal down regulation of MBF dependent transcription by res1+
PMID:11781565	PBO:0098713	(Fig. 7B) res1S130A prevents the normal down regulation of MBF dependent transcription by res1+
PMID:11781565	PBO:0105915	(Fig. 6)
PMID:11781565	PBO:0106293	(Fig. 4D)
PMID:11781565	PBO:0106292	(Fig. 3A)
PMID:11781565	PBO:0106292	(Fig. 3B)
PMID:11781565	PBO:0106292	(Fig. 3B)
PMID:11781565	PBO:0106293	(Fig. 4D)
PMID:11781565	FYPO:0002060	(Fig. 5) res1-S130A can rescue the pat1-114 mutant at low levels of over expression
PMID:11792803	PBO:0093462	(Fig. 6)
PMID:11792803	PBO:0093462	(Fig. 6)
PMID:11792803	FYPO:0005738	(Figure 2b)
PMID:11792803	FYPO:0004255	(Figure 2b)
PMID:11792803	FYPO:0000276	(Figure 2b) chromsome detached from spindle
PMID:11792803	PBO:0033839	(Fig. 8)
PMID:11792803	PBO:0093462	(Fig. 6)
PMID:11792803	PBO:0092680	(Fig. 8)
PMID:11792803	PBO:0023853	(Fig. 8)
PMID:11792803	FYPO:0005739	(Figure 2b)
PMID:11792803	FYPO:0003758	(Figure 2a) ( stretched chromaitn along elongating spindle at anaphase B)
PMID:11818066	FYPO:0002052	(comment: not really sure freq is normal, because wt not shown, but text suggests it's close)
PMID:11818066	FYPO:0002060	does not undergo meiosis under conditions where pat1-114 single mutant does
PMID:11839792	PBO:0110538	56% of sar1-1, 68% of sec31-1, and 50% of pmm1-1 cells had accumulated ER membranes and dilated nuclear and ER lumens (Table 1).
PMID:11839792	PBO:0110537	56% of sar1-1, 68% of sec31-1, and 50% of pmm1-1 cells had accumulated ER membranes and dilated nuclear and ER lumens (Table 1).
PMID:11839792	PBO:0110536	Pap1p was localized predominantly to the cytoplasm in wild-type cells (Fig. 5A) as well as in the sar1-1, sec31-1 and pmm1- 1 mutants grown at the restrictive temperature, suggesting that nuclear protein export was not adversely affected in these cells (Fig. 5C,E,G).
PMID:11839792	PBO:0110536	Pap1p was localized predominantly to the cytoplasm in wild-type cells (Fig. 5A) as well as in the sar1-1, sec31-1 and pmm1- 1 mutants grown at the restrictive temperature, suggesting that nuclear protein export was not adversely affected in these cells (Fig. 5C,E,G).
PMID:11839792	PBO:0110535	Pap1p was localized predominantly to the cytoplasm in wild-type cells (Fig. 5A) as well as in the sar1-1, sec31-1 and pmm1- 1 mutants grown at the restrictive temperature, suggesting that nuclear protein export was not adversely affected in these cells (Fig. 5C,E,G).
PMID:11839792	PBO:0110535	Pap1p was localized predominantly to the cytoplasm in wild-type cells (Fig. 5A) as well as in the sar1-1, sec31-1 and pmm1- 1 mutants grown at the restrictive temperature, suggesting that nuclear protein export was not adversely affected in these cells (Fig. 5C,E,G).
PMID:11839792	PBO:0110535	Pap1p was localized predominantly to the cytoplasm in wild-type cells (Fig. 5A) as well as in the sar1-1, sec31-1 and pmm1- 1 mutants grown at the restrictive temperature, suggesting that nuclear protein export was not adversely affected in these cells (Fig. 5C,E,G).
PMID:11839792	PBO:0110534	Pap1p was localized predominantly to the cytoplasm in wild-type cells (Fig. 5A) as well as in the sar1-1, sec31-1 and pmm1- 1 mutants grown at the restrictive temperature, suggesting that nuclear protein export was not adversely affected in these cells (Fig. 5C,E,G).
PMID:11839792	PBO:0110533	56% of sar1-1, 68% of sec31-1, and 50% of pmm1-1 cells had accumulated ER membranes and dilated nuclear and ER lumens (Table 1).
PMID:11839792	PBO:0110532	56% of sar1-1, 68% of sec31-1, and 50% of pmm1-1 cells had accumulated ER membranes and dilated nuclear and ER lumens (Table 1).
PMID:11839792	PBO:0110531	56% of sar1-1, 68% of sec31-1, and 50% of pmm1-1 cells had accumulated ER membranes and dilated nuclear and ER lumens (Table 1).
PMID:11839792	PBO:0110530	56% of sar1-1, 68% of sec31-1, and 50% of pmm1-1 cells had accumulated ER membranes and dilated nuclear and ER lumens (Table 1).
PMID:11839792	PBO:0110529	56% of sar1-1, 68% of sec31-1, and 50% of pmm1-1 cells had accumulated ER membranes and dilated nuclear and ER lumens (Table 1).
PMID:11839792	PBO:0110528	19% were septated, binucleated cells with condensed chromosomes. (comment: vw:2c binucleate? should this be WT knockdown?)
PMID:11839792	FYPO:0002280	These data confirm that pmm1 is an essential gene. Microscopic examination of the tetrad dissection plates revealed that, of 54 pmm1 null spores examined, 98% germinated. Of these, 52% formed single, rounded cells and 47% arrested as single, septated cells.
PMID:11839792	PBO:0110526	sar1, sec31 and pmm1 are essential genes vw:2c binucleate? should this be WT knockdown?
PMID:11839792	FYPO:0002061	sar1, sec31 and pmm1 are essential genes
PMID:11839792	FYPO:0002061	sar1, sec31 and pmm1 are essential genes
PMID:11839792	FYPO:0002061	sar1, sec31 and pmm1 are essential genes
PMID:11839792	FYPO:0003935	The glycosylation profile of acid phosphatase in sec31-1 cells also revealed a block in secretion from the ER (Fig. 2B). In sec31-1 cells at 25°C (Fig. 2B, lane 3), a low level of the 72 kDa form of acid phosphatase (arrow) and high molecular weight smears indicated normal protein secretion. However, sec31-1 cells incubated at 36°C for 4 hours, accumulated a high level of the 72 kDa ER form of acid phosphatase (Fig. 2B, lane 4), indicating that protein secretion from the ER is inhibited
PMID:11839792	FYPO:0003935	In sar1-1 cells, acid phosphatase accumulated in its 72 kDa core glycosylated form (arrow) even at 25°C (Fig. 2A, lane 5), and this form increased in abundance upon incubation at 36°C (Fig. 2A, lanes 6-8), indicating a block in its secretion from the ER
PMID:11839792	PBO:0110540	56% of sar1-1, 68% of sec31-1, and 50% of pmm1-1 cells had accumulated ER membranes and dilated nuclear and ER lumens (Table 1).
PMID:11839792	PBO:0110539	56% of sar1-1, 68% of sec31-1, and 50% of pmm1-1 cells had accumulated ER membranes and dilated nuclear and ER lumens (Table 1).
PMID:11854402	PBO:0101936	(comment: CHECK during premeiotic DNA replication)
PMID:11854402	PBO:0099076	(comment: CHECK during premeiotic DNA replication)
PMID:11854402	PBO:0101937	(comment: CHECK during premeiotic DNA replication)
PMID:11854402	PBO:0101936	(comment: CHECK during premeiotic DNA replication)
PMID:11854402	PBO:0101936	(comment: CHECK during premeiotic DNA replication)
PMID:11854409	FYPO:0003440	(Fig. 2, 3)
PMID:11854409	PBO:0097222	(Fig. 1A) (comment: CHECK inviable)
PMID:11854409	GO:0005515	(comment: UPR)
PMID:11854409	FYPO:0006558	(Fig. 2, 3)
PMID:11854409	GO:0005515	(comment: UPR)
PMID:11854409	GO:0005515	(comment: UPR)
PMID:11854409	GO:0005515	(Figure 5C)
PMID:11854409	GO:0005515	(Figure 5B)
PMID:11854409	GO:0005515	(Figure 5A)
PMID:11856374	FYPO:0002061	(comment: Loss of cia1+ led to a lethal phenotype)
PMID:11861551	FYPO:0002061	(Fig. 7a)
PMID:11861551	FYPO:0000229	(Fig. 7a)
PMID:11861551	FYPO:0000131	(Fig. 4)
PMID:11861551	GO:0000776	(Figure 7)
PMID:11861551	FYPO:0004101	(Fig. 4)
PMID:11861551	FYPO:0004101	(Fig. 4)
PMID:11861551	FYPO:0003286	(Fig. 4c)
PMID:11861551	PBO:0097993	(Fig. 3)
PMID:11861551	PBO:0035224	(Fig. 3)
PMID:11861551	PBO:0023853	(Fig. 1a)
PMID:11861551	PBO:0022963	(Fig. 1)
PMID:11861551	GO:0005634	(Fig. 1a)
PMID:11861551	GO:1990023	(Figure 7)
PMID:11861551	PBO:0112057	(Fig. 7)
PMID:11861765	FYPO:0002061	(Fig. 8B)
PMID:11861765	PBO:0105971	(Fig. 7C)
PMID:11861765	PBO:0105970	(Fig. 7B)
PMID:11861765	FYPO:0000581	(Fig. 5B)
PMID:11861765	FYPO:0000925	(Fig. 5A)
PMID:11861765	PBO:0033665	(Fig. 3C)
PMID:11861765	FYPO:0002061	(Fig. 3B)
PMID:11861765	PBO:0093562	(Fig. 3A)
PMID:11861765	FYPO:0002578	(Fig. 2B)
PMID:11861765	PBO:0093586	(Fig. 2B)
PMID:11861765	PBO:0093617	(Fig. 2B)
PMID:11861765	PBO:0105969	(Fig. 2A)
PMID:11861765	PBO:0093629	(Fig. 2)
PMID:11861765	FYPO:0002060	(Fig. 1)
PMID:11861765	PBO:0033209	(Fig. 4B,C)
PMID:11861765	FYPO:0000141	(Fig. 4D)
PMID:11861765	FYPO:0001234	(Fig. 4D)
PMID:11861765	PBO:0035685	(Fig. 4B,C)
PMID:11861765	FYPO:0001779	(Fig. 3D)
PMID:11861765	FYPO:0003241	(Fig. 4B)
PMID:11861765	FYPO:0000141	(Fig. 8C)
PMID:11861765	FYPO:0000839	(Fig. 8C)
PMID:11861765	PBO:0096828	(Fig. 4A)
PMID:11861765	FYPO:0001779	(Fig. 3D)
PMID:11861765	FYPO:0004507	(Fig. 3C)
PMID:11861765	FYPO:0001513	(Fig. 3C)
PMID:11861765	FYPO:0003165	(Fig. 3C)
PMID:11861765	FYPO:0001234	(Fig. 8B)
PMID:11861765	PBO:0035688	(Fig. 8A)
PMID:11861905	PBO:0092180	(Figure 1a)
PMID:11861905	FYPO:0007627	The 210-nt region resides downstream of the distal poly(A) site and it is not included in the mature rrg1+ mRNA, in contrast to other regulatory elements for post-transcriptional control. However, some recent studies on S.pombe have shown that RNA pol II transcription proceeds beyond the poly(A) site and that the downstream sequences located in the 3′ noncoding region are responsible for transcription termination and mRNA 3′-end formation, which are closely coupled to efficient gene expression
PMID:11861905	PBO:0092337	(Figure 1a)
PMID:11870212	PBO:0023853	(Fig. 3B)
PMID:11870212	PBO:0033837	(Fig. 3B)
PMID:11870212	PBO:0108184	(Fig. 3B)
PMID:11870212	FYPO:0000141	(comment: movement in anap[hase A)
PMID:11870212	PBO:0023853	(Fig. 3B)
PMID:11870212	PBO:0033837	(Fig. 3B)
PMID:11870212	PBO:0108184	(Fig. 3B)
PMID:11882285	PBO:0102360	(Fig. 5a)
PMID:11882285	PBO:0102359	S1
PMID:11882285	FYPO:0000091	(Fig. 2D)
PMID:11882285	FYPO:0001532	(Fig. 1)
PMID:11882285	FYPO:0000274	(Fig. 1)
PMID:11882285	FYPO:0000639	(Fig. 1)
PMID:11882285	FYPO:0003307	(Fig. 1)
PMID:11882285	PBO:0102358	(Fig. 1C)
PMID:11882285	PBO:0094474	(Fig. 1) (3-4um normal metaphese lenght 2-2.5 um
PMID:11882285	PBO:0023558	(Fig. 4)
PMID:11882285	FYPO:0000091	(Fig. 2D)
PMID:11882285	PBO:0102359	S1
PMID:11882285	PBO:0102359	S1
PMID:11882285	PBO:0102359	S1
PMID:11882285	PBO:0092680	(Figure 3)
PMID:11882285	PBO:0102361	(Fig. 5a) (comment: ie wt like)
PMID:11884512	FYPO:0000268	(Figure 3C)
PMID:11884512	FYPO:0000097	data not shown
PMID:11884512	FYPO:0001253	(Fig. 3B)
PMID:11884512	PBO:0098732	NEM, which inhibit the Pmt3-processing activity of Ulp1, and the serine protease inhibitor PMSF, have no effect on Pmt3 deconjugating activity
PMID:11884512	PBO:0099111	Of the inhibitors we tested, only iodoacetamide (10 mM) and NEM (10 mM) inhibited Ulp1 activity
PMID:11884512	PBO:0093629	(comment: same as rad17 single mutant, epistatic)
PMID:11884512	PBO:0095634	data not shown
PMID:11884604	PBO:0098977	(comment: not much evidence of specificity for H3 vs. H4 or position)
PMID:11884604	PBO:0114597	(comment: broad specificity;) actually inferred from combination of phenotype and sequence similarity
PMID:11884604	PBO:0114598	(comment: broad specificity;) actually inferred from combination of phenotype and sequence similarity
PMID:11884604	PBO:0114599	(comment: broad specificity;) actually inferred from combination of phenotype and sequence similarity
PMID:11884604	PBO:0114600	(comment: broad specificity;) actually inferred from combination of phenotype and sequence similarity
PMID:11884604	PBO:0114596	actually inferred from combination of phenotype and sequence similarity
PMID:11884604	PBO:0114595	actually inferred from combination of phenotype and sequence similarity
PMID:11884604	GO:0000785	(comment: CHECK not (coincident_with(SO:0001789) | coincident_with(SO:0001795)))
PMID:11884604	PBO:0114603	(comment: broad specificity;) actually inferred from combination of phenotype and sequence similarity
PMID:11884604	PBO:0114602	(comment: broad specificity;) actually inferred from combination of phenotype and sequence similarity
PMID:11884604	PBO:0114596	(comment: broad specificity;) actually inferred from combination of phenotype and sequence similarity
PMID:11884604	GO:0004407	actually inferred from combination of phenotype and sequence similarity
PMID:11884604	PBO:0114601	(comment: broad specificity;) actually inferred from combination of phenotype and sequence similarity
PMID:11884604	PBO:0114595	(comment: broad specificity;) actually inferred from combination of phenotype and sequence similarity
PMID:11884604	PBO:0114597	actually inferred from combination of phenotype and sequence similarity
PMID:11886869	FYPO:0002588	a pronounced protective effect of the Zhf inactivation could be detected also for Ni2+
PMID:11886869	FYPO:0000763	In contrast to that, the zhf disruption was found to significantly protect cells from toxicity of Cd2+ ions, the third known substrate of CDF proteins. At the IC50 concentration for wild-type cells of 100 μM, Δzhf cells were inhibited by only 4% (±3%) (Fig. 1D).
PMID:11886869	FYPO:0001245	Similarly, the absence of a functional Zhf protein rendered the S. pombe cells Co2+-hypersensitive (Fig. 1C). At 1 mM Co2+ in EMM, wild-type cells showed 94% (±11%) of the optical density of untreated control cells, whereas Δzhf cells reached only 36% (±3.5%).
PMID:11886869	PBO:0111429	To determine whether the main pathway for Cd2+ detoxification in S. pombe, the formation of phytochelatins, is required for the Δzhf-dependent protection, the zhf gene was disrupted in the Δpcs strain Sp27 (20). Toxicity assays showed that the protective effect was even more pronounced in this genetic background.
PMID:11886869	GO:0140209	(comment: storage)
PMID:11886869	PBO:0110448	In the presence of elevated Zn2+ levels, however, they were severely growth-inhibited (Fig. 1, A and B).
PMID:11886869	PBO:0093559	Δzhf strain were viable and showed only a minor reduction in growth rate under control conditions without any added heavy metal salts.
PMID:11895484	FYPO:0003835	ell and nucleishapes in meu10∆ cells during the horse-tail, meiosisI and meiosis II stages were normal (data not shownand uppermost panel at 8 h in Fig. 4A)
PMID:11895484	FYPO:0004925	Moreover, the thickness of the walls of the meu10∆spores was not homogeneous. In some parts, the sporewall was approximately threefold thicker than wild-type spore walls and seemed to be composed of sparsematerial, whereas in other parts, they were abnormallythin and looked very weak. The enlarged image of anabnormal ascospore shows a scattered stripe structureacross the spore wall (Fig. 5C) that is not observed in thewall of wild-type ascospores. The abnormal spore wallseems fragile, as some of them appear to be broken,allowing the cytoplasmic material to leak out. In addi-tion, at the later time point (22 h), most of the ascosporewalls disappeared. This fragility of the ascospore walls islikely to be why the meu10∆ spore nuclei are stainingabnormally with Hoechst33342 (as seen in Fig. 4A).
PMID:11895484	GO:0005619	At meiosis II, however, Meu10-GFP appearedthroughout the cytoplasm and displayed a homogene-ous subcellular distribution (Fig. 6Aiv). As sporulationcommenced and progressed, the Meu10-GFP proteingradually moved to the peripheral region of the spores(Fig. 6Av), finally being distributed as a ring around eachof the four spores (Fig. 6Avi). Following sporulation, theGFP signal relocalized into the cytoplasm, where it wasfound as punctuated granules (Fig. 6Avii).
PMID:11895484	PBO:0112886	As visualized by the goldparticles, 1,3-β-glucan was found at the inner layer ofthe spore wall in the wild-type ascospores but in meu10∆ascospores it was scattered throughout the spore wall(Fig. 7A).Thus, Meu10 is required for the accurate local-ization of 1,3-β-glucan in the spore wall
PMID:11895484	FYPO:0000196	Like the meu10∆mutant (Fig. 3C), mature ascospores were not generatedby this mutant.
PMID:11895484	FYPO:0002150	Like the meu10∆ mutant, the spores from this mutantwere not viable (Fig. 8B)
PMID:11895484	PBO:0112887	Moreover, Meu10-N117∆-GFP signals in the abnormally shaped ascospores werenot detected (Fig. 8Ciii), indicating that this domain isessential for the spore wall localization of Meu10
PMID:11895484	FYPO:0002150	In this mutant, all the spores wereunviable and only faint signals from Meu10-C120∆-GFP were detected. (Fig. 8B, Cii)
PMID:11895484	FYPO:0002150	No mature ascospores were observed in the meu10∆mutant (Fig. 3C and see Fig. 4A).
PMID:11895484	PBO:0112885	Northern blot analysis on RNA from these cells usingmeu10 + cDNA as a probe revealed that meu10+ was tran-scribed during meiosis, even in mei4-null mutant cells(Fig. 1D).
PMID:11895484	FYPO:0002060	Thus,the meu10+ gene is not essential for vegetative growth.
PMID:11895484	FYPO:0000196	No mature ascospores were observed in the meu10∆mutant (Fig. 3C and see Fig. 4A).
PMID:11895484	FYPO:0000583	No mature ascospores were observed in the meu10∆mutant (Fig. 3C and see Fig. 4A).
PMID:11895484	FYPO:0002043	We next measured the DNA content of the meu10∆ and wild-type cells after nitrogenstarvation by flow cytometry. No apparent differencewas observed (data not shown), which indicates thatMeu10 is not required for pre-meiotic DNA synthesis.No mature ascospores were observed in the meu10∆mutant (Fig. 3C and see Fig. 4A).
PMID:11907273	FYPO:0000172	(comment: using chromosome III)
PMID:11909965	FYPO:0004318	(Figure 2C)
PMID:11909965	PBO:0033937	(Fig. 2B)
PMID:11909965	PBO:0096196	(Fig. 2B)
PMID:11909965	PBO:0096196	(Fig. 2B)
PMID:11909965	PBO:0096195	(Fig. 2B)
PMID:11909965	FYPO:0004318	(Figure 2C)
PMID:11909965	PBO:0023853	(Figure 5A)
PMID:11909965	PBO:0096197	(Figure 3a) (comment: CHECK DECREASED cell cycle arrest in mitotic anaphase)
PMID:11909965	FYPO:0003762	(Figure 3a) (comment: CHECK cell cycle arrest in mitotic metaphase)
PMID:11909965	FYPO:0003762	(Figure 3a) (comment: CHECK cell cycle arrest in mitotic metaphase)
PMID:11909965	FYPO:0000069	(Fig. 2A)
PMID:11927555	FYPO:0003738	(Fig. 6)
PMID:11927555	FYPO:0000620	(Fig. 6) resulted in a synthetic arrest at metaphase of mitosis. This contrasts with the G1 cell cycle arrest of pim1-d1 single mutant cells (Krien et al., 1998).
PMID:11927555	PBO:0093562	(Fig. 6)
PMID:11927555	PBO:0093564	(Figure 6)
PMID:11927555	FYPO:0000276	(Figure 6)
PMID:11927555	PBO:0101165	(Figure 6) which was enhanced by the presence of the pim1-d1 mutation at 36°C to include all mitotic cells (arrowed
PMID:11927555	FYPO:0000338	(Fig. 6)
PMID:11927555	FYPO:0001489	(Fig. 6)
PMID:11927555	FYPO:0006821	The double ®n1Dbub1D mutants were viable, though substantially retarded in colony formation and showed extensive chromosome segregation defects (Figure 7A).
PMID:11927555	FYPO:0000141	The double ®n1Dbub1D mutants were viable, though substantially retarded in colony formation and showed extensive chromosome segregation defects (Figure 7A).
PMID:11927555	FYPO:0002061	Double mutants between ®n1D and the temperature-sensitive allele rad21-K1 (Tatebayashi et al., 1998) were synthetically lethal at all temperatures
PMID:11927555	PBO:0101166	(in. non mitotic cells)
PMID:11927555	GO:0006998	suggesting the lethal synthetic interaction between ®n1D and cut11 might relate of the nuclear envelope rather than SPB anchoring during mitosis
PMID:11927555	PBO:0093564	(Figure 6)
PMID:11927555	PBO:0101164	(Figure 5)
PMID:11927555	PBO:0018346	(Figure 5)
PMID:11927555	PBO:0037408	(Figure 5)
PMID:11927555	FYPO:0007566	These data show that Fin1p- mediated compaction of the chromosomes is not functionally related to mitotic chromosome condensation and the mechanism by which it occurs remains obscure.
PMID:11927555	FYPO:0007566	These data show that Fin1p- mediated compaction of the chromosomes is not functionally related to mitotic chromosome condensation and the mechanism by which it occurs remains obscure.
PMID:11927555	FYPO:0007566	These data show that Fin1p- mediated compaction of the chromosomes is not functionally related to mitotic chromosome condensation and the mechanism by which it occurs remains obscure.
PMID:11927555	FYPO:0007566	These data show that Fin1p- mediated compaction of the chromosomes is not functionally related to mitotic chromosome condensation and the mechanism by which it occurs remains obscure.
PMID:11950879	PBO:0092680	(comment: vw: nda3 tubulin mutant does not assemble spindle and shows Mad2 is localized to unattached kinetochores)
PMID:11950879	FYPO:0003570	...majority of the Mad2-GFP was localized to the spindle
PMID:11950879	FYPO:0003570	...majority of the Mad2-GFP was localized to the spindle
PMID:11950879	FYPO:0002638	...majority of the Mad2-GFP was localized to the spindle
PMID:11950884	PBO:0102924	(Fig. 2A)
PMID:11950884	FYPO:0007810	(Fig. 5 Table 4)
PMID:11950884	FYPO:0007810	(Fig. 5 Table 3,4)
PMID:11950884	FYPO:0007810	(Fig. 5, Table 3,4)
PMID:11950884	PBO:0102925	(Fig. 6A)
PMID:11950884	PBO:0102926	(Fig. 6C)
PMID:11950884	PBO:0102927	location is abolished during mating Fig4Dc and Fig4Ec
PMID:11950884	FYPO:0000761	(Fig. 6C)
PMID:11950884	FYPO:0000761	(Fig. 6C)
PMID:11950884	FYPO:0006772	(Fig. 8D,E) pom1 has a role in the relocalisation of actin to the shmooing cell tip
PMID:11950884	GO:0043332	After pheromone addition, Tea1GFP became mostly lost from the growing end and was redistributed along the cell periphery at the nongrowing larger end (Fig. 3E). After pheromone addition, Tea2GFP and Tip1YFP were also reduced at the growing end, accumulating at the non-growing end and in the cytoplasm, often as dots in a row (Fig. 3E). The same relocalisation was observed for Tea2GFP during an h90 mating. In conjugating cells, Tea2GFP was found to localise to the nongrowing ends with some dots in the..
PMID:11950884	GO:0043332	After pheromone addition, Tea1GFP became mostly lost from the growing end and was redistributed along the cell periphery at the nongrowing larger end (Fig. 3E). After pheromone addition, Tea2GFP and Tip1YFP were also reduced at the growing end, accumulating at the non-growing end and in the cytoplasm, often as dots in a row (Fig. 3E). The same relocalisation was observed for Tea2GFP during an h90 mating. In conjugating cells, Tea2GFP was found to localise to the nongrowing ends with some dots in the..
PMID:11950884	GO:0043332	After pheromone addition, Tea1GFP became mostly lost from the growing end and was redistributed along the cell periphery at the nongrowing larger end (Fig. 3E). After pheromone addition, Tea2GFP and Tip1YFP were also reduced at the growing end, accumulating at the non-growing end and in the cytoplasm, often as dots in a row (Fig. 3E). The same relocalisation was observed for Tea2GFP during an h90 mating. In conjugating cells, Tea2GFP was found to localise to the nongrowing ends with some dots in the..
PMID:11950884	PBO:0102927	(Fig. 4F) location also exists during mating
PMID:11950884	FYPO:0007563	(Fig. 6B) All three mutants were able to detect and respond to pheromone by arresting in G1, as shown by FACS analysis (Fig. 6B)
PMID:11950884	FYPO:0007563	(Fig. 6B)
PMID:11950884	FYPO:0007563	(Fig. 6B)
PMID:11950884	PBO:0102928	regulation of
PMID:11950884	PBO:0102925	(Fig. 6A)
PMID:11950884	PBO:0102925	(Fig. 6A)
PMID:11950884	PBO:0102921	(Fig. 1)
PMID:11950884	PBO:0102922	(Fig. 2A)
PMID:11950884	PBO:0102923	(Fig. 2A)
PMID:11950927	FYPO:0001575	(comment: dominent negative effect)
PMID:11950927	PBO:0098340	Pic1- 765-924, which lacks the IN box, failed to bind Ark1p
PMID:11950927	FYPO:0000134	(Figure 6A)
PMID:11950927	FYPO:0001234	(Figure 6A)
PMID:11950927	FYPO:0001575	(comment: dominent negative effect)
PMID:11950927	FYPO:0003165	(Figure 1C)
PMID:11950927	PBO:0098338	(Figure 2)
PMID:11950927	FYPO:0000134	(Fig. 3c)
PMID:11950927	FYPO:0001513	(Fig. 3c)
PMID:11950927	FYPO:0001357	(Fig. 4)
PMID:11950927	FYPO:0001575	(comment: dominent negative effect)
PMID:11950932	PBO:0110443	The CAA20785 GFP fusion protein localized normally in cdc16-116, spg1-106, cdc7-24, and sid2-250 temperature-sensitive mutants...(Figure 3)
PMID:11950932	PBO:0110443	The CAA20785 GFP fusion protein localized normally in cdc16-116, spg1-106, cdc7-24, and sid2-250 temperature-sensitive mutants...(Figure 3)
PMID:11950932	PBO:0018346	The single and merged images indicate that CAA20785 colocalizes with Sid4p to SPBs throughout the cell cycle (Figure 2B).
PMID:11950932	PBO:0110445	At 36°C, Spg1p-GFP was detected at SPBs in wild-type cells but was absent from SPBs in the cdc11 mutant strains (Figure 4B).
PMID:11950932	PBO:0110445	At 36°C, Spg1p-GFP was detected at SPBs in wild-type cells but was absent from SPBs in the cdc11 mutant strains (Figure 4B).
PMID:11950932	PBO:0110444	However, its localization to the SPB was lost in the sid4-SA1 mutant at restrictive temperature (Figure 3).
PMID:11950932	PBO:0110443	The CAA20785 GFP fusion protein localized normally in cdc16-116, spg1-106, cdc7-24, and sid2-250 temperature-sensitive mutants...(Figure 3)
PMID:11950932	PBO:0110443	The CAA20785 GFP fusion protein localized normally in cdc16-116, spg1-106, cdc7-24, and sid2-250 temperature-sensitive mutants...(Figure 3)
PMID:11950932	PBO:0018634	The single and merged images indicate that CAA20785 colocalizes with Sid4p to SPBs throughout the cell cycle (Figure 2B).
PMID:11950932	PBO:0110447	Overproduction of Cdc11p(631-1045) had no effect on the localization of Sid4p-GFP but caused the loss of Cdc11p-GFP and Spg1p-GFP from SPBs (Figure 5B).
PMID:11950932	PBO:0110446	Overproduction of Cdc11p(631-1045) had no effect on the localization of Sid4p-GFP but caused the loss of Cdc11p-GFP and Spg1p-GFP from SPBs (Figure 5B). This is consistent with the with the idea that Cdc11p(631-1045) saturates the SPB binding site for Cdc11p, thus eliminating the opportunity for the full-length protein to localize to the SPB.
PMID:11950932	FYPO:0007569	Interestingly, we found that overproduction of GFP-Cdc11p(631-1045) gener-ated a sid phenotype (Figure 5A).
PMID:11950932	PBO:0110443	GFP- Cdc11p(1- 630) was distributed throughout the cytoplasm (our unpublished results), but GFP-Cdc11p(631-1045) localized to SPBs (Figure 5A).
PMID:11950932	PBO:0110444	GFP- Cdc11p(1- 630) was distributed throughout the cytoplasm (our unpublished results), but GFP-Cdc11p(631-1045) localized to SPBs (Figure 5A).
PMID:11952833	FYPO:0004537	(comment: premature SIN)
PMID:11952833	PBO:0113865	(comment: even though cdc13 is present)
PMID:11952833	PBO:0113866	(comment: even though cdc13 is present)
PMID:11955632	FYPO:0003655	(comment: CHECK tRNA)
PMID:11967147	FYPO:0001840	(comment: DNS)
PMID:11967147	FYPO:0006171	(Figure 5D) (comment: abolished pausing)
PMID:11967147	FYPO:0005343	(Figure 5D)
PMID:11967147	FYPO:0002638	(Figure 5D)
PMID:11967147	FYPO:0002638	(Figure 5D)
PMID:11967147	FYPO:0003969	(Figure 5B)
PMID:11967147	FYPO:0003969	(Figure 5B)
PMID:11967147	FYPO:0000670	(Figure 5B)
PMID:11967147	FYPO:0000670	(Figure 5B)
PMID:11967147	FYPO:0000141	(Figure 5B)
PMID:11967147	FYPO:0002061	(Fig. 5A)
PMID:11967147	FYPO:0002061	(Fig. 5A)
PMID:11967147	FYPO:0002061	(Fig. 5A)
PMID:11967147	PBO:0024749	(Fig. 2d)
PMID:11967147	PBO:0024749	(Fig. 2d)
PMID:11967147	PBO:0103982	(Fig. 2a)
PMID:11967147	PBO:0103982	(Fig. 2a)
PMID:11967147	PBO:0020141	(Fig. 2b)
PMID:11967147	PBO:0020141	(Fig. 2b)
PMID:11967147	PBO:0103981	(Fig. 1D)
PMID:11967147	PBO:0103981	(Fig. 1D)
PMID:11967147	FYPO:0001840	(comment: DNs)
PMID:11967147	FYPO:0001840	(Fig. 1C)
PMID:11967147	FYPO:0000274	(Fig. 1A)
PMID:11967147	FYPO:0000274	(Fig. 1A)
PMID:11967147	PBO:0103980	(Fig. 1A)
PMID:11967147	PBO:0103980	(Fig. 1A)
PMID:11967147	FYPO:0002060	(Figure S1) (comment: CHECK 20% longer)
PMID:11967147	FYPO:0002060	(Figure S1) (comment: CHECK 20% longer)
PMID:11967147	PBO:0093767	(Figure S1)
PMID:11967147	FYPO:0002060	(Figure S1) (comment: CHECK 20% longer)
PMID:11967147	FYPO:0002060	(Figure S1)
PMID:11967147	FYPO:0002060	(Figure S1)
PMID:11972332	PBO:0109322	(Figure 1A)
PMID:12000964	FYPO:0003438	(comment: vw: I added this as an inference, because the checkpoint is never satisfied)
PMID:12000964	FYPO:0003545	(comment: vw: I added this as an inference, because the checkpoint is never satisfied)
PMID:12000964	FYPO:0004588	(comment: vw: delayed)
PMID:12000964	FYPO:0000611	(comment: vw: DNA checkpoint dept)
PMID:12006645	FYPO:0002059	(comment: tetrads only)
PMID:12007420	PBO:0019143	Fig. 4D (comment: tea3 does not affect polarity and the elongated cells do not branch. This is different to pom1 where cdc11-119 cells form branches)
PMID:12007420	FYPO:0001406	Fig. 3B
PMID:12007420	FYPO:0002060	Fig. 3B
PMID:12007420	PBO:0101140	Fig. 1D
PMID:12007420	PBO:0103185	Fig. 1C
PMID:12007420	FYPO:0003150	Fig. 1B
PMID:12007420	PBO:0099942	Fig. 1
PMID:12007420	PBO:0097442	Fig. 4B
PMID:12007420	FYPO:0002452	Fig. 3B
PMID:12007420	FYPO:0002060	Fig. 3B
PMID:12007420	FYPO:0002060	Fig. 3B
PMID:12007420	PBO:0103191	Fig. 3D
PMID:12007420	FYPO:0002061	Fig. 3B
PMID:12007420	PBO:0103192	Fig. 4A
PMID:12007420	PBO:0103192	Fig. 4C
PMID:12007420	PBO:0103190	Fig. 3C
PMID:12007420	PBO:0103189	Fig. 2D (comment: tea3GFP staining cell middle after nda3 block and release)
PMID:12007420	PBO:0103188	Fig. 2D (comment: no tea3GFP staining cell middle in nda3 block)
PMID:12007420	PBO:0103187	Fig. 2A
PMID:12007420	PBO:0101140	Fig. 1D
PMID:12007420	PBO:0103185	Fig. 1C
PMID:12019258	FYPO:0005433	(comment: assayed using 160-bp palindromic sequence inserted into ade6 locus)
PMID:12023299	PBO:0101530	(comment: mah: same as rad51delta alone)
PMID:12023299	PBO:0093629	(comment: mah: same as rad51delta alone)
PMID:12023299	PBO:0093629	(comment: mah: same as rad51delta alone)
PMID:12023299	PBO:0093619	(comment: mah: same as rad51delta alone)
PMID:12023299	PBO:0093619	(comment: mah: same as rad51delta alone)
PMID:12023299	PBO:0093619	(comment: mah: same as rad51delta alone)
PMID:12023299	PBO:0100481	(comment: mah: slighly more severe than rad50delta alone)
PMID:12023299	PBO:0096052	(comment mah: assayed substrate: exogenous histone H1)
PMID:12023299	PBO:0101526	(comment: CHECK mah: residue=T215)
PMID:12023299	PBO:0101530	(comment: mah: same as rad51delta alone)
PMID:12023299	PBO:0093619	(comment: mah: same as rad51delta alone)
PMID:12023299	PBO:0093620	(comment: mah: same as rqh1delta alone)
PMID:12023299	PBO:0093620	(comment: mah: sensitivity depends on how highly overexpressed top3+ is; more top3+ -> lower sensitivity)
PMID:12023299	GO:0000724	(comment: mah: localization to DSB sites also contributes to inference)
PMID:12034771	PBO:0103832	(Fig. 3C)
PMID:12034771	PBO:0103833	(Fig. 3C)
PMID:12034771	PBO:0103834	(Fig. 3C)
PMID:12034771	PBO:0103834	(Fig. 3C)
PMID:12034771	PBO:0103834	(Fig. 3C)
PMID:12034771	PBO:0103831	(Fig. 4A)
PMID:12034771	PBO:0100778	(Fig. 4B) (comment: I know that the protein is localising to the plus end but they did not say this in this paper although they do say it is on the tips of polymerizing microtubules so it could be FYPO 0004731)
PMID:12034771	PBO:0103835	(Fig. 4B)
PMID:12034771	PBO:0103836	(Fig. 3C, 5A) (comment: CHECK STILL TO ADD curved around cell end during mitotic interphase)
PMID:12034771	FYPO:0003702	(Fig. 5A)
PMID:12034771	FYPO:0003702	(Fig. 5A)
PMID:12034771	PBO:0037573	(Fig. 5B)
PMID:12034771	PBO:0037573	(Fig. 5B)
PMID:12034771	PBO:0037574	(Fig. 5B)
PMID:12034771	PBO:0103837	(Fig. 6)
PMID:12034771	PBO:0103838	(Fig. 6)
PMID:12034771	PBO:0018421	(comment: used endogenous tea2 gene tagged at C term with GFP). Fig1A
PMID:12034771	PBO:0037211	(comment: used endogenous tea1 gene tagged at C term with YFP and tubulin CFP for live cell imaging of tea1 on microtubules) Fig1C
PMID:12034771	PBO:0103829	(comment: used endogenous tea2 gene tagged at C term with GFP). Fig1A
PMID:12034771	PBO:0103830	(Figure 2A)
PMID:12034771	PBO:0103831	(Fig. 2C) (comment: OUTSTANDING Q IS IT ALONG OR ON?)
PMID:12034771	PBO:0103839	(Fig. 6)
PMID:12050156	PBO:0110449	FIG. 1. Zhf is required for growth on high and low zinc
PMID:12050156	PBO:0093530	Cadmium increased the proportion of longer zym1 transcripts as observed previously following the exposure to copper (Fig. 6B).
PMID:12050156	FYPO:0000116	The growth of the resulting zym1Δ showed only a small but reproducible impairment in rich medium (YE5S) supplemented with 10-100 μm zinc (Fig. 5A).
PMID:12050156	PBO:0110451	The abundance of zym1 transcripts was also reduced in cells lacking Pcr1, a bZIP transcription factor that in conjunction with Atf1 functions downstream of Sty1 (41, 42) (Fig. 3C).
PMID:12050156	PBO:0110451	but this pathway is not obligatory for zinc perception because zinc induction was retained in Wis1 mutants albeit at reduced magnitude.
PMID:12050156	PBO:0110450	Both the basal and zinc-induced levels of zym1 transcripts were severely reduced in wis1Δ (Fig. 3C).
PMID:12050156	PBO:0111362	Zinc caused the accumulation of zym1 transcripts with up to 10 -20-fold increase 30 min after the addition of ZnSO4 (Fig. 3, A and C).
PMID:12050156	PBO:0110449	Zhf Is Required for Growth on Low Zinc
PMID:12050156	PBO:0110448	Most importantly, the zhfΔ strain was hypersensitive to zinc showing impaired growth on rich medium (YE5S) compared with the equivalent control strain and was unable to grow in medium supplemented with 20 μm ZnSO4 (Fig. 1C).
PMID:12050156	PBO:0110448	FIG. 1. Zhf is required for growth on high and low zinc
PMID:12062100	PBO:0097586	(comment: longer transcript)
PMID:12062100	PBO:0097585	(comment: longer transcript)
PMID:12062100	PBO:0092132	(comment: longer transcript)
PMID:12065422	FYPO:0002061	DNS
PMID:12065422	FYPO:0002061	DNS
PMID:12065422	PBO:0095087	(comment: CONDITION 25 degrees) Figure 5d
PMID:12065422	FYPO:0001124	(comment: recessive, loss-of-function mutation)
PMID:12065422	FYPO:0002061	Introduction of either ®n1.ts1 or ®n1.D to a cut12.s11 cdc25.22 mutant background abolished the growth of cdc25.22 above 30°C that had been conferred by the cut12.s11 mutation (Figure 6C).
PMID:12065422	PBO:0095089	(comment: CONDITION 25 degrees) Figure 7
PMID:12065422	PBO:0095085	(Figures 1C and 2C)
PMID:12065422	PBO:0095088	(comment: CONDITION 25 degrees) Figure 7
PMID:12065422	PBO:0095086	(Figure 5d)
PMID:12065422	FYPO:0000620	(Figure 2B and C)
PMID:12065422	PBO:0095084	(Figure 1C)
PMID:12065422	PBO:0095084	(Figure 1C)
PMID:12065422	PBO:0095084	(Figure 1B)
PMID:12065422	PBO:0095083	(Figure 1A) We concluded that the severe phenotype of a ®n1.ts1 mutant is a transitory response to loss of Fin1 function. This implied that ®n1.D haploids adapted to loss of Fin1 after the ®rst division of a germinating spore.
PMID:12065422	FYPO:0001124	(Table II)
PMID:12065422	FYPO:0003481	(Table II)
PMID:12065422	FYPO:0001399	(comment: recessive, loss-of-function mutation)
PMID:12065422	FYPO:0003481	(Figure 2A; Table II)
PMID:12074602	PBO:0111133	(comment: binds to 54-bp element at 1186-1239)
PMID:12093738	PBO:0093769	(comment: CHECK fypo/issues/3165) Fig5B in the absence of cig2 there is a delay in the appearance of cut cells
PMID:12093738	PBO:0100990	(Fig. 1D)
PMID:12093738	PBO:0100989	(Fig. 1D) The protein cdc2 protein assayed is in complex with cig2 as there is no cdc2-cdc13 complex present
PMID:12093738	PBO:0100988	(comment: CHECK fypo/issues/3165) Fig5C
PMID:12093738	PBO:0100987	(Fig. 5C)
PMID:12093738	PBO:0100986	(Fig. 4A) cells block normally with 1C DNA content even when cig2 is over expressed
PMID:12093738	PBO:0100985	(Fig. 5B)
PMID:12093738	FYPO:0000017	(Fig. 5A)
PMID:12093738	FYPO:0003449	(Fig. 5A)
PMID:12093738	PBO:0100984	(Fig. 5A) used forward scatter to measure cell size small peak of short cells
PMID:12093738	PBO:0019210	(Fig. 3) data not shown cell viability is reduced at late time points
PMID:12093738	PBO:0100983	(Fig. 5A) small peak of less that 1C DNA content
PMID:12093738	PBO:0100982	(Fig. 3B) no G1 peak is observed showing that S phase onset is not delayed
PMID:12093738	PBO:0100981	(Fig. 3C) (comment: cig2 over expression from ~10hours after thiamine removal)
PMID:12093738	PBO:0099234	(Fig. 3A, D)
PMID:12093738	PBO:0100981	(Fig. 4B) cig2 over expression also occurs when cells blocked with HU
PMID:12093738	PBO:0100980	(Fig. 2C) the cdc2-cig2 and cdc2-cdc13 complexe have no tyrosine 15 phosphorylation
PMID:12093738	PBO:0099888	(Fig. 2C) the cdc2-cig2 and cdc2-cdc13 complexes have increased kinase activity
PMID:12093738	PBO:0100979	(Fig. 1C)
PMID:12093738	PBO:0100978	(Fig. 1C)
PMID:12093738	PBO:0100977	(Fig. 1C)
PMID:12093738	PBO:0024304	(Fig. 1A)
PMID:12095692	GO:0001181	Neither the pol I/Rrn3p (Fig. 3, lane 3) nor the SpRrn7h complex fraction (Fig. 3, lanes 1 and 2) support accurate initiation of the S. pombe rRNA template 30 D 131, on their own. However, when both are present, accurate transcriptional initiation of the S. pombe rDNA gene promoter is reconstituted (Fig. 3, lanes 4 and 5).
PMID:12095692	GO:0001181	Neither the pol I/Rrn3p (Fig. 3, lane 3) nor the SpRrn7h complex fraction (Fig. 3, lanes 1 and 2) support accurate initiation of the S. pombe rRNA template 30 D 131, on their own. However, when both are present, accurate transcriptional initiation of the S. pombe rDNA gene promoter is reconstituted (Fig. 3, lanes 4 and 5).
PMID:12095692	GO:0001181	3.4. The putative SpRrn11h co-fractionates with Sp-MHRrn7h and rDNA transcription initiation activity
PMID:12095692	GO:0001164	3.7. Association of SpRrn7h with rDNA core promoter sequences
PMID:12112233	FYPO:0002522	(comment: actually accumulation)
PMID:12112233	FYPO:0003027	(Figure 1)
PMID:12112233	FYPO:0001357	(Figure 1)
PMID:12181326	FYPO:0006661	data not shown
PMID:12181336	PBO:0107189	(Fig. 5)
PMID:12181336	PBO:0107189	(Fig. 5)
PMID:12181336	PBO:0107191	(comment: small amount)
PMID:12181336	PBO:0107189	(Fig. 6)
PMID:12181336	PBO:0107192	(Fig. 7)
PMID:12181336	PBO:0107193	(Fig. 7)
PMID:12181336	PBO:0107187	(Fig. 4)
PMID:12181336	PBO:0107186	(Fig. 4)
PMID:12181336	PBO:0107185	(Fig. 3)
PMID:12181336	PBO:0107184	(Fig. 3)
PMID:12181336	PBO:0107188	(Fig. 4)
PMID:12181336	PBO:0107184	(Fig. 3)
PMID:12181336	GO:0005737	(Fig. 5) Consistent with previous immunolocalization studies (Gaits et al., 1998), wild-type Wis1-GFP showed solely cytoplasmic localization and little GFP signal was seen in the nuclear region (Figure 5A).
PMID:12181336	PBO:0107189	(Fig. 5)
PMID:12181336	PBO:0107183	(Fig. 3)
PMID:12181336	PBO:0107183	(Fig. 3)
PMID:12181336	PBO:0107182	(Figure 2B)
PMID:12181336	PBO:0107181	(Figure 2B)
PMID:12181336	PBO:0107182	(Figure 2B)
PMID:12185500	FYPO:0002061	(comment: CONDITION 29 degrees C)
PMID:12185500	FYPO:0002061	(comment: CONDITION 29 degrees C)
PMID:12185500	FYPO:0002061	(comment: CONDITION 27 degrees C)
PMID:12185500	FYPO:0002061	(condition 25 degrees C)
PMID:12185500	FYPO:0002061	(comment: CONDITION 25 degrees C)
PMID:12185500	FYPO:0002060	(comment: CONDITION 25 degrees C)
PMID:12185500	FYPO:0000082	(comment: CONDITION restrictive temp 32)
PMID:12185500	FYPO:0000082	(comment: CONDITION restrictive temp 36)
PMID:12185500	FYPO:0002061	(comment: CONDITION 27 degrees C)
PMID:12185840	PBO:0101611	(Figure 2C)
PMID:12185840	GO:0005739	(Fig. 2C)
PMID:12186944	GO:0032153	"(comment: localization requires microtubules (assayed using thiabendazole or carbendazim) but not F-actin (assayed using latrunculin A)"""
PMID:12186947	PBO:0021453	(comment: CHECK penetrance low if cells exposed to UV)
PMID:12193640	PBO:0107146	As expected, Swi6, which depends on histone modification for chromatin binding, was delocalized from the ura4+ transgenes (Fig. 3C).
PMID:12193640	FYPO:0003412	Two transgenes located centromere distal to the tRNA genes were de-repressed in ago1- , dcr1- , and rdp1- , but a transgene located within the central region remained silent. Similar results were obtained in all three mutant strains, as assayed by growth on medium lacking uracil and by Northern blots (Fig. 1, B) (21).
PMID:12193640	FYPO:0003412	Two transgenes located centromere distal to the tRNA genes were de-repressed in ago1- , dcr1- , and rdp1- , but a transgene located within the central region remained silent. Similar results were obtained in all three mutant strains, as assayed by growth on medium lacking uracil and by Northern blots (Fig. 1, B) (21).
PMID:12193640	FYPO:0003412	Two transgenes located centromere distal to the tRNA genes were de-repressed in ago1- , dcr1- , and rdp1- , but a transgene located within the central region remained silent. Similar results were obtained in all three mutant strains, as assayed by growth on medium lacking uracil and by Northern blots (Fig. 1, B) (21).
PMID:12193640	FYPO:0004331	Two transgenes located centromere distal to the tRNA genes were de-repressed in ago1- , dcr1- , and rdp1- , but a transgene located within the central region remained silent. Similar results were obtained in all three mutant strains, as assayed by growth on medium lacking uracil and by Northern blots (Fig. 1, B) (21).
PMID:12193640	FYPO:0004331	Two transgenes located centromere distal to the tRNA genes were de-repressed in ago1- , dcr1- , and rdp1- , but a transgene located within the central region remained silent. Similar results were obtained in all three mutant strains, as assayed by growth on medium lacking uracil and by Northern blots (Fig. 1, B) (21).
PMID:12193640	FYPO:0004331	Two transgenes located centromere distal to the tRNA genes were de-repressed in ago1- , dcr1- , and rdp1- , but a transgene located within the central region remained silent. Similar results were obtained in all three mutant strains, as assayed by growth on medium lacking uracil and by Northern blots (Fig. 1, B) (21).
PMID:12193640	PBO:0094684	However, three major transcripts that hybridized to the repeats were found to accumulate at high levels in each of the RNAi mutants (Fig. 1C).
PMID:12193640	PBO:0094684	However, three major transcripts that hybridized to the repeats were found to accumulate at high levels in each of the RNAi mutants (Fig. 1C).
PMID:12193640	PBO:0094684	However, three major transcripts that hybridized to the repeats were found to accumulate at high levels in each of the RNAi mutants (Fig. 1C).
PMID:12193640	PBO:0097227	These transcripts were also found in swi6- (Fig. 1D) but at a much lower lev
PMID:12193640	FYPO:0007337	dcr1- , rdp1- , and ago1- cells had increased levels of K4 in the centromeric region in comparison to actin controls (Fig. 3B).
PMID:12193640	FYPO:0007337	dcr1- , rdp1- , and ago1- cells had increased levels of K4 in the centromeric region in comparison to actin controls (Fig. 3B).
PMID:12193640	FYPO:0007337	dcr1- , rdp1- , and ago1- cells had increased levels of K4 in the centromeric region in comparison to actin controls (Fig. 3B).
PMID:12193640	FYPO:0003096	In contrast, levels of K9 were greatly reduced.
PMID:12193640	FYPO:0003096	In contrast, levels of K9 were greatly reduced.
PMID:12193640	FYPO:0003096	In contrast, levels of K9 were greatly reduced.
PMID:12193640	PBO:0107146	As expected, Swi6, which depends on histone modification for chromatin binding, was delocalized from the ura4+ transgenes (Fig. 3C).
PMID:12193640	PBO:0107146	As expected, Swi6, which depends on histone modification for chromatin binding, was delocalized from the ura4+ transgenes (Fig. 3C).
PMID:12196391	PBO:0093637	(comment: same as rad26delta alone)
PMID:12196391	PBO:0093637	(comment: same as rad3delta alone)
PMID:12196391	PBO:0093637	(comment: same as rad3delta alone)
PMID:12196391	PBO:0093637	(comment: same as rad3delta alone)
PMID:12196391	PBO:0093637	(comment: same as rad3delta alone)
PMID:12196391	PBO:0093633	(comment: same as either single mutant)
PMID:12196391	PBO:0093633	(comment: same as either single mutant)
PMID:12207036	FYPO:0002060	(Fig. 6)
PMID:12207036	FYPO:0002060	(Fig. 6)
PMID:12207036	FYPO:0002060	(Fig. 6)
PMID:12242222	FYPO:0005870	(Fig. 4)
PMID:12242222	FYPO:0002946	(Fig. 4E)
PMID:12242222	FYPO:0000647	(Fig. 4)
PMID:12242294	PBO:0103973	data not shown
PMID:12242294	PBO:0103974	data not shown
PMID:12242294	PBO:0095634	(Fig. 8d)
PMID:12242294	FYPO:0002638	(Fig. 8a)
PMID:12242294	FYPO:0002638	(Fig. 8a)
PMID:12242294	FYPO:0001355	(Fig. 8a)
PMID:12242294	FYPO:0004085	(Fig. 8a)
PMID:12242294	PBO:0099328	data not shown
PMID:12242294	FYPO:0002390	(Fig. 1a) (comment: CHECK maintenence of)
PMID:12242294	PBO:0103972	data not shown
PMID:12242294	FYPO:0001355	(Fig. 8b)
PMID:12242294	FYPO:0001355	(Fig. 8b)
PMID:12242294	FYPO:0000324	(Fig. 1a)
PMID:12242294	PBO:0034020	(Figure 9)
PMID:12242294	FYPO:0002061	(Fig. 8d)
PMID:12354095	PBO:0101752	(Fig. 1)
PMID:12354095	PBO:0101752	(Fig. 1)
PMID:12354095	FYPO:0001357	(Fig. 1)
PMID:12354095	FYPO:0000118	(Fig. 2B)
PMID:12354095	FYPO:0001470	(Fig. 4A)
PMID:12354095	FYPO:0001470	(Fig. 4B)
PMID:12354095	PBO:0093641	(Fig. 4B)
PMID:12354095	PBO:0093641	(Fig. 4B)
PMID:12354095	PBO:0093641	(Fig. 4B)
PMID:12354095	PBO:0093558	(Fig. 4A)
PMID:12354095	PBO:0093641	(Fig. 4A)
PMID:12354095	PBO:0112785	(Fig. 3C and D)
PMID:12354095	PBO:0112784	(Fig. 3B and D)
PMID:12354095	PBO:0112783	(Fig. 3C and D)
PMID:12354095	PBO:0112782	(Fig. 3B and D)
PMID:12354095	PBO:0110822	(Fig. 3A and D)
PMID:12354095	PBO:0112781	(Fig. 3C and D)
PMID:12354095	PBO:0112780	(Fig. 3B and D)
PMID:12354095	PBO:0112779	(Fig. 3C and D)
PMID:12354095	PBO:0112778	(Fig. 3B and D)
PMID:12354095	PBO:0112777	(Fig. 3A and D)
PMID:12354095	FYPO:0000674	(Fig. 2C)
PMID:12354095	FYPO:0000674	(Fig. 2C)
PMID:12354095	PBO:0112776	(Fig. 2B)
PMID:12354095	PBO:0104246	(Fig. 2B)
PMID:12354095	PBO:0094642	(Fig. 2B)
PMID:12354095	FYPO:0001315	(Fig. 2B)
PMID:12354095	FYPO:0001315	(Fig. 2B)
PMID:12354095	FYPO:0001357	(Fig. 1)
PMID:12354095	PBO:0093641	(Fig. 1)
PMID:12354095	PBO:0093641	(Fig. 1)
PMID:12354095	PBO:0093557	(Fig. 5A)
PMID:12354095	PBO:0093557	(Fig. 5A)
PMID:12354095	PBO:0093557	(Fig. 5A)
PMID:12354095	PBO:0093558	(Fig. 4B)
PMID:12354095	PBO:0093558	(Fig. 4B)
PMID:12354095	PBO:0093558	(Fig. 4B)
PMID:12354095	PBO:0093558	(Fig. 4B)
PMID:12354095	FYPO:0001315	(Fig. 2B)
PMID:12354095	FYPO:0001315	(Fig. 2B)
PMID:12354095	FYPO:0001315	(Fig. 2B)
PMID:12354095	PBO:0093558	(Fig. 4A)
PMID:12354095	PBO:0093558	(Fig. 1)
PMID:12354095	PBO:0093558	(Fig. 1)
PMID:12354095	FYPO:0005970	(Fig. 1)
PMID:12354095	PBO:0101760	(Fig. 1)
PMID:12354095	FYPO:0001406	(Fig. 6)
PMID:12354095	PBO:0095096	(Fig. 5C and D)
PMID:12354095	PBO:0093558	(Fig. 5B)
PMID:12354095	PBO:0093558	(Fig. 5B)
PMID:12354095	PBO:0093557	(Fig. 5B)
PMID:12354095	PBO:0093557	(Fig. 5B)
PMID:12354095	PBO:0093558	(Fig. 5A)
PMID:12390246	PBO:0034015	penetrance is mentioned in EXP accompanying fig 6A
PMID:12390246	PBO:0034018	penetrance is mentioned in EXP accompanying fig 6A
PMID:12390246	PBO:0034017	penetrance is mentioned in EXP accompanying fig 6A
PMID:12390246	PBO:0034015	(Fig. 6A)
PMID:12390246	FYPO:0005349	(Fig. 4a,b)
PMID:12390246	PBO:0034014	penetrance is mentioned in EXP accompanying fig 6A
PMID:12390246	PBO:0034016	penetrance is mentioned in EXP accompanying fig 6A
PMID:12399381	PBO:0107302	(Figure 4) (comment: CHECK cdr phenotype)
PMID:12399381	PBO:0107309	(Figure 1) (comment: CHECK cdr phenotype)
PMID:12399381	FYPO:0006822	(Table 4)
PMID:12399381	PBO:0107308	(Figure 6b) (comment: CHECK during x phase?)
PMID:12399381	PBO:0094966	(comment: semi wee)
PMID:12399381	PBO:0094730	(Figure 6A)
PMID:12399381	FYPO:0000590	(Fig. 5C, D)
PMID:12399381	PBO:0037055	(Figure 5C, D)
PMID:12399381	GO:0034399	(Fig. 5A)
PMID:12399381	GO:0005737	(Fig. 5A)
PMID:12399381	GO:0005634	(Fig. 5A)
PMID:12399381	PBO:0107305	(Fig. 5)
PMID:12399381	PBO:0107305	(Fig. 5)
PMID:12399381	PBO:0107305	(Fig. 5)
PMID:12399381	PBO:0107304	(Figure 4) (comment: CHECK cdr phenotype)
PMID:12399381	PBO:0107304	(Figure 4) (comment: CHECK cdr phenotype)
PMID:12399381	PBO:0107304	(Figure 4) (comment: CHECK cdr phenotype)
PMID:12399381	PBO:0107304	(Figure 4) (comment: CHECK cdr phenotype)
PMID:12399381	PBO:0107302	(Figure 4) (comment: CHECK cdr phenotype)
PMID:12399381	PBO:0107302	(Figure 4) (comment: CHECK cdr phenotype)
PMID:12399381	PBO:0107302	(Figure 4) (comment: CHECK cdr phenotype)
PMID:12399381	FYPO:0001490	(Figure 3)
PMID:12399381	PBO:0107303	(Figure 2C, D)
PMID:12399381	PBO:0095634	(Figure 2a)
PMID:12399381	PBO:0037050	(Figure 2a)
PMID:12399381	PBO:0095685	(Figure 1)
PMID:12399381	PBO:0095634	(Figure 1)
PMID:12399381	PBO:0107302	(Figure 1) (comment: CHECK cdr phenotype)
PMID:12399381	PBO:0037050	(Figure 1)
PMID:12411492	PBO:0107490	(comment: same as plo1-ts35 alone)
PMID:12411492	PBO:0107491	(comment: same as plo1-ts35 alone)
PMID:12411492	PBO:0107489	(comment: same as plo1-ts35 alone)
PMID:12419251	PBO:0105826	(comment: normal binding periodicity over cell cycle)
PMID:12419251	FYPO:0000333	(comment: CHECK actually ectopic expression, throughout cell cycle)
PMID:12419251	PBO:0105826	(comment: CHECK normal binding periodicity over cell cycle)
PMID:12419251	PBO:0100913	(comment: CHECK actually ectopic expression, throughout cell cycle)
PMID:12419251	PBO:0097194	(comment: normal binding periodicity over cell cycle)
PMID:12426374	FYPO:0006179	(Figure 1B, rows 4±6 )
PMID:12426374	PBO:0092680	(Figure 1A and C)
PMID:12426374	FYPO:0006179	(Figure 1B, rows 4±6)
PMID:12426374	PBO:0092680	(Figure 1A and C)
PMID:12426374	FYPO:0002638	(comment: vw: assayed by increased mad2 at kinetochore - checkpoint active)
PMID:12426374	FYPO:0006190	(comment: vw: assayed by increased mad2 at kinetochore - checkpoint active)
PMID:12426374	FYPO:0000141	(Figure 1B)
PMID:12426374	FYPO:0006179	(Figure 1B, rows 4±6)
PMID:12427731	GO:0007163	(comment: CHECK based just on this paper, candidate for involved_in_or_regulates qualifier)
PMID:12427731	GO:0004672	(comment: assayed using myelin basic protein; doesn't rule out tyrosine phosphorylation)
PMID:12442907	FYPO:0006822	small daughter at g1 Fig 1c The mutant produced daughter cells with an average length of 6 μm; whereas, the wild-type cells averaged 7.5 μm
PMID:12442907	FYPO:0001046	(Fig. 1c) The mutant produced daughter cells with an average length of 6 μm; whereas, the wild-type cells averaged 7.5 μm
PMID:12442907	FYPO:0003481	(Figs. 3A and 3B). there were cells that initiated and completed the mitosis in a small portion (Table 1), which eventually led to cell proliferation until the stationary phase (Fig. 2A).
PMID:12442907	FYPO:0007628	(Figs. 3A and 3B).
PMID:12442907	FYPO:0001406	a considerable portion of the Rrg1-overproduced cells that undergo mitosis showed an abnormal accumulation of septum material (Figs. 3F, 3G, and 3H).
PMID:12442907	FYPO:0000636	(Fig. 1b) The estimated doubling time of the mutant was 110 min in a rich (YE) medium, while that of the wild-type cells was 150 min.
PMID:12442907	FYPO:0001234	As shown in Fig. 2A, the rate of cell proliferation was immediately reduced after the amount of Rrg1 was increased.
PMID:12442907	FYPO:0003306	(Table 1)
PMID:12455694	FYPO:0002061	(comment: CONDITION 32 degrees) (comment: CHECK mcl1-1 semi-permissive)
PMID:12455694	FYPO:0002061	(comment: CONDITION 32 degrees) (comment: CHECK mcl1-1 semi-permissive)
PMID:12455993	GO:0031533	Surprisingly, the S. pombe capping enzyme subunits do not interact with each other.
PMID:12455993	GO:0031533	Surprisingly, the S. pombe capping enzyme subunits do not interact with each other.
PMID:12479804	PBO:0105165	(Figure 4C)
PMID:12479804	FYPO:0005781	Table1
PMID:12479804	GO:0005515	(Fig. 4)
PMID:12479804	PBO:0094087	(Figure 5)
PMID:12479804	PBO:0101132	(Figure 5)
PMID:12479804	PBO:0095090	(Fig. 5)
PMID:12479804	PBO:0022584	(Figure 3A)
PMID:12479804	PBO:0096052	(Fig. 6)
PMID:12479804	PBO:0096053	(Fig. 6)
PMID:12479804	FYPO:0004106	(Figure 2)
PMID:12479804	PBO:0096153	(Figure 3E, 3F)
PMID:12479804	PBO:0105159	(Figure 3E, 3F)
PMID:12479804	FYPO:0003762	(Fig. 1A) I'm modelling this as normal becasue nda3 is providing microtubule damage. Checkpoint would be expected to be o in WT in this scenario. cells failed to maintain the microtubule damage-induced checkpoint arrest and began to aberrantly form septa
PMID:12479804	PBO:0105163	(Figure 4A)
PMID:12479804	FYPO:0005781	(Fig. 1A) I'm modelling this as decreased because nda3 is providing microtubule damage. Checkpoint would be expected to be o in WT in this scenario. cells failed to maintain the microtubule damage-induced checkpoint arrest and began to aberrantly form septa
PMID:12479804	FYPO:0005781	Table1
PMID:12479804	FYPO:0005781	Table1
PMID:12479804	PBO:0105162	(Figure 4A) (comment: CHECK 10% (2/20) of anaphase cells displayed Dma1p-GFP SPB signal)
PMID:12479804	PBO:0105161	(Figure 3E, 3F)
PMID:12479804	PBO:0105155	(Figure 2A)
PMID:12479804	PBO:0105157	(Figure 3A)
PMID:12479804	PBO:0024374	(comment: faintly) Figure 3A, panel 2, arrowhead
PMID:12479804	PBO:0100276	(Figure 2D)
PMID:12479804	PBO:0105156	(Figure 2A)
PMID:12479804	PBO:0105154	(Fig. 1B)
PMID:12479804	GO:0031030	The observation that Clp1p/Flp1p is required for septation in dma1μ mutants is consistent with a model where Dma1p inhibits SIN activation
PMID:12479804	PBO:0105161	(Figure 3E, 3F)
PMID:12479804	PBO:0105161	(Figure 3E, 3F)
PMID:12479804	PBO:0105160	(Figure 3E, 3F)
PMID:12479804	PBO:0105160	(Figure 3E, 3F)
PMID:12479804	FYPO:0005781	Table1
PMID:12479804	PBO:0105160	(Figure 3E, 3F)
PMID:12479804	FYPO:0005781	Table1
PMID:12479804	PBO:0105158	(Figure 3E, 3F)
PMID:12479804	PBO:0105160	(Figure 4B)
PMID:12479804	PBO:0105164	(Figure 4C)
PMID:12482946	PBO:0098310	(Fig. 2B)
PMID:12482946	PBO:0098309	(Fig. 2B)
PMID:12482946	FYPO:0000220	(Fig. 2B)
PMID:12482946	FYPO:0002834	(Fig. 2B)
PMID:12482946	PBO:0098308	(Fig. 2A)
PMID:12482946	FYPO:0000091	(Fig. 1D)
PMID:12526748	PBO:0106596	(Figure 1e)
PMID:12526748	PBO:0106595	(Figure 1C)
PMID:12526748	PBO:0106594	(Figure S1)
PMID:12526748	PBO:0096191	(Figure S1)
PMID:12526748	PBO:0106602	(comment: D.N.S?)
PMID:12526748	PBO:0093562	(Fig. 1)
PMID:12526748	PBO:0096770	(Fig. 1)
PMID:12526748	FYPO:0006993	(Fig. 1b)
PMID:12526748	FYPO:0003411	(Figure S1)
PMID:12526748	PBO:0106604	(Fig. 3)
PMID:12526748	PBO:0093562	(Fig. 1)
PMID:12526748	PBO:0093562	(Fig. 1)
PMID:12526748	FYPO:0002827	(Figure S1)
PMID:12526748	PBO:0106607	(Fig. 3)
PMID:12526748	PBO:0106606	(Fig. 3)
PMID:12526748	PBO:0106607	(Fig. 3)
PMID:12526748	PBO:0106600	(Figure 1e)
PMID:12526748	PBO:0106605	(Fig. 3)
PMID:12526748	PBO:0106606	(Fig. 3)
PMID:12526748	PBO:0106605	(Fig. 3)
PMID:12526748	PBO:0106604	(Fig. 3)
PMID:12526748	PBO:0106603	Pst1p colocalizes with the otr/imr region in a cell cycle-specific manner.
PMID:12526748	PBO:0096039	(comment: D.N.S?)
PMID:12526748	PBO:0096785	(comment: D.N.S?)
PMID:12526748	PBO:0106599	(Figure 1e)
PMID:12526748	PBO:0106598	(Figure 1e)
PMID:12526748	PBO:0106597	(Figure 1e)
PMID:12546793	PBO:0094970	(see the Supplementary) Additional experiments indicated that neither mph1p nor fin1p regulate the phosphorylation of cdc11p
PMID:12546793	PBO:0094970	(see the Supplementary) Additional experiments indicated that neither mph1p nor fin1p regulate the phosphorylation of cdc11p
PMID:12546793	PBO:0094976	Less than 10% of these cells had cdc7p on the spindle pole body, consistent with previous studies [25].
PMID:12546793	FYPO:0007890	(Figure 2B). Immunofluorescence showed that byr4p was also present on the SPB in the arrested cells
PMID:12546793	PBO:0094973	(Figure 3B). However, at 36+C, when cdc11p is no longer associated with the SPB [3, 4], most of the cdc11p was hypophosphorylated (form 1)
PMID:12546793	PBO:0094970	(see the Supplementary) Additional experiments indicated that neither mph1p nor fin1p regulate the phosphorylation of cdc11p
PMID:12546793	PBO:0094970	(Figure 1D) The hyperphosphorylated form (3) of cdc11p was observed during mitosis in both sid2-250 and sid1- 239 mutants
PMID:12546793	PBO:0094970	(Figure 1D) The hyperphosphorylated form (3) of cdc11p was observed during mitosis in both sid2-250 and sid1- 239 mutants
PMID:12546793	PBO:0094970	(Figure 1D) The hyperphosphorylated form (3) of cdc11p was observed during mitosis in both sid2-250 and sid1- 239 mutants
PMID:12546793	PBO:0094973	(Figure 1E) In contrast, in cdc7-24, the hyperphosphorylated form of cdc11p (3) was greatly reduced, and the intensity of the hypophosphorylated forms (1 and 2) increased
PMID:12546793	PBO:0094973	(comment: DNS)
PMID:12546793	PBO:0094973	(Figure 1G) No significant hyperphosphorylation of cdc11p occurred at 36+C.
PMID:12546793	PBO:0108961	In contrast, in cdc7-24, the hyperphosphorylated form of cdc11p (3) was greatly reduced, and the intensity of the hypophosphorylated forms (1 and 2) increased (Figure 1E). A similar result was observed in cdc7-A20 (data not shown). Furthermore, no mitotic hyperphosphorylation of cdc11p was seen in spg1-B8 at the nonpermissive temperature (Figure 1E), when cdc7p does not localize to the SPB [13]. Finally, when cdc7 was expressed ectopically in G2-arrested cells, cdc11p accumulated in the hyperphosphorylated form (3) (Figure 1F).
PMID:12546793	PBO:0094973	(Figure 1G) No significant hyperphosphorylation of cdc11p occurred at 36+C .
PMID:12546793	PBO:0094972	(Figure 1C, and data not shown) Immunofluorescence indicated that both byr4p and cdc7p showed a normal, asymmetric distribution during mitosis
PMID:12546793	PBO:0094971	(Figure 1C, and data not shown) Immunofluorescence indicated that both byr4p and cdc7p showed a normal, asymmetric distribution during mitosis
PMID:12546793	PBO:0094970	(comment: CHECK HYPERPHOSPHORYLATION) (Figure 1C) In the mutant plo1-ts4, which is defective in SIN signaling but not spindle formation [10], hyperphosphorylated cdc11p was observed during mitosis, even though the cells were not septating .
PMID:12546793	GO:0031028	(comment: CHECK HYPERPHOSPHORYLATD FORM) Together, these data demonstrate, first, that mitotic cdc2p activity is not required for hyperphosphorylation of cdc11p and, second, that activation of the SIN correlates with accumulation of hyperphosphorylated cdc11p.
PMID:12546793	PBO:0094969	(Figure 1B) n G2-arrested cdc2-17 cells overexpressing spg1p, cdc11p was predominantly in the hyperphosphorylated form
PMID:12546793	PBO:0094968	(Figure 1A) In a mob1-R4 byr4::ura4Δ mutant, and also in cdc16-116 grown for 5 hr at 36+C, cdc11p accumulated in the hyperphosphorylated (3) form. Later: in mutants such as cdc16-116 or byr4::ura4Δ, in which cdc7p is present on both spindle pole bodies, the hyperphosphorylated form (3) of cdc11p is more abundant.
PMID:12546793	PBO:0094968	(Figure 1A) In a mob1-R4 byr4::ura4Δ mutant, and also in cdc16-116 grown for 5 hr at 36+C, cdc11p accumulated in the hyperphosphorylated (3) form
PMID:12565823	FYPO:0001035	(Fig. 4a)
PMID:12565827	PBO:0018339	(Fig. 2C)
PMID:12565827	PBO:0018345	(Fig. 2C)
PMID:12569356	PBO:0093631	UV irradiation resulted in the same phenotypes as those seen in the case of phleomycin: hob1D cells were more sensitive to the effects of UV irradiation than wild-type cells, while hob3D cells were as resistant to UV as were their wild-type cohorts (Figure 4b).
PMID:12569356	PBO:0093773	Treatment of hob1D cells with the DNA strand-breaking drug phleomycin, a bleomycin analog that is cytotoxic to yeasts (Pramanik et al., 1995), resulted in a marked hypersensitivity in hob1D cells (Figure 4a). In
PMID:12569356	PBO:0112860	Thus, unlike RVS167 in budding yeast, hob1+ was dispensable for endocytosis in fission yeast.
PMID:12569356	PBO:0112859	On nitrogen-poor medium or on medium of high osmolarity (i.e. YE/250 mm NaCl), we observed no differences in the growth of hob1+ and hob1D cells (Figure 2c).
PMID:12569356	FYPO:0003183	(Figure 4a). In contrast, treatment of hob3D cells did not produce a hypersensitive phenotype.
PMID:12569356	PBO:0093770	Microscopic examination of hob1D cells revealed them to be slightly but not significantly elongated, relative to an isogenic hob1+ strain (Figure 2b).
PMID:12569356	FYPO:0000969	UV irradiation resulted in the same phenotypes as those seen in the case of phleomycin: hob1D cells were more sensitive to the effects of UV irradiation than wild-type cells, while hob3D cells were as resistant to UV as were their wild-type cohorts (Figure 4b).
PMID:12589755	FYPO:0000268	same as crb2delta alone
PMID:12604790	GO:1904931	(comment: assayed with other MCM subunits present)
PMID:12606573	PBO:0099170	In zygotes undergoing meiotic divisions, WT Bub1±GFPp became associated with the centromeres after meiotic prophase and remained associated until anaphase I, con®rming previous reports using ®xed cells (Bernard et al., 2001; Figure 7B, WT, f±h).
PMID:12606573	PBO:0099173	normal rate of spindle phase I elongation. MI spindle elongation time is reduced to 40 min in rec7-146 bub1D cells (Figure 8Ad, upper panel)
PMID:12606573	PBO:0099171	(Figure 7B)
PMID:12606573	PBO:0099172	(Figure 7C,a)
PMID:12606573	PBO:0099173	decreased rate of spindle phase I elongation (70 mins. vs 40 wt)
PMID:12606573	FYPO:0005634	(Figure 4E)
PMID:12606573	FYPO:0005634	(Figure 7A)
PMID:12606573	FYPO:0005634	(Figure 7A)
PMID:12606573	FYPO:0005634	(Figure 7A)
PMID:12606573	PBO:0099167	(Figure 7A)
PMID:12606573	FYPO:0000091	(Figure 3A) during spindle checkpoint
PMID:12606573	PBO:0116210	in vitro assay for activity, phenotype for process
PMID:12606573	PBO:0099171	(Figure 7B)
PMID:12606573	PBO:0035223	In zygotes undergoing meiotic divisions, WT Bub1±GFPp became associated with the centromeres after meiotic prophase and remained associated until anaphase I, con®rming previous reports using ®xed cells (Bernard et al., 2001; Figure 7B, WT, f±h).
PMID:12653962	PBO:0035689	(Fig. 6B)
PMID:12653962	PBO:0035689	(Fig. 6B)
PMID:12653962	PBO:0106919	(Fig. 6B)
PMID:12653962	PBO:0106919	(Fig. 6B)
PMID:12654901	FYPO:0002141	DNS
PMID:12654901	FYPO:0001022	DNS
PMID:12654901	GO:0036391	(Fig. 6)
PMID:12654901	PBO:0101311	(Fig. 7a)
PMID:12654901	FYPO:0001971	data not shown
PMID:12654901	PBO:0101313	(Fig. 8)
PMID:12654901	PBO:0101312	(Fig. 7)
PMID:12654901	FYPO:0001971	(Fig. 7b)
PMID:12654901	GO:0032176	(Fig. 6)
PMID:12654901	PBO:0101310	(Fig. 2) (comment: maximum 3 septa)
PMID:12654901	GO:0036391	(Fig. 6)
PMID:12654901	GO:0032176	(Fig. 6)
PMID:12654901	FYPO:0001420	DNS
PMID:12654901	PBO:0101311	(Fig. 7c)
PMID:12654901	FYPO:0004652	"""exhibited well-defined, normal actin rings"""
PMID:12654901	FYPO:0001971	(Fig. 2)
PMID:12654901	FYPO:0004097	(Fig. 3)
PMID:12654901	FYPO:0001971	(Fig. 2)
PMID:12654901	FYPO:0006399	(Fig. 4, B and C)
PMID:12654901	PBO:0101309	(Fig. 2) (comment: maximum 3 septa)
PMID:12654901	FYPO:0001037	DNS
PMID:12654901	FYPO:0000674	DNS
PMID:12654901	PBO:0098144	(Fig. 8)
PMID:12668659	FYPO:0001492	(Fig. 8)
PMID:12668659	FYPO:0000132	(Fig. 8)
PMID:12668659	FYPO:0001234	(Fig. 8)
PMID:12668659	FYPO:0006821	(Fig. 8)
PMID:12668659	FYPO:0000021	(Fig. 8)
PMID:12668659	PBO:0094588	(Fig. 5)
PMID:12668659	PBO:0106201	unpublished obsevation
PMID:12668659	FYPO:0000339	(Fig. 1)
PMID:12668659	FYPO:0001971	(Fig. 1)
PMID:12668659	FYPO:0002060	(Fig. 1)
PMID:12668659	PBO:0098144	(Fig. 7D)
PMID:12668659	PBO:0106209	(Fig. 5)
PMID:12668659	PBO:0106209	(Fig. 5)
PMID:12668659	PBO:0106209	(Fig. 5)
PMID:12668659	FYPO:0001971	(Fig. 5)
PMID:12668659	FYPO:0001971	(Fig. 5)
PMID:12668659	FYPO:0001971	(Fig. 5)
PMID:12668659	GO:0036391	(Fig. 2a) colocalizes with sep3
PMID:12668659	PBO:0101311	(Fig. 5)
PMID:12668659	FYPO:0001971	(Fig. 5)
PMID:12668659	FYPO:0001971	(Fig. 5)
PMID:12668659	PBO:0106208	(Fig. 4)
PMID:12668659	PBO:0102770	(Fig. 4)
PMID:12668659	PBO:0106202	(Fig. 3C)
PMID:12668659	PBO:0106202	(Fig. 3C)
PMID:12668659	PBO:0106207	(Fig. 3)
PMID:12668659	PBO:0106206	(Fig. 3)
PMID:12668659	PBO:0106205	(Fig. 3)
PMID:12668659	PBO:0106204	(Fig. 3)
PMID:12668659	PBO:0106203	(Fig. 3A, lanes 1 and 7) (control)
PMID:12668659	PBO:0106202	(Fig. 3A, lanes 1 and 7)
PMID:12668659	GO:0031097	(Fig. 2a)
PMID:12668659	PBO:0106201	unpublished obsevation
PMID:12676088	PBO:0099284	(comment: CHECK telomerase regulator)
PMID:12697806	FYPO:0002687	(comment: after 100 generations)
PMID:12715160	FYPO:0001490	(comment: salt stres)
PMID:12715160	PBO:0020891	(comment: salt stress)
PMID:12719471	FYPO:0000732	(comment: at anaphase?)
PMID:12719471	FYPO:0003217	(comment: CHECK abolished)
PMID:12719471	FYPO:0000732	(comment: CHECK at anaphase?)
PMID:12748297	PBO:0114953	ChIP assay indicated that Rad21 associates with ribosomal DNA (rDNA) rather than telomere-associated sequences (see below). Moreover, fluorescence microscopy revealed that Rad21 tagged with GFP colocalizes mostly with a nucleolar protein, Gar1 (3), tagged with CFP in the horsetail nucleus (Fig. 1A). These results suggest that Rad21 is enriched in the nucleolus, rather than telomere-adjacent DNA sequences, although residual association with other chromosomal regions might also occur
PMID:12748297	PBO:0114954	The rad21-K1 mutation by itself showed no meiotic defect. However, when rec8 was combined with rad21-K1, the equational segregation at meiosis I was partly disrupted with the reductional population increasing to ∼40% (Fig. 2B).
PMID:12748297	GO:0045143	We conclude that Rad21 plays a role in ensuring equational segregation during meiosis I in rec8 cells.
PMID:12750522	PBO:0114994	(Figure 1B)
PMID:12750522	PBO:0105669	Moreover, the overexpression of psc3 leads to partial recovery of the arm cohesion defect of rec11 , but the recombination defect remains unimproved (fig. S3).
PMID:12750522	PBO:0114996	Nonrandom segregation of homologs in rec11Δ cells (different from rec12 cells) can be explained by residual levels of recombination (15) and presumably, residual cohesion as well. rec11Δ cells undergo faithful disjunction during meiosis II (fig. S2C), indicating that centromeric cohesion persists through meiosis I.
PMID:12750522	FYPO:0006521	Mitotic cells carrying a temperature-sensitive allele of psc3 (psc3-2T) (18) displayed extensive separation of cut3-GFP dots (fig. S2B)
PMID:12750522	FYPO:0003613	whereas arm cohesion of psc3-2T cells is completely intact during meiotic prophase (fig. S2C).
PMID:12750522	FYPO:0000488	In contrast to the dramatic reduction of meiotic recombination in rec11 cells, wild-type levels of recombination occur in psc3-2T cells (fig. S2D).
PMID:12750522	GO:0071962	Thus, Psc3 plays a crucial role in kinetochore regulation at both meiotic divisions, and this function of Psc3cannot be replaced by overexpression of Rec11.
PMID:12750522	FYPO:0001355	In contrast, the Rec8-Rec11 pair sustains mitotic growth better than Rec8-Psc3 (Fig. 1D; fig. S4A), underscoring the meiosis specificity of kinetochore regulation by Rec8-Psc3.
PMID:12750522	PBO:0109096	During meiotic prophase, Rec8 first appears at thecentromeres and later distributes throughout thechromosome (Fig. 2A) The data reveal that Rec8 associates more with centromere regions than with chromosome arms (20)
PMID:12750522	PBO:0114998	At anaphase of meiosis I, Rec11 signals become faint in the nucleus, but Psc3 persists, together with Rec8, at the clustered centromeres (Fig. 2C). The centromeric Rec8-Psc3 dots disappear at meiosis II.
PMID:12750522	PBO:0114998	At anaphase of meiosis I, Rec11 signals become faint in the nucleus, but Psc3 persists, together with Rec8, at the clustered centromeres (Fig. 2C).The centromeric Rec8-Psc3 dots disappear at meiosis II.
PMID:12750522	FYPO:0000670	(comment: CHECK ******premature sister kinetochore separation in meiosis I********) Reinforcing the foregoing results, clr4 cells frequently display precocious separation of cen2-GFP signals (Fig. 3C) and a decreased level of Rec8 at the centromeres if arrested after meiosis I (Fig. 3D).
PMID:12750522	PBO:0109096	In contrast, Psc3 associates exclusively with the centromere, showing a centromere-enrichment ratio 4 times higher than Rec8 and 20 times higher than Rec11 (Fig. 2B).
PMID:12750522	PBO:0114995	Experiments in which cen3 were marked with GFP on both homologs revealed that >20% of rec11Δ cells exhibit homolog nondisjunction, in which both homolog pairs move to the same pole at meiosis I (Fig. 1C).
PMID:12750522	FYPO:0002219	(Figure 1B)
PMID:12750522	PBO:0115000	(comment: CHECK MEIOTIC!********************) The level of Rec8 association with pericentromeric regions is markedly reduced in these mutants, whereas Rec8 is still enriched at the central core (Fig. 3A).
PMID:12750522	PBO:0114999	At anaphase of meiosis I, Rec11 signals become faint in the nucleus
PMID:12750522	FYPO:0002219	The control rec8 overexpressing (o.p.) psc3 rec11 cells undergo proper meiotic chromosome segregation, both reductional (meiosis I) and equational (meiosis II).
PMID:12750522	FYPO:0003178	The control rec8 overexpressing (o.p.) psc3 rec11 cells undergo proper meiotic chromosome segregation, both reductional (meiosis I) and equational (meiosis II).
PMID:12750522	FYPO:0004159	expression of the Rec8-Rec11 pair sustains viability of rad21 psc3 cells (Fig. 1D), thus allowing meiotic induction in the complete absence of Psc3). However, rec8 o.p. psc3 rec11 o.p. cellsshow defective sister chromatid movement atboth meiotic divisions (Fig. 1D).
PMID:12750522	FYPO:0003182	expression of the Rec8-Rec11 pair sustains viability of rad21 psc3 cells (Fig. 1D), thus allowing meiotic induction in the complete absence of Psc3However, rec8 o.p. psc3 rec11 o.p. cellsshow defective sister chromatid movement atboth meiotic divisions (Fig. 1D).
PMID:12750522	GO:0051754	Thus, Psc3 plays a crucial role in kinetochore regulation at both meiotic divisions, and this function of Psc3 cannot be replaced by overexpression of Rec11.
PMID:12750522	FYPO:0002219	(Figure 1B)
PMID:12750522	PBO:0115003	At meiosis II, however, sisters fail to segregate properly, undergoing nondisjunction in 20 to 40% of cells (Fig. 3B). The defect in meiosis II is more penetrating in clr4 cells than in swi6 cells, with a pattern approximating random segregation.
PMID:12750522	PBO:0112497	At meiosis II, however, sisters fail to segregate properly, undergoing nondisjunction in 20 to 40% of cells (Fig. 3B).
PMID:12750522	FYPO:0002219	Moreover, homologous chromosomes undergo faithful disjunction at meiosis I in these mutants (Fig. 3C) (17).
PMID:12750522	FYPO:0006426	In swi6 and clr4 cells marked on one pair of sister chromatids with cen1-GFP, sister chromatid pairs move together to the same nucleus during meiosis I, indicating that monopolar attachment is intact in these mutants (Fig. 3B).
PMID:12750522	PBO:0114997	Moreover, the overexpression of psc3 leads to partial recovery of the arm cohesion defect of rec11 , but the recombination defect remains unimproved (fig. S3).
PMID:12750522	FYPO:0002219	Moreover, homologous chromosomes undergo faithful disjunction at meiosis I in these mutants (Fig. 3C) (17).
PMID:12750522	FYPO:0006426	In swi6 and clr4 cells marked on one pair of sister chromatids with cen1-GFP, sister chromatid pairs move together to the same nucleus during meiosis I, indicating that monopolar attachment is intact in these mutants (Fig. 3B).
PMID:12750522	PBO:0115002	(comment: CHECK MEIOTIC!MEIOTIC.*************) whereas Rec8 is still enriched at the central core (Fig. 3A).
PMID:12750522	PBO:0115002	(comment: CHECK MEIOTIC!MEIOTIC.*************) whereas Rec8 is still enriched at the central core (Fig. 3A).
PMID:12750522	PBO:0115001	(comment: CHECK MEIOTIC!MEIOTIC!***********************) The level of Rec8 association with pericentromeric regions is markedly reduced in these mutants, whereas Rec8 is still enriched at the central core (Fig. 3A).
PMID:12750522	PBO:0115000	(comment: CHECK MEIOTIC!MEIOTIC!***********************) The level of Rec8 association with pericentromeric regions is markedly reduced in these mutants, whereas Rec8 is still enriched at the central core (Fig. 3A).
PMID:12750522	PBO:0115001	(comment: CHECK MEIOTIC!***********************) The level of Rec8 association with pericentromeric regions is markedly reduced in these mutants, whereas Rec8 is still enriched at the central core (Fig. 3A).
PMID:12750522	FYPO:0005509	Indeed, psc3-2T cells show defects in sister chromatid segregation during meiosis (fig. S2E). To
PMID:12750522	PBO:0114993	However, rec11Δ cells often contain three or four cut3-GFP dots (Fig. 1A), representing dissociation in these regions, as observed in rec11Δ cells.
PMID:12759375	FYPO:0000737	(comment: CHECK meiosis II)
PMID:12764130	PBO:0038194	(Fig. 3A) tea1 delta is a temperature dependent suppressor of loss of skb15
PMID:12764130	PBO:0098304	(Fig. 1) GST tea1 directly phosphorylated by Shk1 in vitro Fig2A GST-tea1 is phosphorylated in vivo in a Shk1 dependent manner
PMID:12764130	PBO:0038207	Data not shown. (comment: CHECK pREP3X tea1 is a multi copy plasmid and is over expressed from the nmt1 promoter)
PMID:12764130	PBO:0038206	(Fig. 8) (comment: CHECK pREP3X tea1 is a multi copy plasmid and is over expressed from the nmt1 promoter)
PMID:12764130	PBO:0038205	(Fig. 7B, C) (comment: Penetrance refers to the penetrance of the NTR old-new end growth pattern)
PMID:12764130	PBO:0102652	(Fig. 2B) shk1 K415R mutant is expressed from a weak allele of nmt1 promoter ON but does not say whether it is expressed at wild type levels. pREP4XGST-tea1 is a multi copy plasmid promoter ON
PMID:12764130	PBO:0101140	(Fig. 7A)
PMID:12764130	PBO:0035685	(Fig. 5D)
PMID:12764130	PBO:0103985	(Fig. 4B)
PMID:12764130	PBO:0099010	(Fig. 4C, D) Cells shown a normal tea1 delta actin morphology
PMID:12764130	PBO:0103986	(Fig. 4E)
PMID:12764130	PBO:0038199	(Fig. 4F) Cells have a similar defect to a tea1 delta cell wall defect
PMID:12764130	PBO:0038200	(Fig. 5B)
PMID:12764130	PBO:0038201	(Fig. 5C, D)
PMID:12764130	PBO:0038202	Data not shown
PMID:12764130	PBO:0038203	(Fig. 6D)
PMID:12764130	PBO:0033269	(Fig. 6B, C)
PMID:12764130	PBO:0038196	(Fig. 4B)
PMID:12764130	PBO:0103984	(Fig. 1B,C) demonstrates in vitro kinase activity. 2A in vivo
PMID:12764130	PBO:0038195	(Fig. 3B) ii
PMID:12764130	PBO:0093701	(Fig. 3B) Cells shown a normal tea1 delta morphology
PMID:12773390	FYPO:0002106	(Figure 1b) (comment: is described as a pear, but is cylindrical short and wide....)
PMID:12773390	FYPO:0002060	(Fig. 1a)
PMID:12773390	FYPO:0002060	(Fig. 1a)
PMID:12773390	FYPO:0002061	(Fig. 1a)
PMID:12773390	FYPO:0002061	(Figure 1a)
PMID:12773390	FYPO:0002060	(Figure 1a)
PMID:12773390	FYPO:0002061	(Figure 1a)
PMID:12773390	FYPO:0000113	(Figure 1E)
PMID:12773390	FYPO:0000113	(Figure 1E)
PMID:12773390	FYPO:0000113	(Figure 1E)
PMID:12773390	FYPO:0000113	(Figure 1E)
PMID:12773390	GO:0005515	(Figure 1F)
PMID:12773390	GO:0005515	(Figure 1F)
PMID:12773390	PBO:0092730	(Fig. 2)
PMID:12773390	PBO:0025603	(Fig. 2)
PMID:12773390	PBO:0093562	(Fig. 3a)
PMID:12773390	PBO:0093562	(Fig. 3a)
PMID:12773390	PBO:0093562	(Fig. 3a)
PMID:12773390	FYPO:0000964	(Fig. 3a)
PMID:12773390	FYPO:0000964	(Fig. 3a)
PMID:12773390	PBO:0093562	(Fig. 3a)
PMID:12773390	PBO:0106635	(Fig. 3b) (comment: WT 11%)
PMID:12773390	PBO:0106636	(Fig. 3b) ((comment: WT 11%)
PMID:12773390	PBO:0100335	(Fig. 4a)
PMID:12773390	PBO:0099328	(Fig. 4a)
PMID:12773390	GO:1905560	(Figure 4A and B)
PMID:12773390	GO:0000785	(Figure 5B)
PMID:12773390	FYPO:0002060	(Fig. 6a)
PMID:12773390	FYPO:0002061	(Fig. 6a)
PMID:12773390	MOD:00046	(Figure 7A and B)
PMID:12773390	MOD:00047	(Figure 7A and B)
PMID:12773390	MOD:00046	(Figure 7A and B)
PMID:12773390	PBO:0112007	(Figure 4A and B)
PMID:12773392	PBO:0093587	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	GO:0032221	Identi®cation of Clr6-associated proteins, (Figure 1B)/ Alp13, Prw1 and Pst2 are stably associated with Clr6 in vivo (Figure 3A)
PMID:12773392	FYPO:0005309	Interestingly, we noticed that Dprw1 causes an increase in the acetylation of H4 Lys5 and Lys12, a pattern of acetylation known to be associated with newly synthesized histones (Sobel et al., 1995).
PMID:12773392	FYPO:0000892	Moreover, Dprw1 cells showed an increase in acetylation of H3 Lys9 and Lys14.
PMID:12773392	FYPO:0000892	Cells carrying Dalp13 were speci®cally defective in the removal of acetyl groups present on H3 Lys9 and Lys14, as well as H4 Lys5 and Lys8.
PMID:12773392	FYPO:0005308	Cells carrying Dalp13 were speci®cally defective in the removal of acetyl groups present on H3 Lys9 and Lys14, as well as H4 Lys5 and Lys8.
PMID:12773392	GO:0004407	Af®nity-puri®ed Clr6-HA and control wild-type fractions were incubated with [3H]acetyllabelled histones. Quantitation of released [3H]acetyl groups revealed that the Clr6-HA fraction possesses deacetylase activity and that this activity is sensitive to trichostatin A (TSA), a speci®c inhibitor of HDACs (Figure 1C).
PMID:12773392	FYPO:0005310	The Dpst2 cells showed a signi®cant increase in acetylation of most lysine residues on H3 and H4 tails, except H4 Lys8.
PMID:12773392	FYPO:0007632	The Dpst2 cells showed a signi®cant increase in acetylation of most lysine residues on H3 and H4 tails, except H4 Lys8.
PMID:12773392	GO:0032129	These data suggest that Clr6 and its associated factors are involved in the deacetylation of histones in vivo.
PMID:12773392	GO:0031078	These data suggest that Clr6 and its associated factors are involved in the deacetylation of histones in vivo.
PMID:12773392	GO:0034739	These data suggest that Clr6 and its associated factors are involved in the deacetylation of histones in vivo.
PMID:12773392	GO:0140937	These data suggest that Clr6 and its associated factors are involved in the deacetylation of histones in vivo.
PMID:12773392	PBO:0103767	Our analysis revealed that mutant strains display defects in the segregation, resolution and/or condensation of chromosomes during mitosis (Figure 6A), and mis-segregated the mini-chromosome Ch16 (a 530 kb derivative of chromosome 3; Niwa et al., 1986) at a signi®cantly higher rate than wild-type cells (Figure 6C).
PMID:12773392	FYPO:0000082	and irreversible temperature-sensitive (Ts±) growth defects (Figure 5B±D).
PMID:12773392	PBO:0093587	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	PBO:0093587	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	PBO:0093616	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	PBO:0093616	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	FYPO:0000082	and irreversible temperature-sensitive (Ts±) growth defects (Figure 5B±D).
PMID:12773392	PBO:0093616	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	GO:0005730	Our analyses showed that all four proteins were localized predominantly in the nucleus on chromatin but excluded from the nucleolus (Figure 4A and B).
PMID:12773392	GO:0005730	Our analyses showed that all four proteins were localized predominantly in the nucleus on chromatin but excluded from the nucleolus (Figure 4A and B).
PMID:12773392	GO:0005730	Our analyses showed that all four proteins were localized predominantly in the nucleus on chromatin but excluded from the nucleolus (Figure 4A and B).
PMID:12773392	GO:0005730	Our analyses showed that all four proteins were localized predominantly in the nucleus on chromatin but excluded from the nucleolus (Figure 4A and B).
PMID:12773392	GO:0005634	Our analyses showed that all four proteins were localized predominantly in the nucleus on chromatin but excluded from the nucleolus (Figure 4A and B).
PMID:12773392	GO:0005634	Our analyses showed that all four proteins were localized predominantly in the nucleus on chromatin but excluded from the nucleolus (Figure 4A and B).
PMID:12773392	GO:0005634	Our analyses showed that all four proteins were localized predominantly in the nucleus on chromatin but excluded from the nucleolus (Figure 4A and B).
PMID:12773392	GO:0005634	Our analyses showed that all four proteins were localized predominantly in the nucleus on chromatin but excluded from the nucleolus (Figure 4A and B).
PMID:12773392	PBO:0103767	Our analysis revealed that mutant strains display defects in the segregation, resolution and/or condensation of chromosomes during mitosis (Figure 6A), and mis-segregated the mini-chromosome Ch16 (a 530 kb derivative of chromosome 3; Niwa et al., 1986) at a signi®cantly higher rate than wild-type cells (Figure 6C).
PMID:12773392	PBO:0111994	Our analysis revealed that mutant strains display defects in the segregation, resolution and/or condensation of chromosomes during mitosis (Figure 6A), and mis-segregated the mini-chromosome Ch16 (a 530 kb derivative of chromosome 3; Niwa et al., 1986) at a signi®cantly higher rate than wild-type cells (Figure 6C).
PMID:12773392	FYPO:0008183	We found that H3 Ser10 phosphorylation levels were considerably reduced in alp13, pst2 and clr6 mutant cells, except at 2±3 foci near the nuclear periphery, presumably representing heterochromatic loci (Figure 7)
PMID:12773392	FYPO:0008183	We found that H3 Ser10 phosphorylation levels were considerably reduced in alp13, pst2 and clr6 mutant cells, except at 2±3 foci near the nuclear periphery, presumably representing heterochromatic loci (Figure 7)
PMID:12773392	PBO:0103767	Our analysis revealed that mutant strains display defects in the segregation, resolution and/or condensation of chromosomes during mitosis (Figure 6A), and mis-segregated the mini-chromosome Ch16 (a 530 kb derivative of chromosome 3; Niwa et al., 1986) at a signi®cantly higher rate than wild-type cells (Figure 6C).
PMID:12773392	PBO:0093629	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	PBO:0093629	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	FYPO:0005310	Moreover, Dprw1 cells showed an increase in acetylation of H3 Lys9 and Lys14.
PMID:12773392	FYPO:0005310	Cells carrying Dalp13 were speci®cally defective in the removal of acetyl groups present on H3 Lys9 and Lys14, as well as H4 Lys5 and Lys8.
PMID:12773392	FYPO:0002363	The results presented in Figure 5E demonstrate that mutant strains show a signi®cant increase in histone acetylation levels compared with the wild-type control. Mutation in clr6 results in elevated acetylation levels at all residues tested on the histone H3 and H4 tails.
PMID:12773392	FYPO:0000892	The Dpst2 cells showed a signi®cant increase in acetylation of most lysine residues on H3 and H4 tails, except H4 Lys8.
PMID:12773392	FYPO:0007631	The Dpst2 cells showed a signi®cant increase in acetylation of most lysine residues on H3 and H4 tails, except H4 Lys8.
PMID:12773392	FYPO:0002365	The results presented in Figure 5E demonstrate that mutant strains show a signi®cant increase in histone acetylation levels compared with the wild-type control. Mutation in clr6 results in elevated acetylation levels at all residues tested on the histone H3 and H4 tails.
PMID:12773392	PBO:0093629	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	PBO:0093629	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	PBO:0093616	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	PBO:0093586	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	FYPO:0000082	and irreversible temperature-sensitive (Ts±) growth defects (Figure 5B±D).
PMID:12773392	FYPO:0000082	and irreversible temperature-sensitive (Ts±) growth defects (Figure 5B±D).
PMID:12773392	GO:0032221	Identi®cation of Clr6-associated proteins, (Figure 1B) /Alp13, Prw1 and Pst2 are stably associated with Clr6 in vivo (Figure 3A)
PMID:12773392	GO:0032221	Identi®cation of Clr6-associated proteins, (Figure 1B)/Alp13, Prw1 and Pst2 are stably associated with Clr6 in vivo (Figure 3A)
PMID:12773392	FYPO:0005309	Cells carrying Dalp13 were speci®cally defective in the removal of acetyl groups present on H3 Lys9 and Lys14, as well as H4 Lys5 and Lys8.
PMID:12773392	FYPO:0007631	Interestingly, we noticed that Dprw1 causes an increase in the acetylation of H4 Lys5 and Lys12, a pattern of acetylation known to be associated with newly synthesized histones (Sobel et al., 1995).
PMID:12773392	GO:0032221	Identi®cation of Clr6-associated proteins, (Figure 1B)/Alp13, Prw1 and Pst2 are stably associated with Clr6 in vivo (Figure 3A)
PMID:12773576	FYPO:0001859	(Figure 6C)
PMID:12773576	FYPO:0000892	(Figure 6C)
PMID:12773576	FYPO:0005310	(Figure 6C)
PMID:12773576	FYPO:0002827	(Figure 6A, 6B)
PMID:12773576	PBO:0104708	(comment: CHECK normal spatial extent of heterochromatin assembly (comment: JUST)
PMID:12773576	PBO:0104706	(comment: CHECK increased spatial extent of heterochromatin assembly) (comment: JUST)
PMID:12773576	PBO:0104707	(comment: outer repeats)
PMID:12773576	PBO:0104706	(comment: CHECK increased spatial extent of heterochromatin assembly) (comment: JUST, not at prpote4in coding gene!)
PMID:12773576	FYPO:0004238	(Figure 6C)
PMID:12786945	PBO:0112181	(comment: This comes from point mutation in FLEX moitf abolished transcription. Phenotype is not captured because the precise mutant could not be established.)
PMID:12789340	PBO:0097160	inferred from combination of FYPO:0005798 and FYPO:0005828
PMID:12791993	PBO:0095631	(Fig. 3E,F)
PMID:12791993	PBO:0095632	(Fig. 3E)
PMID:12791993	PBO:0094421	(Fig. 3E)
PMID:12791993	FYPO:0002026	(Fig. 4D)
PMID:12791993	PBO:0094469	(Fig. 3C)
PMID:12791993	FYPO:0006004	(Fig. 1A)
PMID:12791993	FYPO:0003838	(Fig. 1B, C) Cells arrest with a stable actinomyosin ring and fail to undergo cytokinesis
PMID:12791993	FYPO:0005689	(Fig. 1B) (comment: cell cycle arrest with post anaphase microtubule array)
PMID:12791993	FYPO:0003126	(Fig. 1A)
PMID:12791993	FYPO:0003126	(Fig. 2 E,F)
PMID:12791993	FYPO:0003303	(Fig. 4D, E, F)
PMID:12791993	PBO:0095628	(Fig. 3A)
PMID:12791993	FYPO:0003245	(Fig. 4D, E, F)
PMID:12791993	FYPO:0003126	data not shown
PMID:12791993	FYPO:0006004	data not shown
PMID:12791993	FYPO:0003126	data not shown
PMID:12791993	FYPO:0006004	data not shown
PMID:12791993	PBO:0095630	(Fig. 3C)
PMID:12791993	FYPO:0006005	(Fig. 4C) (displacemetn is supressed by inhibiting membrane trafficking
PMID:12791993	FYPO:0001400	(Fig. 2 E,F)
PMID:12791993	PBO:0095196	(Fig. 3C)
PMID:12791993	PBO:0095629	(Fig. 3C)
PMID:12796476	FYPO:0002021	(Figure 1D) but lacked both actin contractile rings and polarized actin patches (Fig. 1 D)
PMID:12796476	FYPO:0001357	(comment: control, functional fragment)
PMID:12796476	FYPO:0002061	Thus, Cdc12(FH1FH2)p can replace the essential functions of Cdc12p in vivo when Cdc12p is nonfunctional, but is toxic when overexpressed in the presence of functional Cdc12p.
PMID:12796476	FYPO:0005853	(Figure 1D) impressive enrichment of actin filaments in aberrant thick cables and aster-like accumulations
PMID:12796476	FYPO:0002437	(Figure 1D) impressive enrichment of actin filaments in aberrant thick cables and aster-like accumulations
PMID:12796476	PBO:0024260	(Figure 1D) but lacked both actin contractile rings and polarized actin patches (Fig. 1 D)
PMID:12796476	FYPO:0001493	(Figure 1D) arrested after 􏰖24 h (Fig. 1 E)
PMID:12796476	FYPO:0003210	(comment: CHECK abnormal (partial, broad, and misoriented) septa) (Fig. 1 G)
PMID:12796476	GO:0051015	(comment: barbed end actin capping)
PMID:12796476	GO:0051016	(comment: MF?)
PMID:12796476	GO:0030041	fission yeast Cdc12 (FH1FH2)p purified from bacteria (Fig. 1 B) stimulated actin polymerization, as detailed below (see Fig. 4). This is consistent with Cdc12(FH1FH2)p and MmCPcapping the barbed (fast depolymerizing) ends of the filaments with high affinity (Kd + 0.1 􏰂M), allowing dissociation only from the slowly depolymerizing (Pollard, 1986) pointed ends (Caldwell et al., 1989)
PMID:12796476	PBO:0106850	(comment: actin binding inhibitor pointed end)
PMID:12805221	MOD:00046	(comment: CHECK referred to in PMID:33137119)
PMID:12808043	PBO:0023748	(comment: dependent on sme2 expression)
PMID:12810074	GO:0005737	Comparison of mitochondria staining with GFP-Ung1 showed no detectable co-localization of Ung1 and mitochondria (Fig. 1B, right). Thus, these cellular localization studies indicate that fission yeast Ung1 is more similar to the nuclear form of human UNG as they both localized predominantly in the nucleus
PMID:12815070	PBO:0101128	(Fig. 2A)
PMID:12815070	FYPO:0001683	plo1.ts2 strains entered mitosis but did not form spindles
PMID:12815070	PBO:0101128	(Fig. 2A)
PMID:12815070	PBO:0101131	Kinase assays of these mitotic samples indicated that the cut12.s11 mutation promoted a 1.6 (±0.18; n = 5) in-crease in Plo1-specific activity during mitosis(Fig. 2D).
PMID:12815070	FYPO:0002061	Both plo1.ts2 and plo1.ts19 conferred temperature sensitivity for growth on minimal medium
PMID:12815070	FYPO:0002061	Both plo1.ts2 and plo1.ts19 conferred temperature sensitivity for growth on minimal medium
PMID:12815070	FYPO:0002061	ability to form colonies o nrich medium at 36°C was indistinguishable from that of wild-typec ells
PMID:12815070	FYPO:0002060	ability to form colonies o nrich medium at 36°C was indistinguishable from that of wild-typec ells
PMID:12815070	PBO:0101132	Western blot analysis showed that Plo1 levels in plo1.ts2cellswerenotradicallydifferentfromwild-type
PMID:12815070	PBO:0101133	full-length protein appeared to be largely absent from plo1.ts19 on either minimal or rich medium at either 25°C or 36°C (Fig. 7B)
PMID:12815070	PBO:0101133	full-length protein appeared to be largely absent from plo1.ts19 on either minimal or rich medium at either 25°C or 36°C (Fig. 7B)
PMID:12815070	FYPO:0000620	Unlike classic “cut” mutants (Hirano et al. 1986), septation did not always follow on from the mitoticarrest.
PMID:12815070	FYPO:0000276	plo1.ts2 strains entered mitosis but did not form spindles
PMID:12815070	FYPO:0000400	Whereas single plo1.ts2 and plo1.ts19 mutant and double cut12.s11 cdc25.22 mutant cells all entered mitosis (Fig. 9B,C), the single cdc25.22 mutant and both double cdc25.22 plo1.ts and triple cut12.s11 cdc25.22 plo1.ts mutants did not.
PMID:12815070	FYPO:0000400	Whereas single plo1.ts2 and plo1.ts19 mutant and double cut12.s11 cdc25.22 mutant cells all entered mitosis (Fig. 9B,C), the single cdc25.22 mutant and both double cdc25.22 plo1.ts and triple cut12.s11 cdc25.22 plo1.ts mutants did not.
PMID:12815070	PBO:0101135	Whereas cells in which the expression of the constitutively active mutant remained repressed arrested cell cycle progression in interphase, 11% of those in which it had been expressed entered mitosis.This degree of suppression is very similar to the level of suppression of cdc25.22 arising from the presence of the cut12.s11 mutation (Fig. 9B) and established that activation of Plo1 is sufficient to suppress the deficiency in Cdc25 function in cdc25.22 cells.
PMID:12815070	PBO:0101136	The extended and more random size of plo1.ts2 cells at division suggested that this may be the case. Despite the fact that these cells are able to enter mitosis,the appear to be doing so in a less efficient, or more random manner (Fig. 8B).
PMID:12815070	PBO:0101134	We concluded that the Plo1-dependent kinase activity of both plo1.ts2 and plo1.ts19 was greatly reduced.
PMID:12815070	PBO:0101137	Plo1.K65R, the “kinase dead” mutant protein,only associated with mitotic but not with interphase SPBs(data not shown).
PMID:12815070	PBO:0101129	This suggested that the inability to promote mitotic Plo1-associated kinase activity in cut12.1 cells was not a simple consequence of an inability to assemble a bipolar spindle,or an inability to commit to mitosis.Rather,the data indicate that Cut12 function was required for full activationof Plo1-associated kinase activity during mitotic commitment. Alspp Fig. 6B
PMID:12815070	PBO:0101128	(Fig. 2B)
PMID:12815070	FYPO:0002061	triple cut12.s11 cdc25.22 plo1.ts19 cells were unable to grow (Fig. 9A).
PMID:12815070	PBO:0101134	We concluded that the Plo1-dependent kinase activity of both plo1.ts2 and plo1.ts19 was greatly reduced.
PMID:12815070	FYPO:0002061	This established that mutating plo1 in a way that did not affect cell viability compromised the ability of cut12.s11 to suppress cdc25.22. Fig 9A. cdc25.22 and cdc25.22 plo1.ts19 cells, on the other hand, could not form colonies on this medium at this temperature, but cdc25.22 cut12.s11 cells could
PMID:12815070	PBO:0100189	(Figs. 1A,4C)
PMID:12815070	FYPO:0002061	(Fig. 9A) cdc25.22 and cdc25.22 plo1.ts19 cells, on the other hand, could not form colonies on this medium at this temperature, but cdc25.22 cut12.s11 cells could
PMID:12815070	PBO:0101130	Plo1-associated kinase activity of extracts from arrested cdc2.33 cut12.s11 cells was 2.4-fold(±0.35;n=6)higher than that of the control cdc2.33 cut12+ cells (Fig. 4D). This established that cut12.s11 increased Plo1 activity ininterphase.
PMID:12815070	PBO:0101128	(Fig. 2A)
PMID:12840005	FYPO:0005356	(comment: assayed using RTS1 mut2 or mut8 on plasmid)
PMID:12840005	FYPO:0005356	(comment: assayed using RTS1 mut2 or mut8 on plasmid)
PMID:12840005	PBO:0100890	(comment: assayed using RTS1 mut2 or mut8 on plasmid)
PMID:12840005	FYPO:0003084	(comment: assayed using RTS1 mut2 or mut8 on plasmid)
PMID:12840005	FYPO:0003084	(comment: assayed using RTS1 mut2 or mut8 on plasmid)
PMID:12840005	PBO:0100889	(comment: assayed using RTS1 mut2 or mut8 on plasmid)
PMID:12857865	FYPO:0003788	(Figure 7) (this protrusion is opposite side of nucleus to the SPB)
PMID:12857865	GO:0061496	(Fig. 2,3)
PMID:12857865	FYPO:0002061	(Fig. 4)
PMID:12857865	FYPO:0000276	(Fig. 4)
PMID:12857865	FYPO:0003738	(Fig. 4)
PMID:12857865	FYPO:0002061	(Figure 6A)
PMID:12857865	FYPO:0003165	(Figure 6A)
PMID:12857865	FYPO:0005023	(Figure 7) (this protrusion is opposite side of nucleus to the SPB)
PMID:12857865	FYPO:0002061	data not shown
PMID:12857865	FYPO:0002061	data not shown
PMID:12857865	FYPO:0000608	(Figure 7)
PMID:12861005	PBO:0093616	(comment: same as rad51d alone)
PMID:12861005	FYPO:0005402	(comment: same as taz1d alone)
PMID:12861005	FYPO:0005402	(comment: same as taz1d alone)
PMID:12861005	FYPO:0005402	(comment: same as taz1d alone)
PMID:12861005	FYPO:0005402	(comment: same as taz1d alone)
PMID:12861005	FYPO:0005402	(comment: same as taz1d alone)
PMID:12861005	FYPO:0005402	(comment: same as taz1d alone)
PMID:12861005	FYPO:0005402	(comment: same as taz1d alone)
PMID:12867036	FYPO:0000470	We observed a strong reduction in staining of sir2Δ compared to sir2+ cells, which indicated a reduced rate of switching to the opposite mating type in sir2Δ cells (Figure 2E, column 1).
PMID:12867036	PBO:0112507	Consistent with its weaker effect on silencing of otr1R::ura4+, deletion of sir2+ had only a weak effect on methylation of this ura4+ reporter (Figure 3B).
PMID:12867036	PBO:0108388	Consistent with its weaker effect on silencing of otr1R::ura4+, deletion of sir2+ had only a weak effect on methylation of this ura4+ reporter (Figure 3B).
PMID:12867036	PBO:0097399	Histone H3-K9 methylation levels at Kint2::ura4+ and imr1R::ura4+ were strongly reduced in sir2Δ compared to sir2+ cells (32- and 13-fold, respectively) (Figure 3B).
PMID:12867036	PBO:0111282	Moreover, the level of Swi6 associated with imr1R::ura4+ and otr1R::ura4+ reporters was reduced 8- and 3-fold, respectively, in sir2Δ compared to wild-type cells (Figure 3B).
PMID:12867036	PBO:0120487	Moreover, the level of Swi6 associated with imr1R::ura4+ and otr1R::ura4+ reporters was reduced 8- and 3-fold, respectively, in sir2Δ compared to wild-type cells (Figure 3B).
PMID:12867036	PBO:0111016	ChIP analysis showed that the level of Swi6 associated with Kint2::ura4+ was reduced 47-fold in sir2Δ compared to wild-type cells (Figure 3B).
PMID:12867036	FYPO:0006815	Compared to wild-type cells, in sir2Δ cells, acetylation of K9 was increased by 16-, 11-, and 7-fold at the ura4+ reporter inserted in the mating locus (Kint2::ura4+), the inner (imr1R::ura4+), and the outer centromeric repeats (otr1R::ura4+), respectively (Figure 3A).
PMID:12867036	FYPO:0007633	Compared to wild-type cells, in sir2Δ cells, acetylation of K9 was increased by 16-, 11-, and 7-fold at the ura4+ reporter inserted in the mating locus (Kint2::ura4+), the inner (imr1R::ura4+), and the outer centromeric repeats (otr1R::ura4+), respectively (Figure 3A).
PMID:12867036	PBO:0096301	Compared to wild-type cells, in sir2Δ cells, acetylation of K9 was increased by 16-, 11-, and 7-fold at the ura4+ reporter inserted in the mating locus (Kint2::ura4+), the inner (imr1R::ura4+), and the outer centromeric repeats (otr1R::ura4+), respectively (Figure 3A).
PMID:12867036	FYPO:0006681	Compared to wild-type cells, in sir2Δ cells, acetylation of K9 was increased by 16-, 11-, and 7-fold at the ura4+ reporter inserted in the mating locus (Kint2::ura4+), the inner (imr1R::ura4+), and the outer centromeric repeats (otr1R::ura4+), respectively (Figure 3A).
PMID:12867036	FYPO:0004690	Compared to wild-type cells, in sir2Δ cells, acetylation of K9 was increased by 16-, 11-, and 7-fold at the ura4+ reporter inserted in the mating locus (Kint2::ura4+), the inner (imr1R::ura4+), and the outer centromeric repeats (otr1R::ura4+), respectively (Figure 3A).
PMID:12867036	PBO:0094282	Deletion of sir2+ caused derepression of ura4+ at both loci (Figure 2D). However, this effect was much stronger at the imr repeats than at the otr repeats. While sir2Δ cells carrying imr1R::ura4+ did not form colonies on FOA-containing plates, mutant cells carrying otr1R::ura4+ showed appreciable growth on FOA plates (Figure 2D). These results indicated that Sir2 was required for silencing at the S. pombe centromeric DNA regions.
PMID:12867036	PBO:0096189	Deletion of sir2+ caused derepression of ura4+ at both loci (Figure 2D). However, this effect was much stronger at the imr repeats than at the otr repeats. While sir2Δ cells carrying imr1R::ura4+ did not form colonies on FOA-containing plates, mutant cells carrying otr1R::ura4+ showed appreciable growth on FOA plates (Figure 2D). These results indicated that Sir2 was required for silencing at the S. pombe centromeric DNA regions.
PMID:12867036	FYPO:0006670	We combined the sir2Δ mutant with REIIΔ and found that the sir2Δ REIIΔ double mutant had a strong haploid meiosis phenotype (Figure 2E).
PMID:12867036	FYPO:0007336	In contrast, sir2Δ L(BglII)::ade6+ cells formed white colonies, indicating loss of silencing of the reporter gene (Figure 2C).
PMID:12867036	GO:0046969	spSir2 efficiently deacetylated an H4 peptide with acetyl-lysine at position 16 (AcK16) and an H3 peptide with acetyl-lysine at position 9 (AcK9), compared to H4 peptides with acetyl-lysine at positions 5 (AcK5), 8 (AcK8), and 12 (AcK12) (Figure 1B).
PMID:12867036	GO:0046970	spSir2 efficiently deacetylated an H4 peptide with acetyl-lysine at position 16 (AcK16) and an H3 peptide with acetyl-lysine at position 9 (AcK9), compared to H4 peptides with acetyl-lysine at positions 5 (AcK5), 8 (AcK8), and 12 (AcK12) (Figure 1B).
PMID:12868054	FYPO:0000076	(comment: at 5 μg/ml)
PMID:12868054	FYPO:0004483	(Fig. 3)
PMID:12868054	FYPO:0000369	(Fig. 2b)
PMID:12868054	FYPO:0002061	While both wild-type and vps33Δ cells grew at 26 ◦ C, vps33􏰗 cells exhibited a temperature-sensitive growth at 37 ◦C (Figure 2A).
PMID:12868054	FYPO:0000096	(Fig. 7a)
PMID:12868054	FYPO:0005547	(Fig. 6)
PMID:12868054	FYPO:0000583	(Fig. 5)
PMID:12868054	PBO:0096587	strong sensitivity to 100 mM CaCl2 (Figure 4A)
PMID:12868054	PBO:0095634	n liquid YES medium at 27 ◦ C, the cells had a doubling time of ∼8 h, in contrast to 2 h 30 min for wild-type cells.
PMID:12868054	FYPO:0007286	(Fig. 7) (comment: CHECK prevacuolar compartment membrane)
PMID:12868054	FYPO:0003656	(comment: 4 mM)
PMID:12871901	FYPO:0000611	(comment: CHECK permissive for cdc25-22; restrictive for cdt2-M1)
PMID:12893961	FYPO:0004009	(Fig. 5)
PMID:12893961	FYPO:0001234	(Fig. 3)
PMID:12893961	FYPO:0002060	(Fig. 3)
PMID:12893961	FYPO:0002061	(Fig. 4)
PMID:12893961	FYPO:0002060	(Fig. 4)
PMID:12893961	FYPO:0002060	(Fig. 4)
PMID:12893961	FYPO:0002061	(Fig. 4)
PMID:12894167	PBO:0102429	"""These results indicate that Mal3 is required for the proper association of Tea2 with microtubules and suggest that Mal3 stabilizes the kinesin-microtubule interaction"""
PMID:12894167	PBO:0102431	(comment: LOCALIZES OK, IS NOT RETAINED)
PMID:12925774	PBO:0097003	(comment: during mitotic DNA replication initiation)
PMID:12951601	FYPO:0006346	(Fig. 1a) (comment: CHECK thinner discontinuous spindles fypo/issues/3208)
PMID:12951601	PBO:0104346	(Fig. 1c) cells 1 and 3 Furthermore, multiple Mad2 dots, which have never been seen in wild type cells
PMID:12951601	FYPO:0002061	(Fig. 1d)
PMID:12951601	FYPO:0003165	(Fig. 1e)
PMID:12951601	FYPO:0002061	(Fig. 1d)
PMID:12951601	FYPO:0002061	(Fig. 1d)
PMID:12951601	FYPO:0002061	(Fig. 1d)
PMID:12966087	GO:0000724	(comment: CHECK epistasis with Rhp51)
PMID:12966087	GO:0000724	(comment: CHECK epistasis with Rhp51)
PMID:12972434	PBO:0099028	These data indicate that the decrease in ribosomal protein L25-A observed in cpc2::ura4 cells is probably due to a defect in recruitment of its mRNA to polyribosomes. The decreased amounts of both sam1 and thi2 RNAs are sufficient to account for the lowered protein abundance of each in cpc2::ura4 cells. In contrast, the decline in the level of ribosomal protein Rpl25 in cpc2::ura4 cells is not likely to be caused by an inability to accumulate its mRNA transcript.
PMID:12972434	PBO:0099027	These data indicate that the decrease in ribosomal protein L25-A observed in cpc2::ura4 cells is probably due to a defect in recruitment of its mRNA to polyribosomes. The decreased amounts of both sam1 and thi2 RNAs are sufficient to account for the lowered protein abundance of each in cpc2::ura4 cells. In contrast, the decline in the level of ribosomal protein Rpl25 in cpc2::ura4 cells is not likely to be caused by an inability to accumulate its mRNA transcript.
PMID:12972434	GO:2000765	e pyruvate kinase, thiazole biosynthetic enzyme, and ribosomal protein L25-A
PMID:12972571	PBO:0100551	(comment: mcm4ts-td phenotype indicates that Cdc23 chromatin localization is independent of Mcm4)
PMID:12972571	PBO:0101303	(comment: CHECK ADD? late anaphase)
PMID:12972571	PBO:0104571	(comment: CHECK ADD? late anaphase)
PMID:1314171	GO:0015385	(comment: CHECK inhibited by CCCP)
PMID:1316996	FYPO:0002060	(comment: cdc2-E8 suppresses mitotic catastrophe at high temperature)
PMID:1316996	FYPO:0002060	(comment: CHECK cdc2-A21 suppresses mitotic catastrophe at high temperature)
PMID:1316996	PBO:0096052	(comment; HI used as substrate)
PMID:1316996	FYPO:0000839	cells inviable at all temperatures in presence of wee1+
PMID:1316996	FYPO:0000839	(comment: G2 arrest shown by FACS analysis)
PMID:1316996	FYPO:0004922	(comment: G2 arrest shown by FACS analysis)
PMID:1316996	FYPO:0000839	(comment: crosses with this mutant generate a high level of diploids.
PMID:1316996	FYPO:0001382	(comment: Hi used as substrate)
PMID:1316996	FYPO:0001382	(comment: Hi used as substrate)
PMID:1316996	PBO:0096052	(comment: HI used as substrate)
PMID:1316996	FYPO:0002060	(comment: cdc2-E9 suppresses mitotic catastrophe at high temperature)
PMID:1324908	GO:0003882	(comment: CHECK regulated by inositol)
PMID:1324908	FYPO:0000663	(comment: CHECK GO:0008444 CDP-DG synthase and GO:0003882 PS synthase)
PMID:1324908	GO:0008444	(comment: CHECK regulated by inositol)
PMID:1332977	GO:0003918	phosphorylated and dephosphorylated forms both active; no PR col 17 because no evidence that dephosphorylated form is physiologically relevant (dephosphorylated in vitro)
PMID:1332977	MOD:00046	3 sites in N-terminus (1-75) and 7 in C-terminus (1221-1485), but positions not determined
PMID:1372994	PBO:0107331	(comment: val: I used this to link to process term even though it isn't shown directly in this paper)
PMID:1396704	PBO:0094498	(comment: CHECK activated_by(CHEBI:17234))
PMID:1427071	PBO:0019031	(comment: CHECK hydroxyurea absent)
PMID:14519123	FYPO:0003270	(Fig. 4)
PMID:14519123	FYPO:0000087	(Fig. 4)
PMID:14519123	FYPO:0000103	(Fig. 4)
PMID:14519123	FYPO:0001712	(Fig. 3)
PMID:14519123	FYPO:0000037	(Fig. 3)
PMID:14528010	GO:1990238	(comment: specific for dsDNA at ds/ssDNA junction)
PMID:14528010	GO:0008821	( is not a resolvase - makes symmetric cuts on opposed strands across the junction but does not convert products to linear DNA molecules)
PMID:14532136	GO:0007129	(comment: there is good evidence for this, but not bullet proof)
PMID:14585996	PBO:0103276	(comment: CHECK in presence of hydroxyurea)
PMID:14585996	GO:0000785	phenotype indicates that mrc1/Phos:S604 has higher affinity for chromatin than Unphos:S604
PMID:14585996	PBO:0103275	(comment: CHECK in presence of hydroxyurea)
PMID:14585996	PBO:0094250	(comment: CHECK residue S604)
PMID:14585996	PBO:0094250	(comment: CHECK residue S604)
PMID:14599746	GO:0006284	(comment: rationale: increased transversion frequency indicates that 8-oxoG persists more in mutant, but normal indel frequency suggests not NER)
PMID:14599746	GO:0070914	(comment: inferred from increased mutation rate upon UV exposure in mutant)
PMID:14602073	PBO:0024047	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0110085	(comment: dependent on F-actin (assayed using Latruncilin A))
PMID:14602073	GO:0110085	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:14602073	PBO:0024047	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14602073	PBO:0024047	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14602073	PBO:0024047	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14602073	PBO:0024047	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0110085	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0110085	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:14602073	PBO:0018677	(comment: before late interphase)
PMID:14602073	PBO:0018844	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0110085	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:14602073	PBO:0018470	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14602073	PBO:0018470	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14602073	PBO:0018470	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14602073	PBO:0018470	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0110085	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0110085	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0110085	(comment: independent of F-actin (assayed using Latrunculin A))
PMID:14612233	GO:0004382	(comment: CHECK activated_by(CHEBI:29108)| activated_by(CHEBI:29035))
PMID:14633985	PBO:0094767	(Figure 7A)
PMID:14633985	PBO:0094770	(comment: from genetics and Sty1 consensus. Later papers say Activated Sty1 also phosphorylates Csx1)
PMID:14633985	PBO:0094766	(Figure 6B) decreased stability in response to oxidative stress
PMID:14633985	PBO:0094765	(Figure 6B). decreased stability in response to oxidative stress
PMID:14633985	PBO:0094765	decreased stability in response to oxidative stress (Figure 6B)
PMID:14633985	PBO:0094766	(Figure 6B) decreased stability in response to oxidative stress
PMID:14633985	PBO:0094759	This decrease correlated with a large drop in the amount of Atf1 protein (Figure 4C).
PMID:14633985	PBO:0094758	the large increase in atf1+ mRNA that is induced by H2O2 in wild-type cells was abolished in csx1D cells.
PMID:14633985	FYPO:0002061	The csx1D single mutant was less sensitive to H2O2 than the spc1D mutant, whereas the csx1D spc1D double mutant was more sensitive than the spc1D strain. These ®ndings were consistent with the idea that Csx1 and Spc1 have independent functions in oxidative stress tolerance.
PMID:14633985	PBO:0093578	(Fig. 1)
PMID:14633985	PBO:0093577	(Fig. 1)
PMID:14633985	PBO:0094756	As shown in Figure 2C, H2O2 induced robust phosphorylation of Spc1 in csx1D cells..... Csx1 is not necessary for Spc1 activation.
PMID:14633985	PBO:0093578	(Fig. 1c)
PMID:14633985	PBO:0093578	(Fig. 1c)
PMID:14633985	PBO:0093578	(Fig. 1)
PMID:14633985	FYPO:0005947	(Fig. 1)
PMID:14633985	PBO:0094387	(Fig. 1c)
PMID:14633985	PBO:0093612	(Fig. 1c)
PMID:14633985	PBO:0094760	The H2O2-induced increase in expression of pcr1+ mRNA, which encodes a binding partner of Atf1, was similarly eliminated in csx1D cells (Figure 4A
PMID:14633985	PBO:0094761	mRNA expression levels of two other transcription factor genes involved in oxidative stress, pap1+ and prr1+, were unaffected by the csx1D mutation (Figure 4A).
PMID:14633985	PBO:0094762	mRNA expression levels of two other transcription factor genes involved in oxidative stress, pap1+ and prr1+, were unaffected by the csx1D mutation (Figure 4A).
PMID:14633985	PBO:0094763	mRNA expression levels of two other transcription factor genes involved in oxidative stress, pap1+ and prr1+, were unaffected by the csx1D mutation (Figure 4A).
PMID:14633985	PBO:0094764	(Figure 4E)
PMID:14633985	GO:0005737	(Figure 6A) Csx1±GFP was detected in the cytoplasm and appeared to be excluded from the nucleus. This pattern of Csx1±GFP localization was unaffected by oxidative stress.
PMID:14633985	GO:0005634	(Figure 6A) Csx1±GFP was detected in the cytoplasm and appeared to be excluded from the nucleus. This pattern of Csx1±GFP localization was unaffected by oxidative stress.
PMID:14654689	PBO:0093620	(comment: same as rad50delta alone)
PMID:14654689	PBO:0093621	(comment: same as rad11-D223Y alone)
PMID:14654689	FYPO:0002239	(comment: same as rad11-D223Y alone)
PMID:14663827	PBO:0110127	(Figure 3)
PMID:14663827	PBO:0110125	(Figure 3)
PMID:14663827	PBO:0100628	(Figure 3) Our tea1 result differs from that of Rupes et al. (1999), who found that tea1 cells did not switch to bipolar growth after a LatA pulse. This may be due to differences in scoring or temperature between the experiments.
PMID:14663827	FYPO:0008131	(Figure 1) Tea3 cells resumed growth from their old end after division, indicating that the cell inheriting a growing end had no difficulty in reidentifying it as the appropriate site for growth after division (Figure 1).
PMID:14663827	PBO:0110124	(Figure 1) (comment: about 60% from old end)
PMID:14663827	PBO:0110124	(Figure 1) (comment: about 60% from old end)
PMID:14663827	PBO:0110123	(Figure 1) (comment: about 30% from old end)
PMID:14663827	PBO:0110126	(Figure 3)
PMID:14663827	PBO:0110127	(Figure 3)
PMID:14663827	PBO:0099081	(Figure 3)
PMID:14663827	PBO:0110128	(Figure 3)
PMID:14663827	PBO:0110129	(Figure 3)
PMID:14663827	PBO:0110132	(Figure 4) shows that tea1 cells at high temperatures displayed microtubules bending round the cell ends in accordance with previously published results (Mata and Nurse, 1997).
PMID:14663827	PBO:0110133	(Figure 4)
PMID:14663827	PBO:0110134	(Figure 4)
PMID:14663827	PBO:0110134	(Figure 4)
PMID:14663827	PBO:0110135	(Figure 4)
PMID:14663827	PBO:0110135	(Figure 4)
PMID:14663827	PBO:0110136	(Figure 5)
PMID:14663827	PBO:0037207	(Figure 5)
PMID:14663827	PBO:0110136	(Figure 5)
PMID:14663827	PBO:0106644	(Figure 5)
PMID:14663827	PBO:0110137	(Figure 5)
PMID:14663827	PBO:0110137	(Figure 5)
PMID:14663827	PBO:0110137	(Figure 5)
PMID:14663827	PBO:0110123	(Figure 1) about 30% from new end. In contrast, 14% of tea1 cells and 30% of pom1 cells failed to resume growth from a previously growing end (Figure 1).
PMID:14663827	PBO:0110122	(Figure 1) about 14% from new end In contrast, 14% of tea1 cells and 30% of pom1 cells failed to resume growth from a previously growing end (Figure 1).
PMID:14663827	FYPO:0003150	(Figure 2)
PMID:14704433	PBO:0110922	Furthermore, deletion of ago1+, dcr1+, or rdp1+ abolished the association of Chp1-Flag and Tas3-TAP with otr1::ura4+, as well as with centromeric repeat sequences (Fig. 4, A and B).
PMID:14704433	FYPO:0002834	A tas3 deletion strain carrying the ura4+ reporter gene inserted at innermost (imr) or outermost (otr) centromeric repeats of chromosome 1 (imr1R::ura4+ and otr1R::ura4+, respectively) displayed a loss of silencing of both reporter genes (Fig. 2D) to an extent similar to that of the deletion of sir2, chp1, or ago1 (Fig. 2D)
PMID:14704433	PBO:0110922	Furthermore, deletion of ago1+, dcr1+, or rdp1+ abolished the association of Chp1-Flag and Tas3-TAP with otr1::ura4+, as well as with centromeric repeat sequences (Fig. 4, A and B).
PMID:14704433	FYPO:0002834	A tas3 deletion strain carrying the ura4+ reporter gene inserted at innermost (imr) or outermost (otr) centromeric repeats of chromosome 1 (imr1R::ura4+ and otr1R::ura4+, respectively) displayed a loss of silencing of both reporter genes (Fig. 2D) to an extent similar to that of the deletion of sir2, chp1, or ago1 (Fig. 2D)
PMID:14704433	FYPO:0002566	Further, chromatin immunoprecipitation (ChIP) showed that Tas3 was required for H3-K9 methylation and Swi6 localization of a ura4+ reporter gene inserted at each of the above loci (Fig. 2E).
PMID:14704433	FYPO:0002834	A tas3 deletion strain carrying the ura4+ reporter gene inserted at innermost (imr) or outermost (otr) centromeric repeats of chromosome 1 (imr1R::ura4+ and otr1R::ura4+, respectively) displayed a loss of silencing of both reporter genes (Fig. 2D) to an extent similar to that of the deletion of sir2, chp1, or ago1 (Fig. 2D)
PMID:14704433	PBO:0110922	Furthermore, deletion of ago1+, dcr1+, or rdp1+ abolished the association of Chp1-Flag and Tas3-TAP with otr1::ura4+, as well as with centromeric repeat sequences (Fig. 4, A and B).
PMID:14704433	PBO:0110923	Deletion of tas3+ abolished the association of Chp1-Flag with otr1::ura4+, as well as with native cen sequences (Fig. 4C).
PMID:14704433	FYPO:0002834	A tas3 deletion strain carrying the ura4+ reporter gene inserted at innermost (imr) or outermost (otr) centromeric repeats of chromosome 1 (imr1R::ura4+ and otr1R::ura4+, respectively) displayed a loss of silencing of both reporter genes (Fig. 2D) to an extent similar to that of the deletion of sir2, chp1, or ago1 (Fig. 2D)
PMID:14730319	PBO:0104843	(Fig. 2c)
PMID:14730319	PBO:0104842	(Fig. 2c)
PMID:14730319	FYPO:0005648	(Fig. 2c)
PMID:14730319	PBO:0104847	(Fig. 4c)
PMID:14730319	PBO:0104848	(Fig. 4d,e)
PMID:14730319	PBO:0104849	(Fig. 4c)
PMID:14730319	PBO:0096804	(Fig. 4c)
PMID:14730319	PBO:0104851	(Fig. 4d)
PMID:14730319	FYPO:0002219	(Fig. 2a)
PMID:14730319	FYPO:0002060	(Fig. 4a)
PMID:14730319	PBO:0104845	(Fig. 2 and 3d)
PMID:14730319	FYPO:0000091	(Fig. 4a)
PMID:14730319	PBO:0112496	(Fig. 2a)
PMID:14739927	GO:0005515	(comment: CHECK interaction increases during cellular response to UV)
PMID:14739927	GO:0005515	(comment: CHECK proteins dissociate during cellular response to UV)
PMID:14742702	FYPO:0005343	(Figure 1B)
PMID:14742702	FYPO:0001978	(Figure 8E)
PMID:14742702	FYPO:0001733	(Figure 8E)
PMID:14742702	FYPO:0001355	(Figure 8E)
PMID:14742702	GO:0070850	(Figure 5A, lane 4)
PMID:14742702	GO:0070850	(Figure 5A, lane 4)
PMID:14742702	FYPO:0002400	(Figure 8E)
PMID:14742702	FYPO:0006195	(Figure 8E)
PMID:14742702	PBO:0094141	(Figure 4F)
PMID:14742702	PBO:0100547	(Figure 4E)
PMID:14742702	PBO:0100546	(Figure 4D)
PMID:14742702	PBO:0100545	(Figure 4D)
PMID:14742702	PBO:0100544	(Figure 3B)
PMID:14742702	PBO:0100543	(Figure 3B)
PMID:14742702	PBO:0100539	(Figure 4A)
PMID:14742702	PBO:0100542	(Figure 3B)
PMID:14742702	PBO:0100541	(Figure 3B)
PMID:14742702	PBO:0018346	(Figure 2A)
PMID:14742702	PBO:0100538	(Figure 1D)
PMID:14742702	PBO:0100540	(Figure 2D)
PMID:14742702	PBO:0100539	On temperature shift down to 20°C, Alp7-YFP localized only to the SPB (Figure 2B). This also indicates that Alp7 does not require a microtubule cytoskeleton to localize to the SPB.
PMID:14742702	PBO:0018346	(Figure 2A)
PMID:14742702	PBO:0100538	(Figure 1D)
PMID:14742702	PBO:0022298	(Figure 1D)
PMID:14742702	FYPO:0000177	(Figure 1C)
PMID:14742702	FYPO:0006048	(Figure 1C rows 2 and 3) (comment: chromosome missegregation in the cell of row 3, and see Supplementary Figure S1 for quantification of spindle intensity)
PMID:14742702	FYPO:0000141	(Figure 1C)
PMID:14742702	PBO:0100544	(Fig. 8C)
PMID:14742702	FYPO:0006173	(Figure 1B)
PMID:14742702	FYPO:0002638	(Figure 1A) inferred from increased duration of mitosis
PMID:14742702	FYPO:0000274	(Figure 1A)
PMID:14742702	GO:0005515	(Figure 6A)
PMID:14742702	GO:0005515	(Figure 6A)
PMID:14742702	PBO:0100548	(Figure 6B)
PMID:14766746	FYPO:0004384	(comment: filter binding assay)
PMID:14766746	PBO:0097028	(comment: filter binding assay)
PMID:14766746	FYPO:0004386	(comment: filter binding assay)
PMID:14766746	PBO:0097029	(comment: filter binding assay)
PMID:14972679	PBO:0022058	By metaphase I, 100% of cells (n 􏰆 100) contained a strong nuclear signal. Sgo1-GFP was concentrated in distinct foci in about half of these metaphase I cells (Figure 3A-2).
PMID:14972679	PBO:0106725	(Figures 1A and 2)
PMID:14972679	FYPO:0005509	(Figures 1A and 2)
PMID:14972679	PBO:0106721	(Figure 1B)
PMID:14972679	PBO:0106731	Furthermore, no Rec8-specific fluorescence at all could be detected in 10% of the mutant binucleates. In contrast, the distribution of Rec8- GFP fluorescence in Δsgo2 mutant binucleates was indistinguishable from wild-type.
PMID:14972679	FYPO:0004159	(Figures 1A and 2)
PMID:14972679	PBO:0106723	(Figure 1B)
PMID:14972679	PBO:0106722	(Figure 1B)
PMID:14972679	PBO:0106724	(Figures 1A and 2)
PMID:15004232	FYPO:0004766	(Figure 5F)
PMID:15040954	GO:0120542	(comment: CHECK qualifier=major)
PMID:15047861	FYPO:0000426	When the cells were labeled with FM4-64 for 60 min, the Δapm1 cells were highly fragmented compared with wild-type cells, consistent with the findings obtained by (Figure 7B)
PMID:15047861	FYPO:0002061	(Fig. 8c)
PMID:15047861	FYPO:0002258	When the cells were labeled with FM4-64 for 60 min, the Δapm1 cells were highly fragmented compared with wild-type cells, consistent with the findings obtained by (Figure 7B)
PMID:15047861	FYPO:0000650	(Fig. 6)
PMID:15047861	FYPO:0000349	(Figure 3B, a-c) accumulation of presumptive post-Golgi secretory vesicles and abnormal Golgi-like structures were also characteristic of the ypt3-i5 mutants that we reported previously (Cheng et al., 2002).
PMID:15047861	FYPO:0003279	(Figure 3B, a-c)
PMID:15047861	PBO:0093641	(Fig. 1)
PMID:15047861	PBO:0093595	(Fig. 1)
PMID:15047861	FYPO:0002061	(Fig. 1)
PMID:15047861	FYPO:0002060	(comment: DNS)
PMID:15047861	FYPO:0002061	(Fig. 1)
PMID:15047861	PBO:0093595	(Fig. 1)
PMID:15047861	PBO:0093641	(Fig. 1)
PMID:15047861	FYPO:0002061	(Fig. 1)
PMID:15047861	FYPO:0002060	(Fig. 1)
PMID:15052323	GO:0036374	Mix of IMP evidence & a proxy assay for hydrolase function
PMID:15062095	FYPO:0000901	the variant caused abnormal microtubule behavior in cell-end regions, which is likely to be the cause of the previously reported shape abnormalities
PMID:15068790	PBO:0104122	(Fig. 1)
PMID:15068790	PBO:0104133	(Fig. 7)
PMID:15068790	FYPO:0002818	(Fig. 7)
PMID:15068790	PBO:0104134	(Fig. 7)
PMID:15068790	PBO:0104132	(Fig. 7)
PMID:15068790	PBO:0104131	(Fig. 6)
PMID:15068790	PBO:0104131	(Fig. 6)
PMID:15068790	PBO:0104125	(Fig. 1)
PMID:15068790	PBO:0104130	(Fig. 2)
PMID:15068790	FYPO:0007985	(Fig. 2)
PMID:15068790	PBO:0104129	(Fig. 2)
PMID:15068790	PBO:0104128	(Fig. 2)
PMID:15068790	PBO:0104127	(Fig. 1)
PMID:15068790	PBO:0104126	(Fig. 1)
PMID:15068790	FYPO:0007114	(Fig. 1)
PMID:15068790	FYPO:0007983	(Fig. 1)
PMID:15068790	PBO:0104124	(Fig. 1)
PMID:15068790	PBO:0104123	(Fig. 1)
PMID:15068790	FYPO:0000339	(Fig. 1)
PMID:15121844	FYPO:0002134	three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site
PMID:15121844	FYPO:0002134	three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site
PMID:15121844	FYPO:0002134	three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site
PMID:15121844	FYPO:0002134	three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site
PMID:15121844	FYPO:0002357	three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site
PMID:15132994	FYPO:0006917	(comment: CHECK is this the correct term?)
PMID:15132994	PBO:0107121	We draw two conclusions from these data; first, association of Fin1 with the SPB requires activation of the SIN; second, recruitment of Fin1 to the SPB requires the SIN inhibitor Byr4, with which it interacts.
PMID:15132994	PBO:0107120	Fin1 failed to bind to the SPB when byr4+ was deleted (Table 1).
PMID:15132994	PBO:0107120	Fin1 binds Byr4. (A) Fin1 failed to associate withSPBs when the SIN was either inactive or hyperactive. Fin1 failed to bind to the SPB when byr4+ was deleted (Table 1).
PMID:15132994	PBO:0107120	(comment: Fin1 binds Byr4. (A) Fin1 failed to associate with SPBs when the SIN was either inactive or hyperactive.)
PMID:15132994	PBO:0033837	(Fig. 1c)
PMID:15132994	PBO:0018346	(Fig. 1c)
PMID:15147872	PBO:0096454	(Table 1)
PMID:15147872	PBO:0096453	(Table 1)
PMID:15147872	PBO:0037884	(Fig. 1A,B)
PMID:15147872	PBO:0096452	(Fig. 1A,B)
PMID:15147872	PBO:0037885	(Fig. 1C, 2)
PMID:15147872	PBO:0096456	(Fig. 2)
PMID:15147872	FYPO:0005342	(Fig. 3A)
PMID:15147872	PBO:0037889	(Fig. 4) abnormally segregating nuclear membrane #2863 PENDING
PMID:15147872	PBO:0096455	(Table 1)
PMID:15155581	PBO:0103071	(comment: basal phosphorylation on T412 & S423)
PMID:15155581	FYPO:0003489	(Fig. 3)
PMID:15155581	FYPO:0000267	(Fig. 3)
PMID:15155581	PBO:0103062	(Fig. 1)
PMID:15155581	FYPO:0000267	(Fig. 3)
PMID:15155581	PBO:0100925	(Fig. 1)
PMID:15155581	PBO:0103062	(Fig. 1)
PMID:15155581	PBO:0094252	(Fig. 1)
PMID:15155581	PBO:0103061	(Fig. 1)
PMID:15155581	PBO:0094252	(Fig. 1)
PMID:15155581	PBO:0103061	(Fig. 1)
PMID:15155581	PBO:0094252	(Fig. 1)
PMID:15155581	PBO:0093579	(Fig. 3)
PMID:15155581	PBO:0103061	(Fig. 1)
PMID:15155581	PBO:0094252	(Fig. 1)
PMID:15155581	PBO:0103061	(Fig. 1)
PMID:15155581	PBO:0103063	(Fig. 4)
PMID:15155581	FYPO:0000267	(Fig. 3)
PMID:15155581	PBO:0093579	(Fig. 3)
PMID:15155581	PBO:0093579	(Fig. 3)
PMID:15155581	PBO:0103064	(Fig. 2)
PMID:15155581	PBO:0103064	(Fig. 2)
PMID:15155581	PBO:0103062	(Fig. 2)
PMID:15155581	PBO:0103061	(Fig. 2)
PMID:15155581	PBO:0100925	(Fig. 2)
PMID:15155581	FYPO:0000267	(Fig. 3) (comment: same as either single mutant)
PMID:15155581	PBO:0093581	(Fig. 3)
PMID:15155581	PBO:0096806	(Fig. 3)
PMID:15155581	PBO:0097512	(Fig. 3)
PMID:15155581	PBO:0093579	(Fig. 3)
PMID:15155581	PBO:0093580	(Fig. 3)
PMID:15155581	FYPO:0003489	(Fig. 3)
PMID:15155581	PBO:0096806	(Fig. 3)
PMID:15155581	PBO:0103065	(Fig. 4)
PMID:15155581	PBO:0103065	(Fig. 4)
PMID:15155581	PBO:0103065	(Fig. 4)
PMID:15155581	PBO:0100317	(Fig. 5)
PMID:15155581	PBO:0100318	(Fig. 5)
PMID:15155581	PBO:0103063	(Fig. 4)
PMID:15155581	PBO:0103066	(Fig. 5)
PMID:15155581	PBO:0100317	(Fig. 5)
PMID:15155581	PBO:0103066	(Fig. 5)
PMID:15155581	PBO:0100318	(Fig. 5)
PMID:15161942	FYPO:0004418	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	FYPO:0004418	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	FYPO:0004418	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	FYPO:0004418	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	FYPO:0004418	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	FYPO:0004418	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	FYPO:0004418	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	FYPO:0004418	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	FYPO:0004418	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	FYPO:0004418	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	FYPO:0004397	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	FYPO:0004418	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	FYPO:0004418	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	FYPO:0004121	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	FYPO:0004418	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15161942	FYPO:0004418	a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.
PMID:15173168	PBO:0094255	(comment: CHECK residue T11)
PMID:15173168	PBO:0094255	(comment: CHECK residue T11)
PMID:15173168	PBO:0094255	(comment: CHECK residue T11)
PMID:15173168	PBO:0094255	(comment: CHECK residue T11)
PMID:15173168	PBO:0094254	(comment: CHECK residue T11)
PMID:15173168	PBO:0094255	(comment: CHECK residue T11)
PMID:15173168	PBO:0094255	(comment: CHECK residue T11)
PMID:15173168	PBO:0094255	(comment: CHECK residue T11)
PMID:15173168	PBO:0102382	(comment: CHECK residue T11)
PMID:15173168	PBO:0094255	(comment: CHECK residue T11)
PMID:15173168	PBO:0094255	(comment: CHECK residue T11)
PMID:15173168	PBO:0109147	inferred from phenotypes of mrc1delta, rad3delta, Cds1-Rad26 fusion, other cds1 alleles, and combinations thereof
PMID:15173383	FYPO:0002061	(comment: TEV protease present; Cdc6 truncated)
PMID:15173383	FYPO:0000444	(comment: TEV protease present; Cdc6 truncated)
PMID:15175657	FYPO:0002060	dns
PMID:15177031	PBO:0108149	data not shown
PMID:15177031	PBO:0103837	(Fig. 4A, B)
PMID:15177031	PBO:0108151	(Fig. 4A, B)
PMID:15177031	PBO:0103837	(Fig. 4E-H) Tip1YFP is expressed from endogenous tip1 gene tagged with YFP
PMID:15177031	PBO:0108151	(Fig. 4C) Tip1YFP is expressed from endogenous tip1 gene tagged with YFP
PMID:15177031	PBO:0108156	(Fig. 5A,B) (comment: Endogenous tea2 tagged with GFP)
PMID:15177031	PBO:0108157	(Fig. 5E,F) (comment: CHECK tea2-GFP is mildly overexpressed from the repressed integrated nmt1 promoter)
PMID:15177031	PBO:0108158	(comment: plus end directed)
PMID:15177031	PBO:0102694	(Fig. 6A,B) (comment: CHECK GFPmal3 is mildly overexpressed from the repressed nmt1 promoter)
PMID:15177031	PBO:0108159	(Fig. 6C,D) (comment: CHECK GFPmal3 is mildly overexpressed from the repressed nmt1 promoter)
PMID:15177031	PBO:0108155	(Fig. 6E)
PMID:15177031	PBO:0108160	(Fig. 6E)
PMID:15177031	PBO:0018345	colocalises with tip1
PMID:15177031	FYPO:0002060	(Fig. 2) (comment: CHECK same phenotype as tea2delta and tip1delta single mutants)
PMID:15177031	PBO:0108154	(Fig. 5C)
PMID:15177031	PBO:0108153	(Fig. 4I)
PMID:15177031	PBO:0102425	(Fig. 4E-H)
PMID:15177031	PBO:0103838	(Fig. 5A,B) (comment: Endogenous tea2 tagged with GFP)
PMID:15177031	PBO:0108155	(Fig. 5A,B) (comment: Endogenous tea2 tagged with GFP)
PMID:15177031	PBO:0037217	(Fig. 1) (comment: live imaging of Tip1YFP and CFP tubulin)
PMID:15177031	FYPO:0002760	(Fig. 2) (comment: CHECK same phenotype as tea2delta and tip1delta single mutants)
PMID:15177031	PBO:0037218	(Fig. 2) (comment: CHECK same phenotype as tea2delta and tip1delta single mutants)
PMID:15177031	PBO:0093701	(Fig. 2) (comment: CHECK same phenotype as tea2delta and tip1delta single mutants)
PMID:15177031	PBO:0108152	(Fig. 4C)
PMID:15177031	FYPO:0002760	(Fig. 5E,F) (comment: CHECK tea2-GFP is mildly overexpressed from the repressed integrated nmt1 promoter)
PMID:15177031	PBO:0037217	co-localises with tip1
PMID:15177031	PBO:0108150	data not shown
PMID:15184401	PBO:0097592	(Fig. 1C)
PMID:15184401	PBO:0097593	(Fig. 1C)
PMID:15184401	PBO:0097593	(Fig. 1C)
PMID:15184401	PBO:0097592	(Fig. 1C)
PMID:15184401	FYPO:0001122	(Fig. 1E)
PMID:15184401	FYPO:0001122	(Fig. 1E)
PMID:15184401	PBO:0094468	(Fig. 1C)
PMID:15184401	PBO:0094424	(Fig. 1C,3)
PMID:15184401	PBO:0097593	(Fig. 4D)
PMID:15184401	PBO:0097592	(Fig. 4D)
PMID:15184401	PBO:0097022	(Fig. 4F)
PMID:15184401	PBO:0097022	(Fig. 4F)
PMID:15184401	PBO:0097022	(Fig. 4F)
PMID:15184401	PBO:0097022	(Fig. 4F)
PMID:15184401	PBO:0097799	(G2) Fig. 6B
PMID:15184401	PBO:0097800	(Fig. 6B) (comment: CHECK G2)
PMID:15184401	PBO:0097799	(Fig. 6C) (comment: CHECK G2)
PMID:15184401	PBO:0097801	(Fig. 6F)
PMID:15184401	PBO:0097802	(Fig. 6F)
PMID:15184401	PBO:0097801	(Fig. 6F)
PMID:15184402	PBO:0037217	During mitosis, tea1p persists at the cell tips, whereas for3p and bud6p leave the cell tip and accumulate more at the cell division plane.
PMID:15184402	PBO:0100352	During mitosis, tea1p persists at the cell tips, whereas for3p and bud6p leave the cell tip and accumulate more at the cell division plane.
PMID:15189983	FYPO:0001490	(Figure 2)
PMID:15189983	FYPO:0001490	(Figure 2)
PMID:15189983	FYPO:0000961	he FWP190 (git2􏰇) cells can grow in the presence of 2 M sorbitol, which is lethal to JSP12 (git2􏰇 spc1-12) and JSP29 (git2􏰇 wis1-29) cells. Therefore, the loss of adenylate cyclase appears to confer a salt-sensitive, but not an osmotically sensitive, growth defect.
PMID:15189983	FYPO:0000961	he FWP190 (git2􏰇) cells can grow in the presence of 2 M sorbitol, which is lethal to JSP12 (git2􏰇 spc1-12) and JSP29 (git2􏰇 wis1-29) cells. Therefore, the loss of adenylate cyclase appears to confer a salt-sensitive, but not an osmotically sensitive, growth defect.
PMID:15189983	PBO:0092140	(Fig. 7) (lanes 1 and 2), we observed that both cgs1Δ and pka1Δ are transcriptionally induced by glucose starvation.
PMID:15189983	PBO:0099904	(Table 3)
PMID:15189983	PBO:0099904	(Table 3)
PMID:15189983	FYPO:0001214	git2􏰇 strains themselves were severely defective for growth on YEA medium containing 1 M KCl (Fig. 1).
PMID:15189983	FYPO:0001490	(Figure 2)
PMID:15189983	FYPO:0002199	unlike JSP12 (git2􏰇 spc1-12) and JSP29 (git2􏰇 wis1-29), cells that elongate and die, cells of the parental strain FWP190 (git2􏰇) appear to simply arrest growth (Fig. 2)
PMID:15189983	PBO:0095677	(Fig. 6)
PMID:15189983	PBO:0099903	(Fig. 6)
PMID:15189983	PBO:0093605	(Fig. 6)
PMID:15189983	PBO:0093605	(Fig. 6)
PMID:15189983	FYPO:0000245	(Fig. 6)
PMID:15189983	PBO:0099902	he FWP190 (git2􏰇) cells can grow in the presence of 2 M sorbitol, which is lethal to JSP12 (git2􏰇 spc1-12) and JSP29 (git2􏰇 wis1-29) cells. Therefore, the loss of adenylate cyclase appears to confer a salt-sensitive, but not an osmotically sensitive, growth defect.
PMID:15189983	PBO:0099908	(Fig. 7)
PMID:15189983	PBO:0099907	(Fig. 7)
PMID:15189983	PBO:0099906	(Fig. 7)
PMID:15189983	PBO:0093824	For cgs1-1 mutant cells, pregrowth on YEA medium results in a nearly 100- fold loss of mating efficiency, as expected. More surprisingly, we found that pregrowth of the cgs1-1 strain on PM medium reduces the mating efficiency defect to only fourfold (Table 2).
PMID:15189983	PBO:0093825	For cgs1-1 mutant cells, pregrowth on YEA medium results in a nearly 100- fold loss of mating efficiency, as expected. More surprisingly, we found that pregrowth of the cgs1-1 strain on PM medium reduces the mating efficiency defect to only fourfold (Table 2).
PMID:15189983	PBO:0099902	he FWP190 (git2􏰇) cells can grow in the presence of 2 M sorbitol, which is lethal to JSP12 (git2􏰇 spc1-12) and JSP29 (git2􏰇 wis1-29) cells. Therefore, the loss of adenylate cyclase appears to confer a salt-sensitive, but not an osmotically sensitive, growth defect.
PMID:15189983	PBO:0099905	(Fig. 7)
PMID:15189983	PBO:0092140	(Fig. 7) (lanes 1 and 2), we observed that both cgs1Δ and pka1Δ are transcriptionally induced by glucose starvation.
PMID:15189983	PBO:0093784	(Figure 1)
PMID:15189983	FYPO:0006141	(Figure 1)
PMID:15189983	FYPO:0006141	(Figure 1)
PMID:15189983	FYPO:0006141	(Figure 1)
PMID:15194812	PBO:0097127	(comment: Cdc45 reappears quickly after shift from restrictive to permissive temperature)
PMID:15218150	PBO:0097399	(Fig. 2A)
PMID:15218150	FYPO:0002336	(Fig. 1B)
PMID:15218150	FYPO:0002336	(Fig. 1B)
PMID:15218150	FYPO:0002336	(Fig. 1B)
PMID:15218150	FYPO:0002336	(Fig. 1B)
PMID:15218150	PBO:0095653	(Fig. 1B)
PMID:15218150	PBO:0095653	(Fig. 1B)
PMID:15218150	PBO:0095651	(Fig. 1B)
PMID:15218150	PBO:0095651	(Fig. 1B)
PMID:15218150	PBO:0095653	(Fig. 1B)
PMID:15218150	PBO:0095653	(Fig. 1B)
PMID:15218150	FYPO:0002336	(Fig. 1C)
PMID:15218150	PBO:0095651	(Fig. 1C)
PMID:15218150	PBO:0095651	(Fig. 1C)
PMID:15218150	PBO:0095651	(Fig. 1C)
PMID:15218150	FYPO:0007336	(Fig. 1C)
PMID:15218150	FYPO:0007336	(Fig. 1C)
PMID:15218150	FYPO:0007336	(Fig. 1C)
PMID:15218150	FYPO:0007336	(Fig. 1C)
PMID:15218150	FYPO:0007336	(Fig. 1C)
PMID:15218150	FYPO:0007336	(Fig. 1C)
PMID:15218150	PBO:0110928	(Fig. 1B)
PMID:15218150	PBO:0110928	(Fig. 1B)
PMID:15218150	PBO:0110928	(Fig. 1B)
PMID:15218150	PBO:0112698	(Fig. 1B)
PMID:15218150	PBO:0112540	(Fig. 1B)
PMID:15218150	PBO:0112540	(Fig. 1B)
PMID:15218150	PBO:0112540	(Fig. 1B)
PMID:15218150	PBO:0112540	(Fig. 1B)
PMID:15218150	PBO:0112540	(Fig. 1B)
PMID:15218150	PBO:0112540	(Fig. 1B)
PMID:15218150	FYPO:0005865	(Fig. 1B)
PMID:15218150	FYPO:0005865	(Fig. 1B)
PMID:15218150	FYPO:0005865	(Fig. 1B)
PMID:15218150	FYPO:0005865	(Fig. 1B)
PMID:15218150	PBO:0097399	(Fig. 1B)
PMID:15218150	PBO:0097399	(Fig. 1B)
PMID:15218150	PBO:0097399	(Fig. 1B)
PMID:15218150	PBO:0097399	(Fig. 1B)
PMID:15218150	PBO:0097399	(Fig. 1B)
PMID:15218150	PBO:0097399	(Fig. 1B)
PMID:15218150	PBO:0110928	(Fig. 1C)
PMID:15218150	PBO:0112540	(Fig. 1C)
PMID:15218150	PBO:0112540	(Fig. 1C)
PMID:15218150	PBO:0112540	(Fig. 1C)
PMID:15218150	PBO:0112683	(Fig. 1C)
PMID:15218150	PBO:0112683	(Fig. 1C)
PMID:15218150	PBO:0112683	(Fig. 1C)
PMID:15218150	PBO:0112683	(Fig. 1C)
PMID:15218150	PBO:0112683	(Fig. 1C)
PMID:15218150	PBO:0112683	(Fig. 1C)
PMID:15218150	FYPO:0005865	(Fig. 1C)
PMID:15218150	PBO:0097399	(Fig. 1C)
PMID:15218150	PBO:0097399	(Fig. 1C)
PMID:15218150	PBO:0097399	(Fig. 1C)
PMID:15218150	FYPO:0008212	(Fig. 1C)
PMID:15218150	FYPO:0008212	(Fig. 1C)
PMID:15218150	FYPO:0008212	(Fig. 1C)
PMID:15218150	FYPO:0008212	(Fig. 1C)
PMID:15218150	FYPO:0008212	(Fig. 1C)
PMID:15218150	FYPO:0008212	(Fig. 1C)
PMID:15218150	FYPO:0002336	(Fig. 2A)
PMID:15218150	PBO:0095651	(Fig. 2A)
PMID:15218150	PBO:0095651	(Fig. 2A)
PMID:15218150	PBO:0095651	(Fig. 2A)
PMID:15218150	PBO:0095651	(Fig. 2A)
PMID:15218150	PBO:0095651	(Fig. 2A)
PMID:15218150	PBO:0095651	(Fig. 2A)
PMID:15218150	FYPO:0002336	(Fig. 2B)
PMID:15218150	FYPO:0007336	(Fig. 2B)
PMID:15218150	FYPO:0007336	(Fig. 2B)
PMID:15218150	FYPO:0007336	(Fig. 2B)
PMID:15218150	FYPO:0007336	(Fig. 2B)
PMID:15218150	FYPO:0007336	(Fig. 2B)
PMID:15218150	FYPO:0007336	(Fig. 2B)
PMID:15218150	PBO:0112698	(Fig. 2A)
PMID:15218150	PBO:0112540	(Fig. 2A)
PMID:15218150	PBO:0112540	(Fig. 2A)
PMID:15218150	PBO:0112683	(Fig. 2A)
PMID:15218150	PBO:0112683	(Fig. 2A)
PMID:15218150	PBO:0112683	(Fig. 2A)
PMID:15218150	PBO:0112683	(Fig. 2A)
PMID:15218150	FYPO:0005865	(Fig. 2A)
PMID:15218150	PBO:0097399	(Fig. 2A)
PMID:15218150	PBO:0097399	(Fig. 2A)
PMID:15218150	PBO:0097399	(Fig. 2A)
PMID:15218150	PBO:0097399	(Fig. 2A)
PMID:15218150	PBO:0097399	(Fig. 2A)
PMID:15218150	PBO:0112540	(Fig. 2B)
PMID:15218150	PBO:0112683	(Fig. 2B)
PMID:15218150	PBO:0112683	(Fig. 2B)
PMID:15218150	PBO:0112683	(Fig. 2B)
PMID:15218150	FYPO:0005865	(Fig. 2B)
PMID:15218150	FYPO:0008212	(Fig. 2B)
PMID:15218150	FYPO:0008212	(Fig. 2B)
PMID:15218150	FYPO:0008212	(Fig. 2B)
PMID:15218150	FYPO:0008212	(Fig. 2B)
PMID:15218150	FYPO:0008212	(Fig. 2B)
PMID:15218150	FYPO:0008212	(Fig. 2B)
PMID:15218150	PBO:0112699	(Fig. 4B)
PMID:15218150	PBO:0112700	(Fig. 4B)
PMID:15218150	GO:0141194	(Fig. 3)
PMID:15218150	GO:0141194	(Fig. 3)
PMID:15219990	GO:0051537	(comment: spectra looks the same as Adx)
PMID:15226405	FYPO:0004602	frequency of different stages of LE development is different though, but morphology is normal
PMID:15226405	FYPO:0004602	frequency of different stages of LE development is different though, but morphology is normal
PMID:15249580	GO:0016314	(Fig. 1c)
PMID:15249580	PBO:0109046	(comment: vw fixed from GO:0052812 to GO:0016308 based on e-mail from Pgaudet) The data are consistent with a model in which its3p, like its mammalian homologue, can convert PI(3)P to PI(3,4)P2 and PI(3,4,5)P3.
PMID:15249580	PBO:0103033	(comment: mishapen)
PMID:15249580	GO:0004439	(Fig. 1c)
PMID:15249580	PBO:0103032	The data are consistent with a model in which its3p, like its mammalian homologue, can convert PI(3)P to PI(3,4)P2 and PI(3,4,5)P3.
PMID:15278909	PBO:0019995	(comment: CHECK during premeiotic DNA replication)
PMID:15292231	PBO:0111992	(Fig. 2B)
PMID:15292231	GO:0090055	The results presented above suggest that the kinase activity of Wis1 and Sty1/Spc1 is required for proper control of hetero chromatin assembly by Atf1 and Pcr1.
PMID:15292231	PBO:0111990	(Fig. 6B)
PMID:15292231	PBO:0111991	(Fig. 6B)
PMID:15292231	PBO:0111976	(Fig. 3)
PMID:15292231	PBO:0111976	(Fig. 3)
PMID:15292231	GO:0030466	(comment: RNAi-independent mechanism)
PMID:15292231	GO:0090055	The results presented above suggest that the kinase activity of Wis1 and Sty1/Spc1 is required for proper control of hetero chromatin assembly by Atf1 and Pcr1.
PMID:15292231	PBO:0111980	(Fig. 2B) Furthermore, ChIP analysis showed that the absence of atf1 and pcr1 resulted in a considerable increase in histone H3/H4 acetylation and euchromatic-specific H3 Lys-4 methylation of the selected region
PMID:15292231	PBO:0111980	(Fig. 2B)
PMID:15292231	PBO:0111989	(Fig. 6B)
PMID:15292231	GO:0030466	(comment: RNAi-independent mechanism)
PMID:15292231	GO:0030466	(comment: RNAi-independent mechanism)
PMID:15292231	PBO:0111988	(Fig. 2C)
PMID:15292231	PBO:0111987	(Fig. 2C)
PMID:15292231	PBO:0111987	(Fig. 2C)
PMID:15292231	PBO:0111986	(Fig. 2B)
PMID:15292231	PBO:0111984	(Fig. 2B)
PMID:15292231	PBO:0111983	(Fig. 2B)
PMID:15292231	PBO:0111982	(Fig. 2B)
PMID:15292231	PBO:0111981	(Fig. 2B)
PMID:15292231	PBO:0111985	(Fig. 2B)
PMID:15292231	PBO:0111984	(Fig. 2B)
PMID:15292231	PBO:0111983	(Fig. 2B)
PMID:15292231	PBO:0111982	(Fig. 2B)
PMID:15292231	PBO:0111981	(Fig. 2B)
PMID:15292231	PBO:0112047	(comment: ATF/CREB-binding)
PMID:15292231	PBO:0111976	(Fig. 3) Moreover, the ade6-off to ade6-on conversion in Δsty1 and Δwis1 mutants was significantly reduced relative to wild-type cells, indicating that sty1 and wis1 deletions enhanced stabilization of the epigenetic inheritance of the silent states (Fig. 3B).
PMID:15292231	PBO:0111978	(Fig. 1)
PMID:15292231	PBO:0111977	(Fig. 1B)
PMID:15292231	PBO:0111976	(Fig. 1) Similar to atf1 mutants, Δpcr1 showed reduced silencing, but the effect was weaker than that of Δatf1 or Δatf1Δpcr1 (Fig. 1B).
PMID:15292231	PBO:0101106	(Fig. 1A) In contrast, the atf1 deletion resulted in increased transcriptional repression at both centromeres and telomeres (Fig. 1A).
PMID:15292231	PBO:0111981	(Fig. 6B)
PMID:15292231	PBO:0112047	(comment: ATF/CREB-binding)
PMID:15292231	PBO:0111975	(Fig. 1A) In contrast, the atf1 deletion resulted in increased transcriptional repression at both centromeres and telomeres (Fig. 1A).
PMID:15292231	PBO:0112046	(Fig. 1) An atf1 deletion strain carrying the ade6+ reporter gene inserted at the mat3-M locus displayed a loss of silencing of the reporter gene (Fig. 1A).
PMID:15292231	PBO:0111979	(Fig. 3)
PMID:15297457	GO:0031573	(comment: CHECK would it be better/safer to annotate to parent generic intra-S checkpoint term?)
PMID:15314153	PBO:0093561	(comment: CONDITION 25 degrees)
PMID:15314153	FYPO:0002061	(comment: CONDITION 30 degrees)
PMID:15316017	GO:0052658	(comment: CHECK activated_by(CHEBI:18420)| inhibited_by(CHEBI:29108))
PMID:15329725	FYPO:0005428	(Fig. 1f)
PMID:15329725	FYPO:0005429	(Fig. 1h)
PMID:15329725	FYPO:0002102	(Fig. 1d and Fig. 1h)
PMID:1533272	PBO:0104194	(Fig. 7) (comment: HECK Cdc2-DL2 over expressed from an integrated pREP1/pMNS21 plasmid). (comment: Binds to cdc13 but this is reduced compared to binding of cdc2+ to cdc13)
PMID:1533272	FYPO:0001491	(comment: CHECK cdc13 expressed from own promoter on multi copy plasmid pUR18)
PMID:1533272	PBO:0104193	(Fig. 5) (comment: Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid. Phosphorylation on threonine, but position(s) not determined.)
PMID:1533272	PBO:0102314	(Fig. 4) (comment: CHECK Histone H1 used as substrate. Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid.)
PMID:1533272	PBO:0104192	(Fig. 2) (comment: CHECK Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid.)
PMID:1533272	PBO:0097954	(Fig. 3) (comment: CHECK Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid.)
PMID:15340008	PBO:0111726	(Fig. 7)
PMID:15340008	FYPO:0008162	(Fig. 1,3,4)
PMID:15340008	FYPO:0003306	(Fig. 1C)
PMID:15340008	PBO:0102116	(Fig. 3A)
PMID:15340008	PBO:0111724	(Fig. 3A)
PMID:15340008	FYPO:0001513	(Fig. 3)
PMID:15340008	PBO:0102116	(Fig. 3A)
PMID:15340008	PBO:0111722	(Fig. 1)
PMID:15340008	PBO:0111723	(Fig. 1D, Fig. 2)
PMID:15340008	FYPO:0001761	(Fig. 2)
PMID:15340008	FYPO:0001513	(Fig. 2)
PMID:15340008	PBO:0111724	(Fig. 3A)
PMID:15340008	FYPO:0001513	(Fig. 3)
PMID:15340008	PBO:0111725	(Fig. 4C)
PMID:15340008	FYPO:0003612	(Fig. 5C)
PMID:15340008	FYPO:0003612	(Fig. 5D)
PMID:15340008	FYPO:0002150	(Fig. 5A)
PMID:15340008	FYPO:0002150	(Fig. 5A)
PMID:15340008	PBO:0020742	(Fig. 3)
PMID:15340008	PBO:0020742	(Fig. 3)
PMID:15340008	FYPO:0002150	(Fig. 5B)
PMID:15340008	FYPO:0002150	(Fig. 5B)
PMID:15359282	PBO:0111732	(Fig. 3)
PMID:15359282	PBO:0111731	(Fig. 3A)
PMID:15359282	PBO:0111730	(Fig. 3A)
PMID:15359282	GO:0005634	(Figure 2)
PMID:15359282	PBO:0093562	(Fig. 4A)
PMID:15359282	PBO:0103456	(Fig. 4B)
PMID:15359282	PBO:0111735	(Figure 3) (comment: CHECK E1, activating)
PMID:15359282	PBO:0111734	(Figure 3) (comment: CHECK E2)
PMID:15359282	PBO:0111733	(Figure 3) (comment: CHECK E3)
PMID:15359282	FYPO:0002687	(Fig. 6B)
PMID:15359282	FYPO:0002687	(Fig. 6B)
PMID:15359282	FYPO:0002687	(Fig. 6B)
PMID:15359282	PBO:0096188	(Fig. 4C)
PMID:15359282	PBO:0093632	(Fig. 6B)
PMID:15359282	PBO:0093634	(Fig. 6B)
PMID:15359282	FYPO:0002150	(Fig. 6A)
PMID:15359282	PBO:0093564	(Fig. 4A)
PMID:15359282	FYPO:0002150	(Fig. 6A)
PMID:15359282	FYPO:0002150	(Fig. 6A)
PMID:15359282	FYPO:0002150	(Fig. 6A)
PMID:15359282	PBO:0097301	(Fig. 6A)
PMID:15359282	PBO:0097301	(Fig. 6A)
PMID:15359282	PBO:0097301	(Fig. 6A)
PMID:15359282	PBO:0103455	(Fig. 4B)
PMID:15359282	PBO:0096191	(Fig. 4C)
PMID:15359282	PBO:0096191	(Fig. 4C)
PMID:15359282	PBO:0096189	(Fig. 4C)
PMID:15359282	PBO:0096188	(Fig. 4C)
PMID:15359282	PBO:0097301	(Fig. 6A)
PMID:15367656	PBO:0033073	(comment: no hydroxyurea)
PMID:15369671	PBO:0101419	(Fig. 4)
PMID:15369671	PBO:0101421	(Fig. 4)
PMID:15369671	PBO:0096686	(Fig. 4)
PMID:15371542	FYPO:0001840	(Fig. 1)
PMID:15371542	FYPO:0001839	(Fig. 1a)
PMID:15371542	FYPO:0000091	(Fig. 1)
PMID:15371542	FYPO:0000964	(Fig. 1a)
PMID:15372076	GO:0030466	The present data also demonstrate that Chp1 function is required not only for the centromeres but also for the mating-type region and telomeres.
PMID:15372076	PBO:0111019	(Figure 1)
PMID:15372076	PBO:0111018	(Figure 1)
PMID:15372076	PBO:0111017	(Figure 1)
PMID:15372076	PBO:0111016	(Figure 1)
PMID:15372076	PBO:0111015	(Figure 1)
PMID:15372076	FYPO:0003097	Interestingly, we found that swi6þ deletion caused a loss of the H3-K9 methylation at CEN (dg223) in the Dchp1 background (Figure 5D, Dchp1Dswi6), suggesting that Swi6 is required for the maintenance of centromeric H3- K9 methylation in the Dchp1 strain.
PMID:15372076	PBO:0111014	(Figure 1)
PMID:15372076	PBO:0111013	(Figure 1)
PMID:15372076	GO:0030466	H3-K9 methylation at the three heterochromatic regions (CEN-dg223,MAT-K-R, or TEL-E12) was reduced to a level comparable to that in Dclr4 (Figure 6A), suggesting that Rik1 has a critical role in H3-K9 methylation at the native heterochromatic regions.
PMID:15372076	PBO:0111020	We found that H3-K9 methylation at the three heterochromatic regions (CEN- dg223, MAT-K-R, or TEL-E12) was reduced to a level comparable to that in Dclr4 (Figure 6A)
PMID:15372076	PBO:0111008	We found that the association of Chp1-13myc with the three heterochromatic regions (CEN, MAT, and TEL) was not affected in the absence of swi6 þ or chp2 þ (Figure 2A).
PMID:15372076	PBO:0110927	We found that the association of Chp1-13myc with the three heterochromatic regions (CEN, MAT, and TEL) was not affected in the absence of swi6 þ or chp2 þ (Figure 2A).
PMID:15372076	PBO:0110927	We found that the association of Chp1-13myc with the three heterochromatic regions (CEN, MAT, and TEL) was not affected in the absence of swi6 þ or chp2 þ (Figure 2A).
PMID:15372076	FYPO:0003235	n Dswi6 or Dchp2 cells, the three heterochromatic regions were enriched in K9-methylated H3 at the same level as in wild-type cells (Figure 5B).
PMID:15372076	FYPO:0003235	Intriguingly, we found that, even in the Dchp1 cells, histone H3 in native centromeric heterochromatin (CEN-dg223 locus) remained methylated at lysine 9 (Figure 4B, Dchp1).
PMID:15372076	GO:0031509	The present data also demonstrate that Chp1 function is required not only for the centromeres but also for the mating-type region and telomeres.
PMID:15372076	PBO:0110929	We found that the association of Chp1-13myc with the three heterochromatic regions (CEN, MAT, and TEL) was not affected in the absence of swi6 þ or chp2 þ (Figure 2A).
PMID:15372076	PBO:0111009	In contrast, the centromeric localization of Swi6 or Chp2-13myc was specifically decreased in the Dchp1 cells (Figures 2B and C, Dchp1)
PMID:15372076	PBO:0111012	Interestingly, Swi6 was required for the localization of Chp2 to the mating-type region or telomeres but not to the centromeres (Figure 2B, Dswi6).
PMID:15372076	FYPO:0003235	Intriguingly, we found that, even in the Dchp1 cells, histone H3 in native centromeric heterochromatin (CEN-dg223 locus) remained methylated at lysine 9 (Figure 4B, Dchp1).
PMID:15372076	PBO:0108387	We found that H3-K9 methylation at the three heterochromatic regions (CEN- dg223, MAT-K-R, or TEL-E12) was reduced to a level comparable to that in Dclr4 (Figure 6A)
PMID:15372076	FYPO:0003096	Interestingly, we found that, although deletion of either swi6 þ or chp2 þ did not affect the H3-K9 methylation at MAT (K-R) and TEL (E12) in the Dchp1 background, the methylation level in these regions was severely decreased in the triple-mutant strain (Figure 5D, Dchp1Dchp2Dswi6). Again, these results demonstrate that Swi6 and Chp2 are required for the maintenance of H3-K9 methylation at the three heterochromatic regions, and also indicate that Swi6 and Chp2 have overlapping functions in the maintenance of H3-K9 methylation.
PMID:15372076	PBO:0107146	(Figure 1)
PMID:15372076	PBO:0111008	We found that the association of Chp1-13myc with the three heterochromatic regions (CEN, MAT, and TEL) was not affected in the absence of swi6 þ or chp2 þ (Figure 2A).
PMID:15372076	PBO:0111011	Interestingly, Swi6 was required for the localization of Chp2 to the mating-type region or telomeres but not to the centromeres (Figure 2B, Dswi6).
PMID:15372076	PBO:0107146	In contrast, the centromeric localization of Swi6 or Chp2-13myc was specifically decreased in the Dchp1 cells (Figures 2B and C, Dchp1)
PMID:15372076	PBO:0111010	Interestingly, Swi6 was required for the localization of Chp2 to the mating-type region or telomeres but not to the centromeres (Figure 2B, Dswi6).
PMID:15372076	GO:0031508	Therefore, Chp1 protein was also involved in the production or processing of centromeric RNA transcripts, which might be linked to heterochromatin establishment.
PMID:15372076	GO:0005721	(Figure 1)
PMID:15372076	GO:0140720	(Figure 1)
PMID:15372076	GO:0031934	(Figure 1)
PMID:15372076	GO:0005721	(Figure 1)
PMID:15372076	GO:0005721	(Figure 1)
PMID:15372076	GO:0140720	(Figure 1)
PMID:15372076	GO:0140720	(Figure 1)
PMID:15372076	GO:0031934	(Figure 1)
PMID:15372076	GO:0031934	(Figure 1)
PMID:15372076	PBO:0097399	We found that H3-K9 methylation at the three heterochromatic regions (CEN- dg223, MAT-K-R, or TEL-E12) was reduced to a level comparable to that in Dclr4 (Figure 6A)
PMID:15372076	GO:0031508	H3-K9 methylation at the three heterochromatic regions (CEN-dg223,MAT-K-R, or TEL-E12) was reduced to a level comparable to that in Dclr4 (Figure 6A), suggesting that Rik1 has a critical role in H3-K9 methylation at the native heterochromatic regions.
PMID:15372076	GO:0031509	H3-K9 methylation at the three heterochromatic regions (CEN-dg223,MAT-K-R, or TEL-E12) was reduced to a level comparable to that in Dclr4 (Figure 6A), suggesting that Rik1 has a critical role in H3-K9 methylation at the native heterochromatic regions.
PMID:15372076	PBO:0111009	(Figure 1)
PMID:15372076	PBO:0097399	We found that H3-K9 methylation at the three heterochromatic regions (CEN- dg223, MAT-K-R, or TEL-E12) was reduced to a level comparable to that in Dclr4 (Figure 6A)
PMID:15372076	FYPO:0003096	nexpectedly, the centromeric H3-K9 methylation was also severely decreased in the Dchp1Dchp2 strain (Figure 5D, Dchp1Dchp2).
PMID:15372076	PBO:0110929	We found that the association of Chp1-13myc with the three heterochromatic regions (CEN, MAT, and TEL) was not affected in the absence of swi6 þ or chp2 þ (Figure 2A).
PMID:15372076	PBO:0111020	We found that H3-K9 methylation at the three heterochromatic regions (CEN- dg223, MAT-K-R, or TEL-E12) was reduced to a level comparable to that in Dclr4 (Figure 6A)
PMID:15372076	PBO:0108387	We found that H3-K9 methylation at the three heterochromatic regions (CEN- dg223, MAT-K-R, or TEL-E12) was reduced to a level comparable to that in Dclr4 (Figure 6A)
PMID:15385632	FYPO:0006062	(Fig. 6)
PMID:15385632	FYPO:0006062	(Figure 6A, D, and E)
PMID:15385632	PBO:0098865	(Figure 6A, D, and E)
PMID:15385632	GO:0000921	Combining this observation with our biochemical data, we conclude that a subcomplex of Spn1p-Spn4p is sufficient for formation of ectopic structures and localizing to the medial cortex, but at least one other septin is required for assembly of a ring structure.
PMID:15385632	PBO:0098862	(Figure 6A, D, and E)
PMID:15385632	FYPO:0006062	(Figure 6A, D, and E)
PMID:15385632	GO:0005515	(Figure 2A, Figure 2, D and E)
PMID:15385632	PBO:0098858	(Figure 5C)
PMID:15385632	PBO:0098859	(Figure 5)
PMID:15385632	PBO:0098864	(Figure 6A, D, and E)
PMID:15385632	PBO:0098861	(Figure 5)
PMID:15385632	PBO:0098859	(Figure 5)
PMID:15385632	PBO:0098864	(Figure 6A, D, and E)
PMID:15385632	PBO:0098863	(Figure 6A, D, and E)
PMID:15385632	GO:0000921	Combining this observation with our biochemical data, we conclude that a subcomplex of Spn1p-Spn4p is sufficient for formation of ectopic structures and localizing to the medial cortex, but at least one other septin is required for assembly of a ring structure.
PMID:15385632	GO:0031106	In this case, Spn3p-GFP was recruited to the medial region before mitosis as before (Figure 8A) and it was now assembled into highly organized ring structures that were easily visualized as split rings once septa had formed (Figure 8, B and C). Virtually no diffuse disk structures were observed (Figure 8, B-D). We conclude from this experiment that Mid2p is solely responsible directly or indirectly for regulating septin ring coalesence in S. pombe.
PMID:15385632	PBO:0098860	(Figure 5)
PMID:15385632	PBO:0098860	(Figure 5)
PMID:15385632	FYPO:0006063	erexpression was the relative persistence of septin rings and the inhibition of mitotic progression, as determined by monitoring the formation of binucleates (Figure 8A). This result is consistent with our previous results, indicating that prolonged expression of Mid2p stabilizes septin ring structures and influences cell cycle progression (Tasto et al., 2003). erexpression was the relative persistence of septin rings and the inhibition of mitotic progression, as determined by monitoring the formation of binucleates (Figure 8A). This result is consistent with our previous results, indicating that prolonged expression of Mid2p stabilizes septin ring structures and influences cell cycle progression (Tasto et al., 2003).
PMID:15385632	PBO:0098855	(Figure 1H, Table 1)
PMID:15385632	GO:0005515	(Figure 2A)
PMID:15385632	GO:0005515	(Figure 2A Figure 2B and C)
PMID:15385632	GO:0005515	(Figure 2A)
PMID:15385632	PBO:0098862	(Figure 6A, D, and E)
PMID:15385632	GO:0005515	(Figure 2A, Figure 2, D and E)
PMID:15385632	GO:0005515	(Figure 2A)
PMID:15385632	FYPO:0001972	(Fig. 5)
PMID:15385632	PBO:0098152	(Fig. 5)
PMID:15385632	GO:0005515	(Figure 2, D and E)
PMID:15385632	PBO:0098857	(Figure 1J) Based on the lower recovery of coimmunoprecipitated proteins, this Spn1p-Spn4p complex appears to be less stable than in the presence of Spn2p or Spn3p.
PMID:15385632	PBO:0098856	(Figure 1I)
PMID:1538784	GO:0044732	(comment: CHECK throughout_cell_cycle)
PMID:15470240	FYPO:0002903	(Fig. 2)
PMID:15470240	FYPO:0004256	(Fig. 2)
PMID:15470240	FYPO:0002903	(Fig. 2)
PMID:15471884	GO:0070337	lower affinity than for Y-form DNA
PMID:15475954	GO:0031934	(Fig. 1)
PMID:15475954	FYPO:0005865	(Fig. 7B)
PMID:15475954	PBO:0120532	(Fig. 7B)
PMID:15475954	PBO:0112900	(Fig. 7B)
PMID:15475954	FYPO:0008236	(Fig. 7A)
PMID:15475954	GO:0030466	These results indicate that RITS and Atf1-Pcr1 participate in distinct and parallel pathways to nucleate heterochromatin at the mat locus.
PMID:15475954	FYPO:0008236	(Fig. 7A)
PMID:15475954	FYPO:0008011	(Fig. 7A)
PMID:15475954	PBO:0112898	(Fig. 6B)
PMID:15475954	FYPO:0008212	(Fig. 6A)
PMID:15475954	PBO:0112900	(Fig. 6B)
PMID:15475954	PBO:0097399	(Fig. 6A)
PMID:15475954	PBO:0112894	(Fig. 6B)
PMID:15475954	PBO:0108389	(Fig. 6A)
PMID:15475954	PBO:0095653	(Fig. 5D)
PMID:15475954	PBO:0095653	(Fig. 5D)
PMID:15475954	PBO:0095652	(Fig. 5B)
PMID:15475954	PBO:0095652	(Fig. 5B)
PMID:15475954	PBO:0112899	(Fig. 4)
PMID:15475954	PBO:0112898	(Fig. 4)
PMID:15475954	PBO:0112897	(Fig. 4)
PMID:15475954	PBO:0112896	(Fig. 4)
PMID:15475954	PBO:0112895	(Fig. 3)
PMID:15475954	PBO:0112894	(Fig. 3)
PMID:15475954	PBO:0097399	(Fig. 2C)
PMID:15475954	PBO:0097399	(Fig. 2C)
PMID:15475954	FYPO:0007336	(Fig. 2C)
PMID:15475954	FYPO:0007336	(Fig. 2C)
PMID:15475954	PBO:0112683	(Fig. 2C)
PMID:15475954	PBO:0112683	(Fig. 2C)
PMID:15475954	PBO:0097399	(Fig. 2C)
PMID:15475954	PBO:0097399	(Fig. 2C)
PMID:15475954	FYPO:0007336	(Fig. 2C)
PMID:15475954	GO:0005721	(Fig. 1)
PMID:15475954	FYPO:0007336	(Fig. 2C)
PMID:15475954	PBO:0112683	(Fig. 2C)
PMID:15475954	GO:0140720	(Fig. 1)
PMID:15475954	GO:0031934	(Fig. 1)
PMID:15475954	PBO:0110928	(Fig. 2B)
PMID:15475954	FYPO:0005865	(Fig. 2B)
PMID:15475954	FYPO:0002336	(Fig. 2B)
PMID:15475954	PBO:0112683	(Fig. 2C)
PMID:15475954	PBO:0112683	(Fig. 2C)
PMID:15475954	PBO:0112683	(Fig. 2C)
PMID:15475954	PBO:0097399	(Fig. 2C)
PMID:15475954	PBO:0097399	(Fig. 2C)
PMID:15475954	FYPO:0007336	(Fig. 2C)
PMID:15475954	FYPO:0007336	(Fig. 2C)
PMID:15475954	GO:0005721	(Fig. 1)
PMID:15475954	GO:0005721	(Fig. 1)
PMID:15475954	GO:0140720	(Fig. 1)
PMID:15475954	GO:0140720	(Fig. 1)
PMID:15475954	FYPO:0005865	(Fig. 2C)
PMID:15475954	PBO:0110928	(Fig. 2C)
PMID:15475954	FYPO:0002336	(Fig. 2C)
PMID:15475954	PBO:0108389	(Fig. 2C)
PMID:15475954	PBO:0112540	(Fig. 2C)
PMID:15475954	PBO:0095653	(Fig. 2C)
PMID:15475954	PBO:0112540	(Fig. 2C)
PMID:15475954	PBO:0108389	(Fig. 2C)
PMID:15475954	PBO:0095653	(Fig. 2C)
PMID:15475954	PBO:0112540	(Fig. 2C)
PMID:15475954	PBO:0108389	(Fig. 2C)
PMID:15475954	PBO:0095653	(Fig. 2C)
PMID:15475954	PBO:0112683	(Fig. 2B)
PMID:15475954	PBO:0112683	(Fig. 2B)
PMID:15475954	PBO:0095651	(Fig. 2B)
PMID:15475954	PBO:0095651	(Fig. 2B)
PMID:15475954	PBO:0097399	(Fig. 2B)
PMID:15475954	PBO:0097399	(Fig. 2B)
PMID:15475954	PBO:0108389	(Fig. 2B)
PMID:15475954	PBO:0108389	(Fig. 2B)
PMID:15475954	PBO:0112540	(Fig. 2B)
PMID:15475954	PBO:0112540	(Fig. 2B)
PMID:15475954	PBO:0095653	(Fig. 2B)
PMID:15475954	PBO:0095653	(Fig. 2B)
PMID:15475954	PBO:0112698	(Fig. 2B)
PMID:15475954	PBO:0112698	(Fig. 2B)
PMID:15475954	PBO:0111989	(Fig. 2B)
PMID:15475954	PBO:0111989	(Fig. 2B)
PMID:15475954	PBO:0095652	(Fig. 2B)
PMID:15475954	PBO:0095652	(Fig. 2B)
PMID:15475954	FYPO:0005865	(Fig. 2B)
PMID:15475954	PBO:0110928	(Fig. 2B)
PMID:15475954	FYPO:0002336	(Fig. 2B)
PMID:15475954	FYPO:0005865	(Fig. 2B)
PMID:15475954	FYPO:0002336	(Fig. 2B)
PMID:15475954	PBO:0110928	(Fig. 2B)
PMID:15475954	FYPO:0005865	(Fig. 2B)
PMID:15475954	PBO:0110928	(Fig. 2B)
PMID:15475954	FYPO:0002336	(Fig. 2B)
PMID:15475954	GO:0030466	These results indicate that RITS and Atf1-Pcr1 participate in distinct and parallel pathways to nucleate heterochromatin at the mat locus.
PMID:15475954	FYPO:0008011	(Fig. 7C)
PMID:15475954	FYPO:0008011	(Fig. 7C)
PMID:15475954	PBO:0108387	(Fig. 7B)
PMID:15475954	GO:0031934	(Fig. 1)
PMID:15475954	GO:0030466	These results indicate that RITS and Atf1-Pcr1 participate in distinct and parallel pathways to nucleate heterochromatin at the mat locus.
PMID:15485922	FYPO:0005402	(comment: same as taz1delta alone)
PMID:15485922	FYPO:0005402	(comment: same as taz1delta alone)
PMID:15504913	FYPO:0000418	(Fig. 4C)
PMID:15504913	PBO:0112670	(Table 1)
PMID:15504913	FYPO:0008207	(Table 1)
PMID:15504913	FYPO:0008207	(Table 1)
PMID:15504913	FYPO:0008207	(Table 1)
PMID:15504913	FYPO:0008207	(Table 1)
PMID:15504913	PBO:0112669	(Table 1)
PMID:15504913	PBO:0112669	(Table 1)
PMID:15504913	PBO:0112669	(Table 1)
PMID:15504913	PBO:0112669	(Table 1)
PMID:15504913	PBO:0112668	(Table 1)
PMID:15504913	FYPO:0001367	(Fig. 6C)
PMID:15504913	FYPO:0001357	(Fig. 6B)
PMID:15504913	FYPO:0001357	(Fig. 6B)
PMID:15504913	PBO:0112667	(Fig. 6B)
PMID:15504913	GO:0110085	Rng3p-GFP3 and Rng3p-YFP3 concentrated in contractile rings from anaphase B through constriction (Fig. 5).
PMID:15504913	PBO:0107510	Rng3p-GFP3 and Rng3p-YFP3 concentrated in contractile rings from anaphase B through constriction (Fig. 5).
PMID:15504913	PBO:0099316	Rng3p-GFP3 and Rng3p-YFP3 concentrated in contractile rings from anaphase B through constriction (Fig. 5).
PMID:15504913	FYPO:0001252	(Fig. 4C)
PMID:15504913	FYPO:0001252	(Fig. 4B)
PMID:15504913	FYPO:0001252	(Fig. 4A)
PMID:15504913	FYPO:0000161	(Fig. 4C)
PMID:15504913	FYPO:0000418	(Fig. 4B)
PMID:15504913	FYPO:0000161	(Fig. 4B)
PMID:15504913	FYPO:0000418	(Fig. 4A)
PMID:15504913	FYPO:0000161	(Fig. 4A)
PMID:15504913	GO:0033275	(Fig. 3)
PMID:15504913	PBO:0112666	(Fig. 3B, 3C)
PMID:15504913	GO:0016460	(Fig. 1)
PMID:15504913	GO:0016460	(Fig. 1)
PMID:15504913	PBO:0112669	(Table 1)
PMID:15504913	FYPO:0008207	(Table 1)
PMID:15504913	FYPO:0008207	(Table 1)
PMID:15504913	PBO:0112668	(Table 1)
PMID:15504913	PBO:0112670	(Table 1)
PMID:15507118	FYPO:0003763	inviable mononucleate aseptate vegetative cell with cell cycle arrest in mitotic G2 phase
PMID:15509783	FYPO:0000229	(Fig. 7D)
PMID:15509783	PBO:0097814	Table2
PMID:15509783	PBO:0112055	(comment: checkpoint)
PMID:15509783	PBO:0097815	Table2
PMID:15509783	PBO:0097813	Table2
PMID:15509783	PBO:0097812	Table2
PMID:15509783	PBO:0097811	Table2
PMID:15509783	FYPO:0004318	(Figure 1B)
PMID:15509783	FYPO:0000229	(Figure 1B)
PMID:15509783	PBO:0023853	(Figure 2A)
PMID:15509783	PBO:0097818	(Fig. 7B)
PMID:15509783	FYPO:0004318	(Fig. 7D)
PMID:15509783	PBO:0097819	(Fig. 7B)
PMID:15509865	PBO:0033208	(Table 3)
PMID:15509865	PBO:0102573	(Table 3) assayed using pairing of his2 loci
PMID:15509865	FYPO:0000927	(Fig. 2A)
PMID:15509865	FYPO:0000927	(Fig. 2A)
PMID:15509865	FYPO:0005383	(Fig. 2B,C)
PMID:15509865	FYPO:0006128	(comment: CHECK DURATION) Fig. 2B,C
PMID:15509865	FYPO:0003179	(Table 2).leu1 and his2 loc, reduced 12 fold
PMID:15509865	FYPO:0004093	data not shown
PMID:15509865	FYPO:0004764	(Fig. 6B,C). in meiotic cells, shmooing cells
PMID:15509865	FYPO:0005814	(Fig. 6B,C). (comment: in meiotic cells, shmooing cells)
PMID:15509865	FYPO:0005814	(Fig. 6B,C) (comment: in meiotic cells, shmooing cells)
PMID:15509865	FYPO:0003066	data not shown , phenocopies ssm4 & dhc1
PMID:15509865	FYPO:0000927	data not shown , phenocopies ssm4 &dhc1
PMID:15509865	GO:0005515	(Fig. 3C)
PMID:15509865	GO:0005515	(Fig. 3B)
PMID:15509865	GO:0005515	(Fig. 3B)
PMID:15509865	PBO:0033208	(Table 3)
PMID:15509865	FYPO:0006130	(comment: CHECK meiosis)
PMID:15509865	FYPO:0004764	(Fig. 6B,C). (comment: in meiotic cells, shmooing cells)
PMID:15509865	FYPO:0004731	(Fig. 6A-C), (comment: CHECK during meiotic prophase, shmooing)
PMID:15509865	PBO:0033208	(Table 3)
PMID:15525536	GO:0072479	(comment: only required when there are problems , possibly involved in repair of monoorientation)
PMID:15537393	PBO:0109437	(Figure 2e)
PMID:15537393	FYPO:0002061	(Figure 2d)
PMID:15537393	FYPO:0001355	(Figure 2d)
PMID:15537393	PBO:0096587	(Figure 2e)
PMID:15537393	PBO:0109439	(Figure 2f)
PMID:15537393	PBO:0109438	(Figure 2f)
PMID:15537393	FYPO:0001082	(Figure 3d)
PMID:15537393	FYPO:0001082	(Figure 3d)
PMID:15537393	FYPO:0002196	(Figure 2f)
PMID:15537393	FYPO:0001190	(Figure 3c)
PMID:15537393	FYPO:0001190	(Figure 3c)
PMID:15537393	FYPO:0002050	(Figure 3b)
PMID:15537393	FYPO:0000647	(Figure 3b)
PMID:15537393	FYPO:0001327	(Figure 2g)
PMID:15537393	PBO:0109434	(Figure 2e)
PMID:15537393	PBO:0109435	(Figure 2e)
PMID:15537393	PBO:0109436	(Figure 2e)
PMID:15537537	GO:0005634	(Fig. 2B)
PMID:15537537	FYPO:0002360	(Fig. S1)
PMID:15537537	FYPO:0002336	(Fig. S1)
PMID:15537537	PBO:0113769	(Fig. 2G)
PMID:15537537	PBO:0113768	(Fig. 2G)
PMID:15537537	PBO:0111016	(Fig. 2G)
PMID:15537537	PBO:0111016	(Fig. 2G)
PMID:15537537	PBO:0113767	(Fig. 2G)
PMID:15537537	PBO:0113767	(Fig. 2G)
PMID:15537537	PBO:0112663	(Fig. 2G)
PMID:15537537	PBO:0112663	(Fig. 2G)
PMID:15537537	GO:0031934	(Fig. 2F)
PMID:15537537	PBO:0112927	(Fig. 1A)
PMID:15537537	PBO:0112927	(Fig. 1A)
PMID:15537537	PBO:0112929	(Fig. 1A)
PMID:15537537	PBO:0112929	(Fig. 1A)
PMID:15537537	PBO:0113770	(Fig. 5)
PMID:15537537	GO:0031934	Swi5 localization pattern closely resembled that of Swi2. Fig. 5
PMID:15537537	FYPO:0008070	(Fig. S1)
PMID:15537537	FYPO:0005865	(Fig. S1)
PMID:15546915	FYPO:0002150	(Fig. 3A)
PMID:15546915	PBO:0102105	(Figure 5) These results indicate that Rgf3p acts as a specific Rho1p activator in S. pombe.
PMID:15546915	FYPO:0002061	(Figure 4)
PMID:15546915	FYPO:0004892	(Figure 4) GI Rho1 OEX rescues echinocandin sensitivity
PMID:15546915	FYPO:0000951	(Figure 3C) (comment: CHECK shrunken cell)
PMID:15546915	FYPO:0007949	(1-3 beta D) As shown in Fig. 6C, there was an increase in the amount of β-glucan in cells that overexpressed rgf3+ compared with wild-type cells (16% and 10%, respectively)
PMID:15546915	FYPO:0002159	(Fig. 1A)
PMID:15546915	FYPO:0001968	(Fig. 6B)....an increase in enzymatic activity was detected in cells overexpressing rgf3+ compared with the activity observed in the wild-type strain
PMID:15546915	FYPO:0007949	As shown in Fig. 6C, there was an increase in the amount of β-glucan in cells that overexpressed rgf3+ compared with wild-type cells (16% and 10%, respectively)
PMID:15546915	PBO:0101163	(comment: CHECK replace with cytokinetic phase)
PMID:15546915	FYPO:0000951	(Figure 3C) (comment: CHECK shrunken cell)
PMID:15546915	FYPO:0001123	(Figure 3B) indicates a bypass of cytokinesis checkpoint
PMID:15546915	FYPO:0000647	(Fig. 1A)
PMID:15546915	FYPO:0001253	(Fig. 6A) + DAPI staining revealed that, in most multiseptate cells, each compartment contained one nucleus, indicative of a defect in cell separation after septum assembly (not shown)
PMID:15548596	FYPO:0002134	(comment: three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site)
PMID:15550243	PBO:0093613	(Fig. 3)
PMID:15550243	FYPO:0000964	Neither loss of Set9 protein, its catalytic activity, nor its H4-K20 substrate rendered cells hypersensitive to TBZ over a range of concentrations (10-30 μg/ml) or temperatures (18°C-36°C) (Figure 2D
PMID:15550243	GO:0010468	(Fig. 2B)
PMID:15550243	PBO:0112170	(Fig. 1, 3 and 4)
PMID:15550243	PBO:0112169	(Fig. 1, 3 and 4)
PMID:15550243	PBO:0112167	(Figure 1)
PMID:15550243	PBO:0112168	(Figure 1)
PMID:15550243	PBO:0112176	(Figure 1)
PMID:15550243	PBO:0112165	(Fig. 1, 3 and 4)
PMID:15550243	PBO:0112164	(Fig. 5) Crb2 phosphorylation is markedly compromised in the absence of Set9, even at low IR doses (Figure 5A).
PMID:15550243	PBO:0097793	(Fig. 5) Further, the double mutant displays a checkpoint defect equivalent to that of the crb2Δ mutant (Figure 5C).
PMID:15550243	PBO:0097793	(Fig. 5)
PMID:15550243	PBO:0112163	(Fig. 5B) Clearly, this is not the case, as the sensitivity of the double crb2T215A-set9Δ mutant is much greater than either single mutant alone and equal to deletion of crb2+ (Figure 5B).
PMID:15550243	PBO:0112161	(Fig. 5B)
PMID:15550243	PBO:0112162	(Fig. 5)
PMID:15550243	PBO:0112161	(Fig. 4D)
PMID:15550243	PBO:0112163	(Fig. 4D)
PMID:15550243	PBO:0112163	(Fig. 4D)
PMID:15550243	PBO:0112163	(Fig. 4D)
PMID:15550243	PBO:0112163	(Fig. 4D)
PMID:15550243	PBO:0112191	(Fig. 4D)
PMID:15550243	PBO:0112191	(Fig. 4D)
PMID:15550243	PBO:0112191	(Fig. 4D)
PMID:15550243	PBO:0112191	(Fig. 4D)
PMID:15550243	PBO:0112191	(Fig. 4D)
PMID:15550243	PBO:0112191	(Fig. 4D)
PMID:15550243	PBO:0112161	(Fig. 4D)
PMID:15550243	PBO:0112191	(Fig. 4D)
PMID:15550243	PBO:0112161	(Fig. 4D)
PMID:15550243	PBO:0112160	(Fig. 4C)
PMID:15550243	PBO:0097794	set9 cells arrested similar to wt but reentered mitosis markedly faster. Unlike wt, 20%-30% of set9 cells exhibited an abberant or “cut-like” mitotic phenotype. Fig. 4
PMID:15550243	GO:0006289	Genetic studies indicated that loss of Set9 protein further increased the UV sensitivity of excision repair mutants (rad13, uvde, and rad13-uvde, data not shown), arguing that Set9 does not function in excision repair.
PMID:15550243	PBO:0105171	(Fig. 3)
PMID:15550243	PBO:0105171	(Fig. 3)
PMID:15550243	PBO:0105171	(Fig. 3)
PMID:15550243	PBO:0105171	(Fig. 3)
PMID:15550243	PBO:0093613	(Fig. 3)
PMID:15550243	PBO:0093613	(Fig. 3)
PMID:15550243	PBO:0093613	resulted in cells hyper-sensitive to DNA damage induced by ultraviolent (UV) light, ionizing radiation (IR), and the topoisomerase I poison camptothecin (CPT) (Figure 3A).
PMID:15550243	GO:0031508	(Fig. 2B) Fission yeast centromeric gene silencing was also found not to be dependent upon H4-K20 methylation (Figures 2B and 2C).
PMID:15550243	PBO:0112159	(Fig. 1)
PMID:15550243	FYPO:0004217	(Fig. 1)
PMID:15550243	FYPO:0004218	(Fig. 1) Expression of exogenous wt HA- tagged Set9 but not Set9Y220A was able to rescue H4- K20 methylation in set9Δ cells (Figure 1E).
PMID:15550243	PBO:0112158	(Fig. 1)
PMID:15550243	FYPO:0004217	(Fig. 1, Figure 1D) shows that the modification is specifically Set9 dependent, as loss of Set9 but not Set1, Set2, Set6, or Clr4 resulted in essentially undetectable mono-, di-, and trimethylated H4-K20.
PMID:15550243	FYPO:0004218	(Fig. 1, Figure 1D) shows that the modification is specifically Set9 dependent, as loss of Set9 but not Set1, Set2, Set6, or Clr4 resulted in essentially undetectable mono-, di-, and trimethylated H4-K20.
PMID:15550243	FYPO:0004126	(Fig. 1)
PMID:15550243	GO:0042393	(Fig. 1A)
PMID:15572668	PBO:0112623	(Table 2)
PMID:15572668	PBO:0112633	(Fig. 2D)
PMID:15572668	PBO:0112631	Cter-GFP mutated in the helix (Helix* Cter-GFP) was concentrated in the nucleus, even during mitosis (arrow in Fig. 2C)
PMID:15572668	PBO:0112630	Cter-GFP was then observed in the region of septum formation (Fig. 1B, 16 to 52 min), where it was probably associated with the ingressing plasma membrane of the cleavage furrow. [...] An association with the cell tips and septum region was never observed for wild-type mid1p and may either result from the truncation of mid1p or from the higher concentration of this construct.
PMID:15572668	PBO:0112629	Finally, Cter-GFP remained more concentrated at the new tip compared to the old tip in short cells after sister cell separation. [...] An association with the cell tips and septum region was never observed for wild-type mid1p and may either result from the truncation of mid1p or from the higher concentration of this construct.
PMID:15572668	PBO:0112628	(Table 2)
PMID:15572668	PBO:0112620	(Table 2)
PMID:15572668	PBO:0112619	(Table 2)
PMID:15572668	PBO:0112618	(Table 2)
PMID:15572668	PBO:0112617	(Table 2)
PMID:15572668	PBO:0112620	(Table 2)
PMID:15572668	PBO:0112620	(Table 2)
PMID:15572668	PBO:0112620	(Table 2)
PMID:15572668	PBO:0112620	(Table 2)
PMID:15572668	PBO:0112632	When mutations in the helix were combined with mutations in the NLS (Helix* NLS* Cter-GFP), Cter-GFP was found in the cytoplasm. Fig. 2C
PMID:15572668	PBO:0112640	These observations indicate that Helix* NLS* mid1-mRFP colocalize with myo2-GFP and cdc12-GFP in early mitosis. This suggests that in wild-type cells mid1p mediates anchorage of myo2p and cdc12p to the central cortex in early mitosis.
PMID:15572668	PBO:0112639	(Fig. 4A)
PMID:15572668	PBO:0112638	(Fig. 4A)
PMID:15572668	PBO:0112620	(Table 2)
PMID:15572668	PBO:0112620	(Table 2)
PMID:15572668	PBO:0112620	(Table 2)
PMID:15572668	PBO:0112620	(Table 2)
PMID:15572668	PBO:0112620	(Table 2)
PMID:15572668	PBO:0112620	(Table 2)
PMID:15572668	PBO:0112620	(Table 2)
PMID:15572668	PBO:0112621	(Table 2)
PMID:15572668	PBO:0112622	(Table 2)
PMID:15572668	PBO:0112620	(Table 2)
PMID:15572668	PBO:0112624	(Table 2)
PMID:15572668	PBO:0112636	(Fig. 4A)
PMID:15572668	PBO:0112634	(Fig. 2D)
PMID:15572668	PBO:0112641	These observations indicate that Helix* NLS* mid1-mRFP colocalize with myo2-GFP and cdc12-GFP in early mitosis. This suggests that in wild-type cells mid1p mediates anchorage of myo2p and cdc12p to the central cortex in early mitosis.
PMID:15572668	PBO:0112625	(Table 2)
PMID:15572668	PBO:0112626	(Table 2)
PMID:15572668	PBO:0112627	(Table 2)
PMID:15572668	PBO:0112631	(Fig. 4A)
PMID:15572668	PBO:0112635	(Fig. 4A)
PMID:15572668	PBO:0112637	(Fig. 4A)
PMID:15601865	PBO:0109326	As expected from the two-hybrid results, neither the U-box (His6-Prp19p 1-58) nor the C terminus containing the WD40 repeats (His6-Prp19p 165-503) was able to tetramerize (data not shown).
PMID:15601865	PBO:0109325	As expected from the two-hybrid results, neither the U-box (His6-Prp19p 1-58) nor the C terminus containing the WD40 repeats (His6-Prp19p 165-503) was able to tetramerize (data not shown).
PMID:15601865	PBO:0109324	(Fig. 3)
PMID:15601865	PBO:0109325	As expected from the two-hybrid results, neither the U-box (His6-Prp19p 1-58) nor the C terminus containing the WD40 repeats (His6-Prp19p 165-503) was able to tetramerize (data not shown).
PMID:15607976	PBO:0112893	(Fig. 6C and E)
PMID:15607976	FYPO:0008235	(Table 1)
PMID:15607976	FYPO:0008235	(Table 1)
PMID:15607976	PBO:0098583	(Fig. 2B)
PMID:15607976	FYPO:0008011	(Fig. 3D)
PMID:15607976	FYPO:0008235	(Table 1)
PMID:15607976	PBO:0112892	(Fig. 3C)
PMID:15607976	PBO:0112892	(Fig. 3C)
PMID:15607976	PBO:0096189	(Fig. 2A)
PMID:15607976	PBO:0117195	The deletion analysis then indicates that the RNA synthesis activity observed in our experiments is intrinsic to Rdp1. Finally, loss of enzymatic activity for the above Rdp1 truncations correlated with the loss of centromeric silencing (Figure 6F). We also examined the activity of an Rdp1 active site point mutation and found that it lacked activity in vitro and silencing function in vivo (T. Sugiyama et al., submitted). Together these results suggest that activity of Rdp1 is required for RNAi-mediated transcriptional gene silencing.
PMID:15607976	PBO:0096189	(Fig. 6F)
PMID:15607976	PBO:0096189	(Fig. 6F)
PMID:15607976	PBO:0120491	(Fig. 2C and D)
PMID:15607976	PBO:0120491	(Fig. 2C and D)
PMID:15607976	PBO:0096189	(Fig. 6F)
PMID:15607976	PBO:0112893	(Fig. 6E)
PMID:15607976	PBO:0096189	(Fig. 2A)
PMID:15607976	FYPO:0008011	(Fig. 3D)
PMID:15607976	PBO:0112890	(Fig. 3C)
PMID:15607976	PBO:0098583	(Fig. 2B)
PMID:15607976	PBO:0098583	(Fig. 2B)
PMID:15607976	FYPO:0008011	(Fig. 3D)
PMID:15607976	FYPO:0008011	(Fig. 3D)
PMID:15607976	PBO:0112888	(Table 1)
PMID:15607976	PBO:0112891	(Fig. 3C)
PMID:15607976	PBO:0112888	(Table 1)
PMID:15615784	FYPO:0003000	(comment: CHECK assayed in vitro)
PMID:15615784	GO:0007163	(comment: CHECK based just on this paper, candidate for involved_in_or_regulates qualifier)
PMID:15615784	GO:0007163	(comment: CHECK based just on this paper, candidate for involved_in_or_regulates qualifier)
PMID:15615784	FYPO:0003000	(comment: CHECK assayed in vitro)
PMID:15615848	FYPO:0003096	(Fig. 2D). cells localization of both methylated H3-K9 and Swi6 at centromeric otr1R::ura4+ was severely affected in rdp1D903A cells (Fig. 2D).
PMID:15615848	PBO:0120490	(Fig. 5A) Although all three components of RITS (Ago1, Chp1, and Tas3) are found to be dramatically enriched at otr1R::ura4+ and centromeric repeats in wild-type cells, these proteins completely fail to localize to these centromeric loci in rdp1D903A cells
PMID:15615848	PBO:0120489	(Fig. 5A) Although all three components of RITS (Ago1, Chp1, and Tas3) are found to be dramatically enriched at otr1R::ura4+ and centromeric repeats in wild-type cells, these proteins completely fail to localize to these centromeric loci in rdp1D903A cells
PMID:15615848	PBO:0120488	(Fig. 5A) Although all three components of RITS (Ago1, Chp1, and Tas3) are found to be dramatically enriched at otr1R::ura4+ and centromeric repeats in wild-type cells, these proteins completely fail to localize to these centromeric loci in rdp1D903A cells
PMID:15615848	FYPO:0008011	(Fig. 4B). We found that, whereas siRNAs could be readily detected in the affinity-purified fraction of RITS from wild-type cells, there were no detectable RITS- associated siRNAs present in rdp1D903A, rdp1Δ, or dcr1Δ cells
PMID:15615848	GO:0140720	(Fig. 1A)
PMID:15615848	GO:0031934	(Fig. 1A) (comment: CenH)
PMID:15615848	GO:0005721	(Fig. 1A) (comment: CenH)
PMID:15615848	PBO:0104870	(Fig. 1B)
PMID:15615848	PBO:0104870	(Fig. 1B)
PMID:15615848	PBO:0104870	(Fig. 1B)
PMID:15615848	PBO:0104870	(Fig. 1B)
PMID:15615848	FYPO:0008011	(Fig. 4B). We found that, whereas siRNAs could be readily detected in the affinity-purified fraction of RITS from wild-type cells, there were no detectable RITS- associated siRNAs present in rdp1D903A, rdp1Δ, or dcr1Δ cells
PMID:15615848	FYPO:0008011	(Fig. 4B). We found that, whereas siRNAs could be readily detected in the affinity-purified fraction of RITS from wild-type cells, there were no detectable RITS- associated siRNAs present in rdp1D903A, rdp1Δ, or dcr1Δ cells
PMID:15615848	FYPO:0008010	In contrast, a noticeably larger fraction of rdp1D903A cells exhibited an increased number of Swi6 foci, and most of these Swi6 foci still colocalized with Taz1, suggesting a declustering of telomeres even though the localization of telomeres to the nuclear periphery was unaffected (Fig. 3 C and D)
PMID:15615848	PBO:0117195	herefore, we conclude from these analyses that the RdRP activity of Rdp1 is essential for the generation of RITS-associated siRNAs. plus centrromeric chromatin assays
PMID:15615848	FYPO:0004974	In contrast, a noticeably larger fraction of rdp1D903A cells exhibited an increased number of Swi6 foci, and most of these Swi6 foci still colocalized with Taz1, suggesting a declustering of telomeres even though the localization of telomeres to the nuclear periphery was unaffected (Fig. 3 C and D)
PMID:15615848	FYPO:0008009	(Fig. 3C and D) In contrast, a noticeably larger fraction of rdp1D903A cells exhibited an increased number of Swi6 foci, and most of these Swi6 foci still colocalized with Taz1, suggesting a declustering of telomeres even though the localization of telomeres to the nuclear periphery was unaffected
PMID:15615848	PBO:0032780	. We found that rdp1 mutants have a significantly higher percentage (∼20%) of cells with lagging chromosomes during late anaphase than in the wild-type strain (􏰆1%) (Fig. 3B)
PMID:15615848	PBO:0093562	hypersensitive to TBZ, indicating that chromosome segregation is not robust in these mutant cells (Fig. 3A).
PMID:15615848	PBO:0104870	(Fig. 1B)
PMID:15615848	PBO:0120486	(Fig. 1B)
PMID:15615848	PBO:0104872	(Fig. 2B) Immunoblotting assay showed that the protein level of the Rdp1 mutant (Rdp1D903A) is comparable to that of wild-type Rdp1, suggesting that the D903A mutation does not affect the stability of the mutant protein
PMID:15615848	FYPO:0007334	(Fig. 2C). (otr1R::ura4+) (Fig. 2B) Immunoblotting assay showed that the protein level of the Rdp1 mutant (Rdp1D903A) is comparable to that of wild-type Rdp1, suggesting that the D903A mutation does not affect the stability of the mutant protein
PMID:15615848	PBO:0120487	(Fig. 2D). cells localization of both methylated H3-K9 and Swi6 at centromeric otr1R::ura4+ was severely affected in rdp1D903A cells (Fig. 2D).
PMID:15616156	GO:0005674	e, we found that more Tfg3-H formed complexes with GST-Tfg3 (Figure 1D), confirming our hypothesis that Tfg3 forms dimers or multimers. Our observations indicated that Tfg3 is a component of TFIIF in S.pombe as it is in S.cerevisiae.
PMID:15616156	PBO:0093595	When S.pombe cells that lacked Tfg3 were streaked on a plate that contained 0.9 M KCl, they did not grow. In contrast, tfg3+ cells were able to grow (Figure 2G).
PMID:15616156	PBO:0093607	(Figure 2I).
PMID:15616156	PBO:0093558	At 38 C, however, the growth rate of both JY741/tfg3::ura4 and JY741/tfg3D was significantly reduced than JY741, and only small-sized colonies were detected after prolonged incubation, indicating that tfg3+ was essential for cell growth at elevated temperatures.
PMID:15616156	FYPO:0002060	our spores from each tetrad grew (Figure 2B) and each tetrad contained two Ura+ and two Ura− spores (data not shown), indicating that tfg3+ was nonessential for cell growth under the conditions employed.
PMID:15616156	GO:0005737	(Figure 2A)
PMID:15616156	GO:0005730	(Figure 2A)
PMID:15616156	GO:0005654	(Figure 2A)
PMID:15625190	PBO:0100071	(comment: three-hybrid assay; also binds exogenous ESEs)
PMID:15632064	GO:0005666	Mutated Rpc11p subunits associate with Pol III and impair its RNA 3' cleavage activity.
PMID:15632064	PBO:0108882	(comment: trna chaperone)
PMID:15632064	FYPO:0007008	(Fig. 1) The data suggest that the mutants are not deficient in termination efficiency.
PMID:15632064	FYPO:0007326	(Fig. 1) The data suggest that the mutants are not deficient in termination efficiency.
PMID:15632064	FYPO:0007326	(Fig. 1) The data suggest that the mutants are not deficient in termination efficiency.
PMID:15643072	FYPO:0001250	(comment: assayed in strain with cdc10-129 to synchronize)
PMID:15647375	FYPO:0000229	(Fig. 4)
PMID:15647375	FYPO:0002303	(Fig. 4)
PMID:15647375	FYPO:0000252	(Fig. 4)
PMID:15654094	GO:0042138	(comment: assayed using 160-bp palindromic sequence inserted into ade6 locus)
PMID:15654094	GO:0042138	(comment: assayed using 160-bp palindromic sequence inserted into ade6 locus)
PMID:15654094	GO:0007131	(comment: assayed using 160-bp palindromic sequence inserted into ade6 locus)
PMID:15654094	GO:0042138	(comment: assayed using 160-bp palindromic sequence inserted into ade6 locus)
PMID:15665379	PBO:0103509	(Fig. 2)
PMID:15665379	PBO:0103510	(Fig. 3b)
PMID:15665379	PBO:0103509	(Fig. 2)
PMID:15665379	PBO:0103508	(Fig. 2)
PMID:15671491	FYPO:0003933	(comment: assayed using reporter based on S. cerevisiae MFA2)
PMID:15671491	FYPO:0003932	(comment: assayed using reporter based on S. cerevisiae MFA2)
PMID:15671491	FYPO:0003932	(comment: assayed using reporter based on S. cerevisiae MFA2)
PMID:15671491	FYPO:0003933	(comment: assayed using reporter based on S. cerevisiae MFA2)
PMID:15671491	FYPO:0003934	(comment: assayed using reporter based on S. cerevisiae MFA2)
PMID:15689489	PBO:0106123	(comment: In metaphase the difference kinds of microtubules cannot be distinguished, but they can be distinguished during anaphase B)
PMID:15689489	FYPO:0004395	(Fig. 6)
PMID:15689489	FYPO:0007304	(Fig. 6)
PMID:15689489	FYPO:0005722	(Fig. 6)
PMID:15689489	FYPO:0003481	(Fig. 1)
PMID:15689489	FYPO:0005558	(Fig. 2)
PMID:15689489	FYPO:0002401	(Fig. 2)
PMID:15689489	FYPO:0003840	(Fig. 1)
PMID:15689489	PBO:0106125	(Fig. 1)
PMID:15689489	FYPO:0007981	(Fig. 6)
PMID:15689489	FYPO:0003302	(Fig. 5)
PMID:15689489	PBO:0106124	(Fig. 1)
PMID:15710398	FYPO:0000636	Time-course measurements of the doubling times of these cultures showed that at day 5 the growth rate of strains expressing Msp1pK276A, Msp1pD50 and Msp1pD25 was greatly increased... (Fig. 4A).
PMID:15710398	FYPO:0003810	On the contrary, even slight overexpression of Msp1pK276A, Msp1pD50 or Msp1pD25 induced mitochondrial fragmentation; in about 60% of the cells the mitochondria appeared as small more or less clustered individual dots.
PMID:15710398	FYPO:0000636	Time-course measurements of the doubling times of these cultures showed that at day 5 the growth rate of strains expressing Msp1pK276A, Msp1pD50 and Msp1pD25 was greatly increased... (Fig. 4A).
PMID:15710398	FYPO:0003810	On the contrary, even slight overexpression of Msp1pK276A, Msp1pD50 or Msp1pD25 induced mitochondrial fragmentation; in about 60% of the cells the mitochondria appeared as small more or less clustered individual dots.
PMID:15710398	FYPO:0000636	Time-course measurements of the doubling times of these cultures showed that at day 5 the growth rate of strains expressing Msp1pK276A, Msp1pD50 and Msp1pD25 was greatly increased... (Fig. 4A).
PMID:15710398	FYPO:0008108	In the Dmsp1Ddnm1 strain, mtDNA depletion (Fig. 5F) and lethality (not shown) did not occur
PMID:15710398	FYPO:0008108	In the Dmsp1Ddnm1 strain, mtDNA depletion (Fig. 5F) and lethality (not shown) did not occur
PMID:15710398	FYPO:0003810	On the contrary, even slight overexpression of Msp1pK276A, Msp1pD50 or Msp1pD25 induced mitochondrial fragmentation; in about 60% of the cells the mitochondria appeared as small more or less clustered individual dots.
PMID:15710398	FYPO:0002061	GTPase (Msp1pK276A) and coiledcoil deleted (Msp1pD25-D50) mutants did not support the function of Msp1p as they failed to complement the msp1+ gene deletion.
PMID:15710398	FYPO:0002061	while cells that expressed cytosolic Msp1pDMIS or CAT died.
PMID:15710398	FYPO:0002060	In the Dmsp1Ddnm1 strain, mtDNA depletion (Fig. 5F) and lethality (not shown) did not occur.
PMID:15710398	FYPO:0002060	In the Dmsp1Ddnm1 strain, mtDNA depletion (Fig. 5F) and lethality (not shown) did not occur.
PMID:15710398	FYPO:0003896	In the doubledisrupted Dmsp1Ddnm1 strain, the mitochondria formed elongated tubules which resembled those seen in wild-type cells ...... (Fig. 5E).
PMID:15710398	FYPO:0003896	In the doubledisrupted Dmsp1Ddnm1 strain, the mitochondria formed elongated tubules which resembled those seen in wild-type cells ...... (Fig. 5E).
PMID:15710398	FYPO:0002061	while cells that expressed cytosolic Msp1pDMIS or CAT died.
PMID:15710398	FYPO:0003810	fragmented: By 27 h, when repression was almost complete, the mitochondrial network fragmented into clusters of small rounded mitochondria. This phenotype is reminiscent of the mitochondrial morphology defect observed in S. cerevisiae deleted for MGM1 [18].
PMID:15710398	FYPO:0003807	the mitochondrial network appeared as highly interconnected tubules forming net-like structures (Fig. 5A).
PMID:15710398	FYPO:0000492	(Fig. 4B)
PMID:15710398	FYPO:0002061	while cells that expressed cytosolic Msp1pDMIS or CAT died.
PMID:15710398	PBO:0109717	In Msp1p overexpressing cells, more than 85% of the cells had an aggregated filamentous mitochondrial network.
PMID:15710398	FYPO:0003896	while cells that expressed cytosolic Msp1pDMIS or CAT died.
PMID:15710398	FYPO:0000492	(Fig. 4B)
PMID:15710398	GO:0008053	(comment: MEMBRANE)
PMID:15710398	FYPO:0000492	(Fig. 4B), Loss of the GTPase function of Msp1p is thus sufficient to affect the maintenance of the mitochondrial genome and the viability of S. pombe cells.
PMID:15716270	FYPO:0003699	(comment: 18S rRNA position 1204)
PMID:15716270	FYPO:0003699	(comment: 25S rRNA position 1723)
PMID:15716270	FYPO:0003699	(comment: 25S rRNA positions 2298, 2401)
PMID:15716270	FYPO:0003699	(comment: 25S rRNA position 3069)
PMID:15716270	FYPO:0003699	(comment: 25S rRNA position 1074)
PMID:15716270	FYPO:0003699	(comment: 25S rRNA position 3017)
PMID:15716270	FYPO:0003699	(comment: 25S rRNA positions 2216, 2220, 2351)
PMID:15716270	FYPO:0003699	(comment: 18S rRNA positions 208, 2341)
PMID:15716270	FYPO:0003699	(comment: 18S rRNA position 1307)
PMID:15716270	FYPO:0003699	(comment: 25S rRNA position 1084)
PMID:15728720	FYPO:0000209	(comment: CHECK increased centromere spindle pole body detachment during meiotic prophase fission-yeast-phenotype/2055/)
PMID:15731009	GO:0110085	(comment: dependent on F-actin (asayed using Latrunculin A); independent of microtubules (assayed using MBC))
PMID:15731009	GO:0030950	(comment: based just on this paper, candidate for involved_in_or_regulates qualifier)
PMID:15731009	GO:0007163	(comment: based just on this paper, candidate for involved_in_or_regulates qualifier)
PMID:15731009	PBO:0107072	(comment: CHECK same as orb3-167 alone)
PMID:15731009	GO:0030479	(comment: dependent on F-actin (asayed using Latrunculin A); independent of microtubules (assayed using MBC))
PMID:15731009	PBO:0107072	(comment: CHECK same as orb3-167 alone)
PMID:15731009	GO:0004672	(comment: assayed using casein; doesn't quite rule out tyrosine phosphorylation)
PMID:15743828	PBO:0111624	In contrast, ΔCDchp1-6xmyc exhibited a diffuse faint spotty staining pattern throughout the nucleoplasm and was not associated with chromatin (Fig. 2E). Thus, the chromodomain, but not the RRM, is essential for Chp1 localization to all sites of heterochromatin and for normal Chp1 function at centromeric sequences.
PMID:15743828	PBO:0111626	Surprisingly, however, other foci of Chp1-6xmyc and Tas3- 13xmyc persisted in ago1Δ cells. Similar results were obtained in cells from which Dicer was deleted (Fig. 5A and B, right panels).
PMID:15743828	GO:0140720	Thus, Tas3-13xmyc and Chp1-6xmyc colocalize to the mat2/3 locus, to telomeres, and to centromeres and possibly associate with all sites of heterochromatin.
PMID:15743828	PBO:0111013	We also assessed the localization of Chp1-6xmyc and Tas3- 13xmyc in cells lacking tas3 and chp1, respectively (Fig. 6A). In cells with tas3 deleted, Chp1 was delocalized, with a cloud of small foci of staining that mainly accumulated over the nucleolus (Fig. 6A)
PMID:15743828	PBO:0111627	Tas3-13xmyc protein was essentially lost in chp1Δ cells, whereas it was present at normal levels in the ago1Δ cells (Fig. 6B). To address whether loss of Tas3-13xmyc protein in chp1Δ cells was due to suppression of tas3-13xmyc+ transcription, we performed quantitative RT-PCR using RNA prepared from wild-type, chp1Δ, and ago1Δ backgrounds. Deletion of chp1+ had no effect on tas3-13xmyc+ transcript levels (Fig. 6C); therefore, the loss of Tas3 protein in chp1 null cells is a posttranscriptional effect.
PMID:15743828	FYPO:0002827	Nonetheless, deletion of chp1+ or ago1+ only slightly alleviated silencing (20, 38), as revealed by the presence of pink colonies compared with the red, fully repressed colonies (Fig. 8A).
PMID:15743828	FYPO:0002827	Nonetheless, deletion of chp1+ or ago1+ only slightly alleviated silencing (20, 38), as revealed by the presence of pink colonies compared with the red, fully repressed colonies (Fig. 8A).
PMID:15743828	PBO:0110927	Surprisingly, however, other foci of Chp1-6xmyc and Tas3- 13xmyc persisted in ago1Δ cells. Similar results were obtained in cells from which Dicer was deleted (Fig. 5A and B, right panels).
PMID:15743828	FYPO:0000141	These cells exhibited high levels of chromosome segregation defects (Fig. 3C) and defects in centromeric silencing (Fig. 3B).
PMID:15743828	PBO:0111621	These cells exhibited high levels of chromosome segregation defects (Fig. 3C) and defects in centromeric silencing (Fig. 3B).
PMID:15743828	PBO:0111624	Consistent with this result, immunolocalization of 3xHA- chp11-409 with anti-HA antibody revealed that the truncated protein was diffusely localized throughout the chromatin and nucleolus (Fig. 3D).
PMID:15743828	PBO:0111621	Importantly, cells lacking only the Chp1 chromodomain (ΔCDchp1-6xmyc) behaved similar to the chp1 null strain, with elevated transcription of the centromeric marker gene (Fig. 2C) and numerous mitotic chromosome segregation defects (Fig. 2D)
PMID:15743828	PBO:0111622	n contrast, cells lacking the RRM domain of Chp1 (ΔRRMchp1-6xmyc) exhibited no loss of Chp1 function.
PMID:15743828	FYPO:0000141	Importantly, cells lacking only the Chp1 chromodomain (ΔCDchp1-6xmyc) behaved similar to the chp1 null strain, with elevated transcription of the centromeric marker gene (Fig. 2C) and numerous mitotic chromosome segregation defects (Fig. 2D)
PMID:15743828	PBO:0111625	in ago1 cells there is a loss of centromere-associated Chp1 and Tas3, as revealed by loss of costaining of Chp1-6xmyc (Fig. 5A) and Tas3-13xmyc (Fig. 5B)
PMID:15743828	PBO:0111013	in ago1 cells there is a loss of centromere-associated Chp1 and Tas3, as revealed by loss of costaining of Chp1-6xmyc (Fig. 5A) and Tas3-13xmyc (Fig. 5B)
PMID:15743828	PBO:0111626	Surprisingly, however, other foci of Chp1-6xmyc and Tas3- 13xmyc persisted in ago1Δ cells. Similar results were obtained in cells from which Dicer was deleted (Fig. 5A and B, right panels).
PMID:15743828	GO:0031934	Thus, Tas3-13xmyc and Chp1-6xmyc colocalize to the mat2/3 locus, to telomeres, and to centromeres and possibly associate with all sites of heterochromatin.
PMID:15743828	PBO:0110927	Surprisingly, however, other foci of Chp1-6xmyc and Tas3- 13xmyc persisted in ago1Δ cells. Similar results were obtained in cells from which Dicer was deleted (Fig. 5A and B, right panels).
PMID:15743828	GO:0005721	Thus, Tas3-13xmyc and Chp1-6xmyc colocalize to the mat2/3 locus, to telomeres, and to centromeres and possibly associate with all sites of heterochromatin.
PMID:15743828	PBO:0111623	n contrast, cells lacking the RRM domain of Chp1 (ΔRRMchp1-6xmyc) exhibited no loss of Chp1 function.
PMID:15743909	FYPO:0003066	(comment: CHECK homozygous cross)
PMID:15743909	FYPO:0003066	(comment: CHECK homozygous cross)
PMID:15743909	FYPO:0003066	(comment: CHECK homozygous cross)
PMID:15743909	PBO:0095173	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:15743909	PBO:0095174	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:15772152	FYPO:0004724	Consistent with this, we observed that the nuclear envelope formed thin protrusions that grew and shrank (Figure 4, G and H, Supplementary Movie 8). Such intranuclear MTs and nuclear envelope distortions were notobserved in wild-type cells. Several criteria confirmed that these cells with intranuclear MTs were in interphase and not in mitosis
PMID:15772152	FYPO:0000899	(comment: normal length)
PMID:15797383	GO:0032933	(Fig. 2,3,4)
PMID:15797383	GO:0032936	(Fig. 1)
PMID:15797383	GO:0032933	(Fig. 2,5)
PMID:15797383	PBO:0095815	(Fig. 2)
PMID:15797383	GO:0032936	(Fig. 1)
PMID:15797383	PBO:0095816	(Fig. 2 lane 11-12)
PMID:15797925	GO:0034399	punctate, similar to nuclear pore components (comment: localization not dependent on microtubules)
PMID:15797925	FYPO:0004121	(comment: assayed using NLS-LacI-GFP construct)
PMID:15800064	PBO:0106051	(Fig. 5A)
PMID:15800064	PBO:0037744	(Figure 3A)
PMID:15800064	PBO:0106052	(Fig. 5B)
PMID:15800064	FYPO:0003171	(Fig. 6B)
PMID:15800064	PBO:0106051	(Fig. 5A)
PMID:15800064	FYPO:0004611	(Figure 3A)
PMID:15800064	FYPO:0004624	(Figure 3A,3C)
PMID:15800064	FYPO:0003126	(Figure 3A,3C)
PMID:15800064	PBO:0037745	(Figure 3A)
PMID:15800064	FYPO:0005688	(Figure 3A)
PMID:15800064	PBO:0106048	(Figure 3) (comment: CHECK fypo/issues/2830)
PMID:15800064	PBO:0106049	(Figure 3) (comment: CHECK fypo/issues/2830)
PMID:15800064	PBO:0106050	(Figure 3B) (comment: CHECK fypo/issues/2830)
PMID:15800064	FYPO:0004766	(Figure 4)
PMID:15800064	FYPO:0002026	(Fig. 6C)
PMID:15800064	PBO:0023023	(Fig. 2A,2C,2D)
PMID:15800064	PBO:0022298	(Fig. 2A,2D)
PMID:15800064	GO:0005515	(Fig. 1C)
PMID:15800064	PBO:0037743	(Fig. 2A,2D)
PMID:15800064	PBO:0037148	(Fig. 2A,2C,2D)
PMID:15809031	PBO:0097169	inferred from direct physical interactions between tea4,tea1 and tea4,for3, plus tea4delta phenotype
PMID:15827087	PBO:0103541	data not shown, same as Fig 4C
PMID:15827087	PBO:0103538	(Fig. 1B) (comment: This distribution is only seen in cells with a rod shaped appearance)
PMID:15827087	FYPO:0002058	data not shown
PMID:15827087	FYPO:0003150	(Fig. 2A, 2B)
PMID:15827087	PBO:0103539	(Fig. 2A, 2B)
PMID:15827087	PBO:0037448	(Fig. 2D)
PMID:15827087	FYPO:0000426	data not shown
PMID:15827087	PBO:0103535	Table 2 (comment: This distribution is only seen in cells with a rod shaped appearance)
PMID:15827087	PBO:0103543	(Fig. 2A) and data not shown
PMID:15827087	FYPO:0002058	data not shown
PMID:15827087	PBO:0094949	data not shown (comment: Non permissive temperature is 32°C and above)
PMID:15827087	FYPO:0001120	(Fig. 1) (comment: They describe cells as swollen in their middle region)
PMID:15827087	PBO:0037444	(Table 2)
PMID:15827087	PBO:0037439	(Fig. 1C, Table 2)
PMID:15827087	FYPO:0000021	(Fig. 1)
PMID:15827087	FYPO:0000224	(Fig. 1) (comment: They describe cells as swollen in their middle region)
PMID:15827087	PBO:0037443	Table 2 (comment: This distribution is only seen in cells with a rod shaped appearance)
PMID:15827087	PBO:0103536	Table 2 (comment: This distribution is only seen in cells with a rod shaped appearance)
PMID:15827087	FYPO:0000015	(Fig. 1) (comment: permissive temperature is 25°C)
PMID:15827087	FYPO:0001355	data not shown, (comment: permissive temperature 25°C)
PMID:15827087	PBO:0037440	(Fig. 1, Table 2)
PMID:15827087	PBO:0018339	(Fig. 4B)
PMID:15827087	PBO:0103541	(Fig. 4C)
PMID:15827087	FYPO:0003150	(Fig. 2A) and data not shown
PMID:15827087	PBO:0099011	(Fig. 3A, 2B) Deletion of the talin domain suppresses the premature activation of bipolar growth in a cdc10 mutant in latA
PMID:15827087	PBO:0019098	(Fig. 4D)
PMID:15827087	PBO:0103540	(Fig. 4B)
PMID:15827087	PBO:0037449	data for cdc25-22 block not shown but see also Fig4A
PMID:15837798	FYPO:0004700	mto2 deletion strain, which yielded viable but slightly bent cells (Fig. 3 A)
PMID:15837798	FYPO:0005686	The average number of MT bundles in mto2Δ cells (n = 1.3 ± 0.7 SD; Fig. 3 E) was significantly lower than in wild-type cells (3.6 ± 0.9)
PMID:15837798	PBO:0104131	mto2 deletion strain, which yielded viable but slightly bent cells (Fig. 3 A)
PMID:15857958	PBO:0099474	(Fig. 6)
PMID:15857958	PBO:0099473	(Fig. 6)
PMID:15857958	PBO:0099472	(Fig. 7)
PMID:15857958	FYPO:0006917	(Fig. 3)
PMID:15857958	FYPO:0006917	(Fig. 3)
PMID:15857958	PBO:0099464	(Fig. 3) mad2 signal.
PMID:15857958	FYPO:0000729	(Fig. 3)
PMID:15857958	FYPO:0004087	(Fig. 2)
PMID:15857958	FYPO:0000324	(Fig. 2,3) (comment: cdc13 signal)
PMID:15857958	PBO:0099463	(Fig. 2)
PMID:15857958	PBO:0099462	(Fig. 2)
PMID:15857958	PBO:0099471	(Fig. 5)
PMID:15857958	PBO:0099470	(Fig. 5)
PMID:15857958	PBO:0099470	(Fig. 5)
PMID:15857958	PBO:0099469	(Fig. 5)
PMID:15857958	PBO:0099468	(Fig. 5)
PMID:15857958	PBO:0099467	(Fig. 5)
PMID:15857958	PBO:0099467	(Fig. 5)
PMID:15857958	PBO:0099466	(Fig. 5)
PMID:15857958	PBO:0099466	(Fig. 5)
PMID:15857958	PBO:0037128	(Fig. 5)
PMID:15857958	PBO:0037128	(Fig. 5)
PMID:15857958	PBO:0099465	(Fig. 5)
PMID:15857958	PBO:0099465	(Fig. 5)
PMID:15857958	FYPO:0001355	(Fig. 5)
PMID:15857958	FYPO:0002061	(Fig. 7)
PMID:15857958	FYPO:0002060	(Fig. 5)
PMID:15857958	FYPO:0002061	(Fig. 7)
PMID:15857958	FYPO:0002061	(Fig. 7)
PMID:15857958	PBO:0099477	(Fig. 7)
PMID:15857958	PBO:0099476	(Fig. 7)
PMID:15857958	PBO:0099475	(Fig. 7)
PMID:15857958	FYPO:0002060	(Fig. 5)
PMID:15857958	FYPO:0002060	(Fig. 5)
PMID:15857958	FYPO:0002061	(Fig. 5)
PMID:15857958	FYPO:0002061	(Fig. 5)
PMID:15857958	PBO:0023726	(Fig. 4)
PMID:15857958	PBO:0018346	(Fig. 4)
PMID:15857958	FYPO:0000729	(Fig. 3)
PMID:1588914	PBO:0093712	multicopy pwis4 does not suppress cdc2-3w phenotype
PMID:1588914	FYPO:0002060	the spo12 gene on a multi copy plasmid pwis3 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	FYPO:0002060	the wis4 gene on a multi copy plasmid pwis4 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	FYPO:0002061	multicopy pwis1 does not suppress cdc25-22 ts phenotype showing that wis1 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	PBO:0097558	Table 2 the wis1 gene on a multi copy plasmid pwis1 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	PBO:0100670	the wis2 gene on a multi copy plasmid pwis2 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	FYPO:0002061	multicopy pwis3 does not suppress cdc25-22 ts phenotype showing that spo12 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	PBO:0019154	multicopy pwis1 does not suppress cdc2-33 ts phenotype
PMID:1588914	FYPO:0002061	multicopy pwis1 does not suppress cdc13-117 ts phenotype
PMID:1588914	FYPO:0002061	multicopy pwis2 does not suppress cdc2-33 ts phenotype
PMID:1588914	FYPO:0002061	multicopy pwis2 does not suppress cdc13-117 ts phenotype
PMID:1588914	FYPO:0002061	multicopy pwis3 does not suppress cdc2-33 ts phenotype
PMID:1588914	FYPO:0002061	multicopy pwis3 does not suppress cdc13-117 ts phenotype
PMID:1588914	FYPO:0002061	multicopy pwis4 does not suppress cdc2-33 ts phenotype
PMID:1588914	FYPO:0002061	multicopy pwis4 does not suppress cdc13-117 ts phenotype
PMID:1588914	PBO:0019154	multicopy pwis2 does not suppress cdc25-22 ts phenotype showing that wis2 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	PBO:0100671	the spo12 gene on a multi copy plasmid pwis3 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	PBO:0100671	the wis4 gene on a multi copy plasmid pwis4 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	PBO:0019154	multicopy pwis1 does not suppress cdc25-22 ts phenotype showing that wis1 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	FYPO:0002061	multicopy pwis2 does not suppress cdc25-22 ts phenotype showing that wis2 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	PBO:0093712	multicopy pwis4 does not suppress cdc2-1w phenotype
PMID:1588914	PBO:0019154	multicopy pwis4 does not suppress cdc13-117 ts phenotype
PMID:1588914	PBO:0019154	multicopy pwis4 does not suppress cdc2-33 ts phenotype
PMID:1588914	PBO:0097762	multicopy pwis3 does not suppress cdr2-69 phenotype
PMID:1588914	PBO:0097762	multicopy pwis3 does not suppress cdr1-34 phenotype
PMID:1588914	PBO:0093712	multicopy pwis3 does not suppress wee1-50 ts phenotype
PMID:1588914	PBO:0093712	multicopy pwis3 does not suppress cdc2-3w phenotype
PMID:1588914	PBO:0093712	multicopy pwis3 does not suppress cdc2-1w phenotype
PMID:1588914	PBO:0019154	multicopy pwis3 does not suppress cdc13-117 ts phenotype
PMID:1588914	PBO:0019154	multicopy pwis3 does not suppress cdc2-33 ts phenotype
PMID:1588914	PBO:0097762	multicopy pwis2 does not suppress cdr2-69 phenotype
PMID:1588914	FYPO:0001492	Table 3 cells are 30-50% longer than wild type
PMID:1588914	PBO:0019154	multicopy pwis4 does not suppress cdc25-22 ts phenotype showing that wis4 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	FYPO:0002176	Table 3 pwis4 surpresses the elongated cell phenotype of win1-1
PMID:1588914	FYPO:0002176	data not shown
PMID:1588914	FYPO:0002060	see Table 2
PMID:1588914	FYPO:0002060	see Table 2
PMID:1588914	FYPO:0002060	see Table 2
PMID:1588914	FYPO:0002060	see Table 2
PMID:1588914	PBO:0097762	multicopy pwis2 does not suppress cdr1-34 phenotype
PMID:1588914	FYPO:0002060	the wis2 gene on a multi copy plasmid pwis2 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	FYPO:0002060	the wis1 gene on a multi copy plasmid pwis1 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	PBO:0093712	multicopy pwis2 does not suppress wee1-50 ts phenotype
PMID:1588914	PBO:0093712	multicopy pwis2 does not suppress cdc2-3w phenotype
PMID:1588914	PBO:0093712	multicopy pwis2 does not suppress cdc2-1w phenotype
PMID:1588914	PBO:0019154	multicopy pwis2 does not suppress cdc13-117 ts phenotype
PMID:1588914	PBO:0019154	multicopy pwis2 does not suppress cdc2-33 ts phenotype
PMID:1588914	PBO:0097762	multicopy pwis1 does not suppress cdr2-69 phenotype
PMID:1588914	PBO:0097762	multicopy pwis1 does not suppress cdr1-34 phenotype
PMID:1588914	PBO:0093712	multicopy pwis1 does not suppress wee1-50 ts phenotype
PMID:1588914	PBO:0093712	multicopy pwis1 does not suppress cdc2-3w phenotype
PMID:1588914	PBO:0093712	multicopy pwis1 does not suppress cdc2-1w phenotype
PMID:1588914	PBO:0019154	multicopy pwis1 does not suppress cdc13-117 ts phenotype
PMID:1588914	FYPO:0002061	multicopy pwis1 does not suppress cdc2-33 ts phenotype
PMID:1588914	FYPO:0002061	multicopy pwis4 does not suppress cdc25-22 ts phenotype showing that wis4 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	PBO:0019154	multicopy pwis3 does not suppress cdc25-22 ts phenotype showing that spo12 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	FYPO:0002060	see Table 2
PMID:1588914	FYPO:0002061	Table 2 pwis4 does not suppress wee1-50 cdc25-22 mcs6-13
PMID:1588914	FYPO:0001490	Table 2 pwis4 does not suppress wee1-50 cdc25-22 mcs6-13
PMID:1588914	PBO:0100671	see Table 2
PMID:1588914	PBO:0100670	see Table 2
PMID:1588914	FYPO:0002061	Table 2 pwis1 does not suppress wee1-50 cdc25-22 mcs6-13
PMID:1588914	FYPO:0001490	Table 2 pwis1 does not suppress wee1-50 cdc25-22 mcs6-13
PMID:1588914	FYPO:0002061	see Table 2 multi copy pwis4 does not suppress cdc25-22 wee1-50 mcs4-13
PMID:1588914	FYPO:0001490	See Table 2 multi copy pwis4 does not suppress cdc25-22 wee1-50 mcs4-13
PMID:1588914	PBO:0100671	see Table 2
PMID:1588914	PBO:0100670	see Table 2
PMID:1588914	PBO:0097558	see Table 2
PMID:1588914	PBO:0097762	multicopy pwis4 does not suppress cdr2-69 phenotype
PMID:1588914	PBO:0097762	multicopy pwis4 does not suppress cdr1-34 phenotype
PMID:1588914	PBO:0093712	multicopy pwis4 does not suppress wee1-50 ts phenotype
PMID:15908586	FYPO:0004331	(Figure 1)
PMID:15908586	PBO:0105932	dhIII transcripts were detectable in hrp1D dcr1D and dcr1D cells, but not in the wild-type and hrp1D cells (Figure 4E). The dhIII transcripts were more abundant in hrp1D dcr1D cells than in dcr1D cells consistent with the reduced silencing observed at dg-dh in hrp1D (Figure 1E). If transcripts read through in hrp1D from dh-dg into the central core region, then they should be readily detectable in the intervening imrIII region. However, imrIII transcripts were not observed in hrp1D cells. From these results, we concluded that the hrp1D mutant does not cause read through of dg-dh transcripts into the central core region. Hrp1 is present at the centromere in a cell
PMID:15908586	FYPO:0001355	The mis6-302 hrp1D double mutant had a reduced growth at 30 C as compared with the mis6-302 and hrp1D single mutants (Figure 3C).
PMID:15908586	FYPO:0001355	The mis6-302 hrp1D double mutant had a reduced growth at 30 C as compared with the mis6-302 and hrp1D single mutants (Figure 3C).
PMID:15908586	FYPO:0008062	(Figure 3) There was a 4- fold reduction of Cnp1 at cnt2 in hrp1D cells
PMID:15908586	PBO:0105931	(Figure 3) There was a 4- fold reduction of Cnp1 at cnt2 in hrp1D cells
PMID:15908586	FYPO:0007313	(Figure 3)
PMID:15908586	FYPO:0007314	(Figure 3)
PMID:15908586	PBO:0105929	(Figure 2) Further examination of the IF samples revealed that hrp1D single and hrp1D hrp3D double mutants cells showed elevated numbers of asymmetric segregation (large and small nuclei) in late anaphase cells
PMID:15908586	PBO:0033665	(Figure 2)
PMID:15908586	PBO:0033885	(Figure 2)
PMID:15908586	PBO:0105928	(Figure 2)
PMID:15908586	FYPO:0002620	(Figure 2)
PMID:15908586	FYPO:0002620	(Figure 2)
PMID:15908586	PBO:0093727	(Figure 2A) However, growth of the double mutant cells was completely inhibited by TSA.
PMID:15908586	FYPO:0001357	(Figure 2A) In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	FYPO:0001357	(Figure 2A) In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	FYPO:0001355	(Figure 2)
PMID:15908586	FYPO:0003937	(Figure 2) In cultures without TSA, the hrp1D cells grew slightly faster than wt cells as reported previously (48).
PMID:15908586	FYPO:0002061	(Figure 2A) In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	FYPO:0002061	(Figure 2A) In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	PBO:0093562	(Figure 2A) In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	PBO:0093562	(Figure 2A) In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	PBO:0093564	(Figure 2A) In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	FYPO:0002827	(Figure 1)
PMID:15908586	FYPO:0004542	(Figure 1)
PMID:15908586	FYPO:0003412	(Figure 1)
PMID:15908586	PBO:0093564	(Figure 2A) In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15915339	PBO:0093629	more sensitive than either single mutant
PMID:15915339	PBO:0093616	more sensitive than either single mutant
PMID:15915339	PBO:0093580	more sensitive than either single mutant
PMID:15915339	PBO:0093587	more sensitive than either single mutant
PMID:15920625	GO:0036374	(comment: Proxy assay for hydrolase function used and IMP evidence for catalytic activity)
PMID:15925945	PBO:0096148	(comment: assayed using AlF4- to mimic GTP-bound Gpa2)
PMID:15933715	PBO:0022666	In early anaphase, Etd1p-GFP became concentrated in the medial region of the cell cortex as a broad band (Figure 2A, cell 2)
PMID:15933715	PBO:0107081	In early anaphase, Etd1p-GFP became concentrated in the medial region of the cell cortex as a broad band (Figure 2A, cell 2)
PMID:15933715	PBO:0107082	We therefore analysed the localisation of Etd1p-GFP in cdc8-110 mutant cells and found that, at the restrictive temperature of 361C, Etd1p never formed a ring (Figure 3B upper panels).
PMID:15933715	PBO:0107082	We therefore analysed the localisation of Etd1p-GFP in cdc8-110 mutant cells and found that, at the restrictive temperature of 361C, Etd1p never formed a ring (Figure 3B upper panels).
PMID:15933715	PBO:0109989	Etd1p-GFP, demonstrating that Etd1p interacts physically with Cdc15p. Similarly, Cdc15p was detected in anti-GFP immune complexes (data not shown). Thus, Etd1p may localise to the actomyosin ring by association with Cdc15p. (comment: the anchor is using 2022 knowledge)
PMID:15933715	FYPO:0003838	However, in etd1-1 mutant cells, the medial ring marked with Cdc15p-GFP seems to fail constriction. To bette
PMID:15933715	PBO:0107085	Etd1p-GFP failed to localise to the medial ring at the restrictive temperature. Instead, these mutant cells accumulated Etd1-GFP in a broad band at the plasma membrane overlying the site of cytokinesis (Figure 6A, upper panel
PMID:15933715	PBO:0107086	(comment: missing annotation, we dont have that cdc7 is on old SPB in metaphase) Cdc7p-GFP appeared at both SPBs at the initiation of mitosis and only at one SPB as cells progressed through anaphase until the completion of cell division.
PMID:15933715	GO:0031028	suggesting that Etd1p is somehow necessary to maintain Spg1p activity during anaphase until the completion of cytokinesis
PMID:15933715	MOD:01148	These results indicate that Etd1p is polyubiquitinated and degraded through the ubiquitin-dependent 26S-proteasome pathway.
PMID:15933715	FYPO:0001493	(Figure 1A and B)
PMID:15933715	FYPO:0000842	(Figure 1A and B)
PMID:15933715	FYPO:0002816	Spores deleted for etd1 (etd1D) germinated and accumulated multiple nuclei without septation, an identical phenotype to that of etd1-1 mutant cells under restrictive conditions (Figure 1C).
PMID:15933715	FYPO:0002024	Under derepressed conditions ( thiamine), Etd1p overproduction generated elongated and multinucleate cells in both etd1-1 mutant and wild-type backgrounds (Figure 1D and data not shown). Thus, the phenotypic defect caused by an excess of Etd1p was identical to that produced by a deficiency of this protein, suggesting that Etd1p functions in a stoichiometric protein complex.
PMID:15933715	PBO:0018345	In interphase cells, Etd1p-GFP was located at the cell cortex and was more concentrated at the cell tips (Figure 2A, cell 1).
PMID:15933715	PBO:0022665	In early anaphase, Etd1p-GFP became concentrated in the medial region of the cell cortex as a broad band (Figure 2A, cell 2)
PMID:15936270	PBO:0106644	highly bent or branched morphology (Figure 2a) (penetrance from Figure 6B)
PMID:15936270	PBO:0106644	highly bent or branched morphology (Figure 2a) (penetrance from Figure 6B)
PMID:15936270	PBO:0037676	(penetrance from 6B) highly bent or branched morphology (Figure 2a)
PMID:15936270	PBO:0106649	We also found that, even under the optimal growth condition, the Δspc1 mutation exacerbates the morphology defects of the Δtea1 mutant; the Δtea1 Δspc1 double mutant grown at 30oC in rich YES medium contain large fractions of significantly bent and branched cells (Figure 6D).
PMID:15936270	PBO:0106648	We also found that, even under the optimal growth condition, the Δspc1 mutation exacerbates the morphology defects of the Δtea1 mutant; the Δtea1 Δspc1 double mutant grown at 30oC in rich YES medium contain large fractions of significantly bent and branched cells (Figure 6D).
PMID:15936270	FYPO:0007379	Cell polarity defects with bent and branched morphology were observed after shifting the Δspc1 mutant from 25oC to 36oC (Figure 6C).
PMID:15936270	PBO:0106644	(penetrance from 6B) nWe found that high osmolarity stress by 0.6 M KCl also promotes appearance of T-shaped cells in the Δtea1 strain, to the levels comparable to the Δwsh3 mutant (Figure 6B).
PMID:15936270	PBO:0106647	Δwsh3 cells, the cell-end localization of Pom1 was lost and Pom1-GFP often accumulated in vesicle-like structures in the cytoplasm (Figure 5D)
PMID:15936270	PBO:0106646	In contrast, most of Δwsh3 cells showed highly concentrated Tea1-GFP signals at one end, while the other end contained significantly less Tea1-GFP dots (Figure 5A, right panel)
PMID:15936270	PBO:0097149	The specific localization of Wsh3-GFP was lost in the Δtea1 mutant and the Wsh3-GFP signal was diffused throughout the cytoplasm (Figure 4A)
PMID:15936270	PBO:0106645	Wsh3-GFP was abrogated by a mutation in β- tubulin, nda3-KM311 [39] even at its permissive temperature, 30oC (Figure 3B, left).
PMID:15936270	FYPO:0001019	Actin patches, which are localized to the growing tips of fission yeast cells [38], were detected mostly in one tip of the Δwsh3 cell (Figure 2C).
PMID:15936270	FYPO:0007380	(Figure 2B)
PMID:15936270	FYPO:0007398	DNS
PMID:15936270	FYPO:0001018	2c Δwsh3 cells were found to grow exclusively in a monopolar fashion.
PMID:15936270	FYPO:0001357	DNS
PMID:15936270	FYPO:0002104	On the other hand, oxidative stress by hydrogen peroxide, which also induces Spc1 activation [34], did not significantly affect Δwsh3 cells (data not shown).
PMID:15937127	PBO:0100663	(Figure 4D)
PMID:15937127	FYPO:0001355	(Fig. 3)
PMID:15937127	PBO:0107946	(Fig. 3 B-2) (comment: 1.1% WT)
PMID:15937127	PBO:0107947	(Fig. 3 B-2) (comment: never seen in WT)
PMID:15937127	FYPO:0003165	(Fig. 3C)
PMID:15937127	FYPO:0006338	(comment: DNA at the tips, telophase delay)
PMID:15937127	GO:0005634	(Figure 3F-3)
PMID:15937127	GO:0034399	(Figure 3F-3)
PMID:15937127	GO:0005634	(Figure 3F-3)
PMID:15937127	GO:0034399	(Figure 3F-3)
PMID:15937127	PBO:0107949	(Figure 4D)
PMID:15937127	PBO:0100894	(Figure 4D)
PMID:15937127	PBO:0107140	(Figure 4D)
PMID:15937127	FYPO:0002060	(Fig. 3)
PMID:15937127	PBO:0107944	(Figure 2)
PMID:15937127	PBO:0107950	(Figure 5B)
PMID:15937127	PBO:0107950	(Figure 5B)
PMID:15937127	PBO:0107944	(Fig. 2)
PMID:15937127	PBO:0107945	(Fig. 2)
PMID:15937127	GO:0006606	(Fig. 2)
PMID:15937127	GO:0006606	(Fig. 2)
PMID:15941470	FYPO:0002060	(comment: Tev protease present; Cdc23 truncated)
PMID:15941470	FYPO:0001430	(comment: Tev protease present; Cdc23 truncated; N starvation/recovery synchronizes cells)
PMID:15941470	FYPO:0000611	(comment: Tev protease present; Cdc23 truncated; cells not synchronized)
PMID:15941470	PBO:0101304	(comment: Tev protease present; Cdc23 truncated; Cdc23 C-terminal fragment not retained in nucleus)
PMID:15941470	PBO:0101305	(comment: Tev protease present; Cdc23 truncated; Cdc23 C-terminal fragment not retained in nucleus)
PMID:15941470	FYPO:0002061	(comment: Tev protease present; Cdc23 truncated)
PMID:15957215	GO:0006265	(comment: from the catenated plasmid experiment and failure to separate sisters)
PMID:15992541	PBO:0105630	(comment: thiamine absent; expression level lower than with endogenous promoter but higher than when repressed)
PMID:15992541	PBO:0105631	(comment: CHECK promoter repressed)
PMID:16055437	PBO:0109312	(Figure 1a)
PMID:16079916	FYPO:0007632	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0007631	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0005309	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0005310	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0005310	(comment: protein-coding genes and intergenic regions)
PMID:16079916	GO:0031509	Sir2 and Clr3 act cooperatively upon histone H3 at K9/K14 throughout the genome, including all the silent regions (rDNA, centromeres, mat2/3 and telomeres).
PMID:16079916	FYPO:0007631	(comment: assayed in intergenic regions)
PMID:16079916	FYPO:0007632	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0007631	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0005309	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0007632	(comment: assayed in intergenic regions)
PMID:16079916	FYPO:0005309	(comment: assayed in intergenic regions)
PMID:16079916	FYPO:0005310	(comment: assayed in intergenic regions)
PMID:16079916	FYPO:0000892	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0000892	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0005310	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0000892	(comment: protein-coding genes and intergenic regions)
PMID:16085489	GO:0044878	(comment: clp1 cytoplasmic localization not maintained during cytokinetic stress. cdc7 localization to SPB not maintained during cytokinetic stress)
PMID:16087707	GO:0000147	(comment: also from timing of localization to patches)
PMID:16087707	GO:0071933	(comment: specific Arp2/3 complex subunit(s) not identified; authors use Myo1 tail as representative of whole protein)
PMID:16087707	GO:0030479	(comment: dependent on F-actin, assayed using Latrunculin A)
PMID:16087707	GO:0000147	(comment: also from synthetic lethality with myo1, timing of localization to patches, and vrp1 mutant phenotype)
PMID:16087707	GO:0030479	(comment: dependent on F-actin, assayed using Latrunculin A)
PMID:16087707	GO:0071933	(comment: specific Arp2/3 complex subunit(s) not identified; authors use Myo1 tail as representative of whole protein)
PMID:16087707	GO:0000147	(comment: also from timing of localization to patches)
PMID:16087707	GO:0030479	(dependent on F-actin, assayed using Latrunculin A)
PMID:16087707	GO:0000147	(comment: also from timing of localization to patches)
PMID:16087749	PBO:0111674	The results revealed that histone H3 was the only histone methylated (Fig. 3B).
PMID:16087749	GO:0140673	. No unmodifiedPol II could be detected in these immunoprecipitates, althoughunmodified Pol II could be readily detected in the input extracts. These data demonstrate that SpSet2 is associated withthe elongating form of Pol II in S. pombe.
PMID:16087749	PBO:0111680	As shown in Fig. Fig. 2D,3D, SpSet2 was able to methylate an H3 peptide of residues 27 to 45, but not that of an H3 N-terminal peptide (residues 1 to 20). These data demonstrate that SpSet2 is a robust nucleosome-selective HMT specific for K36 methylation.
PMID:16087749	PBO:0111679	As shown in Fig. Fig. 2D,3D, SpSet2 was able to methylate an H3 peptide of residues 27 to 45, but not that of an H3 N-terminal peptide (residues 1 to 20). These data demonstrate that SpSet2 is a robust nucleosome-selective HMT specific for K36 methylation.
PMID:16087749	PBO:0111678	As shown in Fig. Fig. 2D,3D, SpSet2 was able to methylate an H3 peptide of residues 27 to 45, but not that of an H3 N-terminal peptide (residues 1 to 20). These data demonstrate that SpSet2 is a robust nucleosome-selective HMT specific for K36 methylation.
PMID:16087749	PBO:0111677	The results revealed that histone H3 was the only histone methylated (Fig. 3B).
PMID:16087749	FYPO:0002919	As shown in Fig. 4A, deletion of set2+ resulted in a complete abolishment of K36 methylation (mono-, di-, and trimethylation), but not K4 methylation or H3 K9 acetylation, in bulk histones
PMID:16087749	FYPO:0002060	set2Δ cells grew normally on rich YEA medium, they showed a strong growth defect in synthetic medium (EMM), which is nutrient depleted compared to YEA (Fig. 4B).
PMID:16087749	FYPO:0001355	set2Δ cells grew normally on rich YEA medium, they showed a strong growth defect in synthetic medium (EMM), which is nutrient depleted compared to YEA (Fig. 4B).
PMID:16087749	PBO:0111676	The results revealed that histone H3 was the only histone methylated (Fig. 3B).
PMID:16087749	PBO:0111675	As shown in Fig. Fig. 2D,3D, SpSet2 was able to methylate an H3 peptide of residues 27 to 45, but not that of an H3 N-terminal peptide (residues 1 to 20). These data demonstrate that SpSet2 is a robust nucleosome-selective HMT specific for K36 methylation.
PMID:16096637	PBO:0113771	In sharp contrast, on a cdc7-24 or sid1-239 mutant background, no Pmo25 was detected at the mitotic SPB(s) (Figure 8B and C).
PMID:16096637	PBO:0113771	In sharp contrast, on a cdc7-24 or sid1-239 mutant background, no Pmo25 was detected at the mitotic SPB(s) (Figure 8B and C).
PMID:16096637	PBO:0102313	Pmo25 formed a complex with Nak1 and was required for both the localization and kinase activity of Nak1.
PMID:16096637	PBO:0018346	(comment: both SPBs in early mitosis)
PMID:16111942	FYPO:0000590	S1D
PMID:16111942	FYPO:0004796	Interestingly, however, azygotic asci arising from diploid hrs1D cells did not show an apparent defect in spore formation (Figure S1D
PMID:16111942	PBO:0018718	(Fig. 1A) appeared at the SPB upon conjugation of haploid cells, persisted until the onset of meiosis I, and disappeared thereafter
PMID:16111942	GO:0030989	(comment: various exp, and ectoptic mitotic expression)
PMID:16111942	GO:0032118	(comment: various exp, and ectoptic mitotic expression)
PMID:16120966	GO:0003899	(comment: can incorporate NTPs or dNTPs; changed from primase activity because not tested with unprimed template)
PMID:16120966	GO:0003887	(comment: distributive; substrate preference: small gaps with a 5′-phosphate group)
PMID:16127433	PBO:0098773	(Fig. 2B)
PMID:16127433	PBO:0110865	(Fig. 5D)
PMID:16127433	FYPO:0000468	(Fig. 3C)
PMID:16127433	PBO:0112651	(Fig. 2B)
PMID:16127433	PBO:0112650	(Fig. 2B)
PMID:16127433	PBO:0120525	(Fig. 2B)
PMID:16127433	PBO:0112648	(Fig. 2B)
PMID:16127433	PBO:0112817	(Fig. 4B)
PMID:16127433	PBO:0093561	(Fig. 4A)
PMID:16127433	FYPO:0007334	(Fig. 4A)
PMID:16127433	FYPO:0004745	(Fig. 4B)
PMID:16127433	PBO:0112644	(Fig. 2B)
PMID:16127433	PBO:0094681	(Fig. 2A)
PMID:16127433	FYPO:0007336	(Fig. 2A)
PMID:16127433	PBO:0094283	(Fig. S3)
PMID:16127433	FYPO:0004745	(Fig. 4B)
PMID:16127433	FYPO:0001861	(Fig. 3B)
PMID:16127433	PBO:0112653	(Fig. 4B)
PMID:16127433	PBO:0112653	(Fig. 4B)
PMID:16127433	FYPO:0002331	(Fig. 4B)
PMID:16127433	PBO:0095057	(Fig. 3A)
PMID:16127433	PBO:0094283	(Fig. S3)
PMID:16127433	FYPO:0007334	(Fig. S3)
PMID:16127433	FYPO:0001357	(Fig. S3)
PMID:16127433	FYPO:0003412	(Fig. S3)
PMID:16127433	FYPO:0001357	(Fig. S3)
PMID:16127433	FYPO:0001357	(Fig. S3)
PMID:16127433	PBO:0093560	(Fig. S3)
PMID:16127433	FYPO:0002331	(Fig. 4B)
PMID:16127433	PBO:0120526	(Fig. 5A)
PMID:16127433	PBO:0112655	(Fig. 5A)
PMID:16127433	PBO:0112656	(Fig. 5C)
PMID:16127433	PBO:0112520	(Fig. 5C)
PMID:16138082	FYPO:0008059	From these results, we conclude that the F330A mutation significantly reduces the affinity of the Mud1 UBA domain for K48-linked polyUb chains without significantly affecting monoUb binding.
PMID:16138082	FYPO:0008060	From these results, we conclude that the F330A mutation significantly reduces the affinity of the Mud1 UBA domain for K48-linked polyUb chains without significantly affecting monoUb binding.
PMID:16141239	FYPO:0000422	(Fig. 5A,B)
PMID:16141239	FYPO:0000422	(Fig. 5A,B)
PMID:16141239	FYPO:0000426	(Fig. 5A,B)
PMID:16141239	FYPO:0000034	(comment: endocytosis restricted to cell end)
PMID:16141239	FYPO:0006341	(comment: endocytosis restricted to cell end)
PMID:16141239	FYPO:0006341	(comment: endocytosis restricted to cell end)
PMID:16141239	FYPO:0006341	(comment: endocytosis restricted to cell end)
PMID:16157682	PBO:0095653	(Fig. 7)
PMID:16157682	FYPO:0005063	(Fig. 8C)
PMID:16157682	FYPO:0005063	(Fig. 8C)
PMID:16157682	FYPO:0002336	(Fig. 7)
PMID:16157682	PBO:0098583	(Fig. 7)
PMID:16157682	PBO:0098583	(Fig. 7)
PMID:16157682	PBO:0098583	(Fig. 7)
PMID:16157682	FYPO:0005063	(Fig. 8C)
PMID:16157682	FYPO:0006112	(Fig. 8B)
PMID:16157682	PBO:0112644	(Fig. 8B)
PMID:16157682	PBO:0094681	(Fig. 7)
PMID:16157682	PBO:0112644	(Fig. 8B)
PMID:16157682	FYPO:0007336	(Fig. 2C)
PMID:16157682	PBO:0103456	Table 2 and Fig. 4
PMID:16157682	PBO:0103456	Table 2 and Fig. 4
PMID:16157682	PBO:0112643	(Fig. 5)
PMID:16157682	PBO:0094681	(Fig. 7)
PMID:16157682	PBO:0112643	(Fig. 5)
PMID:16157682	PBO:0095651	(Fig. 7)
PMID:16157682	PBO:0097950	(Fig. 2B)
PMID:16157682	PBO:0097950	(Fig. 2B)
PMID:16157682	PBO:0094681	(Fig. 7)
PMID:16157682	FYPO:0007336	(Fig. 2C)
PMID:16157682	FYPO:0000468	(Fig. 1C)
PMID:16157682	FYPO:0000468	(Fig. 1C)
PMID:16157682	PBO:0098583	(Fig. 2A)
PMID:16157682	PBO:0098583	(Fig. 2A)
PMID:16169489	FYPO:0000581	(27% of spores produce viable colonies)
PMID:16169489	FYPO:0002059	(comment: knocked out in diploid. Can't tell if it vegetative or spore?)
PMID:16169489	FYPO:0002059	(comment: knocked out in diploid. Can't tell if it vegetative or spore?)
PMID:1617727	GO:0045292	(comment: CHECK splicing of artificial construct with wt or mutated splice sites assayed in mutants)
PMID:16199877	FYPO:0000268	DNS
PMID:16199877	FYPO:0002061	(Fig. 3A)
PMID:16199877	FYPO:0000229	(Fig. 3B)
PMID:16199877	FYPO:0000266	DNS
PMID:16199877	FYPO:0000091	DNS
PMID:16199877	FYPO:0001234	(Fig. 1D)
PMID:16199877	PBO:0106353	(Fig. 1B)
PMID:16199877	FYPO:0000229	DNS
PMID:16199877	PBO:0106353	(Fig. 1E)
PMID:16199877	FYPO:0001234	(Fig. 1D)
PMID:16199877	FYPO:0002061	(Fig. 1A)
PMID:16199877	FYPO:0001490	(Fig. 3B)
PMID:16199877	FYPO:0001494	(Fig. 3B)
PMID:16199877	PBO:0023853	(Fig. 3C)
PMID:16199877	PBO:0022134	(Fig. 3C)
PMID:16199877	FYPO:0008164	(Fig. 3C)
PMID:16199877	PBO:0106355	(Fig. 3C)
PMID:16199877	FYPO:0000316	(Fig. 4)
PMID:16199877	PBO:0106356	(Figure 4B)
PMID:16199877	FYPO:0000229	(Figure 4B)
PMID:16199877	FYPO:0000228	(Figure 4B)
PMID:16199877	FYPO:0000284	(Figure 4B)
PMID:16199877	PBO:0022134	(Fig. 3C)
PMID:16199877	PBO:0023853	(Fig. 3C)
PMID:16199877	PBO:0112051	(Fig. 5D,E)
PMID:16199877	FYPO:0000316	Supp: S1A
PMID:16199877	FYPO:0000141	Supp: S1B
PMID:16199877	PBO:0106358	(Fig. S1C)
PMID:16199877	PBO:0106359	(Fig. S1C)
PMID:16246721	FYPO:0007633	deletion of clr3 resulted in an increase in acetylation at H3K14 (H3K14ac) (Figure 6A), a mark of active chromatin that is absent at heterochromatic loci.
PMID:16246721	FYPO:0007891	ChIP analysis revealed that the Clr3 mutant protein was mainly restricted to the nucleation site adjacent to the mat3 locus and the spreading of Clr3 across the mat2/3 region was severely affected (Figure 2A).
PMID:16246721	GO:0030466	(comment: [NUCLEATION])
PMID:16246721	GO:0030466	(comment: [NUCLEATION] Same pathway as clr3)
PMID:16246721	PBO:0111115	Remarkably, loss of Swi6 and Chp2 but not Chp1 completely abolished the localization of Clr3 at Kint2::ura4+ (Figure 1)
PMID:16246721	PBO:0111016	We next explored whether loss of Clr3 affects Swi6 binding at the mat locus. Deletion of clr3 resulted in severely reduced Swi6 levels at Kint2::ura4+ even though Swi6 expression was not affected (Figure 5C; Figure S3).
PMID:16246721	FYPO:0005845	.....Interestingly, identical modification patterns were also observed in a swi6 mutant, consistent with Swi6 involvement in Clr3 spreading (Figure 5A).
PMID:16246721	FYPO:0007891	In the absence of Swi6, Clr3 localization was confined to a small region near the mat3 locus (Figure 2A), which is distinct from the cenH element responsible for RNAi-mediated targeting of heterochromatin to this region.
PMID:16246721	FYPO:0003097	Remarkably, whereas clr3D or dcr1D single mutant strains still maintained H3K9 methylation, H3K9me at centromeric repeats was almost completely abolished in clr3Ddcr1D double mutant cells (Figure 4C).
PMID:16246721	GO:0030466	(comment: [SPREADING] ) Subsequently, Clr3 spreads across the entire mat2/3 interval that is dependent upon its own HDAC activity, Swi6 and Sir2 proteins, and possibly other factors, such as Chp2, involved in heterochromatin assembly.
PMID:16246721	PBO:0109217	Surprisingly, except for a small but reproducible enrichment of Clr3 at the nucleation site, Clr3 was virtually absent from the entire mat2/3 region in a sir2D strain (Figure 2A).
PMID:16246721	PBO:0111118	Similar changes were observed in the swi6 mutant; however, the effect on H3S10ph was weaker than in the clr3 mutant (Figure 6A).
PMID:16246721	FYPO:0008153	Whereas H3K9me levels at Kint2:: ura4+ were not affected in clr3D, dcr1D, or atf1D single mutants compared to wild-type, H3K9me was completely abolished in a clr3D dcr1D double mutant strain (Figure 4A).
PMID:16246721	GO:0030466	(comment: [SPREADING] ) Subsequently, Clr3 spreads across the entire mat2/3 interval that is dependent upon its own HDAC activity, Swi6 and Sir2 proteins, and possibly other factors, such as Chp2, involved in heterochromatin assembly.
PMID:16246721	GO:0030466	(comment: [SPREADING]) Subsequently, Clr3 spreads across the entire mat2/3 interval that is dependent upon its own HDAC activity, Swi6 and Sir2 proteins, and possibly other factors, such as Chp2, involved in heterochromatin assembly.
PMID:16246721	GO:0031934	Our results revealed that Clr3 is indeed enriched throughout the 20 kb heterochromatic domain surrounded by the IR-R and IR-L boundary elements but is absent at the surrounding euchromatic regions (Figure 2A).
PMID:16246721	PBO:0111117	Remarkably, loss of Swi6 and Chp2 but not Chp1 completely abolished the localization of Clr3 at Kint2::ura4+ (Figure 1)
PMID:16246721	FYPO:0008158	Furthermore, the levels of H3S10 phosphorylation (H3S10ph), another modification mark associated with active chromatin as well as mitotic chromosomes (Nowak and Corces, 2004), were also increased at the mat locus (Figure 6A).
PMID:16246721	PBO:0111115	Remarkably, loss of Swi6 and Chp2 but not Chp1 completely abolished the localization of Clr3 at Kint2::ura4+ (Figure 1)
PMID:16246721	FYPO:0008159	Our analyses revealed that a temperature-sensitive mutation in the survivin homolog Cut17/ Bir1 (cut17-275), which is known to bind centromeric repeats and is required for proper localization of fission yeast aurora kinase Ark1 (Morishita et al., 2001), almost completely abolished H3S10ph at the mat locus in clr3D cells (Figure 6C).
PMID:16246721	GO:0031508	We show that Cir3, a fission yeast homolog of mammalian class |I HDACs, acts in a distinct pathway parallel to RNAi-directed heterochromatin nucleation to recruit Cl4 and mediate H3K9 methylation at the silent mating-type region and centromeres.
PMID:16246721	FYPO:0008157	mutant cells are defective in histone deacetylation and silencing at the mat2/3 locus (see Figure S1
PMID:16246721	FYPO:0005845	..... However, in clr3D cells, H3K9me3 was significantly reduced, while there was a substantial increase in H3K9me1. Furthermore, H3K9me2 levels were slightly elevated (Figure 5A).
PMID:16246721	PBO:0111115	(comment: [ vw specifically to REIII/ CAS, nucleation site]) In double mutant cells lacking Pcr1 and Swi6, the localization of Clr3 was almost completely abolished from REIII (Figure 3).
PMID:16246721	GO:0030466	(comment: [NUCLEATION/SPREADING]) Subsequently, Clr3 spreads across the entire mat2/3 interval that is dependent upon its own HDAC activity, Swi6 and Sir2 proteins, and possibly other factors, such as Chp2, involved in heterochromatin assembly. These results suggest that Clr3 operates in a pathway parallel to RNAi to nucleate heterochromatin at the mat locus.
PMID:16246721	PBO:0111116	These data, together with results showing defects in Swi6 localization at the mat locus in clr3-735 cells (see below; Figure S2)
PMID:16246721	PBO:0111663	At the mat locus, Clr3 is recruited at a specific site through a mechanism involving ATF/CREB family proteins
PMID:16246721	PBO:0111115	Remarkably, loss of Swi6 and Chp2 but not Chp1 completely abolished the localization of Clr3 at Kint2::ura4+ (Figure 1)
PMID:16251348	GO:0006364	(Fig. 3B)
PMID:16251348	GO:0005730	(Fig. 2c)
PMID:16252005	PBO:0093613	(comment: same as cdt2delta alone)
PMID:16252005	GO:0006511	(comment: CHECK -regulation - can also infer from GO:0030674)
PMID:16252005	PBO:0093615	(comment: same as csn1delta alone)
PMID:16252005	PBO:0093618	(comment: same as cdt2delta alone)
PMID:16252005	PBO:0093618	(comment: same as ddb1delta alone)
PMID:16252005	PBO:0093613	(comment: same as ddb1delta alone)
PMID:16252005	PBO:0093618	(comment: same as pcu4delta alone)
PMID:16252005	PBO:0093613	(comment: same as pcu4delta alone_
PMID:16262791	PBO:0108887	detectable in mutants that increase bound GTP:GDP ratio, implying that protein-protein interaction is GTP-dependent
PMID:16272747	FYPO:0001914	In wild type cells, most haploid nuclei produced by meiotic second divisions were encapsulated by the FSM (Fig. 4A). In sec9-10 mutant cells, FSMs initiated normally at both poles of the meiosis II spindles (Fig. 4A), but extension of the FSMs was soon blocked, resulting in anucleated small prespores (Fig. 4B). These results indicated that the FSM initiated normally, but its subsequent development was abnormal.
PMID:16272747	FYPO:0002061	Therefore, sec9+ is essential for vegetative cell growth and spore germination.
PMID:16272747	PBO:0110453	The level of sec9 mRNA began to increase about 6 hr after induction and peaked at about 9 hr, when cells were in early meiosis II (Fig. 2A, 2B).
PMID:16272747	FYPO:0000622	In marked contrast, sec9-10 cells exhibited a rather uniform arrest morphology at the restrictive temperature (Fig. 3C). At 12 hr after the shift to 34°C, approximately 43% of the sec9-10 cells had a single septum, and 4% exhibited multiple septa (Table II).
PMID:16272747	PBO:0104431	In marked contrast, sec9-10 cells exhibited a rather uniform arrest morphology at the restrictive temperature (Fig. 3C). At 12 hr after the shift to 34°C, approximately 43% of the sec9-10 cells had a single septum, and 4% exhibited multiple septa (Table II).
PMID:16272747	FYPO:0002061	In addition to causing a defect in ascospore formation, the sec9-10 mutation compromised vegetative growth. As shown in Fig. 3B, the sec9-10 mutant grew well at 25°C but was unable to form colonies at 37°C.
PMID:16272747	PBO:0112761	As shown in Fig. 2A, accumulation of sec9 mRNA was completely abolished in the mei4Δ mutant. Furthermore, ectopic overexpression of mei4+ was found to induce sec9+ mRNA in vegetative cells (Fig. 2C). sec9+ has a consensus recognition sequence for Mei4, GTAAAYA (Horie et al., 1998) in the 5' upstream region. We conclude that transcription of sec9+ during meiosis is strictly regulated by Mei4.
PMID:16272747	PBO:0110455	As shown in Fig. 2A, accumulation of sec9 mRNA was completely abolished in the mei4Δ mutant. Furthermore, ectopic overexpression of mei4+ was found to induce sec9+ mRNA in vegetative cells (Fig. 2C). sec9+ has a consensus recognition sequence for Mei4, GTAAAYA (Horie et al., 1998) in the 5' upstream region. We conclude that transcription of sec9+ during meiosis is strictly regulated by Mei4.
PMID:16272747	FYPO:0001234	Therefore, sec9+ is essential for vegetative cell growth and spore germination.
PMID:16272747	FYPO:0001234	Therefore, sec9+ is essential for vegetative cell growth and spore germination.
PMID:16291723	PBO:0096397	To determine whether Rgf3p production was controlled by Ace2p, we examined whether Rgf3p levels were altered in cells lacking or overproducing Ace2p. Overproduction of Ace2p led to increased Rgf3p levels whereas Rgf3p was less abundant in cells lacking Ace2p (Fig. 7B
PMID:16291723	FYPO:0001367	(Fig. 6)
PMID:16291723	FYPO:0002060	(comment: rgf3+ is essential)
PMID:16291723	FYPO:0002061	(comment: rgf3+ is essential)
PMID:16291723	FYPO:0002061	(comment: CHECK `SYNTHETIC LETHAL)
PMID:16291723	PBO:0096394	(Figure 5C) Interestingly, overexpression of gpt10+ (Fig. 5G), but not rho1+ (data not shown) restored the localization of Rgf3 in lad1-1 cells at 36°C.
PMID:16291723	PBO:0096393	(Figure 5C)
PMID:16291723	PBO:0096392	(Figure 5C)
PMID:16291723	GO:0051286	Rgf1p-GFP was also detected at cell ends (Fig. 4B).
PMID:16291723	GO:0031097	.By contrast, Rgf3p-GFP was not detected at cell ends, only at the medial region of the cell (Fig. 4D). Furthermore, Rgf3p rings constricted (Fig. 4D, inset). These differences in pattern are illustrated in Fig. 4E
PMID:16291723	GO:0000935	Both proteins localized to the division site(Fig. 4B,D). Rgf1p-GFP formed rings (Fig. 4B) late in mitosis as only cells containing segregated DNA masses contained them (data not shown and Fig. 7A)
PMID:16291723	GO:0016192	Consistent with a role in vesicular trafficking, gyp10 showed a strong negative genetic interaction with cells lacking the exocyst subunit, Exo70p (Wang et al., 2002) (Fig. 3C).
PMID:16291723	PBO:0096391	(Fig. 3C)
PMID:16291723	PBO:0096395	asked whether Rho1p was able to localize correctly to the medial region of the cell in the lad1-1 strain that we had shown lacks medially placed Rgf3p (Fig. 5C). We found that it did (Fig. 6B).
PMID:16291723	PBO:0096396	Ace2p, we examined whether Rgf3p levels were altered in cells lacking or overproducing Ace2p. Overproduction of Ace2p led to increased Rgf3p levels whereas Rgf3p was less abundant in cells lacking Ace2p (Fig. 7B). However, Rgf3p-Myc13 was clearly detectable in the absence of Ace2p suggesting that other factors cooperate with Ace2p to regulate rgf3+ expression.
PMID:16291723	FYPO:0000132	with lysis (these are not chained cells) (Fig. 2C).....cells septum degradation appeared to initiate at a single position around the cell circumference and the entire cell wall disappeared from this area
PMID:16291723	GO:0005783	(Fig. 3B). Gyp10 localized to structures reminiscent of the endoplasmic reticulum (Broughton et al., 1997) when expressed from the low strength nmt81 promoter
PMID:16291723	PBO:0096398	To determine whether Rgf3p production was controlled by Ace2p, we examined whether Rgf3p levels were altered in cells lacking or overproducing Ace2p. Overproduction of Ace2p led to increased Rgf3p levels whereas Rgf3p was less abundant in cells lacking Ace2p (Fig. 7B
PMID:16291723	GO:0140279	Rgf3p appears necessary to stimulate Rho1p-mediated activation of a glucan synthase crucial after septation for proper new cell-end formation.
PMID:16291723	FYPO:0002060	(Fig. 3C)
PMID:16291723	FYPO:0001234	(Fig. 3C).
PMID:16291723	FYPO:0003369	(comment: CONDITION 50 mM)
PMID:16291723	PBO:0020891	(Fig. 3C).
PMID:16291723	FYPO:0002061	(Fig. 3C)
PMID:16291723	FYPO:0002200	(Fig. 3C)
PMID:16291723	FYPO:0001234	(Fig. 1A)
PMID:16291723	PBO:0096390	(Fig. 1A) All cells lysed while undergoing division and the daughter cells remained attached to one another.
PMID:16291723	FYPO:0001366	(Fig. 1A) All cells lysed while undergoing division and the daughter cells remained attached to one another.
PMID:16317005	PBO:0101093	(comment: CHECK activated_by CHEBI:15422 | inhibited_by CHEBI:16284)
PMID:16317005	PBO:0101093	(comment: CHECK activated_by CHEBI:15422 | inhibited_by CHEBI:16284)
PMID:16317047	PBO:0113822	(Fig. 2B)
PMID:16317047	FYPO:0005115	(Fig. 2A)
PMID:16317047	PBO:0095096	(Fig. 3C)
PMID:16317047	PBO:0033269	(Fig. 3C)
PMID:16317047	PBO:0033269	(Fig. 3C)
PMID:16317047	PBO:0113820	(Fig. 1G)
PMID:16317047	PBO:0113821	(Fig. 1F)
PMID:16317047	PBO:0113821	(Fig. 1E)
PMID:16317047	PBO:0095096	(Fig. 3C)
PMID:16317047	PBO:0113821	(Fig. 1D)
PMID:16317047	PBO:0113820	(Fig. 1B)
PMID:16317047	PBO:0113820	(Fig. 1G)
PMID:16317047	PBO:0113833	(Fig. 5C)
PMID:16317047	PBO:0113832	(Fig. 5C)
PMID:16317047	MOD:01148	(Fig. 4F)
PMID:16317047	MOD:00696	(Fig. 4E)
PMID:16317047	PBO:0113831	(Fig. 4C)
PMID:16317047	PBO:0113830	(Fig. 4B)
PMID:16317047	PBO:0092393	Ace2p-Myc13 was periodically produced through the cell cycle (Fig. 4A). It began to accumulate during anaphase as determined by the coincidence of binucleate formation, and it peaked in abundance concomitantly with the peak of septation.
PMID:16317047	PBO:0096598	(Fig. 3C)
PMID:16317047	FYPO:0006399	(Fig. 3D)
PMID:16317047	PBO:0113829	(Fig. 3B, 3C)
PMID:16317047	PBO:0113828	(Fig. 3B, 3C)
PMID:16317047	PBO:0113828	(Fig. 3B, 3C)
PMID:16317047	PBO:0095096	(Fig. 3C)
PMID:16317047	PBO:0095096	(Fig. 3C)
PMID:16317047	PBO:0113825	(Fig. 3A)
PMID:16317047	PBO:0113825	(Fig. 3A)
PMID:16317047	PBO:0113826	(Fig. 3B, 3C)
PMID:16317047	PBO:0113827	(Fig. 3B, 3C)
PMID:16317047	PBO:0032847	(Fig. 3C)
PMID:16317047	PBO:0095096	(Fig. 3C)
PMID:16317047	PBO:0113825	(Fig. 3A)
PMID:16317047	PBO:0113825	(Fig. 3A)
PMID:16317047	PBO:0113824	(Fig. 2C)
PMID:16317047	FYPO:0006399	(Fig. 2D)
PMID:16317047	PBO:0113823	(Fig. 2B)
PMID:16325576	PBO:0109783	(Fig. S1)
PMID:16325576	FYPO:0004212	(comment: VW, I am not sure that I captured this correctly?) A ChIP assay revealed that the association of Rec8(TEV) with chromatin is partly, but not entirely, impaired only at the centromeric central core region when cen-TEV protease is coexpressed (Figure 7C), suggesting that Rec8(TEV) is cleaved in a region-specific manner. We reasoned that, even if central core Rec8 is cleaved by cen-TEV protease, newly produced or free Rec8 complexes can be reloaded, resulting in the observed association of low levels of Rec8 at the central core. Nevertheless, such ‘‘turnover’’ of cohesin complexes would eventually abolish cohesion because newly associated cohesins do not reestablish cohesion after DNA replication.
PMID:16325576	PBO:0096958	This hypothesis makes the key prediction that the increase of Rec8 at the centromeric central core would depend on DNA replication. To test this possibility, we blocked DNA replication by adding HU to the synchronized meiotic culture and examined by ChIP the localization pattern of Rec8 (Figure 6C). Levels of central core-associated Rec8 were the same before (+HU) or after DNA replication (-HU) in wild-type cells. Remarkably, HU treatment abolished the increase of central core Rec8 in moa1D cells, and the pattern became similar to that in moa1+ cells (Figure 6C, +HU).
PMID:16325576	PBO:0096957	Surprisingly, moa1D cells displayed slightly stronger signals of Rec8-GFP at the cluster of centromeres (Figure 6A, GFP dots in the nucleus). Subsequent ChIP assays revealed that the association of Rec8 to chromatin increased nearly 2-fold in moa1D cells, particularly at the centromeric central core region (Figure 6B).
PMID:16325576	PBO:0096955	(Figure 5C) However, the ChIP assay demonstrated intact localization of Moa1 in rec8D meiotic cells (Figure 5C). Instead, we discovered that Moa1 localization was abolished in cells lacking CENP-C (Cnp3) (Figure 5C)
PMID:16325576	PBO:0096955	(Figure 5C) However, the ChIP assay demonstrated intact localization of Moa1 in rec8D meiotic cells (Figure 5C). Instead, we discovered that Moa1 localization was abolished in cells lacking CENP-C (Cnp3) (Figure 5C)
PMID:16325576	GO:0005515	(Fig. 5A)
PMID:16325576	PBO:0092319	(comment: induced)
PMID:16325576	PBO:0096952	Whereas monopolar attachment is obviously impaired in moa1D rec12D meiosis I, the protection of centromere cohesion also appears defective since almost all sister chromatids eventually separate.
PMID:16325576	FYPO:0004393	Whereas monopolar attachment is obviously impaired in moa1D rec12D meiosis I, the protection of centromere cohesion also appears defective since almost all sister chromatids eventually separate.
PMID:16325576	FYPO:0005648	(Figure 2D) Although deletion of moa1+ thus causes a centromere-specific defect, recombination appears to promote reductional segregation in moa1D cells because the defect in monopolar attachment is lessened in diploid recombination-proficient meiosis compared to haploid meiosis or diploid
PMID:16325576	FYPO:0000488	(Fig. S2)
PMID:16325576	PBO:0109786	(Fig. S1)
PMID:16325576	PBO:0109786	(Fig. S1)
PMID:16325576	PBO:0109786	(Fig. S1)
PMID:16325576	PBO:0109785	(Fig. S1)
PMID:16325576	PBO:0109784	(Fig. S1)
PMID:16325576	PBO:0109782	(Figure 2C)
PMID:16325576	FYPO:0004159	(Figure 2C)
PMID:16325576	PBO:0109782	(Figure 2C, 3b)
PMID:16325576	PBO:0109781	(Figure 2C)
PMID:16325576	PBO:0109676	(Figure 2b)
PMID:16325576	FYPO:0001894	(Figure 2a)
PMID:16325576	FYPO:0001894	(Figure 2a)
PMID:16325576	PBO:0109780	(Figure 1)
PMID:16325576	PBO:0109780	(Figure 1)
PMID:16325576	PBO:0109780	(Figure 1)
PMID:16325576	PBO:0109780	(Figure 1)
PMID:16325576	PBO:0109780	(Figure 1)
PMID:16360688	PBO:0112576	(Figure 3a) Interestingly, no additive effect was seen in the bub11-179 sgo2D double mutant, indicating that Sgo2 and the kinase domain of Bub1 act in the same pathway (Figure 3A).
PMID:16360688	PBO:0112589	However, we found that Bub1K762M was properly localized in metaphase I cells and that the amount of protein at centromeres was close to wild-type levels (Figure S1).
PMID:16360688	PBO:0112582	Interestingly, no additive effect was seen in the bub11-179 sgo2D double mutant, indicating that Sgo2 and the kinase domain of Bub1 act in the same pathway (Figure 3A).
PMID:16360688	PBO:0112588	(Figure 1c) a high frequency of sister-chromatid nondisjunction during MII (Figure 1C), consistent with Sgo1’s being largely nonfunctional in this mutant background.
PMID:16360688	PBO:0112576	(Figure 1c)
PMID:16360688	PBO:0112587	, Sgo1 is seen as nuclear staining with punctate dots of fluorescence along the spindle (Figure 1D and [2, 9]). This localization is abolished in a bub1D background but preserved in the truncated mutants (Figure 1D), although the signal intensity was variable; in bub11-585, Sgo1 staining was as strong as in the wild-type, but it was weaker in bub11-179 and bub11-826 backgrounds. We conclude that the N terminus of Bub1 is sufficient to promote correct Sgo1 localization and function during MI.
PMID:16360688	PBO:0112587	, Sgo1 is seen as nuclear staining with punctate dots of fluorescence along the spindle (Figure 1D and [2, 9]). This localization is abolished in a bub1D background but preserved in the truncated mutants (Figure 1D), although the signal intensity was variable; in bub11-585, Sgo1 staining was as strong as in the wild-type, but it was weaker in bub11-179 and bub11-826 backgrounds. We conclude that the N terminus of Bub1 is sufficient to promote correct Sgo1 localization and function during MI.
PMID:16360688	PBO:0112587	, Sgo1 is seen as nuclear staining with punctate dots of fluorescence along the spindle (Figure 1D and [2, 9]). This localization is abolished in a bub1D background but preserved in the truncated mutants (Figure 1D), although the signal intensity was variable; in bub11-585, Sgo1 staining was as strong as in the wild-type, but it was weaker in bub11-179 and bub11-826 backgrounds. We conclude that the N terminus of Bub1 is sufficient to promote correct Sgo1 localization and function during MI.
PMID:16360688	PBO:0112586	, Sgo1 is seen as nuclear staining with punctate dots of fluorescence along the spindle (Figure 1D and [2, 9]). This localization is abolished in a bub1D background but preserved in the truncated mutants (Figure 1D), although the signal intensity was variable; in bub11-585, Sgo1 staining was as strong as in the wild-type, but it was weaker in bub11-179 and bub11-826 backgrounds. We conclude that the N terminus of Bub1 is sufficient to promote correct Sgo1 localization and function during MI.
PMID:16360688	PBO:0112585	(Figure 1c)
PMID:16360688	PBO:0112584	(Figure 1c)
PMID:16360688	PBO:0112582	(Figure 1c)
PMID:16360688	PBO:0112583	(Figure 1c)
PMID:16360688	PBO:0112576	(Figure 1c)
PMID:16360688	PBO:0112582	(Figure 1c) Interestingly, no additive effect was seen in the bub11-179 sgo2D double mutant, indicating that Sgo2 and the kinase domain of Bub1 act in the same pathway (Figure 3A).
PMID:16360688	PBO:0112581	(Figure 1a)
PMID:16360688	PBO:0112580	(Figure 1a)
PMID:16360688	PBO:0112579	(Figure 1a)
PMID:16360688	PBO:0112578	(Figure 1a)
PMID:16360688	PBO:0112577	(Figure 1a)
PMID:16360688	PBO:0112577	(Figure 1a)
PMID:16360688	FYPO:0006315	As reported previously [13], expression of Rec8RDRD in wild-type cells prevented homolog segregation (no bi-nucleate cells), but homolog segregation was restored to a certain extent by the deletion of rec11 (approximately 40% binucleated cells).
PMID:16360688	PBO:0100757	but homolog segregation was restored to a certain extent by the deletion of rec11 (approximately 40% binucleated cells).
PMID:16360688	PBO:0112586	Similarly, we found that Sgo1 was mislocalized in a different allele (Figure 1D, K762M [6])
PMID:16360688	PBO:0112576	(Figure 1b)
PMID:16394105	FYPO:0002060	(Fig. 5e)
PMID:16394105	FYPO:0002061	table 4
PMID:16394105	FYPO:0002060	table 4
PMID:16394105	FYPO:0002060	table 4
PMID:16394105	FYPO:0002060	table 4
PMID:16394105	PBO:0037149	(Figure 6B, C)
PMID:16394105	PBO:0037150	(Figure 6B, C)
PMID:16394105	FYPO:0001234	(Fig. 7b)
PMID:16394105	FYPO:0001357	(Fig. 7a)
PMID:16394105	FYPO:0001357	(Fig. 7a)
PMID:16394105	PBO:0102084	(Figure 8A, B)
PMID:16394105	PBO:0102085	(Figure 8C)
PMID:16394105	PBO:0102086	(Figure 8D)
PMID:16394105	PBO:0102086	(Figure 8D)
PMID:16394105	PBO:0102086	(Figure 8D)
PMID:16394105	FYPO:0005691	(Figure 9)
PMID:16394105	FYPO:0000903	both the growth and shrinkage rates were decreased down to 33 and 60%, respectively
PMID:16394105	FYPO:0005703	both the growth and shrinkage rates were decreased down to 33 and 60%, respectively
PMID:16394105	FYPO:0005683	(Fig. 4)
PMID:16394105	FYPO:0005684	(Fig. 4)
PMID:16394105	FYPO:0005684	(Fig. 4)
PMID:16394105	FYPO:0005683	(Fig. 4)
PMID:16394105	FYPO:0005706	(Fig. 4)
PMID:16394105	FYPO:0002061	(Fig. 5d)
PMID:16394105	FYPO:0002061	table 4
PMID:16394105	PBO:0102076	(Figure 1B)
PMID:16394105	PBO:0102077	(Figure 1B)
PMID:16394105	FYPO:0002638	(Figure 1B)
PMID:16394105	PBO:0102078	Supplemental data
PMID:16394105	PBO:0102079	(Figure 1B)
PMID:16394105	PBO:0102080	(Figure 1B)
PMID:16394105	FYPO:0000899	(comment: morphology)
PMID:16394105	PBO:0037146	(Fig. 3)
PMID:16394105	PBO:0037147	(Fig. 3)
PMID:16394105	FYPO:0005706	(Fig. 4)
PMID:16407242	PBO:0098225	higher protein level than in absence of HU, in both wild type and mutant
PMID:16407242	PBO:0094176	higher protein level than in absence of HU, in both wild type and mutant
PMID:16421249	FYPO:0003535	(Figure 3B) 55% of cdc10-129 cells displayed bipolar growth, whereas only 4% of cdc10-129 rgf1+ cells were bipolar
PMID:16421249	GO:0140472	(Figure 8A)
PMID:16421249	PBO:0098289	(Figure 8A)
PMID:16421249	PBO:0020227	(Figure 8A)
PMID:16421249	PBO:0018345	(Figure 8A)
PMID:16421249	FYPO:0001357	(Figure 7C)
PMID:16421249	GO:0090334	(comment: positive regulation)
PMID:16421249	FYPO:0002060	DNS
PMID:16421249	FYPO:0001357	(Figure 7A)
PMID:16421249	FYPO:0001357	(Figure 7A)
PMID:16421249	FYPO:0001357	(Figure 7A)
PMID:16421249	FYPO:0001357	(Figure 7A) only a moderate expression of bgs4+ restored growth of an rgf1+ mutant in the presence of the antifungal agent
PMID:16421249	FYPO:0001968	(Figure 6B) GS activity increased during rgf1+ overexpression. This activity was fourfold higher than that observed in the wild-type strain
PMID:16421249	PBO:0099851	(Figure 2B) regardless of the growth temperature 30 -35% of the cells were lysed
PMID:16421249	PBO:0099857	(comment: decreased gtp-bound gtpase, inactive)
PMID:16421249	PBO:0099856	(comment: increased gtp-bound gtpase, active)
PMID:16421249	PBO:0099855	(comment: rescue of multiseptate, swollen)
PMID:16421249	PBO:0094648	rga1+ cells were severely impaired for growth, whereas rgf1+rga1+ exhibited a better growth pattern and resembled rgf1+ cells.
PMID:16421249	PBO:0095634	(Figure 2A The resulting strain, rgf1+, showed a slow growth pattern at 28°C
PMID:16421249	FYPO:0007436	(Figure 4c) Lack of Rga1p produces small colonies and the cells show a swollen, multiseptated or branched shape; a phenotype similar to that seen in cells in which Rho1p is excessively activated
PMID:16421249	FYPO:0000079	(Figure 4A) the Csp hypersensitivity of the rgf1delta mutant was suppressed by rho1delta in .... None of the other genes was able to suppress the hypersensitivity of rgf1+
PMID:16421249	FYPO:0000079	(Figure 4A) the Csp hypersensitivity of the rgf1delta mutant was suppressed by rho1delta in .... None of the other genes was able to suppress the hypersensitivity of rgf1+
PMID:16421249	FYPO:0000079	(Figure 4A) the Csp hypersensitivity of the rgf1delta mutant was suppressed by rho1delta in .... None of the other genes was able to suppress the hypersensitivity of rgf1+
PMID:16421249	FYPO:0000079	(Figure 4A) the Csp hypersensitivity of the rgf1delta mutant was suppressed by rho1delta in .... None of the other genes was able to suppress the hypersensitivity of rgf1+
PMID:16421249	FYPO:0000079	(Figure 4A) the Csp hypersensitivity of the rgf1delta mutant was suppressed by rho1delta in .... None of the other genes was able to suppress the hypersensitivity of rgf1+
PMID:16421249	FYPO:0005152	(Figure 4A) the Csp hypersensitivity of the rgf1delta mutant was suppressed by rho1delta in .... None of the other genes was able to suppress the hypersensitivity of rgf1+
PMID:16421249	GO:0030866	(comment: positive regulation)
PMID:16421249	PBO:0099854	(Figure 2B) regardless of the growth temperature 30 -35% of the cells were lysed
PMID:16421249	PBO:0094648	(Figure 2A The resulting strain, rgf1+, showed a slow growth pattern at 28°C
PMID:16421249	PBO:0099850	(Figure 2A)
PMID:16421249	PBO:0099851	(Figure 2B) regardless of the growth temperature 30 -35% of the cells were lysed
PMID:16421249	PBO:0099851	(Figure 2B) regardless of the growth temperature 30 -35% of the cells were lysed
PMID:16421249	PBO:0099852	(Figure 2B) regardless of the growth temperature 30 -35% of the cells were lysed
PMID:16421249	GO:0090334	(comment: positive regulation)
PMID:16421249	PBO:0099853	this being consistent with the idea that rgf1+ could act in the same pathway as rho1+ (Figure 4A). Figure 5. The amount of active Rho1p increased considerably in the strain overexpressing Rgf1p compared with the wild-type strain. Moreover, only a minor amount of GTP-Rho1p was detected in the strain lacking Rgf1p.
PMID:16421249	FYPO:0001397	(Figure 3A) As shown in Figure 3A, the rgf1 mutants showed a defect in actin organization in that they organized actin patches mostly at one end of the cell only
PMID:16421249	FYPO:0001366	(Figure 3A) (comment: at cell division site)
PMID:16421249	GO:0051523	(comment: positive regulation)
PMID:16428309	FYPO:0002691	(Fig. 1)
PMID:16428309	PBO:0114472	(Fig. 2)
PMID:16428309	PBO:0114472	(Fig. 2)
PMID:16428309	PBO:0093578	(Fig. 2)
PMID:16428309	PBO:0093578	(Fig. 2)
PMID:16428309	PBO:0093576	(Fig. 2)
PMID:16428309	PBO:0114471	(Fig. 2)
PMID:16428309	PBO:0114471	(Fig. 2)
PMID:16428309	PBO:0114467	(Fig. 2)
PMID:16428309	PBO:0114466	(Fig. 2)
PMID:16428309	FYPO:0002690	(Fig. 1)
PMID:16428309	PBO:0114470	(Fig. 1)
PMID:16428309	PBO:0093577	(Fig. 1)
PMID:16428309	PBO:0093578	(Fig. 1)
PMID:16428309	FYPO:0000962	(Fig. 1)
PMID:16428309	PBO:0093577	(Fig. 1)
PMID:16428309	PBO:0114469	(Fig. 1)
PMID:16428309	PBO:0114468	(Fig. 1)
PMID:16428309	FYPO:0002691	(Fig. 1)
PMID:16428309	PBO:0095678	(Fig. 1)
PMID:16428309	FYPO:0002691	(Fig. 1)
PMID:16428309	PBO:0114467	(Fig. 1)
PMID:16428309	PBO:0114466	(Fig. 1)
PMID:16428435	FYPO:0002150	Thus, the carboxyl terminus of Cdk9 [...] is required for cell viability. Table 2
PMID:16428435	PBO:0112186	(Fig. 2D)
PMID:16428435	PBO:0112036	(Fig. 2C and D)
PMID:16428435	FYPO:0004481	(Fig. 4)
PMID:16428435	PBO:0093558	(Fig. 4)
PMID:16428435	PBO:0093558	(Fig. 4)
PMID:16428435	PBO:0093557	(Fig. 4)
PMID:16428435	PBO:0093557	(Fig. 4)
PMID:16428435	PBO:0093561	(Fig. 4)
PMID:16428435	PBO:0093559	(Fig. 4)
PMID:16428435	PBO:0093560	(Fig. 4)
PMID:16428435	PBO:0093560	(Fig. 4)
PMID:16428435	PBO:0093559	(Fig. 4)
PMID:16428435	PBO:0093554	(Fig. 4)
PMID:16428435	FYPO:0005369	(Fig. 4)
PMID:16428435	FYPO:0005369	(Fig. 4)
PMID:16428435	FYPO:0005369	(Fig. 4)
PMID:16428435	FYPO:0002061	Tetrad analysis revealed a 2:2 segregation of viability, and all viable progeny were G418 sensitive, indicating that cdk9 + is essential (data not shown).
PMID:16428435	PBO:0112035	(Fig. 2B)
PMID:16428435	PBO:0120029	(Fig. 2)
PMID:16428435	PBO:0093559	(Fig. 4)
PMID:16428435	PBO:0093561	(Fig. 4)
PMID:16428435	PBO:0093560	(Fig. 4)
PMID:16428435	PBO:0093560	(Fig. 4)
PMID:16428435	PBO:0093560	(Fig. 4)
PMID:16428435	FYPO:0004481	(Fig. 4)
PMID:16428435	PBO:0112035	(Fig. 3B and C)
PMID:16428435	PBO:0112037	(Fig. 3)
PMID:16428435	PBO:0112187	(Fig. 2D)
PMID:16453724	FYPO:0003758	(comment: CHECK ABOLISHED SEPARATION)
PMID:16453724	FYPO:0000608	(comment: with re-replication)
PMID:16453724	FYPO:0003758	(comment: CHECK ABOLISHED SEPARATION)
PMID:16453733	FYPO:0001357	(Table 1)
PMID:16453733	FYPO:0001357	(Table 1)
PMID:16453733	FYPO:0000674	(Table 1)
PMID:16453733	FYPO:0001357	(Table 1)
PMID:16453733	FYPO:0001357	(Table 1)
PMID:16453733	FYPO:0001357	(Table 1)
PMID:16453733	FYPO:0001357	(Table 1)
PMID:16453733	FYPO:0001357	(Table 1)
PMID:16453733	FYPO:0001357	(Table 1)
PMID:16453733	FYPO:0001357	(Table 1)
PMID:16453733	FYPO:0001357	(Table 1)
PMID:16453733	FYPO:0001357	(Table 1)
PMID:16453733	FYPO:0001357	(Table 1)
PMID:16453733	FYPO:0001357	(Table 1)
PMID:16453733	FYPO:0000674	(Table 1)
PMID:16453733	FYPO:0001357	(Table 1)
PMID:16453733	FYPO:0001357	(Table 1)
PMID:16453733	FYPO:0001357	(Table 1)
PMID:16453733	FYPO:0000674	(Table 1)
PMID:16453733	FYPO:0000674	(Table 1)
PMID:16453733	FYPO:0000674	(Table 1)
PMID:16453733	FYPO:0000674	(Table 1)
PMID:1645660	GO:0016791	(comment: CHECK inhibited_by zinc(2+) activated_by magnesium(2+))
PMID:16467379	GO:0031097	(comment: localization dependent on F-actin (assayed using Latrunculin A))
PMID:16481403	PBO:0101741	(Fig. 1)
PMID:16481403	GO:0051415	(comment: emtoc)
PMID:16481403	PBO:0020565	(Figure 5B)
PMID:16481403	FYPO:0006397	(comment: from both ends)
PMID:16481403	GO:0008017	(Fig. 1c)
PMID:16481403	FYPO:0005558	(comment: from both ends)
PMID:16481403	FYPO:0006195	(Fig. 1D) (comment: actually 2 bundles)
PMID:16489217	GO:0010515	(comment: maybe not shown strongly in this paper but I'm trying to get the git genes annotated to this term because pka1 phosphorylates rst2 which excludes rst2 from the nucleus. rst2 when in the nucleus activates ste11 transcription.)
PMID:16537923	PBO:0098521	(comment: genes specified in extensions assayed in low-throughput Northern blots; additional genes assayed in high-throughput microarrays not listed)
PMID:16537923	FYPO:0001357	(comment: CHECK aerobic conditions)
PMID:16537923	PBO:0098522	(comment: genes specified in extensions assayed in low-throughput Northern blots; additional genes assayed in high-throughput microarrays not listed)
PMID:16537923	PBO:0098520	(comment: genes specified in extensions assayed in low-throughput Northern blots; additional genes assayed in high-throughput microarrays not listed)
PMID:16541024	PBO:0097366	Supplementary Fig. S2a
PMID:16541024	GO:0000159	(Fig. 1)
PMID:16541024	GO:0000159	(Fig. 1)
PMID:16541024	FYPO:0003176	Supplementary Fig. S2a
PMID:16541024	FYPO:0003176	Supplementary Fig. S2a
PMID:16541024	PBO:0097016	Supplementary Fig. S2a
PMID:16541024	GO:0000159	(Fig. 2)
PMID:16541024	FYPO:0002219	(Fig. 2a)
PMID:16541024	PBO:0097367	(Fig. 2a)
PMID:16541024	FYPO:0002219	(Fig. 2a)
PMID:16541024	FYPO:0002219	(Fig. 2a)
PMID:16541024	PBO:0112500	(Fig. 2b)
PMID:16541024	PBO:0112500	(Fig. 2b)
PMID:16541024	PBO:0112501	(Fig. 2b)
PMID:16541024	PBO:0112501	(Fig. 2b)
PMID:16541024	PBO:0097370	(Fig. 2b)
PMID:16541024	PBO:0097370	(Fig. 2b)
PMID:16541024	PBO:0097370	(Fig. 2b)
PMID:16541024	PBO:0097371	(Fig. 4)
PMID:16541024	PBO:0097371	(Fig. 4)
PMID:16541024	GO:0000775	(Fig. 4b)
PMID:16541024	GO:0000775	(Fig. 4b)
PMID:16541024	GO:0000775	(Fig. 4b)
PMID:16541024	GO:0000775	(Fig. 4b)
PMID:16541024	PBO:0097372	(Fig. 2b)
PMID:16541024	FYPO:0003176	Supplementary Fig. S2a
PMID:16541024	PBO:0097373	(Fig. 4)
PMID:16541024	PBO:0109333	(comment: this is an inference, but almost certainly true based on the genetics)
PMID:16541024	PBO:0109336	(comment: Notably, we detected only a single combination of PP2A subunits associated with SpSgo1, namely SpPaa1A-SpPar1B′-SpPpa2C)
PMID:16541025	FYPO:0005648	(Supplementary Fig. 7)...both of these mutant cell types showed precocious centromeric dissociation after meiosis I, and random chromosome segregation following meiosis II
PMID:16541025	PBO:0102397	(Fig. 5b) (comment: CHECK however, it colocalizes with Sgo1 at centromeres during meiosis I)
PMID:16541025	PBO:0095117	(comment: dns)
PMID:16541025	PBO:0102398	(Fig. 5b).
PMID:16541025	PBO:0102399	We found that, like sgo1D cells, par1D cells mostly lost centromeric Rec8 localization at this stage (Fig. 5d)
PMID:16541025	PBO:0109338	(Fig. 5a)
PMID:16541025	FYPO:0005648	(Supplementary Fig. 7).
PMID:16541025	FYPO:0003182	(Supplementary Fig. 7)
PMID:16541025	FYPO:0003182	(Supplementary Fig. 7)
PMID:16541025	PBO:0109338	(Fig. 5a)
PMID:1655416	PBO:0033742	(Figure 10C)
PMID:1655416	FYPO:0000333	(comment: transient)
PMID:1655416	FYPO:0000333	(comment: is delayed but the delay is reduced compared to the single mutant)
PMID:1655416	PBO:0033741	(Figure 10C)
PMID:1655416	GO:0005515	(comment: CHECK ADD MODIFIED FORMS)
PMID:1655416	PBO:0033737	(comment: length)
PMID:1657594	PBO:0099549	(Fig. 6)
PMID:1657594	GO:0030552	(Fig. 6)
PMID:16585273	FYPO:0000927	(Fig. 4E)
PMID:16611237	PBO:0095920	(comment: indicates a G2 delay)
PMID:16618806	PBO:0094255	(comment: CHECK residue T11)
PMID:16618806	PBO:0102098	(comment: CHECK has output PR:000037300)
PMID:16618806	PBO:0102097	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	PBO:0102097	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	PBO:0102097	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	PBO:0102097	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	PBO:0102096	abolished dimerization in kinase-dead cds1-D312E
PMID:16618806	PBO:0099533	induced dimerization increases Cds1 autophosphorylation without prior phosphorylation on T11
PMID:16618806	PBO:0102095	(comment: CHECK effect of mutation in substrate Cds1 molecule)
PMID:16618806	PBO:0102094	(comment: CHECK effect of mutation in substrate Cds1 molecule)
PMID:16618806	PBO:0098128	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	PBO:0098128	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	PBO:0098128	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	PBO:0098128	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	PBO:0098128	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	PBO:0098128	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	PBO:0102093	(comment: CHECK effect of mutation in substrate Cds1 molecule)
PMID:16618806	PBO:0094206	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	PBO:0102092	(comment: CHECK residue T11)
PMID:16618806	PBO:0102090	(comment: CHECK residue T11)
PMID:16618806	PBO:0102090	(comment: CHECK residue T11)
PMID:16618806	PBO:0102091	(comment: CHECK residue T11)
PMID:16618806	PBO:0102090	(comment: CHECK residue T11)
PMID:16618806	PBO:0093581	(comment: cells otherwise haploid)
PMID:16618806	PBO:0093581	(comment: cells otherwise haploid)
PMID:16618806	PBO:0093581	(comment: cells otherwise haploid)
PMID:16624923	FYPO:0007168	cortical location/microtubules did not show a lateral interaction with the cell corte/Ninety-two percent of microtubules in num1D cells underwent catastrophe Figure 3.—Nuclear behavior in wild-type and num1D zygotes. Chromosomal DNA in zygotes (JY450 or JV627) was stained with Hoechst 33342 and monitored. The numbers on the left indicate time in minutes. Microtubules were visualized simultaneously by GFP-tagged a-tubulin. Stained DNA is shown in red, and GFP fluorescence in green. Bar, 5 mm. within 2 min of contacting the cell cortex (n 1⁄4 59). In contrast, 80% of microtubules that interacted with the cell cortex laterally in wild-type cells remained at the cell ends for .2 min (n 1⁄4 15).
PMID:16624923	PBO:0105249	(comment: CHECK membrane anchor)
PMID:16682348	PBO:0101859	(comment: CHECK- add background? G1 arrested cells)
PMID:16682348	PBO:0103025	(comment: CHECK add background G1 arrested cells)
PMID:16687577	PBO:0106107	(Fig. 3)
PMID:16687577	PBO:0094433	(Fig. 3)
PMID:16687577	PBO:0106108	(Fig. 4)
PMID:16687577	PBO:0106106	(Fig. 2)
PMID:16687577	PBO:0095196	(Fig. 2)
PMID:16687577	PBO:0095630	(Fig. 1)
PMID:16687577	PBO:0038073	(Fig. 5)
PMID:16687577	PBO:0106110	(Fig. 5)
PMID:16687577	PBO:0095630	(Fig. 1)
PMID:16687577	PBO:0095630	(Fig. 1)
PMID:16687577	PBO:0106109	(Fig. 4)
PMID:16687577	FYPO:0002026	(Fig. 4)
PMID:16687577	PBO:0106111	(Fig. 5) (comment: during ectopic SIN activation)
PMID:16687577	PBO:0106112	(Figure 5, D and E)
PMID:16687577	GO:1903475	(comment: different pathway)
PMID:16687577	PBO:0106113	(Figure 5, D and E)
PMID:16687577	GO:1903475	(comment: different pathway)
PMID:16687577	PBO:0106115	(Figure 7)
PMID:16687577	PBO:0106114	(Figure 6) (comment: asymetric during cytokinesis delay)
PMID:16738311	FYPO:0001355	(comment: CONDITION 32 °C)
PMID:16738311	FYPO:0001355	(comment: CONDITION 32 °C)
PMID:16738311	FYPO:0001355	(comment: CONDITION 32 °C;) very slightly worse than without cid12delta
PMID:16738311	FYPO:0001355	(comment: CONDITION 32 °C)
PMID:16738311	PBO:0093560	(comment: CONDITION 32 °C)
PMID:16738311	FYPO:0002061	(comment: CONDITION 26 °C)
PMID:16738311	FYPO:0002061	(comment: CONDITION 26 °C)
PMID:16738311	FYPO:0001357	(comment: CONDITION 32 °C)
PMID:16738311	FYPO:0002928	(comment: CHECK centromere outer repeat transcripts)
PMID:16738311	PBO:0093560	(comment: CONDITION 32 °C;) same as without cid12delta
PMID:16738311	PBO:0093560	(comment: CONDITION 32 °C)
PMID:16738311	FYPO:0001355	(comment: CONDITION 32 °C;) better than without cid12delta
PMID:16738311	FYPO:0001355	(comment: CONDITION 32 °C)
PMID:16762840	PBO:0097227	However, abundant transcripts corresponding to centromeric repeats and cenH are detectable in RNAi- defective Dago1 cells. We found that the levels of transcripts in Depe1Dago1 double mutant cells were significantly reduced (Figures 5A and 5B), indicating that Epe1 facilitates transcription of the heterochromatic repeats.
PMID:16762840	PBO:0111031	Remarkably, loss of Epe1 resulted in a diminished access of Pol II to cenH in Dclr3 cells, as indicated by substantial reduction in Pol II levels in Depe1 Dclr3 double mutant as compared to Dclr3 single mutant (Figure 5E).
PMID:16762840	PBO:0097227	However, abundant transcripts corresponding to centromeric repeats and cenH are detectable in RNAi- defective Dago1 cells. We found that the levels of transcripts in Depe1Dago1 double mutant cells were significantly reduced (Figures 5A and 5B), indicating that Epe1 facilitates transcription of the heterochromatic repeats.
PMID:16762840	PBO:0111021	Moreover, Epe1 was detected at certain meiotic genes, some of which are coated with heterochromatic markers (Figure 2A; [Cam et al., 2005]).
PMID:16762840	GO:0000792	Localization of Epe1-GFP revealed two to three discrete foci at the nuclear periphery (Figure S1 available in the Supplemental Data with this article online), in a pattern that is similar to those of proteins associated with heterochromatin such as Swi6 (Ekwall et al., 1995).
PMID:16762840	GO:0031934	heterochromatic loci, including centromeres, telomeres, and the mat locus (Figure 2A).
PMID:16762840	GO:0140720	heterochromatic loci, including centromeres, telomeres, and the mat locus (Figure 2A).
PMID:16762840	GO:0005721	heterochromatic loci, including centromeres, telomeres, and the mat locus (Figure 2A).
PMID:16762840	FYPO:0006373	A similar increase in H3K9me2 levels was also observed in swi6 mutant cells defective in Epe1 recruitment to meiotic genes (Figure 6E).
PMID:16762840	PBO:0111030	Deletion of clr3 results in a dramatic increase in Pol II occupancy at cenH element within silent mat domain.
PMID:16762840	PBO:0097227	Our analysis revealed that Epe1 is required for the increase in transcription of repeats in Dclr3 background, as suggested by the dramatic reduction in transcript levels in Depe1 Dclr3 double mutant compared to Dclr3 single mutant (Figures 5A and 5B).
PMID:16762840	PBO:0098231	Moreover, Epe1 was detected at certain meiotic genes, some of which are coated with heterochromatic markers (Figure 2A; [Cam et al., 2005]).
PMID:16762840	PBO:0110802	ChIP analysis showed that mutant protein is recruited to heterochromatic loci (Figure 6B), consistent with data showing that Y307A mutation has no effect on Epe1 interaction with Swi6 in vitro (Figure 3D)
PMID:16762840	FYPO:0002335	The Y307 mutation abolished the ability of Epe1 to destabilize heterochromatic silencing (Figure 6A).
PMID:16762840	PBO:0110571	a glutathione S-transferase (GST) pull-down assay showed that in vitro-translated Epe1 directly binds to GST-Swi6, but not GST alone (Figure 3D). This interaction is not affected by a mutation in JmjC domain of Epe1 (Y307A) that impairs Epe1 function. Based on these analyses, Swi6-mediated recruitment of Epe1 might involve direct interaction between these factors. ChIP analysis revealed that mutations in swi6 or clr4 resulted in loss of Epe1 from mcp5, mcp7, mei4, and ssm4, and from the LC region (Figures 4A and 4B), suggesting Swi6 facilitated recruitment of Epe1 to these loci.
PMID:16762840	PBO:0094684	However, abundant transcripts corresponding to centromeric repeats and cenH are detectable in RNAi- defective Dago1 cells. We found that the levels of transcripts in Depe1Dago1 double mutant cells were significantly reduced (Figures 5A and 5B), indicating that Epe1 facilitates transcription of the heterochromatic repeats.
PMID:16762840	FYPO:0000877	Remarkably, loss of Epe1 resulted in a diminished access of Pol II to cenH in Dclr3 cells, as indicated by substantial reduction in Pol II levels in Depe1 Dclr3 double mutant as compared to Dclr3 single mutant (Figure 5E). These results suggest that Epe1 has an important role in promoting access of transcriptional machinery to heterochromatic sequences, thereby facilitating transcription of repeat elements. Therefore, the balance of activities between Clr3 and Epe1, both of which are recruited by Swi6, seems critical in determining the transcriptional state of repeat elements.
PMID:16762840	PBO:0111028	Moreover, ChIP analysis revealed that mutation in Swi6 or an H3K9-specific methyltransferase Clr4 abolished Epe1 localization at centromeres, telomeres, and the mat locus, concurrent with loss of Swi6 at these loci (Figure 3B)
PMID:16762840	PBO:0111027	Moreover, ChIP analysis revealed that mutation in Swi6 or an H3K9-specific methyltransferase Clr4 abolished Epe1 localization at centromeres, telomeres, and the mat locus, concurrent with loss of Swi6 at these loci (Figure 3B)
PMID:16762840	PBO:0111026	In swi6 mutant background, Epe1-GFP was no longer localized to discrete spots at the nuclear periphery (Figure 3A).
PMID:16762840	PBO:0111025	Moreover, Epe1 was detected at certain meiotic genes, some of which are coated with heterochromatic markers (Figure 2A; [Cam et al., 2005]).
PMID:16762840	PBO:0111024	Moreover, Epe1 was detected at certain meiotic genes, some of which are coated with heterochromatic markers (Figure 2A; [Cam et al., 2005]).
PMID:16762840	PBO:0098232	Moreover, Epe1 was detected at certain meiotic genes, some of which are coated with heterochromatic markers (Figure 2A; [Cam et al., 2005]).
PMID:16762840	PBO:0111023	Moreover, Epe1 was detected at certain meiotic genes, some of which are coated with heterochromatic markers (Figure 2A; [Cam et al., 2005]).
PMID:16762840	PBO:0097227	Our analysis revealed that Epe1 is required for the increase in transcription of repeats in Dclr3 background, as suggested by the dramatic reduction in transcript levels in Depe1 Dclr3 double mutant compared to Dclr3 single mutant (Figures 5A and 5B).
PMID:16762840	PBO:0111029	Moreover, ChIP analysis revealed that mutation in Swi6 or an H3K9-specific methyltransferase Clr4 abolished Epe1 localization at centromeres, telomeres, and the mat locus, concurrent with loss of Swi6 at these loci (Figure 3B)
PMID:16762840	PBO:0111032	We next investigated the possible involvement of Epe1 in boundary function of the IRC elements. Remarkably, deletion of epe1 resulted in spreading of Swi6 and H3K9me into euchromatic regions surrounding cen1 (Figure 7D).
PMID:16762840	PBO:0094684	Our analysis revealed that Epe1 is required for the increase in transcription of repeats in Dclr3 background, as suggested by the dramatic reduction in transcript levels in Depe1 Dclr3 double mutant compared to Dclr3 single mutant (Figures 5A and 5B).
PMID:16762840	PBO:0111022	Moreover, Epe1 was detected at certain meiotic genes, some of which are coated with heterochromatic markers (Figure 2A; [Cam et al., 2005]).
PMID:16762840	FYPO:0002335	We found that loss of Epe1 restores Swi6 localization and silencing in Dago1 and Dclr3 mutants to levels comparable to wild-type cells (Figure 5C and Figure S3)
PMID:16762840	FYPO:0002335	We found that loss of Epe1 restores Swi6 localization and silencing in Dago1 and Dclr3 mutants to levels comparable to wild-type cells (Figure 5C and Figure S3)
PMID:16762840	PBO:0094684	Indeed, in a situation wherein heterochromatin has been completely abolished, such as in a Dclr4 background, loss of Epe1 had no detectable effect on transcript levels (Figure 5D).
PMID:16762840	PBO:0094684	Indeed, in a situation wherein heterochromatin has been completely abolished, such as in a Dclr4 background, loss of Epe1 had no detectable effect on transcript levels (Figure 5D).
PMID:16762840	FYPO:0000862	Indeed, we found that loss of H3K9me2 in cells overexpressing Epe1 is dependent upon Swi6 (Figure 6D).
PMID:16762840	FYPO:0006373	We also tested the effect of Epe1 on heterochromatic markers at meiotic genes. Interestingly, loss of Epe1 resulted in considerable increase in H3K9me2 and H3K9me3 levels, concomitant with moderate increase in Swi6 binding at the ssm4 gene (Figures 6E and 6F).
PMID:16775007	FYPO:0002061	(Figure 7A)
PMID:16775007	GO:0044732	(Fig. 1A)
PMID:16775007	PBO:0098902	(Fig. 2A)
PMID:16775007	PBO:0098905	(Fig. 5D)
PMID:16775007	GO:0005515	(Fig. 2A)
PMID:16775007	FYPO:0002061	(Figure 5, A and B)
PMID:16775007	GO:0005515	(Figure 4C)
PMID:16787941	PBO:0035494	(Fig. 1B)
PMID:16787941	FYPO:0008402	(Fig. 8)
PMID:16787941	FYPO:0000478	(Fig. 8B)
PMID:16787941	FYPO:0000478	(Fig. 8B)
PMID:16787941	PBO:0119930	(Fig. 7A)
PMID:16787941	PBO:0119948	(Fig. 7A)
PMID:16787941	FYPO:0000478	(Fig. 3B, 3C, Fig. 4, Fig. 5)
PMID:16787941	PBO:0119947	(Fig. 2C)
PMID:16787941	FYPO:0002708	(Fig. 3, Fig. 6)
PMID:16787941	PBO:0035493	(Fig. 1C)
PMID:16787941	PBO:0035494	(Fig. 1C)
PMID:16787941	PBO:0035493	(Fig. 1D)
PMID:16787941	PBO:0035494	(Fig. 1E)
PMID:16787941	PBO:0035494	(Fig. 1F)
PMID:16787941	PBO:0035493	(Fig. 1G)
PMID:16787941	PBO:0035494	(Fig. 1G)
PMID:16787941	PBO:0035493	(Fig. 1H)
PMID:16787941	PBO:0035494	(Fig. 1H)
PMID:16787941	PBO:0119943	(Fig. 2C)
PMID:16787941	PBO:0119944	(Fig. 2C)
PMID:16787941	PBO:0119943	(Fig. 2C)
PMID:16787941	PBO:0119945	(Fig. 2C)
PMID:16787941	PBO:0119946	(Fig. 2C)
PMID:16787941	PBO:0035493	(Fig. 1A)
PMID:16787941	PBO:0035494	(Fig. 1A)
PMID:16787941	PBO:0035493	(Fig. 1B)
PMID:16822282	FYPO:0004129	(comment: caspase)
PMID:16822282	FYPO:0001310	(Fig. 3A)
PMID:16822282	FYPO:0001310	(Fig. 3A)
PMID:16822282	FYPO:0001309	(Fig. 3A)
PMID:16822282	FYPO:0004129	(comment: caspase)
PMID:16822282	FYPO:0002143	(Fig. 3A)
PMID:16822282	PBO:0097358	(comment: caspase)
PMID:16822282	FYPO:0001309	(Fig. 3A)
PMID:16822282	FYPO:0002143	(Fig. 3A)
PMID:16822282	FYPO:0002143	(Fig. 3A)
PMID:16823445	PBO:0116822	We propose that Mei2 turns off the DSR-Mmi1 system by sequestering Mmi1 to the dot and thereby secures stable expression of meiosis-specific transcripts (Abstract).
PMID:16824200	PBO:0022963	requires intact mitotic spindle, as shown by cold-depolymerizing microtubules and nda3 mad2 double mutant phenotype
PMID:16857197	PBO:0105400	(comment: CHECK might be abolished. Sometimes you see diploidization.)
PMID:16914721	PBO:0094384	microarray data shows 111 genes affected
PMID:16914721	GO:0000184	These findings showed that Upf1 is required for degradation of the ade6-M26 mRNA in S. pombe.
PMID:16914721	GO:0000184	These findings showed that Upf1 is required for degradation of the ade6-M26 mRNA in S. pombe.
PMID:16914721	PBO:0097312	microarray data shows 111 genes affected
PMID:16914721	PBO:0097311	microarray data shows 111 genes affected
PMID:16914721	FYPO:0003917	(comment: assayed using ade6-M26)
PMID:16914721	PBO:0097313	microarray data shows 111 genes affected
PMID:16916637	PBO:0113982	nrm1D mutants exhibited elevated levels of these MBF-dependent transcripts throughout the cell cycle (cdc22+, Figure 6F; cdc18+ and ste9+, data not shown). We conclude that SpNrm1 is essential for repression of MBF-regulated genes outside of the G1 phase and that both Res2 and the SpNrm1 are required for periodic expression of G1-specific transcripts. I
PMID:16916637	PBO:0113983	nrm1D mutants exhibited elevated levels of these MBF-dependent transcripts throughout the cell cycle (cdc22+ , Figure 6F; cdc18+ and ste9+, data not shown). We conclude that SpNrm1 is essential for repression of MBF-regulated genes outside of the G1 phase and that both Res2 and the SpNrm1 are required for periodic expression of G1-specific transcripts. I
PMID:16916637	PBO:0113984	elevated levels of these MBF-dependent transcripts throughout the cell cycle (cdc22+, Figure 6F; cdc18+ and ste9+, data not shown). We conclude that SpNrm1 is essential for repression of MBF-regulated genes outside of the G1 phase and that both Res2 and the SpNrm1 are required for periodic expression of G1-specific transcripts. I
PMID:16916637	PBO:0092049	Analysis of nrm1+ transcript abundance in temperature-sensitive cdc25-22 cells arrested in G2/M and, subsequently, released into the cell cycle revealed that nrm1+, like the well-established G1-specific targetscdc18+ and ste9+, is a G1-specific transcript (Figure 6D).
PMID:16920624	FYPO:0002141	(Figure 2A)
PMID:16920624	FYPO:0001355	(Figure 2D) whereas mis12 Dis1N3A and mis12 Dis1C3A showed weak inhibition of colony formation
PMID:16920624	FYPO:0002061	In contrast, the Dis16E mutant, which shows the synthetic lethality with Dmtc1, diminished signals along the metaphase spindle. Thus, there is a correlation between the affinity for microtubules of the mutant versions of Dis1 and these mutants’ ability to rescue the Dmtc1 defect.
PMID:16920624	PBO:0106990	(Figure 1C)
PMID:16920624	PBO:0106992	(Figure 2C) The loss rate in Dis16E was lower than Dis16A and slightly higher than that in the wild-type. (The Dis16E mutant appears to mimic at least partially the Cdc2-phosphorylated form of Dis1)
PMID:16920624	PBO:0106989	(Figure 1B)
PMID:16920624	PBO:0106989	(Figure 1B)
PMID:16920624	PBO:0023853	(comment: CHECK PHOSPHORYLATED.) Fig3A The Dis1WT-GFP signals are seen as the kinetochore dots in metaphase. AND 4b
PMID:16920624	PBO:0106994	(comment: CHECK protein localized to spindle (also a child of mislocalized protein))
PMID:16920624	FYPO:0004310	Measurements of the durations of phase 1 (prophase to metaphase), 2 (metaphase to anaphase), and 3 (anaphase B) on each of the 30 movies of Dis1WT, Dis16A, and Dis16E strains indicated that the timing of mitosis did not seem to be affected by any mutations because measured differences were within the boundaries of experimental error (Figure S1C)
PMID:16920624	FYPO:0004310	Measurements of the durations of phase 1 (prophase to metaphase), 2 (metaphase to anaphase), and 3 (anaphase B) on each of the 30 movies of Dis1WT, Dis16A, and Dis16E strains indicated that the timing of mitosis did not seem to be affected by any mutations because measured differences were within the boundaries of experimental error (Figure S1C)
PMID:16920624	PBO:0106996	Curiously, bent spindles were observed in late anaphase of 53 of 121 Dis16A cells in movies, whereas only 18 of 104 Dis1WT and ten of 127 Dis16E cells examined showed the bent spindle (Figure S1D).
PMID:16920624	PBO:0022134	(comment: CHECK UNPHOSPHORYLATED.) In anaphase, Dis1WT-GFP signals abruptly increased along the spindle and at the SPBs despite being absent from the central zone.
PMID:16920624	FYPO:0002061	(Figure 2D) The double mutant mis12 Dis16A failed to produce colonies at 33
PMID:16920624	PBO:0106993	These results established that phosphorylation of Dis1 by Cdc2 is required for the high-fidelity segregation of a minichromosome. (comment: (A little bit of curator licence here))
PMID:16920624	FYPO:0002141	(Figure 2A)
PMID:16920624	PBO:0093564	(Figure 2B)
PMID:16920624	PBO:0093563	(Figure 2B)
PMID:16920624	PBO:0093562	(Figure 2B)
PMID:16920624	PBO:0018845	Because Dis1WT, Dis16A, and Dis16E all associated with anaphase SPBs, this association was independent of modification of the molecule on the Cdc2 phosphorylation sites.
PMID:16920624	FYPO:0000964	(Fig. 6)
PMID:16920624	FYPO:0000964	(Figure 2B) The sensitivities of Dis1N3A and Dis1C3A were similar to that of the wild-type.
PMID:16920624	FYPO:0000964	(Figure 2B) The sensitivities of Dis1N3A and Dis1C3A were similar to that of the wild-type.
PMID:16920624	PBO:0106991	(Figure 2C) The loss rate of CN2 minichromosome in Dis16A was much higher than that of the wild-type integrant...
PMID:16920624	FYPO:0001839	(Figure 2C) .... whereas Dis1N3A and Dis1C3A had loss rates that were comparable to those of the wild-type Dis1 integrant.
PMID:16920624	FYPO:0001839	(Figure 2C) .... whereas Dis1N3A and Dis1C3A had loss rates that were comparable to those of the wild-type Dis1 integrant.
PMID:16920624	FYPO:0001355	(Figure 2D) whereas mis12 Dis1N3A and mis12 Dis1C3A showed weak inhibition of colony formation
PMID:16920624	FYPO:0001357	(Figure 2D) However, the double mutant mis12 Dis16E could form colonies at 33ΔC.
PMID:16921379	GO:0005515	sfr1 protein is not stable without swi5. swi5 alone does not bind rad51.
PMID:16921379	PBO:0105172	(comment: in complex with Swi5)
PMID:16921379	PBO:0105172	(comment: in complex with Sfr1)
PMID:16921379	GO:0005515	(comment: sfr1 protein is not stable without swi5. swi5 alone does not bind rad51.)
PMID:16931764	PBO:0112801	(Fig. 1D)
PMID:16931764	PBO:0112802	(Fig. 1D)
PMID:16931764	PBO:0112802	(Fig. 1D)
PMID:16931764	PBO:0112801	(Fig. 1D)
PMID:16931764	PBO:0120516	(Fig. 2A)
PMID:16931764	PBO:0120515	(Fig. 2A)
PMID:16931764	PBO:0120516	(Fig. 2A)
PMID:16931764	PBO:0120515	(Fig. 2A)
PMID:16931764	FYPO:0002835	(Fig. 1E)
PMID:16931764	FYPO:0002835	(Fig. 1E)
PMID:16931764	PBO:0112802	(Fig. 1D)
PMID:16931764	PBO:0112799	"Thus, Ago1 from fission yeast has ""slicing"" activity and can direct site-specific cleavage of RNA substrates via siRNA."
PMID:16931764	PBO:0112800	(Fig. 1C)
PMID:16931764	PBO:0112800	(Fig. 1C)
PMID:16931764	PBO:0112800	(Fig. 1C)
PMID:16931764	PBO:0112801	(Fig. 1D)
PMID:16931764	PBO:0112802	(Fig. 1D)
PMID:16931764	PBO:0112805	(Fig. 2B)
PMID:16931764	PBO:0112806	(Fig. 2B)
PMID:16931764	PBO:0112807	(Fig. 2C)
PMID:16931764	PBO:0112801	(Fig. 1D)
PMID:16931764	PBO:0112807	(Fig. 2C)
PMID:16931764	PBO:0098772	(Fig. 2C)
PMID:16931764	PBO:0098772	(Fig. 2C)
PMID:16931764	PBO:0094684	(Fig. 3C)
PMID:16931764	PBO:0094684	(Fig. 3C)
PMID:16963626	GO:0016602	using the cross-linking agent EGS, we found that the Php4 protein associates with the Php2/Php3/Php5 complex
PMID:16963626	GO:0016602	(Fig. 6b)
PMID:16963626	PBO:0095322	Consistently, mutations in the php3Δ - and php5Δ -encoded CCAAT-binding proteins were phenocopies of php2􏰂
PMID:16963626	PBO:0095322	Consistently, mutations in the php3Δ - and php5Δ -encoded CCAAT-binding proteins were phenocopies of php2􏰂
PMID:1699136	PBO:0033573	(Figure 2)
PMID:1699136	PBO:0096176	(Figure 1c)
PMID:1699136	PBO:0024124	(Figure 1c) and Double staining using a combination of cdc13- and tubulin- specific antibodies showed that the dots corresponded exactly to the positions of the mitotic spindle poles (Fig. 3a, b)
PMID:1699136	PBO:0024124	(Figure 1c) and Double staining using a combination of cdc13- and tubulin- specific antibodies showed that the dots corresponded exactly to the positions of the mitotic spindle poles (Fig. 3a, b)
PMID:17004072	FYPO:0002061	(Table 2)
PMID:17004072	FYPO:0002060	(Figure 5b)
PMID:17004072	FYPO:0001861	(Figure 2a)
PMID:17004072	FYPO:0001861	(Figure 2a)
PMID:17005570	PBO:0104000	(Fig. 3)
PMID:17005570	GO:0005515	(Fig. 1)
PMID:17005570	PBO:0104003	(Fig. 5C)
PMID:17005570	PBO:0104004	(Fig. 6B, lane 9)
PMID:17005570	PBO:0104000	(Fig. 3)
PMID:17005570	PBO:0104001	(Fig. 1f)
PMID:17005570	PBO:0104003	(Fig. 5A)
PMID:17005570	GO:0005515	(Fig. 1)
PMID:17005570	PBO:0104001	(Fig. 1f)
PMID:17005570	PBO:0103998	(Fig. 1c) lane 9
PMID:17005570	GO:0005515	(Fig. 1)
PMID:17005570	PBO:0104000	(Fig. 3)
PMID:17005570	PBO:0104005	(Fig. 7A)
PMID:17005570	PBO:0104002	(Fig. 3)
PMID:17005570	PBO:0104002	(Fig. 3)
PMID:17005570	PBO:0104005	(Fig. 7A)
PMID:17005570	GO:0005515	(Fig. 1)
PMID:17005570	GO:0005515	(Fig. 1)
PMID:17005570	PBO:0104004	(Fig. 6B, lane 3)
PMID:17005570	PBO:0104004	(Fig. 6A, lane 9)
PMID:17005570	GO:0005515	(Fig. 1)
PMID:17005570	GO:0005515	(Fig. 1)
PMID:17005570	PBO:0103998	(Fig. 1b)
PMID:17005570	PBO:0104002	(Fig. 3)
PMID:17005570	PBO:0103999	(Fig. 1b)
PMID:17005570	PBO:0103999	(Fig. 1c)
PMID:17005570	PBO:0104000	(Fig. 1d)
PMID:17005570	GO:0005515	(Fig. 1F)
PMID:1703321	FYPO:0002060	cdc2-F15 (comment: gene is expressed from episomal pIRT2)
PMID:1703321	PBO:0093712	cdc2-F15 (comment: gene is expressed from episomal pIRT2)
PMID:1703321	PBO:0093712	(comment: CHECK Also think this is previously annotated)
PMID:1703321	FYPO:0006822	(comment: cdc2-F15 gene is expressed from episomal pIRT2)
PMID:1703321	PBO:0093712	(comment: cdc25 over expressed from the constitutive ADH promoter. Data not shown)
PMID:1703321	PBO:0093712	data not shown
PMID:1703321	PBO:0097952	(Figure 4D)
PMID:1703321	PBO:0093712	data not shown
PMID:1703321	PBO:0097952	(Figure 4D)
PMID:1703321	PBO:0097952	(Figure 4)
PMID:1703321	PBO:0093712	(comment: CHECK I'm sure this has already been annotated. But previous annotations didn't come up, should they?)
PMID:1703321	FYPO:0002060	(comment: cdc2-F15 gene is expressed from episomal pIRT2)
PMID:1703321	PBO:0097952	(Figure 4D)
PMID:17035632	PBO:0109097	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0018649	These 4 proteins share homology with the S. cerevisiae DASH complex, DAM1, DAD2, ASK1, and SPC34 (Miranda et al., 2005), and the observation that their centromere localization is limited to the M phase has been previously reported in S. pombe (Liu et al., 2005). Thus, we assigned these four proteins to the DASH complex (Table 2)
PMID:17035632	PBO:0018649	These 4 proteins share homology with the S. cerevisiae DASH complex, DAM1, DAD2, ASK1, and SPC34 (Miranda et al., 2005), and the observation that their centromere localization is limited to the M phase has been previously reported in S. pombe (Liu et al., 2005). Thus, we assigned these four proteins to the DASH complex (Table 2)
PMID:17035632	PBO:0018649	These 4 proteins share homology with the S. cerevisiae DASH complex, DAM1, DAD2, ASK1, and SPC34 (Miranda et al., 2005), and the observation that their centromere localization is limited to the M phase has been previously reported in S. pombe (Liu et al., 2005). Thus, we assigned these four proteins to the DASH complex (Table 2)
PMID:17035632	PBO:0018649	These 4 proteins share homology with the S. cerevisiae DASH complex, DAM1, DAD2, ASK1, and SPC34 (Miranda et al., 2005), and the observation that their centromere localization is limited to the M phase has been previously reported in S. pombe (Liu et al., 2005). Thus, we assigned these four proteins to the DASH complex (Table 2)
PMID:17035632	PBO:0103971	In contrast, four proteins (Dam1, Dad2, Ask1, and Spc34) were localized at the centromere only at the M phase (Table 2; group 2).
PMID:17035632	PBO:0103971	In contrast, four proteins (Dam1, Dad2, Ask1, and Spc34) were localized at the centromere only at the M phase (Table 2; group 2).
PMID:17035632	PBO:0103971	In contrast, four proteins (Dam1, Dad2, Ask1, and Spc34) were localized at the centromere only at the M phase (Table 2; group 2).
PMID:17035632	PBO:0103971	In contrast, four proteins (Dam1, Dad2, Ask1, and Spc34) were localized at the centromere only at the M phase (Table 2; group 2).
PMID:17035632	PBO:0103971	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103971	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103971	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103971	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0109096	Sgo1 protein signal intensity increased in two steps (52 and 20 min before the metaphase-anaphase transition of meiosis I) in a way similar to the NMS (Ndc80- Mis12-Spc7) complex proteins (Figure 7B).
PMID:17035632	PBO:0109097	Sgo1 protein signal intensity increased in two steps (52 and 20 min before the metaphase-anaphase transition of meiosis I) in a way similar to the NMS (Ndc80- Mis12-Spc7) complex proteins (Figure 7B).
PMID:17035632	PBO:0109097	The DASH complex proteins (Dam1, Spc34, Dad2, and Ask1) were not detected during meiotic prophase. They reappeared at the centromere shortly before metaphase of meiosis I (Figure 4)
PMID:17035632	PBO:0109097	The DASH complex proteins (Dam1, Spc34, Dad2, and Ask1) were not detected during meiotic prophase. They reappeared at the centromere shortly before metaphase of meiosis I (Figure 4)
PMID:17035632	PBO:0109097	The DASH complex proteins (Dam1, Spc34, Dad2, and Ask1) were not detected during meiotic prophase. They reappeared at the centromere shortly before metaphase of meiosis I (Figure 4)
PMID:17035632	PBO:0109097	The DASH complex proteins (Dam1, Spc34, Dad2, and Ask1) were not detected during meiotic prophase. They reappeared at the centromere shortly before metaphase of meiosis I (Figure 4)
PMID:17035632	PBO:0109099	In addition, their centromere localization depended on Mis6: Cnl2 and Fta7 proteins lost their centromere localization in a mis6-302 temperature-sensitive mutant at the restricted temperature of 36°C (Figure 1E)
PMID:17035632	PBO:0109098	In addition, their centromere localization depended on Mis6: Cnl2 and Fta7 proteins lost their centromere localization in a mis6-302 temperature-sensitive mutant at the restricted temperature of 36°C (Figure 1E)
PMID:17035632	PBO:0109097	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0103970	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103970	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103970	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103970	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103970	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103970	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103970	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103970	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103970	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103970	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103970	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103970	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103970	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103970	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103970	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103970	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103970	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103970	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103971	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103971	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103971	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103971	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103971	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103971	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103971	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103971	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103971	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103971	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103971	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103971	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103971	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0103971	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	PBO:0109097	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109096	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109096	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109096	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109096	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109096	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109096	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109096	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109096	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	PBO:0109096	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17036054	PBO:0101893	(Fig. 1b)
PMID:17036054	PBO:0101888	(Figure 1a)
PMID:17036054	PBO:0101891	(comment: CHECK Supplement)
PMID:17036054	PBO:0101889	(Figure 1a)
PMID:17036054	PBO:0101887	(Figure 1a)
PMID:17036054	FYPO:0005720	(Fig. 1b)
PMID:17036054	PBO:0101893	(Fig. 1b)
PMID:17036054	PBO:0101893	(Fig. 1b)
PMID:17036054	PBO:0101894	(Fig. 1b)
PMID:17036054	PBO:0101887	(Figure 1a)
PMID:17036054	PBO:0101888	(Figure 1a)
PMID:17036054	PBO:0101888	(Figure 1a)
PMID:17036054	PBO:0101887	(Figure 1a)
PMID:17036054	PBO:0101890	(Figure 1a)
PMID:17038309	GO:0003677	(comment: binds both circular and linear DNA fragments)
PMID:17038309	GO:0097680	(comment: CHECK i) xlf1 deletion is epistatic with lig4 deletion ii) IR sensitivity during spore state and inability to ligate linearised plasmids during vegetative state)
PMID:17039252	PBO:0094400	(comment: especially during S and G2 phases)
PMID:17039252	PBO:0094400	(comment: especially during S and G2 phases)
PMID:17039252	PBO:0094400	(comment: especially during S and G2 phases)
PMID:17039252	PBO:0094400	(comment: especially during S and G2 phases)
PMID:17043360	PBO:0093581	(Fig. 1B)
PMID:17043360	PBO:0112856	(Fig. 4A)
PMID:17043360	FYPO:0000012	(Fig. 1C)
PMID:17043360	FYPO:0000650	(Fig. 2)
PMID:17043360	PBO:0093579	(Fig. 1B)
PMID:17043360	PBO:0112857	(Fig. 4C)
PMID:17046992	GO:1900087	TORC1 senses nutrients and pushes cells into the next cell cycle. Removing TORC1 activity, you get a buildup of rum1 and srw1 which inhibit G1/S
PMID:17046992	FYPO:0004481	cells stop growing at high temperature, but remain viable and resume growth and division when returned to standard temperature
PMID:17046992	FYPO:0002060	cells stop growing at high temperature, but remain viable and resume growth and division when returned to standard temperature
PMID:17085965	GO:1902929	localization depends on microtubule cytoskeleton, as determined by treatment with carbendazim (methyl 2-benzimidazolecarbamate; MBC), and on actin cytoskeleton, as determined by treatment with latrunculin B or cytochalasin D
PMID:17112379	FYPO:0001974	(comment: CONDITION 30 degrees)
PMID:17112379	PBO:0093561	(comment: CONDITION 25 degrees)
PMID:17112379	PBO:0093561	(comment: CONDITION 25 degrees)
PMID:17112379	FYPO:0002061	(comment: CONDITION 30 degrees)
PMID:17112379	PBO:0093559	(comment: CONDITION 25 degrees)
PMID:17121544	PBO:0097202	(comment: CONDITION at 30 degrees) Tor1 becomes necessary for cell growth when Tor2 function is compromised.
PMID:17121544	FYPO:0005097	(mimic nitrogen starvation response, When starved for nitrogen, on the other hand, the cells divide twice and then arrest at G1) At 4 h and 8 h after the shift to36 °C, the average cell length was reduced to 6.4 μm and6.2 μm, respectively, which were ∼50% decreases com-pared to wild-type cells (13.0 μm and 12.9 μm). Similar tsresults were obtained for tor2 -19. It is of note that, in contrast to the reduced length, the cell width remained constant in these mutant cells.
PMID:17121544	FYPO:0002578	As expected, these double mutants behaved the same as tor1∆rhb1+o/e cells, in which growth was restored under stress conditions (the fourth row).
PMID:17121544	FYPO:0000400	tor1∆tor2 -19 showed only the 2C peak, and no 1C peak appeared at 36 °C
PMID:17121544	PBO:0103531	(comment: CONDITION at 30 degrees)
PMID:17121544	PBO:0103529	70% of ts the tor2 -13 cells committed sexual development to ts form zygotes and spores (Fig. 3B,C)
PMID:17121544	FYPO:0005097	(mimic nitrogen starvation response, When starved for nitrogen, on the other hand, the cells divide twice and then arrest at G1) At 4 h and 8 h after the shift to36 °C, the average cell length was reduced to 6.4 μm and6.2 μm, respectively, which were ∼50% decreases com-pared to wild-type cells (13.0 μm and 12.9 μm). Similar tsresults were obtained for tor2 -19. It is of note that, in contrast to the reduced length, the cell width remained constant in these mutant cells.
PMID:17121544	FYPO:0002061	(Figure 1B)
PMID:17121544	PBO:0103528	(mimic nitrogen starvation response, When starved for nitrogen, on the other hand, the cells divide twice and then arrest at G1) At 4 h and 8 h after the shift to36 °C, the average cell length was reduced to 6.4 μm and6.2 μm, respectively, which were ∼50% decreases com-pared to wild-type cells (13.0 μm and 12.9 μm). Similar tsresults were obtained for tor2 -19. It is of note that, in contrast to the reduced length, the cell width remained constant in these mutant cells.
PMID:17121544	PBO:0103528	(mimic nitrogen starvation response, When starved for nitrogen, on the other hand, the cells divide twice and then arrest at G1) At 4 h and 8 h after the shift to36 °C, the average cell length was reduced to 6.4 μm and6.2 μm, respectively, which were ∼50% decreases com-pared to wild-type cells (13.0 μm and 12.9 μm). Similar tsresults were obtained for tor2 -19. It is of note that, in contrast to the reduced length, the cell width remained constant in these mutant cells.
PMID:17121544	FYPO:0002061	(Figure 1B)
PMID:17130122	FYPO:0003669	(comment: assayed using artificial reporter construct ura4 containing two introns and one exon from nda3)
PMID:17130122	FYPO:0003669	(comment: assayed using artificial reporter construct ura4 containing two introns and one exon from nda3)
PMID:17130122	FYPO:0003669	(comment: assayed using artificial reporter construct ura4 containing two introns and one exon from nda3)
PMID:17130122	FYPO:0003669	(comment: assayed using artificial reporter construct ura4 containing two introns and one exon from nda3)
PMID:17178839	FYPO:0005435	(Fig. 3c)
PMID:17178839	FYPO:0002061	(Fig. 1B)
PMID:17178839	FYPO:0002058	(Fig. 1B)
PMID:17178839	FYPO:0002060	(Fig. 1A)
PMID:17178839	FYPO:0002060	(Fig. 1A)
PMID:17178839	FYPO:0002060	(Fig. 1A)
PMID:17178839	FYPO:0002060	(Fig. 1B)
PMID:17178839	FYPO:0002061	(Fig. 1B)
PMID:17178839	FYPO:0003165	(Fig. 1c,d)
PMID:17178839	PBO:0035372	(Fig. 2 a,b)
PMID:17178839	FYPO:0005437	(Fig. 4D)
PMID:17178839	FYPO:0000671	(comment: CHECK not sure if this is correct....)
PMID:17178839	FYPO:0000671	(comment: CHECK not sure if this is correct....)
PMID:17178839	PBO:0035377	(Fig. 4C)
PMID:17178839	PBO:0035376	(Fig. 4B)
PMID:17178839	PBO:0035375	(Fig. 4B)
PMID:17178839	PBO:0035373	(Fig. 2 a,b)
PMID:17178839	PBO:0093586	(Fig. 4A)
PMID:17178839	PBO:0093630	(Fig. 4A)
PMID:17178839	PBO:0093616	(Fig. 4A)
PMID:17178839	PBO:0093580	(Fig. 4A)
PMID:17178839	FYPO:0002060	(Fig. 3C)
PMID:17178839	FYPO:0002061	(Fig. 3B)
PMID:17178839	FYPO:0002060	(Fig. 3A)
PMID:17178839	PBO:0035374	(Fig. 2 a,b)
PMID:17178839	FYPO:0002061	(Fig. 1B)
PMID:17192844	FYPO:0000488	The wild-type cross yielded 81 ± 7.5% viable spores, the pnu1Δ cross 82 ± 3%. As far as tested, no change of meiosis and recombination was detected in mutants abolishing the function of the Pnu1 (End1) nuclease.
PMID:17211518	FYPO:0002800	proteasomal
PMID:17213188	FYPO:0002926	(comment: binding by Pab2)
PMID:17222800	FYPO:0003720	(comment: CHECK 25S rRNA positions 2304, 2497)
PMID:17276356	FYPO:0002321	However, similar to dap1D, yeast carrying the HA-dap1 Y138F plasmid accumulated 24-methylene lanosterol, ergosta-5,7,24(28)-trienol, and ergosta-5,7- dienol, reflecting defects in Erg11 and Erg5 (Figure 3B). These data indicate that dap1 Y138F is a loss-of-function mutation and that Dap1 function requires bound heme.
PMID:17276356	PBO:0112616	These data demonstrate that Dap1 is required in vivo for the activity of Erg11 and Erg5, the entire complement of cytochrome P450 enzymes in fission yeast.
PMID:17276356	FYPO:0009071	sensitive to the inhibitors of sterol synthesis itraconazole and CoCl2 (Figure 1D).
PMID:17276356	FYPO:0008297	elevated amounts of the ergosterol biosynthetic intermediates 2. upon loss of Dap1, cells accumulated 24-methylene lanosterol, ergosta5,7,24(28)-trienol, and ergosta-5,7-dienol, substrates for Erg11 and Erg5. 4-methylene lanosterol, ergosta-5,7,24(28)-trienol, and ergosta-5,7-dienol, Figure 1B. Ergosta-5,7-dienol is not a normal pathway intermediate, but forms when Erg5 is inhibited (Figure S1)
PMID:17276356	FYPO:0002321	...contained a reduced amount of ergosterol and elevated amounts of the ergosterol biosynthetic intermediates 24-methylene lanosterol, ergosta-5,7,24(28)-trienol, and ergosta-5,7-dienol, consistent with defects at the Erg11 and Erg5 enzymatic steps (Figure 1B).
PMID:17276356	PBO:0092067	Expression of dap1+ mRNA was induced in the absence of oxygen in a Sre1-dependent manner (Figure 1A)
PMID:17276356	PBO:0112614	These data demonstrate that Dap1 is required in vivo for the activity of Erg11 and Erg5, the entire complement of cytochrome P450 enzymes in fission yeast.
PMID:17276356	FYPO:0002060	dap1D cells were viable under normal growth conditions but .....
PMID:17276356	PBO:0112615	These data demonstrate that Dap1 is required in vivo for the activity of Erg11 and Erg5, the entire complement of cytochrome P450 enzymes in fission yeast.
PMID:17276356	FYPO:0008298	elevated amounts of the ergosterol biosynthetic intermediates 2. upon loss of Dap1, cells accumulated 24-methylene lanosterol, ergosta-5,7,24(28)-trienol, and ergosta-5,7-dienol, substrates for Erg11 and Erg5. 4-methylene lanosterol, ergosta-5,7,24(28)-trienol, and ergosta-5,7-dienol, Figure 1B. Ergosta-5,7-dienol is not a normal pathway intermediate, but forms when Erg5 is inhibited (Figure S1)
PMID:17276356	FYPO:0008296	elevated amounts of the ergosterol biosynthetic intermediates 2. upon loss of Dap1, cells accumulated 24-methylene lanosterol, ergosta-5,7,24(28)-trienol, and ergosta-5,7-dienol, substrates for Erg11 and Erg5. 4-methylene lanosterol, ergosta-5,7,24(28)-trienol, and ergosta-5,7-dienol, Figure 1B. Ergosta-5,7-dienol is not a normal pathway intermediate, but forms when Erg5 is inhibited (Figure S1)
PMID:17289569	GO:0000183	(comment: by TGS)
PMID:17289569	GO:0000183	(comment: by TGS)
PMID:17289569	PBO:0100952	(comment: part of TGS)
PMID:17289569	PBO:0100953	(Figure 4B) clr3 at telomeres were reduced to the same extent in mutant strains disrupted for either Ccq1 or Taz1
PMID:17289569	PBO:0100953	(Figure 4B) clr3 at telomeres were reduced to the same extent in mutant strains disrupted for either Ccq1 or Taz1
PMID:17289569	PBO:0100954	(Figure 4B) while the levels of Ccq1 at telomeres, relative to those in wild-type cells, were unchanged in clr3D cells but decreased in taz1D
PMID:17289569	PBO:0100955	(Figure 4B) while the levels of Ccq1 at telomeres, relative to those in wild-type cells, were unchanged in clr3D cells but decreased in taz1D
PMID:17289569	PBO:0100953	(Figure 4B)
PMID:17289569	PBO:0100956	(Figure 4B) We found that Clr3 localization at telomere ends was completely abolished in cells defective in both Taz1 and RNAi pathways.
PMID:17289569	PBO:0100955	(Figure 4B) However, defect in RNAi pathway had no impact on Ccq1 localization
PMID:17289569	PBO:0100952	(comment: part of TGS)
PMID:17289569	PBO:0095651	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	PBO:0095651	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	PBO:0095651	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	PBO:0095651	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	PBO:0094681	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	FYPO:0000966	(Figure 5B) we found increases in H3K14ac levels and greater Pol II occupancy at the reporter embedded within pericentromeric heterochromatin in....strains lacking SHREC components
PMID:17289569	PBO:0112083	(Figure 5B) we found increases in H3K14ac levels and greater Pol II occupancy at the reporter embedded within pericentromeric heterochromatin in....strains lacking SHREC components
PMID:17289569	PBO:0100962	The role of SHREC in transcriptional silencing could be decoupled from the cis-PTGS function of the RNAi machinery since impaired SHREC had no effect on the localization of RITS Agol subunit at heterochromatin (Figure 5D).
PMID:17289569	FYPO:0002836	(Figure 5E). Enhanced transcriptional-machinery occupancy at heterochromatic repeats in SHREC defective cells,..should result in elevated repeat transcripts ...corresponding increase in siRNA production.
PMID:17289569	FYPO:0002836	(Figure 5E). Enhanced transcriptional-machinery occupancy at heterochromatic repeats in SHREC defective cells,..should result in elevated repeat transcripts ...corresponding increase in siRNA production.
PMID:17289569	FYPO:0002836	(Figure 5E). Enhanced transcriptional-machinery occupancy at heterochromatic repeats in SHREC defective cells,..should result in elevated repeat transcripts ...corresponding increase in siRNA production.
PMID:17289569	FYPO:0002836	(Figure 5E). Enhanced transcriptional-machinery occupancy at heterochromatic repeats in SHREC defective cells,..should result in elevated repeat transcripts ...corresponding increase in siRNA production.
PMID:17289569	PBO:0094283	(Figure 6A) both clr3D232N and mit1K587A mutant alleles alleviated silencing of a marker gene inserted at pericentromeric repeats
PMID:17289569	PBO:0094283	(Figure 6A) both clr3D232N and mit1K587A mutant alleles alleviated silencing of a marker gene inserted at pericentromeric repeats
PMID:17289569	PBO:0095651	(Figure 6B)
PMID:17289569	PBO:0095651	(Figure 6B)
PMID:17289569	FYPO:0000966	(Figure 5B) we found increases in H3K14ac levels and greater Pol II occupancy at the reporter embedded within pericentromeric heterochromatin in....strains lacking SHREC components
PMID:17289569	PBO:0094681	(Figure 6B)
PMID:17289569	PBO:0094681	(Figure 6B)
PMID:17289569	GO:0031508	(comment: by TGS)
PMID:17289569	FYPO:0003704	(Figure 6D)
PMID:17289569	FYPO:0000966	(Figure 5B) we found increases in H3K14ac levels and greater Pol II occupancy at the reporter embedded within pericentromeric heterochromatin in....strains lacking SHREC components
PMID:17289569	FYPO:0000966	(Figure 5B) we found increases in H3K14ac levels and greater Pol II occupancy at the reporter embedded within pericentromeric heterochromatin in....strains lacking SHREC components
PMID:17289569	PBO:0094681	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	PBO:0094681	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	PBO:0094283	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	PBO:0094283	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	PBO:0094283	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	PBO:0094283	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	PBO:0094681	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	PBO:0100960	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	PBO:0100960	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	PBO:0100960	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	PBO:0100960	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	PBO:0094688	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	PBO:0100959	In contrast to heterochromatic loci, SHREC recruitment to euchromatic sites was unaffected in the absence of Swi6, as shown by Clr3 and Mit1 localization at a locus encoding a noncoding RNA and an intergenic region (Figure 4D).
PMID:17289569	PBO:0100958	In contrast to heterochromatic loci, SHREC recruitment to euchromatic sites was unaffected in the absence of Swi6, as shown by Clr3 and Mit1 localization at a locus encoding a noncoding RNA and an intergenic region (Figure 4D).
PMID:17289569	PBO:0100957	(Figure 4C), Levels of Clr3 and Mit1 were dramatically reduced at subtelomeres in swi6 mutant strains
PMID:17289569	FYPO:0001168	(Figure 6D)
PMID:17289569	FYPO:0000853	(Figure 6E)
PMID:17289569	GO:0031509	(comment: by TGS)
PMID:17289569	GO:0030466	(comment: by TGS)
PMID:17289569	GO:0000183	(comment: by TGS)
PMID:17289569	GO:0031509	(comment: by TGS)
PMID:17289569	GO:0031509	(comment: by TGS)
PMID:17289569	GO:0031509	(comment: by TGS)
PMID:17289569	GO:0030466	(comment: by TGS)
PMID:17289569	GO:0030466	(comment: by TGS)
PMID:17289569	GO:0030466	(comment: by TGS)
PMID:17289569	GO:0000183	(comment: by TGS)
PMID:17289569	GO:0031508	(comment: by TGS)
PMID:17289569	GO:0031508	(comment: by TGS)
PMID:17289569	GO:0031508	(comment: by TGS)
PMID:17304215	GO:0005634	(Figure 1A) In normally growing cells, Swi5-EGFP localized to the nucleus and exhibited diffuse nuclear staining with a few distinct foci
PMID:17304215	PBO:0111971	On the other hand, the nuclei of sfr1D cells contained Swi5-EGFP foci
PMID:17304215	GO:0005634	(Figure 2A)
PMID:17304215	PBO:0111973	(Figure 1B) The absence of Swi2 or Sfr1 did not affect the cellular expression level of the Swi5-EGFP protein .
PMID:17304215	PBO:0111973	(Figure 1B) The absence of Swi2 or Sfr1 did not affect the cellular expression level of the Swi5-EGFP protein .
PMID:17304223	FYPO:0005165	(comment: CHECK foci disappear in HU; without HU foci appear but with abnormal dynamics)
PMID:17304223	FYPO:0005165	(comment: CHECK foci disappear in HU; without HU foci appear but with abnormal dynamics)
PMID:17307401	PBO:0093616	(comment: same as mus81delta alone)
PMID:17307401	PBO:0093613	(comment: worse than either single mutant)
PMID:17307401	PBO:0093580	(comment: worse than either single mutant)
PMID:17307401	PBO:0093630	(comment: same as mus81delta alone)
PMID:17307401	PBO:0093613	(comment: worse than either single mutant)
PMID:17307401	PBO:0093616	(comment: worse than either single mutant)
PMID:17307401	PBO:0093560	(comment: worse than either single mutant)
PMID:17307401	PBO:0093629	(comment: worse than either single mutant)
PMID:17307401	PBO:0093580	(comment: same as mus81delta alone)
PMID:17307401	PBO:0093613	(comment: same as mus81delta alone)
PMID:17307401	PBO:0093616	(comment: worse than either single mutant)
PMID:17307401	PBO:0093629	(comment: worse than either single mutant)
PMID:17310250	PBO:0105770	(Fig. 1C)
PMID:17310250	GO:0005634	(Fig. 3A)
PMID:17310250	FYPO:0002835	(Fig. 2C)
PMID:17310250	GO:0005737	(Fig. 3A)
PMID:17310250	PBO:0112828	Nonetheless Arb1, by itself and/or together with Arb2, is a direct inhibitor of the slicer activity of fission yeast Ago1. Fig. 4D
PMID:17310250	FYPO:0006992	(Fig. 5B)
PMID:17310250	FYPO:0004201	(Fig. 5C)
PMID:17310250	FYPO:0004201	(Fig. 5C)
PMID:17310250	FYPO:0004743	(Fig. 6A)
PMID:17310250	FYPO:0004743	(Fig. 6A)
PMID:17310250	PBO:0120503	(Fig. 6A)
PMID:17310250	PBO:0120504	(Fig. 6A)
PMID:17310250	PBO:0112834	(Fig. 6A)
PMID:17310250	PBO:0112834	(Fig. 6A)
PMID:17310250	GO:0005721	(Fig. 2E)
PMID:17310250	PBO:0105770	(Fig. 1C)
PMID:17310250	PBO:0120501	(Fig. 1D)
PMID:17310250	PBO:0095652	(Fig. 1C)
PMID:17310250	PBO:0098773	(Fig. 1D)
PMID:17310250	PBO:0098773	(Fig. 1D)
PMID:17310250	PBO:0095652	(Fig. 1C)
PMID:17310250	PBO:0105770	(Fig. 1C)
PMID:17310250	PBO:0120501	(Fig. 1D)
PMID:17310250	GO:0005721	(Fig. 2D and E)
PMID:17310250	PBO:0104710	(Fig. 5B)
PMID:17310250	PBO:0105770	(Fig. 5B)
PMID:17310250	PBO:0104710	(Fig. 5B)
PMID:17310250	PBO:0112829	These results indicate that the slicer activity of Ago1 is required for the in vivo conversion of double-stranded siRNA to single-stranded siRNA
PMID:17310250	PBO:0120502	(Fig. 6A)
PMID:17310250	PBO:0120502	(Fig. 6A)
PMID:17310250	PBO:0120502	(Fig. 6A)
PMID:17310250	PBO:0112831	(Fig. 6A)
PMID:17310250	PBO:0098760	(Fig. 6A)
PMID:17310250	PBO:0098773	(Fig. 6A)
PMID:17317928	FYPO:0001382	(comment: assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25)
PMID:17317928	FYPO:0001382	(comment: assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25)
PMID:17317928	FYPO:0002700	(comment: assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25)
PMID:17317928	FYPO:0003075	(comment: assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25)
PMID:17317928	FYPO:0002700	(comment: assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25)
PMID:17317928	FYPO:0002700	(comment: assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25)
PMID:17339332	GO:0006357	(comment: same pathway)
PMID:17352737	FYPO:0004439	(comment: CHECK anaphase, elongating beyond cell end resulting in long curved spindle, requested)
PMID:17363370	PBO:0107148	(Fig. 5D)
PMID:17363370	FYPO:0005071	Interestingly, the H2B-K119R mutation significantly enhanced silencing of the otr1::ura4+ (Fig. 5A)
PMID:17363370	PBO:0107147	(Fig. 4A,B)
PMID:17363370	FYPO:0002360	(Fig. 4A,B)
PMID:17363370	PBO:0107147	(Fig. 4A,B)
PMID:17363370	FYPO:0002360	(Fig. 4A,B)
PMID:17363370	PBO:0107147	(Fig. 4A,B)
PMID:17363370	FYPO:0002360	(Fig. 4A,B)
PMID:17363370	FYPO:0007843	(supplemental Fig. 2)
PMID:17363370	PBO:0107146	Interestingly, levels of trimethylated H3K9 (H3K9me3) were significantly reduced, although the levels of monomethylated H3K9 (H3K9me1) were increased at the dg repeat element and otr1::ura4+ (Fig. 3B).
PMID:17363370	FYPO:0007844	Interestingly, levels of trimethylated H3K9 (H3K9me3) were significantly reduced, although the levels of monomethylated H3K9 (H3K9me1) were increased at the dg repeat element and otr1::ura4+ (Fig. 3B).
PMID:17363370	FYPO:0007334	Overexpression of Rhp6 abrogates silencing of the otr1::ura4+ reporter, resulting in the loss of cell viability on medium supplemented with FOA (Fig. 3A)
PMID:17363370	FYPO:0006299	(Figure 2d) Δrhp6 resulted in enhanced silencing of the otr1::ura4+, as shown by reduced growth on medium lacking uracil (Fig. 2D)
PMID:17363370	FYPO:0006299	(Figure 2d) Δrhp6 resulted in enhanced silencing of the otr1::ura4+, as shown by reduced growth on medium lacking uracil (Fig. 2D)
PMID:17363370	FYPO:0006299	(Figure 2d) Δrhp6 resulted in enhanced silencing of the otr1::ura4+, as shown by reduced growth on medium lacking uracil (Fig. 2D)
PMID:17363370	FYPO:0006299	(Figure 2d) Δrhp6 resulted in enhanced silencing of the otr1::ura4+, as shown by reduced growth on medium lacking uracil (Fig. 2D)
PMID:17363370	FYPO:0002922	(Figure 2b)
PMID:17363370	FYPO:0002922	(Figure 2b)
PMID:17363370	FYPO:0002922	(Figure 2b)
PMID:17363370	FYPO:0002922	(Figure 2b)
PMID:17363370	FYPO:0002922	(Figure 2b)
PMID:17363370	PBO:0107145	HULC revealed that slower migrating band representing ubH2B was missing in cells lacking either Bre1 homologs (i.e. Rfp1 or Rfp2) or Shf1. These analyses suggest that components of HULC are required for ubiquitination of H2B.
PMID:17363370	PBO:0107145	HULC revealed that slower migrating band representing ubH2B was missing in cells lacking either Bre1 homologs (i.e. Rfp1 or Rfp2) or Shf1. These analyses suggest that components of HULC are required for ubiquitination of H2B.
PMID:17363370	PBO:0020446	(Fig. 1D)
PMID:17363370	PBO:0020446	(Fig. 1D)
PMID:17363370	PBO:0107149	(Fig. 5D)
PMID:17363370	PBO:0020446	(Fig. 1D)
PMID:17363370	PBO:0020446	(Fig. 1D)
PMID:17363370	PBO:0020446	(Fig. 1D)
PMID:17363370	GO:0033503	(Fig. 1C)
PMID:17363370	GO:0033503	(Fig. 1C)
PMID:17363370	GO:0033503	(Fig. 1C)
PMID:17363370	GO:0033503	(Fig. 1C)
PMID:17369611	PBO:0111587	However, H3-K56R, rtt109Δ, and the H3-K56R/rtt109Δ mutant cells formed colonies of variable pink indicating a slight decrease in silencing at centromeres (Fig. 4A). This might indicate a cross-talk of H3 Lys-56-Ac with the establishment or the maintenance of other activating or repressing histone modifications required for proper centromeric heterochromatin formation.
PMID:17371846	GO:0140720	in peaks in the subtelomeric regions of chromosomes 1 and 2
PMID:17371846	FYPO:0002150	We found that saf140, saf60, and saf50 are essential genes, as viability segregated 2:2 in four-spore tetrads
PMID:17371846	FYPO:0002150	We found that saf140, saf60, and saf50 are essential genes, as viability segregated 2:2 in four-spore tetrads
PMID:17371846	FYPO:0002150	We found that saf140, saf60, and saf50 are essential genes, as viability segregated 2:2 in four-spore tetrads
PMID:17371846	PBO:0093560	(Fig. 2A)
PMID:17371846	FYPO:0004481	(Fig. 2A)
PMID:17371846	FYPO:0001357	(Fig. 2C)
PMID:17371846	FYPO:0001357	(Fig. 2C)
PMID:17371846	FYPO:0001357	(Fig. 2C)
PMID:17371846	PBO:0096647	(Fig. 2C)
PMID:17371846	PBO:0094949	(Fig. 2C)
PMID:17371846	PBO:0094949	(Fig. 2C)
PMID:17371846	FYPO:0000674	(Fig. 2C)
PMID:17371846	GO:0000785	In general, we found SAPHIRE distributed widely throughout the genome and dispersed at genes over all three chromosome arms.
PMID:17371846	GO:0000785	In general, we found SAPHIRE distributed widely throughout the genome and dispersed at genes over all three chromosome arms.
PMID:17371846	GO:0000785	In general, we found SAPHIRE distributed widely throughout the genome and dispersed at genes over all three chromosome arms.
PMID:17371846	GO:0000785	In general, we found SAPHIRE distributed widely throughout the genome and dispersed at genes over all three chromosome arms.
PMID:17371846	GO:0031934	we observed SAPHIRE in the region of the silent mating (MAT) locus
PMID:17371846	GO:0031934	we observed SAPHIRE in the region of the silent mating (MAT) locus
PMID:17371846	GO:0031934	we observed SAPHIRE in the region of the silent mating (MAT) locus
PMID:17371846	GO:0031934	we observed SAPHIRE in the region of the silent mating (MAT) locus
PMID:17371846	GO:0140720	in peaks in the subtelomeric regions of chromosomes 1 and 2
PMID:17371846	GO:0140720	in peaks in the subtelomeric regions of chromosomes 1 and 2
PMID:17371846	GO:0140720	in peaks in the subtelomeric regions of chromosomes 1 and 2
PMID:17371846	GO:0005721	In addition, SAPHIRE occupies the junctions between the central region of the centromeres and the dg/dh repeats
PMID:17371846	GO:0005721	In addition, SAPHIRE occupies the junctions between the central region of the centromeres and the dg/dh repeats
PMID:17371846	GO:0005721	In addition, SAPHIRE occupies the junctions between the central region of the centromeres and the dg/dh repeats
PMID:17371846	GO:0005721	In addition, SAPHIRE occupies the junctions between the central region of the centromeres and the dg/dh repeats
PMID:17371846	PBO:0112936	(Fig. 4B)
PMID:17371846	PBO:0112937	(Fig. 4B)
PMID:17371846	FYPO:0005225	(Fig. 4C)
PMID:17371846	FYPO:0006361	(Fig. 5)
PMID:17412958	FYPO:0003210	(Fig. 3D)
PMID:17412958	FYPO:0006213	(Fig. 3D)
PMID:17412958	PBO:0093561	(Fig. 3C)
PMID:17412958	PBO:0093554	(Fig. 3C)
PMID:17412958	PBO:0093555	(Fig. 3C)
PMID:17412958	PBO:0093561	(Fig. 3C)
PMID:17412958	PBO:0093555	(Fig. 3C)
PMID:17412958	PBO:0093555	(Fig. 3C)
PMID:17412958	PBO:0093558	(Fig. 3A)
PMID:17412958	PBO:0093558	(Fig. 3A)
PMID:17412958	PBO:0093560	(Fig. 3A)
PMID:17412958	FYPO:0000123	(Fig. 3B)
PMID:17412958	FYPO:0000647	(Fig. 3B)
PMID:17412958	FYPO:0001315	(Fig. 3B)
PMID:17412958	FYPO:0003210	(Fig. 3D)
PMID:17412958	FYPO:0003210	(Fig. 3D)
PMID:17434129	GO:0006338	(comment: also from localization and phenotypes)
PMID:17434129	GO:0006338	(comment: also from localization and phenotypes)
PMID:17434129	FYPO:0002061	data not shown
PMID:17434129	FYPO:0002061	data not shown
PMID:17434129	PBO:0107043	(comment: TEL2L only)
PMID:17434129	PBO:0100344	(comment: TEL2L only)
PMID:17434129	FYPO:0007508	(comment: TEL2L only()
PMID:17440621	PBO:0108790	(comment: they only show that this is part of a complex that demethylates H3K9 so there is a chance it is not active?)
PMID:17442892	FYPO:0002638	(comment: inferred from the fact growth is impaired in the double mutant spc7-23/mad2 OR spc7-23/mph1 are growth impaired, so assumption is that spindle checkpoint is active in mutant)
PMID:17450151	FYPO:0003557	(comment: bulk antisense transcripts)
PMID:17450151	FYPO:0002355	(comment: bulk antisense transcripts)
PMID:17450151	FYPO:0004137	(comment: bulk antisense transcripts)
PMID:17450151	FYPO:0000888	(comment: bulk antisense transcripts)
PMID:17450151	FYPO:0003547	(comment: bulk antisense transcripts)
PMID:17450151	FYPO:0006987	(comment: bulk antisense transcripts)
PMID:17450151	FYPO:0006361	(comment: bulk antisense transcripts)
PMID:17450151	FYPO:0000887	(comment: bulk antisense transcripts)
PMID:17450151	FYPO:0005315	(comment: bulk antisense transcripts)
PMID:17450151	FYPO:0005523	(comment: bulk antisense transcripts)
PMID:17450151	PBO:0095841	(comment: sense strand)
PMID:17450151	PBO:0095840	(comment: sense strand)
PMID:17452352	PBO:0102193	"(comment: chromatin binding shown, and regulation of transcription shown. no evidence for dna binding BUT later paper by akayama and Toda state that "" Ams2 directly binds a consensus ""AACCCT-box"" that exists in the 5' franking regions of these histone genes."" and says that ams2 is sole responsible TF + cites this paper)"
PMID:17452352	PBO:0099053	(Fig. 5c)
PMID:17452352	PBO:0099052	(Fig. 5c)
PMID:17452352	PBO:0099051	(Fig. 5c)
PMID:17452352	PBO:0099054	(Fig. 5c)
PMID:17452352	PBO:0099055	(Fig. 5c)
PMID:17452352	GO:0045944	(comment: CHECK bet this is a term Val hates :p)
PMID:17452352	PBO:0102186	(Figure 5a)
PMID:17452352	PBO:0102187	(Figure 5a)
PMID:17452352	PBO:0099054	(Figure 5d)
PMID:17452352	PBO:0099051	(Figure 5d)
PMID:17452352	PBO:0099050	(Fig. 5c)
PMID:17452352	PBO:0099040	(Fig. 6)
PMID:17452352	PBO:0099041	(Fig. 6)
PMID:17452352	PBO:0099039	(Fig. 6)
PMID:17452352	PBO:0099042	(Fig. 6)
PMID:17452352	PBO:0099053	(Figure 5d)
PMID:17452352	PBO:0099050	(Figure 5d)
PMID:17452352	PBO:0099055	(Figure 5d)
PMID:17452352	PBO:0099052	(Figure 5d)
PMID:17452352	PBO:0102188	(Figure 7)
PMID:17452352	PBO:0102186	(Figure 7)
PMID:17452352	PBO:0102189	(Figure 7)
PMID:17452352	PBO:0102190	(Figure 7)
PMID:17452352	PBO:0102187	(Figure 7)
PMID:17452352	PBO:0102191	(Figure 7)
PMID:17452352	PBO:0102190	(Figure 7)
PMID:17452352	PBO:0102186	(Figure 7)
PMID:17452352	PBO:0102189	(Figure 7)
PMID:17452352	PBO:0102187	(Figure 7)
PMID:17452352	PBO:0102191	(Figure 7)
PMID:17452352	PBO:0102192	"(comment: chromatin binding shown, and regulation of transcription shown. no evidence for dna binding BUT later paper by akayama and Toda state that "" Ams2 directly binds a consensus ""AACCCT-box"" that exists in the 5' franking regions of these histone genes."" and says that ams2 is sole responsible TF + cites this paper)"
PMID:17452352	PBO:0102188	(Figure 7)
PMID:17452625	GO:1904530	(comment: regulates binding by myosin; assayed in vitro using rabbit actin and unspecified myosin motor domain)
PMID:17486116	FYPO:0002638	(comment: CHECK assayed using bub1)
PMID:17510629	FYPO:0007656	Hence, from these results it was evident that Hrp1, Hrp3 and Nap1 occupancy in vivo generally correlated with increased nucleosome densities in the corresponding mutants, and that this effect was most pronounced in promoter regions.
PMID:17510629	FYPO:0007656	Hence, from these results it was evident that Hrp1, Hrp3 and Nap1 occupancy in vivo generally correlated with increased nucleosome densities in the corresponding mutants, and that this effect was most pronounced in promoter regions.
PMID:17510629	FYPO:0007656	Hence, from these results it was evident that Hrp1, Hrp3 and Nap1 occupancy in vivo generally correlated with increased nucleosome densities in the corresponding mutants, and that this effect was most pronounced in promoter regions.
PMID:17512405	GO:0031499	Cid14 copurified with two proteins that are homologs of Mtr4 and Air1 (Figures 4A and 4B). Thus, like Trf4 in S. cerevisiae, Cid14 is found in a complex together with Air1 and Mtr4, which we refer to as spTRAMP (S. pombe TRAMP).
PMID:17512405	PBO:0105941	Like cid14D, Cid14 active site mutations had dramatically reduced centromeric siRNA levels (Figure 6D)
PMID:17512405	PBO:0105941	While we were not able to detect any centromeric siRNAs in cid12D cells, centromeric siRNAs were about 22-fold reduced in cid14D compared to wild-type cells (Figure 6B). and However, centromeric siRNAs from cid14D were barely detectable on total RNA northern blots (Figure 6A).
PMID:17512405	PBO:0110934	we observed 7-fold and a 25-fold increases in tlh1+ transcript levels in rrp6D and dis3-54 cells, respectively, and 33- and 100- fold increases in cid14D and clr4D cells, respectively (Figures 4G and S3)
PMID:17512405	PBO:0111106	Quantification of the signals revealed that Ago1 contained about 3-fold more antisense than sense ura4+ siRNAs. etc....(Figure 1)
PMID:17512405	FYPO:0007334	We found that deletion of cid14+ resulted in a complete loss of ura4+ silencing at all the tested loci as assayed by growth on 5-FOA-containing medium (Figures 2A-2C).
PMID:17512405	FYPO:0007335	We found that deletion of cid14+ resulted in a complete loss of ura4+ silencing at all the tested loci as assayed by growth on 5-FOA-containing medium (Figures 2A-2C).
PMID:17512405	FYPO:0007336	We found that deletion of cid14+ resulted in a complete loss of ura4+ silencing at all the tested loci as assayed by growth on 5-FOA-containing medium (Figures 2A-2C).
PMID:17512405	FYPO:0006995	Finally, deletion of the other four members of the fission yeast Cid14/Trf4/5 poly(A) polymerase family did not affect silencing of an imr1R::ura4+ reporter gene (Figure 2H).
PMID:17512405	FYPO:0006995	Finally, deletion of the other four members of the fission yeast Cid14/Trf4/5 poly(A) polymerase family did not affect silencing of an imr1R::ura4+ reporter gene (Figure 2H).
PMID:17512405	FYPO:0006995	Finally, deletion of the other four members of the fission yeast Cid14/Trf4/5 poly(A) polymerase family did not affect silencing of an imr1R::ura4+ reporter gene (Figure 2H).
PMID:17512405	FYPO:0006995	Finally, deletion of the other four members of the fission yeast Cid14/Trf4/5 poly(A) polymerase family did not affect silencing of an imr1R::ura4+ reporter gene (Figure 2H).
PMID:17512405	PBO:0110924	Surprisingly, in cid14D cells, neither Chp1 nor Swi6 binding was significantly reduced at several heterochromatic loci, including mat3M::ura4+, imr1R::ura4+, the subtelomeric tlh1+ gene, and cen-dg and cen-dh repeats, as assayed by chromatin immunoprecipitation experiments (ChIP) (Figures 3A and 3B).
PMID:17512405	PBO:0110925	Surprisingly, in cid14D cells, neither Chp1 nor Swi6 binding was significantly reduced at several heterochromatic loci, including mat3M::ura4+, imr1R::ura4+, the subtelomeric tlh1+ gene, and cen-dg and cen-dh repeats, as assayed by chromatin immunoprecipitation experiments (ChIP) (Figures 3A and 3B).
PMID:17512405	PBO:0110926	Surprisingly, in cid14D cells, neither Chp1 nor Swi6 binding was significantly reduced at several heterochromatic loci, including mat3M::ura4+, imr1R::ura4+, the subtelomeric tlh1+ gene, and cen-dg and cen-dh repeats, as assayed by chromatin immunoprecipitation experiments (ChIP) (Figures 3A and 3B).
PMID:17512405	PBO:0110927	Surprisingly, in cid14D cells, neither Chp1 nor Swi6 binding was significantly reduced at several heterochromatic loci, including mat3M::ura4+, imr1R::ura4+, the subtelomeric tlh1+ gene, and cen-dg and cen-dh repeats, as assayed by chromatin immunoprecipitation experiments (ChIP) (Figures 3A and 3B).
PMID:17512405	PBO:0110928	Surprisingly, in cid14D cells, neither Chp1 nor Swi6 binding was significantly reduced at several heterochromatic loci, including mat3M::ura4+, imr1R::ura4+, the subtelomeric tlh1+ gene, and cen-dg and cen-dh repeats, as assayed by chromatin immunoprecipitation experiments (ChIP) (Figures 3A and 3B).
PMID:17512405	PBO:0110929	Surprisingly, in cid14D cells, neither Chp1 nor Swi6 binding was significantly reduced at several heterochromatic loci, including mat3M::ura4+, imr1R::ura4+, the subtelomeric tlh1+ gene, and cen-dg and cen-dh repeats, as assayed by chromatin immunoprecipitation experiments (ChIP) (Figures 3A and 3B).
PMID:17512405	PBO:0110930	In addition, while H3K9 methylation was lost in clr4D cells, only a slight reduction in H3K9 methylation was observed in cid14D cells (Figures 3A and 3B)
PMID:17512405	PBO:0110931	Furthermore, consistent with a CTGS model for silencing of mat3M::ura4+, none of the tested mutants affected RNApII occupancy at this locus (Figure 3C).
PMID:17512405	GO:0031499	Cid14 copurified with two proteins that are homologs of Mtr4 and Air1 (Figures 4A and 4B). Thus, like Trf4 in S. cerevisiae, Cid14 is found in a complex together with Air1 and Mtr4, which we refer to as spTRAMP (S. pombe TRAMP).
PMID:17512405	FYPO:0007334	Loss of imr1R::ura4+ and mat3M::ura4+ silencing in cid14D cells could be rescued by overexpressing Cid14wt (pRep- Cid14) but not by Cid14DADA (pRep-Cid14DADA) (Figure 5F).
PMID:17512405	GO:0033895	In order to directly determine whether Cid14 is a bona fide poly(A) polymerase, we assayed recombinant wild-type or mutant Cid14 (GST-Cid14wt or GST-Cid14DADA, respectively; Figure 5A) for polyadenylation activity in vitro and found that wild-type Cid14 was able to extend a synthetic oligo(A)15 RNAno activity was detected in the presence of pyrimidines (CTP or UTP) (Figure 5D).
PMID:17512405	PBO:0110936	Importantly, Cid14 activity was completely abolished in Cid14DADA (Figure 5B)
PMID:17512405	GO:1990817	In order to directly determine whether Cid14 is a bona fide poly(A) polymerase, we assayed recombinant wild-type or mutant Cid14 (GST-Cid14wt or GST-Cid14DADA, respectively; Figure 5A) for polyadenylation activity in vitro and found that wild-type Cid14 was able to extend a synthetic oligo(A)15 RNA but not an oligo(dA)15 DNA substrate (Figures 5B, 5C, and 5E).
PMID:17512405	PBO:0110935	we observed a 3-fold increase in tlh1+ RNA levels in dcr1D cells and a 10-fold increase in mtr4-1 cells (Figures 4F and 4H), indicating that both RNAi and TRAMP contribute to the full silencing of this subtelomeric gene.
PMID:17512405	PBO:0110935	we observed a 3-fold increase in tlh1+ RNA levels in dcr1D cells and a 10-fold increase in mtr4-1 cells (Figures 4F and 4H), indicating that both RNAi and TRAMP contribute to the full silencing of this subtelomeric gene.
PMID:17512405	GO:0031499	Cid14 copurified with two proteins that are homologs of Mtr4 and Air1 (Figures 4A and 4B). Thus, like Trf4 in S. cerevisiae, Cid14 is found in a complex together with Air1 and Mtr4, which we refer to as spTRAMP (S. pombe TRAMP).
PMID:17512405	FYPO:0002335	We found that the deletion of air1+ had no effect on heterochromatic gene silencing (Figure S2
PMID:17512405	FYPO:0007336	However, we observed loss of silencing of mat3M:::ura4+ in cells carrying a hypomorphic allele of mtr4+ (mtr4-1, Figures 4F and 4H), suggesting the involvement of a TRAMP-like complex.
PMID:17512405	PBO:0110932	Consistent with a role for the exosome in degrading heterochromatic ura4+ transcripts, we observed elevated ura4+ transcript levels in rrp6D compared to wild-type cells (Figures 4C-4E).
PMID:17512405	FYPO:0002834	(Figure 2,4)
PMID:17512405	FYPO:0002834	(Figure 2,4)
PMID:17512405	FYPO:0002834	(Figure 2,4)
PMID:17512405	FYPO:0004604	we observed 7-fold and a 25-fold increases in tlh1+ transcript levels in rrp6D and dis3-54 cells, respectively, and 33- and 100- fold increases in cid14D and clr4D cells, respectively (Figures 4G and S3)
PMID:17512405	PBO:0110933	we observed 7-fold and a 25-fold increases in tlh1+ transcript levels in rrp6D and dis3-54 cells, respectively, and 33- and 100- fold increases in cid14D and clr4D cells, respectively (Figures 4G and S3)
PMID:17512405	PBO:0110934	we observed 7-fold and a 25-fold increases in tlh1+ transcript levels in rrp6D and dis3-54 cells, respectively, and 33- and 100- fold increases in cid14D and clr4D cells, respectively (Figures 4G and S3)
PMID:17531813	PBO:0108401	(Fig. 4A)
PMID:17531813	PBO:0108402	(Fig. 4D) In the absence of rad26, cdc18 is unable to stabilise rad3 on chromatin
PMID:17531813	PBO:0108403	(Fig. 5A) cdc18 disappears at the end of S-phase in cig2+ strain and accumulates in the absence of cig2
PMID:17531813	PBO:0105277	(Fig. 5B)
PMID:17531813	PBO:0108404	(Fig. 5B)
PMID:17531813	PBO:0108405	(Fig. 6B)
PMID:17531813	PBO:0094961	(Fig. 6B)
PMID:17531813	PBO:0108392	(Fig. 1C)
PMID:17531813	PBO:0108394	(Figure 2B) rad3 is not present in the chromatin fraction in the absence of cdc18
PMID:17531813	PBO:0108395	(Figure 2B) In the cytosol rad3 is present in absence of cdc18
PMID:17531813	PBO:0092600	(Fig. 2A)
PMID:17531813	PBO:0108410	The same experiment was repeated, but HU was added at the time of release, allowing cells to progress through mitosis and stall after initiation of DNA replication. In that case, Cdc2 tyrosine 15 phosphorylation reappeared after 100 min and increased further with time. Cig2 remained present at a high level, indicating that the Cdc2-Cig2 complex was inhibited (Figure 5B)
PMID:17531813	PBO:0098712	(Fig. 1C)
PMID:17531813	PBO:0108396	(Figure 2C) cds1 is no longer phosphorylated because rad3 is absent in absence of cdc18
PMID:17531813	PBO:0108397	(Figure 2D)
PMID:17531813	PBO:0108392	(Fig. 1B)
PMID:17531813	PBO:0108392	(Fig. 1B)
PMID:17531813	PBO:0108398	(Figure 3) Replication Structures Are Not Lost When Cdc18 Is Depleted)
PMID:17531813	PBO:0108399	(Fig. 4A)
PMID:17531813	PBO:0108399	(Fig. 4A)
PMID:17531813	PBO:0108400	(Fig. 4A)
PMID:17531813	PBO:0108406	(Fig. 6B)
PMID:17531813	PBO:0108409	(Fig. 1C)
PMID:17531813	PBO:0108393	(Fig. 1C) (comment: vw data not shown, but assume are elongated)
PMID:17531813	PBO:0092600	(Fig. 2A) (comment: CHECK during mitotic DNA replication checkpoint)
PMID:17531813	PBO:0108392	(Fig. 1C)
PMID:17531816	PBO:0101401	We have previously demonstrated that Tas3 binds directly to Chp1 (Petrie et al., 2005). In addition, Tas3 binds to Ago1 and this interaction is independent of Chp1 (Figure 1A). Thus, Tas3 forms a bridge linking the Chp1 chromodomain protein to Ago1.
PMID:17531816	PBO:0094679	(dg repeat) Centromeric transcripts were only marginally elevated in tas3WG cells, in marked contrast to the 10- to 20-fold accumulation of transcripts in tas3-, dcr1-, or ago1-null cells (Figure 2B).
PMID:17531816	FYPO:0001513	Consistent with these findings, tas3WG mutant cells showed no defects in chromosome segregation (Table S2).
PMID:17531816	PBO:0101405	Chromatin immunoprecipitation (ChIP) analyses showed that Ago1 was indeed localized at centromeres in the tas3WG mutant, a
PMID:17531816	FYPO:0002837	Further, centromeric siRNAs were similarly abundant in tas3WG and tas3+ cells (Figure 2D).
PMID:17531816	PBO:0101406	......as were Chp1 and the mutant Tas3WG protein (Figure 2C).
PMID:17531816	PBO:0101407	......as were Chp1 and the mutant Tas3WG protein (Figure 2C).
PMID:17531816	PBO:0094679	F276A-ago1 (Figure S3B) caused a slight defect in silencing of the dg cen::ura4+ reporter (Figure S3C).
PMID:17531816	PBO:0094684	the double mutant (tas3WG, F276Aago1) displayed markedly elevated levels of total centromeric transcripts (Figure 2E), similar to an ago1 null.
PMID:17531816	FYPO:0006076	centromeric siRNAs were present in the F276Aago1 and tas3WG single mutants but were undetectable in the double mutant (Figure 2F).
PMID:17531816	FYPO:0003241	centromeric siRNAs were present in the F276Aago1 and tas3WG single mutants but were undetectable in the double mutant (Figure 2F).
PMID:17531816	GO:0031508	The reestablishmentof centromeric heterochromatin was then monitored after reintroduction of clr4+. Addition of clr4+to tas3+ cells allowed efficient establishment of heterochromatinand silencing of the cen::ura4+ transgene atdg (Figure 3A). In marked contrast, on reintroduction ofclr4+, cells expressing tas3WG failed to silence the cen::ura4+ reporter
PMID:17531816	FYPO:0003098	Tas3WG Cells Cannot Efficiently Establish De Novo Centromeric Heterochromatin
PMID:17531816	FYPO:0004744	Tas3WG Cells Cannot Efficiently Establish De Novo Centromeric Heterochromatin
PMID:17538026	FYPO:0002060	(Fig. 1a)
PMID:17538026	PBO:0102471	(Fig. 6B)
PMID:17538026	PBO:0102471	(Fig. 6B)
PMID:17538026	PBO:0102470	(Fig. 4)
PMID:17538026	PBO:0102469	(Fig. 4)
PMID:17538026	PBO:0102469	(Fig. 4)
PMID:17538026	FYPO:0002061	(Table 2)
PMID:17538026	FYPO:0002061	(Table 2)
PMID:17538026	FYPO:0002060	(Fig. 1a)
PMID:17538026	PBO:0033837	(Figure 3, B and D)
PMID:17538026	GO:0005730	(Figure 3, B and D)
PMID:17538026	GO:0005730	(Fig. 3a)
PMID:17538026	FYPO:0004506	(Fig. 1B)
PMID:17538026	FYPO:0004506	(Fig. 1B)
PMID:17538026	PBO:0037119	(Fig. 1, 2)
PMID:17538026	PBO:0037118	(Fig. 1, 2)
PMID:17538026	FYPO:0002060	(Fig. 1a)
PMID:17538026	FYPO:0002061	(Fig. 1a)
PMID:17556368	PBO:0096993	(comment: CHECK get double mutant phenotypes)
PMID:17556368	PBO:0096992	(comment: CHECK get double mutant phenotypes)
PMID:17556368	PBO:0096991	(comment: CHECK get double mutant phenotypes)
PMID:17556368	PBO:0096990	(comment: CHECK get double mutant phenotypes)
PMID:17561805	FYPO:0002638	(comment: tested through observing no delay when checkpoint is inactivated)
PMID:17579515	FYPO:0001734	(Figure 3A and 3B, and Video S3)
PMID:17579515	FYPO:0003787	(Figure 2C) (comment: check (also nuclear envelope protrusion?)
PMID:17579515	FYPO:0004396	(Figure S4)
PMID:17579515	FYPO:0005380	(Figure S4; Figure 3A,B; Video S3)
PMID:17579515	FYPO:0004536	(APC) activation occurred and chromosome cohesion was lost (Figure 1A and 1B).
PMID:17579515	FYPO:0002061	(Fig. S1)
PMID:17579515	FYPO:0000619	(APC) activation occurred and chromosome cohesion was lost (Figure 1A and 1B).
PMID:17579515	PBO:0033900	(Figure 6C) (ablated Nuclear envelope)
PMID:17579515	PBO:0096906	(Figure 6C)
PMID:17579515	PBO:0096905	(Fig. 4G)
PMID:17579515	PBO:0096904	(Figure 1).
PMID:17596513	PBO:0115005	(comment: E. coli ispA mutant used as assay system)
PMID:17596513	PBO:0115004	(comment: E. coli ispA mutant used as assay system)
PMID:17596513	PBO:0115005	(comment: E. coli ispA mutant used as assay system)
PMID:17614284	PBO:0113691	Table S1
PMID:17614284	FYPO:0001357	(Fig. 2A)
PMID:17614284	PBO:0093554	(Fig. 2A)
PMID:17614284	PBO:0093557	(Fig. 2A)
PMID:17614284	PBO:0104709	(Fig. 2B)
PMID:17614284	PBO:0096188	(Fig. 2B)
PMID:17614284	PBO:0096191	(Fig. 2B)
PMID:17614284	PBO:0095653	(Fig. 2C)
PMID:17614284	FYPO:0008265	(Fig. 2C)
PMID:17614284	FYPO:0003555	(Fig. 2C)
PMID:17614284	PBO:0095058	(Fig. 3A, B)
PMID:17614284	PBO:0113641	(Fig. 3C)
PMID:17614284	PBO:0113642	(Fig. 3C)
PMID:17614284	PBO:0093562	(Fig. 3D)
PMID:17614284	GO:0140727	our results indicate that Pob3 function at the centromere does not appear to affect the production or accumulation of both unprocessed transcripts and siRNAs.
PMID:17614284	FYPO:0004743	(Fig. 4C)
PMID:17614284	PBO:0113643	(Fig. 4C)
PMID:17614284	FYPO:0002150	(Fig. S3)
PMID:17614284	PBO:0093581	(Fig. S6A)
PMID:17614284	PBO:0093614	(Fig. S6B)
PMID:17614284	PBO:0093631	(Fig. S6C)
PMID:17614284	PBO:0113644	(Fig. S6D)
PMID:17614284	PBO:0113644	(Fig. S6D)
PMID:17614284	PBO:0101148	(Fig. S6D)
PMID:17614284	PBO:0113645	Table S1
PMID:17614284	PBO:0113646	Table S1
PMID:17614284	PBO:0113647	Table S1
PMID:17614284	PBO:0113648	Table S1
PMID:17614284	PBO:0113649	Table S1
PMID:17614284	PBO:0113650	Table S1
PMID:17614284	PBO:0113651	Table S1
PMID:17614284	PBO:0113652	Table S1
PMID:17614284	PBO:0113653	Table S1
PMID:17614284	PBO:0113654	Table S1
PMID:17614284	PBO:0113655	Table S1
PMID:17614284	PBO:0113656	Table S1
PMID:17614284	PBO:0113657	Table S1
PMID:17614284	PBO:0113658	Table S1
PMID:17614284	PBO:0113659	Table S1
PMID:17614284	PBO:0113660	Table S1
PMID:17614284	PBO:0113661	Table S1
PMID:17614284	PBO:0113662	Table S1
PMID:17614284	PBO:0110747	Table S1
PMID:17614284	PBO:0110737	Table S1
PMID:17614284	PBO:0110745	Table S1
PMID:17614284	PBO:0113663	Table S1
PMID:17614284	PBO:0110744	Table S1
PMID:17614284	PBO:0113664	Table S1
PMID:17614284	PBO:0110761	Table S1
PMID:17614284	PBO:0113665	Table S1
PMID:17614284	PBO:0113666	Table S1
PMID:17614284	PBO:0113667	Table S1
PMID:17614284	PBO:0113668	Table S1
PMID:17614284	PBO:0113669	Table S1
PMID:17614284	PBO:0110767	Table S1
PMID:17614284	PBO:0113670	Table S1
PMID:17614284	PBO:0113672	Table S1
PMID:17614284	PBO:0113671	Table S1
PMID:17614284	PBO:0113673	Table S1
PMID:17614284	PBO:0113674	Table S1
PMID:17614284	PBO:0113675	Table S1
PMID:17614284	PBO:0113676	Table S1
PMID:17614284	PBO:0113677	Table S1
PMID:17614284	PBO:0113678	Table S1
PMID:17614284	PBO:0113679	Table S1
PMID:17614284	PBO:0113680	Table S1
PMID:17614284	PBO:0113681	Table S1
PMID:17614284	PBO:0113682	Table S1
PMID:17614284	PBO:0113683	Table S1
PMID:17614284	PBO:0113684	Table S1
PMID:17614284	PBO:0113685	Table S1
PMID:17614284	PBO:0113686	Table S1
PMID:17614284	PBO:0113687	Table S1
PMID:17614284	PBO:0113688	Table S1
PMID:17614284	PBO:0113689	Table S1
PMID:17614284	PBO:0113690	Table S1
PMID:17632059	FYPO:0003835	(Fig. S3)
PMID:17632059	FYPO:0003835	(Fig. S3)
PMID:17632059	PBO:0096125	Table S3
PMID:17632059	PBO:0096108	(Fig. 1B)
PMID:17632059	PBO:0096109	(Fig. 1B)
PMID:17632059	PBO:0096110	(Fig. 1B)
PMID:17632059	PBO:0096111	(Fig. 1B)
PMID:17632059	FYPO:0000485	(Fig. 1c)
PMID:17632059	FYPO:0000485	(Fig. 1c)
PMID:17632059	FYPO:0000485	(Fig. 1c)
PMID:17632059	FYPO:0006389	In taz1Dlig4D zygotes, SPBs move normally during the horsetail stage even though they are rarely associated with chromatin. However, as the horsetail stage ends and meiosis I begins, the Pcp1-GFP signals appear brighter than in WT cells and are markedly disorganized (Figure 2B; 75 min
PMID:17632059	FYPO:0006363	(Fig. 3)
PMID:17632059	PBO:0096117	(Fig. 3)
PMID:17632059	PBO:0096118	(Fig. 3)
PMID:17632059	PBO:0096119	(Fig. 3) (comment: V-shaped patterns indicating multiple spindles)
PMID:17632059	PBO:0096120	(Fig. 3)
PMID:17632059	PBO:0096121	(Fig. 3D)
PMID:17632059	PBO:0096122	Table S3
PMID:17632059	PBO:0096123	Table S3
PMID:17632059	PBO:0096124	Table S3
PMID:17632059	FYPO:0004077	(Fig. 1b)
PMID:17632059	FYPO:0000681	(Fig. 1c)
PMID:17632059	PBO:0096101	(Fig. 1c)
PMID:17632059	FYPO:0000681	(Fig. 1e) (comment: twice their share of DNA and SPBs.)
PMID:17632059	FYPO:0006383	(Fig. 1f)
PMID:17632059	PBO:0096102	(Fig. 1B)
PMID:17632059	PBO:0096103	(Fig. 1B)
PMID:17632059	PBO:0096104	(Fig. 1B)
PMID:17632059	PBO:0096105	(Fig. 1b)
PMID:17632059	PBO:0096131	(Fig. 3D) (I)
PMID:17632059	PBO:0096130	Table S3
PMID:17632059	FYPO:0006365	(comment: CHECK Matching synonym SPB detached from nucleuss fix syn)
PMID:17632059	PBO:0096126	(Fig. s4e, movie S2)
PMID:17632059	FYPO:0002890	(Fig. S3)
PMID:17632059	FYPO:0000927	(Fig. S3)
PMID:17632059	FYPO:0000927	(Fig. S3)
PMID:17632059	FYPO:0000927	(Fig. S3)
PMID:17632059	PBO:0096104	(Fig. 1B)
PMID:17632059	PBO:0096103	(Fig. 1B)
PMID:17632059	PBO:0096106	(Fig. 1b)
PMID:17632059	PBO:0096107	(Fig. 1c)
PMID:17632059	FYPO:0002890	(Fig. S3)
PMID:17677001	GO:0061638	(Figure S1)
PMID:17677001	PBO:0100882	(Figure 2B)
PMID:17677001	PBO:0100880	(Figure 2B)
PMID:17677001	PBO:0100881	(Figure 2B)
PMID:17677001	PBO:0100882	(Figure 2B)
PMID:17677001	FYPO:0004331	(Figure 3A) EXP says increased, but is normal compared to WT (i.e ura4 insertion derepresses)
PMID:17677001	PBO:0100883	(Figure 3B)
PMID:17677001	PBO:0100884	(Figure 3C) spreading is still within the central domain, to the flanking tRNAs
PMID:17677001	PBO:0100885	(Figure 4B)
PMID:17677001	PBO:0095962	(Figure 4C)
PMID:17677001	PBO:0100886	(Figure S8)
PMID:17677001	PBO:0100881	(Figure 2B)
PMID:17677001	PBO:0100880	(Figure 2B)
PMID:17677001	PBO:0100882	(Figure 2B)
PMID:17677001	PBO:0100881	(Figure 2B)
PMID:17677001	PBO:0100880	(Figure 2B)
PMID:17677001	PBO:0100882	(Figure 2B)
PMID:17677001	PBO:0100881	(Figure 2B)
PMID:17677001	PBO:0100880	(Figure 2B)
PMID:17677001	PBO:0100879	(Figure 2B)
PMID:17677001	PBO:0100879	(Figure 2B)
PMID:17677001	PBO:0100879	(Figure 2B)
PMID:17677001	PBO:0100879	(Figure 2B)
PMID:17677001	FYPO:0003217	(Figure 2A)
PMID:17677001	FYPO:0003217	(Figure 2A)
PMID:17677001	FYPO:0003217	(Figure 2A)
PMID:17690116	PBO:0098709	(Fig. 9B, C) reb1D reduces amount inappropriate recombination at DNA repeats leading to a reduction in cell elongation during checkpoint activation
PMID:17690116	PBO:0037515	(Fig. 5B)
PMID:17690116	PBO:0102120	(Fig. 5A)
PMID:17690116	PBO:0020446	(Fig. 4C) (comment: at the permissive temperature rad3ts is active and the checkpoint is activated in absence of mrc1)
PMID:17690116	PBO:0020446	(Fig. 4C) (comment: at 25°C rad3ts is active and the checkpoint is activated in absence of cds1)
PMID:17690116	PBO:0102122	(Fig. 5C)
PMID:17690116	PBO:0102123	(Fig. 6A, B)
PMID:17690116	PBO:0037130	(Fig. 2A) (comment: non permissive temperature for rad3ts )
PMID:17690116	PBO:0102117	(Fig. 2A,C)
PMID:17690116	PBO:0102115	(Fig. 2B) (comment: cells arrested due to activation of the rad3 checkpoint gene do not rereplicate)
PMID:17690116	PBO:0102116	(Fig. 2A) (cdc18T6A expression at 25°C causes cell elongation due to activation of the mitotic DNA replication checkpoint -permissive temperature for rad3ts)
PMID:17690116	PBO:0102115	(Fig. 1C) rad3ts cells over expressing the mutated pREP4X-cdc18 construct do not rereplicate at 25°C or 36°C (the permissive and non permissive temperatures for rad3ts). This is in contrast to Control cells expressing cdc18+ from pREP3X promoter at 32°C (Fig1D , Table 2) which don't activate the mitotic DNA checkpoint and undergo DNA re-replicatiom
PMID:17690116	PBO:0102114	(Fig. 1B) At 25°C the permissive temperature rad3ts the checkpoint is active and cells expressing the mutant form of pREP4X cdc18 from the screen elongate
PMID:17690116	PBO:0102121	(Fig. 5C)
PMID:17690116	FYPO:0002176	(Fig. 4C) At 25°C rad3 is active but checkpoint cannot be activated in absence of hus1
PMID:17690116	PBO:0102124	(Fig. 3) lack of re replication with moderate increase in cdc18 protein level
PMID:17690116	PBO:0102125	(Fig. 3) lack of re replication with moderate increase in cdc18 protein level
PMID:17690116	PBO:0102126	(Fig. 6C) shows Chromosome III smear is present throughout the cell cycle
PMID:17690116	FYPO:0006494	(Fig. 7A, B, C) after crossing out of cdc18TA6 chromosome size is stabilised and a single band is seen on PFGE which varies in size. If strains with larger Chr III are culture for <30 generations Chromosome III gradually reduces in size
PMID:17690116	FYPO:0007513	(Fig. 8A, B)
PMID:17690116	PBO:0102127	(Fig. 9A)
PMID:17690116	PBO:0102125	(comment: The western blot in Fig 3 actually shows the TAP tagged version but they use the two strains interchangeable so don't actually show data for this strain CCL9)
PMID:17690116	PBO:0102128	(Fig. 3) (comment: CHECK This is the mutant form of pREP4X cdc18 from the screen)
PMID:17690116	PBO:0102129	(Fig. 1B) At 36°C the restrictive temperature for rad3ts the checkpoint is inactive and cells expressing the mutant form of pREP4X cdc18 from the screen do not elongate and are able to form colonies
PMID:17690116	PBO:0102130	(Fig. 3) cdc18 expressed from pREP3X is at a high level. They argue that higher levels cdc18 lead to rereplication and lower levels lead to a rad3 dependent block but no rereplication
PMID:17690116	PBO:0094205	(Fig. 9B, C) rad52D reduces amount inappropriate recombination at DNA repeats leading to a reduction in cell elongation during checkpoint activation
PMID:17690116	PBO:0102115	(Fig. 1C) rad3ts cells over expressing the mutated pREP4X-cdc18 construct do not rereplicate at 25°C or 36°C (the permissive and non permissive temperatures for rad3ts). This is in contrast to Control cells expressing cdc18+ from pREP3X promoter at 32°C (Fig1D , Table 2) which don't activate the mitotic DNA checkpoint and undergo DNA re-replicatiom
PMID:17690116	PBO:0102117	(Fig. 2 A,C) (comment: cells arrested due to active rad3)
PMID:17690116	PBO:0102123	(Fig. 6A,B)
PMID:17690116	PBO:0019114	(Fig. 4C) (comment: At 25°C rad3 is active but checkpoint cannot be activated in absence of crb2)
PMID:17690116	PBO:0019114	(Fig. 4C) (comment: At 25°C rad3 is active but checkpoint cannot be activated in absence of rad26)
PMID:17690116	PBO:0019114	(Fig. 4C) (comment: At 25°C rad3 is active but checkpoint cannot be activated in absence of rad1)
PMID:17690116	PBO:0019114	(Fig. 4C) (comment: At 25°C rad3 is active but checkpoint cannot be activated in absence of rad17)
PMID:17690116	PBO:0019114	(Fig. 4C) (comment: At 25°C rad3 is active but checkpoint cannot be activated in absence of rad9)
PMID:17690116	PBO:0019114	(Fig. 4C) (comment: At the permissive temperature 25*C rad3 is active but checkpoint cannot be activated in absence of chk1)
PMID:17690116	PBO:0102119	(Fig. 4A)
PMID:17690116	PBO:0102118	(Fig. 2D) (comment: different to when pREP3X cdc18+ is over expressed in G2 block which show replicate intermediates and cells undergo re replication)
PMID:17868468	GO:0006264	(comment: deleted existing genome maintence term, and annotated this instead, all things considered...)
PMID:17881496	FYPO:0005719	(comment: CHECK ABOLISHED Figure 3B)
PMID:17881496	FYPO:0003302	(Fig. 1B)
PMID:17881496	FYPO:0000620	(Figure 3A)
PMID:17881496	PBO:0119288	(Fig. 1A)
PMID:17881496	GO:1990942	(Fig. 3A)
PMID:17881496	FYPO:0005719	(Figure 3A)
PMID:17881729	PBO:0105768	(comment: the evidence isn't great)
PMID:17933563	GO:0042973	(Figure 1a)
PMID:17936710	GO:0000706	actually inferred (IC) from combination of phenotype plus GO:0000014 MF
PMID:17937917	GO:0043531	(comment: site A)
PMID:17937917	GO:0005524	(comment:site B)
PMID:17937917	GO:0016208	(comment: site B)
PMID:18030666	FYPO:0002336	(comment: spatial extent)
PMID:18030666	FYPO:0002336	(comment: spatial extent)
PMID:18030666	FYPO:0002336	"(comment: spatial extent ********)"" These results suggested that the 5-FOA-resistant phenotype of the original mutants was indeed due to ura4 repression, presumably as a result of heterochromatin assembly occurring outside the inverted repeat region."""
PMID:18030666	FYPO:0002336	(comment: spatial extent)
PMID:18030666	FYPO:0002336	(comment: spatial extent)
PMID:18030666	FYPO:0002336	(comment: spatial extent ******)The assay is Ura4 expression as a reporter gene for whether heterochromatin is spreading beyond the normal boundry, which it isn't here and so the toxic analogue results in growth attenuation. But sensitivity to FOA isn't the phenotype of interest, that's just the tool
PMID:18030666	FYPO:0002336	(comment: spatial extent)
PMID:18030666	FYPO:0002336	(comment: spatial extent)
PMID:18030666	FYPO:0002336	(comment: spatial extent)
PMID:18030666	FYPO:0002336	"(comment: spatial extent. )"" These results suggested that the 5-FOA-resistant phenotype of the original mutants was indeed due to ura4 repression, presumably as a result of heterochromatin assembly occurring outside the inverted repeat region."""
PMID:18030666	FYPO:0007477	epigenetic variegation both 5-FOA-resistant and -sensitive colonies were found
PMID:18042546	PBO:0102861	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	PBO:0101588	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	PBO:0102863	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	PBO:0102864	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	PBO:0102865	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	PBO:0102866	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	PBO:0102867	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	PBO:0102868	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	PBO:0102869	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	PBO:0102870	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	PBO:0102871	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	PBO:0102872	time course after transcription shutoff, so actually measuring degradation
PMID:18042546	PBO:0102862	all microarray (table 1); arz1 also northern (fig 1)
PMID:18057023	PBO:0112413	(Fig. 1B)
PMID:18057023	PBO:0112418	(Fig. 8A)
PMID:18057023	PBO:0112417	(Fig. 7A)
PMID:18057023	PBO:0112416	(Fig. 7A)
PMID:18057023	PBO:0112415	(Fig. 7A)
PMID:18057023	PBO:0112417	(Fig. 7A)
PMID:18057023	PBO:0112416	(Fig. 7A)
PMID:18057023	PBO:0112415	(Fig. 7A)
PMID:18057023	PBO:0112419	(Fig. 8A)
PMID:18057023	PBO:0112410	(Fig. 1B)
PMID:18057023	PBO:0112412	(Fig. 1B)
PMID:18057023	PBO:0112411	(Fig. 1B)
PMID:18057023	FYPO:0001315	(Fig. 1A)
PMID:18057023	PBO:0112417	(Fig. 7A)
PMID:18057023	PBO:0112416	(Fig. 7A)
PMID:18057023	PBO:0112415	(Fig. 7A)
PMID:18057023	FYPO:0001315	(Fig. 1A)
PMID:18057023	PBO:0112404	(Fig. 1A)
PMID:18057023	PBO:0112405	(Fig. 1A)
PMID:18057023	PBO:0112406	(Fig. 1A)
PMID:18057023	PBO:0112406	(Fig. 1A)
PMID:18057023	PBO:0112416	(Fig. 7A)
PMID:18057023	PBO:0112417	(Fig. 7A)
PMID:18057023	PBO:0112407	(Fig. 1A)
PMID:18057023	PBO:0112407	(Fig. 1A)
PMID:18057023	PBO:0112414	(Fig. 2B)
PMID:18057023	PBO:0112408	(Fig. 1A)
PMID:18057023	PBO:0112408	(Fig. 1A)
PMID:18057023	FYPO:0001315	(Fig. 1B)
PMID:18057023	PBO:0112414	(Fig. 2B)
PMID:18057023	PBO:0112414	(Fig. 2B)
PMID:18057023	FYPO:0001315	(Fig. 1B)
PMID:18057023	FYPO:0001315	(Fig. 1B)
PMID:18057023	PBO:0112409	(Fig. 1B)
PMID:18057023	PBO:0112410	(Fig. 1B)
PMID:18057023	PBO:0112423	(Fig. 8B)
PMID:18057023	PBO:0112422	(Fig. 8B)
PMID:18057023	PBO:0112421	(Fig. 8B)
PMID:18057023	PBO:0112420	(Fig. 8A)
PMID:18057023	PBO:0095113	(Fig. 3)
PMID:18057023	PBO:0112415	(Fig. 7A)
PMID:18059460	GO:0008574	speckles in Fig. 4A
PMID:18060866	GO:0051285	(comment: localization independent of actin cytoskeleton (assayed using latrunculin A) and microtubule cytoskeleton (assayed using carbendazim))
PMID:18061564	PBO:0099338	(Figure 6F)
PMID:18061564	PBO:0099339	(Figure 6F)
PMID:18061564	PBO:0099337	(Figure 6)
PMID:18079700	PBO:0098315	(Figure 3A, 3B)
PMID:18079700	FYPO:0000450	(comment: CHECK Rad21)
PMID:18079700	PBO:0098313	(Figure 3A)
PMID:18079700	GO:0007064	(comment: maintenence)
PMID:18079700	PBO:0098318	(Figure 3C, 3E) (comment: CHECK during G1)
PMID:18079700	PBO:0098316	(Figure 3C, 3E)
PMID:18079700	PBO:0098316	(Figure 3C, 3E)
PMID:18079700	PBO:0098313	(Figure 3B)
PMID:18079700	PBO:0098317	(Figure 3B)
PMID:18079700	PBO:0098316	(Figure 3C, 3E)
PMID:18079700	FYPO:0002060	Supplementary Figure S2
PMID:18079700	PBO:0098314	(Figure 3A) (comment: but not S phase)
PMID:18093330	FYPO:0007068	(Fig. 8)
PMID:18093330	FYPO:0007068	(Fig. 8)
PMID:18093330	FYPO:0001982	(Fig. 1)
PMID:18157152	MOD:00427	(comment: CHECK this is a protein modification so should be changed once we can do RNA mods)
PMID:18160711	FYPO:0002702	(comment: CHECK truncated at PacI site)
PMID:18160711	FYPO:0002702	(comment: CHECK region between NsiI sites deleted)
PMID:18160711	FYPO:0002702	(comment: CHECK region between NdeI and XhoI sites deleted)
PMID:18165685	GO:0051015	(comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887))
PMID:18165685	GO:0051015	(comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887))
PMID:18165685	GO:0051015	(comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887))
PMID:18165685	GO:0051015	(comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887))
PMID:18165685	GO:0051015	(comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887))
PMID:18165685	GO:0051015	(comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887))
PMID:18165685	GO:0051015	(comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887))
PMID:18184749	GO:0042175	supp 1A
PMID:18184749	PBO:0110559	(Figure 1A, right panel). Figure 1C
PMID:18184749	PBO:0110560	(Figure 1A, right panel). Figure 1C
PMID:18184749	FYPO:0002872	(comment: to cell division site) We confirmed that the actomyosin ring structure was important for polarization of the early secretory compartments by examiningthe spatial distribution of the tER and Golgi compartmentsin cells with compromised function of the myosin lightchainCdc4p
PMID:18184749	FYPO:0002872	(comment: CHECK abnormal ER polarization (ectopic))
PMID:18184749	FYPO:0002872	(comment: CHECK abnormal ER polarization) We observed a striking reduction in the number of cells exhibiting clear polarization of the tER in cdc15-140 cells already at the permissive temperature of 24°C (Figure 5A, bottom panel)
PMID:18184749	GO:0032541	supp 1A
PMID:18184749	GO:0042175	supp 1A
PMID:18184749	PBO:0110558	(Figure 1B, left panel)
PMID:18184749	PBO:0110557	(Figure 1B, left panel)
PMID:18184749	PBO:0110556	(Figure 1B, left panel)
PMID:18184749	GO:0032541	supp 1A
PMID:18184749	PBO:0110555	(Figure 1A, right panel). Figure 1C
PMID:18203864	PBO:0114668	(Fig. 2B)
PMID:18203864	PBO:0114667	(Fig. 2B)
PMID:18223116	PBO:0107015	(Fig. 2)
PMID:18223116	PBO:0107747	(Fig. 2)
PMID:18223116	PBO:0107746	(Fig. 2)
PMID:18223116	PBO:0107745	(Fig. 2)
PMID:18223116	PBO:0106352	(Fig. 2)
PMID:18223116	PBO:0107016	(Fig. 2)
PMID:18223116	PBO:0107750	(Fig. 2)
PMID:18223116	PBO:0107749	(Fig. 2)
PMID:18223116	PBO:0107748	(Fig. 2)
PMID:18223116	PBO:0107752	(Fig. 2)
PMID:18223116	PBO:0107753	(Fig. 2)
PMID:18223116	PBO:0107754	(Fig. 2)
PMID:18223116	PBO:0107755	(Fig. 2)
PMID:18223116	PBO:0116390	(Fig. 6) (comment: it doesn't bind dna according to later studies)
PMID:18223116	PBO:0107756	(Fig. 2)
PMID:18223116	PBO:0107751	(Fig. 2)
PMID:18256284	PBO:0033845	(Figure 1B) (comment: plus end)
PMID:18256284	PBO:0033849	(Figure 1B) (comment: plus end)
PMID:18256284	PBO:0033843	(Figure 1B) (comment: plus end)
PMID:18256284	PBO:0033842	(Figure 1A)
PMID:18256284	PBO:0033844	(Figure 1B) (comment: plus end)
PMID:18256284	PBO:0033846	(Figure 1A)
PMID:18256290	PBO:0096598	(comment: increased more than pxl1delta alone)
PMID:18256290	PBO:0096598	(comment: increased more than pxl1delta alone)
PMID:18256290	PBO:0096598	(comment: increased more than pxl1delta alone)
PMID:18256290	PBO:0096598	(comment: increased more than pxl1delta alone)
PMID:18256290	PBO:0096598	(comment: increased more than pxl1delta alone)
PMID:18256290	GO:0110085	(comment: localization dependent on filamentous actin (GO:0031941); tested using latrunculin A)
PMID:18256290	PBO:0096598	(comment: less levere than pxl1 null)
PMID:18256290	PBO:0096598	(comment: less levere than pxl1 null)
PMID:18262494	FYPO:0001919	(comment: CHECK after chromosome segregation)
PMID:18262494	FYPO:0000030	(comment: CHECK with extreme sister chromtid oscillations)
PMID:18262494	PBO:0033440	(Fig. 1B)
PMID:18272786	FYPO:0001365	data from table; nothing more specific shown
PMID:18272786	FYPO:0001365	data from table; nothing more specific shown
PMID:18272786	FYPO:0001365	data from table; nothing more specific shown
PMID:18272786	FYPO:0001365	data from table; nothing more specific shown
PMID:18272786	GO:0110085	(comment: dependent on F-actin, assayed using Latrunculin A)
PMID:18272786	FYPO:0001365	data from table; nothing more specific shown
PMID:18276645	PBO:0109064	(comment: CHECK normal oxygen level)
PMID:18276645	PBO:0107664	(comment: CHECK normal oxygen level)
PMID:18303049	PBO:0114308	(Fig. 5)
PMID:18303049	PBO:0114312	(Table 2)
PMID:18303049	PBO:0019301	(Fig. 3A)
PMID:18303049	PBO:0114305	(Fig. 3B)
PMID:18303049	PBO:0114306	(Fig. 3B)
PMID:18303049	PBO:0114307	(Fig. 3D)
PMID:18303049	PBO:0114304	(Fig. 1)
PMID:18303049	PBO:0114307	(Fig. 3D)
PMID:18303049	FYPO:0001315	(Fig. 3C)
PMID:18303049	PBO:0114310	(Table 2)
PMID:18303049	FYPO:0001315	(Fig. 3C)
PMID:18303049	PBO:0114311	(Table 2)
PMID:18303049	PBO:0114313	(Fig. 6B)
PMID:18303049	PBO:0114309	(Table 2)
PMID:18303049	PBO:0114315	(Table 2)
PMID:18303049	PBO:0114315	(Table 2)
PMID:18303049	FYPO:0007743	(Fig. 6C)
PMID:18303049	PBO:0114314	(Table 2)
PMID:18303049	PBO:0114314	(Table 2)
PMID:18303049	FYPO:0000252	(Table 1)
PMID:18303049	PBO:0096052	(Fig. 2C)
PMID:18328707	PBO:0100644	(Figure 3A)
PMID:18328707	PBO:0104857	(Fig. 1D)
PMID:18328707	PBO:0104862	(Fig. 2C)
PMID:18328707	PBO:0104861	(Fig. 1SE) to cell cortex of (new) cell tip from medial cortex
PMID:18328707	PBO:0104861	(Fig. 1SE) to cell cortex of (new) cell tip from medial cortex
PMID:18328707	PBO:0096623	(Fig. S1D)
PMID:18328707	PBO:0104860	(Fig. 1SE) to cell cortex of (new non growing) cell tip from medial cortex
PMID:18328707	PBO:0104856	(Fig. 1)
PMID:18328707	PBO:0104865	(comment: CHECK GTP-bound) Figure 4E
PMID:18328707	PBO:0104859	(comment: old end)
PMID:18328707	PBO:0104866	(comment: CHECK GTP-bound) Figure 4E, polarization localization to both cell ends
PMID:18328707	PBO:0104863	(comment: CHECK GTP bound)
PMID:18328707	GO:0005515	(Figure 3B)
PMID:18328707	PBO:0104858	(Fig. 1D)
PMID:18328707	PBO:0104868	(comment: *****OLD*****waiting for GO)
PMID:18328707	PBO:0104856	(Fig. 1)
PMID:18328707	PBO:0104856	(Fig. 1)
PMID:18328707	MOD:01455	(Fig. 1D)
PMID:18328707	PBO:0104858	(Fig. 1)
PMID:18328707	PBO:0104858	(Fig. 1D) (comment: pom1 is catalytically active but not localized to cell ends)
PMID:18328707	FYPO:0000024	(Figure 4E)
PMID:18328707	PBO:0104864	(comment: CHECK GTP bound) fig 3C
PMID:18328707	PBO:0103573	(comment: CHECK active GTP bound form)
PMID:18328707	PBO:0020227	(comment: CHECK GTP bound active form)
PMID:18331722	GO:1990949	First, we have shown that a true APC/C substrate regulates the activity of the APC/C. Cells might precisely control protein levels of each or a subset of APC/C substrate to fine-tune the APC/C itself....Mes1 transcripts and protein levels peak in late MI (Izawa et al., 2005; Mata et al., 2002) when Mes1 sequesters the Fizzy family of proteins to inhibit APC/C, in turn slowing down cyclin B proteolysis (‘‘APC/C inhibited’’ in Figure 4G). At the same time, Mes1 is inhibited through ubiquitylation by APC/C to allow partial APC/C activation required for anaphase I onset.
PMID:18331722	PBO:0104195	in vitro assay
PMID:18337696	FYPO:0003118	(comment: at time 0. they don't look at nitrogen starvation for very long, only 60 mins)
PMID:18344406	FYPO:0002151	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2Δ and rad3Δ are shown in Fig. 2A
PMID:18344406	FYPO:0004928	Our fluorescence microscopic analysis also clearly indicated that a significant percentage of the hst4Δ cells in culture had fragmented DNA (see Fig. S1 in the supplemental material).
PMID:18344406	PBO:0093616	Interestingly, hst4Δ cells were sensitive to MMS and CPT (Fig. 1A)
PMID:18344406	PBO:0093613	Interestingly, hst4Δ cells were sensitive to MMS and CPT (Fig. 1A)
PMID:18344406	FYPO:0000963	(comment: CHECK significantly sensitive to HU.)
PMID:18344406	PBO:0093631	(comment: CHECK significantly sensitive to HU. less than that of wild-type cells but higher than that of checkpoint mutant rad3Δ cells) (Fig. 1B).
PMID:18344406	PBO:0093616	Interestingly, similar to the hst4Δ mutant, both K56R and K56Q mutants were sensitive to MMS and CPT.
PMID:18344406	PBO:0093617	Interestingly, similar to the hst4Δ mutant, both K56R and K56Q mutants were sensitive to MMS and CPT. However, the histone H3 K56Q mutant, which mimics the constitutively acetylated state, was less sensitive to MMS and CPT than the K56R mutant, which mimics the constitutively deacetylated state.
PMID:18344406	PBO:0111114	Like hst4Δ cells, both histone H3 mutant cells were very elongated, and a percentage of these cells exhibited abnormal DAPI staining (Fig. 7A).
PMID:18344406	PBO:0111113	Like hst4Δ cells, both histone H3 mutant cells were very elongated, and a percentage of these cells exhibited abnormal DAPI staining (Fig. 7A).
PMID:18344406	FYPO:0002060	Both mutant strains were viable and able to grow at 32°C.
PMID:18344406	PBO:0093559	Both mutant strains were viable and able to grow at 32°C. However, like the hst4Δ strain, the histone H3 K56R mutant strains had slight growth defects compared to the strain containing a single copy of the H3 histone (Fig. 7B, first panel).
PMID:18344406	GO:0140861	These results collectively suggest that alterations in K56 acetylation are dependent upon the presence of Hst4 in the cell, and more importantly, they suggest that the levels of Hst4 are regulated in response to cell cycle progression and DNA damage.
PMID:18344406	PBO:0093616	H184Y mutation were as sensitive to MMS as the hst4Δ strains were, indicating that Hst4 enzymatic activity was important for cells to be resistant to MMS.
PMID:18344406	PBO:0114594	These results (Fig. 4C) showed that the acetylation of H3 K56 is cell cycle regulated and occurred during the S phase of the cell cycle.
PMID:18344406	FYPO:0007632	In the absence of Sir2, we observed elevated levels of histone H3 K9 and histone H4 K16, which was consistent with previous reports (17, 48).
PMID:18344406	FYPO:0000871	In the absence of Sir2, we observed elevated levels of histone H3 K9 and histone H4 K16, which was consistent with previous reports (17, 48).
PMID:18344406	FYPO:0001925	hst4Δ cells behaved as wild-type cells did and were able to survive exposure to gamma irradiation (Fig. 1C).
PMID:18344406	PBO:0111111	(comment: If this signal is not generated, cells mutant go through the cell cycle with damage and eventually die.)
PMID:18344406	FYPO:0003481	Like hst4Δ cells, both histone H3 mutant cells were very elongated, and a percentage of these cells exhibited abnormal DAPI staining (Fig. 7A).
PMID:18344406	FYPO:0002151	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2Δ and rad3Δ are shown in Fig. 2A
PMID:18344406	FYPO:0002151	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2Δ and rad3Δ are shown in Fig. 2A
PMID:18344406	FYPO:0002151	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2Δ and rad3Δ are shown in Fig. 2A
PMID:18344406	FYPO:0002151	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2Δ and rad3Δ are shown in Fig. 2A
PMID:18344406	FYPO:0008162	In cells lacking Hst4, Chk1 was phosphorylated even in the absence of MMS exposure, and this phosphorylation did not significantly increase upon exposure to MMS (Fig. 2B).
PMID:18344406	FYPO:0000502	Wild-type cells showed a peak of septation approximately 80 min after release, whereas the hst4Δ cells showed a delayed peak of septation at 120 min (see Fig. S2 in the supplemental material).
PMID:18344406	FYPO:0002060	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2Δ and rad3Δ are shown in Fig. 2A
PMID:18344406	FYPO:0002060	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2Δ and rad3Δ are shown in Fig. 2A
PMID:18344406	FYPO:0002060	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2Δ and rad3Δ are shown in Fig. 2A
PMID:18344406	FYPO:0002060	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2Δ and rad3Δ are shown in Fig. 2A
PMID:18344406	FYPO:0002061	However, every single repair mutant that we tested was synthetically sick in combination with hst4Δ when cells were grown on medium containing MMS (Fig. 3).
PMID:18344406	FYPO:0002061	However, every single repair mutant that we tested was synthetically sick in combination with hst4Δ when cells were grown on medium containing MMS (Fig. 3).
PMID:18344406	FYPO:0002061	However, every single repair mutant that we tested was synthetically sick in combination with hst4Δ when cells were grown on medium containing MMS (Fig. 3).
PMID:18344406	FYPO:0002061	However, every single repair mutant that we tested was synthetically sick in combination with hst4Δ when cells were grown on medium containing MMS (Fig. 3).
PMID:18344406	FYPO:0002061	However, every single repair mutant that we tested was synthetically sick in combination with hst4Δ when cells were grown on medium containing MMS (Fig. 3).
PMID:18344406	FYPO:0003223	The hst4 mutant did not show significant changes in the acetylation levels of histone H3 K9 or K14 and histone H4 K16 compared to the wild-type control (Fig. 4A).
PMID:18344406	FYPO:0008161	The hst4Δ mutant did not show significant changes in the acetylation levels of histone H3 K9 or K14 and histone H4 K16 compared to the wild-type control (Fig. 4A).
PMID:18344406	FYPO:0008160	The hst4Δ mutant did not show significant changes in the acetylation levels of histone H3 K9 or K14 and histone H4 K16 compared to the wild-type control (Fig. 4A).
PMID:18345014	PBO:0114329	(Fig. 5D)
PMID:18345014	PBO:0114331	(Fig. 2A)
PMID:18345014	GO:0140720	(Fig. 1)
PMID:18345014	GO:0005721	(Fig. 1)
PMID:18345014	GO:0031934	(Fig. 1)
PMID:18345014	GO:0140720	(Fig. 1)
PMID:18345014	GO:0140720	(Fig. 1)
PMID:18345014	GO:0140720	(Fig. 1)
PMID:18345014	GO:0140720	(Fig. 1)
PMID:18345014	GO:0005721	(Fig. 1)
PMID:18345014	GO:0005721	(Fig. 1)
PMID:18345014	GO:0005721	(Fig. 1)
PMID:18345014	GO:0005721	(Fig. 1)
PMID:18345014	GO:0031934	(Fig. 1)
PMID:18345014	GO:0031934	(Fig. 1)
PMID:18345014	GO:0031934	(Fig. 1)
PMID:18345014	GO:0031934	(Fig. 1)
PMID:18345014	PBO:0119857	The results presented here show that binding of Clr4 to H3K9me via its chromodomain is crucial for the spreading of heterochromatic structures.
PMID:18345014	PBO:0119858	The results presented here show that binding of Clr4 to H3K9me via its chromodomain is crucial for the spreading of heterochromatic structures.
PMID:18345014	GO:0033553	(Fig. 1)
PMID:18345014	GO:0033553	(Fig. 1)
PMID:18345014	PBO:0114329	(Fig. 2A)
PMID:18345014	FYPO:0002827	(Fig. 6B)
PMID:18345014	GO:0141194	Our analyses suggest that Rik1 is a crucial factor involved in RNAi- mediated targeting of ClrC to heterochromatic repeat elements.
PMID:18345014	PBO:0114329	(Fig. 5B)
PMID:18345014	PBO:0119856	The results presented here show that binding of Clr4 to H3K9me via its chromodomain is crucial for the spreading of heterochromatic structures.
PMID:18345014	PBO:0120542	(Fig. 5A)
PMID:18345014	PBO:0120541	(Fig. 5A)
PMID:18345014	PBO:0120522	(Fig. 2B)
PMID:18345014	PBO:0114332	(Fig. 2A)
PMID:18345014	PBO:0114339	(Fig. 5B)
PMID:18345014	PBO:0114330	(Fig. 5B)
PMID:18345014	PBO:0114331	(Fig. 5B)
PMID:18345014	PBO:0120522	(Fig. 5C)
PMID:18345014	PBO:0120541	(Fig. 5C)
PMID:18345014	PBO:0120542	(Fig. 5C)
PMID:18345014	PBO:0114330	(Fig. 5D)
PMID:18345014	PBO:0114331	(Fig. 5D)
PMID:18345014	PBO:0120523	(Fig. 5A)
PMID:18345014	FYPO:0002355	(Fig. 6A)
PMID:18345014	PBO:0111016	(Fig. 6A)
PMID:18345014	PBO:0120522	(Fig. 5A)
PMID:18345014	FYPO:0008195	(Fig. 4C)
PMID:18345014	FYPO:0008195	(Fig. 4C)
PMID:18345014	PBO:0114340	(Fig. 3B)
PMID:18345014	PBO:0114330	(Fig. 2A)
PMID:18345014	PBO:0114339	(Fig. S5)
PMID:18345014	PBO:0114339	(Fig. S5)
PMID:18345014	PBO:0114339	(Fig. S5)
PMID:18345014	PBO:0114339	(Fig. S5)
PMID:18345014	PBO:0120523	(Fig. S5)
PMID:18345014	PBO:0120523	(Fig. S5)
PMID:18345014	PBO:0120523	(Fig. S5)
PMID:18345014	PBO:0120523	(Fig. S5)
PMID:18345014	FYPO:0002827	(Fig. 2E)
PMID:18345014	PBO:0114338	(Fig. 2D)
PMID:18345014	PBO:0120544	(Fig. 2D)
PMID:18345014	PBO:0120544	(Fig. 2D)
PMID:18345014	PBO:0120543	(Fig. 2D)
PMID:18345014	PBO:0120543	(Fig. 2D)
PMID:18345014	PBO:0120543	(Fig. 2D)
PMID:18345014	FYPO:0002835	(Fig. 2C)
PMID:18345014	FYPO:0002836	(Fig. 2C)
PMID:18345014	PBO:0114335	(Fig. 2B and D)
PMID:18345014	PBO:0120542	(Fig. 2B)
PMID:18345014	PBO:0120541	(Fig. 2B)
PMID:18378696	PBO:0093619	(comment: same as rad51delta alone)
PMID:18378696	PBO:0093630	(comment: same as either single mutant)
PMID:18378696	FYPO:0000088	(comment: same as nbs1delta alone)
PMID:18378696	FYPO:0000089	(comment: same as nbs1delta alone)
PMID:18378696	PBO:0093586	(comment: same as nbs1delta alone)
PMID:18378696	PBO:0093630	(comment: same as nbs1delta alone)
PMID:18378696	PBO:0093586	(comment: same as either single mutant)
PMID:18378696	FYPO:0000089	(comment: same as either single mutant)
PMID:18388861	FYPO:0000316	Table 1. Fig. 3C and D
PMID:18388861	FYPO:0000316	Table 1. Fig. 3C and D
PMID:18388861	FYPO:0003612	Table 1, Fig. 3A, C and D
PMID:18388861	PBO:0112927	None of the single helicase and essential topoisomerase 3 (in rqh1D background) mutant strains exhibit MT switching and/or viability defect, except for the pfh1 mutant where a mild MT switching defect was observed (Table I, data not shown).
PMID:18388861	FYPO:0000470	Table 1. Fig. 3C and D
PMID:18388861	FYPO:0000470	Table 1. Fig. 3C and D
PMID:18388861	FYPO:0000470	(Table 1)
PMID:18388861	FYPO:0003612	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0000316	(Table 1)
PMID:18388861	FYPO:0003612	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	GO:0007533	Interestingly, upon re-streaking, the h 90 rhp57D cells progressively produced colonies defective in MT switching, indicating that Rhp57 participates in efficient MT switching.
PMID:18388861	PBO:0038005	However, the h90 rhp57D swi5D double mutant is not viable (Figure 2C). Table 1
PMID:18388861	PBO:0038005	However, the h90 rhp57D swi5D double mutant is not viable (Figure 2C). Table 1
PMID:18388861	PBO:0112929	h90 swi5D mutant produces healthy colonies but MT switching is drastically reduced. Fig. 2C. Table 1
PMID:18388861	PBO:0112927	The h90 rhp57D strain produces colonies with a mild defect in MT switching. Fig. 2C. Table 1
PMID:18388861	PBO:0097301	the double h90 rad50D exo1D mutant is not viable, but can eventually form micro-colonies (Figure 2B, left panel). Table 1
PMID:18388861	PBO:0097301	the double h90 rad50D exo1D mutant is not viable, but can eventually form micro-colonies (Figure 2B, left panel). Table 1
PMID:18388861	FYPO:0000472	The h90 exo1D mutant is viable and does not exhibit MT switching defects. Fig. 2B. Table 1
PMID:18388861	FYPO:0003612	The h90 exo1D mutant is viable. Fig. 2B. Table 1
PMID:18388861	FYPO:0003612	(Table 1)
PMID:18388861	FYPO:0003612	(Table 1)
PMID:18388861	FYPO:0003612	(Table 1)
PMID:18388861	FYPO:0003612	(Table 1)
PMID:18388861	FYPO:0003612	(Table 1)
PMID:18388861	FYPO:0003612	(Table 1)
PMID:18388861	FYPO:0000278	the h90 rad50D or h90 mre11D (data not shown) mutant forms small colonies. However, these colonies contain many dead cells and few spores. Table 1.
PMID:18388861	FYPO:0000278	(Table 1)
PMID:18388861	FYPO:0000278	the h90 rad50D or h90 mre11D (data not shown) mutant forms small colonies. However, these colonies contain many dead cells and few spores.
PMID:18388861	FYPO:0003082	(Fig. 5)
PMID:18388861	FYPO:0003082	(Fig. 5)
PMID:18388861	FYPO:0003082	(Fig. 5)
PMID:18388861	FYPO:0003612	rhp22AD, rhp51D and rhp54D mutants do not form colonies in the wild-type h90 strain, as already shown for rhp22AD, although they are viable in mat1-Msmt-0 and mat1-PD17 backgrounds.
PMID:18388861	FYPO:0003612	rhp22AD, rhp51D and rhp54D mutants do not form colonies in the wild-type h90 strain, as already shown for rhp22AD, although they are viable in mat1-Msmt-0 and mat1-PD17 backgrounds.
PMID:18388861	FYPO:0003612	rhp22AD, rhp51D and rhp54D mutants do not form colonies in the wild-type h90 strain, as already shown for rhp22AD, although they are viable in mat1-Msmt-0 and mat1-PD17 backgrounds.
PMID:18388861	FYPO:0003612	rhp22AD, rhp51D and rhp54D mutants do not form colonies in the wild-type h90 strain, as already shown for rhp22AD, although they are viable in mat1-Msmt-0 and mat1-PD17 backgrounds. Fig. 2A
PMID:18388861	FYPO:0003612	rhp22AD, rhp51D and rhp54D mutants do not form colonies in the wild-type h90 strain, as already shown for rhp22AD, although they are viable in mat1-Msmt-0 and mat1-PD17 backgrounds.
PMID:18388861	FYPO:0003612	rhp22AD, rhp51D and rhp54D mutants do not form colonies in the wild-type h90 strain, as already shown for rhp22AD, although they are viable in mat1-Msmt-0 and mat1-PD17 backgrounds.
PMID:18388861	PBO:0113793	Table 1. Further observation of the germinating spores showed that the mutated h90 cells elongated and eventually divided, but never formed visible colonies (data not shown).
PMID:18388861	PBO:0113793	Table 1. Fig. 2A. Further observation of the germinating spores showed that the mutated h90 cells elongated and eventually divided, but never formed visible colonies (data not shown).
PMID:18388861	PBO:0113793	Table 1. Further observation of the germinating spores showed that the mutated h90 cells elongated and eventually divided, but never formed visible colonies. Table 1
PMID:18388861	FYPO:0000316	(Table 1)
PMID:18388861	FYPO:0000316	(Table 1)
PMID:18388861	FYPO:0000316	(Table 1)
PMID:18388861	FYPO:0000316	(Table 1)
PMID:18388861	PBO:0113794	Table 1, Fig. 3A and B
PMID:18388861	FYPO:0000316	(Table 1)
PMID:18388861	FYPO:0000316	(Table 1)
PMID:18391219	GO:0002143	"(comment: provides the sulfur....seems ok based on the def ""The process in which a uridine residue at position 34 in the anticodon of a tRNA is post-transcriptionally thiolated at the C2 position. **This process involves transfer of a sulfur from cysteine to position C2 by several steps"""
PMID:18397994	FYPO:0002708	(Fig. 8A)
PMID:18397994	FYPO:0000943	(Fig. 9)
PMID:18397994	FYPO:0000943	(Fig. 9)
PMID:18397994	FYPO:0002708	(Fig. 8)
PMID:18397994	FYPO:0002708	(Fig. 8)
PMID:18397994	FYPO:0002708	(Fig. 8A)
PMID:18397994	PBO:0114354	We found that Slk1 was also localized to the SPB during metaphase II and anaphase II. Fig. 7
PMID:18397994	PBO:0023321	We found that Slk1 was also localized to the SPB during metaphase II and anaphase II. Fig. 7
PMID:18397994	GO:0005628	(Fig. 7)
PMID:18397994	FYPO:0002708	(Fig. 6A)
PMID:18397994	FYPO:0002708	(Fig. 6A)
PMID:18397994	FYPO:0002708	(Fig. 6A)
PMID:18397994	FYPO:0002708	(Fig. 6A)
PMID:18397994	FYPO:0000346	(Fig. 6A)
PMID:18397994	GO:0032120	(Fig. 5)
PMID:18397994	PBO:0114353	(Fig. 4)
PMID:18397994	FYPO:0000478	(Fig. 3B)
PMID:18397994	FYPO:0000346	(Fig. 3A)
PMID:18397994	PBO:0092176	(Fig. 2B)
PMID:18397994	PBO:0092330	(Fig. 2A)
PMID:18399988	PBO:0095423	(comment: they show transfer to a heterologous cytochrome p450 enzyme, but pombe doesn't have any mitochondrial ones.)
PMID:18411246	FYPO:0001914	(Fig. 5B)
PMID:18411246	FYPO:0004952	enclosure arrow in Figs 4Ci,ii)
PMID:18411246	PBO:0103894	(Fig. 2A)
PMID:18411246	PBO:0103895	(Fig. 3A)
PMID:18411246	PBO:0103896	(Fig. 3A)
PMID:18411246	PBO:0023044	(Fig. 2B)
PMID:18414064	FYPO:0001387	(comment: same with or without TBZ)
PMID:18414064	PBO:0098974	(comment: penetrance at 4 hours)
PMID:18414064	PBO:0098973	(comment: penetrance at 4 hours)
PMID:18414064	FYPO:0001387	(comment: same with or without TBZ)
PMID:18414064	PBO:0098969	(comment: penetrance at 4 hours; increases upon longer time at restrictive temp)
PMID:18416603	PBO:0113788	Based on these results, we propose a model for the early step of the strand exchange reaction involving Rhp51 and the two mediators. Rad22 recruits Rhp51 to RPA-coated ssDNA.
PMID:18459978	GO:0045899	Quantification of the results shown in Fig. 4A is illustrated in Fig. 4B. Taken together, these experiments reveal that PC4 stimulates the rate of preinitiation complex formation.
PMID:1849107	PBO:0103716	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103717	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103717	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103716	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103716	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103717	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103717	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103716	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103716	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103716	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103716	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103716	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103717	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103716	(comment: also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103717	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103716	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103716	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103716	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0001869	(comment: git2-1 is effectively null, even though it isn't a complete deletion of the coding sequence)
PMID:1849107	FYPO:0001660	(comment: git2-1 is effectively null, even though it isn't a complete deletion of the coding sequence)
PMID:1849107	PBO:0103715	(comment: glycerol = derepressing for glucose repression) (comment: also assayed using lacZ under fbp1 promoter and maltose carbon source, also derepressing)
PMID:1849107	PBO:0103716	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103717	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103716	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103717	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103717	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	PBO:0103716	(comment: also assayed using lacZ under fbp1 promoter)
PMID:18493607	PBO:0093564	(comment: CHECK slighly more severe than sir2+ overexpression alone)
PMID:18493607	PBO:0094679	(comment: CHECK same as sir2+ overexpression alone)
PMID:18493607	PBO:0092751	present throughout mitotic cell cycle
PMID:18495844	PBO:0104281	(Fig. 3B)
PMID:18495844	PBO:0104278	(Fig. 1B and 2B,C) normal MTs required to establish early orientation of mitotic spindle by aligning SPBs with long axis of cell
PMID:18495844	FYPO:0005691	(Fig. 2A-C) This oscillatory movement was not perturbed by Latrunculin A treatment, but was lost in cells treated with MBC or in mto1Δ cells, and was reduced in tip1Δ cells
PMID:18495844	FYPO:0005691	(Fig. 2B)
PMID:18495844	PBO:0104280	(Fig. 3B, C) As expected, the range of SPB trajectory angles was much wider than in wild-type cells (Fig. 2C, Fig. 3B,C
PMID:18495844	PBO:0104280	(Fig. 3B, C)
PMID:18495844	PBO:0104278	(Fig. 1B) normal interphase MTs required to establish early orientation of mitotic spindle by aligning SPBs with long axis of cell
PMID:18495844	PBO:0104277	(Fig. 1B)
PMID:18495844	PBO:0104279	(Fig. 3B)
PMID:18504300	PBO:0021460	(Fig. 5)
PMID:18504300	PBO:0099112	(Fig. 5)
PMID:18504300	PBO:0112313	(Fig. 5)
PMID:18504300	PBO:0112312	(Fig. 5)
PMID:18514516	PBO:0095386	(comment:same as either single mutant)
PMID:18514516	PBO:0095386	(comment:same as either single mutant)
PMID:18514516	PBO:0095386	(comment:same as either single mutant)
PMID:18514516	PBO:0095390	(comment:same as either single mutant)
PMID:18514516	PBO:0095390	(comment:same as either single mutant)
PMID:18562692	FYPO:0000324	(Table 1)
PMID:18562692	FYPO:0000324	(Fig. 6C)
PMID:18562692	FYPO:0000324	(Fig. 6C)
PMID:18562692	FYPO:0006917	(Fig. 6C)
PMID:18562692	FYPO:0006917	(Fig. 1)
PMID:18562692	FYPO:0007388	(Fig. 2)
PMID:18562692	FYPO:0006917	(Fig. 6C)
PMID:18562692	FYPO:0006917	(Fig. 6C)
PMID:18562692	FYPO:0006917	(Fig. 6C)
PMID:18562692	FYPO:0006917	(Fig. 6C)
PMID:18562692	FYPO:0006917	(Fig. 6C)
PMID:18562692	FYPO:0006917	(Fig. 6C)
PMID:18562692	FYPO:0007388	(Fig. 2)
PMID:18562692	FYPO:0006917	(Fig. 6C)
PMID:18562692	FYPO:0000324	(Fig. 1)
PMID:18562692	FYPO:0000324	(Fig. 6C)
PMID:18562692	PBO:0099147	(Fig. 5A)
PMID:18562692	PBO:0099146	(Fig. 5A)
PMID:18562692	PBO:0099145	(Fig. 5B)
PMID:18562692	FYPO:0001778	(Fig. 5B)
PMID:18562692	FYPO:0000324	(Fig. 5A)
PMID:18562692	FYPO:0006917	(Fig. 4)
PMID:18562692	FYPO:0002022	(Fig. 3)
PMID:18562696	FYPO:0000583	(Fig. S3)
PMID:18562696	PBO:0035493	(Fig. 2)
PMID:18562696	PBO:0035494	(Fig. 2)
PMID:18562696	PBO:0092090	(Fig. 2A)
PMID:18562696	PBO:0114361	(Fig. 3A)
PMID:18562696	PBO:0114362	(Fig. 3C)
PMID:18562696	PBO:0114363	(Fig. 3D and E)
PMID:18562696	PBO:0114363	(Fig. 3F)
PMID:18562696	PBO:0114363	(Fig. 3F)
PMID:18562696	PBO:0114363	(Fig. 3G)
PMID:18562696	PBO:0114363	(Fig. 3G)
PMID:18562696	PBO:0114364	(Fig. S1A)
PMID:18562696	PBO:0114365	(Fig. S1A)
PMID:18562696	PBO:0114366	(Fig. S1A)
PMID:18562696	PBO:0114367	(Fig. S1A)
PMID:18562696	PBO:0114368	(Fig. S1A)
PMID:18562696	FYPO:0000346	(Fig. 4A and B)
PMID:18562696	FYPO:0000346	(Fig. 4A)
PMID:18562696	PBO:0033641	(Fig. 4C)
PMID:18562696	PBO:0033641	(Fig. 4C)
PMID:18562696	FYPO:0000581	(Fig. 4D)
PMID:18562696	FYPO:0000581	(Fig. 4D)
PMID:18562696	PBO:0114369	(Fig. 4F)
PMID:18562696	PBO:0114370	(Fig. 4F)
PMID:18562696	PBO:0114371	(Fig. 5A and B)
PMID:18562696	PBO:0114372	(Fig. S2)
PMID:18562696	PBO:0114373	(Fig. S2)
PMID:18562696	PBO:0114374	(Fig. 5C)
PMID:18562696	FYPO:0006777	(Fig. 4H)
PMID:18562696	PBO:0114375	(Fig. 5D)
PMID:18562696	FYPO:0005737	(Fig. 5E)
PMID:18562696	FYPO:0000346	(Fig. 6A)
PMID:18562696	FYPO:0000583	(Fig. 6B)
PMID:18562696	FYPO:0000583	(Fig. 6B)
PMID:18562696	PBO:0114375	(Fig. 6D)
PMID:18562696	PBO:0114374	(Fig. 6C)
PMID:18562696	FYPO:0006777	(Fig. 6E)
PMID:18562696	FYPO:0006777	(Fig. 6E)
PMID:18562696	FYPO:0000583	(Fig. S3)
PMID:18562696	FYPO:0000583	(Fig. S3)
PMID:18562696	FYPO:0000583	(Fig. S3)
PMID:18562696	PBO:0033557	(Fig. 7B)
PMID:18562696	PBO:0033641	(Fig. 7B)
PMID:18562696	FYPO:0006777	(Fig. 8B)
PMID:18562696	FYPO:0006777	(Fig. 8B)
PMID:18562696	GO:1903023	(Fig. 4C, 4F, 5A,B, 5E)
PMID:18615848	FYPO:0002019	(comment: same as swi7-H4 alone, i.e. it's dominant)
PMID:1863602	GO:0010515	(comment: maybe not shown strongly in this paper but I'm trying to get the git genes annotated to this term because pka1 phosphorylates rst2 which excludes rst2 from the nucleus. rst2 when in the nucleus activates ste11 transcription.)
PMID:18640983	FYPO:0007061	(comment: CHECK in vitro)
PMID:18653539	FYPO:0004168	(Figure 8B)
PMID:18653539	FYPO:0004168	(Figure 8B)
PMID:18653539	FYPO:0004168	(Figure 8B)
PMID:18653539	FYPO:0002060	(Figure 1A)
PMID:18653539	FYPO:0001673	(Figure 1C)
PMID:18653539	PBO:0096560	(Figure 1A, 8A)
PMID:18653539	FYPO:0006275	(Fig. 1D)
PMID:18653539	FYPO:0006276	(Fig. 1D, Fig. 1F)
PMID:18653539	FYPO:0006289	(Figure 2A)
PMID:18653539	FYPO:0003975	(Fig. 2F) (comment: CHECK during veg phase)
PMID:18653539	FYPO:0004168	(Figure 8B)
PMID:18653539	FYPO:0004695	(Figure 2A)
PMID:18653539	FYPO:0005585	(Figure 2A)
PMID:18653539	PBO:0096560	(Figure 1B)
PMID:18658154	FYPO:0000878	We found that ers1Δ cells display a defect in both H3 Lys9 dimethylation and trimethylation (both normalized for nucleosome density) at the endogenous dh and dg regions of the centromeric outer repeats (Fig. 1B).
PMID:18658154	FYPO:0000884	We found that ers1Δ cells display a defect in both H3 Lys9 dimethylation and trimethylation (both normalized for nucleosome density) at the endogenous dh and dg regions of the centromeric outer repeats (Fig. 1B).
PMID:18658154	FYPO:0000890	We found that ers1Δ cells display a defect in both H3 Lys9 dimethylation and trimethylation (both normalized for nucleosome density) at the endogenous dh and dg regions of the centromeric outer repeats (Fig. 1B).
PMID:18658154	FYPO:0003744	As shown in Fig. 1C, recruitment of RITS to both sites was abolished in ers1Δ cells.
PMID:18658154	FYPO:0002567	nalysis revealed robust accumulation of the centromeric dg transcript in ers1Δ cells (Fig. 2A).
PMID:18658154	FYPO:0006076	We observed an apparently complete defect in siRNA production (Fig. 2B).
PMID:18658154	FYPO:0000888	We found that ers1Δ cells display a defect in both H3 Lys9 dimethylation and trimethylation (both normalized for nucleosome density) at the endogenous dh and dg regions of the centromeric outer repeats (Fig. 1B).
PMID:18658154	FYPO:0007334	ers1Δ mutant is completely defective in the silencing of ura4+ genes placed in the inner or outer repeats of cen1.
PMID:18658154	FYPO:0002336	no defect in silencing of ura4+ reporter genes placed at mat3M or tel2R, where RNAi- dependent mechanisms act redundantly with RNAi-independent silencing mechanisms.
PMID:18658154	FYPO:0003555	no defect in silencing of ura4+ reporter genes placed at mat3M or tel2R, where RNAi- dependent mechanisms act redundantly with RNAi-independent silencing mechanisms.
PMID:18662319	GO:0034634	(comment: also L-gamma-glutamyl-L-cysteine)
PMID:18667531	FYPO:0001234	(comment: CHECK synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81) (Figure 2, C and D).
PMID:18667531	GO:0006281	On the basis of these data, we propose that the Nse1 NH-RING contributes to the DNA repair functions of the Smc5-Smc6 holocomplex.
PMID:18667531	FYPO:0000674	The C219A mutant was not temperature sensitive (Figure 2A).
PMID:18667531	FYPO:0001357	The 􏰂RING, C197A, C199A, and C197A/C199A mutants were mildly temperature sensitive but grew normally at 25°C (Figure 2A and data not shown)
PMID:18667531	FYPO:0001357	The 􏰂RING, C197A, C199A, and C197A/C199A mutants were mildly temperature sensitive but grew normally at 25°C (Figure 2A and data not shown)
PMID:18667531	FYPO:0001357	The 􏰂RING, C197A, C199A, and C197A/C199A mutants were mildly temperature sensitive but grew normally at 25°C (Figure 2A and data not shown)
PMID:18667531	PBO:0093556	The 􏰂RING, C197A, C199A, and C197A/C199A mutants were mildly temperature sensitive but grew normally at 25°C (Figure 2A and data not shown)
PMID:18667531	PBO:0093556	The 􏰂RING, C197A, C199A, and C197A/C199A mutants were mildly temperature sensitive but grew normally at 25°C (Figure 2A and data not shown)
PMID:18667531	PBO:0093556	The 􏰂RING, C197A, C199A, and C197A/C199A mutants were mildly temperature sensitive but grew normally at 25°C (Figure 2A and data not shown)
PMID:18667531	PBO:0104010	The Nse1-Nse3 interaction is not perturbed by deletion of Nse1 NH-RING as tested by yeast two-hybrid assay, which is consistent with a previous report (Figure 5B and Sergeant et al., 2005).
PMID:18667531	FYPO:0002061	(comment: CHECK synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81) (Figure 2, C and D).
PMID:18667531	FYPO:0002061	(comment: CHECK synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81) (Figure 2, C and D).
PMID:18667531	FYPO:0001234	(comment: CHECK synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81) (Figure 2, C and D).
PMID:18667531	FYPO:0004329	(comment: nulcleolus inheritance)
PMID:18676809	FYPO:0000268	(Fig. 4a)
PMID:18676809	PBO:0105612	Conversely, mutations disrupting dimerization did not disrupt -H2A.1 binding (Fig. 3C).
PMID:18676809	PBO:0105612	Conversely, mutations disrupting dimerization did not disrupt -H2A.1 binding (Fig. 3C).
PMID:18676809	PBO:0105611	Conversely, mutations disrupting dimerization did not disrupt -H2A.1 binding (Fig. 3C).
PMID:18676809	PBO:0105611	Conversely, mutations disrupting dimerization did not disrupt -H2A.1 binding (Fig. 3C).
PMID:18676809	PBO:0105610	the Ser666Arg and Cys663Arg mutants ran as monomeric species in gel filtration, indicative of disruption of their dimerization
PMID:18676809	PBO:0105610	the Ser666Arg and Cys663Arg mutants ran as monomeric species in gel filtration, indicative of disruption of their dimerization
PMID:18676809	FYPO:0000006	(Fig. 4a)
PMID:18676809	PBO:0105609	Consistent with their observed structural roles, charge reversal mutations Arg616Glu, Lys617Glu, and Lys619Glu all abolished Crb2-BRCT2 interaction with the peptide (Fig. 3A)
PMID:18676809	PBO:0105609	Consistent with their observed structural roles, charge reversal mutations Arg616Glu, Lys617Glu, and Lys619Glu all abolished Crb2-BRCT2 interaction with the peptide (Fig. 3A)
PMID:18676809	PBO:0105609	Consistent with their observed structural roles, charge reversal mutations Arg616Glu, Lys617Glu, and Lys619Glu all abolished Crb2-BRCT2 interaction with the peptide (Fig. 3A)
PMID:18676809	FYPO:0000085	(Fig. 4a)
PMID:18676809	PBO:0105608	"(comment: CHECK "")"
PMID:18676809	FYPO:0000085	(Fig. 4a)
PMID:18676809	PBO:0105608	"(comment: CHECK "")"
PMID:18676809	FYPO:0000088	(Fig. 4a)
PMID:18676809	PBO:0105607	Consistent with their observed structural roles, charge reversal mutations Arg616Glu, Lys617Glu, and Lys619Glu all abolished Crb2-BRCT2 interaction with the peptide (Fig. 3A)
PMID:18676809	PBO:0105607	Consistent with their observed structural roles, charge reversal mutations Arg616Glu, Lys617Glu, and Lys619Glu all abolished Crb2-BRCT2 interaction with the peptide (Fig. 3A)
PMID:18676809	PBO:0105608	"(comment: CHECK "")"
PMID:18676809	PBO:0105607	Consistent with their observed structural roles, charge reversal mutations Arg616Glu, Lys617Glu, and Lys619Glu all abolished Crb2-BRCT2 interaction with the peptide (Fig. 3A)
PMID:18676809	FYPO:0000085	(Fig. 4a)
PMID:18676809	FYPO:0000088	(Fig. 4a)
PMID:18676809	FYPO:0000268	(Fig. 4a)
PMID:18676809	FYPO:0000088	(Fig. 4a)
PMID:18676809	FYPO:0000268	(Fig. 4a)
PMID:18716626	PBO:0096735	(Figure 1g) (comment: 30% cells?)
PMID:18716626	PBO:0096739	(Fig. 2e) Sgo1 localization is impaired in swi6D cells
PMID:18716626	PBO:0096738	(Supplementary Fig. 4). The transcriptional silencing of Swi6 is not relevant to this function, because swi6-sm1 cells have intact meiotic chromosome segregation
PMID:18716626	FYPO:0003182	(Fig. 2a, 2b) As with sgo1D cells, swi6D cells undergo intact meiosis I but suffer a nondisjunction of sister chromatids in meiosis II
PMID:18716626	PBO:0112511	(Fig. 2a, 2b) As with sgo1D cells, swi6D cells undergo intact meiosis I but suffer a nondisjunction of sister chromatids in meiosis II
PMID:18716626	FYPO:0007994	(Fig. 3f and Supplementary Fig. 8). The Sgo1-VE protein, when fused with CDand thereby localized to the centromere, can perform its full functionin protecting Rec8
PMID:18716626	FYPO:0003182	(Fig. 3f). The assay of chromosome segregation further revealed that sgo1-VE cells provoke nondisjunction in meiosis II, similarly to swi6D cells
PMID:18716626	PBO:0109343	various: These results indicate that Swi6 is crucial in localizing Sgo1 and thereby promotes the protection of cohesin from separase during anaphase I.
PMID:18716626	FYPO:0007993	(Fig. 3c) Accordingly, the replacement of Val 242 with Glu (VE) in Sgo1 abolished the interaction with Swi6 while preserving the interaction with Par1, a subunit of PP2A. An immunoprecipitation assay also supports the loss of the interaction of Sgo1-VE with Swi6
PMID:18716626	PBO:0096744	(Fig. 3c) Accordingly, the replacement of Val 242 with Glu (VE) in Sgo1 abolished the interaction with Swi6 while preserving the interaction with Par1, a subunit of PP2A. An immunoprecipitation assay also supports the loss of the interaction of Sgo1-VE with Swi6
PMID:18716626	FYPO:0002353	(Supplementary Fig. 3a). We confirmed that the expression of Psc3-2CD does not restore transcriptional silencing in swi6D cells
PMID:18716626	PBO:0096734	(Fig. 1e, 1f) As predicted, the additional expression of Psc3-2CD (but not of 2CD alone) improved the localization of the cohesin complex to the peri-centromeric regions and also centromeric cohesion in swi6D cells
PMID:18716626	PBO:0096734	(Supplementary Fig. 2a) , but not in another heterochromatin-defective strain, clr4D, which lacks H3K9me (ref. 7)
PMID:18716626	PBO:0096734	(Supplementary Fig. 2a) We confirmed that Psc3-2CD, as well as 2CD, itself localizesat discrete nuclear dots in swi6D cell
PMID:18716626	PBO:0096733	(Fig. 1a-d)
PMID:18716626	FYPO:0000964	(Fig. 1a-d)
PMID:18716626	FYPO:0001513	(Fig. 1a-d)
PMID:18716626	FYPO:0002353	(Fig. 1a)
PMID:18716626	PBO:0096743	(Fig. 3c) Accordingly, the replacement of Val 242 with Glu (VE) in Sgo1 abolished the interaction with Swi6 while preserving the interaction with Par1, a subunit of PP2A. An immunoprecipitation assay also supports the loss of the interaction of Sgo1-VE with Swi6
PMID:18716626	PBO:0096740	(Fig. 2f) Sgo1-CD did indeed localize at the centromere regardless of swi6D
PMID:18716626	PBO:0112512	(Fig. 2a, 2b) As with sgo1D cells, swi6D cells undergo intact meiosis I but suffer a nondisjunction of sister chromatids in meiosis II
PMID:18716626	PBO:0112512	(Fig. 2a, 2b) As with sgo1D cells, swi6D cells undergo intact meiosis I but suffer a nondisjunction of sister chromatids in meiosis II
PMID:18723894	FYPO:0003084	no barrier activity with reversed polarity as in rtf1-S154L single mutant
PMID:18723894	FYPO:0003084	no barrier activity with reversed polarity as in rtf1-S154L single mutant
PMID:18723894	FYPO:0003352	"RTS1 inversion background abolishes DSB formation; ""decreased"" level in rtf1-W405G is relative to wild type and above the inverted-RTS1 background level"
PMID:18725402	FYPO:0002060	the pfh1-mt allele (mt) did complement pfh1D (Table 2, line 5)
PMID:18725402	PBO:0119963	(Fig. 2A)
PMID:18725402	FYPO:0002061	The pfh1-nuc allele (nuc) did not complement the pfh1D allele, indicating that the mitochondrial isoform of Pfh1p is essential (Table 2, line 4).
PMID:18725402	GO:0035861	WT Pfh1p-GFP colocalized with Rad22p- RFP in distinct nuclear foci (Fig. 2C).
PMID:18725402	FYPO:0002060	Importantly, combination of the pfh1-mt* allele with the pfh1-nuc allele (mt* X nuc) fully complemented the pfh1D strain at 18°C, arguing that the pfh1-mt* strain was indeed deficient in nuclear Pfh1p function (Table 2, line 12).
PMID:18725402	FYPO:0002060	Importantly, combination of the pfh1-mt* allele with the pfh1-nuc allele (mt* X nuc) fully complemented the pfh1D strain at 18°C, arguing that the pfh1-mt* strain was indeed deficient in nuclear Pfh1p function (Table 2, line 12).
PMID:18725402	FYPO:0002061	because the pfh1-mt* allele did not complement the catalytically inactive pfh1-K338A allele (mt* X cd) (Table 2, line 13), the ATPase/helicase activity of Pfh1p was essential in the nucleus.
PMID:18725402	FYPO:0002061	but the pfh1-nuc allele in combination with the pfh1-K338A allele (nuc X cd) did not (Table 2, line 16). Therefore, the ATPase/helicase activity of Pfh1p was also essential in mitochondria.
PMID:18725402	GO:0006281	Based on their elongated cellular morphology, and large number of Rad22 foci, we conclude that cells depleted of nuclear Pfh1p suffer persistent DNA damage, and this damage triggers a G2 -phase arrest.
PMID:18725402	GO:0006281	Based on their elongated cellular morphology, and large number of Rad22 foci, we conclude that cells depleted of nuclear Pfh1p suffer persistent DNA damage, and this damage triggers a G2 -phase arrest.
PMID:18725402	FYPO:0000088	(Fig. 7A)
PMID:18725402	FYPO:0000095	(Fig. 7A)
PMID:18725402	GO:0043504	Pfh1p was also essential in mitochondria (Table 2), where its depletion resulted in rapid loss of mtDNA and very slow growth (Fig. 3 and 5).
PMID:18725402	GO:0043504	Pfh1p was also essential in mitochondria (Table 2), where its depletion resulted in rapid loss of mtDNA and very slow growth (Fig. 3 and 5).
PMID:18725402	FYPO:0002061	when this strain was grown at 18°C, the pfh1-mt* allele did not complement pfh1D (402/ 407 His+ cells; Table 2, line 7).
PMID:18725402	GO:0005730	Since the two fusion proteins, Gar2p-mCherry and WT Pfh1p-GFP, colocalized (Fig. 2B), we conclude that nuclear Pfh1p is found throughout the nucleus but is concentrated in the nucleolus.
PMID:18725402	PBO:0119964	(Fig. 2A)
PMID:18725402	GO:0035861	WT Pfh1p-GFP colocalized with Rad22p- RFP in distinct nuclear foci (Fig. 2C).
PMID:18769921	FYPO:0001839	(comment: during vegetative growth because non-sporulating strains used)
PMID:18769921	FYPO:0004437	(comment: during vegetative growth because non-sporulating strains used)
PMID:18769921	FYPO:0001386	(comment: during vegetative growth because non-sporulating strains used)
PMID:18769921	FYPO:0000473	(comment: during vegetative growth because non-sporulating strains used)
PMID:18769921	FYPO:0001839	(comment: during vegetative growth because non-sporulating strains used)
PMID:18769921	PBO:0093631	(comment: slightly worse than sfr1delta alone)
PMID:18769921	PBO:0093618	slightly more sensitive at low temperature than standard
PMID:18794373	GO:0110035	(comment: binds at Ter3 site)
PMID:18794373	FYPO:0007206	(comment: arrest at Ter2 and Ter3 sites abolished)
PMID:18794373	FYPO:0007206	(comment: arrest at Ter2 and Ter3 sites abolished)
PMID:18794373	FYPO:0007206	(comment: arrest at Ter2 and Ter3 sites abolished)
PMID:18794373	FYPO:0007206	(comment: arrest at Ter2 and Ter3 sites abolished)
PMID:18794373	FYPO:0007206	(comment: arrest at Ter2 and Ter3 sites abolished)
PMID:18794373	FYPO:0007206	(comment: arrest at Ter2 and Ter3 sites abolished)
PMID:18809570	GO:0140720	(Fig. 7B)
PMID:18809570	PBO:0101110	(Fig. 7B)
PMID:18809570	PBO:0111014	(Fig. 7A)
PMID:18809570	GO:0031934	(Fig. 7A)
PMID:18809570	GO:0140720	(Fig. 7A)
PMID:18809570	GO:0005721	(Fig. 7A)
PMID:18809570	PBO:0112681	(Fig. 7A)
PMID:18809570	PBO:0112680	(Fig. 7B)
PMID:18809570	PBO:0095651	(Fig. 5B)
PMID:18809570	PBO:0095651	(Fig. 5B)
PMID:18809570	PBO:0111587	(Fig. 5A)
PMID:18809570	PBO:0111587	(Fig. 5A)
PMID:18809570	PBO:0108390	(Fig. 5A)
PMID:18809570	PBO:0098583	(Fig. 5A)
PMID:18809570	PBO:0098583	(Fig. 5A)
PMID:18809570	FYPO:0002360	(Fig. 5A)
PMID:18809570	PBO:0112679	(Fig. 4D)
PMID:18809570	PBO:0111115	(Fig. 4D)
PMID:18809570	PBO:0112679	(Fig. 4D)
PMID:18809570	PBO:0111115	(Fig. 4D)
PMID:18809570	PBO:0112678	(Fig. 4D)
PMID:18809570	PBO:0112677	(Fig. 4D)
PMID:18809570	PBO:0095653	(Fig. 8D)
PMID:18809570	PBO:0095652	(Fig. 8H)
PMID:18809570	PBO:0095652	(Fig. 8H)
PMID:18809570	PBO:0095653	(Fig. 8H)
PMID:18809570	PBO:0095651	(Fig. 8H)
PMID:18809570	PBO:0095651	(Fig. 9A)
PMID:18809570	FYPO:0002336	(Fig. 9A)
PMID:18809570	PBO:0112683	(Fig. 9C)
PMID:18809570	FYPO:0007633	(Fig. 9D)
PMID:18809570	FYPO:0008209	(Fig. 9D)
PMID:18809570	PBO:0112676	(Fig. 4A)
PMID:18809570	PBO:0112676	(Fig. 4A)
PMID:18809570	PBO:0112675	(Fig. 4A)
PMID:18809570	PBO:0109218	(Fig. 4A)
PMID:18809570	PBO:0112674	(Fig. 4A)
PMID:18809570	PBO:0112673	(Fig. 4A)
PMID:18809570	GO:0031507	Chp2’s function is not exclusively associated with the establishment step and that its continued activity is critical for the maintenance of heterochromatin. Fig. 3
PMID:18809570	PBO:0095652	(Fig. 2G)
PMID:18809570	PBO:0095653	(Fig. 2E)
PMID:18809570	PBO:0112672	(Fig. 2D)
PMID:18809570	PBO:0112671	(Fig. 2C)
PMID:18809570	PBO:0095652	(Fig. 1E)
PMID:18809570	PBO:0112682	(Fig. 7A)
PMID:18809570	PBO:0095651	(Fig. 1D)
PMID:18809570	FYPO:0002336	(Fig. 1D)
PMID:18809570	PBO:0095651	(Fig. 1D)
PMID:18809570	PBO:0095651	(Fig. 1B and C)
PMID:18809570	PBO:0095653	(Fig. 1B and C)
PMID:18809570	PBO:0095652	(Fig. 8D)
PMID:18809570	PBO:0095653	(Fig. 8D)
PMID:18809570	PBO:0095651	(Fig. 8D)
PMID:18809570	GO:0031934	(Fig. 7B)
PMID:18809570	GO:0005721	(Fig. 7B)
PMID:18820678	FYPO:0004171	Moreover, fbp11 derepression is recovered by deleting both tup111 and tup121, indicating that Atf1 and Rst2 are dispensable for fbp11 induction in the absence of both Tup proteins
PMID:18820678	PBO:0111100	In the atf1- mutant, transcripts a and b are expressed normally, whereas transcripts c and d are absent (Fig. 4A).
PMID:18820678	PBO:0111101	In the atf1- mutant, transcripts a and b are expressed normally, whereas transcripts c and d are absent (Fig. 4A).
PMID:18820678	PBO:0111102	In the atf1- mutant, transcripts a and b are expressed normally, whereas transcripts c and d are absent (Fig. 4A).
PMID:18820678	PBO:0111103	In the atf1- mutant, transcripts a and b are expressed normally, whereas transcripts c and d are absent (Fig. 4A).
PMID:18820678	PBO:0111104	In the rst22 mutant, transcripts a, b, and c are expressed normally, whereas transcript d is absent (Fig. 4A).
PMID:18820678	PBO:0111103	In the rst22 mutant, transcripts a, b, and c are expressed normally, whereas transcript d is absent (Fig. 4A).
PMID:18820678	PBO:0111102	In the rst22 mutant, transcripts a, b, and c are expressed normally, whereas transcript d is absent (Fig. 4A).
PMID:18820678	PBO:0111100	In the rst22 mutant, transcripts a, b, and c are expressed normally, whereas transcript d is absent (Fig. 4A).
PMID:18820678	PBO:0111105	Chromatin remodelling events and RNAPII loading around the TATA box are severely impaired in an atf12 mutant, demonstrating that the progression of ncRNA initiation events mediated by Atf1 is essential to convert chromatin to an RNAPII accessible state (Fig. 4B).
PMID:18820678	FYPO:0008156	Expression of transcript c is not restored in the atf12tup112tup122 mutant, suggesting that Atf1 is essential to induce transcript c.
PMID:18820678	FYPO:0004171	Moreover, fbp11 derepression is recovered by deleting both tup111 and tup121, indicating that Atf1 and Rst2 are dispensable for fbp11 induction in the absence of both Tup proteins
PMID:18849471	GO:0004585	(comment: major)
PMID:18854158	FYPO:0000268	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000268	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000267	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000267	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000085	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	PBO:0100306	(comment: abolished interaction between wt and mutant; interaction partially restored if both copies are mutant)
PMID:18854158	FYPO:0000085	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000267	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000085	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000268	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000267	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000085	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	PBO:0100306	(comment: abolished interaction between wt and mutant; interaction partially restored if both copies are mutant)
PMID:18854158	FYPO:0000268	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18948543	FYPO:0003412	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0003412	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0004201	Moreover, mutants that alleviated cen1:ade6+ silencing also displayed increased levels of noncoding centromeric otr transcripts and concomitant reductions in centromeric siRNA accumulation, with prp10-1 showing the most severe silencing defects (Fig. 1C
PMID:18948543	FYPO:0004201	Moreover, mutants that alleviated cen1:ade6+ silencing also displayed increased levels of noncoding centromeric otr transcripts and concomitant reductions in centromeric siRNA accumulation, with prp10-1 showing the most severe silencing defects (Fig. 1C
PMID:18948543	FYPO:0004201	Moreover, mutants that alleviated cen1:ade6+ silencing also displayed increased levels of noncoding centromeric otr transcripts and concomitant reductions in centromeric siRNA accumulation, with prp10-1 showing the most severe silencing defects (Fig. 1C
PMID:18948543	PBO:0105941	Moreover, mutants that alleviated cen1:ade6+ silencing also displayed increased levels of noncoding centromeric otr transcripts and concomitant reductions in centromeric siRNA accumulation, with prp10-1 showing the most severe silencing defects (Fig. 1C
PMID:18948543	FYPO:0003619	However, at the permissive temperature of 25°C (at which centromeric silencing was alleviated), splicing efficiency was similar to that in wild-type cells (Fig. 2A).
PMID:18948543	FYPO:0003619	However, at the permissive temperature of 25°C (at which centromeric silencing was alleviated), splicing efficiency was similar to that in wild-type cells (Fig. 2A).
PMID:18948543	FYPO:0003619	However, at the permissive temperature of 25°C (at which centromeric silencing was alleviated), splicing efficiency was similar to that in wild-type cells (Fig. 2A).
PMID:18948543	FYPO:0003619	However, at the permissive temperature of 25°C (at which centromeric silencing was alleviated), splicing efficiency was similar to that in wild-type cells (Fig. 2A).
PMID:18948543	PBO:0097401	Chromatin immunoprecipitation (ChIP) revealed that splicing mutants cwf10-1 and prp10-1 (but not prp2-1) exhibited only a modest decrease in levels of H3K9me2 associated with both centromere repeats and cen1:ura4+ (Fig. 3A and fig. S3).
PMID:18948543	FYPO:0004742	we surveyed several additional ts lethal splicing mutants for silencing defects at the permissive temperature (11-14). Only particular splicing mutants affected silencing. Silencing of a centromeric cen1:ade6+ marker gene (Fig. 1A) remained intact in the presence of prp1 (Prp6Sc/Hs), prp2 (U2AFHs), prp3 (Prp3Sc/PRPF3Hs), or prp4 (PRPF4BHs) mutations
PMID:18948543	FYPO:0004742	we surveyed several additional ts lethal splicing mutants for silencing defects at the permissive temperature (11-14). Only particular splicing mutants affected silencing. Silencing of a centromeric cen1:ade6+ marker gene (Fig. 1A) remained intact in the presence of prp1 (Prp6Sc/Hs), prp2 (U2AFHs), prp3 (Prp3Sc/PRPF3Hs), or prp4 (PRPF4BHs) mutations
PMID:18948543	FYPO:0004742	we surveyed several additional ts lethal splicing mutants for silencing defects at the permissive temperature (11-14). Only particular splicing mutants affected silencing. Silencing of a centromeric cen1:ade6+ marker gene (Fig. 1A) remained intact in the presence of prp1 (Prp6Sc/Hs), prp2 (U2AFHs), prp3 (Prp3Sc/PRPF3Hs), or prp4 (PRPF4BHs) mutations
PMID:18948543	FYPO:0004742	we surveyed several additional ts lethal splicing mutants for silencing defects at the permissive temperature (11-14). Only particular splicing mutants affected silencing. Silencing of a centromeric cen1:ade6+ marker gene (Fig. 1A) remained intact in the presence of prp1 (Prp6Sc/Hs), prp2 (U2AFHs), prp3 (Prp3Sc/PRPF3Hs), or prp4 (PRPF4BHs) mutations
PMID:18948543	FYPO:0003412	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0003412	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0003412	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0003412	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0000220	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0000220	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	PBO:0094684	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0000220	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0000220	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0000220	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0003412	We therefore constructed strains in which the endogenous ago1+ and hrr1+ genes were replaced by cDNAs. Even in these strains, the prp10-1 mutation alleviated silencing as in wild-type cells (Fig. 2C, white colonies).
PMID:18948543	FYPO:0003412	We therefore constructed strains in which the endogenous ago1+ and hrr1+ genes were replaced by cDNAs. Even in these strains, the prp10-1 mutation alleviated silencing as in wild-type cells (Fig. 2C, white colonies).
PMID:18948543	PBO:0111071	Chromatin immunoprecipitation (ChIP) revealed that splicing mutants cwf10-1 and prp10-1 (but not prp2-1) exhibited only a modest decrease in levels of H3K9me2 associated with both centromere repeats and cen1:ura4+ (Fig. 3A and fig. S3).
PMID:18948543	PBO:0111071	Chromatin immunoprecipitation (ChIP) revealed that splicing mutants cwf10-1 and prp10-1 (but not prp2-1) exhibited only a modest decrease in levels of H3K9me2 associated with both centromere repeats and cen1:ura4+ (Fig. 3A and fig. S3).
PMID:18948543	PBO:0108387	Chromatin immunoprecipitation (ChIP) revealed that splicing mutants cwf10-1 and prp10-1 (but not prp2-1) exhibited only a modest decrease in levels of H3K9me2 associated with both centromere repeats and cen1:ura4+ (Fig. 3A and fig. S3).
PMID:18948543	FYPO:0003097	(Fig. 3A and fig. S3).
PMID:18948543	PBO:0097401	Chromatin immunoprecipitation (ChIP) revealed that splicing mutants cwf10-1 and prp10-1 (but not prp2-1) exhibited only a modest decrease in levels of H3K9me2 associated with both centromere repeats and cen1:ura4+ (Fig. 3A and fig. S3).
PMID:18948543	FYPO:0003619	However, at the permissive temperature of 25°C (at which centromeric silencing was alleviated), splicing efficiency was similar to that in wild-type cells (Fig. 2A).
PMID:18948543	FYPO:0003619	However, at the permissive temperature of 25°C (at which centromeric silencing was alleviated), splicing efficiency was similar to that in wild-type cells (Fig. 2A).
PMID:18951025	PBO:0106929	(comment: one or more of mutated serine residues)
PMID:18951025	PBO:0106929	(comment: one or more of mutated serine residues)
PMID:18957202	FYPO:0007345	About 50% (2665 out of 5241) of the genes in the genome were downregulated in mutant cells compared to WT (Figure 6C and Table S3), consistent with the formation of ectopic heterochromatin.
PMID:18957202	PBO:0105306	We also examined the GFP-Swi6 distribution in the mutants (Figure 7B). While the lid2-phd1 mutant is similar to the WT, the nuclei in the lid2-phd2 and lid2-phd3 mutants often contained excessive GFP- Swi6 dots, suggesting that euchromatin assembly is disrupted in the mutants (Figure 7B).
PMID:18957202	FYPO:0000877	Obvious reduction of H3K9 methylation was also observed in lid2-phd2 and lid2-phd3 mutants (Figure S9)
PMID:18957202	FYPO:0000877	Obvious reduction of H3K9 methylation was also observed in lid2-phd2 and lid2-phd3 mutants (Figure S9)
PMID:18957202	PBO:0096189	silencing at the imr region in lid2-phd2 and lid2-phd3 mutants was significantly impaired while lid2-phd1 showed only a slight defect (Figure 7A).
PMID:18957202	PBO:0095834	silencing at the imr region in lid2-phd2 and lid2-phd3 mutants was significantly impaired while lid2-phd1 showed only a slight defect (Figure 7A).
PMID:18957202	PBO:0096189	silencing at the imr region in lid2-phd2 and lid2-phd3 mutants was significantly impaired while lid2-phd1 showed only a slight defect (Figure 7A).
PMID:18957202	PBO:0105549	We also examined the GFP-Swi6 distribution in the mutants (Figure 7B). While the lid2-phd1 mutant is similar to the WT, the nuclei in the lid2-phd2 and lid2-phd3 mutants often contained excessive GFP- Swi6 dots, suggesting that euchromatin assembly is disrupted in the mutants (Figure 7B).
PMID:18957202	PBO:0105549	In contrast to the overexpression of Lid2 alone, which leads to a dramatic decrease in H3K4me3 (Figure 4B), reduction of H3K4me3 is minimal when Set1 or Lsd1 is also overexpressed (Figure 4C).
PMID:18957202	FYPO:0000825	We further noted the striking similarity of the genome-wide transcription profiles of the lid2-j and lsd1Δ mutants (Figure 6C), suggest
PMID:18957202	PBO:0105548	(comment: RNAI dependent)
PMID:18957202	PBO:0105306	We next examined Swi6 localization in the lid2-j mutant using N-terminal tagged GFP-Swi6. In WT vegetative cells, 3-4 GFP-Swi6 spots are observed. This is because the three centromeres cluster on the nuclear envelope in the vicinity of the spindle pole body whereas telomeres loosely cluster on the nuclear envelope, apart from centromeres. clr4 and clr8 mutants have a diffuse Swi6 localization due to the disruption of heterochromatin. To our surprise, we did not see the same GFP-Swi6 pattern in the lid2-j mutant as in clr8Δ. Rather, we found that 78% of the cells contain more than 5 GFP-Swi6 spots, with nearly 30% having more than 10 spots (Figure 6A). The abnormal distribution of Swi6 also can be observed in meiotic horsetail stage nuclei (Figure 6A). The aberrant Swi6 localization is not caused by defects in centromere or telomere clustering since the distribution of centromeres and telomeres, as marked by Cnp1-GFP or Taz1-GFP respectively, is unaffected in the lid2-j mutant (Figure S4). We further confirmed that telomeres cluster normally by visualizing their distribution in a lid2-j strain carrying mCherry-Swi6 and the telomere marker Taz1-GFP (Figure S4). These results suggest that heterochromatin is induced in euchromatic regions in lid2-j.
PMID:18957202	PBO:0105547	the point mutation had little effect on the interaction of Lid2 with its interacting partners, such as Cul4 and Set1 (Figure S3 and S8).
PMID:18957202	PBO:0105546	the point mutation had little effect on the interaction of Lid2 with its interacting partners, such as Cul4 and Set1 (Figure S3 and S8).
PMID:18957202	FYPO:0007337	ChIP assays indicated that H3K9me2 methylation at the region was abolished, while H3K4me3 methylation was increased more than seven-fold (Figure S2)
PMID:18957202	FYPO:0004170	ChIP assays indicated that H3K9me2 methylation at the region was abolished, while H3K4me3 methylation was increased more than seven-fold (Figure S2)
PMID:18957202	PBO:0094283	(Figure 5F) the point mutation resulted in a significant loss of silencing at the centromere otr region.
PMID:18957202	PBO:0120498	As shown in Figure 5E, while Lid2 accumulated at centromeres in the WT, the centromere localization of Lid2 in the clr8 mutant is significantly decreased.
PMID:18957202	GO:0005721	GFP-Lid2 is resistant to detergent extraction indicating Lid2 is a chromatin-binding protein (Figure 2A).showed enrichment of DNA from centromeres and the mating-type region, indicating Lid2 is associated with heterochromatin (Figure 2B).
PMID:18957202	PBO:0120497	In WT cells, Myc- Clr8 associates with centromere otr regions, but not in lid2-j suggesting that Lid2 is required for Clr8 association with heterochromatin (Figure 5E).
PMID:18957202	PBO:0120496	As shown in Figure 5D, the association of Ago1 with the centromere is significantly reduced in lid2-j, indicating that Lid2 is required for RITS to load onto centromeres.
PMID:18957202	PBO:0105543	As shown in Figure 5C, siRNA is barely detectable.
PMID:18957202	FYPO:0000220	forward and reverse centromeric strands were detected in lid2-j and accumulated at the same level as in clr8Δ, suggesting that Lid2 is involved in the RNAi pathway.
PMID:18957202	FYPO:0007339	forward and reverse centromeric strands were detected in lid2-j and accumulated at the same level as in clr8Δ, suggesting that Lid2 is involved in the RNAi pathway.
PMID:18957202	PBO:0105542	H3K4me3 staining was reduced to nearly undetectable levels in 82% of the cells overexpressing Lid2, suggesting that Lid2 can specifically demethylate H3K4 me3 (Figure 4B)
PMID:18957202	FYPO:0000874	overexpressing Lid2 enhances H3K9 methylation (Figures 5G and H)
PMID:18957202	PBO:0120495	We then determined whether Lid2 is required for the recruitment of Clr4 to heterochromatin. We carried out a ChIP experiment using lid2-j or clr8Δ containing a N-terminal FLAG-tagged Clr4. The localization of Clr4 at centromeres is abrogated in both mutants (Figure 3E).
PMID:18957202	PBO:0120495	We then determined whether Lid2 is required for the recruitment of Clr4 to heterochromatin. We carried out a ChIP experiment using lid2-j or clr8Δ containing a N-terminal FLAG-tagged Clr4. The localization of Clr4 at centromeres is abrogated in both mutants (Figure 3E).
PMID:18957202	PBO:0120485	drastic reduction of Swi6 binding (Figure 3D).
PMID:18957202	FYPO:0007338	In contrast, H3K4me3 methylation was increased significantly (Figure 3C)
PMID:18957202	FYPO:0004170	As shown in Figure 3B, H3K9 methylation at the centromere was completely abolished.
PMID:18957202	FYPO:0007336	mating-type region was likewise reduced (Figure 3A)
PMID:18957202	FYPO:0007335	We found that deletion of the Lid2 JmjC domain resulted in the complete loss of ura4+ silencing at both the otr and imr loci (Figure 3A and Figure 7A).
PMID:18957202	FYPO:0007334	We found that deletion of the Lid2 JmjC domain resulted in the complete loss of ura4+ silencing at both the otr and imr loci (Figure 3A and Figure 7A).
PMID:18957202	PBO:0093562	As shown in Figure 2E, lid2-j, like clr8Δ, is hypersensitive to TBZ
PMID:18957202	PBO:0105540	28% of the cells contained fragmented nuclear DNA (Figure 2D), indicating that the mutant nucleus is disorganized.
PMID:18957202	FYPO:0003481	WT and frequently exhibited an aberrant elongated cell shape (Figure 2C)
PMID:18957202	FYPO:0002151	We deleted one copy of lid2+ by kanamycin reporter gene replacement (kan+) in a WT diploid strain (lid2+/lid2Δ::kan+) and tetrad analysis was performed after sporulation. Only two germinating spores from a tetrad were viable, confirming that lid2+ is an essential gene
PMID:18957202	GO:0005721	GFP-Lid2 is resistant to detergent extraction indicating Lid2 is a chromatin-binding protein (Figure 2A).showed enrichment of DNA from centromeres and the mating-type region, indicating Lid2 is associated with heterochromatin (Figure 2B).
PMID:18957202	GO:0031934	GFP-Lid2 is resistant to detergent extraction indicating Lid2 is a chromatin-binding protein (Figure 2A).showed enrichment of DNA from centromeres and the mating-type region, indicating Lid2 is associated with heterochromatin (Figure 2B).
PMID:18957202	GO:0003682	GFP-Lid2 is resistant to detergent extraction indicating Lid2 is a chromatin-binding protein (Figure 2A).
PMID:18957202	GO:0005634	(Figure 2A)
PMID:18957202	PBO:0101470	(Figure 1A)
PMID:1899284	GO:0001228	(comment: also supported by complementation of S.c. deletion)
PMID:19001497	PBO:0098075	(Fig. 2a) (comment: this fig also has expression level for mutant alleles)
PMID:19001497	GO:0044732	(Fig. 2B, 2C)
PMID:19001497	GO:0000923	(Fig. 2B, 2C)
PMID:19001497	GO:0031021	(Fig. 2B, 2C)
PMID:19001497	PBO:0098076	(Fig. 2D-F)
PMID:19001497	PBO:0098076	(Fig. 2D-F)
PMID:19001497	PBO:0094146	(Fig. 2D-F)
PMID:19001497	PBO:0094146	(Fig. 2D-F)
PMID:19001497	PBO:0098077	(Fig. 2D-F)
PMID:19001497	PBO:0098078	(Fig. 2D-F)
PMID:19001497	PBO:0098078	(Fig. 2D-F)
PMID:19001497	PBO:0098079	(Fig. 2D-F)
PMID:19001497	PBO:0094143	(Fig. 2D-F)
PMID:19001497	PBO:0094143	(Fig. 2D-F)
PMID:19001497	PBO:0098080	(Fig. 3)
PMID:19001497	PBO:0098082	(Fig. 4a)
PMID:19001497	PBO:0098081	(Fig. 3)
PMID:19001497	PBO:0098081	(Fig. 3)
PMID:19001497	FYPO:0004619	supplementary material Movies 2-4).
PMID:19001497	FYPO:0002112	(Fig. 4c)
PMID:19001497	PBO:0098083	(Fig. 4c)
PMID:19001497	FYPO:0005696	(Fig. 4D)
PMID:19001497	FYPO:0005699	(Fig. 4D)
PMID:19001497	FYPO:0005696	(Fig. 1E)
PMID:19001497	PBO:0098084	supplementary material Fig. S1)
PMID:19001497	PBO:0098085	(Fig. 4F)
PMID:19001497	PBO:0098084	supplementary material Fig. S1)
PMID:19001497	PBO:0098085	(Fig. 4F)
PMID:19001497	PBO:0098086	(Fig. 1D, 1E)
PMID:19001497	PBO:0098087	we conclude that the function of Mto2 in MT nucleation is mediated primarily, if not exclusively, via its binding to Mto1. Moreover, the failure of Mto1-334 to immunoprecipitate the γ-TuC indicates that the Mto1-Mto2 interaction is required for an efficient association of Mto1 with the γ-TuC, as detected in cytoplasmic extracts.
PMID:19001497	PBO:0098087	we conclude that the function of Mto2 in MT nucleation is mediated primarily, if not exclusively, via its binding to Mto1. Moreover, the failure of Mto1-334 to immunoprecipitate the γ-TuC indicates that the Mto1-Mto2 interaction is required for an efficient association of Mto1 with the γ-TuC, as detected in cytoplasmic extracts.
PMID:19001497	PBO:0098086	(Fig. 1D)
PMID:19001497	PBO:0098086	(Fig. 1D, 1E)
PMID:19001497	PBO:0019206	(Fig. 1C)
PMID:19001497	PBO:0019206	(Fig. 1C)
PMID:19001497	PBO:0019223	(Fig. 1C)
PMID:19001497	PBO:0019206	(Fig. 1C)
PMID:19001497	PBO:0036769	(Fig. 1D)
PMID:19001497	PBO:0036769	(Fig. 1D, 1E)
PMID:19001497	PBO:0036769	(Fig. 1D, 1E)
PMID:19001497	PBO:0098074	(Fig. 1D, 1E)
PMID:19001497	FYPO:0004511	(Fig. 1E)
PMID:19001497	FYPO:0004511	(Fig. 1E)
PMID:19001497	FYPO:0004511	(Fig. 1E)
PMID:19001497	FYPO:0005691	supplementary material Movies 2-4).
PMID:19001497	FYPO:0005691	supplementary material Movies 2-4).
PMID:19001497	FYPO:0005691	supplementary material Movies 2-4).
PMID:19023408	FYPO:0005911	Southern blot
PMID:19023408	FYPO:0005911	Southern blot
PMID:19023408	FYPO:0005136	Southern blot
PMID:19023408	GO:0035861	ChIP
PMID:19023408	FYPO:0005136	microarray
PMID:19023408	FYPO:0005136	Southern blot
PMID:19023408	GO:0045027	forms covalent linkage upon binding (wouldn't normally use ChIP as IDA for DNA binding MF, but the phenol extraction with or without protease adds more confidence)
PMID:19023408	FYPO:0005911	Southern blot
PMID:19026779	PBO:0107732	(Figure 4D)
PMID:19026779	PBO:0107732	(Figure 4D)
PMID:19026779	PBO:0112758	(Figure 4D)
PMID:19026779	PBO:0107730	(Figure 4D)
PMID:19026779	PBO:0107732	(Figure 4D)
PMID:19026779	PBO:0107730	(Figure 4D)
PMID:19026779	PBO:0107732	(Figure 4D)
PMID:19026779	PBO:0107733	(Figure 4D)
PMID:19026779	PBO:0107731	(Figure 4D)
PMID:19026779	PBO:0107730	(Figure 4D)
PMID:19026779	PBO:0094855	(Figure 4D)
PMID:19026779	PBO:0107730	(Figure 4D)
PMID:19026779	PBO:0107730	(Figure 4D)
PMID:19026779	PBO:0107732	(Figure 4D)
PMID:19026779	PBO:0107730	(Figure 4D)
PMID:19026779	PBO:0107733	(Figure 4D)
PMID:19026779	PBO:0107732	(Figure 4D)
PMID:19026779	PBO:0107733	(Figure 4D)
PMID:19026779	PBO:0107730	(Figure 4D)
PMID:19026779	PBO:0107732	(Figure 4D)
PMID:19026779	PBO:0107732	(Figure 4D)
PMID:19026779	PBO:0107733	(Figure 4D)
PMID:19026779	PBO:0107734	(Figure 4D)
PMID:19026779	PBO:0107730	(Figure 4D)
PMID:19026779	PBO:0107732	(Figure 4D)
PMID:19026779	PBO:0107730	(Figure 4D)
PMID:19026779	PBO:0107730	(Figure 4D)
PMID:19026779	PBO:0107730	(Figure 4D)
PMID:19033384	PBO:0033377	(comment: Use of Western blot to assay phosphorylation levels)
PMID:19033384	PBO:0033376	(comment: Use of Western blot to assay phosphorylation levels)
PMID:19033384	PBO:0100016	(comment: Use of Western blot to assay phosphorylation levels)
PMID:19033384	PBO:0033378	(comment: Use of Western blot to assay phosphorylation levels)
PMID:19033384	PBO:0021984	(comment: Use of Western blot to assay phosphorylation levels)
PMID:19033384	PBO:0021985	(comment: Use of Western blot to assay phosphorylation levels)
PMID:19033384	PBO:0021986	(comment: Use of Western blot to assay phosphorylation levels)
PMID:19033384	PBO:0021987	(comment: Use of Western blot to assay phosphorylation levels)
PMID:19033384	GO:0031571	The checkpoint doesn't sense all types of dna damage eg that caused by gamma radiation or DNA adduct formation by PUVA
PMID:19037094	PBO:0102960	(Fig. 3B)
PMID:19037094	PBO:0116916	(Fig. 7B)
PMID:19037094	PBO:0116915	(Fig. 7B)
PMID:19037094	PBO:0116925	(Fig. 7A)
PMID:19037094	PBO:0116924	(Fig. 6D and Fig. 7A)
PMID:19037094	PBO:0116923	(Fig. 7A)
PMID:19037094	PBO:0116922	(Fig. 6D)
PMID:19037094	PBO:0116922	(Fig. 6D)
PMID:19037094	PBO:0116921	(Fig. 6D)
PMID:19037094	GO:1903139	Rgf1p, a Rho1p-specific GEF, is a new member of the Pmk1p MAPK pathway in fission yeast.
PMID:19037094	FYPO:0001883	(Fig. 1)
PMID:19037094	FYPO:0001883	(Fig. 1)
PMID:19037094	FYPO:0001473	(Fig. 2A)
PMID:19037094	FYPO:0001214	(Fig. 2C)
PMID:19037094	FYPO:0001214	(Fig. 2C)
PMID:19037094	PBO:0116911	(Fig. 2D and Fig. 3B)
PMID:19037094	PBO:0116911	(Fig. 2D and Fig. 3B)
PMID:19037094	PBO:0116911	(Fig. 2D and Fig. 3B)
PMID:19037094	FYPO:0000079	(Fig. 2D)
PMID:19037094	FYPO:0000079	(Fig. 2D)
PMID:19037094	PBO:0102960	(Fig. 1, Fig. 2D and Fig. 3)
PMID:19037094	FYPO:0001883	(Fig. 2D)
PMID:19037094	FYPO:0001883	(Fig. 2D)
PMID:19037094	FYPO:0001883	(Fig. 2D)
PMID:19037094	FYPO:0001883	(Fig. 3A)
PMID:19037094	FYPO:0001883	(Fig. 3A)
PMID:19037094	PBO:0102960	(Fig. 3B)
PMID:19037094	PBO:0102960	(Fig. 3B)
PMID:19037094	PBO:0116912	(Fig. 4A)
PMID:19037094	PBO:0116913	(Fig. 4A)
PMID:19037094	PBO:0116913	(Fig. 4C)
PMID:19037094	PBO:0116914	(Fig. 4B)
PMID:19037094	PBO:0116915	(Fig. 4D)
PMID:19037094	PBO:0116916	(Fig. 4E)
PMID:19037094	PBO:0116917	(Fig. 4F)
PMID:19037094	PBO:0116918	(Fig. 5)
PMID:19037094	PBO:0116919	(Fig. 5)
PMID:19037094	PBO:0116920	(Fig. 6A)
PMID:19037094	PBO:0116912	(Fig. 6C)
PMID:19037094	PBO:0115480	(Fig. 6D)
PMID:19037094	PBO:0115480	(Fig. 6D)
PMID:19037094	PBO:0115480	(Fig. 6D)
PMID:19037094	PBO:0115480	(Fig. 6D)
PMID:19037094	PBO:0115480	(Fig. 6D)
PMID:19037094	PBO:0115480	(Fig. 6D)
PMID:19037094	PBO:0116921	(Fig. 6D)
PMID:19037094	PBO:0116921	(Fig. 6D)
PMID:19037094	PBO:0116921	(Fig. 6D)
PMID:19037094	PBO:0116921	(Fig. 6D)
PMID:19037094	PBO:0116920	(Fig. 6A)
PMID:19037094	FYPO:0002720	(Fig. 2B)
PMID:19037094	FYPO:0002720	(Fig. 2B)
PMID:19037094	FYPO:0001473	(Fig. 2A)
PMID:19037094	FYPO:0001473	(Fig. 2A)
PMID:19037094	PBO:0116916	(Fig. 7C)
PMID:19037094	PBO:0116916	(Fig. 7C)
PMID:19037094	PBO:0116916	(Fig. 7C)
PMID:19037094	PBO:0116917	(Fig. 7C)
PMID:19037094	PBO:0116915	(Fig. 7C)
PMID:19037094	PBO:0116926	(Fig. 7B)
PMID:19037094	PBO:0116916	(Fig. 7B)
PMID:19037096	GO:0008574	(Figure 4, A and B, and Supplemental Movie S1)
PMID:1905818	GO:0003924	(comment: changed to GTPase from signal transducer)
PMID:1905818	FYPO:0000280	(comment: haploid, either mating type)
PMID:19075108	FYPO:0008204	(Fig. 2, Fig. 3)
PMID:19075108	PBO:0112551	(Fig. 2B and C)
PMID:19075108	PBO:0112550	(Fig. 2B and C)
PMID:19075108	PBO:0112550	(Fig. 2B and C)
PMID:19075108	PBO:0112543	(Fig. 1A)
PMID:19075108	PBO:0112544	(Fig. 1A)
PMID:19075108	PBO:0112554	These results furthered the notion that the function of Mid1p and cortical nodes was important for organization of normal actomyosin rings in early mitosis.
PMID:19075108	FYPO:0007827	(Fig. 5D)
PMID:19075108	FYPO:0007827	(Fig. 5D)
PMID:19075108	PBO:0112553	(Fig. 5A, B and C)
PMID:19075108	PBO:0112552	(Fig. 4)
PMID:19075108	FYPO:0008204	(Fig. 2, Fig. 3)
PMID:19075108	FYPO:0006005	(Fig. 2B)
PMID:19075108	PBO:0112551	(Fig. 2B and C)
PMID:19075108	PBO:0112550	(Fig. 2B and C)
PMID:19075108	PBO:0112551	(Fig. 2B and C)
PMID:19075108	PBO:0112551	(Fig. 2B and C)
PMID:19075108	PBO:0112550	(Fig. 2B and C)
PMID:19075108	PBO:0112548	(Fig. 2A and C)
PMID:19075108	PBO:0112549	(Fig. 2A and C)
PMID:19075108	PBO:0112548	(Fig. 2A and C)
PMID:19075108	PBO:0112545	(Fig. 1A)
PMID:19075108	PBO:0112547	(Fig. 2A and C)
PMID:19075108	PBO:0112546	(Fig. 1A)
PMID:19111658	GO:0003723	(comment: binds centromeric transcripts)
PMID:19117951	FYPO:0002346	(comment: mat1Msmto REIIdelta mat2::ura4)
PMID:19117951	FYPO:0000156	(comment: gave dark staining with iodine,switch to the opposite state at a low rate)
PMID:19117951	FYPO:0000156	(comment: gave dark staining with iodine,switch to the opposite state at a low rate)
PMID:19117951	FYPO:0001234	(comment: mat1Msmto REIIdelta mat2::ura4)
PMID:19117951	PBO:0098599	(comment: mat1Msmto REIIdelta mat2::ura4)
PMID:19117951	FYPO:0000156	(comment: mat1Msmto REIIdelta mat2::ura4 gave dark staining with iodine, metastable and switch to the opposite state at a low rate)
PMID:19117951	PBO:0108055	(comment: mat1Msmto REIIdelta mat2::ura4)
PMID:19117951	FYPO:0000877	mat1Msmto REIIdelta mat2::ura4
PMID:19117951	FYPO:0002355	(comment: mat1Msmto REIIdelta mat2::ura4)
PMID:19117951	FYPO:0001886	(comment: mat1Msmto REIIdelta mat2::ura4)
PMID:19136623	PBO:0112917	Similarly, Clr3 and Mit1 localization was decreased in ckb1D and swi6-S18-117A mutants, although this decrease was less in swi6-S18-117A than in ckb1D cells.
PMID:19136623	PBO:0112915	Similarly, Clr3 and Mit1 localization was decreased in ckb1D and swi6-S18-117A mutants, although this decrease was less in swi6-S18-117A than in ckb1D cells.
PMID:19136623	PBO:0112915	Similarly, Clr3 and Mit1 localization was decreased in ckb1D and swi6-S18-117A mutants, although this decrease was less in swi6-S18-117A than in ckb1D cells.
PMID:19136623	PBO:0112917	Similarly, Clr3 and Mit1 localization was decreased in ckb1D and swi6-S18-117A mutants, although this decrease was less in swi6-S18-117A than in ckb1D cells.
PMID:19136623	PBO:0112917	In wild-type cells, both Clr3 and Mit1 were enriched on centromeric repeats; this localization was decreased in swi6D or chp2D cells, though substantial Mit1 was retained in swi6D cells, as reported previously (Sadaie et al. 2008).
PMID:19136623	PBO:0112915	In wild-type cells, both Clr3 and Mit1 were enriched on centromeric repeats; this localization was decreased in swi6D or chp2D cells, though substantial Mit1 was retained in swi6D cells, as reported previously (Sadaie et al. 2008).
PMID:19136623	PBO:0112917	In wild-type cells, both Clr3 and Mit1 were enriched on centromeric repeats; this localization was decreased in swi6D or chp2D cells, though substantial Mit1 was retained in swi6D cells, as reported previously (Sadaie et al. 2008).
PMID:19136623	PBO:0112915	In wild-type cells, both Clr3 and Mit1 were enriched on centromeric repeats; this localization was decreased in swi6D or chp2D cells, though substantial Mit1 was retained in swi6D cells, as reported previously (Sadaie et al. 2008).
PMID:19136623	PBO:0113576	In wild-type cells, both Clr3 and Mit1 were enriched on centromeric repeats; this localization was decreased in swi6D or chp2D cells, though substantial Mit1 was retained in swi6D cells, as reported previously (Sadaie et al. 2008).
PMID:19136623	PBO:0112915	In wild-type cells, both Clr3 and Mit1 were enriched on centromeric repeats; this localization was decreased in swi6D or chp2D cells, though substantial Mit1 was retained in swi6D cells, as reported previously (Sadaie et al. 2008).
PMID:19136623	PBO:0113575	swi6-S192-274A mutations did not affect silencing at the centromere (imr::ura4), while swi6-S18-24A and S18- 117A mutants displayed decreases in silencing (Fig. 3C).
PMID:19136623	PBO:0113575	swi6-S192-274A mutations did not affect silencing at the centromere (imr::ura4), while swi6-S18-24A and S18- 117A mutants displayed decreases in silencing (Fig. 3C).
PMID:19136623	FYPO:0002360	swi6-S192-274A mutations did not affect silencing at the centromere (imr::ura4), while swi6-S18-24A and S18- 117A mutants displayed decreases in silencing (Fig. 3C).
PMID:19136623	MOD:00046	Mass spectrometric analysis of Swi6 prepared from wild-type and ckb1D cells showed that five potential CK2 phosphorylation sites (S18, S24, S46, S52, and S117) in the N-terminal half are really phosphorylated in vivo, and the phosphorylation of four of them (S18, S24, S46, and S117) decreased in ckb1D cells (Supplemental Fig. S5).
PMID:19136623	MOD:00046	Mass spectrometric analysis of Swi6 prepared from wild-type and ckb1D cells showed that five potential CK2 phosphorylation sites (S18, S24, S46, S52, and S117) in the N-terminal half are really phosphorylated in vivo, and the phosphorylation of four of them (S18, S24, S46, and S117) decreased in ckb1D cells (Supplemental Fig. S5).
PMID:19136623	MOD:00046	Mass spectrometric analysis of Swi6 prepared from wild-type and ckb1D cells showed that five potential CK2 phosphorylation sites (S18, S24, S46, S52, and S117) in the N-terminal half are really phosphorylated in vivo, and the phosphorylation of four of them (S18, S24, S46, and S117) decreased in ckb1D cells (Supplemental Fig. S5).
PMID:19136623	MOD:00046	Mass spectrometric analysis of Swi6 prepared from wild-type and ckb1D cells showed that five potential CK2 phosphorylation sites (S18, S24, S46, S52, and S117) in the N-terminal half are really phosphorylated in vivo, and the phosphorylation of four of them (S18, S24, S46, and S117) decreased in ckb1D cells (Supplemental Fig. S5).
PMID:19136623	MOD:00046	Mass spectrometric analysis of Swi6 prepared from wild-type and ckb1D cells showed that five potential CK2 phosphorylation sites (S18, S24, S46, S52, and S117) in the N-terminal half are really phosphorylated in vivo, and the phosphorylation of four of them (S18, S24, S46, and S117) decreased in ckb1D cells (Supplemental Fig. S5).
PMID:19136623	PBO:0113573	Conversely, mutations at the five CK2 sites located in the C-terminal region of Swi6 (Fig. 3A) (swi6-S192-274A) did not influence the mobility of Swi6 (Fig. 3B).
PMID:19136623	PBO:0113571	The lesser mobility change in ckb1D cells than that of Swi6-S18-117A would reflect the partial phosphorylation of Swi6 by residual activity of CK2 in ckb1D cells (Fig. 2A,C).
PMID:19136623	PBO:0113572	Mutations at the five CK2 sites located in the N-terminal half (S18-117A in Fig. 3A) resulted in an increase in mobility
PMID:19136623	PBO:0113571	whereas mutant Swi6 harboring S18A and S24A showed a slight mobility change
PMID:19136623	PBO:0092711	Similarly, CK2 efficiently phosphorylated bacteria-prepared Swi6 in a Ckb1-dependent manner, resulting in slower migrating bands in SDS- PAGE (Fig. 2C).
PMID:19136623	GO:0030466	Therefore, Clr3 and Ckb1 function similarly in Atf1/Pcr1-dependent heterochromatin formation at the mating locus.
PMID:19136623	GO:0090055	Therefore, Clr3 and Ckb1 function similarly in Atf1/Pcr1-dependent heterochromatin formation at the mating locus.
PMID:19136623	PBO:0111989	Similarly, H3K9me on Kint2::ura4 was diminished in dcr1Dckb1D but still retained in atf1Dckb1D cells (Fig. 1D). T
PMID:19136623	PBO:0097399	Similarly, H3K9me on Kint2::ura4 was diminished in dcr1Dckb1D but still retained in atf1Dckb1D cells (Fig. 1D). T
PMID:19136623	PBO:0111989	H3K9me on the ura4 inserted at the mating locus heterochromatin (Kint2 ::ura4) was hardly affected by deletion of either atf1 or dcr1, an essential component of the RNAi-directed pathway (Fig. 1D).
PMID:19136623	PBO:0111989	H3K9me on the ura4 inserted at the mating locus heterochromatin (Kint2 ::ura4) was hardly affected by deletion of either atf1 or dcr1, an essential component of the RNAi-directed pathway (Fig. 1D).
PMID:19136623	GO:0090053	this result suggests that Ckb1 is involved in the spreading of heterochromatin. (in ~GO, spreading is included in formation)
PMID:19136623	FYPO:0008200	In contrast, levels of H3K9me and Swi6 at imr::ura4 were significantly decreased in clr3D and ckb1D cells (Fig. 1C).
PMID:19136623	FYPO:0003235	Both H3K9me and Swi6 were enriched on centromeric repeats (dg223) in ckb1D cells similar to wild-type or clr3D cells (Fig. 1C).
PMID:19136623	FYPO:0003235	Both H3K9me and Swi6 were enriched on centromeric repeats (dg223) in ckb1D cells similar to wild-type or clr3D cells (Fig. 1C).
PMID:19136623	PBO:0098583	The extent of the silencing defects in ckb1D cells was comparable with that caused by disruption of other heterochromatic genes, including clr4, a histone H3K9-specific histone methyltransferase; clr3, a histone deacetylase and a subunit of SHREC; and swi6, a HP1 homolog (Fig. 1B).
PMID:19136623	PBO:0098583	The extent of the silencing defects in ckb1D cells was comparable with that caused by disruption of other heterochromatic genes, including clr4, a histone H3K9-specific histone methyltransferase; clr3, a histone deacetylase and a subunit of SHREC; and swi6, a HP1 homolog (Fig. 1B).
PMID:19136623	PBO:0098583	The extent of the silencing defects in ckb1D cells was comparable with that caused by disruption of other heterochromatic genes, including clr4, a histone H3K9-specific histone methyltransferase; clr3, a histone deacetylase and a subunit of SHREC; and swi6, a HP1 homolog (Fig. 1B).
PMID:19136623	PBO:0098583	disruption of ckb1 alleviated the silencing of marker genes inserted in centromeric heterochromatin (Fig. 1A,B).
PMID:19139265	PBO:0096679	(Fig. 9)
PMID:19139265	FYPO:0002061	(Fig. S5)
PMID:19139265	PBO:0102283	(Fig. 8)
PMID:19139265	FYPO:0002061	(Fig. S5)
PMID:19150433	PBO:0094913	(comment: covalent binding between topoisomerase and DNA)
PMID:19150433	PBO:0094912	(comment: covalent binding between topoisomerase and DNA)
PMID:19150433	PBO:0094915	(comment: covalent binding between topoisomerase and DNA)
PMID:19150433	PBO:0094912	(comment: covalent binding between topoisomerase and DNA)
PMID:19150433	PBO:0094913	(comment: covalent binding between topoisomerase and DNA)
PMID:19150433	PBO:0094913	(comment: covalent binding between topoisomerase and DNA)
PMID:19150433	PBO:0094916	(comment: covalent binding between topoisomerase and DNA)
PMID:19155267	GO:0003941	Table S1, Supplementary Data
PMID:19155267	GO:0030378	Table S1, Supplementary Data
PMID:19155267	GO:0008721	Table S1, Supplementary Data
PMID:19158664	PBO:0095481	"(comment: closest we can get to ""at stalled fork"" with available terms)"
PMID:19164572	FYPO:0008203	(Fig. 1G)
PMID:19164572	PBO:0112527	Table S1
PMID:19164572	PBO:0112526	Table S1
PMID:19164572	PBO:0112525	Table S1
PMID:19164572	PBO:0112524	Table S1
PMID:19164572	PBO:0112523	Table S1
PMID:19164572	PBO:0112522	Table S1
PMID:19164572	PBO:0112521	Table S1
PMID:19164572	PBO:0112520	(Fig. 1H)
PMID:19164572	FYPO:0000863	(Fig. 1F)
PMID:19164572	PBO:0112519	(Fig. 1E)
PMID:19164572	PBO:0112518	(Fig. 1D)
PMID:19164572	PBO:0112517	(Fig. 1C)
PMID:19164572	PBO:0112516	(Fig. 1B)
PMID:19164572	PBO:0112542	(Fig. S2)
PMID:19164572	FYPO:0000472	(Fig. 5)
PMID:19164572	FYPO:0000472	(Fig. 5)
PMID:19164572	FYPO:0000472	(Fig. 5)
PMID:19164572	FYPO:0000472	(Fig. 4E)
PMID:19164572	FYPO:0000472	(Fig. 4E)
PMID:19164572	FYPO:0002827	(Fig. 4D)
PMID:19164572	PBO:0112541	(Fig. 4B)
PMID:19164572	PBO:0112541	(Fig. 4B)
PMID:19164572	PBO:0110928	(Fig. 4B)
PMID:19164572	PBO:0112540	(Fig. 4B)
PMID:19164572	PBO:0112539	(Fig. 3)
PMID:19164572	FYPO:0003412	(Fig. 2A)
PMID:19164572	FYPO:0003412	(Fig. 2A)
PMID:19164572	PBO:0112538	(Fig. 2C)
PMID:19164572	FYPO:0000887	(Fig. 2B)
PMID:19164572	FYPO:0006299	(Fig. 2A)
PMID:19164572	PBO:0112537	Table S1
PMID:19164572	PBO:0112536	Table S1
PMID:19164572	PBO:0112535	Table S1
PMID:19164572	PBO:0112534	Table S1
PMID:19164572	PBO:0112533	Table S1
PMID:19164572	PBO:0112532	Table S1
PMID:19164572	PBO:0112531	Table S1
PMID:19164572	PBO:0112530	Table S1
PMID:19164572	PBO:0112529	Table S1
PMID:19164572	PBO:0112528	Table S1
PMID:19189958	FYPO:0002060	(Figure 5B) However, their growth was rescued in the presence of sorbitol
PMID:19189958	PBO:0102201	Our results indicate that Rgf1p and Rgf2p share an essential role as Rho1p activators, and they suggest that in the absence of Rgf1p, Rgf2p takes over the essential functions for Rho1p during vegetative growth.
PMID:19189958	PBO:0102203	(comment: CHECK 10% of cells)
PMID:19189958	PBO:0102201	Our results indicate that Rgf1p and Rgf2p share an essential role as Rho1p activators, and they suggest that in the absence of Rgf1p, Rgf2p takes over the essential functions for Rho1p during vegetative growth.
PMID:19189958	FYPO:0002060	(Figure 1) Rgf2p, a Rho1-GEF Required for Sporulation in S. pombe 1329 6A (top) shows that rgf2 expressed from plasmids, containing the rgf21 genomic promoter (pGR13) or the strongest nmt1 promoter (pGR70), fully rescued the lysis and the Csp hypersensitivity of rgf1D cells in medium containing thiamine.
PMID:19189958	FYPO:0002061	(Figure 5B) As expected for the rgf31 shut-off, the cells died in the presence of thiamine (promoter off).
PMID:19189958	FYPO:0002060	(Figure 5B) viable and phenotypically indistinguishable from the ehs2-1 mutant
PMID:19189958	FYPO:0002061	None of the 11 spores predicted to be rgf1This31 rgf2Tura1 was viable, strongly supporting the idea that simultaneous disruption of rgf11 and rgf21 is lethal. To eliminate the possibility that these mutations might be affecting only sporulation or germination, we also tested for synthetic lethality during vegetative growth
PMID:19189958	PBO:0102197	(Figure 4c) (comment: positive
PMID:19189958	PBO:0102202	(comment: CHECKB 47% of cells)
PMID:19189958	GO:0140748	"(Figure 3) ""This result indicates that Rgf2p is involved in b-glucan biosynthesis during sporulation."" figure4c These results clearly indicate that Rgf2p is involved in the regulation of b(1,3)-glucan biosynthesis."
PMID:19189958	FYPO:0007905	(Figure 3A)
PMID:19189958	PBO:0102196	(Figure 2A)
PMID:19189958	PBO:0102195	(Figure 2b)
PMID:19189958	FYPO:0004927	(Figure 2A)
PMID:19189958	FYPO:0000590	(Figure 2)
PMID:19189958	FYPO:0000121	(Figure 2)
PMID:19189958	FYPO:0001310	90% viability ? We also examined cell viability of stationary phase rgf2D and rgf21 cultures incubated for 4 days at 28°; both strains were found to be .90% viable during this period.
PMID:19189958	PBO:0102200	GS activity was threefold higher than that observed in the wild-type strain (Figure 4C)
PMID:19189958	PBO:0102199	GS activity was threefold higher than that observed in the wild-type strain (Figure 4C)
PMID:19189958	FYPO:0007436	cells were larger than wild-type cells and displayed multiple abnormal septa.
PMID:19189958	FYPO:0002177	As expected, over-expression of the rgf2-PTTRD mutant in a pREP3X vector produced viable cells and no multiseptated phenotype was seen, even at very long times of derepresion in the absence of thiamine (Figure 4A).
PMID:19189958	FYPO:0001357	We also examined cell viability of stationary phase rgf2D and rgf21 cultures incubated for 4 days at 28°; both strains were found to be .90% viable during this period.
PMID:19189958	FYPO:0002104	(Figure 1)
PMID:19189958	FYPO:0001357	(Figure 1)
PMID:19189958	FYPO:0000478	(Figure 2A)
PMID:19189958	PBO:0102198	the amount of active Rho1p increased considerably in the strain overexpressing Rgf2p as compared with the wild-type strain (Figure 4B
PMID:19189958	GO:0005632	(Figure 3B)
PMID:19189958	PBO:0102196	(Figure 2A)
PMID:19189958	PBO:0102196	(Figure 2A)
PMID:19189958	FYPO:0002060	(Figure 5B) However, their growth was rescued in the presence of sorbitol
PMID:19189958	FYPO:0002061	(Figure 5B) As expected for the rgf31 shut-off, the cells died in the presence of thiamine (promoter off).
PMID:19202278	FYPO:0002447	(comment: absent beta 1,3 gal)
PMID:19202289	FYPO:0000121	(Fig. 1A)
PMID:19202289	FYPO:0003563	(Fig. 1A)
PMID:19202289	FYPO:0003563	(Fig. 1B)
PMID:19202289	FYPO:0003798	(Fig. 1B)
PMID:19202289	FYPO:0002061	(Fig. 1B)
PMID:19202289	FYPO:0003905	(comment: data not shown)
PMID:19202289	FYPO:0000307	(Fig. 2B)
PMID:19202289	GO:0032120	(Fig. 2B)
PMID:19202289	GO:0005886	(Fig. 2D)
PMID:19202289	GO:0005628	(Fig. 2D)
PMID:19202289	FYPO:0002060	(Fig. 3C)
PMID:19202289	FYPO:0002060	(Fig. 3C)
PMID:19202289	FYPO:0000590	(Fig. 3A and B)
PMID:19202289	FYPO:0000590	(Fig. 3A and B)
PMID:19202289	GO:0032120	(Fig. 3B)
PMID:19202289	GO:0032120	(Fig. 3B)
PMID:19205745	PBO:0093561	(comment: temp semi-permissive for cdc6-23 alone)
PMID:19205745	PBO:0093581	(comment: temp semi-permissive for cdc6-23 alone
PMID:19205745	PBO:0093561	(comment: temp semi-permissive for cdc20-M10 alone
PMID:19205745	PBO:0093561	(comment: temp semi-permissive for pol1-1 alone)
PMID:19205745	PBO:0093581	(comment: temp semi-permissive for cdc6-23 alone
PMID:19205745	PBO:0093561	(comment: temp semi-permissive for cdc6-23 alone)
PMID:19214192	PBO:0105817	DNA polymerases present in late S; epsilon (cdc20) earlier than alpha (pol1) or delta (cdc6)
PMID:19214192	GO:0140445	present at roughly constant level throughout cell cycle
PMID:19214192	PBO:0105817	present in late S
PMID:19214192	PBO:0105817	DNA polymerases present in late S; epsilon (cdc20) earlier than alpha (pol1) or delta (cdc6)
PMID:19214192	GO:0140445	present throughout cell cycle but at higher level in S phase
PMID:19214192	GO:0140445	present throughout cell cycle but at lower level in S phase
PMID:19214192	GO:0140445	present throughout cell cycle but at higher level in late S phase
PMID:19214192	PBO:0105817	present in late S
PMID:19214192	GO:0140445	present throughout cell cycle but at higher level in S phase
PMID:19214192	PBO:0105817	present in late S
PMID:19214192	PBO:0105817	DNA polymerases present in late S; epsilon (cdc20) earlier than alpha (pol1) or delta (cdc6)
PMID:19214192	PBO:0105817	present in late S, as late as pols alpha & delta
PMID:19217404	FYPO:0003740	(comment: CHECK abolished,) fig1d
PMID:19217404	FYPO:0003740	(comment: CHECK abolished,) fig1d
PMID:19217404	FYPO:0003740	(comment: CHECK abolished,) fig1d
PMID:19217404	FYPO:0003740	(comment: abolished CHECK,) fig1d
PMID:19217404	PBO:0099221	(Fig. S10)
PMID:19217404	FYPO:0003740	(comment: CHECK abolished,) fig1d
PMID:19217404	FYPO:0003740	(comment: CHECK abolished,) fig1d
PMID:19250904	PBO:0093629	(comment: same as either single mutant)
PMID:19250904	PBO:0093629	(comment: same as either single mutant)
PMID:19250904	PBO:0093619	(comment: same as either single mutant)
PMID:19250904	PBO:0093629	(comment: same as either single mutant)
PMID:19250904	PBO:0093619	(comment: same as either single mutant)
PMID:19250904	PBO:0093619	(comment: same as either single mutant)
PMID:19250904	PBO:0093629	(comment: same as either single mutant)
PMID:19250904	GO:0140005	(comment: assayed using purified HeLa histone octamers)
PMID:19250904	PBO:0093620	(comment: same as either single mutant)
PMID:19250904	PBO:0093630	(comment: same as either single mutant)
PMID:19250904	PBO:0093619	(comemnt: same as either single mutant)
PMID:19279143	PBO:0105388	(Fig. 4F)
PMID:19279143	PBO:0105387	(Fig. 4F)
PMID:19279143	PBO:0105385	"""Thus, Nrd1 directly binds with Cdc4 mRNA in vivo and in vitro"""
PMID:19279143	GO:1902413	Notably, Pmk1, the mitogen-activated protein kinase (MAPK), which regulates cell integrity (Toda et al., 1996; Sugiura et al., 1999; Sugiura et al., 2003), directly phosphorylates Nrd1, thereby negatively regulating the activity of Nrd1 to bind to and stabilize Cdc4 mRNA. We propose that the MAPK-dependent phosphorylation of the RNA-binding protein Nrd1 may serve as a novel mechanism for the regulation of myosin mRNA and cytokinesis in fission yeast.
PMID:19328067	PBO:0095887	(comment: All at eng2 CDS)
PMID:19328067	PBO:0103631	(comment: All at eng2 CDS)
PMID:19328067	PBO:0095887	(comment: All at eng2 CDS)
PMID:19328067	PBO:0103630	(comment: All at eng2 CDS)
PMID:19328067	PBO:0103629	(comment: All at eng2 CDS)
PMID:19328067	PBO:0114260	(comment: CHECK positive regulation)
PMID:19328067	PBO:0103633	"(comment: Mcs6 ""primes"" Rpb1 for phosphorylation by cdk9)"
PMID:19330768	FYPO:0004588	(comment: G2 temperature shift)
PMID:19330768	FYPO:0000802	(comment: in arrested cells, indicating independent of cell cycle progression)
PMID:19330768	FYPO:0000141	(comment: G1 temperature shift)
PMID:1934126	FYPO:0000681	(comment: same as cdc25-22 single mutant)
PMID:1934126	FYPO:0000681	(comment: same as cdc25-22 single mutant)
PMID:1934126	FYPO:0000681	(comment: same as cdc25-22 single mutant)
PMID:1934126	FYPO:0000681	(comment: same as cdc25-22 single mutant)
PMID:19357077	PBO:0111600	Activation of Cds1 requires the recruitment by Mrc1 and subsequent phosphorylation of threonine 11 by Rad3. Phosphorylation of threonine 11 promotes homodimerization of Cds1, which facilitates the autophosphorylation of threonine 328 in the kinase domains of the dimer partners. Phosphorylation of threonine 328 directly activates Cds1. The kinase activity of Cds1 is low during a normal cell cycle. However, it increases dramatically during a perturbed S phase.
PMID:19362535	FYPO:0007334	loss of maintenance of heterochromatin was seen in cells expressing both Tas3WG and E23Vchp1, unlike cells expressing either single mutant
PMID:19362535	FYPO:0007334	loss of maintenance of heterochromatin was seen in cells expressing both Tas3WG and E23Vchp1, unlike cells expressing either single mutant
PMID:19362535	FYPO:0007334	loss of maintenance of heterochromatin was seen in cells expressing both Tas3WG and E23Vchp1, unlike cells expressing either single mutant
PMID:19362535	FYPO:0004742	loss of maintenance of heterochromatin was seen in cells expressing both Tas3WG and E23Vchp1, unlike cells expressing either single mutant
PMID:19362535	PBO:0111400	(comment: CHECK ******abolished /de novo**********) Reintegration of clr4+ into cells bearing the chp1 chromodomain mutants showed a striking separation of phenotypes, with some mutants unable to re-establish centromeric heterochromatin (e.g., E23Vchp1clr4D to clr4+, V24Mchp1clr4D to clr4+, and N59Achp1clr4D to clr4+) and others showing efficient re-establishment (e.g., F61Achp1clr4D to clr4+), as assessed by silencing of the cen::ura4+ transgene (Figure 5A).
PMID:19362535	PBO:0111400	(comment: CHECK ******abolished /de novo**********) Reintegration of clr4+ into cells bearing the chp1 chromodomain mutants showed a striking separation of phenotypes, with some mutants unable to re-establish centromeric heterochromatin (e.g., E23Vchp1clr4D to clr4+, V24Mchp1clr4D to clr4+, and N59Achp1clr4D to clr4+) and others showing efficient re-establishment (e.g., F61Achp1clr4D to clr4+), as assessed by silencing of the cen::ura4+ transgene (Figure 5A).
PMID:19362535	PBO:0111400	(comment: CHECK ******abolished /de novo**********) Reintegration of clr4+ into cells bearing the chp1 chromodomain mutants showed a striking separation of phenotypes, with some mutants unable to re-establish centromeric heterochromatin (e.g., E23Vchp1clr4D to clr4+, V24Mchp1clr4D to clr4+, and N59Achp1clr4D to clr4+) and others showing efficient re-establishment (e.g., F61Achp1clr4D to clr4+), as assessed by silencing of the cen::ura4+ transgene (Figure 5A).
PMID:19362535	FYPO:0003099	(comment: CHAECK ******abolished /de novo**********) Reintegration of clr4+ into cells bearing the chp1 chromodomain mutants showed a striking separation of phenotypes, with some mutants unable to re-establish centromeric heterochromatin (e.g., E23Vchp1clr4D to clr4+, V24Mchp1clr4D to clr4+, and N59Achp1clr4D to clr4+) and others showing efficient re-establishment (e.g., F61Achp1clr4D to clr4+), as assessed by silencing of the cen::ura4+ transgene (Figure 5A).
PMID:19362535	FYPO:0003099	(comment: CHAECK ******abolished /de novo**********) Reintegration of clr4+ into cells bearing the chp1 chromodomain mutants showed a striking separation of phenotypes, with some mutants unable to re-establish centromeric heterochromatin (e.g., E23Vchp1clr4D to clr4+, V24Mchp1clr4D to clr4+, and N59Achp1clr4D to clr4+) and others showing efficient re-establishment (e.g., F61Achp1clr4D to clr4+), as assessed by silencing of the cen::ura4+ transgene (Figure 5A).
PMID:19362535	PBO:0094684	High levels of centromeric transcripts also accumulated in these establishment-defective clr4+ reintroduction strains E23Vchp1clr4D to clr4+, V24Mchp1clr4D to clr4+, and N59Achp1clr4D to clr4+, but not in the establishment-competent F61Achp1clr4D to clr4+ cells (Figure 5B; Figure S9A)
PMID:19362535	PBO:0094684	High levels of centromeric transcripts also accumulated in these establishment-defective clr4+ reintroduction strains E23Vchp1clr4D to clr4+, V24Mchp1clr4D to clr4+, and N59Achp1clr4D to clr4+, but not in the establishment-competent F61Achp1clr4D to clr4+ cells (Figure 5B; Figure S9A)
PMID:19362535	PBO:0094684	High levels of centromeric transcripts also accumulated in these establishment-defective clr4+ reintroduction strains E23Vchp1clr4D to clr4+, V24Mchp1clr4D to clr4+, and N59Achp1clr4D to clr4+, but not in the establishment-competent F61Achp1clr4D to clr4+ cells (Figure 5B; Figure S9A)
PMID:19362535	PBO:0111401	The efficiency of chromosome segregation was also monitored in clr4+ reintroduction chp1 mutant cells (Table S4) and closely correlated with Chp1’s binding efficiency. Mutants with>5-fold reduction in H3K9me-binding efficiency that cannot establish centromeric heterochromatin exhibited elevated rates of chromosome missegregation.
PMID:19362535	PBO:0111402	The efficiency of chromosome segregation was also monitored in clr4+ reintroduction chp1 mutant cells (Table S4) and closely correlated with Chp1’s binding efficiency. Mutants with >5-fold reduction in H3K9me-binding efficiency that cannot establish centromeric heterochromatin exhibited elevated rates of chromosome missegregation.
PMID:19362535	PBO:0111403	The efficiency of chromosome segregation was also monitored in clr4+ reintroduction chp1 mutant cells (Table S4) and closely correlated with Chp1’s binding efficiency. Mutants with >5-fold reduction in H3K9me-binding efficiency that cannot establish centromeric heterochromatin exhibited elevated rates of chromosome missegregation.
PMID:19362535	PBO:0111404	The efficiency of chromosome segregation was also monitored in clr4+ reintroduction chp1 mutant cells (Table S4) and closely correlated with Chp1’s binding efficiency. Mutants with >5-fold reduction in H3K9me-binding efficiency that cannot establish centromeric heterochromatin exhibited elevated rates of chromosome missegregation.
PMID:19362535	PBO:0101959	The efficiency of chromosome segregation was also monitored in clr4+ reintroduction chp1 mutant cells (Table S4) and closely correlated with Chp1’s binding efficiency. Mutants with >5-fold reduction in H3K9me-binding efficiency that cannot establish centromeric heterochromatin exhibited elevated rates of chromosome missegregation.
PMID:19362535	PBO:0111405	The efficiency of chromosome segregation was also monitored in clr4+ reintroduction chp1 mutant cells (Table S4) and closely correlated with Chp1’s binding efficiency. Mutants with >5-fold reduction in H3K9me-binding efficiency that cannot establish centromeric heterochromatin exhibited elevated rates of chromosome missegregation.
PMID:19362535	FYPO:0002837	Surprisingly, when we monitored the presence of centromeric siRNAs in these clr4+ reintroduction strains, we found that even mutants that were defective for establishment of centromeric heterochromatin efficiently synthesized siRNAs derived from both the dg and dh centromeric repeats (Figure 5C)
PMID:19362535	FYPO:0002837	Surprisingly, when we monitored the presence of centromeric siRNAs in these clr4+ reintroduction strains, we found that even mutants that were defective for establishment of centromeric heterochromatin efficiently synthesized siRNAs derived from both the dg and dh centromeric repeats (Figure 5C)
PMID:19362535	PBO:0111398	Results for Chp1 localization were similar to those seen in maintenance strains with mutants such as E23Vchp1clr4D to clr4+ and V24Mchp1clr4D to clr4+ showing little association with centromeres, whereas F61Achp1clr4D to clr4+ was enriched at levels close to wild-type Chp1clr4D to clr4+
PMID:19362535	PBO:0111398	Results for Chp1 localization were similar to those seen in maintenance strains with mutants such as E23Vchp1clr4D to clr4+ and V24Mchp1clr4D to clr4+ showing little association with centromeres, whereas F61Achp1clr4D to clr4+ was enriched at levels close to wild-type Chp1clr4D to clr4+
PMID:19362535	PBO:0111406	Results for Chp1 localization were similar to those seen in maintenance strains with mutants such as E23Vchp1clr4D to clr4+ and V24Mchp1clr4D to clr4+ showing little association with centromeres, whereas F61Achp1clr4D to clr4+ was enriched at levels close to wild-type Chp1clr4D to clr4+
PMID:19362535	PBO:0111407	centromeric H3K9me2 levels were low in many of the chp1 chromodomain clr4+ reintroduction strains and closely mirrored the levels of Chp1 recruitment in the various centromeric H3K9me2 levels were low in many of the chp1 chromodomain clr4+ reintroduction strains and closely mirrored the levels of Chp1 recruitment in the various mutant backgrounds (Figure 6B).
PMID:19362535	PBO:0111407	centromeric H3K9me2 levels were low in many of the chp1 chromodomain clr4+ reintroduction strains and closely mirrored the levels of Chp1 recruitment in the various centromeric H3K9me2 levels were low in many of the chp1 chromodomain clr4+ reintroduction strains and closely mirrored the levels of Chp1 recruitment in the various mutant backgrounds (Figure 6B).
PMID:19362535	PBO:0111407	centromeric H3K9me2 levels were low in many of the chp1 chromodomain clr4+ reintroduction strains and closely mirrored the levels of Chp1 recruitment in the various centromeric H3K9me2 levels were low in many of the chp1 chromodomain clr4+ reintroduction strains and closely mirrored the levels of Chp1 recruitment in the various mutant backgrounds (Figure 6B).
PMID:19362535	PBO:0111408	centromeric H3K9me2 levels were low in many of the chp1 chromodomain clr4+ reintroduction strains and closely mirrored the levels of Chp1 recruitment in the various centromeric H3K9me2 levels were low in many of the chp1 chromodomain clr4+ reintroduction strains and closely mirrored the levels of Chp1 recruitment in the various mutant backgrounds (Figure 6B).
PMID:19362535	PBO:0111408	High copy expression of clr4+ in the E23Vchp1clr4D and in the V24Mchp1clr4D cells allowed efficient establishment of centromeric heterochromatin (Figure 6C). Thus, the establishment defect of chp1 mutants with reduced H3K9me-binding affinity can be compensated by an increased dosage of clr4+ .
PMID:19362535	PBO:0111408	High copy expression of clr4+ in the E23Vchp1clr4D and in the V24Mchp1clr4D cells allowed efficient establishment of centromeric heterochromatin (Figure 6C). Thus, the establishment defect of chp1 mutants with reduced H3K9me-binding affinity can be compensated by an increased dosage of clr4+ .
PMID:19362535	PBO:0108963	the Chp1 chromodomain bound both H3K9me2 and H3K9me3 peptides with significantly higher affinity than either Clr4 or Swi6 (Table 1), and all proteins bound H3K9me3 more tightly than H3K9me2. || we solved the crystal structure of the Chp1 chromodomain (CD) in complex with an H3K9me3 peptide (Figure 1C; Table 2).S10 of histone H3 is phosphorylated during mitosis and displaces HP1 proteins (including Swi6) from chromatin (Fischle et al., 2005; Hirota et al., 2005; Yamada et al., 2005). We investigated whether binding of Swi6 and Chp1 to H3K9me peptides was affected by S10 phosphorylation and found a strong reduction in both Chp1- and Swi6-binding affinity (Table S2; Figure S2B)
PMID:19362535	PBO:0108963	the Chp1 chromodomain bound both H3K9me2 and H3K9me3 peptides with significantly higher affinity than either Clr4 or Swi6 (Table 1), and all proteins bound H3K9me3 more tightly than H3K9me2. || we solved the crystal structure of the Chp1 chromodomain (CD) in complex with an H3K9me3 peptide (Figure 1C; Table 2).S10 of histone H3 is phosphorylated during mitosis and displaces HP1 proteins (including Swi6) from chromatin (Fischle et al., 2005; Hirota et al., 2005; Yamada et al., 2005). We investigated whether binding of Swi6 and Chp1 to H3K9me peptides was affected by S10 phosphorylation and found a strong reduction in both Chp1- and Swi6-binding affinity (Table S2; Figure S2B)
PMID:19362535	PBO:0108963	the Chp1 chromodomain bound both H3K9me2 and H3K9me3 peptides with significantly higher affinity than either Clr4 or Swi6 (Table 1), and all proteins bound H3K9me3 more tightly than H3K9me2. || we solved the crystal structure of the Chp1 chromodomain (CD) in complex with an H3K9me3 peptide (Figure 1C; Table 2). S10 of histone H3 is phosphorylated during mitosis and displaces HP1 proteins (including Swi6) from chromatin (Fischle et al., 2005; Hirota et al., 2005; Yamada et al., 2005). We investigated whether binding of Swi6 and Chp1 to H3K9me peptides was affected by S10 phosphorylation and found a strong reduction in both Chp1- and Swi6-binding affinity (Table S2; Figure S2B)
PMID:19362535	PBO:0119827	the Chp1 chromodomain bound both H3K9me2 and H3K9me3 peptides with significantly higher affinity than either Clr4 or Swi6 (Table 1), and all proteins bound H3K9me3 more tightly than H3K9me2. ||we solved the crystal structure of the Chp1 chromodomain (CD) in complex with an H3K9me3 peptide (Figure 1C; Table 2).
PMID:19362535	PBO:0119828	the Chp1 chromodomain bound both H3K9me2 and H3K9me3 peptides with significantly higher affinity than either Clr4 or Swi6 (Table 1), and all proteins bound H3K9me3 more tightly than H3K9me2. || we solved the crystal structure of the Chp1 chromodomain (CD) in complex with an H3K9me3 peptide (Figure 1C; Table 2).
PMID:19362535	PBO:0119829	the Chp1 chromodomain bound both H3K9me2 and H3K9me3 peptides with significantly higher affinity than either Clr4 or Swi6 (Table 1), and all proteins bound H3K9me3 more tightly than H3K9me2. || we solved the crystal structure of the Chp1 chromodomain (CD) in complex with an H3K9me3 peptide (Figure 1C; Table 2).
PMID:19362535	PBO:0111665	the Chp1 chromodomain bound both H3K9me2 and H3K9me3 peptides with significantly higher affinity than either Clr4 or Swi6 (Table 1), and all proteins bound H3K9me3 more tightly than H3K9me2. || we solved the crystal structure of the Chp1 chromodomain (CD) in complex with an H3K9me3 peptide (Figure 1C; Table 2). S10 of histone H3 is phosphorylated during mitosis and displaces HP1 proteins (including Swi6) from chromatin (Fischle et al., 2005; Hirota et al., 2005; Yamada et al., 2005). We investigated whether binding of Swi6 and Chp1 to H3K9me peptides was affected by S10 phosphorylation and found a strong reduction in both Chp1- and Swi6-binding affinity (Table S2; Figure S2B)
PMID:19362535	PBO:0111665	the Chp1 chromodomain bound both H3K9me2 and H3K9me3 peptides with significantly higher affinity than either Clr4 or Swi6 (Table 1), and all proteins bound H3K9me3 more tightly than H3K9me2. || we solved the crystal structure of the Chp1 chromodomain (CD) in complex with an H3K9me3 peptide (Figure 1C; Table 2).S10 of histone H3 is phosphorylated during mitosis and displaces HP1 proteins (including Swi6) from chromatin (Fischle et al., 2005; Hirota et al., 2005; Yamada et al., 2005). We investigated whether binding of Swi6 and Chp1 to H3K9me peptides was affected by S10 phosphorylation and found a strong reduction in both Chp1- and Swi6-binding affinity (Table S2; Figure S2B)
PMID:19362535	PBO:0111665	the Chp1 chromodomain bound both H3K9me2 and H3K9me3 peptides with significantly higher affinity than either Clr4 or Swi6 (Table 1), and all proteins bound H3K9me3 more tightly than H3K9me2. || we solved the crystal structure of the Chp1 chromodomain (CD) in complex with an H3K9me3 peptide (Figure 1C; Table 2).S10 of histone H3 is phosphorylated during mitosis and displaces HP1 proteins (including Swi6) from chromatin (Fischle et al., 2005; Hirota et al., 2005; Yamada et al., 2005). We investigated whether binding of Swi6 and Chp1 to H3K9me peptides was affected by S10 phosphorylation and found a strong reduction in both Chp1- and Swi6-binding affinity (Table S2; Figure S2B)
PMID:19362535	FYPO:0003431	and the V24R mutant abolished the specificity of the chromodomain interaction for K9 methylated peptides (Kd > 500 mM).
PMID:19362535	PBO:0112171	A third class showed a more profound reduction in binding affinity: the E23V,V24M mutant reduced binding affinity 40 fold
PMID:19362535	PBO:0112172	A second class of mutants showed a 5- to 17-fold reduction in binding affinity for H3K9me2 compared with the wild-type Chp1 chromodomain (V21A, E23V, N59A, and V24M). A
PMID:19362535	PBO:0112172	A second class of mutants showed a 5- to 17-fold reduction in binding affinity for H3K9me2 compared with the wild-type Chp1 chromodomain (V21A, E23V, N59A, and V24M). A
PMID:19362535	PBO:0112172	A second class of mutants showed a 5- to 17-fold reduction in binding affinity for H3K9me2 compared with the wild-type Chp1 chromodomain (V21A, E23V, N59A, and V24M). A
PMID:19362535	PBO:0112172	A second class of mutants showed a 5- to 17-fold reduction in binding affinity for H3K9me2 compared with the wild-type Chp1 chromodomain (V21A, E23V, N59A, and V24M). A
PMID:19362535	PBO:0112173	The observed affinities ranged from close to wild-type to complete loss of specific binding. The F61A mutant showed little reduction in binding affinity compared with wild-type Chp1. A
PMID:19362535	PBO:0112174	The Swi6 V82E mutant bound H3K9me2 with 5-fold higher affinity than wild-type Swi6 (Table 1; Figure S2A)
PMID:19362535	PBO:0112175	Introduction of an E80V mutation, corresponding to V21 of Chp1, into Swi6V82E further increased Swi6’s affinity by 2-fold (Table 1; Figure S2A).
PMID:19362535	FYPO:0004742	Interestingly, cells expressing most of the mutant alleles of chp1 showed no defect in heterochromatin assembly as measured in this assay (Figure 3A), with the exception of the double mutant E23V V24M and the V24R chp1 mutant, which did show silencing defects.
PMID:19362535	FYPO:0004742	Interestingly, cells expressing most of the mutant alleles of chp1 showed no defect in heterochromatin assembly as measured in this assay (Figure 3A), with the exception of the double mutant E23V V24M and the V24R chp1 mutant, which did show silencing defects.
PMID:19362535	FYPO:0003412	Interestingly, cells expressing most of the mutant alleles of chp1 showed no defect in heterochromatin assembly as measured in this assay (Figure 3A), with the exception of the double mutant E23V V24M and the V24R chp1 mutant, which did show silencing defects.
PMID:19362535	FYPO:0003412	Interestingly, cells expressing most of the mutant alleles of chp1 showed no defect in heterochromatin assembly as measured in this assay (Figure 3A), with the exception of the double mutant E23V V24M and the V24R chp1 mutant, which did show silencing defects.
PMID:19362535	FYPO:0004982	Interestingly, cells expressing most of the mutant alleles of chp1 showed no defect in heterochromatin assembly as measured in this assay (Figure 3A), with the exception of the double mutant E23V V24M and the V24R chp1 mutant, which did show silencing defects.
PMID:19362535	PBO:0111396	Unlike chp1 null cells, which showed 23% of mitotic cells undergoing chromosome missegregation, the chromodomain point-mutated strains, with the exception of V24Rchp1, showed few cells undergoing aberrant mitoses (Table S3).
PMID:19362535	FYPO:0002835	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0002835	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0002835	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0002837	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0002837	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0002837	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0002837	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0002837	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0002837	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0004201	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	PBO:0111397	Surprisingly, in contrast to robust association of wild-type Chp1 at the centromeric outer repeat sites, we found only very low levels of many of the mutant Chp1 proteins at centromeres under our standard ChIP conditions (Figure 4A and Figure S5A)
PMID:19362535	PBO:0111013	Surprisingly, in contrast to robust association of wild-type Chp1 at the centromeric outer repeat sites, we found only very low levels of many of the mutant Chp1 proteins at centromeres under our standard ChIP conditions (Figure 4A and Figure S5A)
PMID:19362535	FYPO:0002835	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0002835	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	PBO:0111398	Surprisingly, in contrast to robust association of wild-type Chp1 at the centromeric outer repeat sites, we found only very low levels of many of the mutant Chp1 proteins at centromeres under our standard ChIP conditions (Figure 4A and Figure S5A)
PMID:19362535	PBO:0111398	Surprisingly, in contrast to robust association of wild-type Chp1 at the centromeric outer repeat sites, we found only very low levels of many of the mutant Chp1 proteins at centromeres under our standard ChIP conditions (Figure 4A and Figure S5A)
PMID:19362535	PBO:0111398	Surprisingly, in contrast to robust association of wild-type Chp1 at the centromeric outer repeat sites, we found only very low levels of many of the mutant Chp1 proteins at centromeres under our standard ChIP conditions (Figure 4A and Figure S5A)
PMID:19362535	PBO:0111398	Surprisingly, in contrast to robust association of wild-type Chp1 at the centromeric outer repeat sites, we found only very low levels of many of the mutant Chp1 proteins at centromeres under our standard ChIP conditions (Figure 4A and Figure S5A)
PMID:19362535	PBO:0111398	Surprisingly, in contrast to robust association of wild-type Chp1 at the centromeric outer repeat sites, we found only very low levels of many of the mutant Chp1 proteins at centromeres under our standard ChIP conditions (Figure 4A and Figure S5A)
PMID:19362535	PBO:0111399	Surprisingly, in contrast to robust association of wild-type Chp1 at the centromeric outer repeat sites, we found only very low levels of many of the mutant Chp1 proteins at centromeres under our standard ChIP conditions (Figure 4A and Figure S5A)
PMID:19362535	PBO:0111399	Surprisingly, in contrast to robust association of wild-type Chp1 at the centromeric outer repeat sites, we found only very low levels of many of the mutant Chp1 proteins at centromeres under our standard ChIP conditions (Figure 4A and Figure S5A)
PMID:19362535	FYPO:0008070	unlike chp1 null cells, there was no significant decrease in centromeric H3K9me2 or Swi6 association in any of the chp1 mutants tested (Figures 4B and 4C; Figure S5B).
PMID:19362535	FYPO:0008070	unlike chp1 null cells, there was no significant decrease in centromeric H3K9me2 or Swi6 association in any of the chp1 mutants tested (Figures 4B and 4C; Figure S5B).
PMID:19362535	FYPO:0008070	unlike chp1 null cells, there was no significant decrease in centromeric H3K9me2 or Swi6 association in any of the chp1 mutants tested (Figures 4B and 4C; Figure S5B).
PMID:19362535	FYPO:0008070	unlike chp1 null cells, there was no significant decrease in centromeric H3K9me2 or Swi6 association in any of the chp1 mutants tested (Figures 4B and 4C; Figure S5B).
PMID:19362535	FYPO:0008070	unlike chp1 null cells, there was no significant decrease in centromeric H3K9me2 or Swi6 association in any of the chp1 mutants tested (Figures 4B and 4C; Figure S5B).
PMID:19362535	FYPO:0008070	unlike chp1 null cells, there was no significant decrease in centromeric H3K9me2 or Swi6 association in any of the chp1 mutants tested (Figures 4B and 4C; Figure S5B).
PMID:19362535	FYPO:0008070	unlike chp1 null cells, there was no significant decrease in centromeric H3K9me2 or Swi6 association in any of the chp1 mutants tested (Figures 4B and 4C; Figure S5B).
PMID:19362535	FYPO:0007334	We found, however, that introduction of F276Aago1 into either the E23Vchp1 or V24Mchp1 mutants resulted in loss of silencing of cen::ura4+ .
PMID:19362535	FYPO:0007334	We found, however, that introduction of F276Aago1 into either the E23Vchp1 or V24Mchp1 mutants resulted in loss of silencing of cen::ura4+ .
PMID:19362535	FYPO:0007334	We found, however, that introduction of F276Aago1 into either the E23Vchp1 or V24Mchp1 mutants resulted in loss of silencing of cen::ura4+ .
PMID:19362535	FYPO:0007334	We found, however, that introduction of F276Aago1 into either the E23Vchp1 or V24Mchp1 mutants resulted in loss of silencing of cen::ura4+ .
PMID:19362535	FYPO:0004742	In contrast, the F61Achp1; F276Aago1 mutant strain showed no defect in the silencing of the reporter (Figure 4D).
PMID:19363481	FYPO:0002150	(Figure 5)
PMID:19363481	FYPO:0001234	(Figure 5)
PMID:19363481	FYPO:0001234	(Figure 5)
PMID:19363481	FYPO:0001234	(Figure 5)
PMID:19363481	FYPO:0001234	(Figure 5)
PMID:19363481	GO:0005515	(comment: CHECK SLD1)
PMID:19363481	PBO:0099528	Strikingly, a GST-Rad60 SLD2E380R construct did not detectably interact with Ubc9-TAP (Fig. 3a)
PMID:19363481	PBO:0099529	slow growth phenotype and heterogeneity in cell length; reflecting elevated levels of spontaneous DNA damage and “constitutive” activation of the DNA damage checkpoint in these cells (Fig. 4a and data not shown).
PMID:19363481	FYPO:0001355	slow growth phenotype and heterogeneity in cell length; reflecting elevated levels of spontaneous DNA damage and “constitutive” activation of the DNA damage checkpoint in these cells (Fig. 4a and data not shown).
PMID:19363481	FYPO:0001234	(Figure 5)
PMID:19363481	FYPO:0000088	slow growth phenotype and heterogeneity in cell length; reflecting elevated levels of spontaneous DNA damage and “constitutive” activation of the DNA damage checkpoint in these cells (Fig. 4a and data not shown).
PMID:19363481	FYPO:0002150	(Figure 5)
PMID:19363481	FYPO:0002150	(Figure 5)
PMID:19363481	FYPO:0002150	(Figure 5)
PMID:19363481	FYPO:0001234	(Figure 5)
PMID:19363481	FYPO:0001234	(Figure 5)
PMID:19363481	FYPO:0001234	(Figure 5)
PMID:19363481	FYPO:0001234	(Figure 5)
PMID:19363481	FYPO:0001234	(Figure 5)
PMID:19363481	FYPO:0001234	(Figure 5)
PMID:19363481	FYPO:0001234	(Figure 5)
PMID:19363481	FYPO:0001234	(Figure 5)
PMID:19363481	FYPO:0001234	(Figure 5)
PMID:19366728	FYPO:0006518	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	(comment: CHECK fragmented)
PMID:19373772	FYPO:0000251	(comment: CONDITION non fermentable carbon source)
PMID:19373772	PBO:0019716	(comment: CHECK during mitotic M phase?)
PMID:19373772	PBO:0019715	"(comment: happens during mitotic M phase? term will be renames ""mitochondrial membrane fission"")"
PMID:19373772	PBO:0019714	"(comment: happens during mitotic M phase? term will be renames ""mitochondrial membrane fission"")"
PMID:19394293	FYPO:0004205	To determine the effect of tas3-TAM mutations on cen siRNAs levels, we performed northern blot analysis on RNAs isolated from wild-type, tas3D, and tas3-TAM mutant cells. We found a dramatic reduction in the levels of both total (Figure 4C) and Ago1-purified (Figure 4D) cen siRNAs in all tas3-TAM mutants compared to wild-type.
PMID:19394293	FYPO:0005929	At the dg and dh repeats, we found a consistent 2- to 3-fold reduction in mutant Tas3 occupancy compared to wild-type (Figure 5B, compare lanes 3-6 with lane 2; and Figure 5C). Also, consistent with the otr1R::ura4+ silencing data (Figure 3B), mutant Tas3-TAM proteins associated with the ura4+ insert at otr1R less efficiently than wild-type Tas3 (Figure 5D, compare lanes 3-6 with lane 2; and Figure 5E). In
PMID:19394293	FYPO:0008072	Surprisingly, we found no defect in H3K9me in tas3DTAM compared to wild-type cells at native centromeric repeats (dg1, imr1, imr2-1, or imr2-2) or the ura4+ inserts (for imr1R::ura4+
PMID:19394293	FYPO:0003411	(Figure 3)
PMID:19394293	FYPO:0003411	(Figure 3) tas3-TAM Mutations Cause a Dramatic Loss of ura4+ Silencing at imr1 but Only a Modest Loss at otr1
PMID:19394293	FYPO:0003411	(Figure 3) tas3-TAM Mutations Cause a Dramatic Loss of ura4+ Silencing at imr1 but Only a Modest Loss at otr1
PMID:19394293	FYPO:0003411	(Figure 3) tas3-TAM Mutations Cause a Dramatic Loss of ura4+ Silencing at imr1 but Only a Modest Loss at otr1
PMID:19394293	FYPO:0003411	(Figure 3) tas3-TAM Mutations Cause a Dramatic Loss of ura4+ Silencing at imr1 but Only a Modest Loss at otr1
PMID:19394293	PBO:0101404	(Figure 3) To rule out that the observed silencing defects were due to instability of the mutant Tas3 proteins, we examined the levels of wild-type and mutant Tas3 protein by western blotting and found that the mutant proteins were expressed to similar levels as the wild-type protein (Figure 3C).
PMID:19394293	PBO:0101404	(Figure 3C)
PMID:19394293	PBO:0101404	(Figure 3C)
PMID:19394293	PBO:0101404	(Figure 3C)
PMID:19394293	FYPO:0008073	We found that mutant proteins coimmunoprecipitated with Chp1 and FLAG-Ago1 with similar efficiency as the wild-type protein (Figures 4A and 4B, compare lane 1 with lanes 2-5). This result demonstrates that RITS complex formation is not affected in tas3-TAM mutants and that theCterminus of Tas3 is not involved in Chp1 or Ago1 binding (also shown in Partridge et al. [2007]).
PMID:19394293	FYPO:0004205	To determine the effect of tas3-TAM mutations on cen siRNAs levels, we performed northern blot analysis on RNAs isolated from wild-type, tas3D, and tas3-TAM mutant cells. We found a dramatic reduction in the levels of both total (Figure 4C) and Ago1-purified (Figure 4D) cen siRNAs in all tas3-TAM mutants compared to wild-type.
PMID:19394293	FYPO:0004205	To determine the effect of tas3-TAM mutations on cen siRNAs levels, we performed northern blot analysis on RNAs isolated from wild-type, tas3D, and tas3-TAM mutant cells. We found a dramatic reduction in the levels of both total (Figure 4C) and Ago1-purified (Figure 4D) cen siRNAs in all tas3-TAM mutants compared to wild-type.
PMID:19394293	FYPO:0004205	To determine the effect of tas3-TAM mutations on cen siRNAs levels, we performed northern blot analysis on RNAs isolated from wild-type, tas3D, and tas3-TAM mutant cells. We found a dramatic reduction in the levels of both total (Figure 4C) and Ago1-purified (Figure 4D) cen siRNAs in all tas3-TAM mutants compared to wild-type.
PMID:19416828	FYPO:0003352	"RTS1 inversion background abolishes DSB formation; ""decreased"" level in rtf1-W405G is relative to wild type and above the inverted-RTS1 background level"
PMID:19417105	PBO:0102566	(Supplemental Table S1).
PMID:19417105	PBO:0102566	(Supplemental Table S1).
PMID:19417105	PBO:0102566	(Supplemental Table S1).
PMID:19417105	PBO:0102566	Supplemental Table S1; Supplemental Fig. S3
PMID:19417105	GO:0018444	(Figure 1)
PMID:19417105	PBO:0102566	Supplemental Table S1; Supplemental Fig. S3
PMID:19417105	PBO:0102566	Supplemental Table S1; Supplemental Fig. S3
PMID:19417105	PBO:0102566	Supplemental Table S1; Supplemental Fig. S3
PMID:19417105	FYPO:0001645	(Fig. 5B)
PMID:19417105	PBO:0102566	Supplemental Table S1; Supplemental Fig. S3
PMID:19417105	GO:0018444	(Figure 1)
PMID:19417105	FYPO:0001645	(Fig. 5B)
PMID:19417105	FYPO:0001645	(Fig. 5B)
PMID:19417105	FYPO:0001355	(Figure 5A)
PMID:19417105	FYPO:0002061	(Figure 5A)
PMID:19417105	FYPO:0001355	(Figure 5A)
PMID:19417105	PBO:0102568	(Supplemental Table S1).
PMID:19417105	PBO:0102568	(Supplemental Table S1).
PMID:19417105	PBO:0102566	(Supplemental Table S1).
PMID:19417105	PBO:0102567	(Supplemental Table S1).
PMID:19422421	FYPO:0001357	(comment: actually 25 degrees, but calling it low to make distinction from inviable at 30)
PMID:19422421	PBO:0093629	(comment: 25 degrees, permissive for hsk1-89)
PMID:19422421	GO:0000785	(comment: increased chromatin association in presence of HU)
PMID:19422421	FYPO:0002061	(comment: CONDITION 30 degrees)
PMID:19422421	PBO:0093631	(comment: 25 degrees, but calling it low to make distinction from inviable at 30)
PMID:19422421	PBO:0093581	(comment: 25 degrees, but calling it low to make distinction from inviable at 30)
PMID:19422421	PBO:0093617	(comment: 25 degrees, but calling it low to make distinction from inviable at 30)
PMID:19422421	PBO:0103154	(comment: actually 25 degrees, but calling it low to make distinction from inviable at 30)
PMID:19422421	PBO:0103155	(comment: actually 25 degrees, but calling it low to make distinction from inviable at 30)
PMID:19422421	PBO:0093559	(comment: 25 degrees, permissive for hsk1-89)
PMID:19422421	PBO:0093580	(comment: 25 degrees, permissive for hsk1-89)
PMID:19422421	PBO:0093616	(comment: 25 degrees, permissive for hsk1-89)
PMID:19422421	PBO:0093561	(comment: 25 degrees, permissive for hsk1-89)
PMID:19422421	PBO:0093580	(comment: 25 degrees, permissive for hsk1-89)
PMID:19422421	PBO:0093616	(comment: 25 degrees, permissive for hsk1-89)
PMID:19427212	GO:1902408	(Fig. 4)
PMID:19427212	PBO:0112449	(Fig. 3B)
PMID:19427212	PBO:0112453	(Fig. 3A)
PMID:19427212	PBO:0112452	(Fig. 2D)
PMID:19427212	PBO:0112456	(Fig. 3C,D)
PMID:19427212	PBO:0112455	(Fig. 3C,D)
PMID:19427212	PBO:0112454	(Fig. 3C,D)
PMID:19427212	PBO:0112457	We conclude that fission yeast cytokinesis uses two overlapping mechanisms to position Mid1 at the central cortex. First, Cdr2 anchors Mid1 at the medial cortex during interphase through a physical interaction.
PMID:19427212	PBO:0112451	(Fig. 2D)
PMID:19427212	PBO:0112450	(Fig. 2B)
PMID:19427212	PBO:0112287	(Fig. 2B)
PMID:19427212	PBO:0112449	(Fig. 2B)
PMID:19427212	PBO:0112446	(Fig. 2C)
PMID:19427212	PBO:0112446	(Fig. 2C)
PMID:19427212	PBO:0112447	(Fig. 2C)
PMID:19427212	PBO:0112448	(Fig. 2C)
PMID:19427212	PBO:0112447	(Fig. 1C)
PMID:19427212	PBO:0112446	(Fig. 1C)
PMID:19427212	PBO:0112445	(Fig. 1B)
PMID:19427212	PBO:0112445	(Fig. 1B)
PMID:19427212	PBO:0112445	(Fig. 1B)
PMID:19427212	PBO:0112445	(Fig. 1B)
PMID:19427212	PBO:0112285	(Fig. 1B)
PMID:19427212	PBO:0112285	(Fig. 1B)
PMID:19427212	PBO:0112285	(Fig. 1B)
PMID:19427212	PBO:0112449	(Fig. 3B)
PMID:19430462	GO:0036450	urg1, gar2, act1, adh1, pof9 and hcn1 mRNAs were shown to be direct targets by cRACE sequence analysis.
PMID:19430466	PBO:0104403	(Fig. 2d)
PMID:19430466	PBO:0104404	(Fig. 2j)
PMID:19430466	GO:0005872	(comment: CHECK homodimer)
PMID:19430466	PBO:0104402	(Fig. 1f) (comment: ATP-dependent) Supplementary Information, Movie 1)
PMID:19430466	PBO:0104404	(Fig. 2j)
PMID:19430466	GO:0008017	(Fig. 2c)
PMID:19431238	GO:0051285	(comment: ocalization independent of actin cytoskeleton (assayed using latrunculin A) and microtubule cytoskeleton (assayed using carbendazim))
PMID:19431238	GO:0005938	(comment: ocalization independent of actin cytoskeleton (assayed using latrunculin A) and microtubule cytoskeleton (assayed using carbendazim))
PMID:1943699	PBO:0098027	(comment: assay construct also has nt change G36C to distinguish from snu2+ transcript)
PMID:1943699	PBO:0098027	(comment: assay construct also has nt change G36C to distinguish from snu2+ transcript)
PMID:1943699	PBO:0106466	(comment: assay construct also has nt change G36C to distinguish from snu2+ transcript)
PMID:1943699	PBO:0098027	(comment: assay construct also has nt change G36C to distinguish from snu2+ transcript)
PMID:1944266	FYPO:0001759	(comment: assayed substrate: rabbit muscle phosphorylase)
PMID:19443688	PBO:0120535	(Fig. 3D)
PMID:19443688	PBO:0094282	(Fig. 1)
PMID:19443688	PBO:0094679	(Fig. 1)
PMID:19443688	PBO:0094283	(Fig. 1)
PMID:19443688	PBO:0094283	(Fig. 4C)
PMID:19443688	PBO:0120536	(Fig. S3A)
PMID:19443688	PBO:0120537	(Fig. S3A)
PMID:19443688	PBO:0120538	(Fig. S3B)
PMID:19443688	PBO:0094679	(Fig. S5)
PMID:19443688	PBO:0094283	(Fig. 2D)
PMID:19443688	PBO:0094282	(Fig. 4C)
PMID:19443688	PBO:0094679	(Fig. 4C)
PMID:19454013	PBO:0095499	Rad21
PMID:19454013	PBO:0095500	Rad21
PMID:19474789	PBO:0018540	(Fig. 1a, b)
PMID:19474789	PBO:0018540	(Fig. 1a, b)
PMID:19474789	PBO:0024116	(Fig. 2c, d, e)
PMID:19474789	PBO:0107426	(Fig. 2a, S3a)
PMID:19474789	PBO:0107426	(Fig. 2a, S3a)
PMID:19474789	PBO:0107426	(Fig. 2a, S3a)
PMID:19474789	PBO:0107426	(Fig. 2a, S3a)
PMID:19474789	PBO:0108330	(Fig. 3a)
PMID:19474789	PBO:0095711	(Fig. 3)
PMID:19474789	PBO:0094619	Supplementary Fig. 10
PMID:19474789	GO:0031569	all data These data indicate that Pom1 functions in a dose-dependent manner to delay entry into mitosis through negative regulation of the Cdr2-Cdr1-Wee1 pathway. The pom1D size phenotype is not as severe as wee11 deletion, indicating that further Wee1 regulatory mechanisms are likely to be operating. We conclude that Pom1 is a potential functional link between polarized cell growth and mitotic entry by regulating these two processes.
PMID:19474789	PBO:0108336	all data These data indicate that Pom1 functions in a dose-dependent manner to delay entry into mitosis through negative regulation of the Cdr2-Cdr1-Wee1 pathway. The pom1D size phenotype is not as severe as wee11 deletion, indicating that further Wee1 regulatory mechanisms are likely to be operating. We conclude that Pom1 is a potential functional link between polarized cell growth and mitotic entry by regulating these two processes.
PMID:19474789	PBO:0107661	all data These data indicate that Pom1 functions in a dose-dependent manner to delay entry into mitosis through negative regulation of the Cdr2-Cdr1-Wee1 pathway. The pom1D size phenotype is not as severe as wee11 deletion, indicating that further Wee1 regulatory mechanisms are likely to be operating. We conclude that Pom1 is a potential functional link between polarized cell growth and mitotic entry by regulating these two processes.
PMID:19474789	PBO:0096311	Supplementary Table 2
PMID:19474789	PBO:0018346	(Fig. 2c, d, e)
PMID:19474789	PBO:0018540	(Fig. 2c, d, e)
PMID:19474789	FYPO:0003481	(Supplementary Table 1)
PMID:19474789	PBO:0094428	(Fig. 2a, Supplementary Fig. 3a)
PMID:19474789	PBO:0108327	(Fig. 2a, Supplementary Fig. 3a)
PMID:19474789	PBO:0096314	(Fig. 3)
PMID:19474789	PBO:0107426	(Fig. 2a, Supplementary Fig. 3a)
PMID:19474789	PBO:0110567	Supplementary Fig. 6
PMID:19474789	PBO:0107817	(Fig. S6)
PMID:19474789	PBO:0107428	(Fig. 2a, S3a)
PMID:19474789	PBO:0107428	(Fig. 2a, S3a)
PMID:19474789	PBO:0107817	(Fig. 2a, S3a)
PMID:19474789	PBO:0107426	(Fig. 2a, Supplementary Fig. 3a)
PMID:19474789	PBO:0096312	Supplementary Table 2 These experiments support the pom1 gradient model, pom1 is delocalized in tea1 delete
PMID:19474789	PBO:0018540	(Fig. 1a, b)
PMID:19474789	PBO:0095711	Supplementary Table 2 These experiments support the pom1 gradient model, pom1 is delocalized in tea1 delete
PMID:19474789	PBO:0096314	Supplementary Table 2 These experiments support the pom1 gradient model, pom1 is delocalized in tea1 delete
PMID:19474789	PBO:0103729	(Figure 4d)
PMID:19474789	PBO:0107426	(Fig. 2a, Supplementary Fig. 3a)
PMID:19474789	PBO:0096314	(Fig. 3)
PMID:19474789	PBO:0096314	(Fig. 3)
PMID:19474789	PBO:0096314	(Fig. 3)
PMID:19474789	PBO:0096314	(Fig. 3)
PMID:19474789	PBO:0096312	(Fig. 3)
PMID:19474789	PBO:0096314	(Fig. 3)
PMID:19474789	PBO:0096314	(Fig. 3)
PMID:19474789	PBO:0095711	(Fig. 3)
PMID:19474789	PBO:0103732	all data These data indicate that Pom1 functions in a dose-dependent manner to delay entry into mitosis through negative regulation of the Cdr2-Cdr1-Wee1 pathway. The pom1D size phenotype is not as severe as wee11 deletion, indicating that further Wee1 regulatory mechanisms are likely to be operating. We conclude that Pom1 is a potential functional link between polarized cell growth and mitotic entry by regulating these two processes.
PMID:19474789	PBO:0108328	(Fig. 2a, Supplementary Fig. 3a)
PMID:19474789	PBO:0096314	(Fig. 3)
PMID:19474789	PBO:0096311	(Fig. 3)
PMID:19474789	PBO:0095712	(Fig. 3)
PMID:19474789	PBO:0108335	Supplementary Figure S8
PMID:19474789	PBO:0108334	Supplementary Figure S8
PMID:19474789	PBO:0108333	Supplementary Figure S8
PMID:19474789	PBO:0108332	Supplementary Figure S8
PMID:19474789	PBO:0108331	(Fig. 2a, S3a)
PMID:19474789	PBO:0108331	(Fig. 2a, S3a)
PMID:19474789	PBO:0018540	(Fig. 1c, Supplementary Fig. 2a)
PMID:19474792	GO:0051285	(Supplementary Fig. 2)
PMID:19474792	PBO:0103732	(Fig. 1e) in vitro link from epistastis and delayed cdc2 phosphorylation
PMID:19474792	FYPO:0003736	(Fig. 3b).
PMID:19474792	FYPO:0003307	(Fig. 3b).
PMID:19474792	FYPO:0003736	(Fig. 3b).
PMID:19474792	FYPO:0003736	(Fig. 3b).
PMID:19474792	PBO:0103731	Table 1, Fig. 2d
PMID:19474792	FYPO:0001234	Table 1, Fig. 2d
PMID:19474792	FYPO:0003481	Table 1, Fig. 2d
PMID:19474792	FYPO:0001357	(comment: or is this reduced with low exressivity?)
PMID:19474792	FYPO:0001355	(Fig. 1b)
PMID:19474792	FYPO:0001355	(Fig. 1b)
PMID:19474792	PBO:0103730	(comment: cortex)
PMID:19474792	PBO:0103729	(Fig. 2a) and data not shown
PMID:19474792	PBO:0103729	(Fig. 2a) and data not shown
PMID:19474792	PBO:0103729	(Fig. 2a) and data not shown
PMID:19474792	PBO:0103728	(Supplementary Fig. 4)
PMID:19474792	PBO:0024047	(Supplementary Fig. 3)
PMID:19474792	PBO:0024047	(Supplementary Fig. 3)
PMID:19474792	GO:0051285	(Supplementary Fig. 2)
PMID:19474792	PBO:0094966	table1
PMID:19474792	PBO:0096311	Table 1
PMID:19474792	FYPO:0003481	Table 1
PMID:19474792	FYPO:0001355	(Fig. 1b)
PMID:19474792	FYPO:0003481	Table 1
PMID:19474792	PBO:0103724	Table 1
PMID:19474792	FYPO:0003481	Table 1
PMID:19474792	PBO:0103724	Table 1
PMID:19474792	PBO:0094966	table1
PMID:19474792	FYPO:0002516	(Fig. 3b).
PMID:19474792	PBO:0095712	table1
PMID:19474792	PBO:0095711	table1
PMID:19474792	PBO:0095712	table1
PMID:19474792	FYPO:0003481	Table 1
PMID:19474792	PBO:0096311	Table 1
PMID:19474792	FYPO:0003481	Table 1
PMID:19474792	PBO:0096311	Table 1
PMID:19474792	PBO:0096311	Table 1
PMID:19474792	PBO:0094966	table1
PMID:19474792	PBO:0094966	table1
PMID:19474792	PBO:0103725	(Fig. 1d) ie not blocked in g2
PMID:19474792	PBO:0103726	(Fig. 1e, 1f)
PMID:19474792	PBO:0103727	(Fig. 1e) in vitro link from epistastis and delayed cdc2 phosphorylation
PMID:19474792	PBO:0096180	(Fig. 1g)
PMID:19486165	FYPO:0000046	(Fig. 5C)
PMID:19486165	GO:0005635	(Fig. 2B)
PMID:19486165	GO:0042175	(Fig. 2A)
PMID:19486165	FYPO:0000110	(Fig. 1C)
PMID:19486165	FYPO:0002061	(data not shown).
PMID:19486165	FYPO:0002061	(Fig. 1A)
PMID:19486165	FYPO:0001234	(Fig. 1A)
PMID:19486165	FYPO:0000086	(Fig. 1A)
PMID:19486165	PBO:0093574	(Fig. 7B)
PMID:19486165	PBO:0097639	(Fig. 7B)
PMID:19486165	PBO:0097639	(Fig. 7B)
PMID:19486165	PBO:0093574	(Fig. 7B)
PMID:19486165	PBO:0093574	(Fig. 7B)
PMID:19486165	FYPO:0000110	(Figure 7A)
PMID:19486165	PBO:0097638	(Fig. 6C)
PMID:19486165	FYPO:0000046	(Fig. 5C)
PMID:19486165	FYPO:0000046	(Fig. 5C)
PMID:19486165	FYPO:0002720	(Fig. 5B)
PMID:19486165	FYPO:0002060	(Fig. 5A)
PMID:19486165	FYPO:0000032	(Figure 4C)
PMID:19486165	FYPO:0000046	(Figure 4C)
PMID:19486165	FYPO:0002061	(Figure 4C)
PMID:19486165	PBO:0097639	(Fig. 7B)
PMID:19486165	FYPO:0000650	(Fig. 4B)
PMID:19487457	FYPO:0007428	(comment: CHECK monopolar)
PMID:19487457	FYPO:0007426	(Figure 1 and 2) We conclude that it is the new SPB that fails to activate and insert into the nuclear envelope in cut12.1 mutants.
PMID:19487457	GO:0140480	(comment: CHECK insertion)
PMID:19487457	FYPO:0007427	our ability to identify cells in which an active SPB had apparently lost its association with the membrane completely and fallen into the middle of the nucleus (Fig. 3 E) and the proximity of the SPB to these gaps in the membrane (Fig. 3, A-C).
PMID:19487457	PBO:0107114	Surprisingly, in 50% (n = 79) of the cut12.1 cells that successfully completed mitosis, an efflux of the NLS-GFP--Gal marker accompanied mitotic commitment (Fig. 7, C and D).
PMID:19487457	FYPO:0007427	our ability to identify cells in which an active SPB had apparently lost its association with the membrane completely and fallen into the middle of the nucleus (Fig. 3 E) and the proximity of the SPB to these gaps in the membrane (Fig. 3, A-C).
PMID:19487457	FYPO:0007428	(comment: CHECK monopolar)
PMID:19487457	PBO:0107111	(Fig. 4 C and Video 3)
PMID:19487457	PBO:0107111	gapped membrane distortions in the nuclear envelope of cut12.1 cells at 36°C (Fig. 3, A-D). 7D
PMID:19487457	FYPO:0007426	(Figure 1 and 2) We conclude that it is the new SPB that fails to activate and insert into the nuclear envelope in cut12.1 mutants.
PMID:19487461	FYPO:0006822	(Fig. 1A) BrdU incorporation wee1-50 strain analysed at 32°C
PMID:19487461	PBO:0021770	(Fig. 1B)
PMID:19487461	PBO:0100211	(Fig. 1G) amount of tos1-GFP in nucleus is dependent on cdc10
PMID:19487461	FYPO:0006575	section titled MBF-dependent gene expression...these cells undergo G1 transcription, a seemingly normal Sphase (no region specific amplifications) and can only reinitiate replication once size per genome is minimal size.
PMID:19487461	FYPO:0001425	(Fig. 5A)
PMID:19502236	PBO:0114264	(Fig. 1B)
PMID:19502236	PBO:0114265	(Fig. 1C)
PMID:19502236	PBO:0022974	(Fig. 2)
PMID:19502236	PBO:0034991	(Fig. 2)
PMID:19502236	PBO:0114266	(Fig. 4B)
PMID:19502236	SO:0001531	Nonetheless, taken together, our results are consistent with the 93-100-amino acid region of Php4 functioning as an NES in S. pombe.
PMID:19502236	PBO:0114268	(Fig. 7B)
PMID:19502236	PBO:0114268	(Fig. 7B)
PMID:19502236	PBO:0114269	(Fig. 7B)
PMID:19502236	PBO:0114269	(Fig. 7B)
PMID:19502236	PBO:0114270	(Fig. 7B)
PMID:19502236	PBO:0114270	(Fig. 7B)
PMID:19502236	PBO:0114270	(Fig. 7B)
PMID:19502236	PBO:0114270	(Fig. 7B)
PMID:19502236	PBO:0114272	(Fig. 9A)
PMID:19502236	PBO:0114273	(Fig. 9A)
PMID:19502236	PBO:0114271	(Fig. 9A)
PMID:19502236	PBO:0114271	(Fig. 9A)
PMID:19502236	PBO:0114272	(Fig. 9A)
PMID:19502236	PBO:0114271	(Fig. 9A)
PMID:19502236	PBO:0114266	(Fig. 7C)
PMID:19502236	PBO:0114263	(Fig. 1A)
PMID:19502236	PBO:0114264	(Fig. 1B)
PMID:19523829	FYPO:0002638	((comment: CHECK increased localization of mad2 to kinetochore)
PMID:19543678	PBO:0099031	(comment: from PM ) (Fig. 3c
PMID:19543678	PBO:0099033	(Fig. 3)
PMID:19543678	PBO:0099032	(Fig. 3)
PMID:19546237	GO:0010971	(comment: CHECK during recovery from stress)
PMID:19567474	PBO:0093560	(Fig. 3A)
PMID:19567474	PBO:0093560	(Fig. 3A)
PMID:19567474	PBO:0114392	(Fig. 4)
PMID:19567474	PBO:0114391	(Fig. 4)
PMID:19567474	PBO:0093560	(Fig. 3A)
PMID:19570908	GO:1902404	(comment: request and use GO:new positive regulation of (MF) microfilament motor activity instead? depends on ancestry of motor activity branch)
PMID:19570908	PBO:0095205	(comment: CONDITION 25 degrees C, i.e. lower end of normal temp. range; penetrance higher at 29 degrees C)
PMID:19571115	PBO:0108193	(Fig. 1)
PMID:19571115	PBO:0108195	(Fig. 5D)
PMID:19571115	FYPO:0007572	(Fig. 5a)
PMID:19571115	FYPO:0000411	(Fig. 5B)
PMID:19571115	FYPO:0002060	(Fig. 5B)
PMID:19571115	PBO:0108194	(Fig. 1)
PMID:19592249	PBO:0095924	(Figure 2a) abolished
PMID:19592249	GO:1902426	(Fig. 2)
PMID:19592249	FYPO:0002638	(Figure 2)
PMID:19592249	PBO:0095923	(Figure 1E)
PMID:19592249	PBO:0095922	(Figure 1E)
PMID:19592249	GO:0090267	(Fig. 1)
PMID:19592249	PBO:0095921	(Figure 1a)
PMID:19592249	PBO:0095920	(Figure 1a)
PMID:19592249	FYPO:0002638	(Figure 2)
PMID:19592249	PBO:0095925	(Figure 2a) (comment: CHECK abolished)
PMID:19597328	PBO:0099108	Kin1-GFP was detected on the new cell end in early G2 as previously reported24 but also on the old end soon after growth resumption (arrow, Fig. 1C) conversely to the previous report.24
PMID:19597328	PBO:0115021	he par1Δ mutant shows a nuclear and septum (arrowhead, Fig. 6C; 25.6% of asymmetric septa versus 10.2% in wild type cells)
PMID:19597328	FYPO:0003302	Hence, Kin1-K154R acts as a dominant negative mutant and its primary effect is to inhibit maintenance of the nucleus at the geometric cell centre.
PMID:19597328	FYPO:0003013	Thus, Kin1 downregulation in tea4Δ uncoupled packed ring formation and constriction but also altered ring disassembly in a subset of cells.
PMID:19597328	FYPO:0000161	Kin1 was downregulated. Upon Kin1 repression, we observed a defect in F-actin incorporation into the CAR at mitosis compared to Kin1 ON. In 84% of anaphase cells, F-actin patches and/or cables were present outside
PMID:19597328	FYPO:0000117	Kin1 downregulation promoted aberrant septum material synthesis in tea4Δ: a main asymmetric septal structure was observed together with aberrant septal deposits along the cortex or stretched structures that run along the main cell axis were detected (Fig. 4B)
PMID:19597328	FYPO:0003302	of the nucleus relative to the cell ends in late G2 cells (≥10 μm) and we observed that a higher proportion of nuclei were misplaced towards the new cell end
PMID:19597328	FYPO:0001125	Cell shape or interphase F-actin polarity defects were not observed (Suppl. Fig. S1) conversely to the deletion strain.
PMID:19597328	FYPO:0000339	In Kin1 downregulating cells, we observed that septa were orthogonal to the long cell axis but their positions seemed to be frequently eccentric (Kin1 OFF, Fig. 3A).
PMID:19597328	PBO:0115020	During mitosis, the tip signal was detected on the most distant cell end relative to the asymmetric ring (arrow, Fig. 1B). Kin1-GFP was also detected at the division site in tea4Δ (arrowhead, Fig. 1B). We conclude that correct localization of Kin1-GFP does not require Tea4.
PMID:19597328	PBO:0115019	During mitosis, the tip signal was detected on the most distant cell end relative to the asymmetric ring (arrow, Fig. 1B). Kin1-GFP was also detected at the division site in tea4Δ (arrowhead, Fig. 1B). We conclude that correct localization of Kin1-GFP does not require Tea4.
PMID:19597328	PBO:0093560	Moreover, double mutant cells completey lose their polarity and appeared almost round. This phenotype is strickingly similar to that of kin1Δ tea1Δ (Fig. 2A and B).
PMID:19597328	PBO:0093560	Moreover, double mutant cells completey lose their polarity and appeared almost round. This phenotype is strickingly similar to that of kin1Δ tea1Δ (Fig. 2A and B).
PMID:19597328	PBO:0093560	Moreover, double mutant cells completey lose their polarity and appeared almost round. This phenotype is strickingly similar to that of kin1Δ tea1Δ (Fig. 2A and B).
PMID:19597328	PBO:0093560	Moreover, double mutant cells completey lose their polarity and appeared almost round. This phenotype is strickingly similar to that of kin1Δ tea1Δ (Fig. 2A and B).
PMID:19597328	PBO:0114715	Moreover, double mutant cells completey lose their polarity and appeared almost round. This phenotype is strickingly similar to that of kin1Δ tea1Δ (Fig. 2A and B).
PMID:19597328	PBO:0114715	Moreover, double mutant cells completey lose their polarity and appeared almost round. This phenotype is strickingly similar to that of kin1Δ tea1Δ (Fig. 2A and B).
PMID:19597328	PBO:0115018	Moreover, double mutant cells completey lose their polarity and appeared almost round. This phenotype is strickingly similar to that of kin1Δ tea1Δ (Fig. 2A and B).
PMID:19597328	PBO:0115016	Kin1Δ tea4Δ cells showed a severe cytokinetic phenotype (Fig. 2A), with aberrant septal material randomly deposited in a majority of cells (Fig. 2B).
PMID:19597328	PBO:0115015	Kin1Δ cells synthesize normal septa (Fig. 2A) but exhibit a high septation index and a small percentage of multi- septate cells (Fig. 2B), indicating a cell separation defect as previously shown.22-24
PMID:19597328	FYPO:0000650	Kin1Δ cells synthesize normal septa (Fig. 2A) but exhibit a high septation index and a small percentage of multi- septate cells (Fig. 2B), indicating a cell separation defect as previously shown.22-24
PMID:19597328	FYPO:0006213	Kin1Δ cells synthesize normal septa (Fig. 2A) but exhibit a high septation index and a small percentage of multi- septate cells (Fig. 2B), indicating a cell separation defect as previously shown.22-24
PMID:19597328	PBO:0018576	Indeed, in mitotic cells, we detected a Kin1-GFP signal at the division site (arrowheads, Fig. 1A and C). Kin1-GFP appeared as a ring overlying the cell equator prior to nuclei separation at the onset of anaphase B (Fig. 1C).
PMID:19597328	PBO:0115014	The kin1-GFP strain exhibited a wild type phenotype. In living interphase cells, Kin1-GFP signal captured either in static images (Fig. 1A) or by time-lapse video microscopy (Fig. 1C) was localized at the cell tips (arrows, Fig. 1A). The signal appeared as dynamic dots close to the plasma membrane (Suppl. movie S1). Kin1-GFP was detected on the new cell end in early G2 as previously reported24 but also on the old end soon after growth resumption (arrow, Fig. 1C) conversely to the previous report.24
PMID:19605557	PBO:0100329	(Figure 6)
PMID:19605557	GO:0106407	GIIΔ Is Required for an Efficient In Vitro Glucose Trimming from G2M9 and G1M9
PMID:19605557	FYPO:0007797	However, GII activity is significantly reduced in the microsomal fraction of ΔGIIΔ cells (Figure 2B), suggesting that GIIΔ is involved in ER localization of GII+
PMID:19605557	PBO:0100329	(Figure 6)
PMID:19605557	PBO:0100329	(Figure 6)
PMID:19605557	PBO:0100329	(Figure 6)
PMID:19606211	SO:0001528	See Fig. 1
PMID:19606211	SO:0001531	(comment: CHECK Sequence LVIAMDQLNL mentioned in the text)
PMID:19624755	PBO:0093558	Dapl2 and Dapm1 cells were more sensitive when exposed to 34 °C or to 5 mM VPA compared with those of Dapl4 and Daps1 cells
PMID:19624755	PBO:0106298	(comment: localized to large endosomal structures)
PMID:19624755	PBO:0106298	(comment: localized to large endosomal structures)
PMID:19624755	PBO:0106298	(comment: localized to large endosomal structures)
PMID:19624755	PBO:0107027	(comment: localized to large endosomal structures)
PMID:19624755	GO:0005794	n wild-type cells, most of Krp1- red fluorescent protein (RFP) colocalized with GFP- Vrg4 (Fig. 7a), indicating that Krp1 mainly localized to the Golgi apparatus
PMID:19624755	GO:0005794	n wild-type cells, most of Krp1- red fluorescent protein (RFP) colocalized with GFP- Vrg4 (Fig. 7a), indicating that Krp1 mainly localized to the Golgi apparatus
PMID:19624755	PBO:0106298	(comment: localized to large endosomal structures)
PMID:19624755	PBO:0106298	(comment: localized to large endosomal structures)
PMID:19624755	PBO:0106298	(comment: localized to large endosomal structures)
PMID:19624755	PBO:0106298	(comment: localized to large endosomal structures)
PMID:19624755	GO:0005768	(Fig. 6a)
PMID:19624755	GO:0005886	(Fig. 6a)
PMID:19624755	PBO:0107026	(Fig. 5)
PMID:19624755	PBO:0107026	(Fig. 5)
PMID:19624755	PBO:0107025	(Fig. 5)
PMID:19624755	PBO:0107025	(Fig. 5)
PMID:19624755	PBO:0107025	(Fig. 5)
PMID:19624755	PBO:0107024	(Fig. 5)
PMID:19624755	PBO:0107023	(Fig. 5)
PMID:19624755	PBO:0107023	(Fig. 5)
PMID:19624755	GO:0005794	(Fig. 4) suggesting that the four adaptin subunits of the AP-1 complex are all localized to the Golgi ⁄ endosomes.
PMID:19624755	PBO:0093558	Dapl2 and Dapm1 cells were more sensitive when exposed to 34 °C or to 5 mM VPA compared with those of Dapl4 and Daps1 cells
PMID:19624755	PBO:0093720	Dapl2 and Dapm1 cells were more sensitive when exposed to 34 °C or to 5 mM VPA compared with those of Dapl4 and Daps1 cells
PMID:19624755	PBO:0093720	Dapl2 and Dapm1 cells were more sensitive when exposed to 34 °C or to 5 mM VPA compared with those of Dapl4 and Daps1 cells
PMID:19624755	PBO:0093558	Dapl2 and Dapm1 cells were more sensitive when exposed to 34 °C or to 5 mM VPA compared with those of Dapl4 and Daps1 cells
PMID:19624755	PBO:0093645	(Fig. 2b) whereas that of Dapl4 and Daps1 cells was partially inhibited
PMID:19624755	PBO:0093641	(Fig. 2b) D-apl2 and D-apm1 cells was completely inhibited in the presence of FK506
PMID:19624755	PBO:0093641	(Fig. 2b) D-apl2 and D-apm1 cells was completely inhibited in the presence of FK506
PMID:19625445	PBO:0101778	(Figure 5B)
PMID:19625445	PBO:0094763	(Figure 5B)
PMID:19625445	PBO:0101762	(Figure 4A)
PMID:19625445	PBO:0099926	(Figure 4A) (comment: IS THIS NORMAL OR EVEN HIGHER THAN WT?)
PMID:19625445	PBO:0101763	(Figure 4A) (comment: IS THIS NORMAL OR EVEN HIGHER THAN WT? this is higher than wis1DD-cpc2delet so must be increased)
PMID:19625445	PBO:0097115	(Figure 3D)
PMID:19625445	PBO:0101755	(Fig. 2A)
PMID:19625445	PBO:0101754	(Fig. 2A)
PMID:19625445	PBO:0101753	(Fig. 2A)
PMID:19625445	PBO:0101752	(Fig. 1D)
PMID:19625445	PBO:0101752	(Fig. 1D)
PMID:19625445	PBO:0101751	(Fig. 1D)
PMID:19625445	PBO:0101751	(Fig. 1D)
PMID:19625445	PBO:0099872	(Fig. 1C)
PMID:19625445	PBO:0101764	(Figure 3D)
PMID:19625445	PBO:0101765	(Figure 3D)
PMID:19625445	PBO:0101769	(Figure 4B)
PMID:19625445	PBO:0101770	(Figure 4B)
PMID:19625445	PBO:0101771	(Figure 4B)
PMID:19625445	PBO:0101772	(Figure 4c)
PMID:19625445	PBO:0101773	(Figure 4c)
PMID:19625445	PBO:0101776	(Figure 5B)
PMID:19625445	PBO:0101766	(Figure 3D)
PMID:19625445	PBO:0101774	(Fig. 2A)
PMID:19625445	PBO:0101767	(Figure 4B)
PMID:19625445	PBO:0101760	(Fig. 2D)
PMID:19625445	PBO:0095501	(Fig. 2D)
PMID:19625445	PBO:0101761	(Figure 3D)
PMID:19625445	PBO:0093577	(Figure 6a)
PMID:19625445	FYPO:0000961	(Figure 6a)
PMID:19625445	FYPO:0001037	(Figure 6a)
PMID:19625445	PBO:0099902	(Figure 6a)
PMID:19625445	PBO:0093612	(Figure 6a)
PMID:19625445	PBO:0099902	(Figure 6a)
PMID:19625445	PBO:0093612	(Figure 6a)
PMID:19625445	PBO:0101780	(Figure 5D)
PMID:19625445	PBO:0101779	(Figure 5D)
PMID:19625445	PBO:0101777	(Figure 5B)
PMID:19625445	PBO:0101775	(Figure 9)
PMID:19625445	PBO:0099871	(Fig. 1C)
PMID:19625445	FYPO:0007520	(Fig. 1C)
PMID:19625445	PBO:0101768	(Figure 4B)
PMID:19625445	PBO:0095212	(Figure 9)
PMID:19625445	PBO:0101786	(Figure 9B)
PMID:19625445	PBO:0097115	(Figure 9B)
PMID:19625445	PBO:0101785	(Fig. 9A)
PMID:19625445	FYPO:0007525	(Fig. 8)
PMID:19625445	FYPO:0002444	(Fig. 8)
PMID:19625445	PBO:0101784	(Figure 7)
PMID:19625445	PBO:0101783	(Figure 7)
PMID:19625445	PBO:0101782	(Figure 7)
PMID:19625445	PBO:0101781	(Figure 6c,d)
PMID:19625445	PBO:0099872	(Fig. 1C)
PMID:19625445	PBO:0099872	(Fig. 1C)
PMID:19625445	PBO:0033281	(Fig. 1)
PMID:19625445	PBO:0032799	(Fig. 1)
PMID:19625445	PBO:0093578	(Figure 6a)
PMID:19625445	PBO:0101750	(Fig. 1)
PMID:19625445	PBO:0101750	(Fig. 1)
PMID:19625445	FYPO:0000223	(Fig. 1)
PMID:19625445	FYPO:0002106	(Fig. 1) (comment: IS THIS SMALL OR STUBBY? 11.6 +/- 0.45)
PMID:19625445	PBO:0101750	(Fig. 1) (comment: 16.5 +/- 0.78)
PMID:19625445	PBO:0101774	(Fig. 2A)
PMID:19625445	PBO:0095212	(Figure 5A)
PMID:19625445	FYPO:0007520	(Fig. 2B)
PMID:19625445	PBO:0101775	(Figure 5A)
PMID:19625445	PBO:0093578	(Figure 6a)
PMID:19625445	PBO:0093576	(Figure 6a)
PMID:19625445	PBO:0101756	(Fig. 2A)
PMID:19625445	PBO:0101756	(Fig. 2B)
PMID:19625445	PBO:0101756	(Fig. 2A)
PMID:19625445	PBO:0101757	(Fig. 2B)
PMID:19625445	PBO:0101758	(Fig. 2B)
PMID:19625445	PBO:0101759	(Fig. 2A)
PMID:19625445	PBO:0101753	(Fig. 2A)
PMID:19627505	GO:0070867	(comment: localization requires F-actin -assayed using latrunculin A and membrane rafts -assayed using filipin)
PMID:19636559	FYPO:0004481	data not shown, from text
PMID:19636559	PBO:0103845	data not shown, from text
PMID:19636559	PBO:0103845	data not shown, from text
PMID:19643199	FYPO:0001423	(Fig. 1d)
PMID:19643199	FYPO:0001423	(Fig. 1d) (comment: CHECK this term should really be trafficing)
PMID:19643199	FYPO:0006266	(Fig. 1d)
PMID:19643199	PBO:0095556	(Fig. 1c)
PMID:19646873	PBO:0095264	(Fig. 2f)
PMID:19646873	PBO:0095264	(Fig. S2)
PMID:19646873	PBO:0105342	(Fig. 2f)
PMID:19646873	PBO:0105340	(Fig. 2f)
PMID:19646873	PBO:0105341	(Fig. 2f)
PMID:19680287	PBO:0105460	(Fig. 3B,C)
PMID:19680287	FYPO:0004318	(Fig. 1A)
PMID:19680287	FYPO:0004318	(Fig. 1A)
PMID:19680287	FYPO:0004318	(Fig. 1A)
PMID:19680287	FYPO:0004318	(Fig. 1A)
PMID:19680287	FYPO:0003762	(Fig. 1A)
PMID:19680287	PBO:0096315	(Fig. 1B, S3)
PMID:19680287	PBO:0096316	(Fig. 1B, S3)
PMID:19680287	PBO:0105458	(Fig. 1B, S3)
PMID:19680287	PBO:0096322	(Fig. 1B, S3)
PMID:19680287	FYPO:0005684	(Fig. 2A) (comment: assayed with plo1 GFP)
PMID:19680287	PBO:0037150	(Fig. 2B)
PMID:19680287	PBO:0105459	(Fig. 2B)
PMID:19680287	PBO:0105461	(Fig. 3B,C)
PMID:19680287	PBO:0105462	(Fig. 3B,C)
PMID:19680287	PBO:0105463	(Fig. 3E)
PMID:19680287	PBO:0105464	(Fig. 3E)
PMID:19680287	PBO:0105464	(Fig. 3E)
PMID:19680287	PBO:0105465	(Fig. 3E, S9)
PMID:19680287	PBO:0105465	(Fig. 3E, S9)
PMID:19680287	FYPO:0004318	(Fig. S2A)
PMID:19680287	FYPO:0004318	(Fig. S2A)
PMID:19680287	FYPO:0003762	(Fig. S2A)
PMID:19680287	FYPO:0004318	(Fig. S2B)
PMID:19680287	FYPO:0004318	(Fig. S2B)
PMID:19680287	FYPO:0003762	(Fig. S2B)
PMID:19680287	PBO:0096322	(Fig. S6A,B)
PMID:19680287	PBO:0096323	(Fig. S6C,D)
PMID:19680287	PBO:0096323	(Fig. S6C,D)
PMID:19680287	PBO:0105466	(Fig. S7)
PMID:19680287	FYPO:0004396	(Fig. S10)
PMID:19680287	FYPO:0006428	(Fig 3C), showed a similar fraction of mono-oriented chromosomes as wild-type cells
PMID:19680287	FYPO:0005720	rarely showed a delay in bi-orienting chromosomes that had been pulled towards one SPB (Fig 3B,D; supplementary Fig S4F online).
PMID:19686686	PBO:0095696	(Figure 3D)
PMID:19686686	PBO:0095690	(comment: cdc2 dependent phophorylation) (fig. 4B)
PMID:19686686	GO:1990023	(Fig. 4a)
PMID:19686686	GO:1990023	(Fig. 4a)
PMID:19686686	FYPO:0003268	(Fig. 5C)
PMID:19686686	FYPO:0005343	(Fig. 5C)
PMID:19686686	PBO:0095689	(Fig. 5C)
PMID:19686686	PBO:0095696	(Figure 3D)
PMID:19686686	PBO:0095696	(Figure 3D)
PMID:19686686	PBO:0033576	(comment: CHECK mitotic anaphase B, mitotic telophase)
PMID:19686686	PBO:0033575	(comment: CHECK mitotic anaphase B, mitotic telophase)
PMID:19686686	FYPO:0000620	(comment: with monopolar spindle)
PMID:19686686	FYPO:0005342	(Fig. 1e)
PMID:19686686	FYPO:0005342	(Fig. 1e)
PMID:19686686	PBO:0095697	(Figure 3D)
PMID:19686686	PBO:0095697	(Figure 3D)
PMID:19686686	PBO:0109478	(comment: CHECK interacts with unmodified Klp9 PR:000027705)
PMID:19686686	FYPO:0005342	(Fig. 1e)
PMID:19686686	FYPO:0005342	(Fig. 1e)
PMID:19686686	FYPO:0005342	(Fig. 1e)
PMID:19686686	FYPO:0005342	(Fig. 1e)
PMID:19686686	FYPO:0005342	(Fig. 1e)
PMID:19686686	PBO:0022963	(comment: CHECK mitotic anaphase B)
PMID:19686686	PBO:0033574	(comment: CHECK interphase, prophase, metaphase,anaphase A)
PMID:19686686	PBO:0021821	(comment: CHECK interphase, prophase, metaphase,anaphase A)
PMID:19686686	PBO:0033573	(comment: CHECK interphase, prophase, metaphase,anaphase A)
PMID:19686686	PBO:0033572	(comment: CHECK interphase, prophase, metaphase,anaphase A)
PMID:19686686	PBO:0109478	(comment: CHECK interacts with unmodified Ase1 PR:000027520)
PMID:19686686	PBO:0095694	(Fig. 5C)
PMID:19686686	PBO:0094040	(comment: cdc2 dependent phophorylation) (fig. 5B)
PMID:19693008	PBO:0110856	When Dpht1 was combined with mutant alleles of clr4 or rik1—components of the Clr4-containing methyltransferase complex (ClrC)7—the resultant double mutants showed severe growth defects and a large, synergistic increase in antisense RNAs at .20% of genes (Fig. 2a and Supplementary Figs 5 and 7a, b). Consistent with ClrC directly participating in antisense suppression, Rik1 was found at the convergent loci (Supplementary Fig. 7c).
PMID:19693008	PBO:0110856	When Dpht1 was combined with mutant alleles of clr4 or rik1—components of the Clr4-containing methyltransferase complex (ClrC)7—the resultant double mutants showed severe growth defects and a large, synergistic increase in antisense RNAs at .20% of genes (Fig. 2a and Supplementary Figs 5 and 7a, b). Consistent with ClrC directly participating in antisense suppression, Rik1 was found at the convergent loci (Supplementary Fig. 7c).
PMID:19693008	PBO:0110850	When Dpht1 was combined with mutant alleles of clr4 or rik1—components of the Clr4-containing methyltransferase complex (ClrC)7—the resultant double mutants showed severe growth defects and a large, synergistic increase in antisense RNAs at .20% of genes (Fig. 2a and Supplementary Figs 5 and 7a, b). Consistent with ClrC directly participating in antisense suppression, Rik1 was found at the convergent loci (Supplementary Fig. 7c).
PMID:19693008	PBO:0110850	When Dpht1 was combined with mutant alleles of clr4 or rik1—components of the Clr4-containing methyltransferase complex (ClrC)7—the resultant double mutants showed severe growth defects and a large, synergistic increase in antisense RNAs at .20% of genes (Fig. 2a and Supplementary Figs 5 and 7a, b). Consistent with ClrC directly participating in antisense suppression, Rik1 was found at the convergent loci (Supplementary Fig. 7c).
PMID:19693008	PBO:0110850	When Dpht1 was combined with mutant alleles of clr4 or rik1—components of the Clr4-containing methyltransferase complex (ClrC)7—the resultant double mutants showed severe growth defects and a large, synergistic increase in antisense RNAs at .20% of genes (Fig. 2a and Supplementary Figs 5 and 7a, b). Consistent with ClrC directly participating in antisense suppression, Rik1 was found at the convergent loci (Supplementary Fig. 7c).
PMID:19693008	PBO:0110850	When Dpht1 was combined with mutant alleles of clr4 or rik1—components of the Clr4-containing methyltransferase complex (ClrC)7—the resultant double mutants showed severe growth defects and a large, synergistic increase in antisense RNAs at .20% of genes (Fig. 2a and Supplementary Figs 5 and 7a, b). Consistent with ClrC directly participating in antisense suppression, Rik1 was found at the convergent loci (Supplementary Fig. 7c).
PMID:19693008	PBO:0110850	(Delta)pht1 caused a disproportionate increase in antisense transcripts at many (,5-8%) euchromatic loci (Fig. 1e-g and Supplementary Fig. 5), as confirmed by PCR with strand-specific reverse transcription (RT-PCR; Fig. 1f).
PMID:19693008	PBO:0110855	At euchromatic loci, H2A.Z localizes preferentially in intergenic regions (Supplementary Fig. 3b)
PMID:19693008	FYPO:0005071	Dpht1 causes a slight increase in silencing at the pericentromeric region, but H3K9me distribution at heterochromatic loci is not severely altered (Supplementary Fig. 4a).
PMID:19693008	PBO:0110857	However, antisense RNAs did not accumulate extensively in Dswi6 cells and the synergistic increase in antisense RNAs observed in the Dclr4 Dpht1 mutant was not observed in the Dswi6 Dpht1 mutant (Fig. 2a). Thus, ClrC and Ago1 contribute to antisense suppression by a new mechanism(s).
PMID:19693008	PBO:0110856	Deletion of exosome subunit rrp6 led to an antisense profile closely resembling that of Dclr4 Dpht1, with read-through antisense RNA covering entire ORFs at convergent genes (Fig. 3b). When Dpht1 was combined with mutant alleles of clr4 or rik1—components of the Clr4-containing methyltransferase complex (ClrC)7—the resultant double mutants showed severe growth defects and a large, synergistic increase in antisense RNAs at .20% of genes (Fig. 2a and Supplementary Figs 5 and 7a, b). Consistent with ClrC directly participating in antisense suppression, Rik1 was found at the convergent loci (Supplementary Fig. 7c).
PMID:19693008	PBO:0110850	the synergistic increase in antisense RNAs observed in the Dclr4 Dpht1 mutant was not observed in the Dswi6 Dpht1 mutant (Fig. 2a).
PMID:19693008	PBO:0110856	Combining Dago1 with Dpht1 resulted in synergistic upregulation of antisense transcripts, as in Dclr4 Dpht1 (Fig. 2a). When Dpht1 was combined with mutant alleles of clr4 or rik1—components of the Clr4-containing methyltransferase complex (ClrC)7—the resultant double mutants showed severe growth defects and a large, synergistic increase in antisense RNAs at .20% of genes (Fig. 2a and Supplementary Figs 5 and 7a, b). Consistent with ClrC directly participating in antisense suppression, Rik1 was found at the convergent loci (Supplementary Fig. 7c).
PMID:19693008	PBO:0110854	affected chromatin association of Swr1, distribution of H2A.Z across the genome (Supplementary Fig. 2c).
PMID:19696784	PBO:0106856	(Fig 3B)
PMID:19696784	PBO:0106852	(Fig. 1C)
PMID:19696784	PBO:0106853	(Fig. 2A,B)
PMID:19696784	PBO:0106851	(Fig. 1C)
PMID:19696784	PBO:0106857	(Fig 3B)
PMID:19696784	PBO:0106859	supplementary Fig S6 online
PMID:19696784	PBO:0106855	(Fig 3B)
PMID:19696784	PBO:0106858	(Figure 5)
PMID:19713940	FYPO:0002437	(comment: CONDITION temperature restrictive for cdc25-22)
PMID:19713940	PBO:0095570	(comment: CONDITION observed after short-duration overexpression)
PMID:19713940	GO:0051015	assayed using N-terminal Rng2-Ns fragment or calponin homology domain (CHD) fragment
PMID:19713940	FYPO:0002437	(comment: CONDITION temperature restrictive for cdc25-22)
PMID:19713940	FYPO:0002437	(comment: CONDITION temperature restrictive for cdc25-22)
PMID:19714215	PBO:0092599	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114033	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114034	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114035	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114036	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114037	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114038	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114039	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114040	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114041	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114032	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114031	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114030	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0110589	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114042	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114043	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114044	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114045	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114046	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114047	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114048	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114049	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114050	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114051	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114052	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114053	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114054	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114028	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114027	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114026	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114025	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114024	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114023	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114022	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114021	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0092550	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114020	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114019	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114018	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114017	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114016	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114015	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0113986	Among 24 genes proposed to be MBF targets (Figure 1A) [14], the promoters of 19 genes were substantially enriched in the Yox1p ChIPs, including yox1 itself (Figure 1B).
PMID:19714215	PBO:0113986	MBF, we performed ChIP-chip using an antibody against the MBF component Cdc10p. As for Yox1p, among the 24 proposed MBF targets, the promoters of the same 19 genes, including cdc10 itself and yox1, were substantially enriched in the Cdc10p ChIPs (Figure 1C)
PMID:19714215	PBO:0092701	Taken together, these data show that yox1 is transcriptionally activated by MBF, and Yox1p in turn binds itself to MBF target genes.
PMID:19714215	GO:0030907	HA-tagged Yox1p revealed an interaction between Cdc10p and Yox1p (Figure 2A). Moreover, anti-myc immuno complexes prepared from cells expressing Res2p-myc, Yox1p-HA or both showed an interaction between Res2p and Yox1p (Figure 2B) These results are confirmed by independent data from a recent mass spectrometry-based analysis of affinity-purified Res2p and Nrm1p complexes [20]. Based on these mass spectrometry data, Yox1p interacts with both Res2p and Nrm1p, with coverage of Yox1p by specific peptides being similar to the MBF component Cdc10p (data not shown). Together, these data indicate that Yox1p physically associates with the MBF complex and thus represents a new component of MBF.
PMID:19714215	PBO:0113987	This analysis revealed that Yox1p binding to the cdc22 promoter depends on both of the MBF components tested, Res2p and Nrm1p (Figure 2C). We conclude that Yox1p can bind to MBF- regulated promoters only via intact MBF.
PMID:19714215	PBO:0113987	This analysis revealed that Yox1p binding to the cdc22 promoter depends on both of the MBF components tested, Res2p and Nrm1p (Figure 2C). We conclude that Yox1p can bind to MBF- regulated promoters only via intact MBF.
PMID:19714215	PBO:0092092	the Yox1p levels were low during M/G1-phase but then strongly increased during S-phase (Figure 2D, top), peaking about 40 minutes after the peak of yox1 mRNA levels.
PMID:19714215	PBO:0113988	The cell cycle-regulated target genes bound by both Yox1p and Cdc10p tended to be more highly expressed in yox1D than in wild-type cells (Figure 3A,B). In yox1D cells, on the other hand, the Yox1p/Cdc10p targets showed little or no cell-cycle regulation, whereas the cell-cycle regulation of Ace2p targets was not affected (Figure 4A).
PMID:19714215	PBO:0113989	kinesin-like protein, which was bound by both Yox1p and Cdc10p and induced in yox1D cells, suggesting that klp8 is regulated by both Ace2p and MBF.
PMID:19714215	PBO:0113991	The Yox1p/Cdc10p target genes showed consistently higher Pol II occupancy in yox1D than in wild-type cells (Figure 3C,D)
PMID:19714215	PBO:0113992	A few genes, however, seem to be positively regulated by Yox1p (Figure 3A,B). An example is mfm2 (Figure 3A), encoding a precursor for the M-factor peptide (a mating pheromone) [33], and the neighbouring SPAC513.04, a sequence orphan that is divergently transcribed from mfm2.
PMID:19714215	PBO:0113993	A few genes, however, seem to be positively regulated by Yox1p (Figure 3A,B). An example is mfm2 (Figure 3A), encoding a precursor for the M-factor peptide (a mating pheromone) [33], and the neighbouring SPAC513.04, a sequence orphan that is divergently transcribed from mfm2.
PMID:19714215	PBO:0113994	Another example is map1, encoding a MADS-box transcription factor involved in the transcriptional response during mating
PMID:19714215	PBO:0113995	Taken together, we conclude that cell-cycle regulated transcription of Yox1p/Cdc10p target genes is highly deficient in yox1D cells, reflecting that these genes are no longer down-regulated after S-phase.
PMID:19714215	PBO:0114014	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114013	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0113996	Taken together, we conclude that cell-cycle regulated transcription of Yox1p/Cdc10p target genes is highly deficient in yox1D cells, reflecting that these genes are no longer down-regulated after S-phase.
PMID:19714215	FYPO:0001357	yox1D cells were viable and did not show any overall growth defect (Figure 4B).
PMID:19714215	PBO:0095095	The septation index was marginally higher in yox1D compared to wild-type cells (10.4% vs 9.4%), suggesting a slight delay in cytokinesis and/or cell separation.
PMID:19714215	PBO:0114012	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114011	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114010	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	FYPO:0003481	The yox1D cells were about 14% longer on average than wild-type cells during septation (17.4 mm vs 15.3 mm) (Figure 4C).
PMID:19714215	PBO:0113997	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0113998	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0101745	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0113999	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0092561	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114000	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114001	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114002	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114003	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114004	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114005	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0092714	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114006	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114007	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114008	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114009	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0105614	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0094372	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0092607	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0097776	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114055	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114056	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114057	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114058	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114059	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0101183	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114060	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0114029	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	PBO:0101430	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19723888	PBO:0095096	(Fig. 2A III)
PMID:19723888	PBO:0093580	(Fig. 1C)
PMID:19723888	PBO:0093581	(Fig. 1C)
PMID:19723888	PBO:0093580	(Fig. 1C,D)
PMID:19723888	PBO:0093629	(Fig. 1A)
PMID:19723888	PBO:0097774	(Fig. 2)
PMID:19723888	PBO:0097774	(Fig. 2)
PMID:19723888	FYPO:0001903	(Figure 2B)
PMID:19723888	FYPO:0001903	(Fig. 2A III)
PMID:19723888	FYPO:0001903	(Fig. 2A III)
PMID:19723888	FYPO:0000650	(Fig. 2A III)
PMID:19723888	PBO:0093581	(Fig. 1C)
PMID:19723888	PBO:0093629	(Figure 1B)
PMID:19723888	PBO:0093580	(Fig. 1C)
PMID:19723888	PBO:0093581	(Fig. 1C)
PMID:19723888	PBO:0097773	(Fig. 1C)
PMID:19723888	PBO:0097773	(Fig. 1C)
PMID:19723888	PBO:0097772	(Fig. 1D)
PMID:19723888	PBO:0093630	(Figure 1B)
PMID:19723888	PBO:0093630	(Fig. 1A)
PMID:19723888	PBO:0093581	(Fig. 1D)
PMID:19723888	PBO:0093581	(Fig. 1C)
PMID:19723888	PBO:0093580	(Fig. 1C)
PMID:19723888	PBO:0093630	(Fig. 1A)
PMID:19723888	PBO:0093630	(Fig. 1A)
PMID:19723888	PBO:0093630	(Fig. 1A)
PMID:19723888	PBO:0093630	(Fig. 1A)
PMID:19723888	PBO:0093629	(Fig. 1A)
PMID:19723888	PBO:0093629	(Fig. 1A)
PMID:19723888	PBO:0093629	(Fig. 1A)
PMID:19723888	PBO:0093629	(Fig. 1A)
PMID:19723888	PBO:0093629	(Fig. 1A)
PMID:19723888	PBO:0093629	(Fig. 1A)
PMID:19723888	PBO:0093630	(Fig. 1A)
PMID:19723888	PBO:0093629	(Figure 1B)
PMID:19723888	PBO:0093629	(Figure 1B)
PMID:19723888	PBO:0097772	(Fig. 1D)
PMID:19723888	PBO:0093629	(Figure 1B)
PMID:19723888	PBO:0093629	(Figure 1B)
PMID:19723888	PBO:0093629	(Figure 1B)
PMID:19723888	PBO:0093631	(Figure 1B)
PMID:19723888	PBO:0093631	(Figure 1B)
PMID:19736319	PBO:0113925	(comment: CHECK 2%) fig 6a. (comment: to dauughter)
PMID:19736319	FYPO:0002000	(comment: CHECL add to def, septated in interphase. one compartment is anucleate)
PMID:19736319	FYPO:0005369	(Fig. S1B)
PMID:19736319	FYPO:0001493	(Fig. S1C)
PMID:19736319	FYPO:0005055	(comment: arrested normal size (multiple rounds of cytokinesis) in interphase)
PMID:19736319	PBO:0018345	(Fig. 4B)
PMID:19736319	PBO:0108321	(Fig. 4D)
PMID:19736319	PBO:0021746	(Fig. 4B)
PMID:19736319	PBO:0108322	(comment: CHECK 2%) fig 6a
PMID:19758558	PBO:0103657	(Fig. S3D)
PMID:19798055	FYPO:0005452	(comment: decreased overall)
PMID:19804755	MOD:01455	(comment: residues include one or more of S77, T78, T79, S87, and T89, and others)
PMID:19804755	PBO:0100522	(comment: ctp-Phosphorylated)
PMID:19879140	GO:0008017	(comment: Biochemistry)
PMID:19879140	FYPO:0001944	(comment: MT spindown assay)
PMID:19879140	FYPO:0006725	(comment: MT spindown assay.)
PMID:19915592	GO:0000812	(Figure 2b)
PMID:19915592	FYPO:0002061	(comment: CHECK lethal >34°C) (Fig. 1c).
PMID:19915592	PBO:0110297	reduction in Pht1Ac (Fig. 1d), indicating that Pht1 acetylation is Mst1-dependent.
PMID:19915592	GO:0000785	Cell fractionation showed that Pht1Ac is chromatin-associated, though acetylation is not required for entry to this cellular compartment (Figs. 1e-f)
PMID:19915592	GO:0000812	(Figure 2b)
PMID:19915592	GO:0000812	(Figure 2b)
PMID:19915592	GO:0000812	(Figure 2b)
PMID:19915592	GO:0000812	(Figure 2b)
PMID:19915592	GO:0000812	(Figure 2b)
PMID:19915592	GO:0000812	(Figure 2b)
PMID:19915592	GO:0000812	(Figure 2b)
PMID:19915592	GO:0000812	(Figure 2b)
PMID:19915592	GO:0000812	(Figure 2b)
PMID:19915592	GO:0000812	(Figure 2b)
PMID:19915592	GO:0000812	(Figure 2b)
PMID:19915592	GO:0000812	(Figure 2b)
PMID:19915592	GO:0000812	(Figure 2b)
PMID:19915592	GO:0000812	(Figure 2b)
PMID:19915592	PBO:0092504	p SWR-C required for the efficient acetylation of the histone (Fig. 2b), most likely because of inefficient assembly of the variant into chromatin in each background (Fig. 2c). Thus a pathway first identified in Sc also operates in Sp: SWR-C inserts Pht1 into chromatin, where it is acetylated by Mst1.
PMID:19915592	FYPO:0000227	Knockout or depletion of H2A.Z in Sc 15 or mammalian cells 5 leads to increased rates of chromosome loss. This phenotype was also observed if any component of the Sp Pht1Ac pathway is disrupted, including mutants in swr1 (and msc1), pht1 (pht1Δ, −4KR or −4KQ), or mst1 (Supplementary Table 2 and 16,25,26).
PMID:19915592	FYPO:0000227	Knockout or depletion of H2A.Z in Sc 15 or mammalian cells 5 leads to increased rates of chromosome loss. This phenotype was also observed if any component of the Sp Pht1Ac pathway is disrupted, including mutants in swr1 (and msc1), pht1 (pht1Δ, −4KR or −4KQ), or mst1 (Supplementary Table 2 and 16,25,26).
PMID:19915592	FYPO:0000227	Knockout or depletion of H2A.Z in Sc 15 or mammalian cells 5 leads to increased rates of chromosome loss. This phenotype was also observed if any component of the Sp Pht1Ac pathway is disrupted, including mutants in swr1 (and msc1), pht1 (pht1Δ, −4KR or −4KQ), or mst1 (Supplementary Table 2 and 16,25,26).
PMID:19915592	FYPO:0000227	Knockout or depletion of H2A.Z in Sc 15 or mammalian cells 5 leads to increased rates of chromosome loss. This phenotype was also observed if any component of the Sp Pht1Ac pathway is disrupted, including mutants in swr1 (and msc1), pht1 (pht1Δ, −4KR or −4KQ), or mst1 (Supplementary Table 2 and 16,25,26).
PMID:19915592	FYPO:0000227	Knockout or depletion of H2A.Z in Sc 15 or mammalian cells 5 leads to increased rates of chromosome loss. This phenotype was also observed if any component of the Sp Pht1Ac pathway is disrupted, including mutants in swr1 (and msc1), pht1 (pht1Δ, −4KR or −4KQ), or mst1 (Supplementary Table 2 and 16,25,26).
PMID:19915592	FYPO:0000227	Knockout or depletion of H2A.Z in Sc 15 or mammalian cells 5 leads to increased rates of chromosome loss. This phenotype was also observed if any component of the Sp Pht1Ac pathway is disrupted, including mutants in swr1 (and msc1), pht1 (pht1Δ, −4KR or −4KQ), or mst1 (Supplementary Table 2 and 16,25,26).
PMID:19915592	FYPO:0000227	Knockout or depletion of H2A.Z in Sc 15 or mammalian cells 5 leads to increased rates of chromosome loss. This phenotype was also observed if any component of the Sp Pht1Ac pathway is disrupted, including mutants in swr1 (and msc1), pht1 (pht1Δ, −4KR or −4KQ), or mst1 (Supplementary Table 2 and 16,25,26).
PMID:19915592	FYPO:0000283	(iii) entanglement leading to breakage, where broken pieces of chromatin with no kinetochore lag on the spindle (Fig. 4b).
PMID:19915592	FYPO:0006372	(iii) entanglement leading to breakage, where broken pieces of chromatin with no kinetochore lag on the spindle (Fig. 4b).
PMID:19915592	FYPO:0001355	This partial rescue was specific, as pht1Δ was synthetic with rad21-K1, a mutant in the condensin-related complex cohesin, which holds sister-chromatids together prior to anaphase onset.
PMID:19915592	FYPO:0001355	This partial rescue was specific, as pht1Δ was synthetic with rad21-K1, a mutant in the condensin-related complex cohesin, which holds sister-chromatids together prior to anaphase onset.
PMID:19933844	GO:0045815	Deletion of this Iec1 protein or the Ino80 complex subunit arp8, ies6, or ies2 causes defects in DNA damage repair, the response to replication stress, and nucleotide metabolism.
PMID:19933844	GO:0045815	Deletion of this Iec1 protein or the Ino80 complex subunit arp8, ies6, or ies2 causes defects in DNA damage repair, the response to replication stress, and nucleotide metabolism.
PMID:19933844	GO:0045815	Deletion of this Iec1 protein or the Ino80 complex subunit arp8, ies6, or ies2 causes defects in DNA damage repair, the response to replication stress, and nucleotide metabolism.
PMID:19933844	GO:0045815	Deletion of this Iec1 protein or the Ino80 complex subunit arp8, ies6, or ies2 causes defects in DNA damage repair, the response to replication stress, and nucleotide metabolism.
PMID:19933844	GO:0140861	Deletion of this Iec1 protein or the Ino80 complex subunit arp8, ies6, or ies2 causes defects in DNA damage repair, the response to replication stress, and nucleotide metabolism.
PMID:19933844	GO:0140861	Deletion of this Iec1 protein or the Ino80 complex subunit arp8, ies6, or ies2 causes defects in DNA damage repair, the response to replication stress, and nucleotide metabolism.
PMID:19933844	GO:0140861	Deletion of this Iec1 protein or the Ino80 complex subunit arp8, ies6, or ies2 causes defects in DNA damage repair, the response to replication stress, and nucleotide metabolism.
PMID:19933844	GO:0140861	Deletion of this Iec1 protein or the Ino80 complex subunit arp8, ies6, or ies2 causes defects in DNA damage repair, the response to replication stress, and nucleotide metabolism.
PMID:19942659	GO:0003978	(comment: major)
PMID:19942659	FYPO:0003728	Like the gms1D mutant, neither the uge1D strain nor the uge1Dgal10D strain reacted with PNA (Fig. 2b
PMID:19942659	PBO:0108463	(comment: minor
PMID:19942852	FYPO:0000274	(Fig. 1D)
PMID:19942852	PBO:0019218	(Fig. 1)
PMID:19942852	PBO:0102705	(Fig. 6a)
PMID:19942852	PBO:0102706	(Fig. 6a)
PMID:19942852	FYPO:0006593	(Fig. 1D)
PMID:19942852	FYPO:0005380	(Fig. 1D)
PMID:19942852	FYPO:0005380	(Fig. 1D)
PMID:19942852	FYPO:0002061	(Fig. 1)
PMID:19942852	PBO:0019218	(Fig. 1)
PMID:19942852	PBO:0102700	(Fig. 3)
PMID:19942852	PBO:0102701	(Fig. 3)
PMID:19942852	PBO:0102702	(Fig. 3)
PMID:19942852	FYPO:0002061	(Fig. 1)
PMID:19942852	PBO:0102698	(Fig. S2, 3)
PMID:19942852	PBO:0102698	(Fig. S2, 3)
PMID:19942852	PBO:0102699	(Fig. 1D)
PMID:19942852	PBO:0102699	(Fig. 1D)
PMID:19942852	FYPO:0000274	(Fig. 1D)
PMID:19942852	FYPO:0006593	(Fig. 1D)
PMID:19948483	FYPO:0008007	(Fig. 3)
PMID:19948483	FYPO:0002061	(Fig. 3)
PMID:19948483	PBO:0101996	(Fig. 3)
PMID:19948483	FYPO:0005045	(Fig. 3)
PMID:19948484	PBO:0095336	(comment: they say periphery in the text but it has TM domains)
PMID:19948484	PBO:0095335	(comment: they say periphery in the text but it has TM domains)
PMID:19965387	FYPO:0006423	(Fig. S3)
PMID:19965387	FYPO:0006423	(Fig. S3)
PMID:19965387	FYPO:0006423	(Fig. S3)
PMID:19965387	PBO:0102062	(Fig. S5)
PMID:19965387	PBO:0102061	(Fig. 3A)
PMID:19965387	PBO:0102060	(Fig. 3A)
PMID:19965387	PBO:0102062	(Fig. 3A)
PMID:19965387	PBO:0102061	(Fig. 3A)
PMID:19965387	PBO:0102060	(Fig. 3A)
PMID:19965387	PBO:0102059	(Fig. 3A)
PMID:19965387	PBO:0102059	(Fig. 3A)
PMID:19965387	PBO:0102073	fusion experiments (Figure 3)
PMID:19965387	PBO:0112750	(comment: CHECK H2A-S121) phosphorylation was completely abolished in bub1-KD cells, although a similar amount of H2A was detected (Fig. 1G).
PMID:19965387	PBO:0102074	fusion experiments (Figure 3)
PMID:19965387	PBO:0102073	fusion experiments (Figure 3)
PMID:19965387	PBO:0102074	fusion experiments (Figure 3)
PMID:19965387	PBO:0102072	(Fig. 4G)
PMID:19965387	PBO:0112748	This signal was abolished in cell extracts prepared from h2a-SA cells, in which Ser 121 is replaced with alanine (H2A-S121A) in both the hta1+ and hta2+ genes (Fig. 1G).
PMID:19965387	PBO:0112749	This signal was abolished in cell extracts prepared from h2a-SA cells, in which Ser 121 is replaced with alanine (H2A-S121A) in both the hta1+ and hta2+ genes (Fig. 1G).
PMID:19965387	FYPO:0004318	(Fig. 2C)
PMID:19965387	PBO:0102059	(Fig. 3A)
PMID:19965387	FYPO:0004318	(Fig. 2C)
PMID:19965387	FYPO:0004318	(Fig. 2C)
PMID:19965387	FYPO:0004318	(Fig. 2C)
PMID:19965387	FYPO:0005634	(Fig. 2E)
PMID:19965387	PBO:0102059	(Fig. 3A)
PMID:19965387	PBO:0102071	(Fig. 4G)
PMID:19965387	FYPO:0005634	(Fig. 2E)
PMID:19965387	FYPO:0005634	(Fig. 2E)
PMID:19965387	FYPO:0005634	(Fig. 2E)
PMID:19965387	PBO:0102072	(Fig. 4G)
PMID:19965387	PBO:0102072	(Fig. 4G)
PMID:19965387	FYPO:0003182	(Fig. 2F)
PMID:19965387	FYPO:0003182	(Fig. 2F)
PMID:19965387	FYPO:0003182	(Fig. 2F)
PMID:19965387	FYPO:0003182	(Fig. 2F)
PMID:19965387	PBO:0102059	(Fig. 3A)
PMID:19965387	PBO:0102070	(Fig. 4c)
PMID:19965387	PBO:0101329	(Fig. 4c)
PMID:19965387	PBO:0102065	(Fig. S6)
PMID:19965387	PBO:0102064	(Fig. S6)
PMID:19965387	PBO:0102064	(Fig. S6)
PMID:19965387	PBO:0102065	(Fig. S6)
PMID:19965387	PBO:0102064	(Fig. S6)
PMID:19965387	PBO:0102065	(Fig. S6)
PMID:19965387	PBO:0102064	(Fig. S6)
PMID:19965387	PBO:0102063	(Fig. 3A)
PMID:19965387	PBO:0102063	(Fig. S3)
PMID:19965387	PBO:0102063	(Fig. S3)
PMID:19965387	FYPO:0006423	(Fig. S3)
PMID:20062003	FYPO:0007010	(Fig. 3)
PMID:20062003	FYPO:0007009	(Fig. 4)
PMID:20062003	FYPO:0007009	(Fig. S1)
PMID:20062003	FYPO:0007009	(Fig. 4)
PMID:20062003	FYPO:0007009	(Fig. 4)
PMID:20062003	FYPO:0007009	(Fig. 4)
PMID:20062003	FYPO:0007009	(Fig. S1)
PMID:20062003	FYPO:0007009	(Fig. 4)
PMID:20062003	FYPO:0006076	(Fig. 2D)
PMID:20062003	FYPO:0007009	(Fig. 4)
PMID:20062003	FYPO:0007009	(Fig. S1)
PMID:20075862	FYPO:0001408	(Figure 3a left panel)
PMID:20089861	FYPO:0008054	Indeed, the R288K and Q364R mutations in SpHCS confer diminished sensitivity to feedback inhibition by L-lysine in vitro and in vivo (Table 2 and Fig. 4)
PMID:20089861	FYPO:0008054	Indeed, the R288K and Q364R mutations in SpHCS confer diminished sensitivity to feedback inhibition by L-lysine in vitro and in vivo (Table 2 and Fig. 4)
PMID:20094029	GO:0005634	(comment: Forms gamma H2A dependent nuclear foci when over-expressed)
PMID:20110347	PBO:0104411	(comment: CONDITION 32 degrees)
PMID:20110347	FYPO:0001357	(comment: CONDITION 25 degrees)
PMID:20110347	FYPO:0003339	(comment: CONDITION 25 degrees)
PMID:20110347	FYPO:0001355	(comment: CONDITION 32 degrees)
PMID:20110347	FYPO:0004430	(comment: CONDITION 25 degrees)
PMID:20110347	PBO:0101716	(comment: CONDITION 32 degrees; semi-permissive for cdc8-27 alone)
PMID:20110347	FYPO:0001355	(comment: CONDITION 25 or 32 degrees; latter semi-permissive for cdc8-27 alone)
PMID:20110347	FYPO:0004895	(comment: CONDITION 32 degrees)
PMID:20110347	FYPO:0004895	(comment: CONDITION 25 degrees)
PMID:20123974	FYPO:0000487	(comment: increased unequal sister chromatid recombination)
PMID:20123974	FYPO:0000487	(comment: increased unequal sister chromatid recombination)
PMID:20123974	FYPO:0000487	(comment: increased unequal sister chromatid recombination)
PMID:20123974	FYPO:0000485	also ctp1,rec12,rad22,rti1,rad51,dmc1 (comment: increased unequal sister chromatid recombination)
PMID:20129053	FYPO:0003701	snoRNAs with extended poly(A) tails accumulate in these foci
PMID:20129053	FYPO:0003701	snoRNAs with extended poly(A) tails accumulate in these foci
PMID:20130084	PBO:0114328	A 6XHis-tagged version of SpYpt2 was purified from E. coli, and the ability of SpSpo13 to stimulate GDP release was examined (Figure 8A). Similar to what was observed with ScSec4 as a substrate (Figure 4B), SpSpo13 stimulated GDP release, although not as efficiently as Sc- Sec2. Thus, SpSpo13 can act on SpYpt2.
PMID:20130084	PBO:0114326	The localization of SpSpo13F79A-mRFP was indistinguishable from the wild-type protein (Figure 6C), indicating that the mutant protein is expressed and properly localized.
PMID:20130084	PBO:0114327	. Growing FSMs were observed adjacent to each of the SPBs in 100% of the cells expressing wild-type Spspo13+ (n = 20), but no FSMs were formed in cells expressing Spspo13-F79A (Figure 7) (n = 20). The GEF activity of SpSpo13 is therefore required for FSM assembly in S. pombe.
PMID:20130084	PBO:0035494	Spo13-mRFP was visible at the SPB, beginning with cells in meiosis I and persisted at the SPB throughout meiosis II, as reported previously (Nakase et al., 2008; Figure 6B).
PMID:20130084	GO:0003924	A 6XHis-tagged version of SpYpt2 was purified from E. coli, and the ability of SpSpo13 to stimulate GDP release was examined (Figure 8A). Similar to what was observed with ScSec4 as a substrate (Figure 4B), SpSpo13 stimulated GDP release, although not as efficiently as Sc- Sec2. Thus, SpSpo13 can act on SpYpt2.
PMID:20130084	PBO:0114648	The pull-down assay revealed that GST- SpSpo13F79A still bound to the nucleotide-free form of ScSec4 but at a lower level than wild-type GST-SpSpo13 (Figure 5A). In the GEF assay, adding GST-SpSpo13F79A did not stimulate mant-GDP dissociation, indicating that the mutant protein has lost GEF activity in vitro (Figure 5B).
PMID:20130084	PBO:0035493	Spo13-mRFP was visible at the SPB, beginning with cells in meiosis I and persisted at the SPB throughout meiosis II, as reported previously (Nakase et al., 2008; Figure 6B).
PMID:20140190	PBO:0101083	(comment: CHECK full-length Rad3 or Rad3-kd-delta)
PMID:20140190	PBO:0106748	(comment: full-length Rad3 or Rad3-kd-delta)
PMID:20140190	PBO:0106743	(comment: same as nbs1-c60-delta alone)
PMID:20140190	PBO:0106743	(comment: same as nbs1-c60-delta alone)
PMID:20164182	PBO:0106771	(comment: unstressed cells)
PMID:20164182	PBO:0095167	(comment: unstressed cells)
PMID:20164182	PBO:0108243	(comment: unstressed cells)
PMID:20164182	PBO:0108243	(comment: unstressed cells)
PMID:20164182	PBO:0108243	(comment: unstressed cells)
PMID:20164182	PBO:0095167	(comment: unstressed cells)
PMID:20164182	PBO:0095167	(comment: unstressed cells)
PMID:20164182	PBO:0095167	(comment: unstressed cells)
PMID:20164182	PBO:0108243	(comment: unstressed cells)
PMID:20164182	PBO:0095167	(comment: unstressed cells)
PMID:20164182	PBO:0108243	(comment: unstressed cells)
PMID:20164182	PBO:0095167	(comment: unstressed cells)
PMID:20164182	PBO:0106771	(comment: unstressed cells)
PMID:20164182	PBO:0106771	(comment: unstressed cells)
PMID:20164182	PBO:0095167	(comment: unstressed cells)
PMID:20164182	PBO:0108243	(comment: unstressed cells)
PMID:20164182	PBO:0095167	(comment: unstressed cells)
PMID:20164182	PBO:0095167	(comment: unstressed cells)
PMID:20178743	GO:1990817	Cid12 had robust adenylation activity when assembled into the RDRC complex, containing either wild-type Rdp1 or catalytically inactive Rdp1D903A (Figure 2G, lanes 1, 3, and 4), suggesting that Cid12 activity was allosterically regulated.
PMID:20178743	PBO:0098772	(Fig. 5 and Fig. S5)
PMID:20178743	PBO:0098772	(Fig. 5E)
PMID:20178743	PBO:0098773	(Fig. 5 and Fig. S5)
PMID:20178743	PBO:0114959	(Fig. 3B)
PMID:20178743	PBO:0114959	(Fig. 3A and B)
PMID:20178743	PBO:0098773	(Fig. 5D)
PMID:20178743	PBO:0105941	(Fig. 3A and B)
PMID:20178743	PBO:0105941	(Fig. 3A and B)
PMID:20178743	PBO:0094691	(Fig. S2D)
PMID:20178743	PBO:0094691	(Fig. S2D)
PMID:20178743	FYPO:0002837	(Fig. 2C)
PMID:20178743	PBO:0094283	(Fig. 4I)
PMID:20178743	FYPO:0002837	(Fig. 2C)
PMID:20178743	FYPO:0002835	(Fig. 2A and B)
PMID:20178743	PBO:0098773	(Fig. 5 and Fig. S5)
PMID:20178743	GO:1990431	we provide evidence that siRNAs undergo processing at their 3'ends, which involves the addition of untemplated nucleotides by the Cid12 and Cid14 nucleotidyltransferases
PMID:20178743	GO:1990431	we provide evidence that siRNAs undergo processing at their 3'ends, which involves the addition of untemplated nucleotides by the Cid12 and Cid14 nucleotidyltransferases
PMID:20178743	PBO:0098760	(Fig. 5G and Fig. S5B)
PMID:20178743	PBO:0098760	(Fig. 5G and Fig. S5B)
PMID:20178743	FYPO:0002835	(Fig. 2A and B)
PMID:20178743	FYPO:0006076	(Fig. 1B and C)
PMID:20178743	FYPO:0006076	(Fig. 1B and C)
PMID:20178743	FYPO:0006076	(Fig. 1B and C)
PMID:20178743	FYPO:0006076	(Fig. 1B and C)
PMID:20178743	PBO:0105543	(Fig. 1B and C)
PMID:20178743	PBO:0105543	(Fig. 1B and C)
PMID:20178743	PBO:0105543	(Fig. 1B and C)
PMID:20178743	PBO:0105543	(Fig. 1B and C)
PMID:20178743	PBO:0105543	(Fig. 1B and C)
PMID:20178743	PBO:0105543	(Fig. 1B and C)
PMID:20178743	PBO:0114957	(Fig. 1B and C)
PMID:20178743	PBO:0114958	(Fig. 1B and C)
PMID:20178743	PBO:0105941	(Fig. 2A and B)
PMID:20178743	PBO:0098772	(Fig. 5C and E)
PMID:20178743	FYPO:0003093	(Fig. 6B, D and E)
PMID:20178743	PBO:0098772	(Fig. 5E)
PMID:20178743	PBO:0098772	(Fig. 5C and E)
PMID:20178743	PBO:0098760	(Fig. 5C and E)
PMID:20178743	PBO:0098773	(Fig. 5C and E)
PMID:20178743	FYPO:0004201	(Fig. 3C)
PMID:20178743	PBO:0114959	(Fig. 3B)
PMID:20178743	PBO:0098760	(Fig. 5E)
PMID:20178743	PBO:0098760	(Fig. 5E)
PMID:20178743	PBO:0094283	(Fig. 4I)
PMID:20211136	PBO:0112179	(comment: not sure which clrc subunit it binds to?)
PMID:20211136	FYPO:0004170	(comment: abolished at exogenous RNA polII transcribed gene)
PMID:20211136	PBO:0098760	(comment: this is the endogenous dg repeat)
PMID:20211136	FYPO:0003412	(comment: endogenous ade6)
PMID:20226666	FYPO:0007664	(Figure 1) (comment: CHECK in interphase)
PMID:20226666	PBO:0102628	(Figure 1)
PMID:20226666	PBO:0102629	(Figure 1)
PMID:20226666	FYPO:0000229	(Figure 1) (comment: CHECK in interphase)
PMID:20230746	PBO:0108901	(comment: involved in negative regulation of transcription via transcription factor catabolism)
PMID:20299449	FYPO:0002837	(Fig. 1E)
PMID:20299449	PBO:0104709	(Fig. 1C)
PMID:20299449	PBO:0113963	(Fig. 1F)
PMID:20299449	PBO:0113969	(Fig. 4D)
PMID:20299449	PBO:0120513	(Fig. 4F)
PMID:20299449	PBO:0120512	(Fig. 4E)
PMID:20299449	PBO:0120511	(Fig. 4C)
PMID:20299449	PBO:0113965	(Fig. 4B)
PMID:20299449	FYPO:0003235	(Fig. 4A)
PMID:20299449	GO:0141222	Taken together, these results show that H3K4ac exists in S. pombe, and that Mst1 and the sirtuin Sir2 are the major HAT and HDAC, respectively, for H3K4.
PMID:20299449	FYPO:0002835	(Fig. 1E)
PMID:20299449	FYPO:0002837	(Fig. 1E)
PMID:20299449	PBO:0113963	(Fig. 1F)
PMID:20299449	PBO:0094283	(Fig. 1B,C)
PMID:20299449	PBO:0113963	(Fig. 1F)
PMID:20299449	PBO:0113964	(Fig. 1F)
PMID:20299449	FYPO:0002837	(Fig. 1E)
PMID:20299449	FYPO:0004238	(Fig. 2A)
PMID:20299449	PBO:0104710	(Fig. 1B and C)
PMID:20299449	PBO:0104710	(Fig. 1B and C)
PMID:20299449	FYPO:0008270	(Fig. 2A)
PMID:20299449	FYPO:0000892	(Fig. 2A)
PMID:20299449	FYPO:0004239	(Fig. 2B)
PMID:20299449	FYPO:0004240	(Fig. 2A)
PMID:20299449	FYPO:0001442	(Fig. 2A)
PMID:20299449	GO:0044016	Taken together, these results show that H3K4ac exists in S. pombe, and that Mst1 and the sirtuin Sir2 are the major HAT and HDAC, respectively, for H3K4. Fig. 2
PMID:20299449	PBO:0096407	(comment: IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT)
PMID:20299449	PBO:0020274	(comment: IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT)
PMID:20299449	MOD:00723	(comment: IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT)
PMID:20299449	PBO:0020274	(comment: IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT)
PMID:20356456	GO:0008379	The peroxidase activity of BCP (bacterioferritin comigratory protein) was similar to that of TPx.
PMID:20360683	FYPO:0003947	(comment: assayed using ypt3 reporter with or without premature stop codons)
PMID:20360683	FYPO:0003917	(comment: assayed using GFP reporter with or without premature stop codons)
PMID:20360683	FYPO:0003917	(comment: assayed using GFP reporter with or without premature stop codons)
PMID:20360683	FYPO:0003947	(comment: assayed using ypt3 reporter with or without premature stop codons)
PMID:2038306	PBO:0024451	(comment: pMNScdc2-DL5 is integrated Cells observed after 12 hours over expression) Figure 2. (comment: In the paper they call this plasmid pMNSDL5 I have added cdc2-DL5 for clarity) (comment: The pMNS21L plasmid used for isolating this cdc2 mutant has since been rename pREP1.)
PMID:2038306	PBO:0096052	(comment: co ip of cdc2-DL5 and endogenous CDC2HS with anti cdc13 SP4 shows reduced kinase activity compared to CDC2HS alone Figure 7. cdc2-DL5 is on episomal pMNS cdc2DL5. The authors argue that inactive cdc2-DL5 may titrate away factors required for cdc2 kinase activity but unless I have misunderstood the experiment I think this could just as well be interpreted as SP4 iping a mixture of active and inactive cdc2 kinase activity and thus less total cdc2 kinase activity)
PMID:2038306	PBO:0102101	(comment: cdc2-DL5 is expressed from episomal pMNScdc2DL5) (comment: CDC2HS is not recognised by anti cdc2 antibody 4711 and so does not contribute to the level of cdc2-DL5 kinase activity Figure 4A)
PMID:2038306	PBO:0102101	(comment: cdc2-DL5 is over expressed from episomal pMNScdc2DL5) (comment: CDC2HS is not recognised by anti cdc2 antibody 4711 and so does not contribute to the level of cdc2-DL5 kinase activity assayed.) (Figure 4A)
PMID:2038306	PBO:0102100	(comment: CDC2HS is not recognised by anti cdc2 antibody 4711 and so does not contribute to the level of kinase activity assayed.) (comment: S. pombe cdc2+ is on a multi copy plasmid pMNScdc2 Figure 4A lane 1)
PMID:2038306	PBO:0093712	(comment: CHECK CDC2HS complements cdc2delete phenotype) Figure 4B)
PMID:2038306	PBO:0037130	(comment: CHECK the endogenous copy of cdc2 has been replaced by cdc2 from human cells CDC2HS) (comment: S. pombe cdc2+ is expressed from episomal pMNScdc2 in presence of thiamine. The cdc2 is therefore not really over expressed but I was unable to say it was 'not assayed) Figure 3C
PMID:2038306	PBO:0024451	(comment: cdc2-DL5 is over expressed from episomal pMNScdc2DL5. The endogenous cdc2+ has been replaced by the human cdc2 gene CDC2HS.) Same phenotype as shown in Figure 2
PMID:2038306	PBO:0093712	(comment: CHECK the endogenous copy of cdc2 has been replaced by cdc2 from human cells CDC2HS. S. pombe cdc2+ is on an episomal plasmid pMNScdc2 Figure 3D)
PMID:2038306	PBO:0037125	(comment: pMNScdc2-DL5 is an episomal plasmid.)
PMID:2038306	PBO:0037128	(comment: pMNScdc2-DL5 is integrated)
PMID:2038306	PBO:0037126	(comment: pMNScdc2-DL5 is integrated cells observed after 30 hours over expression) (Figure 2) (comment: In the paper they call this plasmid pMNSDL5 I have added cdc2-DL5 for clarity). (comment: The pMNS21L plasmid used for isolating this cdc2 mutant has since been rename pREP1.)
PMID:2038306	PBO:0024304	Data not shown. (comment: pMNScdc2-DL5 is integrated)
PMID:2038306	PBO:0037127	Data not shown. (comment: pMNScdc2-DL5 is integrated)
PMID:2038306	PBO:0037125	(comment: pMNScdc2-DL5 fails to rescue cdc2-33 mutant at the restrictive temperature. Do not say how this was assayed)
PMID:20383139	PBO:0101009	(Fig. 1e)
PMID:20383139	FYPO:0001355	(Fig. 1b)
PMID:20383139	FYPO:0001357	(Fig. 1b)
PMID:20383139	FYPO:0001357	(Fig. 1b)
PMID:20383139	FYPO:0001357	(Fig. 1b)
PMID:20383139	PBO:0101008	(Fig. 1d)
PMID:20383139	PBO:0101010	(Fig. 1e)
PMID:20383139	FYPO:0001513	(Fig. 1d)
PMID:20383139	PBO:0033208	(Fig. S1a)
PMID:20383139	PBO:0101013	(Fig. 2b)
PMID:20383139	PBO:0101014	(Fig. 2b)
PMID:20383139	PBO:0101015	(Fig. 2b)
PMID:20383139	PBO:0101016	(Fig. 2b)
PMID:20383139	PBO:0101017	(Fig. 3a)
PMID:20383139	PBO:0101017	(Fig. 3a)
PMID:20383139	PBO:0101018	(Fig. 3c)
PMID:20383139	PBO:0101019	(Fig. 3c)
PMID:20383139	PBO:0101021	(comment: CHECK separation)
PMID:20383139	PBO:0101023	(Fig. 4c)
PMID:20383139	PBO:0101024	(Fig. S5)
PMID:20383139	PBO:0101024	(Fig. S5)
PMID:20383139	PBO:0101025	(Fig. 5b)
PMID:20383139	PBO:0101025	(Fig. 5b)
PMID:20383139	PBO:0101026	(Fig. 5B)
PMID:20383139	PBO:0101027	(Fig. 5c)
PMID:20383139	PBO:0101025	(Fig. 5b)
PMID:20383139	PBO:0101028	(Fig. 5c)
PMID:20383139	PBO:0109329	(Fig. 3a) (comment: par1, the regulatory subunit was used in the assay)
PMID:20383139	PBO:0109330	(Fig. 3a)
PMID:20388730	GO:0005802	These results indicate that all three Imt-GFP fusion proteins primarily localize to the Golgi and trans-Golgi network, similar to S. cerevisiae Sur1p (Lisman et al., 2004).
PMID:20388730	FYPO:0000034	Interestingly, endocytosis of Aat1-GFP was severely impaired and Aat1-GFP remained at the plasma membrane after 5 hours of incubation (Fig. 8A). Thus, we conclude that the MIPC- deficient mutant is impaired in its ability to internalize plasma-membrane proteins to the vacuole.
PMID:20388730	FYPO:0005508	Interestingly, endocytosis of Aat1-GFP was severely impaired and Aat1-GFP remained at the plasma membrane after 5 hours of incubation (Fig. 8A). Thus, we conclude that the MIPC- deficient mutant is impaired in its ability to internalize plasma-membrane proteins to the vacuole.
PMID:20388730	GO:0005886	Expressed in wild-type S. pombe grown in rich medium, Aat1-GFP exhibited punctate fluorescence, suggesting that Aat1-GFP localized to the Golgi apparatus (Fig. 8A,B). When the cells were shifted to a nitrogen-free medium, Aat1-GFP was transported from the Golgi apparatus to the plasma membrane within 30 minutes, followed by endocytosis and transport to the vacuolar lumen.
PMID:20388730	FYPO:0000135	Whereas imt1imt2imt3 cells exhibited enhanced levels of fluorescence, sterols were detected throughout the plasma membrane (Fig. 7). These results suggest that aberrant localization or enrichment of sterols in the plasma membrane caused sensitivity to polyene antibiotics in MIPC-deficient cells.
PMID:20388730	FYPO:0004483	By contrast, imt1imt2imt3 cells had slightly smaller vacuoles compared with those of wild-type cells under normal conditions (Fig. 6)
PMID:20388730	FYPO:0002788	By contrast, imt1imt2imt3 cells had slightly smaller vacuoles compared with those of wild-type cells under normal conditions (Fig. 6)
PMID:20388730	FYPO:0000076	imt1imt2imt3 cells were also found to be sensitive to 3 g/ml nystatin and to 0.5 g/ml amphotericin B (Fig. 5).
PMID:20388730	FYPO:0002642	imt1imt2imt3 cells were also found to be sensitive to 3 g/ml nystatin and to 0.5 g/ml amphotericin B (Fig. 5).
PMID:20388730	FYPO:0000098	Sensitivity to Ca2+ was determined by a visual spot assay on YES medium (Fig. 5). Single imt mutants did not exhibit obvious Ca2+ sensitivity, whereas the imt1imt2imt3 mutant did.
PMID:20388730	FYPO:0000024	"Single and double disruptants had a normal cell shape, but the imt1imt2imt3 disruptants were round or pear shaped under normal growth conditions (Fig. 4). (comment: note that these do not look particularly rounded or pear-shaped and fit our ""stubby"" morphology better)"
PMID:20388730	GO:0005802	These results indicate that all three Imt-GFP fusion proteins primarily localize to the Golgi and trans-Golgi network, similar to S. cerevisiae Sur1p (Lisman et al., 2004).
PMID:20388730	GO:0005802	These results indicate that all three Imt-GFP fusion proteins primarily localize to the Golgi and trans-Golgi network, similar to S. cerevisiae Sur1p (Lisman et al., 2004).
PMID:20388730	GO:0051999	Interestingly, a significant amount of IPC accumulated and MIPC decreased in sur2 cells. The scs7 mutation also caused a reduction in MIPC content. These results suggest that Imt proteins exhibit weak activity towards dihydroceramide-containing IPC, such that a reduction in MIPC was observed in sur2 and scs7 mutants.
PMID:20388730	GO:0051999	Interestingly, a significant amount of IPC accumulated and MIPC decreased in sur2 cells. The scs7 mutation also caused a reduction in MIPC content. These results suggest that Imt proteins exhibit weak activity towards dihydroceramide-containing IPC, such that a reduction in MIPC was observed in sur2 and scs7 mutants.
PMID:20388730	FYPO:0008261	Interestingly, a significant amount of IPC accumulated and MIPC decreased in sur2 cells. The scs7 mutation also caused a reduction in MIPC content. These results suggest that Imt proteins exhibit weak activity towards dihydroceramide-containing IPC, such that a reduction in MIPC was observed in sur2 and scs7 mutants.
PMID:20388730	FYPO:0008261	Interestingly, a significant amount of IPC accumulated and MIPC decreased in sur2 cells. The scs7 mutation also caused a reduction in MIPC content. These results suggest that Imt proteins exhibit weak activity towards dihydroceramide-containing IPC, such that a reduction in MIPC was observed in sur2 and scs7 mutants.
PMID:20388730	GO:0051999	MIPC was not detected, IPC had accumulated and one unidentified sphingolipid spot was observed (Fig. 2A). These results indicate that all three imt genes are required for MIPC synthesis and that MIPC was not produced in imt1imt2imt3 disruptant mutants.
PMID:20388730	GO:0051999	MIPC was not detected, IPC had accumulated and one unidentified sphingolipid spot was observed (Fig. 2A). These results indicate that all three imt genes are required for MIPC synthesis and that MIPC was not produced in imt1imt2imt3 disruptant mutants.
PMID:20388730	GO:0051999	MIPC was not detected, IPC had accumulated and one unidentified sphingolipid spot was observed (Fig. 2A). These results indicate that all three imt genes are required for MIPC synthesis and that MIPC was not produced in imt1imt2imt3 disruptant mutants.
PMID:20388730	FYPO:0008262	MIPC was not detected, IPC had accumulated and one unidentified sphingolipid spot was observed (Fig. 2A). These results indicate that all three imt genes are required for MIPCsynthesis and that MIPC was not produced in imt1imt2imt3 disruptant mutants.
PMID:20434336	PBO:0117370	(Figure S1C)
PMID:20434336	PBO:0117370	(Figure S1B)
PMID:20434336	PBO:0019716	(Fig. 1)
PMID:20434336	GO:0005635	(Fig. 1)
PMID:20434336	PBO:0100841	(Fig. 1)
PMID:20434336	PBO:0100840	(Fig. 1)
PMID:20434336	PBO:0019716	(Fig. 1)
PMID:20434336	PBO:0019716	(Fig. 1)
PMID:20434336	GO:0005635	(Fig. 1)
PMID:20434336	PBO:0100841	(Fig. 1)
PMID:20434336	PBO:0100840	(Fig. 1)
PMID:20434336	PBO:0100841	(Fig. 1)
PMID:20434336	GO:1990608	data not shown
PMID:20434336	PBO:0100840	(Fig. 1)
PMID:20434336	PBO:0100853	(Fig. 4E)
PMID:20434336	PBO:0095196	(Fig. 3C)
PMID:20434336	PBO:0100852	(Fig. 3C)
PMID:20434336	PBO:0100851	(Fig. 3C) (comment: protein distributed in cortex)
PMID:20434336	PBO:0098959	(Figure S3A)
PMID:20434336	PBO:0100850	(Fig. 3)
PMID:20434336	PBO:0100850	(Fig. 3)
PMID:20434336	PBO:0100849	(Fig. 3)
PMID:20434336	PBO:0100849	(Fig. 3)
PMID:20434336	PBO:0100848	(Fig. 3)
PMID:20434336	PBO:0100847	(Fig. 3)
PMID:20434336	PBO:0100846	(Fig. 2D) (comment: tubular/cortical)
PMID:20434336	PBO:0100845	(Figure 2A and 2B) (comment: cortical/tubular)
PMID:20434336	PBO:0100845	(Figure 2A and 2B) (comment: cortical/tubular)
PMID:20434336	PBO:0100845	(Figure 2A and 2B)
PMID:20434336	PBO:0100843	(Figure 2A and 2B)
PMID:20434336	PBO:0100844	(Figure 2A and 2B)
PMID:20434336	PBO:0100844	(Figure 2A and 2B)
PMID:20434336	PBO:0100843	(Figure 2A and 2B)
PMID:20434336	PBO:0099441	(Figure 2A and 2B)
PMID:20452294	FYPO:0005183	assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all
PMID:20452294	FYPO:0005221	(comment: PCNA trimerization)
PMID:20452294	FYPO:0005221	(comment: PCNA trimerization)
PMID:20452294	FYPO:0005183	assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all
PMID:20452294	FYPO:0005183	assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all
PMID:20452294	FYPO:0005183	assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all
PMID:20452294	FYPO:0005183	assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all
PMID:20452294	FYPO:0005183	assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all
PMID:20452294	FYPO:0005183	assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all
PMID:20452294	FYPO:0005183	assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all
PMID:20517925	FYPO:0004652	(Fig. 1B)
PMID:20517925	FYPO:0002022	(comment: CHECK formation)
PMID:20517925	FYPO:0006207	(Fig. 3D)
PMID:20517925	PBO:0099013	(Fig. 3D)
PMID:20517925	FYPO:0004964	(Fig. 1B)
PMID:20517925	FYPO:0001011	(Fig. S1)
PMID:20517925	FYPO:0005430	(Fig. 1B)
PMID:20517925	FYPO:0007151	(Fig. 1B) oreover, actin cables often significantly overgrew in these cells while the actin ring formation seemed to be unaffected.
PMID:20547592	FYPO:0005488	(Fig. 5e)
PMID:20547592	PBO:0037494	(Fig. 2e) suggesting that Vgl1 might escort RNA from ER-associated polyribosomes to the cytosol under thermal stress.
PMID:20547592	FYPO:0000158	(Fig. 1c)
PMID:20547592	PBO:0037737	(Fig. 1) (comment: nuclear)
PMID:20547592	PBO:0037736	(Fig. 1)
PMID:20547592	FYPO:0002060	(Fig. 1)
PMID:20547592	PBO:0037494	(Figure 6E)
PMID:20547592	PBO:0023812	(Figure 6a)
PMID:20547592	PBO:0037741	(Fig. 5b)
PMID:20547592	PBO:0102400	(Figure 7A)
PMID:20547592	FYPO:0002350	(Figure 7B)
PMID:20547592	FYPO:0001487	(Figure 8A and B) (comment: (fairly similar expression orofiles))
PMID:20547592	PBO:0037738	(Figure 5A)
PMID:20547592	FYPO:0001387	(Figure 4)
PMID:20547592	PBO:0021023	(Fig. 5a)
PMID:20547592	PBO:0023514	(Fig. 5b)
PMID:20547592	PBO:0037739	(Figure 5A)
PMID:20547592	FYPO:0002350	(Fig. 6D)
PMID:20547592	FYPO:0002350	(Fig. 6c)
PMID:20603077	PBO:0110173	Cdc12 pulls down only 27% as much Cdc15 in a similar block and release experiment (Supp. Fig. 1B)
PMID:20605454	PBO:0103376	(comment: CHECK at ste11)
PMID:20605454	PBO:0103375	(comment: CHECK at act1 & sam1)
PMID:20605454	PBO:0103375	(comment: CHECK at act1 & sam1)
PMID:20605454	PBO:0103369	(comment: polII CTD; probably S5 but can't rule out effect on S7)
PMID:20605454	PBO:0103369	(comment: pol II CTD; probably S2 but can't rule out effect on S7)
PMID:20605454	PBO:0103383	(comment: CHECK at ste11)
PMID:20605454	PBO:0103376	(comment: CHECK at ste11)
PMID:20605454	PBO:0103382	(comment: CHECK at ste11)
PMID:20622008	FYPO:0002353	(comment: at genes)
PMID:20622014	PBO:0103343	(comment: temperature restrictive for mmi1-ts3)
PMID:20622014	PBO:0103339	(comment: temperature restrictive for mmi1-ts3)
PMID:20622014	PBO:0103340	(comment: temperature restrictive for mmi1-ts3)
PMID:20622014	PBO:0103350	(comment: pol II localization to sme2 locus)
PMID:20622014	PBO:0103342	(comment: temperature restrictive for mmi1-ts3)
PMID:20622014	PBO:0103337	(comment: temperature restrictive for mmi1-ts3)
PMID:20623139	PBO:0093641	(comment: CHECK high expressivity)
PMID:20623139	PBO:0093645	(comment: CHECK low expressivity)
PMID:20624975	FYPO:0005423	(Fig. 5C)
PMID:20624975	FYPO:0005423	(Fig. S5B-E)
PMID:20624975	FYPO:0000904	(comment: depolymerization (cytoplasmic?))
PMID:2065367	PBO:0020025	(comment: incomplete penetrance due to translational frameshifting)
PMID:2065367	PBO:0020023	(comment: incomplete penetrance due to translational frameshifting)
PMID:2065367	FYPO:0000684	(comment: severity is variable, and segregates over successive generations (but not 2:2))
PMID:2065367	PBO:0020021	(comment: incomplete penetrance due to translational frameshifting)
PMID:2065367	PBO:0020022	(comment: incomplete penetrance due to translational frameshifting)
PMID:2065367	PBO:0020020	(comment: incomplete penetrance due to translational frameshifting)
PMID:2065367	PBO:0020024	(comment: incomplete penetrance due to translational frameshifting)
PMID:20661445	PBO:0096218	(comment: Phosphorylated at mating type locus during S-phase) (comment: Rad3 dependent)
PMID:20661445	PBO:0096208	(comment: Rad3 dependent)
PMID:20661445	PBO:0096208	(comment: Rad3 dependent)
PMID:20661445	PBO:0096209	(comment: Rad3 dependent)
PMID:20661445	PBO:0023773	(comment: Rad3 dependent)
PMID:20661445	PBO:0096209	(comment: Rad3 dependent)
PMID:20661445	PBO:0023773	(comment: Rad3 dependent)
PMID:20661445	PBO:0023774	(comment: Rad3 dependent)
PMID:20661445	PBO:0023775	(comment: Rad3 dependent)
PMID:20661445	PBO:0023774	(comment: Rad3 dependent)
PMID:20661445	PBO:0023775	(comment: Rad3 dependent)
PMID:20661445	PBO:0096210	(comment: Phosphorylated at Tf2-type retrotransposons and wtf elements during S-phase)| (comment: Rad3 dependent)
PMID:20661445	PBO:0033541	(comment: Phosphorylated at Tf2-type retrotransposons and wtf elements during S-phase)
PMID:20661445	PBO:0096218	(comment: Phosphorylated at mating type locus during S-phase), (comment: Rad3 dependent)
PMID:20661445	PBO:0096219	(comment: Phosphorylated at centromeres during S-phase) (comment: Rad3 dependent)
PMID:20661445	PBO:0023773	(comment: Phosphorylated at centromeres during S-phase) (comment: Rad3 dependent)
PMID:20661445	PBO:0096219	(comment: Phosphorylated at centromeres during S-phase) (comment: Rad3 dependent)
PMID:20661445	PBO:0023773	(comment: Phosphorylated at centromeres during S-phase) (comment: Rad3 dependent)
PMID:20661445	PBO:0096220	(comment: Phosphorylated at Tf2-type retrotransposons and wtf elements during S-phase)
PMID:20679485	PBO:0119906	Crb2 binds phosphorylated histone H2A (Hta1 Serine-129 and Hta2 Serine-128) through its C-terminal BRCT domains
PMID:20679485	PBO:0119906	Crb2 binds phosphorylated histone H2A (Hta1 Serine-129 and Hta2 Serine-128) through its C-terminal BRCT domains
PMID:20679485	PBO:0119907	Crb2 binds phosphorylated histone H2A (Hta1 Serine-129 and Hta2 Serine-128) through its C-terminal BRCT domains
PMID:20705466	PBO:0098637	(comment: temperature semi-permissive for cdc8-27)
PMID:20705466	PBO:0106972	(comment: temperature semi-permissive for cdc8-27)
PMID:20705466	PBO:0098637	(comment: temperature semi-permissive for cdc8-27)
PMID:20705466	PBO:0106975	(comment: temperature semi-permissive for cdc8-27)
PMID:20705471	PBO:0098637	(comment: temperature permissive for cdc8-27)
PMID:20736315	PBO:0102342	(Fig. 1B)
PMID:20736315	PBO:0102340	(Fig. 4)
PMID:20736315	PBO:0102341	(Fig. 1B)
PMID:20739936	PBO:0098654	Supplementary Fig. 8a)
PMID:20739936	PBO:0098639	(Fig. 1c)
PMID:20739936	PBO:0098640	(Fig. 1d, 1k)
PMID:20739936	PBO:0098641	(Fig. 1c)
PMID:20739936	FYPO:0001007	The cdc13-M7 mutant is suppressed by bir1-8D
PMID:20739936	PBO:0098642	(Fig. 1k)
PMID:20739936	PBO:0093562	(Fig. 1)
PMID:20739936	FYPO:0003503	(comment: CHECK figb)
PMID:20739936	FYPO:0003481	(Fig. 1b)
PMID:20739936	PBO:0098643	(Fig. S1) Nuclear staining of anaphase cells showed that the cdc13-M7 mutant, but not the conventional cdc13-117 mutant, often exhibited lagging chromosomes at anaphase (Fig. 1c).
PMID:20739936	PBO:0098644	(Fig. S1)
PMID:20739936	PBO:0111072	(Fig. 1e, Fig. 1f)
PMID:20739936	PBO:0098646	(Fig. 1e) also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	PBO:0098646	(Fig. 1e) also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	PBO:0098646	(Fig. 1e) also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	PBO:0098646	(Fig. 1e) also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	PBO:0098646	(Fig. 1e) also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	PBO:0098646	(Fig. 1e) also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	PBO:0098646	(Fig. 1e) also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	PBO:0098646	(Fig. 1e) also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	FYPO:0005366	(Fig. 1h)
PMID:20739936	FYPO:0005366	(Fig. 1i)
PMID:20739936	PBO:0093562	(Fig. 1j)
PMID:20739936	PBO:0096770	(Fig. 1j)
PMID:20739936	PBO:0098648	(Fig. 1, S4, S5)
PMID:20739936	PBO:0098649	(Fig. 2a, 2b, S5)
PMID:20739936	PBO:0098650	(Fig. 2a)
PMID:20739936	PBO:0098651	(Fig. 2a)
PMID:20739936	PBO:0111964	(Fig. S6)
PMID:20739936	PBO:0095380	(Fig. S6)
PMID:20739936	PBO:0096770	suppressed at comparable level to Bir1-CD, These results indicate that once they are tethered at centromeres, the functionality is indistinguishable between Bir1 and Bir1-8A. Supporting this conclusion, complex formation of the CPC was intact in bir1-8A cells (Supplementary Fig. 7).
PMID:20739936	PBO:0036900	Supplementary Fig. 8a)
PMID:20739936	PBO:0098653	Bir1-N-5A abolished the interaction with Sgo2, whereas Bir1-N-5D retained the interaction (Fig. 2h)
PMID:20739936	PBO:0098653	Bir1-N-5A abolished the interaction with Sgo2, whereas Bir1-N-5D retained the interaction (Fig. 2h)
PMID:20739936	PBO:0098649	(Fig. 2a, 2b, S5)
PMID:20739936	PBO:0098649	(Fig. 2a, 2b, S5)
PMID:20799962	PBO:0093561	(comment: same as rid2-1 alone)
PMID:20799962	PBO:0093560	(comment: same as rid1-1 alone)
PMID:20805322	PBO:0098360	(comment: assayed substrate MBP)
PMID:20805322	PBO:0098351	(comment: assayed substrate casein)
PMID:20805322	GO:0032956	(comment: CHECK negative reg of polarization/remodelling)
PMID:20805322	PBO:0098361	(comment: assayed substrate MBP)
PMID:20805322	PBO:0098352	(comment: assayed substrate MBP)
PMID:20805322	PBO:0098357	(Fig. 1A and Table I)
PMID:20805322	PBO:0098359	(comment: assayed substrate MBP)
PMID:20805322	PBO:0098359	(comment: assayed substrate MBP)
PMID:20805322	PBO:0098352	(comment: assayed substrate MBP)
PMID:20805322	PBO:0098352	(comment: assayed substrate MBP)
PMID:20807799	PBO:0106962	(comment: CHECK acetylated Cdc82 so could use PR:000037081)
PMID:20807799	PBO:0106964	"(comment: vw: I used ""added by naa20 which is the catalytic subunit for naa25"")"
PMID:20807799	PBO:0020501	(comment: CHECK GO:0051329= mitotic interphase)
PMID:20807799	PBO:0097713	(comment: CHECK PR:000037081= tropomyosin cdc8, acetylated form (fission yeast))
PMID:20826461	PBO:0033557	(Fig. 2A)
PMID:20826461	PBO:0100782	(Fig. 1F
PMID:20826461	PBO:0100787	(Fig. 2C)
PMID:20826461	PBO:0037653	(Fig. 1)
PMID:20826461	PBO:0035494	(Fig. 1)
PMID:20826461	GO:0043332	(Fig. 1C
PMID:20826461	PBO:0100782	(Fig. 1F
PMID:20826461	PBO:0100787	(Fig. 2C)
PMID:20826461	FYPO:0004953	(Fig. 4)
PMID:20826461	PBO:0100788	(Fig. 5)
PMID:20826461	PBO:0100789	(Fig. 5)
PMID:20826461	PBO:0100790	(Fig. 5)
PMID:20826461	PBO:0100791	(Fig. 6)
PMID:20826461	PBO:0100792	(Fig. 6)
PMID:20826461	PBO:0037648	(Fig. 6)
PMID:20826461	PBO:0113920	(Fig. 5)
PMID:20826461	PBO:0100794	(Fig. 6)
PMID:20826461	PBO:0100786	(Fig. 2C)
PMID:20826461	PBO:0100786	(Fig. 2C)
PMID:20826461	PBO:0100785	(Fig. 2B)
PMID:20826461	PBO:0100784	(Fig. 2A)
PMID:20826461	PBO:0100783	(Fig. 2A)
PMID:20826805	PBO:0018576	(comment: if it is there after cytokinesis + during anaphase B, then I guess it is safe to say that it is there during cytokinesis too..)
PMID:20826805	PBO:0021076	(comment: if it is there after cytokinesis + during anaphase B, then I guess it is safe to say that it is there during cytokinesis too..)
PMID:20826805	GO:2000100	(comment: seems to play a minor role - ppk11 physically interacts with pmo25. ppk11 deletion mutants have less pmo25 at the cell division site. This is not so important under optimal conditions but becomes important when cells are stressed. The phenotype of MOR mutants is excaberated by ppk11-delta.)
PMID:20826805	GO:2000100	(comment: seems to play a minor role - ppk11 physically interacts with pmo25. ppk11 deletion mutants have less pmo25 at the cell division site. This is not so important under optimal conditions but becomes important when cells are stressed. The phenotype of MOR mutants is excaberated by ppk11-delta.)
PMID:20826805	GO:0000920	(comment: seems to play a minor role - ppk11 physically interacts with pmo25. ppk11 deletion mutants have less pmo25 at the cell division site. This is not so important under optimal conditions but becomes important when cells are stressed. The phenotype of MOR mutants is excaberated by ppk11-delta.)
PMID:20829365	FYPO:0007098	(Figure 5)
PMID:20829365	FYPO:0001309	(Figure 1a)
PMID:20829365	FYPO:0001420	(Figure 1a)
PMID:20829365	FYPO:0001103	(Figure 2a)
PMID:20829365	PBO:0099780	(Figure 2a)
PMID:20829365	FYPO:0001168	(Figure 3)
PMID:20829365	PBO:0099781	(Figure 3)
PMID:20829365	PBO:0099782	(Figure 3)
PMID:20829365	FYPO:0001158	(Figure 3)
PMID:20829365	FYPO:0004874	(Figure 3)
PMID:20833892	PBO:0035495	(Fig. 3B) WT 10%
PMID:20854854	FYPO:0002637	(Fig. 1c)
PMID:20854854	FYPO:0001420	(Fig. 1b)
PMID:20854854	FYPO:0001234	(Fig. 1b)
PMID:20854854	FYPO:0000106	(Fig. 1c)
PMID:20854854	PBO:0019806	(Fig. 1a)
PMID:20854854	PBO:0103039	(Fig. 1a)
PMID:20854854	FYPO:0002061	(Fig. 1c)
PMID:20854854	FYPO:0002447	(Fig. 3)
PMID:20854854	PBO:0103040	(comment: I don't understand the chemistry well enough to know how the HPLC shows this but I think this is enough evidence?)
PMID:20854854	PBO:0038207	(Fig. 1a)
PMID:20854854	FYPO:0002447	(Fig. 3)
PMID:20876564	PBO:0093558	(Fig. 4A)
PMID:20876564	PBO:0093558	(Fig. 4A)
PMID:20876564	PBO:0093558	(Fig. 4A)
PMID:20876564	FYPO:0000674	(Fig. 4B)
PMID:20876564	PBO:0093558	(Fig. 4A)
PMID:20876564	PBO:0093558	(Fig. 4A)
PMID:20876564	PBO:0093558	(Fig. 4A)
PMID:20876564	PBO:0093558	(Fig. 4A)
PMID:20876564	PBO:0093558	(Fig. 4A)
PMID:20876564	PBO:0093558	(Fig. 4A)
PMID:20876564	FYPO:0000674	(Fig. 4A)
PMID:20876564	FYPO:0000674	(Fig. 4A)
PMID:20876564	FYPO:0000674	(Fig. 4A)
PMID:20876564	PBO:0093558	(Fig. 4A)
PMID:20876564	FYPO:0000674	(Fig. 4B)
PMID:20876564	PBO:0093558	(Fig. 4B)
PMID:20876564	PBO:0093558	(Fig. 4B)
PMID:20876564	PBO:0093558	(Fig. 4B)
PMID:20876564	PBO:0093558	(Fig. 4B)
PMID:20876564	PBO:0093559	(Fig. 4B)
PMID:20876564	PBO:0093559	(Fig. 4B)
PMID:20876564	PBO:0093559	(Fig. 4B)
PMID:20876564	PBO:0093559	(Fig. 4B)
PMID:20876564	PBO:0093559	(Fig. 4B)
PMID:20876564	PBO:0093558	(Fig. 4A)
PMID:20876564	FYPO:0001357	(Fig. 2A)
PMID:20876564	PBO:0093560	(Fig. 2A)
PMID:20876564	PBO:0093560	(Fig. 2A)
PMID:20876564	PBO:0093558	(Fig. 2A)
PMID:20876564	PBO:0093556	(Fig. 2A)
PMID:20876564	FYPO:0004481	(Fig. 2A)
PMID:20876564	FYPO:0002177	(Fig. 2B)
PMID:20876564	FYPO:0006117	(Fig. 2B)
PMID:20876564	FYPO:0003028	(Fig. 6D)
PMID:20876564	FYPO:0003028	(Fig. 6D)
PMID:20876564	FYPO:0002021	(Fig. 6D)
PMID:20876564	FYPO:0003028	(Fig. 6C)
PMID:20876564	FYPO:0003028	(Fig. 6C)
PMID:20876564	PBO:0093560	(Fig. 6B)
PMID:20876564	FYPO:0007388	(Fig. 6A)
PMID:20876564	FYPO:0002021	(Fig. 6A)
PMID:20876564	PBO:0112768	(Fig. 3A)
PMID:20876564	PBO:0112769	(Fig. 3A)
PMID:20876564	PBO:0112770	(Fig. 3A)
PMID:20876564	PBO:0112770	(Fig. 3A)
PMID:20876564	PBO:0093556	(Fig. 4A)
PMID:20876564	FYPO:0000674	(Fig. 4A)
PMID:20876564	FYPO:0000674	(Fig. 4A)
PMID:20876564	PBO:0093558	(Fig. 4A)
PMID:20876564	FYPO:0000674	(Fig. 4A)
PMID:20876564	PBO:0093560	(Fig. 1A)
PMID:20876564	FYPO:0001357	(Fig. 1A and B)
PMID:20876564	FYPO:0001357	(Fig. 1A)
PMID:20876564	FYPO:0001357	(Fig. 1A)
PMID:20876564	FYPO:0002024	(Fig. 1A)
PMID:20876564	FYPO:0004103	(Fig. 1A)
PMID:20876564	FYPO:0004103	(Fig. 1A)
PMID:20876564	FYPO:0004103	(Fig. 1A)
PMID:20876564	FYPO:0000841	(Fig. 1B)
PMID:20876564	GO:0044732	(Fig. 1C)
PMID:20885790	PBO:0093580	(comment: less sensitive than ssb3delta alone)
PMID:20890290	PBO:0104007	Second, eRF1 and Dom34 increase the binding of GTP to eRF3 and Hbs1, respectively, and GTP increases the binding of eRF1 and Dom34 to eRF3 and Hbs1, respectively28,32,33 (Fig. 6 and Supplementary Table 1). These interactions suggest that in both complexes the status of the nucleotide affects the interaction of the proteins and thereby modulates the function of the complex.
PMID:20890290	PBO:0104008	Second, eRF1 and Dom34 increase the binding of GTP to eRF3 and Hbs1, respectively, and GTP increases the binding of eRF1 and Dom34 to eRF3 and Hbs1, respectively28,32,33 (Fig. 6 and Supplementary Table 1). These interactions suggest that in both complexes the status of the nucleotide affects the interaction of the proteins and thereby modulates the function of the complex.
PMID:20924116	FYPO:0006555	ternary complex normally forms with Swi1-Swi3 and Mrc1 on DNA
PMID:20924116	FYPO:0006555	ternary complex normally forms with Swi1-Swi3 and Mrc1 on DNA
PMID:20924116	FYPO:0006555	ternary complex normally forms with Swi1-Swi3 and Mrc1 on DNA
PMID:20924116	FYPO:0006555	ternary complex normally forms with Swi1-Swi3 and Mrc1 on DNA
PMID:20929775	PBO:0104309	(comment: CHECK K9-mehtylated)
PMID:20929775	PBO:0108926	(comment: CHECK phosphorylated)
PMID:20929775	PBO:0108926	(comment: CHECK phosphorylated)
PMID:20929775	PBO:0104309	(comment: CHECK K9 methyl;ated)
PMID:20929775	PBO:0108926	(comment: CHECK phosphorylated)
PMID:20929775	PBO:0104309	(comment: CHECK K9-mehtylated)
PMID:20935472	PBO:0023853	(comment: CHECK during metaphase)
PMID:20935472	PBO:0097541	Thus, we conclude that Cdc2 activity prevents precocious localization of Mde4 to the metaphase spindle.
PMID:20937798	PBO:0093609	in supp fig1 shows weak sensitivity at high cadmium concentrations
PMID:20967237	FYPO:0004318	(Fig. 2B) in this case (high temp + MBC) cells can proceed through cell cycle and replicate their DNA
PMID:20967237	PBO:0097626	(Fig. 1A,B) In the presence of MBC the % cut cells in wild type is almost identical to mad2 Delta at 32 and 35°c suggesting that the spindle assembly checkpoint is not active or overidden above 32°C in wild type cells in presence of MBC.
PMID:20967237	PBO:0100718	(Fig. 1C)
PMID:20967237	PBO:0100718	(Fig. 1E)
PMID:20967237	FYPO:0007858	(Fig. 1D)
PMID:20967237	PBO:0100718	(Fig. 1D)
PMID:20967237	PBO:0100718	(Fig. 1D)
PMID:20967237	PBO:0097954	(Fig. 1D) microtubules absent
PMID:20967237	PBO:0100719	(Fig. 2A)
PMID:20967237	FYPO:0003762	(Fig. 2B) in this case (high temp no MBC) the checkpoint is active at high temperature and cells are blocked in cell cycle progression at 36°C.
PMID:20967237	FYPO:0004367	(Fig. 2c)
PMID:20967237	FYPO:0007858	(Fig. 2c) in presence of MBC cells re-enter S phase earlier than in the absence of MBC
PMID:20967237	FYPO:0002004	(Fig. 3B) just a short microtubule stub remains
PMID:20967237	FYPO:0000133	(Fig. 3C)
PMID:20967237	FYPO:0007859	(Fig. 3D)
PMID:20967237	PBO:0100720	(Fig. 3F)
PMID:20967237	PBO:0100721	(Fig. 3E)
PMID:20967237	FYPO:0007859	Video S3
PMID:20967237	PBO:0095672	(Fig. 3G) (comment: suggests nuclear fission is independent of spindle checkpoint)
PMID:20967237	PBO:0100722	(Fig. 4A)
PMID:20967237	PBO:0100723	(Fig. 4D)
PMID:20967237	PBO:0100724	(Fig. 4B)
PMID:20967237	PBO:0100725	data not shown
PMID:20967237	PBO:0100726	(Fig. 4C) (comment: followed the presence of clp1 in the nucleolus to monitor cen3)
PMID:20967237	PBO:0100723	(Fig. 4E)
PMID:20967237	FYPO:0007862	(Fig. 5A)
PMID:20967237	PBO:0100727	(Fig. 6D,E) in presence of LatA + MBC there is no SPB separation compared to + MBC only where SPBs can separate
PMID:20974849	PBO:0096314	(Fig. 3A)
PMID:20974849	PBO:0112432	(Fig. 3C)
PMID:20974849	PBO:0093559	(Fig. 1C)
PMID:20974849	PBO:0093559	(Fig. 1C)
PMID:20974849	PBO:0093561	(Fig. 1C)
PMID:20974849	PBO:0093556	(Fig. 1C)
PMID:20974849	PBO:0093558	(Fig. 1C)
PMID:20974849	FYPO:0004481	(Fig. 1C)
PMID:20974849	PBO:0096312	(Fig. 1D)
PMID:20974849	FYPO:0000012	(Fig. 1B)
PMID:20974849	PBO:0096311	(Fig. 1A)
PMID:20974849	GO:0010971	As a whole, our findings suggest that both Cdr2-dependent and -independent mechanisms are responsible for the increased Wee1 levels and the G2/M defect in cpc2D cells.
PMID:20974849	PBO:0112443	(Fig. 5F)
PMID:20974849	PBO:0112437	(Fig. 5F)
PMID:20974849	FYPO:0000405	(Fig. 5G)
PMID:20974849	PBO:0112431	(Fig. 5G)
PMID:20974849	PBO:0096312	(Fig. 5E)
PMID:20974849	PBO:0096314	(Fig. 5E)
PMID:20974849	PBO:0096832	(Fig. 5C)
PMID:20974849	GO:2000045	(Fig. 2)
PMID:20974849	PBO:0096311	(Fig. 3A)
PMID:20974849	PBO:0112431	(Fig. 3A)
PMID:20974849	PBO:0112432	(Fig. 3C)
PMID:20974849	FYPO:0000405	(Fig. 3A)
PMID:20974849	PBO:0096311	(Fig. 3B)
PMID:20974849	PBO:0096312	(Fig. 3B)
PMID:20974849	PBO:0112435	(Fig. 4C)
PMID:20974849	PBO:0112434	(Fig. 4B)
PMID:20974849	GO:0043024	Importantly, by using a strain expressing a mutant version of Cpc2 (R36D/K38E) with reduced ability to associate with ribosomes in vivo (22), we also showed that ribosome binding of Cpc2 is critical for proper control of cell size at the G2/M boundary (Fig. 4A).
PMID:20974849	PBO:0096311	(Fig. 4A)
PMID:20974849	FYPO:0004481	(Fig. 3B)
PMID:20974849	PBO:0093558	(Fig. 3B)
PMID:20974849	PBO:0093561	(Fig. 3B)
PMID:20974849	PBO:0093559	(Fig. 3B)
PMID:20974849	PBO:0112433	(Fig. 3C)
PMID:20974849	PBO:0112433	(Fig. 3C)
PMID:20974849	PBO:0096314	(Fig. 1D)
PMID:20974849	PBO:0112438	(Fig. 5A)
PMID:20974849	PBO:0112439	(Fig. 5B)
PMID:20974849	PBO:0112440	(Fig. 5C)
PMID:20974849	PBO:0112441	(Fig. 5D)
PMID:20974849	PBO:0112442	(Fig. 5D)
PMID:20974849	PBO:0112436	(Fig. 4C)
PMID:20974849	PBO:0112437	(Fig. 4C)
PMID:20980623	GO:0035974	(Fig. 2)
PMID:20980623	PBO:0100817	At anaphase II, however, many of the Dma1-GFP signals did not accumulate at SPBs (Fig 2 B&C)
PMID:20980623	PBO:0100818	(Fig. S1)
PMID:20980623	PBO:0100818	(Fig. S1)
PMID:20980623	FYPO:0000587	the initiation of spore formation was delayed for +2 h compared with wild-type cells, and also the efficiency of spore formation was dramatically dropped with only +60% of cells containing spores (Figure 3B).
PMID:20980623	PBO:0100821	Supplemental Figure S3
PMID:20980623	PBO:0111998	(Figure 3B,4B) the initiation of spore formation was delayed for +2 h compared with wild-type cells, and also the efficiency of spore formation was dramatically dropped with only +60% of cells containing spores
PMID:20980623	FYPO:0003066	(Figure 4E)
PMID:20980623	FYPO:0003066	(Figure 4E)
PMID:20980623	PBO:0100820	Supplemental Figure S3
PMID:20980623	PBO:0100822	several types of defects in FSM development in dma1+ cells (Figure 6B). These defects roughly fell into three classes: (1) initially FSM formation was normal and appeared as sphere structure, but subsequently it became smaller or collapsed (asterisks in Figure 6B); (2) crescent-shaped structures did not properly develop into cup-like structures (open arrows in Figure 6B); and (3) crescent-shaped structures broke into multiple GFP-Psy1- contaning structures which could not develop into round mature FSMs (arrows in Figure 6B).
PMID:20980623	FYPO:0000583	dma1+ spg1-106 and dma1+ mob1-1 cells were completely unable to sporulate under conditions in which single spg1-106 or mob1-1 mutants were not apparently compromised for sporulation (Figure 8, A and B), suggesting that Dma1 might function in parallel with Spg1 and Mob1 in sporulation.
PMID:20980623	FYPO:0000583	dma1+ spg1-106 and dma1+ mob1-1 cells were completely unable to sporulate under conditions in which single spg1-106 or mob1-1 mutants were not apparently compromised for sporulation (Figure 8, A and B), suggesting that Dma1 might function in parallel with Spg1 and Mob1 in sporulation.
PMID:20980623	FYPO:0000583	dma1+ spg1-106 and dma1+ mob1-1 cells were completely unable to sporulate under conditions in which single spg1-106 or mob1-1 mutants were not apparently compromised for sporulation (Figure 8, A and B), suggesting that Dma1 might function in parallel with Spg1 and Mob1 in sporulation.
PMID:21035342	GO:0019887	(comment: vw: bit61 is importabt for torc2 regulation by ryh1)
PMID:21035342	PBO:0107586	"From review: Rab small GTPase emerges as a regulator of TOR complex 2 ""Consistently, we successfully collected genetic and biochemical data to support the notion that Sat1 and Sat4 form a GEF complex for Ryh1 GTPase in S. pombe. (7)."
PMID:21035342	PBO:0107586	"From review: Rab small GTPase emerges as a regulator of TOR complex 2 ""Consistently, we successfully collected genetic and biochemical data to support the notion that Sat1 and Sat4 form a GEF complex for Ryh1 GTPase in S. pombe. (7)."
PMID:21035342	PBO:0111686	"(comment: CHECK this is a bit of a fudge. It should probably be molecular signal transducer but that does not exist and I am prevented from using high level terms) vw: From review:Rab small GTPase emerges as a regulator of TOR complex 2""Consistently, we successfully collected genetic and biochemical data to supportthe notion that Sat1 and Sat4 form a GEF complex for Ryh1 GTPase in S. pombe. (7).I agree the data supports this model. Moreover, the Ryh1 I44E mutant fails to promote TORC2 signaling, implying that GTP-dependent interaction of Ryh1 with TORC2 via the effector domain drives TORC2-Gad8 signaling."
PMID:21095590	FYPO:0001931	(Fig. 5b)
PMID:21095590	PBO:0110104	phosphorylation of rad9 by DDK releases rad9 from damaged chromatin and allows repair factors to come in... (Figure 6)
PMID:21095590	FYPO:0001931	(Fig. 5b)
PMID:21095590	GO:0045739	phosphorylation of rad9 by DDK releases rad9 from damaged chromatin and allows repair factors to come in... (Figure 6)
PMID:21095590	GO:0045739	phosphorylation of rad9 by DDK releases rad9 from damaged chromatin and allows repair factors to come in... (Figure 6)
PMID:21098122	FYPO:0000085	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21098122	FYPO:0000268	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21098122	FYPO:0000267	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21098122	FYPO:0000268	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21098122	FYPO:0000085	no expressivity extension because of decreased growth when untreated
PMID:21098122	FYPO:0000267	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21098122	PBO:0104121	(comment: nuclease-dead allele)
PMID:21098122	FYPO:0000268	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21098122	FYPO:0000085	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21098122	FYPO:0000267	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21098141	PBO:0023514	In SGs after hyperosmotic shock (1 M KCl) but not after glucose deprivation
PMID:21099360	PBO:0093581	(comment: same as hsk1-89 alone)
PMID:21099360	PBO:0093581	(comment: same as hsk1-89 alone)
PMID:21099360	GO:0031573	(comment: hsk1 phenotypes more informative than mrc1 itself)
PMID:21099360	PBO:0100905	(comment: at ars2004 and oriChr2-1266, during early S phase)
PMID:21099360	PBO:0102371	(comment: not in SQ/TQ clusters)
PMID:21099360	PBO:0102370	(comment: in SQ/TQ clusters) (comment: CHECK activated_by(CHEBI:29035))
PMID:21099360	PBO:0102368	(comment: CONDITION 25 degrees) (comment: same as hsk1-89 alone)
PMID:21099360	PBO:0100922	(comment: CONDITION 30 degrees) (comment: same as hsk1-89 alone)
PMID:21099360	PBO:0102368	(comment: CONDITION 25 degrees) (comment: same as hsk1-89 alone)
PMID:21099360	PBO:0100922	(comment: CONDITION 30 degrees) (comment: same as hsk1-89 alone)
PMID:21099360	PBO:0102368	(comment: CONDITION 25 degrees) (comment: same as hsk1-89 alone
PMID:21099360	PBO:0100922	(comment: CONDITION 30 degrees) (comment: same as hsk1-89 alone)
PMID:21099360	FYPO:0001357	(comment: CONDITION 30 degrees) restrictive for hsk1-89 alone
PMID:21099360	PBO:0102368	(comment: CONDITION 25 degrees) (comment: same as hsk1-89 alone)
PMID:21099360	PBO:0100922	(comment: CONDITION 30 degrees) (comment: same as hsk1-89 alone)
PMID:21099360	PBO:0102368	(comment: CONDITION 25 degrees)
PMID:21099360	PBO:0100922	(comment: CONDITION 30 degrees)
PMID:21099360	PBO:0093581	(comment: same as hsk1-89 alone)
PMID:21099360	FYPO:0001355	(comment: CONDITION 30 degrees)
PMID:21099360	PBO:0094250	(comment: CONDITION 30 degrees)
PMID:21099360	PBO:0102364	(comment: CONDITION 25 degrees)
PMID:21099360	FYPO:0001382	(comment: MBP substrate)
PMID:21107719	GO:0071944	(comment: CHECK localization independent of actin cytoskeleton (assayed using latrunculin A) and microtubule cytoskeleton (assayed using carbendazim))
PMID:21113731	GO:0005794	Microscopy co-localization
PMID:21118717	GO:0047555	Active against both cAMP and cGMP based on its ability to confer resistance to exogenous cyclic nucleotides. Fig. 1A, B
PMID:21118717	GO:0004115	Active against both cAMP and cGMP based on its ability to confer resistance to exogenous cyclic nucleotides. Fig. 1A, B
PMID:21118717	PBO:0100388	Deletion of both cyr1/git2 and cgs2 produces cells that are hypersensitive to both exogenous cAMP and cGMP as these can activate PKA at low micromolar concentrations. Fig. 1A, B
PMID:21131906	PBO:0098869	(comment: CHECK un-ubiquitinated)
PMID:21148300	PBO:0097265	(comment: Cdc42-GTP assayed with CRIB)
PMID:21148300	PBO:0097265	(comment: Cdc42-GTP assayed with CRIB)
PMID:21148300	PBO:0097265	(comment: Cdc42-GTP assayed with CRIB)
PMID:21148300	PBO:0097265	(comment: Cdc42-GTP assayed with CRIB)
PMID:21151114	PBO:0097281	(comment: independent of Clr4)
PMID:21151114	PBO:0097131	(comment: independent of Clr4)
PMID:21151114	PBO:0020366	(comment: CHECK SO:0000286 = LTR)
PMID:21151114	PBO:0026298	(comment: independent of Clr4)
PMID:21151114	PBO:0103748	(comment: independent of Clr4)
PMID:21151114	PBO:0020366	(comment: CHECK SO:0000286 = LTR)
PMID:21151114	PBO:0098170	(comment: independent of Clr4)
PMID:21151114	PBO:0103746	(comment: independent of Clr4)
PMID:21151114	PBO:0026298	(comment: independent of Clr4)
PMID:21151114	PBO:0097280	(comment: independent of Clr4)
PMID:21151114	PBO:0103747	(comment: independent of Clr4)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECKi) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21211723	PBO:0102548	However, when asf1-1 or hip1Δ were combined with clr6 or alp13 mutant alleles, double mutants did not show additive defects on silencing as compared to the single mutants (Figure 3A and S4).
PMID:21211723	PBO:0102542	We also found that double mutants carrying mutations in clr3 or mit1 along with either asf1-1 or hip1Δ showed cumulative derepression of repeat elements (Figure 3A and S4), indicating overlapping functions for Asf1/HIRA and SHREC.
PMID:21211723	PBO:0102542	We also found that double mutants carrying mutations in clr3 or mit1 along with either asf1-1 or hip1Δ showed cumulative derepression of repeat elements (Figure 3A and S4), indicating overlapping functions for Asf1/HIRA and SHREC.
PMID:21211723	PBO:0102542	We also found that double mutants carrying mutations in clr3 or mit1 along with either asf1-1 or hip1Δ showed cumulative derepression of repeat elements (Figure 3A and S4), indicating overlapping functions for Asf1/HIRA and SHREC.
PMID:21211723	PBO:0102542	We also found that double mutants carrying mutations in clr3 or mit1 along with either asf1-1 or hip1Δ showed cumulative derepression of repeat elements (Figure 3A and S4), indicating overlapping functions for Asf1/HIRA and SHREC.
PMID:21211723	PBO:0102548	We also found that double mutants carrying mutations in clr3 or mit1 along with either asf1-1 or hip1Δ showed cumulative derepression of repeat elements (Figure 3A and S4), indicating overlapping functions for Asf1/HIRA and SHREC.
PMID:21211723	PBO:0102542	Consistent with both TGS and cis-PTGS contributing to heterochromatin silencing, combining asf1-1 or hip1Δ with tas3Δ resulted in synergistic defects in heterochromatic silencing (Figure 3A).
PMID:21211723	FYPO:0003235	Whereas asf1-1 cells showed slight reduction in levels of H3K9me, Swi6 and Chp2, the levels of these factors in hip1Δ appeared comparable to wild type (Figure 2A and 2B).
PMID:21211723	PBO:0111080	ChIP-chip showed that Hip1 was enriched throughout heterochromatin domains in the wild-type cells (Figure 2D, 2E, and S3). In the absence of Swi6, Hip1 localization was restricted to transcribed dg/dh repeats, and it failed to spread outward to the surrounding sequences (Figure 2D, 2E, and S3).
PMID:21211723	GO:0033696	(comment: CHECK not sure if this is quite the correct term, but it is the old spreading term
PMID:21211723	PBO:0102548	Consistent with both TGS and cis-PTGS contributing to heterochromatin silencing, combining asf1-1 or hip1Δ with tas3Δ resulted in synergistic defects in heterochromatic silencing (Figure 3A).
PMID:21211723	PBO:0102548	Consistent with both TGS and cis-PTGS contributing to heterochromatin silencing, combining asf1-1 or hip1Δ with tas3Δ resulted in synergistic defects in heterochromatic silencing (Figure 3A).
PMID:21211723	PBO:0102527	We also found that double mutants carrying mutations in clr3 or mit1 along with either asf1-1 or hip1Δ showed cumulative derepression of repeat elements (Figure 3A and S4), indicating overlapping functions for Asf1/HIRA and SHREC.
PMID:21211723	PBO:0102542	Consistent with both TGS and cis-PTGS contributing to heterochromatin silencing, combining asf1-1 or hip1Δ with tas3Δ resulted in synergistic defects in heterochromatic silencing (Figure 3A).
PMID:21211723	PBO:0102542	Consistent with both TGS and cis-PTGS contributing to heterochromatin silencing, combining asf1-1 or hip1Δ with tas3Δ resulted in synergistic defects in heterochromatic silencing (Figure 3A).
PMID:21211723	PBO:0102542	Consistent with both TGS and cis-PTGS contributing to heterochromatin silencing, combining asf1-1 or hip1Δ with tas3Δ resulted in synergistic defects in heterochromatic silencing (Figure 3A).
PMID:21211723	PBO:0102542	Consistent with both TGS and cis-PTGS contributing to heterochromatin silencing, combining asf1-1 or hip1Δ with tas3Δ resulted in synergistic defects in heterochromatic silencing (Figure 3A).
PMID:21211723	FYPO:0003412	asf1-1 alleviated silencing of the ura4+ inserted at the outer centromeric repeat region (otr1R::ura4+) and within a centromere-homologous (cenH) element at the silent mat locus (Kint2::ura4+), in a manner similar to HIRA null mutants (Figure 1C).
PMID:21211723	FYPO:0000470	asf1-1 and HIRA mutants were defective in mating-type switching, as indicated by the light iodine staining of the colonies (Figure 1F)
PMID:21211723	PBO:0111079	Defective mating-type switching in heterochromatin mutants results in poor iodine staining of colonies, in contrast to the dark staining of wild-type colonies (Jia et al., 2004). asf1-1 and HIRA mutants were defective in mating-type switching, as indicated by the light iodine staining of the colonies (Figure 1F).
PMID:21211723	PBO:0111079	Defective mating-type switching in heterochromatin mutants results in poor iodine staining of colonies, in contrast to the dark staining of wild-type colonies (Jia et al., 2004). asf1-1 and HIRA mutants were defective in mating-type switching, as indicated by the light iodine staining of the colonies (Figure 1F).
PMID:21211723	PBO:0111079	Defective mating-type switching in heterochromatin mutants results in poor iodine staining of colonies, in contrast to the dark staining of wild-type colonies (Jia et al., 2004). asf1-1 and HIRA mutants were defective in mating-type switching, as indicated by the light iodine staining of the colonies (Figure 1F).
PMID:21211723	PBO:0111079	Defective mating-type switching in heterochromatin mutants results in poor iodine staining of colonies, in contrast to the dark staining of wild-type colonies (Jia et al., 2004). asf1-1 and HIRA mutants were defective in mating-type switching, as indicated by the light iodine staining of the colonies (Figure 1F).
PMID:21211723	PBO:0111079	Defective mating-type switching in heterochromatin mutants results in poor iodine staining of colonies, in contrast to the dark staining of wild-type colonies (Jia et al., 2004). asf1-1 and HIRA mutants were defective in mating-type switching, as indicated by the light iodine staining of the colonies (Figure 1F).
PMID:21211723	PBO:0111079	Defective mating-type switching in heterochromatin mutants results in poor iodine staining of colonies, in contrast to the dark staining of wild-type colonies (Jia et al., 2004). asf1-1 and HIRA mutants were defective in mating-type switching, as indicated by the light iodine staining of the colonies (Figure 1F).
PMID:21211723	FYPO:0003096	Whereas asf1-1 cells showed slight reduction in levels of H3K9me, Swi6 and Chp2, the levels of these factors in hip1Δ appeared comparable to wild type (Figure 2A and 2B).
PMID:21211723	FYPO:0008151	We observed nucleosome free regions at 5′ ends of genes followed by positioned nucleosomes in open reading frames (Figure S7A). Comparison of nucleosome occupancy across heterochromatin domains in asf1, clr3 or asf1clr3 mutant cells to wild-type cells identified several sites showing depletion of nucleosomes in mutant cells.
PMID:21211723	FYPO:0005516	We observed nucleosome free regions at 5′ ends of genes followed by positioned nucleosomes in open reading frames (Figure S7A). Comparison of nucleosome occupancy across heterochromatin domains in asf1, clr3 or asf1clr3 mutant cells to wild-type cells identified several sites showing depletion of nucleosomes in mutant cells.
PMID:21211723	FYPO:0005516	In general, changes observed in clr3 and asf1 single mutants were weaker as compared to asf1clr3 double mutant that showed substantial reduction in the nucleosome occupancy (Figure 5).
PMID:21211723	FYPO:0005516	We observed nucleosome free regions at 5′ ends of genes followed by positioned nucleosomes in open reading frames (Figure S7A). Comparison of nucleosome occupancy across heterochromatin domains in asf1, clr3 or asf1clr3 mutant cells to wild-type cells identified several sites showing depletion of nucleosomes in mutant cells.
PMID:21211723	FYPO:0000963	However, both Asf1 and Clr6 complex-II mutants were not sensitive to hydoxyurea (Figure S6)
PMID:21211723	FYPO:0000963	However, both Asf1 and Clr6 complex-II mutants were not sensitive to hydoxyurea (Figure S6)
PMID:21211723	FYPO:0000089	We also found that asf1-1 cells were hypersensitive to genotoxic agents such as bleomycin, camptothecin and methylmethane sulfonate (Figure S6)
PMID:21211723	FYPO:0000085	We also found that asf1-1 cells were hypersensitive to genotoxic agents such as bleomycin, camptothecin and methylmethane sulfonate (Figure S6)
PMID:21211723	FYPO:0000095	more sensitive to bleomycin-induced damage, as indicated by the disappearance of full- length chromosome bands and the appearance of a smear of broken DNA fragments (Figure 4E).
PMID:21211723	GO:0045815	Thus, in addition to silencing heterochromatic repeats, Asf1 prevents antisense transcription at euchromatic loci.
PMID:21211723	FYPO:0003557	Notably, asf1-1 produced a disproportionate increase in antisense transcripts - constituting a large proportion of probes upregulated. Detailed expression profiling of individual loci showed that the antisense transcripts upregulated in asf1-1 mutants were also upregulated in hip1Δ and alp13Δ cells (Figure 4A and 4B).
PMID:21211723	FYPO:0008150	Interestingly, asf1-1, but not hip1Δ, also showed substantial increase in the levels of transcripts derived from intergenic portions of rDNA repeat loci (Figure S5B).
PMID:21211723	FYPO:0005917	Moreover, asf1-1 and hip1Δ showed upregulation of sense and antisense transcripts corresponding to subtelomeric genes located within heterochromatic domains (Figure S5A).
PMID:21211723	FYPO:0005917	Moreover, asf1-1 and hip1Δ showed upregulation of sense and antisense transcripts corresponding to subtelomeric genes located within heterochromatic domains (Figure S5A).
PMID:21211723	FYPO:0004347	Based on the genetic analyses, it was possible that Asf1/HIRA facilitate histone deacetylation by Clr6. Asf1 co-immunoprecipitated with Clr6 complex subunits Alp13 and Clr6 (Figure 3B). Moreover, asf1-1 and hip1Δ exhibited a substantial increase in bulk H3K9ac levels, in a manner similar to alp13Δ (Figure 3C).). To confirm this further, we performed ChIP-chip analyses of H3K9ac. Both alp13Δ and asf1-1 mutants showed widespread increase in H3K9ac, as compared to the wild-type cells. Notably, although 30% of the probes in our microarray correspond to intergenic regions, nearly all probes affected by asf1-1 and alp13Δ reside in coding regions (Figure 3D and 3E).
PMID:21211723	FYPO:0004347	Based on the genetic analyses, it was possible that Asf1/HIRA facilitate histone deacetylation by Clr6. Asf1 co-immunoprecipitated with Clr6 complex subunits Alp13 and Clr6 (Figure 3B). Moreover, asf1-1 and hip1Δ exhibited a substantial increase in bulk H3K9ac levels, in a manner similar to alp13Δ (Figure 3C).). To confirm this further, we performed ChIP-chip analyses of H3K9ac. Both alp13Δ and asf1-1 mutants showed widespread increase in H3K9ac, as compared to the wild-type cells. Notably, although 30% of the probes in our microarray correspond to intergenic regions, nearly all probes affected by asf1-1 and alp13Δ reside in coding regions (Figure 3D and 3E).
PMID:21211723	FYPO:0007217	Based on the genetic analyses, it was possible that Asf1/HIRA facilitate histone deacetylation by Clr6. Asf1 co-immunoprecipitated with Clr6 complex subunits Alp13 and Clr6 (Figure 3B). Moreover, asf1-1 and hip1Δ exhibited a substantial increase in bulk H3K9ac levels, in a manner similar to alp13Δ (Figure 3C).). To confirm this further, we performed ChIP-chip analyses of H3K9ac. Both alp13Δ and asf1-1 mutants showed widespread increase in H3K9ac, as compared to the wild-type cells. Notably, although 30% of the probes in our microarray correspond to intergenic regions, nearly all probes affected by asf1-1 and alp13Δ reside in coding regions (Figure 3D and 3E).
PMID:21211723	FYPO:0004347	Based on the genetic analyses, it was possible that Asf1/HIRA facilitate histone deacetylation by Clr6. Asf1 co-immunoprecipitated with Clr6 complex subunits Alp13 and Clr6 (Figure 3B). Moreover, asf1-1 and hip1Δ exhibited a substantial increase in bulk H3K9ac levels, in a manner similar to alp13Δ (Figure 3C).). To confirm this further, we performed ChIP-chip analyses of H3K9ac. Both alp13Δ and asf1-1 mutants showed widespread increase in H3K9ac, as compared to the wild-type cells. Notably, although 30% of the probes in our microarray correspond to intergenic regions, nearly all probes affected by asf1-1 and alp13Δ reside in coding regions (Figure 3D and 3E).
PMID:21211723	PBO:0102548	However, when asf1-1 or hip1Δ were combined with clr6 or alp13 mutant alleles, double mutants did not show additive defects on silencing as compared to the single mutants (Figure 3A and S4).
PMID:21215368	PBO:0095652	(Fig. S1F, S1G)
PMID:21215368	PBO:0094679	(Fig. 1D, 1E)
PMID:21215368	FYPO:0003555	(Fig. S1E)
PMID:21215368	FYPO:0003555	(Fig. S1E)
PMID:21215368	FYPO:0003555	(Fig. S1E)
PMID:21215368	PBO:0095653	(Fig. 1D, 1E)
PMID:21215368	PBO:0120607	(Fig. 7A, 7B)
PMID:21215368	PBO:0095652	(Fig. S1F, S1G)
PMID:21215368	PBO:0120601	(Fig. 6B)
PMID:21215368	PBO:0120598	(Fig. 4B)
PMID:21215368	PBO:0120599	(Fig. 4C)
PMID:21215368	FYPO:0002336	(Fig. S1F, S1G)
PMID:21215368	FYPO:0002336	(Fig. S1F, S1G)
PMID:21215368	PBO:0096189	(Fig. 7A)
PMID:21215368	PBO:0095652	(Fig. S1F, S1G)
PMID:21215368	PBO:0094681	(Fig. 1C, 1E)
PMID:21215368	PBO:0097950	(Fig. 1C, 1E)
PMID:21215368	PBO:0097950	(Fig. 1C-E)
PMID:21215368	PBO:0095653	(Fig. 1D)
PMID:21215368	PBO:0095653	(Fig. 1D, 1E)
PMID:21215368	PBO:0095653	(Fig. 1C)
PMID:21215368	FYPO:0002336	(Fig. 1D, 1E)
PMID:21215368	PBO:0095651	(Fig. 1C, 1E)
PMID:21215368	PBO:0095653	(Fig. 1C-E)
PMID:21215368	PBO:0095653	(Fig. 1C-E)
PMID:21215368	FYPO:0006995	(Fig. S1B)
PMID:21215368	FYPO:0006995	(Fig. S1B)
PMID:21215368	FYPO:0006995	(Fig. S1B)
PMID:21215368	PBO:0120604	(Fig. 6D)
PMID:21215368	PBO:0120603	(Fig. 6D)
PMID:21215368	PBO:0095834	(Fig. 1C-E)
PMID:21215368	PBO:0120602	(Fig. 6C)
PMID:21215368	PBO:0120596	(Fig. 4A, 6B)
PMID:21215368	FYPO:0003555	(Fig. S1E)
PMID:21215368	FYPO:0003555	(Fig. S1E)
PMID:21215368	FYPO:0003555	(Fig. S1E)
PMID:21215368	FYPO:0003555	(Fig. S1E)
PMID:21215368	FYPO:0003555	(Fig. S1E)
PMID:21215368	PBO:0120595	(Fig. 2)
PMID:21215368	PBO:0120594	(Fig. 2)
PMID:21215368	FYPO:0003555	(Fig. S1E)
PMID:21215368	PBO:0097950	(Fig. S1E)
PMID:21215368	FYPO:0004742	(Fig. S1C, S1D)
PMID:21215368	FYPO:0004742	(Fig. S1C, S1D)
PMID:21215368	FYPO:0004742	(Fig. S1C, S1D)
PMID:21215368	FYPO:0004742	(Fig. S1C, S1D)
PMID:21215368	FYPO:0004742	(Fig. S1C, S1D)
PMID:21215368	PBO:0107682	(Fig. S1C, S1D)
PMID:21215368	PBO:0107682	(Fig. S1C, S1D)
PMID:21215368	PBO:0107682	(Fig. S1C, S1D)
PMID:21215368	FYPO:0002358	(Fig. 1F)
PMID:21215368	FYPO:0004137	(Fig. 1F, 7C)
PMID:21215368	PBO:0120596	(Fig. 6B)
PMID:21215368	PBO:0094681	(Fig. S1E)
PMID:21215368	PBO:0120597	(Fig. 4A)
PMID:21215368	FYPO:0004742	(Fig. 1D, 1E)
PMID:21215368	PBO:0094679	(Fig. S1C, S1D)
PMID:21215368	PBO:0120599	(Fig. 4C)
PMID:21215368	PBO:0094282	(Fig. S1C, S1D)
PMID:21215368	PBO:0120598	(Fig. 4B)
PMID:21215368	PBO:0095834	(Fig. 1D, 1E)
PMID:21215368	PBO:0095834	(Fig. 1C)
PMID:21215368	PBO:0095834	(Fig. 1C-E)
PMID:21215368	PBO:0120600	(Fig. 4D)
PMID:21215368	PBO:0120600	(Fig. 4D)
PMID:21215368	PBO:0104711	(Fig. 6A)
PMID:21215368	PBO:0095834	(Fig. 1D)
PMID:21215368	PBO:0096189	(Fig. 1C, 1E)
PMID:21215368	FYPO:0006995	(Fig. 1D, 1E)
PMID:21215368	FYPO:0002336	(Fig. S1F, S1G)
PMID:21215368	FYPO:0002336	(Fig. S1F, S1G)
PMID:21215368	PBO:0094679	(Fig. 1C-E)
PMID:21215368	PBO:0094679	(Fig. 1C, 1E)
PMID:21215368	PBO:0094283	(Fig. 1C, 1E)
PMID:21215368	FYPO:0000888	(Fig. 1F, 7C)
PMID:21215368	PBO:0094688	(Fig. 1D, 1E)
PMID:21215368	PBO:0094688	(Fig. 1D, 1E)
PMID:21215368	FYPO:0003555	(Fig. 1D, 1E)
PMID:21215368	FYPO:0006995	(Fig. 7A)
PMID:21215368	PBO:0120606	(Fig. 7A)
PMID:21215368	PBO:0104711	(Fig. 6E)
PMID:21215368	PBO:0120608	Here we show that Cul4-Ddb1Cdt2 targets Epe1 in vivo (Figure 2) and that the putative substrate recognition subunit Cdt2 interacts with Epe1 (Figure 3).
PMID:21215368	PBO:0120605	(Fig. 6D)
PMID:21215368	PBO:0120608	Here we show that Cul4-Ddb1Cdt2 targets Epe1 in vivo (Figure 2) and that the putative substrate recognition subunit Cdt2 interacts with Epe1 (Figure 3).
PMID:21215368	PBO:0095651	(Fig. S1F, S1G)
PMID:21215368	PBO:0095653	(Fig. S1F, S1G)
PMID:21215368	FYPO:0004742	(Fig. S1C, S1D)
PMID:21215368	PBO:0120607	(Fig. S1F, S1G)
PMID:21215368	FYPO:0006995	(Fig. S1B)
PMID:21215368	PBO:0095652	(Fig. S1F, S1G)
PMID:21215368	FYPO:0006995	(Fig. S1B)
PMID:21215368	PBO:0095834	(Fig. S1B)
PMID:21215368	PBO:0095834	(Fig. S1B)
PMID:21215368	PBO:0095834	(Fig. S1B)
PMID:21215368	PBO:0095834	(Fig. S1B)
PMID:21215368	PBO:0095834	(Fig. S1B)
PMID:21215368	PBO:0096189	(Fig. S1B)
PMID:21215368	FYPO:0006429	(Fig. 7C)
PMID:21215368	FYPO:0004743	(Fig. 7C)
PMID:21215368	FYPO:0004743	(Fig. 7C)
PMID:21215368	FYPO:0002336	(Fig. 7A, 7B)
PMID:21215368	FYPO:0002336	(Fig. 7A, 7B)
PMID:21217703	PBO:0108126	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	PBO:0108127	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	PBO:0108127	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	FYPO:0002907	Three mutants (Taz1 I379R, Taz1 L383R, and Rap1 I655R) with no detectable Taz1-SpRap1 interaction clearly exhibited altered mobility bands representing intra-chromosome fusions (Fig. 6e).
PMID:21217703	PBO:0093636	Consistent with the published results, deletion of taz1+ or rap1+ from yeast cells resulted in a dramatic increase in telomere length and length heterogeneity compared to wild-type cells (Fig. 6c).
PMID:21217703	PBO:0093636	Three point mutants (Taz1 I379R, Taz1 L383R, and Rap1 I655R) that completely abolished the Taz1-SpRap1 interaction in the ITC assay displayed a rap1Δ- and taz1Δ-like telomere length defect (Figs. 6b and 6c)
PMID:21217703	PBO:0108126	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	PBO:0108127	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	PBO:0108126	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	PBO:0108127	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21256022	GO:0005515	(comment: binding site L405 ndc80 loop
PMID:21256022	PBO:0102183	(comment: affecting dis1
PMID:21300781	PBO:0106616	Lysine 105 and Lysine 106 are acetylated in an Eso1 dependent manner. Psm3 acetylation on K105 K106 contribute to counteract the cohesin release activity of Wpl1.
PMID:21300781	PBO:0021527	Lysine 105 and Lysine 106 are acetylated in an Eso1 dependent manner. Psm3 acetylation on K105 K106 contribute to counteract the cohesin release activity of Wpl1.
PMID:21300781	FYPO:0001355	(Fig. 7)
PMID:21300781	PBO:0106616	Lysine 105 and Lysine 106 are acetylated in an Eso1 dependent manner. Psm3 acetylation on K105 K106 contribute to counteract the cohesin release activity of Wpl1.
PMID:21300781	PBO:0021527	Lysine 105 and Lysine 106 are acetylated in an Eso1 dependent manner. Psm3 acetylation on K105 K106 contribute to counteract the cohesin release activity of Wpl1.
PMID:21307936	GO:0005515	supp fig 9A
PMID:21317872	PBO:0095159	(comment: poly(A) tails longer in rrp6delta alone, but wild type not shown for meiotic cell cycle so can't annotate rrp6delta phenotype as normal or increased length)
PMID:21317872	GO:0071920	Red1 localizes to cleavage bodies in mitotically dividing cells and cooperates with polyadenylation factors to hyperadenylate meiotic mRNAs. (A) Red1 dots co-localize with cleavage factor, Pcf11; the canonical poly(A) polymerase, Pla1; a nuclear exosome subunit, Rrp6; and a nuclear poly(A)-binding protein, Pab2.
PMID:21317872	PBO:0095158	(comment: poly(A) tails longer in rrp6delta alone, but wild type not shown for meiotic cell cycle so can't annotate rrp6delta phenotype as normal or increased length)
PMID:21317872	GO:0071920	Red1 localizes to cleavage bodies in mitotically dividing cells and cooperates with polyadenylation factors to hyperadenylate meiotic mRNAs. (A) Red1 dots co-localize with cleavage factor, Pcf11; the canonical poly(A) polymerase, Pla1; a nuclear exosome subunit, Rrp6; and a nuclear poly(A)-binding protein, Pab2.
PMID:21317872	GO:0071920	Red1 localizes to cleavage bodies in mitotically dividing cells and cooperates with polyadenylation factors to hyperadenylate meiotic mRNAs. (A) Red1 dots co-localize with cleavage factor, Pcf11; the canonical poly(A) polymerase, Pla1; a nuclear exosome subunit, Rrp6; and a nuclear poly(A)-binding protein, Pab2.
PMID:21317872	GO:0071920	Red1 localizes to cleavage bodies in mitotically dividing cells and cooperates with polyadenylation factors to hyperadenylate meiotic mRNAs. (A) Red1 dots co-localize with cleavage factor, Pcf11; the canonical poly(A) polymerase, Pla1; a nuclear exosome subunit, Rrp6; and a nuclear poly(A)-binding protein, Pab2.
PMID:21317872	GO:0071920	Red1 localizes to cleavage bodies in mitotically dividing cells and cooperates with polyadenylation factors to hyperadenylate meiotic mRNAs. (A) Red1 dots co-localize with cleavage factor, Pcf11; the canonical poly(A) polymerase, Pla1; a nuclear exosome subunit, Rrp6; and a nuclear poly(A)-binding protein, Pab2.
PMID:21357609	PBO:0116399	Overexpression of Mtf1 and Rpo41 can induce mitochondrial transcription. Mtf1 and Rpo41 can bind and transcribe mitochondrial promoters in vitro and the initiating nucleotides were the same in vivo and in vitro. Mtf1 is required for efficient transcription.
PMID:21357609	FYPO:0000809	Mitochondrial dye showed diffuse staining. they think it is a loss of membrane potential so the dye is not drawn in properly
PMID:21376595	PBO:0110300	We conclude that Mid1p recruits Rng2p to cortical nodes at the division site and that Rng2p, in turn, recruits other components of the actomyosin ring to cortical nodes, thereby ensuring correct placement of the division site.
PMID:21376600	PBO:0112276	(Fig. 1B)
PMID:21376600	PBO:0112277	(Fig. 1C)
PMID:21376600	PBO:0093476	(Fig. 1C, D and 2A, E)
PMID:21376600	PBO:0112278	(Fig. 1C, D and 2A, E)
PMID:21376600	PBO:0112279	(Fig. 1E)
PMID:21376600	PBO:0112280	Plo1 localization to the contractile ring was abolished in the Mid1-T517A mutant (Figures S1C and S1D; 0 of 66 mitotic T517A cells with Plo1-GFP at the contractile ring compared to 26 of 58 in control mitotic cells)
PMID:21376600	PBO:0094506	(Fig. 2A and E)
PMID:21376600	PBO:0094506	(Fig. 2A and E)
PMID:21376600	MOD:00046	(Fig. 2A and E)
PMID:21376600	PBO:0094506	(Fig. 2A and E)
PMID:21376600	PBO:0094506	(Fig. 2A and E)
PMID:21376600	PBO:0094506	(Fig. 2A and E)
PMID:21376600	PBO:0112281	(Fig. 2B)
PMID:21376600	PBO:0112282	(Fig. 2B)
PMID:21376600	PBO:0112283	(Fig. 2B)
PMID:21376600	PBO:0112284	(Fig. 2B)
PMID:21376600	PBO:0112285	(Fig. S2B)
PMID:21376600	PBO:0112285	(Fig. S2B)
PMID:21376600	PBO:0112285	(Fig. S2B)
PMID:21376600	PBO:0112285	(Fig. S2B)
PMID:21376600	PBO:0112286	(Fig. S2B)
PMID:21376600	PBO:0112286	(Fig. S2B)
PMID:21376600	PBO:0112287	(Fig. S2B)
PMID:21376600	PBO:0112287	(Fig. S2B)
PMID:21376600	PBO:0112288	(Fig. S2E)
PMID:21376600	PBO:0112289	(Fig. S2E)
PMID:21376600	FYPO:0001368	(Fig. 3)
PMID:21376600	PBO:0112290	(Fig. 3C)
PMID:21376600	PBO:0112291	(Fig. 3C)
PMID:21376600	PBO:0112292	(Fig. 3D)
PMID:21376600	PBO:0112293	(Fig. 3D)
PMID:21376600	PBO:0112294	(Fig. 3D)
PMID:21376600	PBO:0112295	(Fig. 3D)
PMID:21376600	GO:1903499	These data altogether reveal mechanisms by which Plo1 acts as a key temporal coordinator of contractile ring assembly events in fission yeast.
PMID:21376600	PBO:0112296	(Fig. S3H)
PMID:21376600	PBO:0114259	Plo1 phosphorylates several residues within the first 100 amino acids of Mid1, which directly interact with the IQGAP Rng2 [17], and influences the timing of myosin II recruitment. Plo1 thereby facilitates contractile ring assembly at mitotic onset.
PMID:21376600	PBO:0112294	(Fig. S3H)
PMID:21376600	PBO:0112297	(Fig. 4B)
PMID:21376600	PBO:0112298	(Fig. 4B)
PMID:21376600	PBO:0112276	(Fig. 1B)
PMID:21389117	FYPO:0003379	(Fig. 1c) no tetranucleates
PMID:21389117	PBO:0107804	(Fig. 2A)
PMID:21389117	FYPO:0003379	(Fig. 2A)
PMID:21389117	FYPO:0003380	(Fig. 2B)
PMID:21389117	FYPO:0003379	(Fig. 2B)
PMID:21389117	PBO:0104199	(Fig. 6C)
PMID:21389117	PBO:0104199	(Fig. 6C)
PMID:21389117	GO:0005515	(Fig. 7A)
PMID:21389117	GO:0005515	(Fig. 7A)
PMID:21389117	GO:0005515	(Fig. 7A)
PMID:21389117	FYPO:0000587	(Fig. 1B) 4 nuclei appear later than normal.
PMID:21389117	FYPO:0005412	(Fig. 1B) 4 nuclei appear later than normal.
PMID:21389117	PBO:0107794	(comment: I'm not completely sure if the Slp1-APC degrades mes1 or only ubiquitinates it, but this is most likely correct?...)
PMID:21389117	FYPO:0005382	(comment: CHECK also fzr2 &3)
PMID:21389117	FYPO:0001000	(Fig. 1B) 4 nuclei appear later than normal.
PMID:21389117	GO:0005515	(Fig. 7A)
PMID:21389117	FYPO:0005382	(comment: also fzr3)
PMID:21389117	PBO:0107807	(Fig. 2A)
PMID:21389117	FYPO:0004994	(Fig. 2B)
PMID:21422229	PBO:0114258	Rng2 subsequently recruits the myosin­II subunits Myo2 and Rlc1.
PMID:21429938	PBO:0097898	(comment: cross between h+ and h- deletions, allowed to sporulate immediately)
PMID:21429938	FYPO:0002485	(comment: cross between h+ and h- deletions, allowed to sporulate immediately)
PMID:21429938	PBO:0095338	(comment: cross between h+ and h- deletions, allowed to sporulate immediately)
PMID:21429938	PBO:0095337	(comment: cross between h+ and h- deletions, allowed to sporulate immediately)
PMID:21436456	FYPO:0003557	Because clr4Δ and ago1Δ enhance antisense RNA levels when combined with a variant histone h2a.zΔ (10), we examined the mlo3-A mutant transcriptome with or without H2A.Z. Like clr4Δ and ago1Δ, mlo3-A also showed weak up- regulation of antisense RNAs (4.7% genes) (fig. S9).
PMID:21436456	FYPO:0002359	(Figure S3) mlo3∆ cells maintain H3K9me2 and Swi6 localization at centromeres, mating type locus and subtelomeric loci
PMID:21436456	FYPO:0000862	(Figure S3) mlo3∆ cells maintain H3K9me2 and Swi6 localization at centromeres, mating type locus and subtelomeric loci
PMID:21436456	PBO:0110843	(Figure S3) mlo3∆ cells maintain H3K9me2 and Swi6 localization at centromeres, mating type locus and subtelomeric loci
PMID:21436456	FYPO:0005522	However, mlo3Δ resulted in a considerable increase in the levels of centromeric repeat transcripts, although to a lesser extent than in clr4Δ (Fig. 1B).
PMID:21436456	PBO:0108265	However, mlo3Δ resulted in a considerable increase in the levels of centromeric repeat transcripts, although to a lesser extent than in clr4Δ (Fig. 1B).
PMID:21436456	PBO:0108263	However, mlo3Δ resulted in a considerable increase in the levels of centromeric repeat transcripts, although to a lesser extent than in clr4Δ (Fig. 1B).
PMID:21436456	PBO:0108263	However, mlo3Δ resulted in a considerable increase in the levels of centromeric repeat transcripts, although to a lesser extent than in clr4Δ (Fig. 1B).
PMID:21436456	GO:0005515	A yeast two-hybrid screen using full-length Clr4 as the bait identified Mlo3 (12) as an interacting protein (table S1). Mlo3 is related to Saccharomyces cerevisiae Yra1 and mammalian Aly/REF (13) and is required for nuclear export of RNA (13). Immunoprecipitation analysis detected Mlo3 interacting with Clr4 (Fig. 1A) and another ClrC subunit, Rik1 (fig. S1). Moreover, recombinant Mlo3 bound Clr4, and this interaction was mediated by the amino-terminal (amino acids 1 to 55) and carboxy-terminal (amino acids 134 to 199) regions of Mlo3 (fig. S2), known to bind mRNA export machinery (13). Thus, Clr4 associates with Mlo3 in vitro and in vivo.
PMID:21436456	PBO:0110844	We found that Mlo3 coimmunoprecipitated with Chp1, a subunit of RITS (Fig. 1C).
PMID:21436456	PBO:0110845	his interaction was not sensitive to DNase I and RNase A treatment but was severely compromised upon loss of Clr4 (Fig. 1C), suggesting that Clr4 connects Mlo3 to RNA interference (RNAi).
PMID:21436456	FYPO:0004201	Indeed, mlo3Δ caused severe reduction in the levels of centromeric siRNAs (Fig. 1D).
PMID:21436456	GO:0140746	(comment: vw: I did not use processing because this seems to be catabolism) Thus, in addition to creating H3K9me binding sites for RITS, Clr4 physically and functionally links RITS to Mlo3 to mediate processing of centromeric transcripts.
PMID:21436456	PBO:0110846	Recombinant Clr4 could methylate the carboxyterminal region of Mlo3, but not the amino-terminal or middle region (Fig. 2A). Within the carboxy-terminal region, lysines 165 and 167 are in a sequence context that resembles H3K9. We mutated these and lysines 179 and 180 to alanine. A methylation assay using recombinant Mlo3 carrying single- or double-mutant combinations showed that Clr4 methylates K167 of Mlo3 in vitro (Fig. 2B).
PMID:21436456	PBO:0110847	A methylation assay using recombinant Mlo3 carrying single- or double-mutant combinations showed that Clr4 methylates K167 of Mlo3 in vitro (Fig. 2B).
PMID:21436456	PBO:0110848	A methylation assay using recombinant Mlo3 carrying single- or double-mutant combinations showed that Clr4 methylates K167 of Mlo3 in vitro (Fig. 2B).
PMID:21436456	FYPO:0004201	Interestingly, mlo3-A caused a decrease in levels of centromeric siRNA as compared to WT (Fig. 2D).
PMID:21436456	FYPO:0004201	Further reduction in siRNAs was observed in mlo3-A H3K9R double mutant (Fig. 2D), although a residual signal seemed to be present when compared to clr4Δ.
PMID:21436456	GO:0000791	Mlo3 showed a broad distribution at euchromatic loci and a relative depletion at heterochromatic regions (figs. S5 and S6).
PMID:21436456	PBO:0110849	Expression profiling of mlo3Δ cells on both DNA strands showed dramatic accumulation of antisense RNAs at euchromatic loci (~23.5% of genes) (fig. S7), in particular at convergent genes (fig. S8)
PMID:21436456	PBO:0110850	However, the mlo3-A h2a.zΔ double mutant showed a synergistic increase in antisense RNAs (18.6% of genes) (Fig. 3C and figs. S8 and S9)Because clr4Δ and ago1Δ enhance antisense RNA levels when combined with a variant histone h2a.zΔ (10), we examined the mlo3-A mutant transcriptome with or without H2A.Z. Like clr4Δ and ago1Δ, mlo3-A also showed weak up- regulation of antisense RNAs (4.7% genes) (fig. S9).
PMID:21436456	PBO:0110851	Mlo3 is required for suppression of antisense RNAs targeted by Clr4 and by the exosome. (A) Strand-specific RTPCR of RNA isolated from WT and mlo3Δ
PMID:21436456	PBO:0110852	Mlo3 is required for suppression of antisense RNAs targeted by Clr4 and by the exosome. (A) Strand-specific RTPCR of RNA isolated from WT and mlo3Δ
PMID:21436456	PBO:0110853	Mlo3 is required for suppression of antisense RNAs targeted by Clr4 and by the exosome. (A) Strand-specific RTPCR of RNA isolated from WT and mlo3Δ
PMID:21436456	GO:0071040	Thus, Mlo3 physically associates with TRAMP, a complex involved in the surveillance and degradation of aberrant RNA by the exosome. In this regard, the antisense profile of mlo3Δ closely resembles that of rrp6Δ (Fig. 3, C and E, and fig. S8).
PMID:21437270	FYPO:0005371	(comment: ch16)
PMID:21441914	FYPO:0000267	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000085	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000085	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000088	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000268	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000268	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000267	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000268	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000085	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000267	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000088	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000268	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000268	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000267	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000088	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000085	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000088	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000085	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000267	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000088	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21444718	FYPO:0000957	However, like pli1 cells, SUMOD81R mutants are not appreciably sensitive to genotoxins (Fig. 4A)
PMID:21444718	PBO:0120370	We next analyzed total SUMO conjugates in SUMOD81R cells by Western blotting for comparison with those in reference strains. Notably, in both SUMOD81R and pli1 cells, the wild-type pattern of SUMO conjugates was undetectable (Fig. 3E). In contrast, bulk SUMO conjugates were readily detected in cells lacking Nse2 SUMO ligase activity (nse2-SA) or the Ubc9:SLD2 complex (Fig. 3E, rad60E380R)
PMID:21444718	FYPO:0000088	K14E at the E1 binding site, which caused HU sensitivity (Fig. 2C)
PMID:21444718	FYPO:0001690	However, like pli1 cells, SUMOD81R mutants are not appreciably sensitive to genotoxins (Fig. 4A)
PMID:21444718	FYPO:0000963	However, like pli1 cells, SUMOD81R mutants are not appreciably sensitive to genotoxins (Fig. 4A)
PMID:21444718	PBO:0093580	Interestingly, rad60E380R mutant cells are hypersensitive to the same DNA-damaging agents as nse2-SA cells (Fig. 4A).
PMID:21444718	FYPO:0000088	In addition, we identified two mutations, P21L and F24S, at the noncovalent Ubc9:SLD2 interface that also result in HU sensitivity (Fig. 2C).
PMID:21444718	PBO:0093616	Interestingly, rad60E380R mutant cells are hypersensitive to the same DNA-damaging agents as nse2-SA cells (Fig. 4A).
PMID:21444718	PBO:0093613	Interestingly, rad60E380R mutant cells are hypersensitive to the same DNA-damaging agents as nse2-SA cells (Fig. 4A).
PMID:21444718	PBO:0093613	Interestingly, rad60E380R mutant cells are hypersensitive to the same DNA-damaging agents as nse2-SA cells (Fig. 4A).
PMID:21444718	PBO:0093616	Interestingly, rad60E380R mutant cells are hypersensitive to the same DNA-damaging agents as nse2-SA cells (Fig. 4A).
PMID:21444718	FYPO:0001690	However, like pli1 cells, SUMOD81R mutants are not appreciably sensitive to genotoxins (Fig. 4A)
PMID:21444718	PBO:0120373	These data provide compelling support for the role of Ubc9:SUMO in facilitating Pli1-dependent sumoylation, which is toxic in STUbL mutant cells.
PMID:21444718	FYPO:0002061	In addition, an nse2-SA SUMOD81R double mutant is synthetically sick and phenocopies an nse2-SA pli1 double mutant (55) (Fig. 4C).
PMID:21444718	FYPO:0001355	Therefore, we tested for an analogous genetic interaction be- tween rad60E380R and SUMOD81R. Whereas either single mu- tant grows well, the rad60E380R SUMOD81R double mutant is extremely synthetically sick (Fig. 4B), exhibiting a similar phe- notype to the rad60E380R pli1 mutant (39).
PMID:21444718	FYPO:0001355	Therefore, we tested for an analogous genetic interaction be- tween rad60E380R and SUMOD81R. Whereas either single mu- tant grows well, the rad60E380R SUMOD81R double mutant is extremely synthetically sick (Fig. 4B), exhibiting a similar phe- notype to the rad60E380R pli1 mutant (39).
PMID:21444718	FYPO:0006887	SUMOD81R is conjugation proficient as it produced a sumoylation pattern indistinguish- able from that of the wild type (Fig. 3C).
PMID:21444718	PBO:0093580	Interestingly, rad60E380R mutant cells are hypersensitive to the same DNA-damaging agents as nse2-SA cells (Fig. 4A).
PMID:21444718	PBO:0120369	We tested in vitro interaction between His6-SLD2 and recombinant wild-type GST-Ubc9 or GST-Ubc9H20D by GSH-Sepharose pulldown and Western analysis, revealing that GST-Ubc9H20D abolishes the interaction (Fig. 2A).
PMID:21444718	PBO:0120368	We tested in vitro interaction between His6-SLD2 and recombinant wild-type GST-Ubc9 or GST-Ubc9H20D by GSH-Sepharose pulldown and Western analysis, revealing that GST-Ubc9H 2 0 D abolishes the interaction (Fig. 2A).
PMID:21444718	GO:0016925	Thus, both Pli1 and the noncovalent Ubc9:SUMO complex are critical for bulk sumoylation but not for modifying key targets in the DNA repair response
PMID:21444718	GO:0016925	Thus, both Pli1 and the noncovalent Ubc9:SUMO complex are critical for bulk sumoylation but not for modifying key targets in the DNA repair response
PMID:21444718	FYPO:0005629	The rad60E380R mutant exhibits elevated SUMO conjugates before and after HU treatment, which, based on the foregoing results, is most likely the result of replicative stress in the sickly rad60E380R strain. Therefore
PMID:21444718	PBO:0120371	We confirmed this hypothesis through in vitro binding assays of recombinant SUMO and Ubc9/ Ubc9H20D (Fig. 3A).
PMID:21444718	FYPO:0000088	In addition, we identified two mutations, P21L and F24S, at the noncovalent Ubc9:SLD2 interface that also result in HU sensitivity (Fig. 2C).
PMID:21444718	FYPO:0000957	Strikingly, compared to SUMO , SUMOD81R cells exhibited nearly wild-type growth rates and sensitivity to genotoxins (Fig. 3D).
PMID:21444718	FYPO:0005630	Interestingly, upon STUbL inactivation SUMOD81R forms a major di-SUMO species but none of the higher-molecular- weight chains observed with wild-type SUMO (Fig. 5B).
PMID:21444718	PBO:0120372	These data provide compelling support for the role of Ubc9:SUMO in facilitating Pli1-dependent sumoylation, which is toxic in STUbL mutant cells.
PMID:21444718	FYPO:0000963	However, like pli1 cells, SUMOD81R mutants are not appreciably sensitive to genotoxins (Fig. 4A)
PMID:21444751	FYPO:0002826	Collectively, these results indicate that in fission yeast, a ?-TuRC- like complex exists as a stable structure in vivo independent of the Mto1/2 complex
PMID:21449049	FYPO:0007100	mei4-N136A combined with pat1-114 was efficiently blocked at the meiosis I onset with telomere clustered at SPBs (in the bouquet configuration) at 32˚C, which arrest can be released by a temperature shift down to 25˚C.
PMID:21449049	FYPO:0007100	mei4-N136A combined with pat1-114 was efficiently blocked at the meiosis I onset with telomere clustered at SPBs (in the bouquet configuration) at 32˚C, which arrest can be released by a temperature shift down to 25˚C.
PMID:21450810	PBO:0100550	C11-F32S was more active in yJI1 than in yYH1, while wild-type C11 had no effect (Sector 4).
PMID:21450810	PBO:0100550	Rpc2-T455I was clearly more active (white) in yJI1 than in yYH1, consistent with dT(6) readthrough as expected.
PMID:21481773	PBO:0112684	Ofd1 was enriched in the nucleus with little cytosolic staining consistent with previous findings (Fig. 3A)(
PMID:21481773	PBO:0112757	(comment: CHECK inhibitor GO:0031543 peptidyl-proline dioxygenase activity) Importantly, Sre1N also failed to accumulate in NLS-ofd1 nro1Δ cells in the absence of oxygen despite the restored Ofd1 nuclear localization (Fig. 4B, lanes 10-12). Taken together, these data support previous studies and demonstrate that Nro1 functions as a direct inhibitor of Ofd1 in Sre1N
PMID:21481773	PBO:0112686	In sre1N nro1Δ cells, Ofd1 showed diffuse cytosolic staining indicating that Nro1 is required for Ofd1 nuclear localization. Staining for Ofd1 was specific as ofd1Δ cells showed no signal. Together, these results show that nuclear localization of Ofd1 is linked to Nro1.
PMID:21481773	PBO:0112689	(comment: CHECK sre1 n terminus isoform***********)In nro1Δ cells with Ofd1 retained in the cytosol due to the loss of Nro1-mediated nuclear localization, Sre1N failed to accumulate in anaerobic conditions (Fig. 4B, lanes 7-9).
PMID:21481773	PBO:0112688	(comment: CHECK with ofd1)
PMID:21481773	PBO:0112690	(comment: CHECK sre1 n terminus isoform***********.) As previously reported, Sre1N accumulated in sre1N cells under anaerobic conditions (Fig. 4B, lanes 1-3)(Lee et al., 2009).
PMID:21481773	PBO:0112685	Ofd1 was enriched in the nucleus with little cytosolic staining consistent with previous findings (Fig. 3A)(
PMID:21518960	FYPO:0001249	(comment: assayed at ars1 and ori1-200, early-firing origins; only affects origins normally bound by Mrc1)
PMID:21518960	FYPO:0005107	(comment: assayed at ars1 and ars2004)
PMID:21518960	FYPO:0005107	(comment: assayed at ars1 and ars2004)
PMID:21518960	PBO:0105448	(comment: assayed elongation from ars1 and ars2004, early-firing origins)
PMID:21518960	FYPO:0001249	(comment: assayed at ars1 and ars2004, early-firing origins)
PMID:21518960	PBO:0100905	(comment: predominantly at early-firing origins including ars1 and ars2004, but not AT1041; Mrc1 associates with origins later than MCM complex, but slightly earlier than Cdc45)
PMID:21518960	FYPO:0005108	(comment: assayed elongation from ori1-200)
PMID:21518960	PBO:0105449	(comment: assayed at ars1 and ars2004)
PMID:21518960	PBO:0105447	(comment: assayed at ars1 and ars2004, early-firing origins)
PMID:21536008	GO:0016651	"(comment: heterologous cytc as acceptor. they had to include this as etp1 wouldn't accept an electron otherwise.) ""S. pombe does not express any endogenous mitochondrial cytochromes P450 that could act as terminal electron acceptors"""
PMID:21540296	PBO:0103824	(comment: t-shift on mitotic entry) Fig. 1c
PMID:21540296	PBO:0035578	(comment: t-shift on mitotic entry) Fig. 1d
PMID:21540296	PBO:0035577	(comment: t-shift on mitotic entry) Fig. 1d
PMID:21540296	FYPO:0002061	(Fig. 1a)
PMID:21540296	FYPO:0002061	(Fig. 1a)
PMID:21540296	FYPO:0002060	(Fig. 1a)
PMID:21540296	FYPO:0005424	(comment: t-shift on mitotic entry) Fig. 1c
PMID:21540296	MOD:00046	(Fig. 5c)
PMID:21540296	PBO:0035583	(Fig. 4)
PMID:21540296	FYPO:0001513	(comment: t-shift on mitotic entry) Fig. 1c
PMID:21540296	PBO:0035579	(comment: t-shift on mitotic entry) Fig. 1c
PMID:21540296	PBO:0035579	(comment: t-shift on mitotic entry) Fig. 1c
PMID:21540296	PBO:0035590	(Fig. 7a)
PMID:21540296	PBO:0035591	(Fig. 7a)
PMID:21540296	PBO:0035590	(Fig. 7a)
PMID:21540296	PBO:0035590	(Fig. 7a)
PMID:21540296	PBO:0035592	(Fig. 7a)
PMID:21540296	PBO:0035592	(Fig. 7a)
PMID:21540296	PBO:0035593	(Figure 7c) (comment: no rescue of cnd-2)
PMID:21540296	PBO:0035594	(Figure 7e)
PMID:21561865	MOD:00047	present at basal level; increased in presence of hydroxyurea
PMID:21561865	MOD:00047	present at basal level; increased in presence of hydroxyurea
PMID:21610214	GO:0043169	(comment: sulphate)
PMID:21633354	PBO:0107914	(comment: H3-pS10 used to detect ark1 activity)
PMID:21633354	PBO:0107913	(comment: centromeric)
PMID:21633354	PBO:0093730	(comment: CHECK condensin, which subunit assayed?)
PMID:21633354	PBO:0093563	we engineered a Cnd2-Cnp3C fusion protein, which targets kinetochores through the Cnp3C domain32, even in pcs1Δ cells. The expression of this fusion protein largely suppresses the growth defect, sensitivity to thiabendazole (TBZ, a microtubule destabilizing drug) and the incidence of lagging chromosomes in pcs1Δ cells, whereas neither Cnd2 nor Cnp3C protein alone suppresses these phenotypes (Fig. 1c and Supplementary Fig. 7). These
PMID:21633354	FYPO:0003286	(comment: decreased along arms)
PMID:21633354	PBO:0093730	(comment: all tested chromosome loci) (Fig. 2g).
PMID:21633354	PBO:0093730	(comment: all tested chromosome loci) (Fig. 2g).
PMID:21633354	FYPO:0001357	In contrast, the growth defect and TBZ sensitivity of pcs1Δ cells are not suppressed by the sfc3-1 mutation, whereas they are suppressed by an increase in kinetochore condensin (Fig. 1d).
PMID:21652630	FYPO:0002858	in fig s4b there is septal material hanging around one cell end
PMID:21652630	FYPO:0000421	(Fig. S5A)
PMID:21664573	FYPO:0002060	(Supplemental Figure 2B)
PMID:21664573	FYPO:0002060	(Figure 1D, Supplemental Figure 2A)
PMID:21664573	FYPO:0002060	(Figure 1D, Supplemental Figure 2A)
PMID:21664573	FYPO:0002060	(Figure 1D, Supplemental Figure 2A)
PMID:21664573	FYPO:0002060	(Figure 1D, Supplemental Figure 2A)
PMID:21664573	PBO:0036897	(comment: CHECK in vitro) (Figure 1C, 2D)
PMID:21664573	PBO:0111958	(Fig. 1A)
PMID:21664573	PBO:0111957	(Fig. 1A)
PMID:21664573	PBO:0111956	(Fig. 1A)
PMID:21664573	FYPO:0002060	(Supplemental Figure 2B)
PMID:21664573	PBO:0036900	(Figure 5B)
PMID:21664573	PBO:0036900	(Figure 5B)
PMID:21664573	FYPO:0005726	(Figure 4E).
PMID:21664573	FYPO:0005726	(Figure 4E).
PMID:21664573	PBO:0105625	(Figure 5B)
PMID:21664573	PBO:0105624	(Figure 5B)
PMID:21664573	PBO:0036897	(Figure 5B)
PMID:21664573	PBO:0036897	(Figure 5B)
PMID:21664573	FYPO:0005728	(Fig. 4d) (comment: NORMAL SILENCING)
PMID:21664573	FYPO:0002060	(Supplemental Figure 2B)
PMID:21664573	FYPO:0002060	(Supplemental Figure 2B)
PMID:21664573	FYPO:0005726	(Fig. 2b, c)
PMID:21664573	FYPO:0005727	(Fig. 2b)
PMID:21664573	FYPO:0000168	(comment: CHECK ABOLISHED) Fig 2C
PMID:21664573	FYPO:0002061	(Fig. 3A) bub3 Δklp5 double mutants arrest as inviable micro-colonies of cells
PMID:21664573	FYPO:0001234	(Fig. 3a)
PMID:21664573	FYPO:0005727	(Fig. 3b)
PMID:21664573	FYPO:0005727	(Fig. 3b)
PMID:21664573	FYPO:0005727	(Fig. 3b)
PMID:21664573	FYPO:0005728	(Fig. 4c) (comment: NORMAL SILENCING)
PMID:21664573	FYPO:0005728	(Fig. 4d) (comment: NORMAL SILENCING)
PMID:21664573	FYPO:0002061	(Supplemental Figure 2B)
PMID:21676862	GO:0071933	(Fig. 1)
PMID:21693583	PBO:0102393	(Fig. 8B)
PMID:21693583	FYPO:0001234	(Fig. 8B)
PMID:21693583	PBO:0102392	(Fig. 8A)
PMID:2170029	FYPO:0002061	comment: CHECK temperature restrictive for dis2cs alone)
PMID:2170029	FYPO:0001234	(comment: CHECK high temp is permissive)
PMID:2170029	FYPO:0001234	comment: CHECK temperature restrictive for dis2cs alone)
PMID:2170029	FYPO:0001234	comment: CHECK temperature restrictive for dis2cs alone)
PMID:2170029	FYPO:0001234	comment: CHECK temperature restrictive for dis2cs alone)
PMID:2170029	FYPO:0001234	comment: CHECK temperature restrictive for dis2cs alone)
PMID:2170029	FYPO:0002061	comment: CHECK temperature restrictive for dis2cs alone)
PMID:2170029	PBO:0095579	(comment: CHECK standard temp is restrictive)
PMID:2170029	PBO:0095578	(comment: CHECK high temp is permissive)
PMID:2170029	FYPO:0006822	(comment: CHECK high temp is permissive)
PMID:21703453	PBO:0093464	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093464	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093464	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093464	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093464	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093464	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093464	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093464	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093464	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093464	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093464	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093464	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093465	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093465	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093465	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093465	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093465	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093464	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093465	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093465	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093465	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00047	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	PBO:0093465	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	GO:0051286	(comment: Requires auto-phosphorylation to be restricted to cell tips -not restricted to cell tips for Pom1-6A and Pom1-KD alleles)
PMID:21703453	GO:0005886	"recombinant Pom1 N-terminus (MBP-Pom11-699) was able to bind directly to several, but not all, negatively charged lipids, namely phosphatidylserine, phosphatidylinositol phosphates, and cardiolipin in a protein-lipid overlay assay (Figure 2D). Phosphatidylserine and phosphatidylinositol phosphates are components of the plasma membrane. Cardiolipin is mostly found in the inner mitochondrial membrane, and so it is unclear whether this interaction exists in vivo. We also note that, probably due to its high global positive charge (+15.5 for MBP-Pom11-699, +25 for Pom11-699 at pH 7), MBP-Pom11-699 bound the nitrocellulose membrane, resulting in significant background. Together, these experiments suggest that Pom1 directly associates with lipids at the plasma membrane through its basic region."""
PMID:21703453	MOD:00046	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	GO:0051285	(comment: Requires auto-phosphorylation to be restricted to cell tips -not restricted to cell tips for Pom1-6A and Pom1-KD alleles)
PMID:21703453	PBO:0096616	(comment: required for detachment from plasma membrane)
PMID:21703453	PBO:0096617	(comment: required for detachment from plasma membrane)
PMID:21703453	MOD:00046	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	GO:0051286	(comment: Requires auto-phosphorylation to be restricted to cell tips -not restricted to cell tips for Pom1-6A and Pom1-KD alleles)
PMID:2172964	FYPO:0000761	(comment: both partners cyr1delta)
PMID:21775631	PBO:0097865	(Figure S2B)
PMID:21775631	PBO:0101475	(Figure S2B)
PMID:21775631	PBO:0101474	(Figure S2A)
PMID:21775631	PBO:0101474	(Figure S2A)
PMID:21775631	PBO:0101474	(Figure S2A)
PMID:21775631	PBO:0100820	(Figure S2B)
PMID:21775631	FYPO:0001915	(Figure 1A, Figure 5D)
PMID:21811607	FYPO:0001460	(comment: basal transcription is meaningless because emm contains calcium)
PMID:21813639	PBO:0114929	(comment: CHECK candidate for involved_in_or_involved_in_regulation_of qualifier)
PMID:21828039	PBO:0113559	(Fig. 3)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0100415	(Fig. 4B)
PMID:21828039	PBO:0100415	(Fig. 4B)
PMID:21828039	PBO:0100415	(Fig. 4B)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0113560	(Fig. 4B)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0113558	(Fig. 3)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0113561	(Fig. 4G)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0108340	(Fig. 4G)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21828039	PBO:0092305	(Table 2)
PMID:21832151	PBO:0024920	(comment: endosomal localization requires F-actin -assayed using latrunculin A)
PMID:21847092	GO:0008270	(comment: bound by the C-terminal dsrbd domain)
PMID:21849474	FYPO:0006616	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0006617	(Fig. 1A)
PMID:21849474	FYPO:0006617	(Fig. 1A)
PMID:21849474	FYPO:0006617	(Fig. 1A,2A)
PMID:21849474	FYPO:0006617	(Fig. 1A)
PMID:21849474	FYPO:0006617	(Fig. 1A,2A)
PMID:21849474	FYPO:0006617	(Fig. 1A)
PMID:21849474	FYPO:0006617	Table 1A
PMID:21849474	FYPO:0006617	(Fig. 1A)
PMID:21849474	FYPO:0006617	(Fig. 1A)
PMID:21849474	FYPO:0006617	(Fig. 1A)
PMID:21849474	FYPO:0006616	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0006616	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0006616	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0006616	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0006616	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0006616	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0006616	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0006616	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0006616	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0002104	Table 1 (comment: CHECK wide phenotype suppressed by sorbitol)
PMID:21849474	FYPO:0006616	(Fig. 1B)
PMID:21849474	FYPO:0006616	(Fig. 1B)
PMID:21849474	FYPO:0006616	(Fig. 1B)
PMID:21849474	FYPO:0006616	(Fig. 1B)
PMID:21849474	FYPO:0006616	(Fig. 1B)
PMID:21849474	FYPO:0006616	(Fig. 1B)
PMID:21849474	FYPO:0006616	(Fig. 1B)
PMID:21849474	FYPO:0006616	(Fig. 1B)
PMID:21849474	PBO:0098568	(Fig. 4B)
PMID:21849474	FYPO:0006616	(Fig. 1B)
PMID:21849474	FYPO:0006616	(Fig. 1B)
PMID:21849474	GO:0031520	(Fig. 4B, 8) (comment: localisation is actin dependent)
PMID:21849474	GO:0031520	(Fig. 4B, 8) (comment: localisation is actin dependent)
PMID:21849474	GO:0097575	(Fig. 4A)
PMID:21849474	PBO:0098569	(Fig. 4C)
PMID:21849474	PBO:0098570	(Fig. 4D)
PMID:21849474	FYPO:0001293	(Fig. 2B)
PMID:21849474	PBO:0098571	(Fig. 5)
PMID:21849474	PBO:0098572	(Fig. 5)
PMID:21849474	PBO:0098573	(Fig. 5)
PMID:21849474	PBO:0098574	(Fig. 6A) (comment: CHECK fusion protein driven from nmt41 promoter)
PMID:21849474	PBO:0098575	(Fig. 6B) (comment: CHECK fusion protein driven from nmt41 promoter)
PMID:21849474	PBO:0098576	(Fig. 6C)
PMID:21849474	PBO:0098577	(Fig. 6C)
PMID:21849474	PBO:0098578	(Fig. 7A,B)
PMID:21849474	PBO:0098579	(Fig. 7A,B) localisation of rga4 by blt1+ is more extensive than wild type rga4 localisation but rescues the wide cell phenotype of the rga4 deletion
PMID:21849474	GO:0031520	(Fig. 9) (comment: cdc42-CRIB-GFP localisation is actin dependent and sensitive to low levels (10mM) Lat A)
PMID:21849474	FYPO:0006616	(Fig. 1B)
PMID:21849474	FYPO:0001293	(Fig. 2B)
PMID:21849474	FYPO:0006616	(Fig. 1A)
PMID:21849474	PBO:0098580	(Fig. 4D)
PMID:21849474	FYPO:0006616	(Fig. 3) (comment: CHECK no increase in cell width compared to single mutants)
PMID:21849474	PBO:0098565	(Figure 4A)
PMID:21849474	PBO:0098565	(Figure 4A)
PMID:21849474	PBO:0098566	(Figure 4A)
PMID:21849474	PBO:0098567	(Fig. 4B)
PMID:21849474	PBO:0098564	(Fig. 3) (comment: cell width is wider than either of the single mutants)
PMID:21849474	PBO:0098563	(Fig. 3) (comment: increased cell width compared to single mutants)
PMID:21849474	PBO:0098563	(Fig. 3) (comment: increased cell width compared to single mutants)
PMID:21849474	FYPO:0001294	(Fig. 2C)
PMID:21849474	FYPO:0001294	(Fig. 2C)
PMID:21885283	PBO:0107965	(Figure 3D)
PMID:21885283	PBO:0107962	(Figures 3B)
PMID:21885283	PBO:0107963	(Figure 3B)
PMID:21885283	FYPO:0005476	(Figure 3B)
PMID:21885283	PBO:0107962	(Figures 2L, S3P- S3R)
PMID:21885283	PBO:0107962	(Figures 2L, S3P- S3R)
PMID:21885283	FYPO:0000190	(Figures 2I - 2K and S3G - S3O)
PMID:21885283	FYPO:0000190	(Figures 2I - 2K and S3G - S3O)
PMID:21885283	GO:0072583	(Figure 2A)
PMID:21885283	GO:0072583	(Figure 2A)
PMID:21885283	FYPO:0000422	(Figure 2A)
PMID:21885283	FYPO:0000422	(Figure 2A)
PMID:21885283	FYPO:0002061	(Table II)
PMID:21885283	FYPO:0002061	(Table II)
PMID:21885283	FYPO:0000082	(Table II)
PMID:21885283	PBO:0107961	(Figure S1K)
PMID:21885283	PBO:0099724	(Figure S1K)
PMID:21885283	GO:0030139	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	PBO:0098289	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	PBO:0097713	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	PBO:0097713	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	PBO:0097629	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	PBO:0018345	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	PBO:0018345	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	PBO:0107960	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	PBO:0018844	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	PBO:0097713	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	PBO:0018470	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	PBO:0018844	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	PBO:0107960	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	PBO:0018844	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	FYPO:0002060	Table I
PMID:21885283	FYPO:0002060	Table I
PMID:21885283	FYPO:0002060	Table I
PMID:21885283	FYPO:0002060	Table I
PMID:21885283	FYPO:0002060	Table I
PMID:21885283	FYPO:0002060	Table I
PMID:21885283	GO:0034314	(Figure 2A)
PMID:21885283	PBO:0107966	(Figure 3G)
PMID:21885283	PBO:0107964	(Figure 3C)
PMID:21892171	PBO:0097401	Remarkably, loss of Cid14 subunit of TRAMP affects RNAi-independent heterochromatin formation in a manner similar to mlo3Δ. Loss of Cid14 restored H3K9me at otr1R::ura4+ and centromeric repeats in ago1Δ mutant (Fig. 4a-b).
PMID:21892171	PBO:0097401	In contrast, mlo3Δ resulted in considerable restoration of H3K9me at centromeres in clr3Δ ago1Δ cells (Fig. 3b).
PMID:21892171	PBO:0104709	Moreover, cid14Δ suppressed the silencing defect caused by ago1Δ, as indicated by reduction in the levels of dg/dh transcript in cid14Δ ago1Δ as compared to ago1Δ (Fig. 4c).
PMID:21892171	PBO:0108387	combining rrp6Δ with ago1Δ largely abolished H3K9me levels at otr1R::ura4+ and dg repeats (Fig. 5c).
PMID:21892171	PBO:0110865	However, we found that simultaneous deletion of mlo3 and ago1 restored Rik1 enrichment at cenH (Fig. 6b).
PMID:21892171	PBO:0108387	trs1delta failed to restore H3K9me at otr1R::ura4+ in clr3Δ ago1Δ cells (Fig. 3a).
PMID:21892171	PBO:0108387	trs1delta failed to restore H3K9me at otr1R::ura4+ in clr3Δ ago1Δ cells (Fig. 3a).
PMID:21892171	PBO:0104709	resulted in variegated suppression of silencing defects in ago1Δ and dcr1Δ mutants (Fig. 2b and Supplementary Fig. 2b)
PMID:21892171	FYPO:0004065	and changes in the distribution of RNAPII at body of genes (Supplementary Fig. 3c)
PMID:21892171	PBO:0110864	Mutant cells lacking SHREC subunit Clr3 show marked increase in RNAPII occupancy at centromeric repeats10,11,31
PMID:21892171	FYPO:0000084	Deletion of tfs1, which led to 6- azauracil (6-AU) sensitivity (Fig. 2a)
PMID:21892171	PBO:0093562	As expected, cells carrying ago1Δ or dcr1Δ showed severe sensitivity to TBZ, (Figure 1e)
PMID:21892171	FYPO:0006992	(Fig. 1a).
PMID:21892171	PBO:0105770	(comment: ***ABOLISHED*****) Whereas ago1Δ alleviated silencing of a ura4+ reporter inserted at an outer centromeric repeat region (otr1R::ura4+), simultaneous deletions of mlo3 and ago1 restored centromeric silencing (Fig. 1a). T
PMID:21892171	PBO:0104709	Whereas ago1Δ alleviated silencing of a ura4+ reporter inserted at an outer centromeric repeat region (otr1R::ura4+), simultaneous deletions of mlo3 and ago1 restored centromeric silencing (Fig. 1a). T
PMID:21892171	FYPO:0006992	(Supplementary Fig. 1)
PMID:21892171	FYPO:0006992	(Supplementary Fig. 1)
PMID:21892171	PBO:0093563	As expected, cells carrying ago1Δ or dcr1Δ showed severe sensitivity to TBZ, (Figure 1e)
PMID:21892171	PBO:0093563	As expected, cells carrying ago1Δ or dcr1Δ showed severe sensitivity to TBZ, (Figure 1e)
PMID:21892171	GO:0000791	As expected for a factor involved in mRNP formation26,30, Mlo3 interacted with a euchromatic gene (fbp1) transcript (Fig. 1f).
PMID:21892171	GO:0000775	Importantly, Mlo3 also interacted with dh transcript (Fig. 1f), consistent with results of ChIP analyses showing Mlo3 enrichment at transcribing centromeric repeats30.As expected for a factor involved in mRNP formation26,30, Mlo3 interacted with a euchromatic gene (fbp1) transcript (Fig. 1f).
PMID:21892171	PBO:0110863	Mutant cells lacking SHREC subunit Clr3 show marked increase in RNAPII occupancy at centromeric repeats10,11,31
PMID:21892171	FYPO:0003235	More importantly, mlo3Δ restored H3K9me and Swi6 localization at otr1R::ura4+ and endogenous centromeric repeats in ago1Δ mutant (Fig. 1 c-d)
PMID:21892171	PBO:0110862	More importantly, mlo3Δ restored H3K9me and Swi6 localization at otr1R::ura4+ and endogenous centromeric repeats in ago1Δ mutant (Fig. 1 c-d)
PMID:21892171	FYPO:0003235	More importantly, mlo3Δ restored H3K9me and Swi6 localization at otr1R::ura4+ and endogenous centromeric repeats in ago1Δ mutant (Fig. 1 c-d)
PMID:21892171	PBO:0104709	mlo3Δ also restored silencing and heterochromatin formation at centromeres in dcr1Δ mutant (Supplementary Fig. 2a).
PMID:21892183	PBO:0104112	(comment: CHECK microtubule sliding brake https://www.ebi.ac.uk/interpro/entry/InterPro/IPR007882/#PUB00070924)
PMID:21920317	PBO:0037711	(Fig. 1D) although sister kinetochore sometimes split, segregation ends up mostly normal
PMID:21920317	PBO:0109773	(Fig. 1D)
PMID:21920317	PBO:0037711	(Fig. 1D) although sister kinetochore split, segregation ends up mostly normal
PMID:21920317	PBO:0112502	(Fig. 1D)
PMID:21920317	FYPO:0003177	(Figure 1C, 1D) (comment: CHECK bipolar attachment of univalents)
PMID:21920317	FYPO:0005512	( Figure 1B) We found that virtually all rec12D cells (n = 240) eventually relocalized Ark1 to the spindle (Figure 1B), indicating that the SAC ultimately becomes satisfied in achiasmate meiosis.
PMID:21920317	PBO:0097907	( Figure 1B)
PMID:21920317	PBO:0035382	( Figure 1A) continuous rate of spindle elongation (I)
PMID:21920317	GO:0031619	(comment: prevents bipolar attachment)
PMID:21920317	GO:0031619	(comment: prevents bipolar attachment)
PMID:21920317	GO:0031619	(comment: prevents bipolar attachment (Ask Takeshi if this fits better rec role))
PMID:21920317	PBO:0112505	(comment: CHECK >inc merotelic kinetochore attachment)
PMID:21920317	PBO:0112504	(Fig. 4B)
PMID:21920317	FYPO:0005383	(Fig. 4A)
PMID:21920317	PBO:0109773	(Fig. 1D)
PMID:21920317	PBO:0035389	( Figure S3A)
PMID:21920317	PBO:0037712	( Figure 1A) phase II (metaphase) was substantially extended
PMID:21920317	PBO:0112503	(Fig. 1D)
PMID:21920317	PBO:0037711	(Fig. 1D) although sister kinetochore split, segregation ends up mostly normal
PMID:21920317	PBO:0112502	(Fig. 1D)
PMID:21920317	PBO:0109773	(Fig. 1D)
PMID:21920317	PBO:0112502	(Fig. 1D)
PMID:21920317	PBO:0097918	(Fig. 6)
PMID:21920317	PBO:0109779	(Fig. 4B)
PMID:21920317	PBO:0112506	(Fig. 4)
PMID:21931816	PBO:0099311	(comment: Ser-2 of the heptad repeat)
PMID:21945095	PBO:0100905	(comment: CHECK during mitotic DNA replication initiation)
PMID:21945095	PBO:0100905	(comment: CHECK during mitotic DNA replication initiation)
PMID:21945095	PBO:0100906	(comment: during replication fork processing)
PMID:21945095	PBO:0100906	(comment: during replication fork processing)
PMID:21945095	PBO:0100906	(comment: during replication fork processing)
PMID:21945095	PBO:0100905	(comment: CHECK during mitotic DNA replication initiation)
PMID:21945095	GO:0043596	(comment: delete if superseded; authors not sure if it's just a detection issue, but they don't see Rad4 moving away from origins as Mcm10 does)
PMID:21945095	GO:0031261	(comment: also inferred from interaction with Cdc23 and from timing of localization to chromatin at origins)
PMID:21945095	PBO:0100906	(comment: during replication fork processing)
PMID:21949882	GO:0016706	(comment: CHECK moved down from GO:0016706 30/8/2014 . activated_by(CHEBI:29033))
PMID:21965289	PBO:0035685	Since Δnsk1 Δdis2 double mutants displayed mitotic abnormalities, we chose Nsk1 for further analysis (Figure 1B).
PMID:21965289	GO:0008608	In the absence of Nsk1, some kinetochores become detached from spindle poles during anaphase B
PMID:21965289	PBO:0116211	To test whether Nsk1 is dephosphorylated by the proline-directed Cdc14- like phosphatase Clp1, cell cycle-dependent modification of Nsk1 was examined in nda3-KM311 nsk1-gfp clp1(C286S) cells, which express a substrate-trapping allele of Clp1 that binds, but does not release, its phosphosubstrates (Jia et al., 1995; Chen et al., 2008). In these cells, the proportion of faster-migrating Nsk1 increases only very slowly after release into anaphase, suggesting that Clp1 dephosphorylates Nsk1 (Figure 5, A and B). Consistent with this, we found that Clp1(C286S) coimmunoprecipitates with Nsk1 from cell lysates (Figure 5C)
PMID:21965289	PBO:0116232	To test whether Nsk1 is dephosphorylated by the proline-directed Cdc14- like phosphatase Clp1, cell cycle-dependent modification of Nsk1 was examined in nda3-KM311 nsk1-gfp clp1(C286S) cells, which express a substrate-trapping allele of Clp1 that binds, but does not release, its phosphosubstrates (Jia et al., 1995; Chen et al., 2008). In these cells, the proportion of faster-migrating Nsk1 increases only very slowly after release into anaphase, suggesting that Clp1 dephosphorylates Nsk1 (Figure 5, A and B). Consistent with this, we found that Clp1(C286S) coimmunoprecipitates with Nsk1 from cell lysates (Figure 5C)
PMID:21965289	GO:1902425	dis2 is required for the retreival of unclustered kinetochores in nsk delete (additive chromosome segregation defects)
PMID:21965289	PBO:0116231	In 9.0% of interphase Δnsk1 cells, one pair of sister kinetochores failed to cluster near the SPB during interphase (Figure 7A).
PMID:21965289	PBO:0116230	This strongly suggests that Nsk1 is required for accurate chromosome segregation, promoting the tethering of kinetochores to SPBs during anaphase B (see Discussion). In 9.0% of interphase Δnsk1 cells, one pair of sister kinetochores failed to cluster near the SPB during interphase (Figure 7A).
PMID:21965289	PBO:0107167	To our surprise, although loss of Msd1 or Alp7 had little or no effect on Nsk1 localization, we were unable to observe Nsk1 at the spindle pole in the absence of Dlc1 in fixed-cell preparations (Figure 6A).
PMID:21965289	PBO:0116229	During anaphase B, Nsk1 appears as two prominent dots that seem to colocalize with SPBs, before it returns to the nucleolus at the end of anaphase B, indicating that Nsk1 undergoes cell cycle-dependent changes in its localization (Figure 2A). (vw Plus that it is at the SPB-kinetochore interface)
PMID:21965289	PBO:0033360	During prometaphase and metaphase, Nsk1 localizes broadly throughout the nucleoplasm, suggesting it is released from the nucleolus at the G2/M transition (Figure 2A).
PMID:21965289	PBO:0018823	We found that Nsk1 localizes predominantly in the nucleolus during interphase, as judged by colocalization with fission yeast fibrillarin, Fib1 (Beauregard et al., 2009; Figures 2A and S3A).
PMID:21965289	FYPO:0005362	Whereas cells lacking Nsk1 displayed no defect in kinetochore retrieval, cells lacking either Dis2 or Dam1 were substantially impaired (Figure 8D).
PMID:21965289	PBO:0116231	Similar results were obtained when kinetochore position was assessed with other GFP-tagged kinetochore proteins and in clp1(C286S) mutant, in which relocalization of Nsk1 to the kinetochore-SPB junction is impaired (Figure S6A).
PMID:21965289	PBO:0116242	These data indicate that Nsk1 is phosphorylated by Cdk1/Cdc2 kinase on multiple sites in early mitosis, and this prevents Nsk1 localization to the spindle and kinetochore-SPB interface until it is dephosphorylated by Clp1 at anaphase onset.
PMID:21965289	PBO:0116241	FIGURE 5: Dephosphorylation of Nsk1 by Clp1 promotes its association to the kinetochore-SPB junction.
PMID:21965289	PBO:0116240	Nevertheless, the chromosome loss rate was considerably worse in Δnsk1 Δmad2 cells than in Δnsk1 single mutant (Table 1).
PMID:21965289	PBO:0116239	(Table 1).
PMID:21965289	PBO:0116238	(Table 1).
PMID:21965289	PBO:0116237	Nevertheless, the chromosome loss rate was considerably worse in Δnsk1 Δmad2 cells than in Δnsk1 single mutant (Table 1).
PMID:21965289	PBO:0116237	Nevertheless, the chromosome loss rate was considerably worse in Δnsk1 Δmad2 cells than in Δnsk1 single mutant (Table 1).
PMID:21965289	FYPO:0002060	Indeed, we found that Δdis2, but not Δnsk1, mutants suppress the proliferation defect of a temperature-sensitive ark1-T7 mutant, indicating that Nsk1 does not counteract Ark1 function (Figure S2B)
PMID:21965289	FYPO:0002060	Indeed, we found that Δdis2, but not Δnsk1, mutants suppress the proliferation defect of a temperature-sensitive ark1-T7 mutant, indicating that Nsk1 does not counteract Ark1 function (Figure S2B)
PMID:21965289	FYPO:0002061	Indeed, we found that Δdis2, but not Δnsk1, mutants suppress the proliferation defect of a temperature-sensitive ark1-T7 mutant, indicating that Nsk1 does not counteract Ark1 function (Figure S2B)
PMID:21965289	FYPO:0002061	Indeed, we found that Δdis2, but not Δnsk1, mutants suppress the proliferation defect of a temperature-sensitive ark1-T7 mutant, indicating that Nsk1 does not counteract Ark1 function (Figure S2B)
PMID:21965289	PBO:0116236	(Figure S2A).
PMID:21965289	PBO:0116235	To distinguish between these possibilities, we monitored Cdc13 (Cyclin B) destruction in single cells following chemical inactivation of Ark1 (Aurora B) kinase in mitotically arrested nda3- KM311 cells. The nda3-KM311 allele encodes a cold-sensitive β-tubulin protein that causes cells to arrest in mitosis at 18°C with no microtubules (Hiraoka et al., 1984). We found that loss of nsk1 had no effect in this assay, indicating that Nsk1 is not required to silence the SAC (Figure S2A).
PMID:21965289	FYPO:0006917	The delay in anaphase onset observed in Δnsk1 cells is abolished by deletion of either mad2 or mad3, indicating that this is due either to activation of, or failure to silence, the SAC (Figure 1E).
PMID:21965289	FYPO:0006917	The delay in anaphase onset observed in Δnsk1 cells is abolished by deletion of either mad2 or mad3, indicating that this is due either to activation of, or failure to silence, the SAC (Figure 1E).
PMID:21965289	FYPO:0000141	Nevertheless, we found that both Δnsk1 and Δdis2 cells missegregate chromosome 1, and that this is exacerbated in Δnsk1 Δdis2 double mutants (Figure 1C).
PMID:21965289	FYPO:0000141	Nevertheless, we found that both Δnsk1 and Δdis2 cells missegregate chromosome 1, and that this is exacerbated in Δnsk1 Δdis2 double mutants (Figure 1C).
PMID:21965289	PBO:0116234	We found that both Δnsk1 and Δdis2 cells are delayed in the timing of anaphase onset and that this effect is exacerbated in Δnsk1 Δdis2 double mutants (Figure 1D).
PMID:21965289	PBO:0116234	We found that both Δnsk1 and Δdis2 cells are delayed in the timing of anaphase onset and that this effect is exacerbated in Δnsk1 Δdis2 double mutants (Figure 1D).
PMID:21965289	PBO:0116233	We found that both Δnsk1 and Δdis2 cells are delayed in the timing of anaphase onset and that this effect is exacerbated in Δnsk1 Δdis2 double mutants (Figure 1D).
PMID:21979813	PBO:0096915	(Fig. 4E) (comment: CHECK decreased kinetochore mono orientation at meiosis I)
PMID:21979813	PBO:0096911	(Fig. 2C)
PMID:21979813	PBO:0096915	(Fig. 4E) (comment: CHECK decreased kinetochore mono orientation at meiosis I)
PMID:21979813	PBO:0096915	(Fig. 4E) (comment: CHECK decreased kinetochore mono orientation at meiosis I)
PMID:21979813	PBO:0096914	(Fig. 4A, 4B)
PMID:21979813	PBO:0096912	(Fig. 2C)
PMID:21979813	PBO:0096911	(Fig. 2C)
PMID:21979813	PBO:0096909	(Fig. 1B)
PMID:21979813	FYPO:0000209	(Fig. 2B) (comment: CHECK abolished mono orientation at meiosis I)
PMID:21979813	FYPO:0000209	(Fig. 2B) (comment: CHECK abolished kinetochore mono orientation at meiosis I)
PMID:21979813	PBO:0096911	(Fig. 2C)
PMID:21981922	PBO:0110275	however, depletion of Mtr4 in the pab2D strain increased the levels of rpl30-2 mRNA and pre-mRNA compared to the single pab2D strain (Figure 2D, compare lanes 4 and 8).
PMID:21981922	FYPO:0002926	Similarly, a Pab2 variant in which the 11 arginine residues within the arginine/glycine-rich domain were substituted to alanine (R-to-A) showed no poly(A) binding (Figure S3)
PMID:21981922	PBO:0110273	specific to one of the two rpl30 paralogs, as the expression of rpl30-1 was unchanged in pab2D cells (Figure 1A).
PMID:21981922	PBO:0110274	Interestingly, the intronless rpl30-2 construct resulted in increased levels of mRNA relative to the intron-containing construct (Figure 1B, lanes 1 and 4); yet, mRNA levels were not increased in the pab2D strain when rpl30-2 was expressed from the intronless construct (Figure 1B, lanes 4 and 5, and Figure 1C).
PMID:21981922	PBO:0110275	Northern blot analysis of RNA prepared from the rrp6D strain revealed robust upregulation of rpl30-2 mRNA and pre-mRNA, 5- and 18-fold, respectively (Figure 2A, lane 7, and Figures 2B and 2C)
PMID:21981922	PBO:0110276	whereas rpl30-2 mRNA and pre-mRNA were upregulated 1.5- and 3.5- fold, respectively, using RNA from the dis3 mutant (Figure 2A, lane 5, and Figures 2B and 2C).
PMID:21981922	PBO:0110275	rpl30-2 mRNA and pre-mRNA were higher in the pab2D dis3-54 double-mutant strain compared to the single dis3-54 mutant (Figure 2A, compare lanes 5 and 6, and Figures 2B and 2C).
PMID:21981922	PBO:0110275	In contrast, no cumulative increase in the levels of rpl30-2 transcripts was observed in the pab2D rrp6D double-mutant strain relative to the single rrp6D strain (Figure 2A, lanes 7 and 8, and Figures 2B and 2C).
PMID:21981922	PBO:0110274	primarily mediated in the nucleus, as the deletion of ski7, which encodes a cytosolic-specific exosome cofactor, did not perturb rpl30-2 expression (Figure 2A, lane 9, and Figures 2B and 2C).
PMID:21981922	PBO:0110274	Analysis of RNA from cid14D cells showed normal levels of rpl30-2 pre-mRNA and mRNA (Figure 2A, lane 3, and Figures 2B and 2C)
PMID:21981922	PBO:0110275	However, the deletion of cid14 in the pab2D strain increased the levels of rpl30-2 mRNA and pre-mRNA compared to the single pab2D strain (Figure 2A, compare lanes 2 and 4).
PMID:21981922	PBO:0110274	Similar results were obtained with a conditional strain in which the genomic copy of mtr4 is expressed from the thiamine-sensitive nmt1+ promoter: depletion of Mtr4 did not affect rpl30-2 premRNA and mRNA levels (Figure 2D, compare lanes 3 and 7)
PMID:21981922	PBO:0110272	RNA level expressed from the ribosomal protein-coding gene, rpl30-2, was increased by 4.5-fold in the absence of Pab2 (Lemay et al., 2010). To independently validate this result, we compared rpl30-2 mRNA levels between wild-type and pab2D strains by northern analysis and confirmed a 3-fold increase of rpl30-2 mRNA in pab2 null cells (Figure 1A, lanes 1 and 2). The use of an intron-specific probe confirmed that the slowermigrating rpl30-2 transcript is the unspliced pre-mRNA (Figure 1A, lane 4).
PMID:21981922	PBO:0110274	Consistent with this, rpl30-2 expression levels were unaffected in the rrp6D strain when rpl30-2 was expressed from the intronless construct (Figure 1B, lanes 4 and 6), similar to results using the pab2D mutant (Figure 1B, lane 5).
PMID:21981922	PBO:0110277	In contrast, the expression of nonpolyadenylated rpl30-2 from the ribozyme construct was largely insensitive to Pab2- and Rrp6-dependent degradation (Figure 3C, lanes 4-6).
PMID:21981922	PBO:0110278	In agreement with the direct role of Rpl30-1 in the control of rpl30-2 expression, excess Rpl30-1 resulted in decreased levels of rpl30-2 mRNA (Figure 6D, lane 4).
PMID:21981922	PBO:0110284	Strikingly, we noted a 6-fold decrease in the percentage of unspliced rpl30-2 transcript in the absence of Rpl30-1 relative to the wild-type (Figure S5A)
PMID:21981922	PBO:0110278	If negative control of pre-mRNA decay is mainly responsible for the upregulation of rpl30-2 after heat shock, we predicted that rpl30-2 expression from the intronless construct, which is insensitive to Pab2/Rrp6-mediated pre-mRNA decay (Figures 1B and 1C), would not respond to heat stress. Accordingly, a wild-type strain that expressed the intronless version of rpl30-2 showed no increase in mRNA levels after heat shock (Figure 4C, lanes 1 and 2, and Figure 4D).
PMID:21981922	PBO:0110278	RNA level expressed from the ribosomal protein-coding gene, rpl30-2, was increased by 4.5-fold in the absence of Pab2 (Lemay et al., 2010). To independently validate this result, we compared rpl30-2 mRNA levels between wild-type and pab2D strains by northern analysis and confirmed a 3-fold incemperature-dependent upregulation of rpl30-2 required Pab2, as it was not observed in a pab2D strain that is defective in pre-mRNA decay (Figure 4A, lanes 3 and 4, and Figure 4B).
PMID:21981922	PBO:0092053	we found a 2-fold increase in rpl30-2 mRNA levels after shifting cells growing at 25C to 37C (Figure 4A, lanes 1 and 2, and Figure 4B).
PMID:21981922	PBO:0110272	Importantly, Pab2 variants F75R and R-to-A did not rescue the increased levels of rpl30-2 transcripts observed in the pab2D strain (Figure 3E, lanes 2-4), although the two Pab2 variants defective in poly(A) binding were expressed at levels similar to wild-type Pab2 (Figure 3F).
PMID:21981922	PBO:0110272	Importantly, Pab2 variants F75R and R-to-A did not rescue the increased levels of rpl30-2 transcripts observed in the pab2D strain (Figure 3E, lanes 2-4), although the two Pab2 variants defective in poly(A) binding were expressed at levels similar to wild-type Pab2 (Figure 3F).
PMID:21981922	FYPO:0002926	the ability of Pab2 to bind a poly(A) substrate was completely lost after the substitution of a conserved phenylalanine (F75R) residue within the RNA recognition motif of Pab2 (Figures S3C and S3D).
PMID:22017871	PBO:0104135	(comment: al: ubiquitin dependent due to need for rhp6)
PMID:22017871	PBO:0104138	(Fig. 7c)
PMID:22017871	PBO:0104136	(comment: al: ubiquitin dependent due to need for rhp6)
PMID:22017871	PBO:0104135	(comment: al: ubiquitin dependent due to need for rhp6)
PMID:22024164	FYPO:0002061	(comment: CONDITION 30 degrees)
PMID:22024164	FYPO:0001249	(comment: early-firing origins; HU absent)
PMID:22024164	FYPO:0001249	(comment: at late-firing or dormant origins)
PMID:22024164	FYPO:0001387	"(comment: 30 degrees, ""high"" compared to 25 degrees)"
PMID:22024164	FYPO:0001250	(comment: assayed using ars2004; not abolished as in hsk1delta alone (but single mutant not shown))
PMID:22024164	FYPO:0001250	(comment: assayed using ars2004; not abolished as in hsk1delta alone (but single mutant not shown))
PMID:22024164	FYPO:0001249	(comment: at late-firing or dormant origins; genome-wide detection)
PMID:22024164	FYPO:0001357	(comment: actually 25 degrees, but calling it low to make distinction from inviable at 30)
PMID:22024164	FYPO:0002061	(comment: 30 degrees)
PMID:22024167	PBO:0095671	(comment: >50% activity)
PMID:22033972	GO:0032798	(comment: structure)
PMID:2203537	PBO:0037182	(comment: 30% at 120 min. (archery bow))
PMID:2203537	PBO:0035360	(comment: 85% at 160 min)
PMID:2203537	PBO:0098343	(Figure 3A)
PMID:2203537	PBO:0035363	(Figure 3A)
PMID:2203537	PBO:0105792	(Figure 3A)
PMID:22042620	FYPO:0002328	(Fig. S5B)
PMID:22042620	FYPO:0002328	(Fig. S5B)
PMID:22042620	FYPO:0002328	(Fig. S5B)
PMID:22042620	GO:0006643	(Fig. 7)
PMID:22042620	FYPO:0000338	(Fig. S5B)
PMID:22042620	GO:0090307	(comment: not required after insertion)
PMID:22042620	FYPO:0007426	(Fig. 3, S3) for comparative images of an inserted pro-metaphase wild-type SPB, see Fig. S1 B
PMID:22042620	PBO:0104497	(Fig. S2, B and C)
PMID:22042620	FYPO:0002237	(Fig. S5B)
PMID:22042620	FYPO:0000135	(Fig. 7) (comment: indicated by NDB cholesterol)
PMID:22042620	GO:0006998	(Fig. 7)
PMID:22042620	GO:0006998	(Fig. 7)
PMID:22042620	FYPO:0002328	(Fig. S5B)
PMID:22042620	FYPO:0002237	(Fig. S5B)
PMID:22042620	PBO:0104497	(Fig. 1, A and B)
PMID:22042869	PBO:0112929	(Fig. 2B)
PMID:22042869	PBO:0113776	(Fig. 3B)
PMID:22042869	PBO:0113776	Abp1 is localized at the swi2 promoter (Fig. 6A), in addition to its localization at LTRs.
PMID:22042869	PBO:0106419	Abp1 is localized at the swi2 promoter (Fig. 6A), in addition to its localization at LTRs.
PMID:22042869	PBO:0113782	(Fig. 6A and B)
PMID:22042869	PBO:0113783	(Fig. 6A)
PMID:22042869	PBO:0113784	(Fig. 6C)
PMID:22042869	PBO:0113785	Abp1 bound to the swi2 promoter region facilitates preferential targeting of Mc, which normally binds an M-box sequence motif to activate M-specific genes
PMID:22042869	FYPO:0000472	(Fig. 2A)
PMID:22042869	FYPO:0000472	(Fig. 2A)
PMID:22042869	PBO:0112929	(Fig. 2B)
PMID:22042869	PBO:0112929	(Fig. 2A and B)
PMID:22042869	PBO:0112929	(Fig. 2A)
PMID:22042869	PBO:0113777	(Fig. 3B)
PMID:22042869	PBO:0113778	(Fig. 3B)
PMID:22042869	PBO:0113779	(Fig. 3B)
PMID:22042869	PBO:0106419	Several Mc peaks correspond to WTF (With Tf) elements on chromosome 3 and solo LTRs dispersed across the genome (Fig. 3).
PMID:22042869	PBO:0113780	(Fig. 4A)
PMID:22042869	PBO:0113781	(Fig. 4B)
PMID:22042869	PBO:0112663	(Fig. 5)
PMID:22064476	FYPO:0003244	tested using several genes, and reporter construct to test mutations at or near splice sites
PMID:22081013	PBO:0107598	In marked contrast, subtelomeric tlh transcripts (Figure 3a) accumulated in chp1ΔC strains (Figure 3b,e Supplementary Figure 9).
PMID:22081013	FYPO:0003412	(Fig. 3g)
PMID:22081013	PBO:0107597	(Fig. 3f)
PMID:22081013	PBO:0107598	(Fig. 3f) In marked contrast, subtelomeric tlh transcripts (Figure 3a) accumulated in chp1ΔC strains (Figure 3b,e Supplementary Figure 9).
PMID:22081013	PBO:0107597	Real time PCR analyses of transcripts derived from the dg or dh outer repeats of the centromere (Figure 3a) demonstrated that whereas cells lacking Chp1 displayed strong accumulation of transcripts, centromeric heterochromatin was unaffected by the loss of the PIN domain in chp1ΔC strains (Figure 3b,c,d Supplementary Figure 9).
PMID:22084197	GO:0006284	(comment: CHECK FYPO:0007229)
PMID:22085934	PBO:0095398	(Supplementary Figure S8C
PMID:22085934	GO:0005515	We used Dcp2 constructs of increasing length (Figure 1D) and found that a Dcp2 region located between residues 255 and 266 is required for the interaction with Edc3 (Figure 1D, lane 3 versus lanes 1 and 2). B
PMID:22085934	GO:0005515	In summary, our data show that the Edc3 and Scd6 LSm domains compete for the same Dcp2- binding motifs and that both interactions are mutually exclusive
PMID:22085934	PBO:0095396	(Figure 6A)
PMID:22093869	FYPO:0003928	(comment: The phenotype is assessed by the high-throughput sequencing)
PMID:22093869	FYPO:0003928	(comment: The phenotype is assessed by the high-throughput sequencing)
PMID:22093869	FYPO:0003928	(comment: The phenotype is assessed by the high-throughput sequencing)
PMID:22093869	FYPO:0003928	(comment: The phenotype is assessed by the high-throughput sequencing)
PMID:22119525	FYPO:0001226	(Fig. 2A)
PMID:22132152	PBO:0107590	(Fig. 6)
PMID:22132152	PBO:0107591	(Fig. 6)
PMID:22132152	PBO:0096345	(Fig. 8) (comment: CHECK increased calcinurin activity)
PMID:22132152	GO:0005789	in agreement, the corresponding fractions 15-22 isolated from the fission yeast strain expressing GFP-tagged Cta4p were immuno-reactive with anti-GFP antibodies
PMID:22132152	FYPO:0006706	(Fig. 2)
PMID:22132152	FYPO:0006707	(Fig. 2,4)
PMID:22132152	FYPO:0001198	(Fig. 1,7)
PMID:22132152	FYPO:0000843	(Fig. 5)
PMID:22132152	PBO:0107589	(Fig. 6)
PMID:22132152	FYPO:0001457	(Fig. 5)
PMID:22134091	FYPO:0000276	(Fig. S1B-j)
PMID:22134091	FYPO:0003307	(comment: 22.3%)
PMID:22134091	FYPO:0006180	(Fig. 1c)
PMID:22134091	FYPO:0000964	(Fig. S2)
PMID:22134091	PBO:0100712	(Fig. 2B)
PMID:22134091	PBO:0100713	(Fig. 2A,B)
PMID:22134091	PBO:0100714	(Fig. 2)
PMID:22134091	FYPO:0000274	(Fig. S3A)
PMID:22134091	FYPO:0000903	(Fig. 3)
PMID:22134091	FYPO:0000903	(Fig. 3)
PMID:22134091	FYPO:0001943	(comment: increased affinity)
PMID:22134091	FYPO:0002636	(Fig. 7F)
PMID:22134091	FYPO:0002636	(Fig. 7F)
PMID:22140232	PBO:0102612	(comment: same as ssp2delta alone)
PMID:22140232	FYPO:0005742	(comment: same as ssp2delta alone)
PMID:22140232	PBO:0102621	(comment: OK, this MF is a stretch, but based on everything we know phenotypes, export of phosphorylated -typical TF regulation, ortholog etc, I'm confident these phenotypes can be used with curator knowledge to infer this._
PMID:22140232	PBO:0102616	(comment: same as ssp2delta alone)
PMID:22140232	PBO:0102610	(comment: same as ssp2delta alone)
PMID:22140232	PBO:0102611	(comment: same as ssp2delta alone)
PMID:22140232	FYPO:0001176	(comment: same as ssp2delta alone)
PMID:22140232	PBO:0093796	(comment: same as ssp2delta alone)
PMID:22140232	PBO:0093796	(comment: same as ssp2delta alone)
PMID:22140232	PBO:0102609	(comment: ssp2 inferred from mutant phenotype)
PMID:22140232	PBO:0038094	(Fig. 2A). We found that Ssp2-GFP mainly localized in the nucleus both in glucose-starved cells and in cells grown in glucose-rich medium
PMID:22140232	PBO:0020037	(Fig. 2A). We found that Ssp2-GFP mainly localized in the nucleus both in glucose-starved cells and in cells grown in glucose-rich medium
PMID:22144463	GO:1902794	(comment: CHECK during vegetative growth, near genes normally expressed in meiotic cell cycle)
PMID:22144463	PBO:0103485	Deletion of sir2 encoding a nicotinamide adenine dinucleotide- dependent HDAC (3) caused defective H3K9me at the majority of islands (fig. S5A), but SHREC subunits were dispensable (fig. S5B).
PMID:22144463	FYPO:0007530	Insertion of the mei4 DSR at the 3′ untranslated region of ura4 resulted in H3K9me at this site, especially when ura4-DSR was expressed (Fig. 2C), and ssm4 lacking its DSR failed to nucleate H3K9me (fig. S8).
PMID:22144463	PBO:0103484	The loss of Dicer (Dcr1) or Argonaute (Ago1) caused only partial or no reduction in H3K9me at heterochromatin islands except island 5, which showed considerable reduction of H3K9me (fig. S4, A and B). . Moreover, de novo targeting of H3K9me to ssm4 and mei4 occurred even in the absence of Ago1, albeit at levels lower than those of the wild type (fig. S4C), suggesting that additional RNAi-independent mechanism(s) target heterochromatin to meiotic loci. W
PMID:22144463	GO:1902801	(comment: CHECK negative ::)
PMID:22144463	GO:1902794	(comment: CHECK during vegetative growth, near genes normally expressed in meiotic cell cycle)
PMID:22144909	PBO:0106387	(comment: CHECK serine 2)
PMID:22172946	PBO:0037494	(Fig. 2)
PMID:22172946	PBO:0093678	(Fig. 1a)
PMID:22172946	PBO:0037495	(Fig. 3)
PMID:22172946	PBO:0093678	(Fig. 1a)
PMID:22172946	PBO:0037494	(Fig. 2)
PMID:22173095	PBO:0102374	(Fig. 7) (comment: sdj mutant is unstable)
PMID:22173095	PBO:0102372	(comment: CHECK abolished homodimerization) Fig. 6
PMID:22173095	PBO:0102373	(Fig. 7)
PMID:22173095	PBO:0102374	(Fig. 7) (comment: sdj mutant is unstable)
PMID:22180499	FYPO:0003335	(comment: CHECK flocculation inhibited by galactose)
PMID:22184248	FYPO:0002060	(Figure 1a)
PMID:22184248	FYPO:0002061	(Fig. 1a)
PMID:22184248	FYPO:0002061	(Fig. 1a)
PMID:22184248	FYPO:0006917	It failed to cause an arrest in a strain lacking mad2+, indicating that the arrest was due to activation of the spindle checkpoint.
PMID:22184248	FYPO:0000620	When Mad2 was turned on, the index of the chromosome condensation gradually increased from 0 to more than 50%. Binucleate cells, which passed through anaphase, however, did not increase. These results indicated that when Mad2 was turned on, the cells, which were initially at the boundary of G2/M, were arrested before anaphase (Fig. 5B).
PMID:22184248	FYPO:0000620	(Fig. 1B) As shown in Fig. 1B, when Mph1-KD was expressed from pREP41, it caused a weak growth inhibition, which was partially relieved by deletion of mad2+ or mph1+, indicating that expression of Mph1-KD from pREP41 caused a weak delay in mitotic progression as well as a growth defect for a reason unrelated to the checkpoint activation. We speculate that partially degraded Mph1-KD proteins (Fig. S2B) might be toxic to some extent.
PMID:22184248	FYPO:0002638	We also examined localization of Mad2. Mad2 remained on kinetochores in more than 80% of the cells, indicating that the spindle checkpoint was kept active (Fig. S1 B and C)
PMID:22184248	FYPO:0002060	(Figure 1a)
PMID:22184248	FYPO:0001234	(Fig. 1B) As shown in Fig. 1B, when Mph1-KD was expressed from pREP41, it caused a weak growth inhibition, which was partially relieved by deletion of mad2+ or mph1+, indicating that expression of Mph1-KD from pREP41 caused a weak delay in mitotic progression as well as a growth defect for a reason unrelated to the checkpoint activation. We speculate that partially degraded Mph1-KD proteins (Fig. S2B) might be toxic to some extent.
PMID:22184248	FYPO:0002060	(Figure 1a)
PMID:22184248	FYPO:0002060	(Figure 1a)
PMID:22184248	FYPO:0000620	As shown in Fig. 3A, expression of Mph1-Ndc80-GFP from pREP81 caused an arrest in the wild-type background.
PMID:22184248	FYPO:0000620	As shown in Fig. 3A, expression of Mph1-Ndc80-GFP from pREP81 caused an arrest in the wild-type background.
PMID:22184248	FYPO:0000620	(Fig. 1B) As shown in Fig. 1B, when Mph1-KD was expressed from pREP41, it caused a weak growth inhibition, which was partially relieved by deletion of mad2+ or mph1+, indicating that expression of Mph1-KD from pREP41 caused a weak delay in mitotic progression as well as a growth defect for a reason unrelated to the checkpoint activation. We speculate that partially degraded Mph1-KD proteins (Fig. S2B) might be toxic to some extent.
PMID:22235339	PBO:0103125	(comment: also assayed using bulk histones from calf thymus)
PMID:22235339	PBO:0103124	(comment: also assayed using bulk histones from calf thymus)
PMID:22235339	PBO:0103123	(comment: also assayed using bulk histones from calf thymus)
PMID:22267499	FYPO:0006802	(Figure 4b)
PMID:22267499	GO:0031029	These data therefore implicate Ypa2p and Ppa2p in establishing SIN protein asymmetry during anaphase.
PMID:22267499	GO:0031029	Together, these data lead us to conclude that Ypa2p is involved in determining the timing of mitotic commitment, establishing cell morphology, positioning of the division site, regulation of the SIN, and in completion of cytokinesis.
PMID:22267499	FYPO:0004103	(Figure 4b)
PMID:22267499	FYPO:0004103	(Figure 4b)
PMID:22267499	FYPO:0000648	(Figure 4b)
PMID:22267499	FYPO:0000648	(Figure 4b)
PMID:22267499	FYPO:0000648	(Figure 4b)
PMID:22267499	FYPO:0006802	(Figure 4b)
PMID:22267499	FYPO:0006802	(Figure 4b)
PMID:22267499	FYPO:0000648	(Figure 4b)
PMID:22267499	PBO:0111480	(Table 2)
PMID:22267499	PBO:0111479	(Table 2)
PMID:22267499	PBO:0111478	(Table 3)
PMID:22267499	PBO:0111477	(Table 3)
PMID:22267499	PBO:0111476	(Table 3)
PMID:22267499	PBO:0111475	(Table 3)
PMID:22267499	PBO:0111474	(Table 3)
PMID:22267499	FYPO:0002280	The double mutant wee1-50 ypa2-D was synthetically lethal, with the germinating spore giving rise to one or two small, rounded cells at 29 (DNS)
PMID:22267499	FYPO:0002061	The double mutant wee1-50 ypa2-D was synthetically lethal, with the germinating spore giving rise to one or two small, rounded cells at 29 (DNS)
PMID:22267499	FYPO:0000648	Measurement of ypa2-D cells revealed that they divide at a reduced cell length at both the permissive and restrictive temperatures, similar to ppa2-D (Table 2).
PMID:22267499	GO:0005737	Both the GFP-Ypa1p and GFP-Ypa2p proteins showed a uniform cytoplasmic localization and a faint nuclear signal.
PMID:22267499	GO:0005737	Both the GFP-Ypa1p and GFP-Ypa2p proteins showed a uniform cytoplasmic localization and a faint nuclear signal.
PMID:22267499	PBO:0094648	(Figure 1A)
PMID:22267499	PBO:0094648	(Figure 1A)
PMID:22267499	FYPO:0001357	(Figure 1A)
PMID:22267499	FYPO:0001357	(Figure 1A)
PMID:22267499	PBO:0095634	(Figure 1A)
PMID:22267499	FYPO:0002061	(Figure 1A)
PMID:22267499	FYPO:0002061	The double mutant ppa2-6 ppa1-D was synthetically lethal (Table 4), even when tetrads were dissected at 36 and 32, the permissive temperature for ppa2-6.
PMID:22267499	FYPO:0002061	The double mutant ppa2-6 ppa1-D was synthetically lethal (Table 4), even when tetrads were dissected at 36 and 32, the permissive temperature for ppa2-6.
PMID:22267499	PBO:0111473	(Table 3)
PMID:22267499	FYPO:0002061	The double mutant ppa2-6 ppa1-D was synthetically lethal (Table 4), even when tetrads were dissected at 36 and 32, the permissive temperature for ppa2-6.
PMID:22267499	FYPO:0002061	The double mutant ppa2-6 ppa1-D was synthetically lethal (Table 4), even when tetrads were dissected at 36 and 32, the permissive temperature for ppa2-6.
PMID:22267499	FYPO:0002430	ppa2-6 is cold sensitive and undergoes only a few divisions after a shift to 19 (Table S1, Figure 1, A and B).
PMID:22267499	FYPO:0002061	ppa2-6 is cold sensitive and undergoes only a few divisions after a shift to 19 (Table S1, Figure 1, A and B).
PMID:22268381	PBO:0096783	localization of Dcr1-GFP and GFP-Ago1 was not affected by the loss of Sal3 activity (Figure S1).
PMID:22268381	FYPO:0000091	(Fig. 4)
PMID:22268381	PBO:0096785	(Fig. 5)
PMID:22268381	FYPO:0001513	(Fig. 5)
PMID:22268381	PBO:0096786	(Fig. 5)
PMID:22268381	FYPO:0003094	Moreover, expression of the Rdp1-SV40-NLS construct appeared to suppress centromeric transcript levels below that those found in wild type
PMID:22268381	FYPO:0003094	Moreover, expression of the Rdp1-SV40-NLS construct appeared to suppress centromeric transcript levels below that those found in wild type
PMID:22268381	PBO:0096784	onsistent with the scenario in which Rdp1 is a cargo for Sal3, we were able to detect stable interaction between tagged Rdp1 and Sal3 by co-immunoprecipitation (Figure 2B).
PMID:22268381	FYPO:0000220	Pericentric transcript levels are increased in sal3 mutants
PMID:22268381	FYPO:0000091	(Fig. 4)
PMID:22268381	PBO:0096787	(Fig. 5)
PMID:22268381	PBO:0096781	GFP-Rdp1 was not detected in the nuclei of most cells (Figure 1B).
PMID:22268381	PBO:0096781	GFP-Rdp1 was not detected in the nuclei of most cells (Figure 1B).
PMID:22268381	PBO:0096782	localization of Dcr1-GFP and GFP-Ago1 was not affected by the loss of Sal3 activity (Figure S1).
PMID:22279046	FYPO:0000268	(comment: same as hsk1-89 alone)
PMID:22279046	FYPO:0001249	(comment: same as hsk1-89 alone)
PMID:22279046	FYPO:0000085	(comment: same as hsk1-89 alone)
PMID:22279046	FYPO:0000088	(comment: same as hsk1-89 alone)
PMID:22279046	FYPO:0000268	(comment: same as hsk1-89 alone)
PMID:22279046	FYPO:0000089	(comment: same as hsk1-89 alone)
PMID:22279046	FYPO:0000085	(comment: same as hsk1-89 alone)
PMID:22279046	FYPO:0000089	(comment: same as hsk1-89 alone)
PMID:22279046	FYPO:0000088	(comment: same as hsk1-89 alone)
PMID:22291963	PBO:0097785	(comment: CHECK mild expressivity)
PMID:22291963	GO:0005634	(comment: CHECK in asf1-33 at higher temperature)
PMID:22292001	PBO:0093557	(Figure 5)
PMID:22292001	PBO:0093558	(Figure 5)
PMID:22292001	PBO:0093557	(Figure 5)
PMID:22292001	PBO:0093558	(Figure 5)
PMID:22292001	FYPO:0000678	(Fig. 4)
PMID:22292001	FYPO:0007105	(Fig. 3e)
PMID:22292001	FYPO:0007105	(Fig. 3e)
PMID:22292001	FYPO:0006419	(Fig. 3d)
PMID:22292001	FYPO:0007101	(comment: CHECK during meiosis I)
PMID:22292001	FYPO:0007104	(Fig. 2)
PMID:22292001	FYPO:0006426	(Fig. 2)
PMID:22292001	FYPO:0000678	(Fig. 2)
PMID:22292001	FYPO:0000913	(Figure 1a)
PMID:22292001	FYPO:0007103	(Figure 1d)
PMID:22292001	FYPO:0007102	(Figure 1d)
PMID:22292001	FYPO:0007101	(Figure 1d)
PMID:22292001	GO:0000712	"(comment: CHECK strong contender for GO's ""acts upstream of or within"" (RO:0002264) gp-term relation)"
PMID:22292001	GO:0000712	"(comment: CHECK strong contender for GO's ""acts upstream of or within"" (RO:0002264) gp-term relation)"
PMID:22292001	FYPO:0007101	(comment: CHECK during meiosis I)
PMID:22292001	FYPO:0007101	(comment: CHECK during meiosis I)
PMID:22292001	PBO:0104345	(Figure 5)
PMID:22292001	FYPO:0000674	(Figure 5)
PMID:22292001	FYPO:0007102	(Figure 5d)
PMID:22292001	FYPO:0007102	(Figure 5d)
PMID:22292001	FYPO:0007102	(Figure 5d)
PMID:22292001	PBO:0104344	(Figure 5c)
PMID:22292001	PBO:0104342	(Figure 5c)
PMID:22292001	PBO:0104343	(Figure 5c)
PMID:22292001	PBO:0104342	(Figure 5c)
PMID:22328580	PBO:0105473	(Fig. 3A)
PMID:22328580	FYPO:0002350	(Figure 4A and B)
PMID:22328580	FYPO:0002350	(Figure 4A and B)
PMID:22328580	PBO:0105472	(Fig. 3A)
PMID:22328580	FYPO:0002350	(Fig. 3B, 4A and B)
PMID:22328580	FYPO:0002350	(Fig. 3B, 4A and B)
PMID:22328580	PBO:0021023	(Figure 2D)
PMID:22328580	PBO:0021023	(Fig. 1)
PMID:22328580	FYPO:0002350	(Figure 4A and B)
PMID:22328580	FYPO:0002350	(Fig. 4D)
PMID:22328580	FYPO:0002350	(Fig. 4D)
PMID:22328580	PBO:0021023	(Figures 5D, 6C)
PMID:22328580	PBO:0021023	(Figures 5D, 6C)
PMID:22328580	FYPO:0002350	(Figure 4A and B)
PMID:22328580	PBO:0021023	(Figures 5D, 6C)
PMID:22328580	FYPO:0002350	(Fig. 4D)
PMID:22328580	FYPO:0002350	(Figure 4A and B)
PMID:22344254	FYPO:0001234	(Fig. 1A) Loss of Gtr1 or Gtr2 resulted in the inability of the cells to grow properly, and they divided with a doubling time longer than that of wild-type cells
PMID:22344254	FYPO:0001234	(Fig. 1A) Loss of Gtr1 or Gtr2 resulted in the inability of the cells to grow properly, and they divided with a doubling time longer than that of wild-type cells
PMID:22344254	GO:0000329	The observed pattern was identical, regardless of the presence or not of amino acids in the medium. To confirm the localization to the vacuole membrane, we stained the gtr1-gfp cells with the lipophilic vacuolar membrane fluorescent dye FM4-64. As shown in Fig. 2B, Gtr1-GFP colocalized with FM4-64 staining, indicating that Gtr1-GFP is concentrated at the membranes of vacuoles in S. pombe.
PMID:22344254	FYPO:0001234	(Fig. 1A) Loss of Gtr1 or Gtr2 resulted in the inability of the cells to grow properly, and they divided with a doubling time longer than that of wild-type cells
PMID:22344254	FYPO:0001420	(Fig. 1A) Loss of Gtr1 or Gtr2 resulted in the inability of the cells to grow properly, and they divided with a doubling time longer than that of wild-type cells
PMID:22344254	FYPO:0001234	(Fig. 1A) Loss of Gtr1 or Gtr2 resulted in the inability of the cells to grow properly, and they divided with a doubling time longer than that of wild-type cells
PMID:22344254	FYPO:0003031	(Fig. 1B, 1C) respectively Gtr2, and in particular Gtr1, inhibit sexual differentiation in rich medium.
PMID:22344254	PBO:0097468	(comment: CHECK ********nitrogen replete/with aa)
PMID:22344254	FYPO:0002716	FM4-64 stained only small vesicles in the cytoplasm of vam6D cells, confirming a defect in vacuolar fusion in these cells.
PMID:22344254	FYPO:0004482	FM4-64 stained only small vesicles in the cytoplasm of vam6D cells, confirming a defect in vacuolar fusion in these cells.
PMID:22344254	PBO:0108022	These results suggest that Vam6 functions upstream of Gtr1, possibly by acting as a GEF.
PMID:22344254	FYPO:0001357	We introduced Gtr1Q61L in a vam6D background and found that the double mutant was able to grow normally (Fig. 5B), indicating that constitutively active Gtr1 rescues the cell growth defect of the vam6D mutant.
PMID:22344254	FYPO:0001234	The doubling time of vam6D was shorter in the presence of amino acids, indicating that these cells were still able to respond, at least partially, to the presence of amino acids (Fig. 5A) and that Vam6 has an important role in regulating cell growth in S. pombe but is not essential for responding to the availability of amino acids.
PMID:22344254	FYPO:0004482	FM4-64 stained only small vesicles in the cytoplasm of vam6D cells, confirming a defect in vacuolar fusion in these cells.
PMID:22344254	PBO:0108021	the Gtr1-Gtr2 heterodimer and TORC1 are located in the vacuolar membrane independently of the presence of amino acids. However, only when amino acids are present in the medium does the Gtr1-Gtr2 heterodimer interact physically with TORC1 and activate the TOR pathway to induce cell growth and repress sexual differentiation.
PMID:22344254	PBO:0108021	the Gtr1-Gtr2 heterodimer and TORC1 are located in the vacuolar membrane independently of the presence of amino acids. However, only when amino acids are present in the medium does the Gtr1-Gtr2 heterodimer interact physically with TORC1 and activate the TOR pathway to induce cell growth and repress sexual differentiation.
PMID:22344254	FYPO:0000280	(Fig. 4a)
PMID:22344254	FYPO:0000280	(Fig. 4a)
PMID:22344254	GO:0000329	As shown in Fig. 3, GFP-Tor2, GFP-Mip1 and Pop3-GFP showed similar GFP signals that colocalized with FM4-64 staining. Thus, the three components of the TORC1 complex showed vacuolar membrane localization, independently of the presence or not of amino acids in the medium.
PMID:22344254	GO:0000329	As shown in Fig. 3, GFP-Tor2, GFP-Mip1 and Pop3-GFP showed similar GFP signals that colocalized with FM4-64 staining. Thus, the three components of the TORC1 complex showed vacuolar membrane localization, independently of the presence or not of amino acids in the medium.
PMID:22344254	GO:0005774	As shown in Fig. 3, GFP-Tor2, GFP-Mip1 and Pop3-GFP showed similar GFP signals that colocalized with FM4-64 staining. Thus, the three components of the TORC1 complex showed vacuolar membrane localization, independently of the presence or not of amino acids in the medium.
PMID:22344254	GO:1990131	We observed that Gtr2-RFP co-precipitated with Gtr1 (Fig. 2D) and that the Gtr1-Gtr2 interaction was stronger in cells growing in the presence of amino acids, indicating that the formation of the heterodimer is stimulated by amino acids.
PMID:22344254	GO:0000329	The observed pattern was identical, regardless of the presence or not of amino acids in the medium. To confirm the localization to the vacuole membrane, we stained the gtr1-gfp cells with the lipophilic vacuolar membrane fluorescent dye FM4-64. As shown in Fig. 2B, Gtr1-GFP colocalized with FM4-64 staining, indicating that Gtr1-GFP is concentrated at the membranes of vacuoles in S. pombe.
PMID:22344254	FYPO:0001234	(Fig. 1A) Loss of Gtr1 or Gtr2 resulted in the inability of the cells to grow properly, and they divided with a doubling time longer than that of wild-type cells
PMID:22344254	GO:0000329	(Fig. 6)
PMID:22344254	FYPO:0003031	(Fig. 1B, 1C) respectively Gtr2, and in particular Gtr1, inhibit sexual differentiation in rich medium.
PMID:22344254	PBO:0108023	(comment: CHECK ***********nitrogen replete/with aa. AND during aa starvation***********)vam6D mutant cells showed similar Rps6 phosphorylation levels to that of wild-type cells in the absence of amino acids. However, in contrast to wild-type cells, vam6D cells did not show an increase in Rps6 phosphorylation in the presence of amino acids.
PMID:22344254	PBO:0097468	(comment: CHECK *****nitrogen replete/with aa*****) vam6D mutant cells showed similar Rps6 phosphorylation levels to that of wild-type cells in the absence of amino acids. However, in contrast to wild-type cells, vam6D cells did not show an increase in Rps6 phosphorylation in the presence of amino acids.
PMID:22344694	PBO:0106009	(comment: not shown direct binding but want to capture the fact that it binds the oxidised form)
PMID:22344694	PBO:0106009	(comment: not shown direct binding but want to capture the fact that it binds the oxidised form)
PMID:22347452	GO:0005634	Consistent with a role in chromatin modification, all three proteins localized to the nucleus (Figure 4A).
PMID:22347452	GO:0005634	Consistent with a role in chromatin modification, all three proteins localized to the nucleus (Figure 4A).
PMID:22347452	GO:0034967	Taken together, these data demonstrate that Hif2p, Set3p, and Snt1p exist as part of a nuclear-localized protein complex in S. pombe.
PMID:22347452	GO:0034967	Taken together, these data demonstrate that Hif2p, Set3p, and Snt1p exist as part of a nuclear-localized protein complex in S. pombe.
PMID:22347452	GO:0034967	Taken together, these data demonstrate that Hif2p, Set3p, and Snt1p exist as part of a nuclear-localized protein complex in S. pombe.
PMID:22347452	FYPO:0004045	(Figure 2c)
PMID:22347452	FYPO:0004513	This reverse genetic approach identified a strain bearing a deletion in the annotated open reading frame, SPCC1235.09, which encodes a WD repeat domain protein (Figure 1).
PMID:22347452	GO:0005634	Consistent with a role in chromatin modification, all three proteins localized to the nucleus (Figure 4A).
PMID:22349564	PBO:0105071	Northern blots revealed no defect in the accumulation of mature messengers (Figure 5B)
PMID:22349564	FYPO:0003730	(Figure 1A)
PMID:22349564	FYPO:0003730	(Figure 1A)
PMID:22349564	FYPO:0001437	(Figure 1A)
PMID:22349564	FYPO:0001437	(Figure 1A)
PMID:22349564	FYPO:0000441	(Figure 1A)
PMID:22349564	FYPO:0007623	(Figure 1B)
PMID:22349564	FYPO:0007623	(Figure 1B)
PMID:22349564	PBO:0105064	(Figure 1C)
PMID:22349564	PBO:0105065	(Figure 1C)
PMID:22349564	PBO:0105066	(Figure 1C)
PMID:22349564	GO:0005739	(Figure S4A, B, C)
PMID:22349564	PBO:0105064	(Figure 1C)
PMID:22349564	PBO:0105065	(Figure 1C)
PMID:22349564	PBO:0105066	(Figure 1C)
PMID:22349564	PBO:0105067	(Figure 2A) Both the cytb and cox2 mRNAs were present at normal levels in the Δcbp6 mutant
PMID:22349564	PBO:0105068	(Figure 2A) Both the cytb and cox2 mRNAs were present at normal levels in the Δcbp6 mutant
PMID:22349564	PBO:0096238	(Figure 2C) Thus, virtually all of the Cytb protein synthesized in the Δcbp6 mutant is degraded
PMID:22349564	FYPO:0007623	(Figure 2D) In both Δcbp6 and control Δcytb mitochondria, complex III was completely lacking (lanes 3 and 4)
PMID:22349564	PBO:0105069	absent respiratory complex III Figure 2D In both Δcbp6 and control Δcytb mitochondria, complex III was completely lacking (lanes 3 and 4)
PMID:22349564	PBO:0105070	absent respiratory complex III. Figure 2D As expected, the higher molecular weight bands of complex III were absent in the Δppr4 mutant, which lacks complex IV
PMID:22349564	GO:0031966	The tagged Mss51 was detected only in the mitochondrial fraction and like Cox2 was strongly resistant to carbonate extraction (Figure 4A), indicating that it is a membrane protein.
PMID:22349564	FYPO:0003730	(Figure 4B) A deletion mutants showed a clear growth defect on galactose medium
PMID:22349564	FYPO:0000441	Similarly to the Δcbp3 and Δcbp6 mutants, Δmss51 cells were resistant to antimycin A on glucose medium, showing that they contain a functional complex V
PMID:22349564	GO:0034551	Thus, in S. pombe, Mss51 appears to be required at a post-translational step of complex IV biogenesis
PMID:22349564	FYPO:0007624	Δmss51 cells showed normal cytochrome b and c1 peaks, but cytochromes aa3 were not detectable.
PMID:22349564	PBO:0105064	Cytb, Cox1, 2 and 3 were clearly visible, although Cox2 was less strongly labeled in both mutants, especially Δmss51 (Figure 5A)
PMID:22349564	PBO:0105065	Cytb, Cox1, 2 and 3 were clearly visible, although Cox2 was less strongly labeled in both mutants, especially Δmss51 (Figure 5A)
PMID:22349564	PBO:0105066	Cytb, Cox1, 2 and 3 were clearly visible, although Cox2 was less strongly labeled in both mutants, especially Δmss51 (Figure 5A)
PMID:22349564	PBO:0105065	As expected, Δppr4 cells clearly lacked Cox1
PMID:22349564	PBO:0105068	Northern blots revealed no defect in the accumulation of mature messengers (Figure 5B)
PMID:22349564	FYPO:0003730	(Figure 1A)
PMID:22349564	PBO:0096238	Cox2 was detectable in Δmss51 purified mitochondria, although its level was greatly reduced (Figure 5C), consistent with the reduced 35S labeling (Figure 5A)
PMID:22349564	PBO:0096237	Cox1 was clearly less stable in the Δmss51 mutant than in the wild-type, while Cox2 was poorly labeled in the mutant even before starting the chase, as noted before (Figure 5C).
PMID:22349564	FYPO:0001938	(Figure 5E)
PMID:22354040	PBO:0098696	(Fig. 7A)
PMID:22354040	GO:0042162	(Fig. 7)
PMID:22354040	PBO:0095770	(Fig. 7B)
PMID:22354040	PBO:0098697	(Fig. 7B)
PMID:22354040	PBO:0098698	(Fig. 7c)
PMID:22354040	FYPO:0002239	(Figure 8A)
PMID:22375066	GO:0010514	AMPK is required for proper advance entry into mitosis in nitrogen-starved cells and arrest in G1 before Start.
PMID:22375066	GO:0031588	These results indicated that Ssp2 interacts physically with Amk2 and Cbs2 in vivo, showing that AMPK is indeed a αβγ heterotrimer and that these three subunits interact even under optimal growth conditions.
PMID:22375066	GO:0031588	These results indicated that Ssp2 interacts physically with Amk2 and Cbs2 in vivo, showing that AMPK is indeed a αβγ heterotrimer and that these three subunits interact even under optimal growth conditions.
PMID:22375066	GO:0031588	These results indicated that Ssp2 interacts physically with Amk2 and Cbs2 in vivo, showing that AMPK is indeed a αβγ heterotrimer and that these three subunits interact even under optimal growth conditions.
PMID:22375066	PBO:0096471	This finding suggested that inactive AMPK is excluded from the nucleus and, upon activation by glucose or nitrogen starvation, part of the AMPK moves into the nucleus.
PMID:22375066	GO:0140648	AMPK is required for proper advance entry into mitosis in nitrogen-starved cells and arrest in G1 before Start.
PMID:22375066	GO:0140648	AMPK is required for proper advance entry into mitosis in nitrogen-starved cells and arrest in G1 before Start.
PMID:22375066	GO:0010514	AMPK is required for proper advance entry into mitosis in nitrogen-starved cells and arrest in G1 before Start.
PMID:22375066	PBO:0096473	This result shows that Ssp2 phosphorylation by Ssp1 is required to trigger the nuclear accumulation of the former upon nitrogen or glucose starvation, and that if Ssp2 is not phosphorylated it remains in a cytoplasmic localization, regardless of the nutritional conditions of the cell.
PMID:22426534	PBO:0101052	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22426534	PBO:0101052	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22426534	PBO:0101051	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22426534	PBO:0101051	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22426534	PBO:0101050	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22426534	PBO:0101050	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22426534	PBO:0101049	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22426534	PBO:0101049	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22426534	PBO:0101053	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22426534	PBO:0101053	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22427686	PBO:0112452	(Fig. S2A)
PMID:22427686	FYPO:0002253	(Fig. 1B, Table 1)
PMID:22427686	PBO:0032798	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114220	(Fig. 2C)
PMID:22427686	FYPO:0002253	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114221	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114222	Table 1
PMID:22427686	PBO:0032843	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114223	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114224	Table 1
PMID:22427686	PBO:0114225	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114226	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114222	Table 1
PMID:22427686	PBO:0103459	Table 1
PMID:22427686	PBO:0114227	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114228	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114222	Table 1
PMID:22427686	PBO:0103459	Table 1
PMID:22427686	PBO:0107134	Table 1
PMID:22427686	PBO:0114229	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114230	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114222	Table 1
PMID:22427686	PBO:0103459	Table 1
PMID:22427686	PBO:0107134	Table 1
PMID:22427686	FYPO:0002253	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0002253	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0002253	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114231	(Fig. 2C)
PMID:22427686	PBO:0114224	Table 1
PMID:22427686	PBO:0114224	Table 1
PMID:22427686	PBO:0114222	Table 1
PMID:22427686	PBO:0114222	Table 1
PMID:22427686	PBO:0114222	Table 1
PMID:22427686	PBO:0103459	Table 1
PMID:22427686	PBO:0103459	Table 1
PMID:22427686	PBO:0103459	Table 1
PMID:22427686	PBO:0103459	Table 1
PMID:22427686	PBO:0103459	Table 1
PMID:22427686	PBO:0103459	Table 1
PMID:22427686	PBO:0107134	Table 1
PMID:22427686	PBO:0107134	Table 1
PMID:22427686	PBO:0107134	Table 1
PMID:22427686	PBO:0107134	Table 1
PMID:22427686	PBO:0107134	Table 1
PMID:22427686	PBO:0107134	Table 1
PMID:22427686	PBO:0114232	(Fig. 1B, Table 1)
PMID:22427686	PBO:0099470	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114226	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114233	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114234	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114235	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114236	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114237	Table 1
PMID:22427686	PBO:0114238	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114239	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114240	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114241	(Fig. 1B, Table 1)
PMID:22427686	PBO:0032817	(Fig. 1B, Table 1)
PMID:22427686	PBO:0032796	(Fig. 1B, Table 1)
PMID:22427686	PBO:0033280	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114242	(Fig. 1B, Table 1)
PMID:22427686	PBO:0094136	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114243	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114244	(Fig. 1B, Table 1)
PMID:22427686	PBO:0114245	(Fig. 1B, Table 1)
PMID:22427686	PBO:0112639	(Fig. 2C)
PMID:22427686	PBO:0114246	(Fig. 2C)
PMID:22427686	PBO:0114231	(Fig. 2C)
PMID:22427686	PBO:0112639	(Fig. 2C)
PMID:22427686	FYPO:0001368	(Fig. 2H)
PMID:22427686	FYPO:0001368	(Fig. 2H)
PMID:22427686	FYPO:0001368	(Fig. 2H)
PMID:22427686	PBO:0114247	(Fig. 3B)
PMID:22427686	PBO:0114248	(Fig. 3B)
PMID:22427686	PBO:0114249	(Fig. 3B)
PMID:22427686	PBO:0114249	(Fig. 3B)
PMID:22427686	PBO:0114248	(Fig. 3B)
PMID:22427686	PBO:0112296	(Fig. 4C)
PMID:22427686	PBO:0032815	(Fig. 4C)
PMID:22427686	PBO:0032815	(Fig. 4C)
PMID:22427686	PBO:0112293	(Fig. 4C)
PMID:22427686	PBO:0114250	(Fig. 4C)
PMID:22427686	PBO:0112293	(Fig. 4C)
PMID:22427686	PBO:0112293	(Fig. 4C)
PMID:22427686	PBO:0099471	(Fig. 4C)
PMID:22427686	PBO:0099470	(Fig. 4C)
PMID:22427686	PBO:0112294	(Fig. 4C)
PMID:22427686	PBO:0099471	(Fig. 4C)
PMID:22427686	PBO:0099471	(Fig. 4C)
PMID:22427686	PBO:0114251	(Fig. 4D)
PMID:22427686	PBO:0114252	(Fig. 4F)
PMID:22427686	PBO:0114253	(Fig. 4F)
PMID:22427686	PBO:0114254	(Fig. 5B and C)
PMID:22427686	PBO:0114255	(Fig. 5D)
PMID:22427686	FYPO:0003338	(Fig. 6B)
PMID:22427686	FYPO:0003338	(Fig. 6A)
PMID:22427686	PBO:0104485	(Fig. 6F and G)
PMID:22427686	PBO:0104485	(Fig. 6F and G)
PMID:22427686	FYPO:0002253	(Fig. 6E)
PMID:22427686	FYPO:0002253	(Fig. 6E)
PMID:22427686	PBO:0032816	(Fig. 6E)
PMID:22427686	PBO:0032816	(Fig. 6E)
PMID:22427686	PBO:0114256	(Fig. 6H)
PMID:22427686	PBO:0114256	(Fig. 6H)
PMID:22427686	PBO:0114254	(Fig. 6H)
PMID:22427686	PBO:0114254	(Fig. 6H)
PMID:22431512	PBO:0102103	(comment: localization independent of Ago1)
PMID:22431512	PBO:0102102	(comment: localization independent of Ago1)
PMID:22431512	PBO:0102102	(comment: localization independent of Ago1)
PMID:22431512	PBO:0102103	(comment: localization independent of Ago1)
PMID:22437499	FYPO:0005446	Disrupting the Leu-binding pocket by replacing Val 196 with a bulky methionine, and substituting Ser for the Cdh1 equivalents of Asp 173, Asp 457 and Glu 458 at the putative Arg-binding site, eliminated the ability of Cdh1 to stimulate APC/C activity (Fig. 4e and Supplementary Fig. 6) but had no affect on co-activator binding to the APC/C (Supplementary Fig. 7)
PMID:22437499	PBO:0116201	This mutation dissociated Mad3 from a Cdc20-C-Mad2 heterodimer when size-exclusion chromatography was performed (Supplementary Fig. 4).
PMID:22437499	PBO:0116202	This mutation dissociated Mad3 from a Cdc20-C-Mad2 heterodimer when size-exclusion chromatography was performed (Supplementary Fig. 4).
PMID:22438582	PBO:0101879	(Figure 1)
PMID:22438582	PBO:0022389	(Figure 1)
PMID:22438582	PBO:0022389	(Figure 1)
PMID:22438582	PBO:0022389	(Figure 1)
PMID:22438582	FYPO:0000151	(Figure 4B)
PMID:22438582	PBO:0022389	(Figure 1)
PMID:22438582	PBO:0101878	(Figure 5A)
PMID:22438582	PBO:0101877	(Figure 5A)
PMID:22438582	PBO:0101882	(Figure 5A)
PMID:22438582	PBO:0101882	(Figure 5)
PMID:22438582	PBO:0101882	(Figure 5)
PMID:22438582	PBO:0101874	(Figure 5F)
PMID:22438582	PBO:0101883	(Figure 6A)
PMID:22438582	PBO:0101884	(Figure 6A)
PMID:22438582	PBO:0101885	(Figure 6A)
PMID:22438582	PBO:0101886	(Figure 6A)
PMID:22438582	GO:1990395	(comment: CHECK MEIOTIC !) Plo1 protein reorganize spindle body during meiosis: Plo1 starts to localize to spindle pole body at the onset of meiosis I, and recruits Cut12 (and Pcp1), which was absent during meiotic prophase.
PMID:22438582	PBO:0100759	(Figure 1)
PMID:22438582	PBO:0101879	(Figure 1)
PMID:22438582	FYPO:0000583	(Figure S6)
PMID:22438582	FYPO:0000583	(Figure S6)
PMID:22438582	PBO:0101879	(Figure 1)
PMID:22438582	PBO:0101879	(Figure 1)
PMID:2245912	PBO:0020446	(comment: cells heterozygous for stf1-1 are more elongated that stf1-1 homozygous cells)
PMID:2245912	FYPO:0001492	(comment: Table 5 This mutant is a revertant of cdc2-M35)
PMID:2245912	FYPO:0006822	(comment: Table 5 no genetic interaction with stf1-1)
PMID:2245912	FYPO:0006822	Table 5 no genetic interaction with stf1-1
PMID:2245912	PBO:0097660	(Table 4)
PMID:2245912	PBO:0020446	(comment: same phenotype as cells homozygous for stf1-1)
PMID:2245912	PBO:0097658	(comment: same phenotype as cells homozygous for stf1-1)
PMID:2245912	FYPO:0001492	Table 4 (comment: suppressor of cdc25-22)
PMID:2245912	FYPO:0001492	Table 4 (comment: suppressor of cdc25-22)
PMID:2245912	FYPO:0001492	Table 4 (comment: stf1-1 is a suppressor of cdc25-M51)
PMID:2245912	FYPO:0001492	Table 4 (comment: suppressor of cdc25-disruption occasional cdc- cells observed)
PMID:2245912	FYPO:0001490	Table 8 (comment: no genetic interaction with stf1-1)
PMID:2245912	FYPO:0001492	Table 8 (comment: no genetic interaction with stf1-1)
PMID:2245912	FYPO:0001491	(Table 5)
PMID:2245912	FYPO:0001492	Table 5 (comment: cdc2-1w rescues cdc25-22 but cells are long)
PMID:2245912	FYPO:0006822	Table 5 (comment: cdc2-1w and stf1-1 have additive effect on cdc25-22 cell size at restrictive temperature)
PMID:2245912	FYPO:0001490	(comment: dis2+ over expression reverses the stf1-1 suppression cdc25-22)
PMID:2245912	PBO:0093770	Table 7 (comment: Cells are slightly shorter at high temperature when stf1-1 present)
PMID:2245912	PBO:0093770	Table 7 (comment: Cells are slightly shorter at high temperature when stf1-1 present)
PMID:2245912	FYPO:0006822	(Table 6)
PMID:2245912	FYPO:0006822	Table 6 (comment: wee1-50 and stf1-1 have an additive effect to suppress cdc25-22 phenotype at the restrictive temperature)
PMID:2245912	FYPO:0006822	Table 5 (comment: cdc2-3w and stf1-1 have additive effect on cdc25-22 cell size at restrictive temperature)
PMID:2245912	FYPO:0006822	Table 5 (comment: no genetic interaction with stf1-1)
PMID:2245912	FYPO:0006822	Table 5 (comment: no genetic interaction with stf1-1)
PMID:2245912	FYPO:0001490	Table 5 (comment: no genetic interaction with stf1-1 cdc2-59 is a cold sensitive cdc2 mutant cdc at low (25°C) temperature and wee at high temperature (35°C))
PMID:2245912	FYPO:0001492	Table 5 (comment: This mutant is a revertant of cdc2-M35)
PMID:2245912	FYPO:0001492	Table 5 (comment: no genetic interaction with stf1-1)
PMID:2245912	FYPO:0001490	Table 5 (comment: no genetic interaction with stf1-1)
PMID:2245912	FYPO:0001490	Table 5 (comment: no genetic interaction with stf1-1)
PMID:2245912	FYPO:0001490	Table 5 (comment: no genetic interaction with stf1-1)
PMID:2245912	PBO:0097660	(Table 4)
PMID:2245912	PBO:0020446	(comment: stf1-1/stf1-3 cells are not as elongated as stf1-1 heterozygous cells at restrictive temperature)
PMID:2245912	FYPO:0000674	Table 4 (comment: suppressor of cdc25-disruption occasional cdc- cells observed)
PMID:2245912	FYPO:0000674	Table 4 (comment: stf1-1 is a suppressor of cdc25-M51)
PMID:2245912	PBO:0097658	(comment: stf1-1/stf1-3 cells form small colonies at restrictive temperature ~20-200 cells)
PMID:2245912	PBO:0097659	(comment: stf1-1/stf1-2 cells are not as elongated as stf1-1 heterozygous cells at restrictive temperature)
PMID:2245912	PBO:0097658	(comment: cells homozygous for stf1-1 form small colonies at restrictive temperature ~20-200 cells)
PMID:2245912	PBO:0020446	(comment: cells homozygous for stf1-1 are not as elongated as stf1-1 heterozygous cells at restrictive temperature)
PMID:2245912	PBO:0097658	(comment: cells heterozygous for stf1-1 form small colonies at restrictive temperature ~20-200 cells)
PMID:2245912	PBO:0097657	(comment: the restrictive temperature for a cdc25-22 diploid is 32°C)
PMID:2245912	FYPO:0000674	Table 3 (comment: suppressor of cdc25-22)
PMID:2245912	FYPO:0000674	Table 4 (comment: suppressor of cdc25-22)
PMID:2245912	FYPO:0000674	Table 4 (comment: suppressor of cdc25-22)
PMID:22474355	PBO:0111713	ChIP analyses showed that Ers1 localization at the mating type locus (cenH) and telomeres was severely decreased in swi6Δ and clr4Δ cells (Fig. S5A).
PMID:22474355	PBO:0111714	ChIP analyses showed that Ers1 localization at the mating type locus (cenH) and telomeres was severely decreased in swi6Δ and clr4Δ cells (Fig. S5A).
PMID:22474355	PBO:0111714	ChIP analyses showed that Ers1 localization at the mating type locus (cenH) and telomeres was severely decreased in swi6Δ and clr4Δ cells (Fig. S5A).
PMID:22474355	PBO:0111715	In contrast, a high level of Ers1 was detected at telomeres in hrr1Δ cells (Fig. S5C).
PMID:22474355	PBO:0111716	In swi6Δ cells, Chp1 association with the centromeric dg or dh repeat locus decreased partially (70- 80%) but was still much greater than that observed in clr4Δ cells (Fig. 5 A and B).
PMID:22474355	PBO:0111717	This was in contrast to Hrr1 or Rdp1, whose association was severely reduced in swi6Δ cells (10-20%) to levels comparable to those of clr4Δ cells.
PMID:22474355	PBO:0111705	In contrast, EGFP-Ers1C62 showed a more diffuse signal with weak nuclear dots (Fig. 4B and Fig. S4 C and D), suggesting that the correct localization of Ers1 was impaired by the C62 mutation.
PMID:22474355	GO:0005721	Similar to that previously observed, EGFP-Ers1WT showed a distinct nuclear dot pattern in WT cells consistent with a localization to heterochromatin (Fig. 4B and Fig. S4B)
PMID:22474355	PBO:0111704	derepression of a ura4+ marker gene integrated into the outermost Fig. 1. (otr) pericentromeric repeat of chromosome 1 (otr1R::ura4+) (Fig. 1a)
PMID:22474355	PBO:0111704	derepression of a ura4+ marker gene integrated into the outermost Fig. 1. (otr) pericentromeric repeat of chromosome 1 (otr1R::ura4+) (Fig. 1a)
PMID:22474355	PBO:0111704	derepression of a ura4+ marker gene integrated into the outermost Fig. 1. (otr) pericentromeric repeat of chromosome 1 (otr1R::ura4+) (Fig. 1a)
PMID:22474355	PBO:0111704	derepression of a ura4+ marker gene integrated into the outermost Fig. 1. (otr) pericentromeric repeat of chromosome 1 (otr1R::ura4+) (Fig. 1a)
PMID:22474355	FYPO:0002835	defective siRNA production (Fig. 1C)
PMID:22474355	FYPO:0000220	increased levels of noncoding centromeric transcripts (Fig. 1B)
PMID:22474355	PBO:0111706	Moreover, the nuclear dot localization of EGFP-Ers1WT was completely abolished in clr4Δ cells (Fig. 4C), indicating that the activity of Clr4 was also required for Ers1 localization in the nucleus.
PMID:22474355	PBO:0111706	To test the hypothesis that the nuclear dot localization of Ers1 was attributable to an interaction with H3K9me-bound CD proteins, EGFP-Ers1WT localization was next examined in swi6Δ, chp1Δ, and chp2Δ cells. The localization of EGFP-Ers1WT was clearly abolished in swi6Δ cells similar to that observed in clr4Δ, whereas WT localization patterns were retained in the chp1Δ and chp2Δ cells (Fig. 4C and Fig. S4C).
PMID:22474355	PBO:0111707	To test the hypothesis that the nuclear dot localization of Ers1 was attributable to an interaction with H3K9me-bound CD proteins, EGFP-Ers1WT localization was next examined in swi6Δ, chp1Δ, and chp2Δ cells. The localization of EGFP-Ers1WT was clearly abolished in swi6Δ cells similar to that observed in clr4Δ, whereas WT localization patterns were retained in the chp1Δ and chp2Δ cells (Fig. 4C and Fig. S4C).
PMID:22474355	PBO:0111707	To test the hypothesis that the nuclear dot localization of Ers1 was attributable to an interaction with H3K9me-bound CD proteins, EGFP-Ers1WT localization was next examined in swi6Δ, chp1Δ, and chp2Δ cells. The localization of EGFP-Ers1WT was clearly abolished in swi6Δ cells similar to that observed in clr4Δ, whereas WT localization patterns were retained in the chp1Δ and chp2Δ cells (Fig. 4C and Fig. S4C).
PMID:22474355	PBO:0111708	suggesting that a physical association with Swi6, but not the other CD proteins, was required for the heterochromatic localization of Ers1.
PMID:22474355	PBO:0111709	Moreover, the interaction between Ers1 and Swi6 was weakened by the presence of the C62 mutation (Fig. 4 D and E). Taken together, these results suggested that Ers1 associates with both Hrr1 and Swi6, and that the C62 mutation impairs both associations.
PMID:22474355	PBO:0111710	The localizations of Hrr1-Flag and Rdp1-Flag at centromeric repeats were also found to be severely compromised in both ers1Δ and swi6Δ mutant cells (Fig. 5 A and B).
PMID:22474355	PBO:0111710	The localizations of Hrr1-Flag and Rdp1-Flag at centromeric repeats were also found to be severely compromised in both ers1Δ and swi6Δ mutant cells (Fig. 5 A and B).
PMID:22474355	PBO:0111703	derepression of a ura4+ marker gene integrated into the outermost Fig. 1. (otr) pericentromeric repeat of chromosome 1 (otr1R::ura4+) (Fig. 1a)
PMID:22474355	PBO:0111718	This was in contrast to Hrr1 or Rdp1, whose association was severely reduced in swi6Δ cells (10-20%) to levels comparable to those of clr4Δ cells.
PMID:22474355	PBO:0111711	The localizations of Hrr1-Flag and Rdp1-Flag at centromeric repeats were also found to be severely compromised in both ers1Δ and swi6Δ mutant cells (Fig. 5 A and B).
PMID:22474355	PBO:0111711	The localizations of Hrr1-Flag and Rdp1-Flag at centromeric repeats were also found to be severely compromised in both ers1Δ and swi6Δ mutant cells (Fig. 5 A and B).
PMID:22474355	PBO:0111712	This is also consistent with a previous report that the deletion of swi6+ decreases the centromeric localization of Rdp1 (14). These results support the idea that the heterochromatic localization of RDRC requires Ers1 and that, in turn, Ers1 localization depends on Swi6.
PMID:22474355	PBO:0111713	ChIP analyses showed that Ers1 localization at the mating type locus (cenH) and telomeres was severely decreased in swi6Δ and clr4Δ cells (Fig. S5A).
PMID:22484924	PBO:0099384	(Fig. 5c)
PMID:22484924	FYPO:0004482	(Fig. 4)
PMID:22484924	PBO:0104296	(comment: vw, moved down to -decreased protein targeting to vacuole, with protein secreted)
PMID:22484924	PBO:0095511	(Fig. 2d)
PMID:22484924	PBO:0104298	(Fig. 2D)
PMID:22484924	GO:0006895	(comment: CHECK (protein))
PMID:22484924	PBO:0104297	(Fig. 2c)
PMID:22484924	FYPO:0000423	(Fig. 4) (comment: (I moved this down from abnormal endocytisis, is that OK?))
PMID:22496451	PBO:0023351	"(comment: allele tyep ""unknown"" because neither nt nor aa position 324 is A)"
PMID:22508988	PBO:0111962	S. pombe Cdk9 also generated Ser2-P and Ser5-P signals but was relatively inefficient at phosphorylating Ser7.
PMID:22508988	GO:0005515	(Fig. 1) (comment: carboxy terminal region)
PMID:22508988	PBO:0099618	(Fig. 1a)
PMID:22508988	PBO:0099618	(Fig. 1a) (comment: CHECK in vitro /in vivo)
PMID:22508988	GO:0005515	(Fig. 1) (comment: carboxy terminal region)
PMID:22508988	PBO:0099619	(Fig. 1a)
PMID:22508988	PBO:0099620	(Fig. 1e) (comment: CHECK in vitro)
PMID:22508988	GO:0004674	We also compared the activities of kinase complexes generated by translation in vitro toward Spt5. By this measurement also, Cdk9 and Cdk9􏰂C were stimulated to similar extents by Csk1 (Fig. 1F),(comment: is this an physiological substrate?)
PMID:22508988	FYPO:0006821	(Fig. 2b)
PMID:22508988	PBO:0093554	(Fig. 2c)
PMID:22508988	PBO:0093560	(Fig. 2c)
PMID:22508988	PBO:0093554	(Fig. 2c)
PMID:22508988	PBO:0093560	(Fig. 2c)
PMID:22508988	FYPO:0002141	(Fig. 2c)
PMID:22508988	FYPO:0001357	(Fig. 2c)
PMID:22508988	PBO:0099621	(Fig. 2c) MPA exacerbates growth impairment in mutants defective in transcript elongation (8, 11, 50), although the precise mechanism of this effect is unknown (34)
PMID:22508988	PBO:0099621	(Fig. 2c)
PMID:22508988	FYPO:0007074	(Fig. 2c)
PMID:22508988	PBO:0099622	(Fig. 2d) (comment: CHECK Spt5-T1P (CTD repeat 1 residue))
PMID:22508988	PBO:0099622	(Fig. 2d) (comment: CHECK Spt5-T1P (CTD repeat 1 residue))
PMID:22508988	PBO:0099623	(Fig. 3B)
PMID:22508988	PBO:0099624	(Fig. 3B)
PMID:22508988	PBO:0099625	(Fig. 4A, B)
PMID:22508988	PBO:0099626	(Fig. 4A, B)
PMID:22508988	PBO:0111494	. The preference of the conserved Cdk9 catalytic domain in fission yeast and metazoans for Ser7-modified CTD substrates, moreover, implies a conserved mechanism to impose order on the Pol II transcription cycle.
PMID:22508988	PBO:0103372	(Fig. 6C) Immunoblot analysis indicated that Mcs6 phosphorylates Ser2, Ser5, and Ser7
PMID:22508988	PBO:0103372	(Fig. 6C) Immunoblot analysis indicated that Mcs6 phosphorylates Ser2, Ser5, and Ser7
PMID:22508988	PBO:0103372	(Fig. 6C) Immunoblot analysis indicated that Mcs6 phosphorylates Ser2, Ser5, and Ser7
PMID:22508988	PBO:0111962	(Fig. 6C) Immunoblot analysis indicated that Mcs6 phosphorylates Ser2, Ser5, and Ser7
PMID:22508988	PBO:0103373	S. pombe Cdk9 also generated Ser2-P and Ser5-P signals but was relatively inefficient at phosphorylating Ser7.
PMID:22508988	PBO:0103373	S. pombe Cdk9 also generated Ser2-P and Ser5-P signals but was relatively inefficient at phosphorylating Ser7.
PMID:22508988	PBO:0099618	(Fig. 1a)
PMID:22558440	PBO:0109949	(comment: I specifically used that term name because I did not want to discriminate whether Cuf2 is a negative or a positive regulator of transcription even though in the paper we have put emphasis on the fact that meiotic genes are up-regulated in the absence of Cuf2 (so that Cuf2 would be a repressor). The reason is that there are also many other genes that are down-regulated in the cuf2delta mutant compare to WT. We still don't know which effect is direct and/or indirect. Thus, we don't want to exclude that Cuf2 might act as an activator, a repressor or both, for now.
PMID:22558440	PBO:0109950	(comment: I specifically used that term name because I did not want to discriminate whether Cuf2 is a negative or a positive regulator of transcription even though in the paper we have put emphasis on the fact that meiotic genes are up-regulated in the absence of Cuf2 (so that Cuf2 would be a repressor). The reason is that there are also many other genes that are down-regulated in the cuf2delta mutant compare to WT. We still don't know which effect is direct and/or indirect. Thus, we don't want to exclude that Cuf2 might act as an activator, a repressor or both, for now.)
PMID:22573890	FYPO:0004653	(Fig. 5)
PMID:22573890	PBO:0098290	(Fig. S2)
PMID:22573890	FYPO:0000651	(Fig. 6)
PMID:22573890	FYPO:0000650	(Fig. 6)
PMID:22573890	FYPO:0006559	(Fig. 5) (comment: 6 min late)
PMID:22573890	FYPO:0004895	(Fig. 5)
PMID:22573890	FYPO:0006187	(Fig. 5)
PMID:22573890	PBO:0098286	(Fig. 2a)
PMID:22573890	PBO:0111999	(Fig. 2a) (comment: CHECK WT 10% @36degrees)
PMID:22573890	PBO:0098288	(Figure 2B, C)
PMID:22573890	PBO:0098289	(Fig. 3A)
PMID:22573890	PBO:0018345	(Fig. 3A)
PMID:22573890	PBO:0097713	(Fig. 3A)
PMID:22582262	GO:0007129	"rec12 phenotype indicates that Sme2 role in synapsis is independent of meiotic recombination; (comment: NEEDS TO BE REGULATION OF SYNAPSISa change to the GO ""pairing"" definition requested""https://sourceforge.net/p/geneontology/ontology-requests/10607/)"
PMID:22582262	GO:0007129	"rec12 phenotype indicates that Sme2 role in synapsis is independent of meiotic recombination; (comment: NEEDS TO BE REGULATION OF SYNAPSISa change to the GO ""pairing"" definition requested""https://sourceforge.net/p/geneontology/ontology-requests/10607/)"
PMID:22645648	FYPO:0001122	(Figure 4e)
PMID:22645648	FYPO:0002060	(Figure 1a)
PMID:22645648	FYPO:0005430	(Figure 4d)
PMID:22645648	FYPO:0000012	(Figure 4a, b)
PMID:22645648	FYPO:0002060	(Figure 6)
PMID:22645648	FYPO:0001019	(Figure 4d)
PMID:22645648	FYPO:0002061	(Figure 1a, 6a)
PMID:22645648	FYPO:0002061	(Figure 1a)
PMID:22645648	FYPO:0002672	(Figure 1a)
PMID:22645648	GO:0038202	(comment: TOR kinase activity was measured using immunoprecipitated proteins) (Fig. 2)
PMID:22645648	FYPO:0002061	(Figure 6)
PMID:22645648	FYPO:0002672	(Figure 6)
PMID:22645654	FYPO:0002573	(Fig. 4)
PMID:22645654	FYPO:0000088	(Fig. 2e)
PMID:22645654	FYPO:0000268	(Fig. 2e)
PMID:22645654	FYPO:0005438	(Fig. 5)
PMID:22645654	FYPO:0004385	(Fig. 5)
PMID:22645654	FYPO:0000268	(Fig. 2d, e, f)
PMID:22645654	FYPO:0002573	(Fig. 3a-g) (comment: evidence: immunpflouresence)
PMID:22645654	FYPO:0003844	(Fig. 1g)
PMID:22645654	FYPO:0000089	(Fig. 1d)
PMID:22645654	FYPO:0004031	(Fig. 1f) (comment: evidence:immunoblot using anti-thymine dimer anitbodies)
PMID:22645654	FYPO:0001930	(Fig. 1d)
PMID:22645654	FYPO:0000085	(Fig. 1d)
PMID:22645654	GO:1990814	Data from three experiments: DNA reannealing (renaturation assay) using heat-denatured DNA (ssDNA); Removal of RPA proteins associated with ssDNA, RPA-coated heat-denatured DNA (ssDNA) is renaturated; Removal of RNA associated with ssDNA, RNA/DNA hybrid is denatured by renaturation activity of condensin SMC
PMID:22645654	FYPO:0001387	(Fig. 1h)
PMID:22645654	FYPO:0000088	(Fig. 1d)
PMID:22645654	FYPO:0001926	(Fig. 2b, c)
PMID:22645654	FYPO:0002060	(Fig. 2b, c)
PMID:22645654	FYPO:0004385	(Fig. 7)
PMID:22658721	PBO:0095272	(comment: bulky)
PMID:22658721	PBO:0095271	(comment: small)
PMID:22658721	FYPO:0004371	(comment: CHECK NMeed to check, its decreased duration of replication arrest?)
PMID:22660415	PBO:0112094	(Fig. 5B)
PMID:22660415	PBO:0112097	(Fig. 2I)
PMID:22660415	PBO:0112097	(Fig. 2I)
PMID:22660415	PBO:0112096	Thus, Thr 77 and the MELT repeats in Spc7 are in vitro target sites of Mph1 kinase. Fig. 2
PMID:22660415	PBO:0112095	(Fig. 1D)
PMID:22660415	PBO:0097991	Moreover, fission yeast Mph1 (MPS1 homologue), which also localizes to kinetochores only at prometaphase (Supplementary Fig. S1a and Fig. 1D)
PMID:22660415	PBO:0097991	(Fig. 1A)
PMID:22660415	FYPO:0002638	The expression of this fusion protein impairs normal cell growth because of robust SAC activation (Supplementary Fig. S1b,c)
PMID:22660415	PBO:0093563	(Fig. 5F)
PMID:22660415	PBO:0103768	(Fig. 5F)
PMID:22660415	PBO:0103768	(Fig. 5F)
PMID:22660415	PBO:0093563	(Fig. 5F)
PMID:22660415	FYPO:0001357	(Fig. 5F)
PMID:22660415	PBO:0093563	(Fig. 5E)
PMID:22660415	GO:0090266	Thus, the dual regulation of Bub1 by Bub3, suppression of ectopic activation out of the kinetochore and the promotion of its kinetochore recruitment, may play a key role in establishing the robust kinetochore-based SAC activation system.
PMID:22660415	PBO:0093562	(Fig. 5E)
PMID:22660415	PBO:0093562	(Fig. 5E)
PMID:22660415	PBO:0093562	(Fig. 5E)
PMID:22660415	PBO:0093559	(Fig. 5E)
PMID:22660415	PBO:0093559	(Fig. 5E)
PMID:22660415	PBO:0103767	(Fig. 5C)
PMID:22660415	PBO:0103767	(Fig. 5C)
PMID:22660415	PBO:0096163	(Fig. 5C)
PMID:22660415	PBO:0096163	(Fig. 5C)
PMID:22660415	PBO:0103768	(Fig. 5C)
PMID:22660415	PBO:0112235	(Fig. 5C)
PMID:22660415	PBO:0112235	(Fig. 5C)
PMID:22660415	PBO:0112235	(Fig. 5C)
PMID:22660415	PBO:0112235	(Fig. 5C)
PMID:22660415	PBO:0112235	(Fig. 5C)
PMID:22660415	PBO:0112235	(Fig. 5C)
PMID:22660415	PBO:0112233	(Fig. 5C)
PMID:22660415	PBO:0112211	(Fig. 5B)
PMID:22660415	PBO:0112106	(Fig. 5B)
PMID:22660415	PBO:0112105	(Fig. 5B)
PMID:22660415	PBO:0112099	(Fig. 2I)
PMID:22660415	PBO:0112094	(Fig. 5B)
PMID:22660415	PBO:0093559	(Fig. 5E)
PMID:22660415	PBO:0112234	(Fig. 5A)
PMID:22660415	PBO:0112234	(Fig. 5A)
PMID:22660415	PBO:0112210	(Fig. 4C)
PMID:22660415	PBO:0112092	(Fig. 4B)
PMID:22660415	PBO:0112094	(Fig. 5B)
PMID:22660415	PBO:0112233	(Fig. 5A)
PMID:22660415	PBO:0112101	(Fig. 2I)
PMID:22660415	PBO:0112101	(Fig. 2I)
PMID:22660415	PBO:0112233	(Fig. 5A)
PMID:22660415	PBO:0112233	(Fig. 5A)
PMID:22660415	PBO:0112234	(Fig. 5A)
PMID:22660415	PBO:0100097	During this analysis, we found that at least four sites (Thr 77, Thr 338, Thr 507 and Thr 552) are phosphorylated by Mph1 in vitro (Supplementary Fig. S2).
PMID:22660415	PBO:0112234	(Fig. 5A)
PMID:22660415	PBO:0112094	(Fig. 5B)
PMID:22660415	PBO:0112091	(Fig. 4B)
PMID:22660415	PBO:0112102	(Fig. 2I)
PMID:22660415	PBO:0112102	(Fig. 2I)
PMID:22660415	PBO:0112100	(Fig. 2I)
PMID:22660415	PBO:0112098	(Fig. 2I)
PMID:22660415	PBO:0112098	(Fig. 2I)
PMID:22660415	FYPO:0004318	Accordingly, the ectopic localization of Bub1 and the mitotic delay induced by Cnp3C-Mph1 were abolished by the spc7-12A mutation (Supplementary Fig. S3a)
PMID:22660415	PBO:0112109	although the kinetochore localization of Spc7-12A protein was intact (Fig. 2f)
PMID:22660415	PBO:0112108	(Fig. 5E)
PMID:22660415	PBO:0100097	During this analysis, we found that at least four sites (Thr 77, Thr 338, Thr 507 and Thr 552) are phosphorylated by Mph1 in vitro (Supplementary Fig. S2).
PMID:22660415	PBO:0100097	During this analysis, we found that at least four sites (Thr 77, Thr 338, Thr 507 and Thr 552) are phosphorylated by Mph1 in vitro (Supplementary Fig. S2).
PMID:22660415	PBO:0100097	During this analysis, we found that at least four sites (Thr 77, Thr 338, Thr 507 and Thr 552) are phosphorylated by Mph1 in vitro (Supplementary Fig. S2).
PMID:22660415	PBO:0093562	(Fig. 5E)
PMID:22660415	PBO:0112085	(Fig. 2G)
PMID:22660415	PBO:0112086	Accordingly, Bub3 and Mad3 localized at kinetochores in a manner identical to Bub1 in spc7-12A and spc7-12E cells
PMID:22660415	PBO:0112087	Accordingly, Bub3 and Mad3 localized at kinetochores in a manner identical to Bub1 in spc7-12A and spc7-12E cells
PMID:22660415	PBO:0112088	(Fig. 1B) This Bub1 enrichment is diminished in the spc7-23 mutant at a restrictive temperature24 (Fig. 1b).
PMID:22660415	PBO:0112055	(Fig. 1E)
PMID:22660415	PBO:0112085	(Fig. 1C)
PMID:22660415	PBO:0112089	Strikingly, in spc7-12E cells, Bub1 localized at kinetochores throughout the entire cell cycle. Fig. 2H, I and S3C
PMID:22660415	PBO:0112209	However, the coexpression of Bub1 and Bub3 enabled this complex to interact with Spc7-12E. Fig. 4C
PMID:22660415	PBO:0112091	(Fig. 4B)
PMID:22660415	PBO:0112092	(Fig. 4B)
PMID:22660415	PBO:0112233	(Fig. 5A)
PMID:22660415	PBO:0103768	(Fig. 5C)
PMID:22665807	PBO:0096303	Table S1, Figure S1
PMID:22665807	PBO:0096314	(Fig. 4b)
PMID:22665807	PBO:0096312	(Fig. 4b)
PMID:22665807	PBO:0096312	(Fig. 4b)
PMID:22665807	PBO:0096312	(Fig. 4b)
PMID:22665807	PBO:0096312	(Fig. 4b)
PMID:22665807	PBO:0096311	(Fig. 4b)
PMID:22665807	PBO:0096311	(Fig. 4b)
PMID:22665807	PBO:0096311	(Fig. 4b)
PMID:22665807	PBO:0096311	(Fig. 4b)
PMID:22665807	PBO:0096311	(Fig. 4b)
PMID:22665807	FYPO:0004474	(Fig. 3b)
PMID:22665807	PBO:0096310	(Fig. 3a)
PMID:22665807	PBO:0096308	(Fig. 2A)
PMID:22665807	PBO:0096308	(Fig. 2A)
PMID:22665807	PBO:0096308	(Fig. 2A)
PMID:22665807	PBO:0096308	(Fig. 2A)
PMID:22665807	PBO:0096308	(Fig. 2A)
PMID:22665807	PBO:0096307	(Fig. 2A)
PMID:22665807	PBO:0096308	(Fig. 1d)
PMID:22665807	FYPO:0006822	(Figure 2A)
PMID:22665807	PBO:0096307	(Fig. 2A)
PMID:22665807	PBO:0096306	(Fig. 1d)
PMID:22665807	PBO:0096305	(Fig. 1c)
PMID:22665807	PBO:0096304	Table S1, Figure S1
PMID:22665807	PBO:0096304	Table S1, Figure S1
PMID:22665807	PBO:0096303	Table S1, Figure S1
PMID:22665807	PBO:0096303	Table S1, Figure S1
PMID:22665807	PBO:0096303	Table S1, Figure S1
PMID:22665807	PBO:0096303	Table S1, Figure S1
PMID:22665807	PBO:0096304	Table S1, Figure S1
PMID:22665807	PBO:0096304	Table S1, Figure S1
PMID:22665807	PBO:0096303	Table S1, Figure S1
PMID:22665807	PBO:0096303	Table S1, Figure S1
PMID:22682245	FYPO:0002060	implies that dna2 K961T alone is viable
PMID:22682245	FYPO:0002061	implies that dna2 E560A alone is inviable
PMID:22682245	GO:1990601	cleaves unpaired nascent DNA in replication forks
PMID:22683269	GO:0003723	assayed using bulk RNA
PMID:22684255	FYPO:0000405	(Figure 4d)
PMID:22684255	PBO:0100303	(Figure 2f lanes 1, 2)
PMID:22684255	FYPO:0000405	(Figure 4d)
PMID:22684255	FYPO:0000400	(Figure 4d)
PMID:22684255	FYPO:0003306	(Figure 4d)
PMID:22684255	PBO:0092296	(Figure 1a)
PMID:22684255	PBO:0100305	(comment: CHECK upstream of pom1)
PMID:22684255	FYPO:0000400	(Figure 4d)
PMID:22684255	FYPO:0000400	(Figure 4d)
PMID:22684255	FYPO:0000400	(Figure 4d)
PMID:22684255	PBO:0100302	(Figure 2f lanes 1, 2)
PMID:22684255	FYPO:0003306	(Figure 3a)
PMID:22684255	GO:0010971	(Figure 4b) confirming that each kinase promotes mitotic commitment.
PMID:22684255	FYPO:0000400	(Figure 4d)
PMID:22684255	FYPO:0000400	(Figure 4d)
PMID:22684255	FYPO:0000400	(Figure 4d)
PMID:22684255	FYPO:0000400	(Figure 4d)
PMID:22684255	PBO:0100302	(Figure 2f lanes 1, 2)
PMID:22684255	PBO:0100301	(Figure 1g)
PMID:22684255	GO:0010971	(comment: CHECK mitotic commitment)
PMID:22684255	FYPO:0003481	(Figure 3A; Table 1) indicating that inhibition of Sid2 or Fin1 delayed the timing of mitotic commitment until a new size threshold for division was me
PMID:22684255	FYPO:0003481	(Figure 3A; Table 1) indicating that inhibition of Sid2 or Fin1 delayed the timing of mitotic commitment until a new size threshold for division was me
PMID:22684255	FYPO:0003306	(Figure 3a)
PMID:22684255	PBO:0100301	(Figure 1g)
PMID:22684255	PBO:0097831	(Figure 1b)
PMID:22684255	PBO:0097831	(Figure 1b)
PMID:22696680	FYPO:0002760	(Figure 1)
PMID:22696680	FYPO:0004731	(Figure 1)
PMID:22696680	PBO:0018346	(Fig. 1A)
PMID:22696680	GO:0061863	(Figure 3) Supplemental Table S2, and Supplemental Figure S4
PMID:22696680	PBO:0037217	(growing) fig 1A
PMID:22696680	PBO:0103480	Supplemental Figure S1, C-E
PMID:22696680	PBO:0098921	Supplemental Figure S1, C-E
PMID:22696680	PBO:0103479	Supplemental Figure S1, C-E
PMID:22696680	FYPO:0005682	(Figure 2D,2F)
PMID:22696680	FYPO:0005681	(Figure 2D,2F)
PMID:22696680	FYPO:0005797	(Figure 2C)
PMID:22696680	FYPO:0002818	(Figure 2B)
PMID:22696680	PBO:0019801	(Fig. 1A)
PMID:22696680	FYPO:0002760	(Figure 1)
PMID:22696680	FYPO:0004731	(Figure 1)
PMID:22696680	FYPO:0002112	(Figure 2A)
PMID:22696680	FYPO:0001234	(Figure 2A)
PMID:22705791	GO:0004518	(comment: CHECK not sure if it is endo, exo, or both. It is def acting on DNA. More specific terms for DNA specify endo or exo.)
PMID:22705791	FYPO:0003164	(comment: CHECK not sure if it is endo, exo or both? so went with more general term)
PMID:22711988	GO:0000776	kinetochore localization requires MIND complex
PMID:22711988	PBO:0103997	implies that MIND complex is required for Sos7 to localize to the kinetochore
PMID:22718908	FYPO:0006728	BrdU incorporation
PMID:22718908	PBO:0103909	inferred from localization of proteins distal to origin
PMID:22718908	PBO:0103928	inferred from localization of proteins distal to origin
PMID:22718908	FYPO:0006726	inferred from normal localization of CMG proteins at origin
PMID:22718908	FYPO:0006727	BrdU incorporation
PMID:22718908	PBO:0103909	inferred from localization of proteins distal to origin
PMID:22718908	FYPO:0006728	BrdU incorporation
PMID:22718908	FYPO:0006728	BrdU incorporation
PMID:22718908	PBO:0103920	inferred from localization of proteins distal to origin
PMID:22723423	GO:0009378	(comment: Fml1 catalyses the dissociation of displacement (D) loops)
PMID:22723423	GO:0000400	(comment: Fml1 binds to the four-way junction at a displacement (D) loop.)
PMID:22727667	PBO:0119840	(comment: binds H3K9me)
PMID:22727667	PBO:0119842	(comment: binds H3K9me)
PMID:22727667	PBO:0119841	(comment: binds H3K9me)
PMID:22737087	FYPO:0007391	data not shown
PMID:22737087	PBO:0093560	(Fig. 2) (comment: decreased aneuploid cell viability during vegetative growth)
PMID:22737087	PBO:0093560	(Fig. 2) (comment: decreased aneuploid cell viability during vegetative growth)
PMID:22737087	PBO:0104054	(Fig. 1, Table 1) (comment: affects C1 and C2 type colonies)
PMID:22737087	PBO:0093560	(Fig. 2)
PMID:22737087	PBO:0093560	(Fig. 2)
PMID:22737087	PBO:0093560	(Fig. 2) (comment: decreased aneuploid cell viability during vegetative growth)
PMID:22737087	PBO:0093559	(Fig. S1) (comment: decreased aneuploid cell viability during vegetative growth)
PMID:22737087	PBO:0093561	(Fig. S1) (comment: decreased aneuploid cell viability during vegetative growth)
PMID:22737087	PBO:0093561	data not shown
PMID:22737087	PBO:0093560	(Fig. S1) (comment: CHECK decreased aneuploid cell viability during vegetative growth)
PMID:22737087	PBO:0104054	(Fig. 2)
PMID:22737087	PBO:0104054	(Fig. 1 Table 1) (comment: affects C1 more than C2 type colonies)
PMID:22737087	PBO:0104055	Table 2 (comment: This strain is disomic for Chromosome 3)
PMID:22737087	PBO:0104055	Table 2 (comment: This strain is disomic for Chromosome 3)
PMID:22737087	PBO:0104054	(Fig. 1, Table 1) (comment: affects C1 type colonies)
PMID:22737087	PBO:0104054	(Fig. 1, Table 1) (comment: affects C1 type colonies)
PMID:22737087	PBO:0104054	(Fig. 1, Table 1) (comment: affects C1 and C2 type colonies)
PMID:22737087	PBO:0093560	(Fig. 6) (comment: reduced growth may not be specific to aneuploidy as it also interacts with gtb1-93)
PMID:22737087	PBO:0093560	(Fig. 6)
PMID:22737087	PBO:0093560	(Fig. 6)
PMID:22737087	PBO:0093560	(Fig. 6)
PMID:22737087	PBO:0093560	(Fig. 6)
PMID:22737087	PBO:0093560	(Fig. 6)
PMID:22737087	PBO:0104055	Table 2 (comment: This strain is disomic for Chromosome 3)
PMID:22737087	FYPO:0001326	(comment: All the genes affect by at least 1.5 fold (17) are reported in Table S2)
PMID:22737087	FYPO:0001326	(comment: All the genes affect by at least 1.5 fold (61) are reported in Table S2)
PMID:22737087	FYPO:0001326	(comment: All the genes affect by at least 1.5 fold (141) are reported in Table S2)
PMID:22737087	FYPO:0007391	(Fig. 4) (comment: Type C1 colonies have highly elongated cells and are due to various types of aneuploidy. Authors suggest that not3 is required to maintain cell growth)
PMID:22737087	PBO:0104055	Table 2 (comment: This strain is disomic for Chromosome 3)
PMID:22737087	PBO:0104055	(Fig. 3B) (comment: This strain is disomic for Chromosome 3)
PMID:22737087	PBO:0093558	(Fig. 3A) (comment: This strain is disomic for Chromosome 3)
PMID:22737087	PBO:0104055	(Fig. 3B) ((comment: This strain is disomic for Chromosome 3)
PMID:22737087	PBO:0093558	(Fig. 3A) (comment: This strain is disomic for Chromosome 3)
PMID:22737087	PBO:0104054	Table1 Fig1 (comment: affects C1 and C2 type colonies)
PMID:22737087	PBO:0093559	(Fig. 2) (comment: reduced growth may not be specific to aneuploidy as it also interact with gtb1 though looks quite good to me)
PMID:22737087	PBO:0093560	(Fig. 2) (comment: reduced growth may not be specific to aneuploidy as it also interacts with gtb1)
PMID:22737087	FYPO:0001357	(Fig. 2) (comment: normal population growth in presence of aneuploid cells)
PMID:22737087	FYPO:0001357	(Fig. 2) (comment: normal population growth in presence of aneuploid cells)
PMID:22737087	FYPO:0007391	data not shown
PMID:22737087	FYPO:0007391	data not shown
PMID:22737087	FYPO:0007391	data not shown
PMID:22768388	FYPO:0005177	(Figure S1C)
PMID:22768388	FYPO:0003218	(Figures S1C and S1D)
PMID:22768388	FYPO:0000082	(Fig. 1A)
PMID:22768388	FYPO:0001234	(Figure 1C)
PMID:22768388	FYPO:0000118	(Figure 1B)
PMID:22768388	FYPO:0000082	(Figure 1A)
PMID:22768388	FYPO:0000082	(Figure 1A)
PMID:22768388	FYPO:0001357	(Figure 1C)
PMID:22768388	FYPO:0002672	(Figure S1E)
PMID:22768388	FYPO:0002672	(Figure S1E)
PMID:22768388	FYPO:0002672	(Figure S1E)
PMID:22768388	FYPO:0002672	(Figure S1E)
PMID:22768388	FYPO:0000674	(Figure S1E)
PMID:22768388	FYPO:0000674	(Figure S1E)
PMID:22768388	FYPO:0001357	(Figure 1C)
PMID:22768388	FYPO:0001357	(Figure 1C)
PMID:22768388	FYPO:0000674	(Figure S1E)
PMID:22768388	FYPO:0000082	(Figure 1A)
PMID:22768388	FYPO:0001234	(Figure 1C)
PMID:22768388	FYPO:0000674	(Figure S1E)
PMID:22768388	FYPO:0000082	(Fig. 1A)
PMID:22768388	FYPO:0001234	(Figure 1C)
PMID:22768388	FYPO:0000118	(Figure 1B)
PMID:22768388	FYPO:0002834	(Figure S4)
PMID:22768388	FYPO:0002360	data not shown
PMID:22768388	PBO:0104835	(Fig. 4C)
PMID:22768388	FYPO:0003503	data not shown
PMID:22768388	FYPO:0001492	(Figure 1B)
PMID:22768388	FYPO:0001492	(Figure 1B)
PMID:22792081	PBO:0111547	(comment: CHECK This interaction depends on the phosphorylation of Crb2 on the T73 and S80 residues.)
PMID:22792081	GO:0005515	(comment: CHECK This interaction depends on the phosphorylation of Crb2 on the T73 and S80 residues.)
PMID:22792081	PBO:0104543	(comment: CHECK This interaction depends on the phosphorylation of Crb2 on the T73 and S80 residues.)
PMID:22809626	PBO:0022948	"(comment: happens during metaphase and happens during anaphase. I can't say ""decreased during cytokinesis"", only option would be to say ""not during cytokinesis"" which isn't strictly true.)"
PMID:22809626	PBO:0022949	"(comment: happens during metaphase and happens during anaphase. I can't say ""decreased during cytokinesis"", only option would be to say ""not during cytokinesis"" which isn't strictly true.)"
PMID:22809626	PBO:0022948	"(comment: happens during metaphase and happens during anaphase. I can't say ""decreased during cytokinesis"", only option would be to say ""not during cytokinesis"" which isn't strictly true.)"
PMID:22809626	PBO:0022949	"(comment: happens during metaphase and happens during anaphase. I can't say ""decreased during cytokinesis"", only option would be to say ""not during cytokinesis"" which isn't strictly true.)"
PMID:22825872	PBO:0096331	(Fig. S9F)
PMID:22825872	PBO:0096316	(Fig. 4A and S8)
PMID:22825872	PBO:0096318	The shorter truncation (Mph1-D1-150) maintained kinetochore localization and SAC signaling
PMID:22825872	PBO:0096319	(Fig. 4C).
PMID:22825872	PBO:0096319	(Fig. 4A and S7)
PMID:22825872	GO:0090267	Together this suggests that Ark1 is directly and continuously required to maintain Mph1 localization to kinetochores.
PMID:22825872	FYPO:0004318	In the presence of Mph1-D1-302, the SAC response in bub3D cells was abrogated (Fig. 2C), demonstrating that recruitment of Mph1 to kinetochores is necessary for SAC function in bub3D cells.
PMID:22825872	PBO:0096318	Mph1 localizes to unattached kinetochores in bub3D cells (Fig. 2A).
PMID:22825872	PBO:0096320	(Fig. 4B and S5)
PMID:22825872	PBO:0096318	(Fig. 4A and S1)
PMID:22825872	PBO:0096321	(Fig. 4A and S9)
PMID:22825872	PBO:0096322	(Fig. S5)
PMID:22825872	PBO:0096323	(Fig. S6) Indeed, Ark1 and Mph1 are fully or partially required for the kinetochore enrichment of all other SAC proteins (Fig. 4A; supplementary material Figs S5-S10).
PMID:22825872	PBO:0096315	(Fig. S7)
PMID:22825872	PBO:0096316	(Fig. S8)
PMID:22825872	PBO:0096322	(Fig. 4B)
PMID:22825872	PBO:0096315	(Fig. 4C)
PMID:22825872	PBO:0096315	Indeed, Ark1 and Mph1 are fully or partially required for the kinetochore enrichment of all other SAC proteins (Fig. 4A; supplementary material Figs S5-S10).
PMID:22825872	PBO:0096317	(Fig. 2A) When proper chromosome attachment was prevented by a conditional mutation in kinesin-5 (cut7-446), Mph1 localized to kinetochores, but the enrichment was abrogated by chemical genetic inhibition of Ark1 with the small molecule 1NM-PP1 (Fig. 3A).
PMID:22825872	PBO:0096316	(Figure S8E and F) Indeed, Ark1 and Mph1 are fully or partially required for the kinetochore enrichment of all other SAC proteins (Fig. 4A; supplementary material Figs S5-S10).
PMID:22825872	PBO:0096324	(Figure S4B and C)
PMID:22825872	PBO:0096325	(Figure S4B and C)
PMID:22825872	PBO:0096326	(Figure S4B and C)
PMID:22825872	PBO:0096327	(comment: CHECK 60% cells) Forced recruitment of wild-type Mph1 to kinetochores lead to apronounced delay in mitosis and a growth defect (Fig. 1E,F)
PMID:22825872	FYPO:0003736	rescued by deletion of mad2, which (forced recruitment of Mph1 artificially promoted SAC signaling andthat the fusion to Mis12 did not impair kinetochore function.
PMID:22825872	PBO:0096328	(comment: CHECK 35% cells) (Fig. 1E,F).
PMID:22825872	FYPO:0003762	and the fraction of cells, in which a signal could be detected (supplementary material Fig. S1), were similar between bub3+ and bub3D cells
PMID:22825872	FYPO:0004318	and the fraction of cells, in which a signal could be detected (supplementary material Fig. S1), were similar between bub3+ and bub3D cells
PMID:22825872	FYPO:0005781	In the presence of Mph1-D1-150, the SAC was still functional in bub3D cells, although the mitotic delay was shorter than in mph1-D1-150 or bub3D cells (Fig. 2C).
PMID:22825872	PBO:0096315	(Fig. 4A and S7)
PMID:22825872	PBO:0096330	(Fig. 3B) Indeed, Ark1 and Mph1 are fully or partially required for the kinetochore enrichment of all other SAC proteins (Fig. 4A; supplementary material Figs S5-S10).
PMID:22825872	PBO:0096316	(Fig. 4A and S8)
PMID:22825872	PBO:0096317	abolished both kinetochore localization and SAC signaling (Fig. 1C,D), suggesting that kinetochore localization is crucial for SAC activity.
PMID:22825872	FYPO:0004318	comment: CHECK ditto
PMID:22825872	FYPO:0003762	The shorter truncation (Mph1-D1-150) maintained kinetochore localization and SAC signaling
PMID:22825872	FYPO:0003307	(Fig. 3C)increased mitotic index (Fig. S4A)
PMID:22825872	FYPO:0003307	(Fig. 3C) (inhibiting Ark1 does not rescue the Mph1-kinetochore targeting, arguing that Ark1 is upstream)
PMID:22848669	PBO:0112962	(Figure 3B)
PMID:22848669	PBO:0093641	(Figure 2)
PMID:22848669	FYPO:0002060	We constructed a null mutation in the ecm33+ and gaz2+ genes, respectively (see Materials and Methods) and found that the gaz2 deletion mutant was also viable (Figure 2A, upper panel), indicating that Gaz2 is not essential for cell viability.
PMID:22848669	FYPO:0002060	We constructed a null mutation in the ecm33+ and gaz2+ genes, respectively (see Materials and Methods) and found that the gaz2 deletion mutant was also viable (Figure 2A, upper panel), indicating that Gaz2 is not essential for cell viability.
PMID:22848669	PBO:0093645	Likewise, these three genes complemented the FK506-sensitive phenotype of the cis4-1 mutant (Figure 1A).
PMID:22848669	PBO:0093645	Likewise, these three genes complemented the FK506-sensitive phenotype of the cis4-1 mutant (Figure 1A).
PMID:22848669	PBO:0093644	Likewise, these three genes complemented the FK506-sensitive phenotype of the cis4-1 mutant (Figure 1A).
PMID:22848669	PBO:0093641	Likewise, these three genes complemented the FK506-sensitive phenotype of the cis4-1 mutant (Figure 1A).
PMID:22848669	PBO:0108284	Notably, overexpression of the ecm33+ gene partially suppressed the MgCl2 sensitivity of cis4-1 mutant, and overexpression of the aah3+ and gaz2+ genes more strongly suppressed the MgCl2 sensitivity of the cis4-1 mutant (Figure 1A).
PMID:22848669	PBO:0108284	Notably, overexpression of the ecm33+ gene partially suppressed the MgCl2 sensitivity of cis4-1 mutant, and overexpression of the aah3+ and gaz2+ genes more strongly suppressed the MgCl2 sensitivity of the cis4-1 mutant (Figure 1A).
PMID:22848669	PBO:0095501	Notably, overexpression of the ecm33+ gene partially suppressed the MgCl2 sensitivity of cis4-1 mutant, and overexpression of the aah3+ and gaz2+ genes more strongly suppressed the MgCl2 sensitivity of the cis4-1 mutant (Figure 1A).
PMID:22848669	PBO:0101760	The cis4-1 mutant cells grew well in rich YPD medium, however, in the presence of 0.15 M MgCl2, the cis4-1 cells failed to grow, whereas wild-type cells grew well (Figure 1A).
PMID:22848669	GO:0099638	Thus, GFP-Ecm33 localized at Golgi/endosome structures in addition to the cell surface and the division site in these mutants, suggesting that GPI-anchored proteins were not correctly transported and were retained at the Golgi/endosome structures in these membrane trafficking mutants
PMID:22848669	GO:0099638	Thus, GFP-Ecm33 localized at Golgi/endosome structures in addition to the cell surface and the division site in these mutants, suggesting that GPI-anchored proteins were not correctly transported and were retained at the Golgi/endosome structures in these membrane trafficking mutants
PMID:22848669	PBO:0112962	(Figure 3B)
PMID:22848669	PBO:0112963	(Figure 3C) The immunoblot analysis detected an appreciable amount of Ecm33 fragments A, C, F, G, and I
PMID:22848669	PBO:0112963	(Figure 3C) The immunoblot analysis detected an appreciable amount of Ecm33 fragments A, C, F, G, and I
PMID:22848669	PBO:0112963	(Figure 3C) The immunoblot analysis detected an appreciable amount of Ecm33 fragments A, C, F, G, and I
PMID:22848669	PBO:0112963	(Figure 3C) The immunoblot analysis detected an appreciable amount of Ecm33 fragments A, C, F, G, and I
PMID:22848669	PBO:0112963	(Figure 3C) The immunoblot analysis detected an appreciable amount of Ecm33 fragments A, C, F, G, and I
PMID:22848669	PBO:0112964	(Figure 3C) but failed to detect fragment B, D, E, H, J or K.
PMID:22848669	PBO:0112964	(Figure 3C) but failed to detect fragment B, D, E, H, J or K.
PMID:22848669	PBO:0112964	(Figure 3C) but failed to detect fragment B, D, E, H, J or K.
PMID:22848669	PBO:0112964	(Figure 3C) but failed to detect fragment B, D, E, H, J or K.
PMID:22848669	PBO:0112964	(Figure 3C) but failed to detect fragment B, D, E, H, J or K.
PMID:22848669	PBO:0112964	(Figure 3C) but failed to detect fragment B, D, E, H, J or K.
PMID:22848669	GO:0009986	Ecm33 localized to the cell surface or the medial regions. (Figure 4)
PMID:22848669	PBO:0114642	As expected, GFP-Ecm33 primarily localized to the ER and to the cell surface in the its8-1 mutant cells (Figure 4D, arrows), suggesting that the impairment of GPI anchor synthesis caused the defective attachment of GPI-anchor to the Ecm33 protein thereby resulting in the abnormal GFP-Ecm33 localization in the ER.
PMID:22848669	PBO:0112967	Similarly, in the wild-type cells, GFP-Gaz2 also clearly localized at the cell surface and medial regions (Figure 6C), while in Dapm1 cells, GFP-Gaz2 localized as intracellular dot-like structures (Figure 6C).
PMID:22848669	PBO:0112967	Similarly, in the wild-type cells, GFP-Gaz2 also clearly localized at the cell surface and medial regions (Figure 6C), while in Dapm1 cells, GFP-Gaz2 localized as intracellular dot-like structures (Figure 6C).
PMID:22848669	PBO:0093641	The results showed that the addition of Zn2+ to the medium significantly rescued the high temperature-sensitive and FK506-sensitive phenotypes of the its8-1 mutant (Figure 5A)
PMID:22848669	PBO:0112961	The results showed that the addition of Zn2+ to the medium significantly rescued the high temperature-sensitive and FK506-sensitive phenotypes of the its8-1 mutant (Figure 5A)
PMID:22848669	PBO:0093558	On the effect of temperature, in the its8-1Dcis4 double mutants, these cells exhibited more marked temperature sensitivity than that of the its8-1 single mutants (Figure 5B), suggesting that there is a genetic interaction between Its8 and Cis4.
PMID:22848669	PBO:0093558	On the effect of temperature, in the its8-1Dcis4 double mutants, these cells exhibited more marked temperature sensitivity than that of the its8-1 single mutants (Figure 5B), suggesting that there is a genetic interaction between Its8 and Cis4.
PMID:22848669	PBO:0093557	On the effect of temperature, in the its8-1Dcis4 double mutants, these cells exhibited more marked temperature sensitivity than that of the its8-1 single mutants (Figure 5B), suggesting that there is a genetic interaction between Its8 and Cis4.
PMID:22848669	PBO:0114643	(comment: ****decreased to cell surface, mislocalized to cytoplasm*****) In Dapm1 cells, in contrast, GFP-Ecm33 primarily localized as dot-like structures that were observed in the cytoplasm (Figure 6A, arrows) as well as at the cell surface and the division site (Figure 6A, arrowheads).
PMID:22848669	PBO:0112966	Thus, GFP-Ecm33 localized at Golgi/endosome structures in addition to the cell surface and the division site in these mutants, suggesting that GPI-anchored proteins were not correctly transported and were retained at the Golgi/endosome structures in these membrane trafficking mutants
PMID:22848669	PBO:0093558	On the effect of temperature, in the its8-1Dcis4 double mutants, these cells exhibited more marked temperature sensitivity than that of the its8-1 single mutants (Figure 5B), suggesting that there is a genetic interaction between Its8 and Cis4.
PMID:22848669	PBO:0112966	Thus, GFP-Ecm33 localized at Golgi/endosome structures in addition to the cell surface and the division site in these mutants, suggesting that GPI-anchored proteins were not correctly transported and were retained at the Golgi/endosome structures in these membrane trafficking mutants
PMID:22848669	GO:0099638	Thus, GFP-Ecm33 localized at Golgi/endosome structures in addition to the cell surface and the division site in these mutants, suggesting that GPI-anchored proteins were not correctly transported and were retained at the Golgi/endosome structures in these membrane trafficking mutants
PMID:22848669	PBO:0112966	Thus, GFP-Ecm33 localized at Golgi/endosome structures in addition to the cell surface and the division site in these mutants, suggesting that GPI-anchored proteins were not correctly transported and were retained at the Golgi/endosome structures in these membrane trafficking mutants
PMID:22848669	PBO:0112962	(Figure 3B)
PMID:22848669	PBO:0112962	(Figure 3B)
PMID:22848669	PBO:0112962	(Figure 3B)
PMID:22848669	PBO:0101760	(Figure 3B)
PMID:22848669	PBO:0101760	(Figure 3B)
PMID:22848669	PBO:0101760	(Figure 3B)
PMID:22848669	PBO:0101760	(Figure 3B)
PMID:22848669	PBO:0101760	(Figure 3B)
PMID:22848669	PBO:0101760	(Figure 3B)
PMID:22848669	PBO:0112962	(Figure 2)
PMID:22848669	PBO:0112961	(Figure 2)
PMID:22848669	PBO:0096587	(Figure 2)
PMID:22848669	PBO:0101760	(Figure 2)
PMID:22891259	GO:0005886	Localized at cell tips, actomyosin contractile ring and septum
PMID:22891259	GO:0032153	(Fig. 1)
PMID:22891259	GO:0031671	Explosive cell separation due to a weak primary septum. Absence of a secondary septum.
PMID:22891259	GO:0032153	(Fig. 1)
PMID:22891673	FYPO:0000639	decreased/delayed septum closure
PMID:22891673	FYPO:0000650	septation index increased gradually over time
PMID:22891673	FYPO:0000650	septation index constantly high
PMID:22891673	FYPO:0000639	decreased septum closure
PMID:22891673	FYPO:0002526	(comment: assayed at 32C, which is semi-permissive for sec3-913)
PMID:22891673	FYPO:0002438	Weak actin cables
PMID:22891673	FYPO:0000424	(comment: Assayed by FM4-64 uptake)
PMID:22891673	FYPO:0000230	At the end of ring constriction Filamentous projections from the unclosed ring toward the cytoplasm
PMID:22891673	PBO:0018345	normal localization in several mutants indicates that Sec3 localization is independent of exocytosis and vesicle-mediated transport along microtubules
PMID:22895252	GO:0030466	(Fig. S2)
PMID:22905165	PBO:0035602	(comment: Cdc15-GFP)
PMID:22905165	PBO:0105433	(Fig. S1)
PMID:22905165	PBO:0022652	(comment: used sorbitol but multiple stresses were tested) Cdc15-GFP However, we observed that a number of the Cdc15-GFP and the GFP-Cdc4 rings were asymmetric or broken.
PMID:22905165	PBO:0105443	(Fig. 1B)
PMID:22905165	PBO:0105442	(Fig. 1B) in which the SIN signal does not turn off, Cfh3p localized to the edge of the growing septa and it remained at the septal area after the septa had been completed. Thus, Cfh3p can arrive at the cell midzone in the absence of the SIN pathway but it requires that the SIN signal must be turned off for it to be removed from the cell equator after mitosis
PMID:22905165	PBO:0105441	(Fig. 1B) in which the SIN signal does not turn off, Cfh3p localized to the edge of the growing septa and it remained at the septal area after the septa had been completed. Thus, Cfh3p can arrive at the cell midzone in the absence of the SIN pathway but it requires that the SIN signal must be turned off for it to be removed from the cell equator after mitosis
PMID:22905165	PBO:0105440	(Figure S2) (comment: A protein distributed in cortex)
PMID:22905165	PBO:0105439	(comment: GFP-Bgs1)
PMID:22905165	PBO:0096859	(comment: GFP-Bgs1)
PMID:22905165	PBO:0035602	(comment: Cdc15-GFP) Supplemental Figure S3
PMID:22905165	PBO:0105434	(Fig. S1)
PMID:22905165	PBO:0022652	(comment: Cdc15-GFP) However, we observed that a number of the Cdc15-GFP and the GFP-Cdc4 rings were asymmetric or broken.
PMID:22905165	PBO:0098289	(comment: GFP-Cfh3) Figure 1A
PMID:22905165	PBO:0018345	(comment: GFP-Cfh3) Figure 1A
PMID:22905165	PBO:0105436	(Fig. S1)
PMID:22905165	PBO:0105435	(Fig. S1)
PMID:22912768	PBO:0096132	(comment: mah: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03))
PMID:22912768	PBO:0096133	(comment: mah: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03))
PMID:22912768	PBO:0096135	(comment: mah: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03))
PMID:22912768	PBO:0096134	(comment: mah: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03))
PMID:22912768	PBO:0095155	(comment: mah: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03))
PMID:22912768	PBO:0096136	(comment: mah: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03))
PMID:22912768	PBO:0095154	(comment: mah: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03))
PMID:22918943	PBO:0095814	(Figure 7)
PMID:22918943	GO:0071341	(Figure 1A, 2A)
PMID:22918943	PBO:0095813	(Figure 5, I, J, and L)
PMID:22918943	GO:0110115	(Figure 1A, 2A)
PMID:22918943	PBO:0095811	(Figure 5, I, J, and L)
PMID:22918943	PBO:0095812	(Figure 5, I, J, and L)
PMID:22918943	FYPO:0004594	(Figure 7)
PMID:22918943	FYPO:0003339	(Figure 3A)
PMID:22918943	FYPO:0001364	(Figure 3A)
PMID:22918952	PBO:0099901	(comment: unspecfied RxxS site(s))
PMID:22918952	PBO:0099900	(comment: unspecfied RxxS site(s))
PMID:22918954	PBO:0099646	(Figure 4)
PMID:22918954	PBO:0099643	(Fig. 3B)
PMID:22918954	FYPO:0003203	(Fig. 3B)
PMID:22918954	FYPO:0004750	(Fig. 3B)
PMID:22918954	PBO:0098959	(Fig. 3B) (comment: COMMENT CHECK asymettrically localized septum)
PMID:22918954	PBO:0099644	(Fig. 3B)
PMID:22918954	PBO:0099644	(Fig. 3B)
PMID:22918954	PBO:0099644	(Fig. 3B)
PMID:22918954	PBO:0099645	(Fig. 3B)
PMID:22918954	PBO:0099645	(Fig. 3B)
PMID:22918954	PBO:0099645	(Fig. 3B)
PMID:22918954	PBO:0099646	(Figure 4)
PMID:22918954	PBO:0099646	(Figure 4)
PMID:22918954	PBO:0099646	(Figure 4)
PMID:22918954	PBO:0099646	(Figure 4)
PMID:22918954	PBO:0099646	(Figure 4)
PMID:22918954	PBO:0099647	(Figure 4)
PMID:22959349	PBO:0104363	Cdc2 phosphorylates Rap1 at Thr378, Ser422, and Ser513 during M phase. Ser456 of Rap1 is also phosphorylated during M phase by an unknown kinase. Ser213 of Rap1 is phosphorylated throughout the cell cycle. These phosphorylations are required for the efficient detachment of telomeres from the nuclear envelope.
PMID:22959349	PBO:0103680	(comment: at Ser/Thr-Pro site)
PMID:22959349	PBO:0103680	(comment: at Ser/Thr-Pro site)
PMID:22959349	PBO:0020538	Cdc2 phosphorylates Rap1 at Thr378, Ser422, and Ser513 during M phase. Ser456 of Rap1 is also phosphorylated during M phase by an unknown kinase. Ser213 of Rap1 is phosphorylated throughout the cell cycle. These phosphorylations are required for the efficient detachment of telomeres from the nuclear envelope.
PMID:22959349	PBO:0020539	Cdc2 phosphorylates Rap1 at Thr378, Ser422, and Ser513 during M phase. Ser456 of Rap1 is also phosphorylated during M phase by an unknown kinase. Ser213 of Rap1 is phosphorylated throughout the cell cycle. These phosphorylations are required for the efficient detachment of telomeres from the nuclear envelope.
PMID:22959349	PBO:0103680	(comment: at Ser/Thr-Pro site)
PMID:22959349	PBO:0104363	Cdc2 phosphorylates Rap1 at Thr378, Ser422, and Ser513 during M phase. Ser456 of Rap1 is also phosphorylated during M phase by an unknown kinase. Ser213 of Rap1 is phosphorylated throughout the cell cycle. These phosphorylations are required for the efficient detachment of telomeres from the nuclear envelope.
PMID:22959349	PBO:0104364	Cdc2 phosphorylates Rap1 at Thr378, Ser422, and Ser513 during M phase. Ser456 of Rap1 is also phosphorylated during M phase by an unknown kinase. Ser213 of Rap1 is phosphorylated throughout the cell cycle. These phosphorylations are required for the efficient detachment of telomeres from the nuclear envelope.
PMID:22959349	PBO:0020543	cdc2 phosphorylates rap1. phosphorylated rap1 binds bqt4 less efficiently. rap1-bqt4 binding is required for telomere tethering at nuclear periphery. In WT cells telomere tehtering is abolished during M phase.
PMID:22976295	PBO:0097469	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	PBO:0097468	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	PBO:0097469	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	PBO:0097468	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	PBO:0097469	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	PBO:0097468	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	PBO:0097469	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	GO:0038202	"(comment: I guess everything in the signaling cascade that isn't the ""final effector"" is part of the signaling cascade?)"
PMID:22976295	GO:0038202	"(comment: I guess everything in the signaling cascade that isn't the ""final effector"" is part of the signaling cascade?)"
PMID:22976295	PBO:0097477	(comment: in vitro assay using rps602 so I am inferring rps601)
PMID:22976295	PBO:0097451	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	PBO:0097453	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	PBO:0097454	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	PBO:0097455	In this experiment, we utilized a Psk1 mutant (Thr415Glu), a phospho-mimetic mutant of its hydrophobic motif, as the mutant exhibited higher activity than the wild-type protein. As shown in Fig. 2C, the Psk1 protein phosphorylated Rsp6 in vitro. However, the Rsp6 mutant that has two potential serine phosphorylation sites changed to alanine was not phosphorylated by Psk1.
PMID:22976295	PBO:0110437	(comment: in vitro assay using rps602 so I am inferring rps601)
PMID:22976295	PBO:0097459	not shown
PMID:22976295	PBO:0097454	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	PBO:0097454	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	PBO:0097468	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	PBO:0025355	(comment: blotted for rps601 & rps602 simultaneously)
PMID:22976295	PBO:0025356	(comment: blotted for rps601 & rps602 simultaneously)
PMID:22976295	PBO:0025357	(comment: blotted for rps601 & rps602 simultaneously)
PMID:22976295	PBO:0025355	(comment: blotted for rps601 & rps602 simultaneously)
PMID:22976295	PBO:0025356	(comment: blotted for rps601 & rps602 simultaneously)
PMID:22976295	PBO:0025357	(comment: blotted for rps601 & rps602 simultaneously)
PMID:22976295	PBO:0097450	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	PBO:0097452	(comment: both rps proteins in extension because blot is for both of them)
PMID:22987637	PBO:0104501	"(comment: for evidence, ""BrdU incorporation assay evidence used in manual assertion"" (ECO:0001155) would be applicable.)"
PMID:22987637	FYPO:0005758	"(comment: for evidence, ""BrdU incorporation assay evidence used in manual assertion"" (ECO:0001155) would be applicable.)"
PMID:22990236	PBO:0034977	(comment: CHECK SO:0001899 = dh repeat)
PMID:23032292	FYPO:0000854	(comment: CHECK spacing is wrong as well as occupancy)
PMID:23035257	PBO:0116402	(comment: this isn't reall demonstrated here but it can ne imputed form this experiment and prior knowledge)
PMID:23051734	GO:0070649	(comment: required for wild-type rates of actin cable retrograde flow in myo52∆ cells)
PMID:23066505	GO:0036498	(comment: CHECK RIDD? - there is no RIDD term in GO, Val wants to wait with this)
PMID:23066505	PBO:0099504	(comment: ire1 breaks down mRNAs during ER stress, however bip1 is unusual in that ire1 cleavage stabilizes it)
PMID:23071723	FYPO:0000972	(comment: CHECK throughout cell cycle, with peak at M/G1)
PMID:23084836	FYPO:0005545	(Figures 6A, 6B) (comment: see above)
PMID:23084836	FYPO:0007270	(Figures 6A, 6B) (comment: CHECK: see above)
PMID:23084836	PBO:0101850	We observed that Ku localization was diffuse after DNA damage, but this diffusion was inhibited by rtt109Δ (Figure 7D)
PMID:23084836	FYPO:0007270	(Figures 6A, 6B) (comment: see above)
PMID:23084836	FYPO:0005545	(Figures 6A, 6B) (comment: see above)
PMID:23084836	FYPO:0007270	(Figures 6A, 6B) hst4Δ and clr6-1 HDAC mutations, but not other HDAC mutations, significantly compromised Tf clustering and the association of Tf cluster with centromeres; Figures 6A and 6B)
PMID:23084836	FYPO:0005545	We found that Tf clustering and the association of Tf cluster with centromeres were significantly compromised in the cut14-208 condensin mutant Figures 4A and 4B)
PMID:23084836	FYPO:0007270	We found that Tf clustering and the association of Tf cluster with centromeres were significantly compromised in the cut14-208 condensin mutant Figures 4A and 4B)
PMID:23084836	FYPO:0007270	(comment: NOTE IS STILL LOCALIZED TO NUCLEAR ERIPHERY) Remarkably, the association of Tf elements with centromeres was significantly compromised in pkuΔ cells (P < 0.00001, Mann-Whitney U test; Figures 3D and 3E).
PMID:23084836	FYPO:0007270	(comment: NOTE IS STILL LOCALIZED TO NUCLEAR ERIPHERY) Remarkably, the association of Tf elements with centromeres was significantly compromised in pkuΔ cells (P < 0.00001, Mann-Whitney U test; Figures 3D and 3E).
PMID:23084836	FYPO:0001870	clustering and tethering of centromeres to the nuclear periphery were not affected in pku70Δ and pku80Δ cells, although Ku does localize at centromeres (Figures 1E, 3A, and 3B)
PMID:23084836	FYPO:0001870	clustering and tethering of centromeres to the nuclear periphery were not affected in pku70Δ and pku80Δ cells, although Ku does localize at centromeres (Figures 1E, 3A, and 3B)
PMID:23084836	FYPO:0005545	Interestingly, Tf clustering was impaired by pku70Δ and pku80Δ at a level similar to that observed in abp1Δ cells (Figure 2A).
PMID:23084836	FYPO:0005545	Interestingly, Tf clustering was impaired by pku70Δ and pku80Δ at a level similar to that observed in abp1Δ cells (Figure 2A).
PMID:23084836	FYPO:0005545	Interestingly, Tf clustering was impaired by pku70Δ and pku80Δ at a level similar to that observed in abp1Δ cells (Figure 2A).
PMID:23084836	FYPO:0004890	As previously shown, telomere tethering was significantly compromised in rap1Δ and bqt4Δ cells (Figure S2C; Chikashige et al., 2009).
PMID:23084836	GO:0099115	(Fig. 1A)
PMID:23084836	GO:0005721	(Fig. 1A)
PMID:23084836	PBO:0101844	(Fig. 1A)
PMID:23084836	FYPO:0002335	(Figure S1C)
PMID:23084836	FYPO:0002335	(Figure S1C)
PMID:23084836	FYPO:0007269	The FISH data revealed that telomere clustering was not affected by pku70Δ and pku80Δ, but telomere tethering to the nuclear periphery was significantly compromised by pkuΔ (P < 0.001, Mann-Whitney U test), suggesting that telomere clustering and tethering to the nuclear periphery are distinct processes (Figures S2A and S2B)
PMID:23084836	FYPO:0007269	(Figures S2A, S2B)
PMID:23084836	PBO:0101845	(Figures S2A, S2B). AND As previously shown, telomere tethering was significantly compromised in rap1Δ and bqt4Δ cells (Figure S2C; Chikashige et al., 2009).
PMID:23084836	FYPO:0004890	As previously shown, telomere tethering was significantly compromised in rap1Δ and bqt4Δ cells (Figure S2C; Chikashige et al., 2009).
PMID:23084836	PBO:0101849	(Figure 6E). H3K56 acetylation antagonizes Tf clustering at centromeres. binding of Ku was reduced and enhanced in hst4Δ and rtt109Δ cells, respectively
PMID:23084836	PBO:0101848	(Figure 6E). H3K56 acetylation antagonizes Tf clustering at centromeres. binding of Ku was reduced and enhanced in hst4Δ and rtt109Δ cells, respectively
PMID:23084836	PBO:0101847	(Figure 6E). H3K56 acetylation antagonizes Tf clustering at centromeres. binding of Ku was reduced and enhanced in hst4Δ and rtt109Δ cells, respectivelyWe examined how H3K56 acetylation antagonizes Tf clustering at centromeres. Remarkably, binding of Ku was reduced and enhanced in hst4Δ and rtt109Δ cells, respectively, suggesting that H3K56 acetylation has an inhibitory effect on Ku binding to Tf elements (Figure 6E).
PMID:23084836	PBO:0101846	(Figure 6E) H3K56 acetylation antagonizes Tf clustering at centromeres. binding of Ku was reduced and enhanced in hst4Δ and rtt109Δ cells, respectively
PMID:23084836	FYPO:0007271	Moreover, only the rtt109Δ HAT mutations, but not other HAT mutations, significantly promoted the association of Tf cluster with centromeres, whereas none of the HAT mutations affected Tf clustering (Figures 6C and 6D).
PMID:23087209	MOD:00046	Sid2 kinase phosphorylates Klp2 on serine residues 113 and 123 based on both in vitro and in vivo evidence. Phosphorylation on these residues disrupts interaction of Klp2 with Mal3.
PMID:23087209	MOD:00046	Sid2 kinase phosphorylates Klp2 on serine residues 113 and 123 based on both in vitro and in vivo evidence. Phosphorylation on these residues disrupts interaction of Klp2 with Mal3.
PMID:23087209	PBO:0102452	Sid2 kinase phosphorylates Klp2 on serine residues 113 and 123 based on both in vitro and in vivo evidence. Phosphorylation on these residues disrupts interaction of Klp2 with Mal3.
PMID:23093942	FYPO:0001740	(comment: assayed by PCR in strain with RTS1 replication fork barrier inserted near ori3006/7)
PMID:23093942	FYPO:0003587	(comment: assayed by PCR in strain with RTS1 replication fork barrier inserted near ori3006/7)
PMID:23093942	FYPO:0003587	(comment: assayed by PCR in strain with RTS1 replication fork barrier inserted near ori3006/7)
PMID:23093942	FYPO:0003588	(comment: assayed in strain with RTS1 replication fork barrier inserted near ori3006/7)
PMID:23093942	FYPO:0001740	(comment: assayed in strain with RTS1 replication fork barrier inserted near ori3006/7)
PMID:23093943	FYPO:0000026	(Figure 4A-4C, S3A-S3B)
PMID:23093943	FYPO:0001355	(Figure S1F)
PMID:23093943	FYPO:0002061	(Figure S1F)
PMID:23093943	PBO:0102282	(Figure 1F-1G)
PMID:23093943	PBO:0102281	(Figure S1B-S1C)
PMID:23093943	PBO:0097167	(Figure S1B-S1C)
PMID:23093943	PBO:0102280	(Figure S1B-S1C)
PMID:23093943	PBO:0102279	(Fig. 1b, 2)
PMID:23093943	FYPO:0003535	(Fig. 1b)
PMID:23093943	PBO:0102283	(Fig. 3C)
PMID:23093943	PBO:0102284	(Figure 3D-3F)
PMID:23093943	PBO:0102285	(Figure 3G)
PMID:23093943	FYPO:0001355	(Figure S1F)
PMID:23093943	PBO:0102286	Mutation of PxxPs 10 and 11 in combination, or P257 of PxxP 11 alone, abolished the two-hybrid interaction (Figure S3D), and the P257A mutation eliminated co-immunoprecipitation of Fic1- FLAG3 with Cdc15 in vivo (Figure 4D).
PMID:23093943	FYPO:0000026	(Figure 4A-4C, S3A-S3B)
PMID:23093943	PBO:0102288	(Fig. 4c)
PMID:23093943	PBO:0102289	(Fig. 4c)
PMID:23093943	PBO:0102290	(Fig. 4c)
PMID:23093943	PBO:0099938	(Fig. S3F)
PMID:23093943	PBO:0097713	Cyk3-GFP localized to the CR and division site during cytokinesis, and it was retained at new ends immediately following cell division (Figure 4F).
PMID:23093943	PBO:0102291	Cyk3-GFP localized to the CR and division site during cytokinesis, and it was retained at new ends immediately following cell division (Figure 4F).
PMID:23093943	PBO:0102292	Fic1 most likely functions during late stages of cytokinesis. In line with this idea, the percentage of fic1D cells that had undergone ingression but were still joined at their division sites was more than four times that of wild-type cells (Figure 5A-5B).
PMID:23093943	GO:1902404	Consistent with early cytokinesis events proceeding appropriately without Fic1, time-lapse imaging of myosin regulatory light chain Rlc1-GFP [47,48] along with spindle pole body marker Sid4-GFP revealed that the CR formed and constricted normally in fic1D cells (Figure 5C-5D). However, at the termination of CR constriction, parts of the CR persisted at the division plane (Figure 5E-5G and Figure S4D).
PMID:23093943	PBO:0102288	(Fig. 4c,6a)
PMID:23093943	PBO:0102293	Loss of Eng1 or its cooperating glucanase, Agn1 [34], resulted in high percentages of monopolar growth (Figure 6C-6D and Figure S5A)
PMID:23093943	PBO:0102293	Loss of Eng1 or its cooperating glucanase, Agn1 [34], resulted in high percentages of monopolar growth (Figure 6C-6D and Figure S5A)
PMID:23093943	PBO:0102296	(Figure S5B)
PMID:23093943	PBO:0102296	(Figure S5B)
PMID:23093943	FYPO:0003776	Cells lacking Fic1 or its interacting partners Cyk3 or Imp2 were significantly more invasive than wild-type cells (Figure 9A-9B).
PMID:23093943	FYPO:0003776	Cells lacking Fic1 or its interacting partners Cyk3 or Imp2 were significantly more invasive than wild-type cells (Figure 9A-9B).
PMID:23093943	FYPO:0003776	Cells lacking Fic1 or its interacting partners Cyk3 or Imp2 were significantly more invasive than wild-type cells (Figure 9A-9B).
PMID:23093943	FYPO:0003776	In addition to these strains, we found other cytokinesis mutants exhibiting high degrees of monopolar growth (spn1D, cdc7-24, and vps24D) to also be highly invasive and to form pseudohyphal projections into 2% agar (Figure 9A-9B and Figure S7A)
PMID:23093943	PBO:0099938	(Fig. 3C)
PMID:23093943	PBO:0018345	As was observed previously [28], cytoplasmic Fic1-GFP localizes to cell tips during interphase and later to the CR during cell division (Figure 3A).
PMID:23093943	PBO:0097713	As was observed previously [28], cytoplasmic Fic1-GFP localizes to cell tips during interphase and later to the CR during cell division (Figure 3A).
PMID:23093943	PBO:0038218	T-shapes always arose in cells that the tea1D growth pattern dictated should grow at their new ends (Figure 2D-2E) but that actually grew at neither (Figure 2E and 2G)
PMID:23112169	GO:0032132	(comment: binds O6-alkylguanine, 2-aminopurine and 2,6-diaminopurine)
PMID:23122962	PBO:0111454	Combining the large-scale phosphoproteome data set and sequence alignment (Figures S4B and S4C), we determined that putative phosphoacceptors and in vitro analysis demonstrated that Cdk11 phosphorylates Med4 on three residues (Figure 3B: S115, S204, and S218
PMID:23122962	GO:2001178	At the contrary, the interaction between the kinase module subunit Cdk8 and the head subunit Med27 was completely abrogated when Cdk11 was inactivated (Figure 4B, middle panel). This role of Cdk11 in Mediator integrity was likely mediated by phosphorylation of Med27 and Med4 on the sites identified above (Figures 3 and 4A), because the interaction between Cdk8 and either the Med27 or Med4 phosphorylation mutants was specifically lost (Figure 4B, right panel). In contrast, the phosphorylation mutants of Med27 and Med4 still interacted with the middle subunit Med7 (Figure 4B, right panel). These data indicate that the association of the kinase submodule and the S-Mediator requires the phosphorylation of Med27 and Med4 by Cdk11.
PMID:23122962	PBO:0111453	Therefore, we found no evidence of Cdk11 being a genuine CTD kinase in fission yeast.
PMID:23122962	PBO:0111454	Combining the large-scale phosphoproteome data set and sequence alignment (Figures S4B and S4C), we determined that putative phosphoacceptors and in vitro analysis demonstrated that Cdk11 phosphorylates Med4 on three residues (Figure 3B: S115, S204, and S218
PMID:23122962	GO:0005634	Fluorescence microscopy revealed that Cdk11 was expressed and mainly concentrated in the nucleus (Figure 1A).
PMID:23122962	GO:0000307	A tandem affinity purification (TAP) identified physical partners of Cdk11, including an uncharacterized cyclin (SPAC1296.05c) that was confirmed to bind Cdk11 in independent coimmunoprecipitation experiments (Figure 1C and 1D).
PMID:23122962	GO:0000307	A tandem affinity purification (TAP) identified physical partners of Cdk11, including an uncharacterized cyclin (SPAC1296.05c) that was confirmed to bind Cdk11 in independent coimmunoprecipitation experiments (Figure 1C and 1D).
PMID:23122962	PBO:0096825	in contrast to Mcs6 (the Cdk7 ortholog), which readily phosphorylated the GST-CTD fusion in vitro (Figure 1E) (Drogat and Hermand, 2012)
PMID:23122962	PBO:0107732	In addition, while the inactivation of the welldescribed CTD serine 5 or serine 2 kinases (Mcs6 [Cdk7] and Lsk1 [Cdk12], respectively) specifically decreased the phosphorylation level of these two residues in vivo, the absence of cdk11 had no effect (Figure 1F).
PMID:23122962	PBO:0107730	In addition, while the inactivation of the well-described CTD serine 5 or serine 2 kinases (Mcs6 [Cdk7] and Lsk1 [Cdk12], respectively) specifically decreased the phosphorylation level of these two residues in vivo, the absence of cdk11 had no effect (Figure 1F).
PMID:23122962	PBO:0111120	in contrast to Mcs6 (the Cdk7 ortholog), which readily phosphorylated the GST-CTD fusion in vitro (Figure 1E) (Drogat and Hermand, 2012)
PMID:23122962	GO:0140834	Therefore, we found no evidence of Cdk11 being a genuine CTD kinase in fission yeast.
PMID:23122962	GO:0140836	Therefore, we found no evidence of Cdk11 being a genuine CTD kinase in fission yeast.
PMID:23122962	GO:0000785	The previously reported connection between Cdk11 and transcription, together with its nuclear localization and copurification with transcription regulators (although at weak level) led us to test its chromatin association. Gene-specific chromatin immunoprecipitation (ChIP) experiments showed that Cdk11- hemagglutinin (HA) was enriched onto chromatin compared to an untagged control (data not shown), and a genome-wide ChIP-on-chip analysis showed a broad distribution of Cdk11- HA.
PMID:23122962	GO:2001178	At the contrary, the interaction between the kinase module subunit Cdk8 and the head subunit Med27 was completely abrogated when Cdk11 was inactivated (Figure 4B, middle panel). This role of Cdk11 in Mediator integrity was likely mediated by phosphorylation of Med27 and Med4 on the sites identified above (Figures 3 and 4A), because the interaction between Cdk8 and either the Med27 or Med4 phosphorylation mutants was specifically lost (Figure 4B, right panel). In contrast, the phosphorylation mutants of Med27 and Med4 still interacted with the middle subunit Med7 (Figure 4B, right panel). These data indicate that the association of the kinase submodule and the S-Mediator requires the phosphorylation of Med27 and Med4 by Cdk11.
PMID:23122962	GO:0060261	This possibility was confirmed by global expression profiling, showing that only 55 genes were significantly affected in the absence of Cdk11. (.....and srb mediator association) showed that the absence of either cdk11 or cdk8 resulted in very similar defects (up- or downregulation) that were more pronounced in the cdk8 mutant (Figure 2C). Quantitative RT-PCR confirmed this effect on representative genes and showed, in addition, that the expression defects were not cumulated in the double cdk8 cdk11 mutant (Figure 2D).
PMID:23122962	PBO:0111452	Therefore, we found no evidence of Cdk11 being a genuine CTD kinase in fission yeast.
PMID:23128140	GO:0051010	(comment: NMR + substrate)
PMID:23133674	GO:0005515	(Fig. 1) (comment: Y2H)
PMID:23133674	GO:0005515	(Fig. 1) (comment: Y2H)
PMID:23133674	GO:0005515	(comment: Y2H) fig 1
PMID:23133674	GO:0005515	(Fig. 1) (comment: only bqt1 is fused to the activation domain (that's why I am not adding this function to bqt2))
PMID:23133674	GO:0005515	(comment: CHECK bqt1 is fused to the activation domain)
PMID:23151475	PBO:0120706	(Fig. 3A)
PMID:23151475	PBO:0120707	(Fig. 4D)
PMID:23151475	PBO:0120717	(Fig. 4D)
PMID:23151475	PBO:0120702	(Fig. 4D)
PMID:23151475	PBO:0120714	(Fig. 3D)
PMID:23151475	PBO:0120714	(Fig. 3D)
PMID:23151475	PBO:0120714	(Fig. 3D)
PMID:23151475	PBO:0120702	(Fig. 3A)
PMID:23151475	PBO:0120703	(Fig. 3A)
PMID:23151475	PBO:0120703	(Fig. 3A)
PMID:23151475	PBO:0120713	(Fig. 3D)
PMID:23151475	PBO:0120712	(Fig. 3D)
PMID:23151475	PBO:0120712	(Fig. 3D)
PMID:23151475	PBO:0120711	(Fig. 3D)
PMID:23151475	PBO:0120711	(Fig. 3D)
PMID:23151475	PBO:0120711	(Fig. 3D)
PMID:23151475	PBO:0120710	(Fig. 3D)
PMID:23151475	PBO:0120710	(Fig. 3D)
PMID:23151475	PBO:0120710	(Fig. 3D)
PMID:23151475	PBO:0120710	(Fig. 3D)
PMID:23151475	PBO:0120704	(Fig. 3A, 4D)
PMID:23151475	PBO:0120703	(Fig. 3A)
PMID:23151475	PBO:0120703	(Fig. 3A)
PMID:23151475	PBO:0120705	(Fig. 3A)
PMID:23151475	PBO:0120705	(Fig. 3A)
PMID:23151475	PBO:0120705	(Fig. 3A)
PMID:23151475	PBO:0120708	(Fig. 4D)
PMID:23151475	PBO:0120706	(Fig. 4D)
PMID:23151475	PBO:0120709	(Fig. 3D)
PMID:23151475	FYPO:0006369	(Fig. 1D, 2B, 3B, 4)
PMID:23151475	PBO:0120708	(Fig. 3A)
PMID:23151475	PBO:0120694	(Fig. 4C)
PMID:23151475	PBO:0120708	(Fig. 3A)
PMID:23151475	PBO:0120707	(Fig. 3A)
PMID:23151475	PBO:0120707	(Fig. 3A)
PMID:23151475	PBO:0120707	(Fig. 3A)
PMID:23151475	PBO:0120707	(Fig. 3A)
PMID:23151475	PBO:0120694	(Fig. 4C)
PMID:23151475	PBO:0120707	(Fig. 3A)
PMID:23151475	PBO:0120707	(Fig. 3A)
PMID:23151475	PBO:0120705	(Fig. 3A)
PMID:23151475	PBO:0120693	(Fig. 4B)
PMID:23151475	PBO:0120693	(Fig. 4B)
PMID:23151475	PBO:0120716	(Fig. 4B)
PMID:23151475	PBO:0120716	(Fig. 4B)
PMID:23151475	PBO:0120692	(Fig. 4C)
PMID:23151475	PBO:0120705	(Fig. 4D)
PMID:23151475	PBO:0120705	(Fig. 4D)
PMID:23151475	PBO:0120702	(Fig. 4D)
PMID:23151475	PBO:0120697	(Fig. 2A, 2E)
PMID:23151475	PBO:0120698	(Fig. 2A)
PMID:23151475	PBO:0120698	(Fig. 2A)
PMID:23151475	PBO:0120699	(Fig. 2E)
PMID:23151475	PBO:0120699	(Fig. 2E)
PMID:23151475	PBO:0120699	(Fig. 2E)
PMID:23151475	PBO:0120699	(Fig. 2E)
PMID:23151475	PBO:0120691	(Fig. 1, 4B)
PMID:23151475	PBO:0120692	(Fig. 1, 4C)
PMID:23151475	PBO:0120693	(Fig. 1)
PMID:23151475	PBO:0120693	(Fig. 1)
PMID:23151475	PBO:0120694	(Fig. 1)
PMID:23151475	PBO:0120694	(Fig. 1)
PMID:23151475	PBO:0120695	(Fig. 2, 4A)
PMID:23151475	PBO:0120696	(Fig. 2A, 2B)
PMID:23151475	PBO:0120696	(Fig. 2A, 2B)
PMID:23151475	PBO:0120693	(Fig. 4B)
PMID:23151475	PBO:0120693	(Fig. 4B)
PMID:23151475	PBO:0120700	(Fig. 3A)
PMID:23151475	PBO:0120700	(Fig. 3A)
PMID:23151475	PBO:0120696	(Fig. 4A)
PMID:23151475	PBO:0120696	(Fig. 4A)
PMID:23151475	PBO:0120701	(Fig. 3A)
PMID:23151475	PBO:0120701	(Fig. 3A)
PMID:23151475	PBO:0120694	(Fig. 4C)
PMID:23151475	PBO:0120694	(Fig. 4C)
PMID:23151475	PBO:0120696	(Fig. 4A)
PMID:23151475	PBO:0120696	(Fig. 4A)
PMID:23151475	PBO:0120702	(Fig. 3A)
PMID:23151475	PBO:0120702	(Fig. 3A)
PMID:23151475	PBO:0120715	(Fig. 4A)
PMID:23151475	PBO:0120702	(Fig. 3A)
PMID:23151475	PBO:0120715	(Fig. 4A)
PMID:23151475	PBO:0120714	(Fig. 3D)
PMID:23188080	FYPO:0004287	(comment: affects intermolecular, but not intramolecular, end joining)
PMID:23188080	FYPO:0004287	(comment: affects intermolecular, but not intramolecular, end joining)
PMID:23188080	FYPO:0004287	(comment: affects intermolecular, but not intramolecular, end joining)
PMID:23188080	FYPO:0004287	(comment: affects intermolecular, but not intramolecular, end joining)
PMID:23188080	FYPO:0004287	(comment: affects intermolecular, but not intramolecular, end joining)
PMID:23188080	FYPO:0004287	(comment: affects intermolecular, but not intramolecular, end joining)
PMID:23188080	FYPO:0004287	(comment: affects intermolecular, but not intramolecular, end joining)
PMID:23200991	GO:1902917	(comment: inferred from localization plus GTPase activity)
PMID:23200991	PBO:0038209	(comment: Observed with probe for active Cdc42 (CRIB))
PMID:23200991	PBO:0037256	(comment: Observed with probe for active Cdc42 (CRIB))
PMID:2320127	PBO:0107935	(Fig. 4a) Cells blocked in G2
PMID:2320127	MOD:00046	(Fig. 1c) Serine is the major phosphoamino acid
PMID:2320127	MOD:00047	(Fig. 1c) threonine is the minor phosphoamino acid
PMID:2320127	PBO:0107935	(Fig. 4a) Cells blocked in mitosis
PMID:23209828	PBO:0099842	Pap1 is ubiquitylated by Rhp6 and Ubr1
PMID:23209828	PBO:0099849	MBC resistance phenotype and pap1 ubiquitylation phenotype
PMID:23209828	PBO:0099843	Pap1 is ubiquitylated by Rhp6 and Ubr1
PMID:23209828	PBO:0099848	MBC sensitivity phenotype and ubiquitylation and degradation phenotype
PMID:23209828	PBO:0099848	MBC sensitivity phenotype and ubiquitylation and degradation phenotype
PMID:23209828	GO:0061631	MBC resistance phenotype and pap1 ubiquitylation phenotype
PMID:23211746	FYPO:0000089	(comment: same as exo1delta alone)
PMID:23211746	FYPO:0002553	(comment: gel electrophoresis + southern blot)
PMID:23211746	PBO:0095371	(comment: same as exo1delta alone)
PMID:23211746	FYPO:0000268	(comment: same as chk1delta alone)
PMID:23211746	FYPO:0000089	(comment: same as chk1delta alone)
PMID:23211746	PBO:0095371	(comment: same as rad2delta alone)
PMID:23211746	FYPO:0000089	(comment: same as rad2delta alone)
PMID:23223230	PBO:0108584	In the array analysis, one of the most repressed genes in response to zinc deficiency was adh1, whereas one of the most highly expressed transcripts under this condition was an antisense transcript at this locus (Fig. 1A).
PMID:23223230	PBO:0092155	In the array analysis, one of the most repressed genes in response to zinc deficiency was adh1, whereas one of the most highly expressed transcripts under this condition was an antisense transcript at this locus (Fig. 1A).
PMID:23223230	PBO:0108759	Taken together, the Northern and array analyses indicate that adh1AS transcripts preferentially accumulate in zinc-limited cells, whereas adh1 mRNAs accumulate in zinc-replete cells.
PMID:23223230	PBO:0108760	In the array analysis, one of the most repressed genes in response to zinc deficiency was adh1, whereas one of the most highly expressed transcripts under this condition was an antisense transcript at this locus (Fig. 1A).
PMID:23223230	PBO:0108585	When adh1AS and adh1 transcript levels were examined in SPCC13B11.02c cells, the adh1AS transcript was not detected, and adh1 mRNAs were detected in both zinc-limited and zinc-replete cells (Fig. 1C).
PMID:23223230	PBO:0108586	When adh1AS and adh1 transcript levels were examined in SPCC13B11.02c cells, the adh1AS transcript was not detected, and adh1 mRNAs were detected in both zinc-limited and zinc-replete cells (Fig. 1C).
PMID:23223230	PBO:0108587	However, the larger band preferentially accumulated under zinc-replete conditions in wild-type cells and constitutively accumulated in SPCC13B11.02c cells. Thus, changes in adh1AS levels influence the levels of Adh1 protein, suggesting that this mechanism may exist to conserve zinc.
PMID:23231582	GO:0000122	represses Pho7-mediated transcription activationin phosphate-replete conditions; does not regulate Pho7 DNA binding
PMID:23231582	PBO:0100021	(comment: also inferred from chromatin localization and reporter gene expression)
PMID:23231582	PBO:0100048	(comment: CHECK at pho1+ and SPBC1271.09)
PMID:23236291	FYPO:0000155	(Figure 3)
PMID:23236291	FYPO:0003335	(Figure 8A)
PMID:23236291	FYPO:0003318	(Figure 8B)
PMID:23236291	FYPO:0003335	(Figure 8B)
PMID:23236291	FYPO:0001252	(Figure 8E)
PMID:23236291	FYPO:0005277	(Figure 8E)
PMID:23236291	GO:1900735	(Figure 6A and 6C)
PMID:23236291	FYPO:0005504	(Figure 6A)
PMID:23236291	FYPO:0004153	(Figure 7A)
PMID:23236291	FYPO:0004153	(Figure 7A)
PMID:23236291	FYPO:0003335	(Figure 8D)
PMID:23236291	FYPO:0003776	(Figure 8D)
PMID:23236291	PBO:0107311	(comment: CHECK Requested new term from Sequence Ontology: CArG-box)
PMID:23236291	FYPO:0000155	(Figure 8D)
PMID:23236291	FYPO:0000155	(Figure 8D)
PMID:23236291	FYPO:0000155	(Figure 3)
PMID:23236291	FYPO:0000155	(Figure 3)
PMID:23236291	FYPO:0000155	(Figure 3)
PMID:23236291	FYPO:0000155	(Figure 3)
PMID:23236291	FYPO:0000155	(Figure 3)
PMID:23236291	FYPO:0000155	(Figure 3)
PMID:23236291	FYPO:0000155	(Figure 3)
PMID:23236291	FYPO:0003318	(Figure 8B)
PMID:23236291	GO:1900735	(Figure 1A and 1B)
PMID:23236291	FYPO:0003335	(Figure 1A)
PMID:23236291	FYPO:0003318	(Figure 1B)
PMID:23236291	FYPO:0000155	(Figure 8D)
PMID:23236291	FYPO:0000155	(Figure 8D)
PMID:23236291	FYPO:0000155	(Figure 8D)
PMID:23245849	PBO:0093616	Supp S1 Also the MMS sensitivity of the nth1 − mutant was suppressed by the deletion of mag1 but not mag2 (Figure S1), which contrasts previous results (Kanamitsu et al., 2007). We do not know the reason for this discrepancy, but it could be because of different strain backgrounds, as the strains used by Kanamisu and co-workers tolerate much higher MMS doses (0.03% versus 0.007% in our experiments)
PMID:23245849	PBO:0093616	(Fig. 1D)
PMID:23245849	FYPO:0000957	(Fig. 1D)
PMID:23245849	PBO:0093616	(Fig. 1D)
PMID:23245849	GO:0003905	Unexpectedly, Mag2 showed no DNA glycosylase activity for alkylated bases, even at very high enzyme concentration and under different assay conditions (titration of NaCl, Mg2+, ATP; data not shown). Further, heterologous expression of Mag2 did neither rescue the extreme alkylation sensitive phenotype of an E. coli mutant lacking the two 3mA DNA glycosylases AlkA and Tag, nor the corresponding Saccharomyces cerevisiae mag1 deletion mutant (data not shown). Mag2 was assayed for activity towards a variety of different base lesions which are known substrates for other DNA glycosylases including alkylated, oxidized and deaminated bases, base mismatches and AP sites; however no enzymatic activity was observed for any of the lesions tested (Table S1) Crystal Structure of Mag2 in Complex With DNA Reveals Novel Non-Enzymatic AP Site Recognition and DNA Sculpting
PMID:23245849	GO:0140431	Mag2 binds stronger to the abasic oligonucleotide than to non-damaged DNA (Figure 2), with a dissociation rate constant more than 15 times higher for non-damaged DNA (kd 26 × 10−3 s −1) as compared to DNA containing the AP site analogue tetrahydrofuran (THF) (kd 1.6 × 10−3 s−1). Mag2 injected on sensor chips coated with oligonucleotides containing a single ethenoadenine or 8-oxoguanine lesion showed the same resonance levels as non-damaged DNA (data not shown), demonstrating that Mag2 preferentially binds to AP sites in DNA.
PMID:23245849	GO:0005634	(Figure 1C)
PMID:23245849	GO:0006307	multiple experiments
PMID:23254763	PBO:0093561	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23254763	PBO:0093561	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23254763	PBO:0093561	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23254763	PBO:0093561	(Figure 2)
PMID:23254763	PBO:0093561	(Figure 2)
PMID:23254763	PBO:0093561	(Figure 2)
PMID:23254763	PBO:0093561	(Figure 2)
PMID:23254763	PBO:0093561	(Figure 2)
PMID:23254763	PBO:0093561	(Figure 2)
PMID:23254763	PBO:0093561	(Figure 2)
PMID:23254763	PBO:0093561	(Figure 2)
PMID:23254763	PBO:0093561	(Figure 2)
PMID:23254763	PBO:0095408	(Figure 2)
PMID:23254763	PBO:0095408	(Figure 2)
PMID:23254763	PBO:0095408	(Figure 2)
PMID:23254763	PBO:0095408	(Figure 2)
PMID:23254763	PBO:0095408	(Figure 2)
PMID:23254763	PBO:0095408	(Figure 2)
PMID:23254763	PBO:0095408	(Figure 2)
PMID:23254763	PBO:0095408	(Figure 2)
PMID:23254763	PBO:0095408	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23254763	PBO:0095407	(comment: CHECK complemented by S. cerevisiae GAL2)
PMID:23254763	FYPO:0001317	(Fig. 5a) There was no difference in ght2+ expression levels between wild-type and uge1Δgal10Δ cells that have a reduced level of cytosolic UDP-galactose (Suzuki et al. 2010), indicating that expression of ght2+ is not influenced by intracellular UDP-galactose concentration
PMID:23254763	FYPO:0001317	(Fig. 5a) There was no difference in ght2+ expression levels between wild-type and uge1Δgal10Δ cells that have a reduced level of cytosolic UDP-galactose (Suzuki et al. 2010), indicating that expression of ght2+ is not influenced by intracellular UDP-galactose concentration
PMID:23254763	FYPO:0003727	(Fig. 3) galactose-specific HRP-PNA staining was used to detect quantitative differences in the galactosylation of cell-surface proteins
PMID:23254763	FYPO:0001317	(Fig. 5a) There was no difference in ght2+ expression levels between wild-type and uge1Δgal10Δ cells that have a reduced level of cytosolic UDP-galactose (Suzuki et al. 2010), indicating that expression of ght2+ is not influenced by intracellular UDP-galactose concentration
PMID:23254763	FYPO:0006807	(Fig. 3) galactose-specific HRP-PNA staining was used to detect quantitative differences in the galactosylation of cell-surface proteins
PMID:23254763	FYPO:0002061	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23254763	FYPO:0002061	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23254763	PBO:0093561	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23254763	PBO:0093561	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23254763	PBO:0093561	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23254763	PBO:0093561	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23260662	GO:0011000	(comment: inferred directness from effects of different alleles and of mutations elsewhere (swi1delta, clr4delta, or mat1-SS2))
PMID:23260662	GO:0071515	(Fig. 3A)
PMID:23260662	PBO:0104354	(comment: same as lsd1-E918 single mutant)
PMID:23260662	PBO:0104354	(comment: same as lsd1-E918 single mutant)
PMID:23260662	PBO:0104354	(comment: same as lsd1-E918 single mutant)
PMID:23260662	PBO:0104354	(comment: same as lsd1-E918 single mutant)
PMID:23260662	GO:1902681	(comment: inferred indirectness from author description and different effect of swi1delta)
PMID:23260662	GO:0071515	(comment: inferred directness from effects of different alleles and of mutations elsewhere (swi1delta, clr4delta, or mat1-SS2))
PMID:23273506	FYPO:0000695	(Figures 4B and 4C) Asp56Ser mutation endows Mag2 with the ability to excise εA at levels similar to Mag1.
PMID:23297348	MOD:00046	(comment: CHECK S321 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	GO:0006606	Sal3 is required for the nuclear import of Clp1 as shown by microscopy.
PMID:23297348	GO:0005654	Localization of Clp1 to nucleoplasm requires the presence of the nuclear localization sequence (NLS), which was identified to locate right at the end of the C-terminal.
PMID:23297348	MOD:00046	(comment: CHECK S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK Phosphorylation site S265 was identified by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S332, S700, and S732 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S332, S700, and S732 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S332, S700, and S732 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	(comment: CHECK T123 and S334 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	(comment: CHECK S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S267 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	(comment: CHECK T297 and S364 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S303 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S57 and S206 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S57 and S206 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S183 and S372 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S183 and S372 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S674 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S502 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S196 and S252 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S196 and S252 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S345 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	(comment: CHECK S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	(comment: CHECK S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	(comment: CHECK S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S411 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	(comment: CHECK T554 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S372 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S436 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S220 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	(comment: CHECK T106 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S148 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S65 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S216 and S298 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S216 and S298 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S301 and S499 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S301 and S499 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S558 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S74 and S95 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S74 and S95 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S370 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	PBO:0101808	(comment: serine residues, presumably some or all of those mutated)
PMID:23297348	PBO:0101808	(comment: serine residues, presumably some or all of those mutated)
PMID:23297348	PBO:0101808	(comment: serine residues, presumably some or all of those mutated)
PMID:23297348	MOD:00047	(comment: CHECK S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	(comment: CHECK T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	(comment: CHECK T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK T297 and S364 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK T123 and S334 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK T123 and S334 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23311928	FYPO:0001357	(comment: non-flocculating cells)
PMID:23314747	PBO:0095974	(comment: AACCCT box, subtelomere)
PMID:23314747	PBO:0097201	(comment: AACCCT box, subtelomere)
PMID:23314747	PBO:0096683	Cnp1 localisation to centromere reduced in teb1-1 cells grown at 36C (based on immunofluorescence)
PMID:23314747	FYPO:0002687	Southern Blot of teb1-1 cells grown at permissive and restrictive temperatures shows no change in telomere length, compared to wild type cells
PMID:23314747	PBO:0099858	(comment: AACCCT box, subtelomere)
PMID:23333317	PBO:0100168	(Fig. 4E) in absence of fin1 activity dis2 remains bound to cut 12
PMID:23333317	PBO:0100167	(Fig. 4A) (comment: an antibody that recognized Cut12 when phosphorylated on T75) [Figure S2C] alone established that MPF phosphorylates T75 in vitro [Figure 4D]).
PMID:23333317	PBO:0100166	(Fig. 4A) fin1 activation is dependent on sid1
PMID:23333317	PBO:0100183	(Fig. 5B)
PMID:23333317	PBO:0093557	(Fig. 1) Rescue of cdc25-22 but not restored to full growth (partial rescue). [ie The cut12.s11 (G71V) mutation enables cdc25+ null cells (cdc25.D) to form microcolonies of 1 to 20 cells [14]. ]
PMID:23333317	PBO:0100160	(Fig. 1C) (comment: 2 hybrid)
PMID:23333317	PBO:0100187	(Fig. 5B) plo1 decreased specific activity
PMID:23333317	PBO:0100193	(Fig. 1H) cdc25-22 cut12R531STOP can grow at higher temperature in presence of cut12. G71V mutation. (comment: vw changed form increased to normal, compared to WT)
PMID:23333317	PBO:0100179	(Fig. 5B)
PMID:23333317	PBO:0100178	(Fig. 5B)
PMID:23333317	PBO:0100177	(Fig. 5B) plo1 increased specific activity
PMID:23333317	PBO:0100192	(Fig. 5B)
PMID:23333317	PBO:0100179	(Fig. 5B)
PMID:23333317	PBO:0100178	(Fig. 5B)
PMID:23333317	PBO:0100188	(Fig. 5B) (comment: CHECK DELAYED)
PMID:23333317	PBO:0100161	(Fig. 1E)
PMID:23333317	PBO:0100162	(Fig. 1E)
PMID:23333317	PBO:0100181	(Fig. 5B) plo1 increased specific activity
PMID:23333317	PBO:0100160	(Fig. 1C) (comment: 2 hybrid)
PMID:23333317	PBO:0100158	(Fig. 1c) (comment: 2-hybrid)
PMID:23333317	PBO:0100166	(Fig. 4A) HU arrest Fig4E synchronous culture
PMID:23333317	PBO:0100165	(Fig. 2I) Fig3C double mutant cut12.T75A T78A binds dis2
PMID:23333317	PBO:0100164	(Fig. 2I) single mutant cut12. T78D reduces dis2 binding
PMID:23333317	PBO:0100164	(Fig. 2I) single mutant cut12. T75D reduces dis2 binding
PMID:23333317	PBO:0100163	(Fig. 2I) single mutant cut12.T78A binds Dis2
PMID:23333317	PBO:0100163	(Fig. 2I) single mutant cut12. T75A binds dis2
PMID:23333317	PBO:0093557	(Fig. 2E) single mutant T75D does not rescue cdc25-22 as well as double T75DT78D or singleT78D mutants. (comment: vw: changed to decreased)
PMID:23333317	PBO:0093557	(Fig. 2E) single mutant T78D does not rescue cdc25-22 as well as double T75DT78D. (vw changed from increased to decreased as we are comparing to WT , bottom row)
PMID:23333317	PBO:0100158	(Fig. 1c) (comment: 2-hybrid)
PMID:23333317	PBO:0100157	(Fig. 1C) (comment: 2 hybrid)
PMID:23333317	PBO:0100198	(Fig. 2H)
PMID:23333317	PBO:0100158	(Fig. 1D)
PMID:23333317	PBO:0097660	(Fig. 2H)
PMID:23333317	FYPO:0000674	(Fig. 2G)
PMID:23333317	PBO:0100172	(Fig. 4F) T75 T78 no longer phosphorylated and dis2 remains bound to cut12
PMID:23333317	PBO:0100171	(Fig. 4F) dis2 remains bound to cut12
PMID:23333317	FYPO:0000674	(Fig. 2E) phospho mimetic cdc12 mutant rescues cdc25 mutant
PMID:23333317	PBO:0100177	(Fig. 5B) plo1 increased specific activity
PMID:23333317	PBO:0100179	(Fig. 5B)
PMID:23333317	PBO:0100178	(Fig. 5B) premature recruitment of protein to the mitotic SPB
PMID:23333317	PBO:0100177	(Fig. 5B) plo1 increased specific activity
PMID:23333317	PBO:0100182	(Fig. 5B)
PMID:23333317	PBO:0100176	(Fig. 5A) plo1 localisation to SPB is dependent on fin1 activity
PMID:23333317	PBO:0100175	(Fig. 5A) plo1 localisation to SPB is dependent on fin1 activity
PMID:23333317	PBO:0100174	(comment: vw: could this one be abolished?) (Fig. 5A) No change in recruitment of plo1 to SPB when fin1 is inactivated T75 T78 mutated to D
PMID:23333317	PBO:0100173	(Fig. 5A) No increase in recruitment of plo1 to SPB when fin1 is active if T75 T78 mutated to A
PMID:23333317	PBO:0100188	(Fig. 5B) (comment: CHECK DELAYED)
PMID:23333317	FYPO:0000674	(Fig. 2E) phospho mimetic cdc12 mutant rescues cdc25 mutant
PMID:23333317	PBO:0100157	(Fig. 1D, E)
PMID:23333317	PBO:0100158	(Fig. 1D)
PMID:23333317	FYPO:0004481	(Fig. 2E) unphosphorylatable cut12 mutants are unable to rescue cdc25 mutant (comment: vw changed from decreased to abolished?)
PMID:23333317	FYPO:0000674	(Fig. 2E) phospho mimetic cdc12 mutant rescues cdc25 mutant
PMID:23333317	PBO:0100181	(Fig. 5B) plo1 increased specific activity
PMID:23333317	PBO:0100183	(Fig. 5B)
PMID:23333317	PBO:0100189	(Fig. 5B)
PMID:23333317	PBO:0100187	(Fig. 5B) plo1 decreased specific activity
PMID:23333317	PBO:0100192	(Fig. 5B)
PMID:23333317	PBO:0100188	(Fig. 5B) (comment: CHECK DELAYED)
PMID:23333317	PBO:0100187	(Fig. 5B) plo1 decreased specific activity
PMID:23333317	PBO:0100191	(Fig. 5B)
PMID:23333317	PBO:0100159	(Fig. 1D)
PMID:23333317	PBO:0100159	(Fig. 1C) increased interaction in 2 hybrid
PMID:23333317	PBO:0100160	(Fig. 1E)
PMID:23333317	PBO:0100160	(Fig. 1E)
PMID:23333317	PBO:0100160	(Fig. 1E)
PMID:23333317	PBO:0100199	(Fig. 2H) (comment: VWI added this and man=de the original 'abnormal cell size' small (variable size at division, mixed sized see #3800)
PMID:23333317	PBO:0100184	(Fig. 5B)
PMID:23333317	PBO:0100190	(Fig. 5B) plo1 increased specific activity
PMID:23333317	PBO:0100180	(Fig. 5B)
PMID:23333317	PBO:0100184	(Fig. 5B)
PMID:23333317	PBO:0100190	(Fig. 5B) plo1 increased specific activity
PMID:23333317	PBO:0100196	(Fig. 1b, F and G) (comment: CHECK T75T78 PHOSPHORYLATED FORM)
PMID:23333317	PBO:0100195	(Fig. 1b, F and G) (comment: CHECK T75T78 UNPHOSPHORYLATED FORM)
PMID:23333317	PBO:0100160	(Fig. 1C) (comment: 2 hybrid)
PMID:23333317	PBO:0100189	(Fig. 5B)
PMID:23333317	PBO:0100182	(Fig. 5B)
PMID:23333317	PBO:0100182	(Fig. 5B)
PMID:23333317	PBO:0100181	(Fig. 5B) plo1 increased specific activity
PMID:23333317	PBO:0100177	(Fig. 5B) plo1 increased specific activity
PMID:23333317	FYPO:0000674	"(Fig. 1A, 2A) vw""Fig 1. Rescue of cdc25-22 but not restored to full growth (partial rescue)"""
PMID:23333317	PBO:0100179	(Fig. 5B)
PMID:23333317	PBO:0100182	(Fig. 5B)
PMID:23333317	PBO:0100181	(Fig. 5B) plo1 increased specific activity
PMID:23333317	PBO:0100179	(Fig. 5B)
PMID:23333317	PBO:0100180	(Fig. 5B)
PMID:23333317	PBO:0100178	(Fig. 5B)
PMID:23333317	PBO:0100177	(Fig. 5B) plo1 increased specific activity
PMID:23333317	PBO:0100179	(Fig. 5B)
PMID:23333317	PBO:0100178	(Fig. 5B)
PMID:23333317	PBO:0111088	(comment: CHECK T75)
PMID:23333317	PBO:0100194	(comment: CHECK T75T78)
PMID:23333317	FYPO:0000674	(Fig. 2E)
PMID:23333317	PBO:0093556	(Fig. 1) Rescue of cdc25-22 but not restored to full growth (partial rescue)
PMID:23333317	PBO:0093557	(Fig. 1) Rescue of cdc25-22 but not restored to full growth (partial rescue)
PMID:23333317	PBO:0093556	(Fig. 1) Rescue of cdc25-22 but not restored to full growth (partial rescue)
PMID:23333317	PBO:0093557	(Fig. 1) Rescue of cdc25-22 but not restored to full growth (partial rescue)
PMID:23333317	PBO:0093557	(Fig. 1) Rescue of cdc25-22 but not restored to full growth (partial rescue)
PMID:23333317	PBO:0100193	(Fig. 1H) cdc25-22 cut12R531STOP can grow at higher temperature in presence of cut12. G71V mutation. (comment: vw changed form increased to normal, compared to WT)
PMID:23348717	PBO:0099730	assayed using cell growth with AspRec8c-FGFP-Mei2SATA construct (degradation frees Mei2SATA to arrest cell cycle)
PMID:23348717	PBO:0099730	assayed using AspRec8c-FGFP construct
PMID:23348717	FYPO:0003299	assayed using ArgDHFRts-HA-Mcm4ts construct or AspRec8c-FGFP construct
PMID:23348717	PBO:0099730	assayed using AspRec8c-FGFP construct
PMID:23348717	PBO:0099730	assayed using ArgDHFRts-HA-Mcm4ts construct or AspRec8c-FGFP construct
PMID:23348717	PBO:0099729	also assayed using AspRec8c-FGFP construct, which persists longer than unmodified full-length Rec8
PMID:23349636	PBO:0099925	(comment: CHECK more specifically, response to mitotic DNA replication checkpoint signaling)
PMID:23349808	PBO:0024047	(comment: CHECK during G2 phase of mitotic cell cycle)
PMID:23349808	PBO:0024047	(comment: CHECK during G2 phase of mitotic cell cycle)
PMID:23349808	PBO:0097713	(comment: CHECK during cytokinesis)
PMID:23349808	PBO:0024047	(comment: CHECK during G2 phase of mitotic cell cycle)
PMID:23349808	PBO:0024047	(comment: CHECK during G2 phase of mitotic cell cycle)
PMID:23394829	PBO:0023023	(comment: CHECK also present in early anaphase; disappears by late anaphase)
PMID:23394829	GO:0044732	(comment: CHECK also present in early anaphase; disappears by late anaphase)
PMID:23395004	PBO:0101942	(comment: mug20::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0003615	((comment: rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag))
PMID:23395004	FYPO:0004585	(comment: mug20::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0003615	(comment: ChIP-CHIP, rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag))
PMID:23395004	FYPO:0003615	(comment: ChIP-CHIP, rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag))
PMID:23395004	FYPO:0004585	(comment: mug20::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0003181	(comment: rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag))
PMID:23395004	PBO:0101942	(comment: mug20::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	PBO:0101943	(comment: rec25-204::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	PBO:0101944	(comment: rec27-205::GFP-kanMX6(C-terminal GFP tag)(comment:
PMID:23395004	PBO:0101941	(comment: ChIP-CHIP, rec27-205::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0004585	(comment: mug20::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0004585	(comment: rec25-204::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0004585	(comment: mug20::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0004585	(comment: rec27-205::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0003615	(comment: rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag))
PMID:23395004	PBO:0101942	(comment: mug20::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	PBO:0101942	(comment: mug20::GFP-kanMX6(C-terminal GFP tag))
PMID:23427262	PBO:0111961	(comment: vw: after attachment)
PMID:23427262	PBO:0111960	(comment: vw: after attachment)
PMID:23442800	GO:1902426	(comment: required for ubiquitination of Slp1)
PMID:23462181	GO:0000935	(Fig. 2A and B)
PMID:23462181	GO:0051286	(Fig. 2A and B)
PMID:23462181	GO:0005730	(Fig. 2A and B)
PMID:23462181	PBO:0018634	(Fig. 2A and B)
PMID:23462181	PBO:0018346	(Fig. 2A and B)
PMID:23496905	PBO:0099398	(Figure 2)
PMID:23496905	FYPO:0002060	(Figure 1)
PMID:23496905	PBO:0099396	(Fig. 2)
PMID:23496905	PBO:0099397	(Figure 3)
PMID:23496905	PBO:0099397	(Figure 3)
PMID:23496905	FYPO:0002060	(Figure 1)
PMID:23496905	PBO:0099396	(Fig. 2)
PMID:23496905	FYPO:0002060	(Figure 1)
PMID:23496905	PBO:0099396	(Fig. 2)
PMID:23496905	PBO:0099397	(Figure 3)
PMID:23496905	PBO:0099397	(Figure 3)
PMID:23496905	FYPO:0002060	(Figure 1)
PMID:23496905	PBO:0099396	(Fig. 2)
PMID:23496905	GO:0000338	(Fig. 2)
PMID:23496905	PBO:0099399	(Fig. 4) (comment: CHECK 40% act remaining)
PMID:23496905	PBO:0099399	(Fig. 4) (comment: CHECK 60%)
PMID:23496905	FYPO:0002060	(Figure 1)
PMID:23503588	FYPO:0002064	(comment: CHECK in vitro)
PMID:23555033	PBO:0092698	(comment: CHECK occurs_at CSL_response_element in vivo)
PMID:23555033	PBO:0096538	(comment: CHECK to CSL_response_element)
PMID:23555033	PBO:0096541	major region affecting localization between aa 395–465
PMID:23555033	PBO:0096540	(comment: CHECK to CSL_response_element)
PMID:23555033	GO:0045944	(comment: CHECK overexpression)
PMID:23555033	PBO:0092698	(comment: CHECK occurs_at CSL_response_element, overexpression, in vitro)
PMID:23576550	PBO:0099232	anti-alpha-tubulin antibody used; included both pombe alpha-tubulin gene names in extension
PMID:23576550	PBO:0099233	anti-alpha-tubulin antibody used; included both pombe alpha-tubulin gene names in extension
PMID:23609449	PBO:0103289	(Figure 10) (comment: HECK check specificity)
PMID:23609449	GO:0140767	(comment: binds the non trimmed part of the N-glycan)
PMID:23609449	PBO:0103289	(Figure 10) (comment: CHECK check specificity). Taken together, the results demonstrate that substitution of Trp-409 in the context of the full-length GIIβ has a moderate to high (60% inhibitory) effect on GII activity.
PMID:23615450	PBO:0104673	(comment: complements deletion) Figure 6A
PMID:23615450	PBO:0096761	(comment: complements deletion) Figure 6A
PMID:23615450	FYPO:0002060	(comment: complements deletion)
PMID:23615450	FYPO:0004097	(comment: complements deletion)
PMID:23615450	PBO:0104670	(Figure 4C)
PMID:23615450	FYPO:0001368	(comment: complements deletion)
PMID:23615450	FYPO:0002060	(comment: complements deletion)
PMID:23615450	FYPO:0002060	(comment: complements deletion)
PMID:23615450	FYPO:0002060	(comment: complements deletion)
PMID:23615450	PBO:0104668	(Figure 1D)
PMID:23615450	PBO:0104667	(Figure 1C and Supplemental Figure S1C)
PMID:23615450	PBO:0104666	(Figure 1E and Supplemental Figure S1C)
PMID:23615450	PBO:0101823	(Figure 1E and Supplemental Figure S1C)
PMID:23615450	PBO:0101822	(Figure 1E and Supplemental Figure S1C)
PMID:23615450	FYPO:0001368	(comment: complements deletion)
PMID:23615450	GO:0051015	(comment: Kd ≈ 20 μM) Supplemental Figure S5B
PMID:23615450	PBO:0101816	(comment: complements deletion)
PMID:23615450	FYPO:0001357	(Figure 4F)
PMID:23615450	PBO:0104669	(Figure 4F) (comment: inferred penetrance because growth not m,uch affected)
PMID:23615450	PBO:0104674	(comment: complements deletion) Figure 6A
PMID:23615450	FYPO:0001496	(Figure 4F)
PMID:23615450	FYPO:0004653	(Fig. 5)
PMID:23615450	PBO:0104671	(Figure 4C)
PMID:23615450	PBO:0104676	(comment: in interphase)
PMID:23615450	GO:0005515	Supplemental Figure S9C)
PMID:23615450	FYPO:0002061	(Figure 3).
PMID:23615450	FYPO:0002061	(Figure 3).
PMID:23615450	FYPO:0000161	(Figure 3).
PMID:23615450	FYPO:0000639	(comment: complements deletion) Figure 6A
PMID:23615450	PBO:0104672	(comment: complements deletion) Figure 6A
PMID:23628763	GO:0045944	boosts expression of the APC activator Fzr1/Mfr1
PMID:23628763	PBO:0101099	(Fig. 3c)
PMID:23628763	FYPO:0002773	(Fig. 2)
PMID:23628763	PBO:0101103	binds chromatin at promoter, and phenotypes suggest this
PMID:23628763	PBO:0101100	(Fig. 3c)
PMID:23658229	PBO:0095155	(comment: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05))
PMID:23658229	PBO:0103135	(comment: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05))
PMID:23658229	PBO:0095151	(comment: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05))
PMID:23658229	PBO:0095154	(comment: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05))
PMID:23658229	PBO:0103137	(comment: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05))
PMID:23658229	PBO:0096136	(comment: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05))
PMID:23658229	PBO:0103136	(comment: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05))
PMID:23658229	PBO:0103138	(comment: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05))
PMID:23671279	GO:0140469	(comment: vw edited)
PMID:23671279	PBO:0099237	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	PBO:0099238	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	PBO:0099239	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	PBO:0099240	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	PBO:0099241	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	PBO:0099242	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	PBO:0099243	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	PBO:0099235	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	PBO:0099254	(comment: worse than cpc2delta alone)
PMID:23671279	PBO:0099244	(comment: same as gcn2delta alone)
PMID:23671279	PBO:0099253	(comment: same as cpc2delta alone)
PMID:23671279	FYPO:0001097	(comment: same as cpc2delta alone)
PMID:23671279	FYPO:0001097	(comment: same as either single mutant)
PMID:23671279	PBO:0099243	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	PBO:0099242	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	PBO:0099241	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	PBO:0099240	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	PBO:0099239	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	PBO:0099238	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	PBO:0099237	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	PBO:0099236	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	PBO:0099236	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	PBO:0099235	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23677513	FYPO:0002344	(comment: CHECK same as hus1delta alone)
PMID:23677513	FYPO:0002344	(comment: CHECK same as rad9delta alone)
PMID:23677513	FYPO:0002345	(comment: CHECK same as hus1delta alone)
PMID:23677513	FYPO:0002345	(comment: CHECK same as rad9delta alone)
PMID:23677513	FYPO:0000095	(comment: CHECK same as rad9delta alone)
PMID:23677513	FYPO:0000095	(comment: CHECK same as hus1delta alone)
PMID:23677513	FYPO:0000102	(comment: CHECK same as hus1delta alone)
PMID:23677513	FYPO:0000102	(comment: CHECK same as rad9delta alone)
PMID:23687372	FYPO:0000708	(comment: homothallic h90)
PMID:23687372	PBO:0102418	(comment: CHECK occurs_during G1 to G0 transition)
PMID:23687372	PBO:0102420	(comment: CHECK occurs_during G1 to G0 transition)
PMID:23687372	FYPO:0000708	(comment: homothallic h90)
PMID:23687372	FYPO:0000712	(comment: CHECK move down to G1, nitrogen induced)
PMID:23687372	PBO:0102422	(comment: CHECK occurs_during G1 to Go transition)
PMID:23687372	PBO:0102419	(comment: CHECK occurs_during G1 to G0 transition)
PMID:23695302	FYPO:0000223	(comment: they don't say whether the OEP populations continue to grow like normal (viable/inviable).) Also data not shown.
PMID:23754748	FYPO:0002059	(Figure S1)
PMID:23770677	PBO:0098967	We incubated cell ghosts in the presence of ATP and the myosin-II ATPase inhibitor blebbistatin (0.1 mM; ref. 17). Whereas rings underwent rapid contraction in the absence of blebbistatin, ring contraction was abolished in the presence of blebbistatin (Fig. 3a, nD8).
PMID:23770679	GO:1990571	The Alp7-Alp14 complex localises to kinetochores prior to meiosis I independently of microtubules, which does not seem to occur in mitosis.
PMID:23770679	PBO:0100756	(Fig. 2g)
PMID:23770679	FYPO:0007112	(Fig. 2b-d) (comment: CHECK involved in kinetochore retrieval during meiotic prophase)
PMID:23770679	FYPO:0007112	(Fig. 2b-d) (comment: CHECK involved in kinetochore retrieval during meiotic prophase)
PMID:23770679	PBO:0100762	(Figure 4)
PMID:23770679	PBO:0100757	(Fig. 2G)
PMID:23770679	FYPO:0007107	(comment: CHECK meiosis I)
PMID:23770679	FYPO:0007108	(Figure 2a)
PMID:23770679	PBO:0100773	The Nuf2 complex interacts with the Alp7-Alp14 complex phosphorylated by the polo kinase Plo1
PMID:23770679	FYPO:0007108	(Fig. 3d)
PMID:23770679	FYPO:0007109	(Fig. 3d)
PMID:23770679	PBO:0100758	(Fig. 3b)
PMID:23770679	FYPO:0007108	(Figure 4c)
PMID:23770679	PBO:0100761	(Fig. 4d)
PMID:23770679	PBO:0100760	(Fig. 4d)
PMID:23770679	FYPO:0000209	(Fig. 5b)
PMID:23770679	FYPO:0007110	(Fig. 4c)
PMID:23770679	FYPO:0007110	(Fig. 4c)
PMID:23770679	PBO:0100764	(Fig. 6a)
PMID:23770679	PBO:0100765	(Figure 6b,d) (comment: d used chromosome tethered polo mutants, I didn't curate these phenotypes)
PMID:23770679	PBO:0100759	(comment: CHECK Is this phase correct)
PMID:23770679	PBO:0100759	(comment: CHECK Is this phase correct?)
PMID:23770679	PBO:0100759	(comment: CHECK Is this phase correct?)
PMID:23770679	PBO:0100766	(comment: polo consensus) fig 6b
PMID:23770679	PBO:0100767	Supp Fig S6
PMID:23770679	PBO:0100768	Supp Fig S6
PMID:23770679	PBO:0100769	(Fig. 6c) (comment: CHeCK or abolished)
PMID:23770679	PBO:0100770	(Fig. 7)
PMID:23770679	FYPO:0000209	(Fig. 7c)
PMID:23770679	GO:1990571	The Alp7-Alp14 complex localises to kinetochores prior to meiosis I independently of microtubules, which does not seem to occur in mitosis.
PMID:23770679	FYPO:0006427	(Fig. 5b)
PMID:23770679	PBO:0100763	(Fig. 5d,e) (comment: CHECK unattached)
PMID:23770679	GO:1990571	The Alp7-Alp14 complex localises to kinetochores prior to meiosis I independently of microtubules, which does not seem to occur in mitosis.
PMID:23770679	PBO:0100755	The Nuf2 complex interacts with the Alp7-Alp14 complex phosphorylated by the polo kinase Plo1
PMID:23851719	GO:0140673	(comment: results in retaining specifically modified histone H3 at the genes in question)
PMID:23874237	PBO:0021602	(comment: CHECK The SO ID's correspond to tRNA lys/gln/glu)
PMID:23874237	PBO:0021600	(comment: CHECK The SO ID's correspond to tRNA lys/gln/glu)
PMID:23874237	PBO:0021601	(comment: CHECK The SO ID's correspond to tRNA lys/gln/glu)
PMID:23885124	GO:0044732	throughout cell cycle; present in approximately equal stoichiometry with Alp4/GCP2 (immunoblotting and quantification of GFP-Mzt1 and GFP-Alp4 signals at the SPB)
PMID:23885124	GO:0008275	throughout cell cycle; present in approximately equal stoichiometry with Alp4/GCP2 (immunoblotting and quantification of GFP-Mzt1 and GFP-Alp4 signals at the SPB)
PMID:23907979	PBO:0102605	. Interestingly, mtl2D and wsc1D mutants contained much less Rho1p-GTP than wild-type cells when the cultures were grown in the presence of 0.1 lg/mL of Csp for 16 h prior to harvesting (Fig. 4C)
PMID:23907979	GO:0005886	Mtl2p-GFP showed an even membrane distribution with little intra- cellular signals.
PMID:23907979	GO:0031520	Wsc1p-GFP was found along the entire plasma membrane, but appeared much more concentrated in patches at the cell ends. We also noted that Wsc1p-GFP accumulated in intracellular compartments (Fig. 3C and D).
PMID:23907979	FYPO:0001357	The wsc1D and mtl2D mutants grew well under standard growth conditions at both 28 and 37°C and entered the stationary phase at the same time as the wild-type cultures.
PMID:23907979	FYPO:0001357	The wsc1D and mtl2D mutants grew well under standard growth conditions at both 28 and 37°C and entered the stationary phase at the same time as the wild-type cultures.
PMID:23907979	FYPO:0001315	wsc1D and mtl2D cells did not exhibit any evident morphological changes (Fig. 1B)
PMID:23907979	FYPO:0001315	wsc1D and mtl2D cells did not exhibit any evident morphological changes (Fig. 1B)
PMID:23907979	PBO:0102599	~8% of the cells in the wsc1D mutant and 15% of the cells in mtl2D were lysed (Fig. 1B)
PMID:23907979	PBO:0102600	~8% of the cells in the wsc1D mutant and 15% of the cells in mtl2D were lysed (Fig. 1B)
PMID:23907979	PBO:0101752	mtl2D cells were unable to grow on plates supplemented with 0.5 lg/mL Csp, whereas the wild-type cells were able to withstand concentrations of up to 5 lg/ mL
PMID:23907979	PBO:0101751	wsc1D cell growth was inhibited above 2 lg/mL of Csp (Fig. 1C)
PMID:23907979	PBO:0102601	We found that GS activity was slightly reduced in mtl2D null cells (Fig. 1D)
PMID:23907979	FYPO:0002627	Moreover, when we looked at the cell wall composition of mtl2D mutants we found a decrease in the total amount of glucose incorporated in the cell wall as compared with wild-type cells (30% in wild-type cells and 25% in mtl2D). The difference was mainly due to a decrease in the b-glucan content (17% in the wild type and 13% in the mtl2D) (Fig. 1E).
PMID:23907979	PBO:0093626	Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1).
PMID:23907979	PBO:0102602	Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1).
PMID:23907979	PBO:0094276	Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1).
PMID:23907979	PBO:0093578	Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1).
PMID:23907979	PBO:0093590	Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1).
PMID:23907979	FYPO:0000760	The mating rate was not affected in mtl2Δh+ × mtl2Δh− or wsc1Δh+ × wsc1Δh− homozygous crosses
PMID:23907979	FYPO:0000760	The mating rate was not affected in mtl2Δh+ × mtl2Δh− or wsc1Δh+ × wsc1Δh− homozygous crosses
PMID:23907979	FYPO:0000647	Repression of mtl2+ promoted cell lysis and the cells shrunk without the release of cytoplasmic material.
PMID:23907979	FYPO:0007910	Repression of mtl2+ promoted cell lysis and the cells shrunk without the release of cytoplasmic material.
PMID:23907979	GO:0005886	Wsc1p-GFP was found along the entire plasma membrane, but appeared much more concentrated in patches at the cell ends. We also noted that Wsc1p-GFP accumulated in intracellular compartments (Fig. 3C and D).
PMID:23907979	PBO:0102603	In tea4D cells, Wsc1p-GFP localized mainly to the growing tip that was stained with Cfw (Fig. 3C).
PMID:23907979	PBO:0101751	mtl2D cells were unable to grow on plates supplemented with 0.5 lg/mL Csp, whereas the wild-type cells were able to withstand concentrations of up to 5 lg/ mL
PMID:23907979	PBO:0101751	(Figure 4A) expression of rho1+, rgf1+, and rgf2+ restored the growth of an mtl2D mutant in the presence of the antifungal agent, whereas overexpression of rgf3+ did not suppress the growth defect.
PMID:23907979	PBO:0101751	(Figure 4A) expression of rho1+, rgf1+, and rgf2+ restored the growth of an mtl2D mutant in the presence of the antifungal agent, whereas overexpression of rgf3+ did not suppress the growth defect.
PMID:23907979	PBO:0101751	(Figure 4A) expression of rho1+, rgf1+, and rgf2+ restored the growth of an mtl2D mutant in the presence of the antifungal agent, whereas overexpression of rgf3+ did not suppress the growth defect.
PMID:23907979	PBO:0101751	mtl2D cells were unable to grow on plates supplemented with 0.5 lg/mL Csp, whereas the wild-type cells were able to withstand concentrations of up to 5 lg/ mL
PMID:23907979	FYPO:0001357	(Figure 4B) the activation of Rho1p, through the expression of a constitutively active form of Rho1p or overexpression of the wild-type Rho1p or Rgf1p, efficiently restored the growth of a strain (P81nmt-mtl2 wsc1D) unable to grow in the presence of thiamine (promoter off).
PMID:23907979	PBO:0099857	GTP bound modified form . Interestingly, mtl2D and wsc1D mutants contained much less Rho1p-GTP than wild-type cells when the cultures were grown in the presence of 0.1 lg/mL of Csp for 16 h prior to harvesting (Fig. 4C)
PMID:23907979	PBO:0099857	GTP bound modified form. Interestingly, mtl2D and wsc1D mutants contained much less Rho1p-GTP than wild-type cells when the cultures were grown in the presence of 0.1 lg/mL of Csp for 16 h prior to harvesting (Fig. 4C)
PMID:23907979	PBO:0102604	. Interestingly, mtl2D and wsc1D mutants contained much less Rho1p-GTP than wild-type cells when the cultures were grown in the presence of 0.1 lg/mL of Csp for 16 h prior to harvesting (Fig. 4C)
PMID:23907979	PBO:0102606	. Interestingly, mtl2D and wsc1D mutants contained much less Rho1p-GTP than wild-type cells when the cultures were grown in the presence of 0.1 lg/mL of Csp for 16 h prior to harvesting (Fig. 4C)
PMID:23907979	FYPO:0002061	The wsc1Drgf2D double mutant was viable, but we failed to find any double- mutant spore wsc1Drgf1D. T
PMID:23907979	FYPO:0000021	(comment: described as rounded , but more 'stubby')
PMID:23907979	FYPO:0001357	The wsc1D and mtl2D mutants grew well under standard growth conditions at both 28 and 37°C and entered the stationary phase at the same time as the wild-type cultures.
PMID:23936074	PBO:0095821	(comment: assayed using minichromosomes and internal telomeric repeat arrays)
PMID:23936074	PBO:0112081	(comment: CHECK increased staining of all chromatin)
PMID:23956092	FYPO:0001496	(comment: was branched, elongated, multiseptate cell )
PMID:23962284	PBO:0103049	(comment: recombinant hal3 not a strong inhibitor in vitro)
PMID:23962284	FYPO:0002059	(comment: we don't know if they germinate or not)
PMID:23966468	PBO:0099793	This is inferred from a combination of genetic interactions, localizations and phenocopy experiments, it has not been directly assayed but it feels 'safe' (VW)
PMID:23977061	GO:0006887	(comment: I changed this to exocytosis. This is required for cell wall organization, as it is causally upstream (val))
PMID:23977061	PBO:0104044	effect on secretion is specific for cell wall enzymes; secretion of acid phosphatase is normal (comment: but assayed acid phosphatase activity in medium, so can't tell which gene(s))
PMID:23986474	FYPO:0000620	dns
PMID:23986474	FYPO:0006917	(Fig. 4c)
PMID:23986474	FYPO:0001357	(Fig. 3c) We therefore compared the ability of wee1.as1 and wee1.as8 to suppress cdc25.22 lethality at 36 ̊C. Inhibition of Wee1.as8 but not Wee1.as1 activity with analogue addition suppressed cdc25.22 lethality at 36 ̊C (Fig. 3B). A comparison of four ATP analogues revealed that the suppression (and therefore Wee1 inhibition) was most effective with 3BrB-PP1 (Fig. 3C).
PMID:23986474	PBO:0108020	(Fig. 2B) orb5.as2 displayed moderate sensitivity to 30 mM of 3BrB-PP1, whereas orb5.as1 showed none
PMID:23986474	PBO:0108020	(Fig. 2B) orb5.as2 displayed moderate sensitivity to 30 mM of 3BrB-PP1, whereas orb5.as1 showed none
PMID:23986474	PBO:0108020	(Fig. 2B) orb5.as2 displayed moderate sensitivity to 30 mM of 3BrB-PP1, whereas orb5.as1 showed none
PMID:23986474	PBO:0108019	(Fig. 2B). The M167F mutation in either the orb5.as1 or orb5.as2 backbone generated the orb5.as8 and orb5.as9 alleles, which were more sensitive to analogue inhibition than the respective parental allele
PMID:23986474	PBO:0108019	(Fig. 1) Chronic exposure to analogue through growth on solid medium reiterated the acute impact of analogue inhibition in liquid culture (Fig. 1A) and established that plo1.as8 is most effectively inhibited by 3BrB- PP1 (Fig. 1B).
PMID:23986474	PBO:0108020	(Fig. 2B) orb5.as2 displayed moderate sensitivity to 30 mM of 3BrB-PP1, whereas orb5.as1 showed none
PMID:23986474	PBO:0108019	(Fig. 1) Chronic exposure to analogue through growth on solid medium reiterated the acute impact of analogue inhibition in liquid culture (Fig. 1A) and established that plo1.as8 is most effectively inhibited by 3BrB- PP1 (Fig. 1B).
PMID:23986474	PBO:0108019	(Fig. 1)
PMID:23986474	PBO:0108019	(Fig. 1)
PMID:23986474	FYPO:0002061	DNS
PMID:23986474	FYPO:0001125	rb5.as8 inhibition did not produce the ‘orb’ phenotype observed in the original orb5.ts mutants at the restrictive temperature (data not shown)
PMID:23986474	PBO:0095711	(Table 1; Fig. 3A)
PMID:23986474	PBO:0095711	(Table 1; Fig. 3A)
PMID:23986474	PBO:0108019	(Fig. 2B). The M167F mutation in either the orb5.as1 or orb5.as2 backbone generated the orb5.as8 and orb5.as9 alleles, which were more sensitive to analogue inhibition than the respective parental allele
PMID:23986474	FYPO:0002061	(Fig. 3c)
PMID:23986474	PBO:0108019	(Fig. 1)
PMID:23986474	FYPO:0000444	The static FACS profiles established that replication was indeed inhibited in analogue-released cdc10.v50 wee1.as8 cdc25.22 cells after analogue addition (Fig. 7B, right panel).
PMID:23986474	FYPO:0005344	as arrested at 36 ̊C for 4.25 hours and released into synchronous mitosis by Wee1 inhibition using 30 mM 3BrB-PP1. The figure shows tubulin immunofluorescence and DAPI signals of cells 3 hours after release to reveal the characteristic ‘crows foot’ configuration of microtubules of cut7 mutants as the two halves of the mitotic spindle fail to interdigitate.
PMID:23986474	FYPO:0001357	(Fig. 3c) We therefore compared the ability of wee1.as1 and wee1.as8 to suppress cdc25.22 lethality at 36 ̊C. Inhibition of Wee1.as8 but not Wee1.as1 activity with analogue addition suppressed cdc25.22 lethality at 36 ̊C (Fig. 3B). A comparison of four ATP analogues revealed that the suppression (and therefore Wee1 inhibition) was most effective with 3BrB-PP1 (Fig. 3C).
PMID:23986474	PBO:0033178	Analogue-released wee1.as8 cdc25.22 cut9.665 cells transiently accumulated much higher levels of metaphase spindles than wild-type cells before they ‘leaked’ through this mitotic arrest to execute telophase and cytokinesis with the classic ‘cut’ phenotype that originally led to the identification of the cut9.665 mutation (Fig. 6A,B)
PMID:24003116	FYPO:0001534	(comment: CONDITION Grown in EMM + 200uM ZnSo). (comment: Measurements made via ICP-MS)
PMID:24003116	FYPO:0001552	(comment: CONDITION Grown in EMM + 200uM ZnSo) (comment: Measurements made via ICP-MS)
PMID:24003116	FYPO:0001552	(comment: CONDITION Grown in EMM + 200uM ZnSo). (comment: Measurements made via ICP-MS)
PMID:24003116	GO:0005634	(comment: CONDITION Visualized via Florescence using an integrated LOZ1::GFP construct) (comment: CONDITION grown in EMM +/- ZnSo4)
PMID:24003116	PBO:0100861	(comment: CHECK directly regulates adh4)
PMID:24003116	PBO:0100862	(comment: Via EMSA binds directly to adh4 promoter).
PMID:24006256	GO:0010971	(comment: Dnt1 down-regulates Wee1 kinase. Had to remove extensions: independent_of(PomBase:Cdc25)| independent_of(PomBase:Rad3)| independent_of(PomBase:Chk1)| independent_of(PomBase:Cds1)| independent_of(PomBase:Clp1)| independent_of(PomBase:Pom1)| independent_of(PomBase:Cut12)| dependent_on(PomBase:Wee1) | acts_upstream_of(wee1))
PMID:24006256	FYPO:0006822	(comment: wee1-50 epistatic to dnt1delta; shows that cell cycle regulation by Dnt1 depends on Wee1)
PMID:24006488	PBO:0098800	(Fig. 4)
PMID:24006488	PBO:0098802	(Fig. 4)
PMID:24006488	PBO:0098799	(Fig. 4)
PMID:24006488	MOD:00696	(comment: annotate - Serine 114 and Threonine 115 are phosphorylated by Cds1 upon activation of the DNA replication checkpoint) (comment: Yox1 phosphorylation by Cds1 releases Yox1 from MBF and activates MBF-dependent transcription)
PMID:24006488	PBO:0098802	(Fig. 4)
PMID:24006488	PBO:0098794	(comment: Phosphorylation releases MBF from DNA and represses transcription of MBF-dependent genes.)
PMID:24006488	PBO:0098801	(Fig. 4)
PMID:24006488	PBO:0098804	(comment: localizes the MBF complex)
PMID:24006488	PBO:0098794	(comment: Phosphorylation releases MBF from DNA and represses transcription of MBF-dependent genes.)
PMID:24006488	PBO:0098801	(Fig. 4)
PMID:24013500	FYPO:0002335	We found that all three mutations are required to produce a silencing defect on 5- FOA medium (Fig. 1B).
PMID:24013500	FYPO:0002335	We found that all three mutations are required to produce a silencing defect on 5- FOA medium (Fig. 1B).
PMID:24013500	PBO:0096188	We found that all three mutations are required to produce a silencing defect on 5- FOA medium (Fig. 1B). However, the mutant with the three amino acid changes (triple mutant) has a milder silencing defect on 5-FOA when compared with the original seb1-1 mutant.
PMID:24013500	FYPO:0000876	In the ectopic heterochromatic silencing reporter strain, the seb1-1 mutation causes an accumulation of the ura4+ transcript (Fig. 1D) and a strong defect in H3K9me2 at the ura4+ gene (Fig. 1E), supporting the growth defect observed using the 5-FOA assay.
PMID:24013500	FYPO:0004170	Furthermore, the elimination of H3K9me2 at dg and dh repeats was also observed in strains that have the dcr1-R1R2 mutation combined with a deletion mutation that eliminates the Clr1, Chp2, or Mit1 subunits of SHREC (Fig. 3A).
PMID:24013500	GO:0031508	(comment: siRNA independent)
PMID:24013500	PBO:0096189	A strain harboring a ura4+ reporter gene inserted into the innermost repeat (imr) region of centromere 1 displays reduced growth on 5-FOA when harboring the seb1-1 allele (Fig. 1C). I
PMID:24013500	PBO:0112911	As expected, Hrr1, an RNAi factor, also associates with dg and dh ncRNAs but not with snR30 or act1+ RNA (Supplemental Fig. S1A).
PMID:24013500	GO:0030515	to assess its association with dg and dh ncRNAs as well as the snoRNA snR30. Seb1 displays a strong association with these ncRNAs but not with the act1+ RNA (Fig. 1A).
PMID:24013500	PBO:0112918	Together, these data support our hypothesis that Seb1 acts by recruiting SHREC to pericentromeric heterochromatin.
PMID:24013500	GO:0031508	(comment: siRNA independent)
PMID:24013500	GO:0031508	(comment: siRNA independent)
PMID:24013500	GO:0031508	(comment: siRNA independent)
PMID:24013500	PBO:0112913	To further test whether Seb1 functions in the same pathway as SHREC in promoting H3K9me, we compared H3K9me2 levels at dg and dh repeats of the seb1-1 clr3D double mutant with those of the corresponding single mutants. Significantly, the double and single mutants display very similar levels of H3K9me2, ;20%-30% of wild-type levels (Fig. 3B).
PMID:24013500	FYPO:0002335	We found that all three mutations are required to produce a silencing defect on 5- FOA medium (Fig. 1B).
PMID:24013500	PBO:0112911	to assess its association with dg and dh ncRNAs as well as the snoRNA snR30. Seb1 displays a strong association with these ncRNAs but not with the act1+ RNA (Fig. 1A).
PMID:24013500	PBO:0111009	We found that every subunit of SHREC tested (Clr3, Clr1, Mit1, and Chp2) is enriched at both dg and dh repeats. However, in the seb1-1 mutant, this enrichment is abolished or strongly reduced (Figs. 5A-D).
PMID:24013500	PBO:0112917	We found that every subunit of SHREC tested (Clr3, Clr1, Mit1, and Chp2) is enriched at both dg and dh repeats. However, in the seb1-1 mutant, this enrichment is abolished or strongly reduced (Figs. 5A-D).
PMID:24013500	PBO:0112916	We found that every subunit of SHREC tested (Clr3, Clr1, Mit1, and Chp2) is enriched at both dg and dh repeats. However, in the seb1-1 mutant, this enrichment is abolished or strongly reduced (Figs. 5A-D).
PMID:24013500	PBO:0112915	We found that every subunit of SHREC tested (Clr3, Clr1, Mit1, and Chp2) is enriched at both dg and dh repeats. However, in the seb1-1 mutant, this enrichment is abolished or strongly reduced (Figs. 5A-D).
PMID:24013500	PBO:0112914	Moreover, we found that the seb1-1 mutation increases Pol II occupancy and H3K14 acetylation levels at dg and dh repeats (Figs. 3D,E)
PMID:24013500	PBO:0112913	Similar results were obtained when comparing H3K9me2 levels at dg and dh repeats of the seb1-1 clr1D double mutant with the levels of the corresponding single mutants (Fig. 3C). T
PMID:24013500	PBO:0112912	Indeed, the level of Seb1 protein is lower in the seb1-1 mutant when compared with its level in the wild-type seb1+ strain (Supplemental Fig. S4)
PMID:24013500	PBO:0112913	Similar results were obtained when comparing H3K9me2 levels at dg and dh repeats of the seb1-1 clr1D double mutant with the levels of the corresponding single mutants (Fig. 3C). T
PMID:24013500	PBO:0112913	To further test whether Seb1 functions in the same pathway as SHREC in promoting H3K9me, we compared H3K9me2 levels at dg and dh repeats of the seb1-1 clr3D double mutant with those of the corresponding single mutants. Significantly, the double and single mutants display very similar levels of H3K9me2, ;20%-30% of wild-type levels (Fig. 3B).
PMID:24013500	PBO:0112913	To further test whether Seb1 functions in the same pathway as SHREC in promoting H3K9me, we compared H3K9me2 levels at dg and dh repeats of the seb1-1 clr3D double mutant with those of the corresponding single mutants. Significantly, the double and single mutants display very similar levels of H3K9me2, ;20%-30% of wild-type levels (Fig. 3B).
PMID:24013500	FYPO:0002837	seb1-1 displays normal levels of pericentromeric siRNA accumulation (Fig. 2A)
PMID:24013500	FYPO:0000220	In contrast, a catalytically dead Dcr1 mutant (dcr1-R1R2) (Colmenares et al. 2007) displays a dramatic increase in dg and dh transcript levels (Fig. 2B).
PMID:24013500	FYPO:0004170	Strikingly, while the levels of H3K9me2 are reduced by only threefold to fivefold in the single mutants, H3K9me2 is virtually abolished in the dcr1-R1R2 seb1-1 double mutant to background levels comparable with those measured in the clr4D mutant (Fig. 2C).
PMID:24013500	GO:0031508	(comment: siRNA independent)
PMID:24013500	PBO:0098584	while H3K9me2 levels at the dg and dh repeats are modestly reduced in the dcr1-R1R2 single mutant, these levels are virtually eliminated in the dcr1-R1R2 clr3D double mutant, a phenotype strikingly similar to that of the dcr1-R1R2 seb1-1 double mutant (Fig. 3A).
PMID:24013500	FYPO:0004170	Finally, a catalytically dead point mutation in the Clr3 HDAC or the Mit1 ATPase domain also eliminates H3K9me in dcr1-R1R2 cells (Fig. 3A).
PMID:24013500	FYPO:0004170	Finally, a catalytically dead point mutation in the Clr3 HDAC or the Mit1 ATPase domain also eliminates H3K9me in dcr1-R1R2 cells (Fig. 3A).
PMID:24013500	FYPO:0004170	Furthermore, the elimination of H3K9me2 at dg and dh repeats was also observed in strains that have the dcr1-R1R2 mutation combined with a deletion mutation that eliminates the Clr1, Chp2, or Mit1 subunits of SHREC (Fig. 3A).
PMID:24013500	FYPO:0004170	Furthermore, the elimination of H3K9me2 at dg and dh repeats was also observed in strains that have the dcr1-R1R2 mutation combined with a deletion mutation that eliminates the Clr1, Chp2, or Mit1 subunits of SHREC (Fig. 3A).
PMID:24013504	FYPO:0003107	(comment: dependent_on(GO:0006312)| not_dependent_on(GO:0007004))
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0005682	(Table 1)
PMID:24014766	GO:0005682	(Table 1)
PMID:24014766	GO:0005682	(Table 1)
PMID:24014766	GO:0005682	(Table 1)
PMID:24014766	GO:0005686	(Table 1)
PMID:24014766	GO:0005686	(Table 1)
PMID:24014766	GO:0005686	(Table 1)
PMID:24014766	GO:0005686	(Table 1)
PMID:24014766	GO:0005686	(Table 1)
PMID:24014766	GO:0005686	(Table 1)
PMID:24014766	GO:0005686	(Table 1)
PMID:24014766	GO:0005686	(Table 1)
PMID:24014766	GO:0005686	(Table 1)
PMID:24014766	GO:0005686	(Table 1)
PMID:24014766	GO:0045292	1,193 introns (of 5,361 possible introns) whose splicing efficiency was significantly compromised in the mutant.
PMID:24014766	PBO:0113766	In the cwf10-ΔNTE background, levels of Brr2 and Prp3 were similar to levels seen in wild-type cells; however, both Cdc5 and Prp1 levels were reduced to 70% and 65%, respectively (Fig. 2I).
PMID:24014766	PBO:0113765	In the cwf10-ΔNTE background, levels of Brr2 and Prp3 were similar to levels seen in wild-type cells; however, both Cdc5 and Prp1 levels were reduced to 70% and 65%, respectively (Fig. 2I).
PMID:24014766	PBO:0113764	In the cwf10-ΔNTE background, levels of Brr2 and Prp3 were similar to levels seen in wild-type cells; however, both Cdc5 and Prp1 levels were reduced to 70% and 65%, respectively (Fig. 2I).
PMID:24014766	PBO:0113763	In the cwf10-ΔNTE background, levels of Brr2 and Prp3 were similar to levels seen in wild-type cells; however, both Cdc5 and Prp1 levels were reduced to 70% and 65%, respectively (Fig. 2I).
PMID:24014766	PBO:0113762	Using quantitative Western blotting, we found that levels of Cwf10 were consistently higher in cwf10-ΔNTE cells than in wild-type cells when quantified against the loading control Cdc2 (Cdk1) (Fig. 2I)
PMID:24014766	FYPO:0003029	GENERAL SPLICING DEFECT RT-PCR analysis of tbp1_a, an mRNA intron highly sensitive to splicing defects (53), indicated that cwf10-ΔNTE cells grown at 25°C accumulate unspliced transcript (Fig. 2C). retrotransposon silencing by mRNA destabilization
PMID:24014766	FYPO:0001234	The cwf10-ΔNTE strain formed slightly smaller colonies on solid media at all temperatures tested (Fig. 2A) and exhibited slow growth in liquid culture at 25°C and 36°C compared with wild-type cells (Fig. 2B and data not shown)
PMID:24014766	FYPO:0001234	The cwf10-ΔNTE strain formed slightly smaller colonies on solid media at all temperatures tested (Fig. 2A) and exhibited slow growth in liquid culture at 25°C and 36°C compared with wild-type cells (Fig. 2B and data not shown)
PMID:24014766	FYPO:0002061	Although cwf10 2-135Δ aligns with snu114ΔN (Fig. 1B), the S. pombe allele did not support growth at either 25°C or 32°C when integrated at the endogenous locus (data not shown), while the S. cerevisiae allele is viable at temperatures below 40°C (30).
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0005682	(Table 1)
PMID:24014766	GO:0005682	(Table 1)
PMID:24014766	GO:0005682	(Table 1)
PMID:24014766	GO:0005682	(Table 1)
PMID:24014766	GO:0005686	(Table 1)
PMID:24014766	GO:0005686	(Table 1)
PMID:24014766	GO:0005686	(Table 1)
PMID:24014766	GO:0005686	(Table 1)
PMID:24014766	GO:0005686	(Table 1)
PMID:24014766	GO:0005682	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0000974	(Table 1)
PMID:24014766	GO:0005681	(Table 1)
PMID:24014766	GO:0005681	(Table 1)
PMID:24014766	GO:0005681	(Table 1)
PMID:24014766	GO:0005681	(Table 1)
PMID:24014766	GO:0005681	(Table 1)
PMID:24014766	GO:0005681	(Table 1)
PMID:24014766	GO:0005681	(Table 1)
PMID:24014766	GO:0005681	(Table 1)
PMID:24014766	GO:0005681	(Table 1)
PMID:24014766	GO:0005681	(Table 1)
PMID:24014766	GO:0005681	(Table 1)
PMID:24014766	GO:0005681	(Table 1)
PMID:24014766	GO:0005681	(Table 1)
PMID:24014766	FYPO:0003029	(comment: GENERAL SPLICING DEFECT) The ratio of mature to premature signal for the tbp1_a intron was almost identical for the two truncations (2.1 ± 0.2 for cwf10-ΔNTE versus 2.0 ± 0.3 for cwf10 2-23Δ), while the ratio in the wild-type strain was 9.7 ± 1.5 (Fig. 6H). Th
PMID:24014766	GO:0005682	(Table 1)
PMID:24014766	GO:0005682	(Table 1)
PMID:24021628	GO:0006360	(comment: CHECK heterologous complemetation of S. c HMO1)
PMID:24039245	PBO:0107152	(comment: CHECK in vitro assay with purified proteins)
PMID:24047646	FYPO:0005207	(Fig. 6) shows nif1delta cells still have G2-M size control
PMID:24047646	FYPO:0005206	(Fig. 6) shows wee1-50 cells at restrictive temperature have lost G2-M size control
PMID:24047646	FYPO:0006822	(Fig. 3, Table 1)
PMID:24047646	FYPO:0005207	(Fig. 6) shows pom1delta cells still have G2-M size control
PMID:24047646	PBO:0103987	(Fig. 1) In early G2 nif1 localisation is monopolar and in late G2 it is bipolar
PMID:24047646	PBO:0103988	(Fig. 1)
PMID:24047646	PBO:0103989	(Fig. 1)
PMID:24047646	PBO:0103988	(Fig. 1)
PMID:24047646	GO:0071341	(Fig. 1)
PMID:24047646	FYPO:0006822	(Fig. 3, Table 1)
PMID:24047646	FYPO:0006822	(Fig. 3, Table 1)
PMID:24055157	PBO:0106630	Hhp1-GFP localization at SPBs is Sid4 independent (Figure S3E)
PMID:24055157	GO:0005816	In cells growing asynchronously, both Hhp1-GFP and Hhp2-GFP localized to the nucleus SPBs, and the cell division site, although Hhp2-GFP was more prominent at the division site compared to Hhp1-GFP (Figure 3B).
PMID:24055157	PBO:0094510	Although mutating S278 to alanine abolished Sid4 ubiquitination (Figure 1D)
PMID:24055157	PBO:0106626	In dma1Δ cells, a single slower migrating form of Sid4 was detected, which was collapsed by phosphatase treatment, indicating that Sid4 is phosphorylated in vivo (Figure 1A, lanes 3 and 4). In vivo radiolabeling experiments validated Sid4 as a phospho-protein and revealed that Sid4 is phosphorylated on serines and threonines (Figure S1A-C).
PMID:24055157	PBO:0106631	assayed with human CK1
PMID:24055157	PBO:0106631	assayed with human CK1, process from phenotypes (dma1 dependent pathway)
PMID:24055157	PBO:0106629	Hhp1-GFP localization at SPBs is Sid4 independent (Figure S3E)
PMID:24055157	GO:0005634	In cells growing asynchronously, both Hhp1-GFP and Hhp2-GFP localized to the nucleus SPBs, and the cell division site, although Hhp2-GFP was more prominent at the division site compared to Hhp1-GFP (Figure 3B).
PMID:24055157	FYPO:0002060	In corroboration of these findings, sid4(T275A) mutants were refractory to dma1 overexpression lethality (Figure 2D).
PMID:24055157	FYPO:0004537	cells bypassed the arrest after 5 hrs (Figure 2C).
PMID:24055157	FYPO:0004537	cells bypassed the arrest after 5 hrs (Figure 2C). ......These data indicate that mutating T275 eliminates Dma1-dependent checkpoint signaling.
PMID:24055157	PBO:0096161	Thus, phosphorylation on both T275 and S278 is necessary and sufficient to support binding of the Dma1 FHA domain to Sid4 and Sid4 ubiquitination.
PMID:24055157	PBO:0094517	Although Dma1-GFP still localized to SPBs in sid4(T275A) mutant cells (Figure S1F)
PMID:24055157	PBO:0106628	Although Dma1-GFP still localized to SPBs in sid4(T275A) mutant cells (Figure S1F)
PMID:24055157	PBO:0094517	Although Dma1-GFP still localized to SPBs in sid4(T275A) mutant cells (Figure S1F)
PMID:24055157	PBO:0106627	mutating S278 to a glutamate did not affect Sid4 ubiquitination (Figure 1D).
PMID:2406029	FYPO:0001916	same as cdc2-ww single mutant
PMID:24074952	MOD:00047	(comment: CHECK residue=T235 | residue=T187, annotation_extension=added_by(CDK COMPLEX, CDC2 AND CDC13) | residue=T215)
PMID:24074952	MOD:00047	(comment: CHECK residue=T235 | residue=T187, annotation_extension=added_by(CDK COMPLEX, CDC2 AND CDC13) | residue=T215)
PMID:24074952	MOD:00047	(comment: CHECK residue=T235 | residue=T187, annotation_extension=added_by(CDK COMPLEX, CDC2 AND CDC13) | residue=T215)
PMID:24081329	PBO:0094607	evidence for all FYPO:0001908 = northern blot
PMID:24095277	PBO:0108681	(comment: CHECK has substrates centromere outer repeat transcripts and polyA mRNA. Activated by mg2+)
PMID:24095277	PBO:0101060	(comment: CHECK has substrates centromere outer repeat transcripts and polyA mRNA. Activated by mg2+)
PMID:24095277	GO:0016891	(comment: does it produce 5' monoesters?)
PMID:24115772	GO:1903475	(comment: dependent on septation initiation signaling (GO:0031028))
PMID:24115772	PBO:0018470	(comment: CHECK during(GO:0051329))
PMID:24118096	GO:0110052	(comment: Trx1's involvement in tis process is to recycle mxr1 for met-O conversion to met )
PMID:24127216	PBO:0096493	(Fig. 1B)
PMID:24127216	PBO:0096493	(Fig. 1B)
PMID:24127216	GO:0030041	(Fig. 1D-G)
PMID:24127216	FYPO:0003000	(Fig. 1D-G)
PMID:24127216	FYPO:0003001	(Fig. 3E)
PMID:24127216	FYPO:0003000	(Fig. 1G-G)
PMID:24127216	FYPO:0002998	(Fig. 1H)
PMID:24127216	FYPO:0001368	(Fig. S1a)
PMID:24127216	FYPO:0001365	(Fig. 2A)
PMID:24127216	FYPO:0003014	(Fig. 2A)
PMID:24127216	PBO:0104781	(Fig. 2A)
PMID:24127216	PBO:0104780	(comment: CHECK exists during anaphase A and anaphase B)
PMID:24127216	FYPO:0003001	(Fig. 3E)
PMID:24127216	PBO:0099316	(comment: CHECK exists during anaphase A and anaphase B)
PMID:24127216	FYPO:0002998	(Fig. 1A)
PMID:24146635	PBO:0020826	(comment: CONDITION prolonged heat exposure (more than ~45 min))
PMID:24146635	PBO:0099108	"""Both Gef1-3YFP and Scd1-GFP exhibited bipolar localization in majority of late wild type cells"""
PMID:24146635	PBO:0099108	"""Both Gef1-3YFP and Scd1-GFP exhibited bipolar localization in majority of late wild type cells"""
PMID:24146635	PBO:0020827	(comment: CONDITION shorter duration of heat exposure (up to ~45 min))
PMID:24146635	PBO:0023812	(comment: punctate; shorter duration of heat exposure (up to ~45 min))
PMID:24146635	PBO:0020827	(comment: CONDITION shorter duration of heat exposure (up to ~45 min))
PMID:24146635	PBO:0020827	(comment: CONDITION shorter duration of heat exposure (up to ~45 min))
PMID:24146635	FYPO:0000082	(comment: 36 degrees (not brief heat shock))
PMID:24146635	FYPO:0001326	Global gene expression profile (RNAseq) of deletion similar to that of heat-stressed wild type.
PMID:24146635	FYPO:0001326	Global gene expression profile (RNAseq) of deletion similar to that of heat-stressed wild type.
PMID:24146635	PBO:0020826	(comment: CONDITION prolonged heat exposure (more than ~45 min))
PMID:24146635	PBO:0020826	(comment: CONDITION prolonged heat exposure (more than ~45 min))
PMID:24146635	PBO:0020826	(comment: CONDITION prolonged heat exposure (more than ~45 min))
PMID:24146635	PBO:0020826	(comment: CONDITION prolonged heat exposure (more than ~45 min))
PMID:24146635	PBO:0020826	(comment: CONDITION prolonged heat exposure (more than ~45 min))
PMID:24147005	FYPO:0006539	(Figure 7c)
PMID:24147005	FYPO:0006538	(Figure 6A)
PMID:24155978	PBO:0102936	(comment: all independent of Sty1 (effects of H2O2 & NAC unchanged in sty1delta))
PMID:24155978	PBO:0093578	(Fig. 5S)
PMID:24155978	PBO:0102935	(Fig. 5X)
PMID:24161933	PBO:0099160	Even reduction to about 10% of the original Mad1 level, which is hardly visible by fluorescence microscopy (Fig. 2e), did not fully abolish the SAC
PMID:24161933	PBO:0112077	(comment: 10% of endogenous mad2 level), Fig. S4
PMID:24161933	PBO:0099162	(Fig. 2d)
PMID:24161933	PBO:0099161	(Fig. 5a)
PMID:24161933	PBO:0018530	(Fig. 1)
PMID:24161933	FYPO:0003762	In cells with 30% Mad1, the checkpoint was markedly impaired in minimal medium, although largely functional in rich medium
PMID:24161933	PBO:0112074	(comment: 300% of endogenous mad1 level), Fig. S4
PMID:24161933	PBO:0112075	(comment: 10% of endogenous mad1 level), Fig. S4
PMID:24161933	PBO:0112076	(comment: 30% of endogenous mad1 level), Fig. S4
PMID:24161933	FYPO:0004318	(comment: CHECK abundances of 40% or lower), cells lacked checkpoint activity.
PMID:24161933	PBO:0112078	(comment: 65% of endogenous mad2 level), Fig. S4
PMID:24161933	PBO:0112079	(comment: 30% of endogenous mad3 level), Fig. S4
PMID:24161933	PBO:0112080	(comment: 40% of endogenous slp1 level), Fig. S4
PMID:24161933	PBO:0112074	(comment: 500% of endogenous mad1 level), Fig. S4
PMID:24167631	FYPO:0001178	(comment: mah: CHECK FYPO:0001178 + PECO:0000240 captures info for requested new term (Term name: loss of viability upon long-term nutrient starvation Definition: A cell population phenotype in which a smaller than normal proportion of the population remains viable when cells in a culture in stationary phase are deprived of nitrogen. Use this term to annotate experiments in which a culture is cultivated in stationary phase under nitrogen-depleted conditions for a long time (more than 1 week), and then the number of cells viable enough to form a colony upon return to conditions supporting vegetative growth is measured and compared to wild type)
PMID:24186976	GO:0005515	Supp fig7
PMID:24186976	GO:0005515	Supp fig7
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	PBO:0093785	(Fig. 6B)
PMID:24223771	PBO:0093786	(Fig. 6B)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	PBO:0093784	(Fig. 6)
PMID:24223771	PBO:0093786	(Fig. 6A)
PMID:24223771	PBO:0093785	(Fig. 4B, 6A)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	FYPO:0007035	(Fig. 6B)
PMID:24223771	PBO:0093786	(Fig. 6C)
PMID:24223771	PBO:0093786	(Fig. 6C)
PMID:24223771	PBO:0093784	(Fig. S3)
PMID:24223771	PBO:0093784	(Fig. 4B)
PMID:24223771	PBO:0093784	(Fig. 4B)
PMID:24223771	FYPO:0007035	(Fig. 4B)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24223771	PBO:0117211	(Table 1)
PMID:24224056	FYPO:0002924	The decrease in cell growth on maltose medium is suppressed by neighboring wild-type cells but not by agl1 delta cells, which are defective in maltase secretion.
PMID:24224056	GO:0045944	in response to carbon source change from glucose to maltose (comment: CHECK regulates agl1)
PMID:24224056	GO:0045944	in response to carbon source change from glucose to maltose (comment: CHECK regulates agl1)
PMID:24239120	PBO:0094477	(Fig. 3)
PMID:24239120	PBO:0094474	(Fig. S1) (comment: CHECK This is a partial rescue of FYPO:0004307)
PMID:24239120	FYPO:0004307	(Fig. 1)
PMID:24239120	FYPO:0006917	(Fig. S1) ((comment: CHECK This is a rescue of FYPO:0000324)
PMID:24239120	FYPO:0006917	(Fig. S1) ((comment: CHECK This is a rescue of FYPO:0000324)
PMID:24239120	FYPO:0006259	(Fig. 1)
PMID:24239120	FYPO:0000324	(Fig. S1) (comment: The authors define it as prolongued prophase-metaphase , but since they use the degradation as cdc13 as a marker it really is anaphase onset that is measured.)
PMID:24239120	FYPO:0000324	(Fig. S1) (comment: The authors define it as prolongued prophase-metaphase , but since they use the degradation as cdc13 as a marker it really is anaphase onset that is measured.)
PMID:24239120	FYPO:0000324	(Fig. S1) (comment: The authors define it as prolongued prophase-metaphase , but since they use the degradation as cdc13 as a marker it really is anaphase onset that is measured.)
PMID:24239120	FYPO:0006259	(Fig. 1)
PMID:24239120	FYPO:0006259	(Fig. 1)
PMID:24239120	FYPO:0006917	(Fig. 2) (comment: CHECK This is a rescue of FYPO:0000324)
PMID:24239120	FYPO:0006259	(Fig. 1)
PMID:24239120	FYPO:0006259	(Fig. 1)
PMID:24239120	FYPO:0004395	(Fig. 1)
PMID:24239120	PBO:0094475	(Fig. 1)
PMID:24239120	PBO:0094474	(Fig. 1)
PMID:24239120	FYPO:0004307	(Fig. 1)
PMID:24239120	PBO:0094476	(Fig. S1) (comment: The authors define it as prolongued prophase-metaphase , but since they use the degradation as cdc13 as a marker it really is anaphase onset that is measured.)
PMID:24239120	FYPO:0006259	(Fig. 2) (comment: CHECK This is a rescue of FYPO:0004395)
PMID:24239120	PBO:0094478	(Fig. 3)
PMID:24239120	FYPO:0007961	(Fig. 4)
PMID:24239120	PBO:0094479	(Fig. 3)
PMID:24239120	PBO:0094480	(Fig. 3)
PMID:24239120	PBO:0094480	(Fig. 3)
PMID:24239120	FYPO:0007959	(Fig. S1)
PMID:24239120	PBO:0094481	(Fig. 4)
PMID:24239120	FYPO:0006259	(Fig. 2) (comment: CHECK This is a rescue of FYPO:0004395)
PMID:24239120	FYPO:0006259	(Fig. 1)
PMID:24239120	FYPO:0007960	(Fig. S1)
PMID:24240238	FYPO:0004744	(comment: experiment introduced otr::ura4+ in either a silenced state (from wild-type cells) or a desilenced state (from clr4delta cells) into poz1delta dcr1delta cells by genetic crosses)
PMID:24240238	FYPO:0002019	(comment: Southern blot to detect telomeric sequence)
PMID:24240238	FYPO:0002687	(comment: Southern blot to detect telomeric sequence)
PMID:24240238	FYPO:0002687	(comment: Southern blot to detect telomeric sequence)
PMID:24240238	FYPO:0004742	(comment: silencing normal as long as heterochromatin assembly can take place normally)
PMID:24240238	FYPO:0002687	(comment: Southern blot to detect telomeric sequence)
PMID:24240238	FYPO:0002019	(comment: Southern blot to detect telomeric sequence)
PMID:24240238	FYPO:0002687	(comment: Southern blot to detect telomeric sequence)
PMID:24240238	FYPO:0002687	(comment: Southern blot to detect telomeric sequence)
PMID:24244528	FYPO:0003526	However, most filaments (99%) bound by -E1 were non-motile while most filaments bound by wild-type Myo2p were motile (Movie S2).
PMID:24244528	PBO:0096789	However, the lower molecular weight form of -E1 failed to accumulate over time following protease addition (Figure 4C), suggesting an altered conformation more sensitive to proteolysis.
PMID:24244528	FYPO:0007603	(comment: CHECK atpase activity assay) However, -E1 motors exhibited relatively low activity under either condition (Figure S1). These experiments performed in the absence of actin suggest that defects in -E1 motors are not specific to actin displacement and motility, and probably reflect a general defect in conformation and function.
PMID:24244528	PBO:0096788	Our data indicates that Rng3p is required to establish active Myo2p motors.The control experiments (where cells were shifted to 37uC at 22hours post-induction) indicated that Rng3p was not essential formaintaining Myo2p motility once an active population of motorshad been synthesized, as previously reported [24]...........Collectively our findings suggest that Rng3p is required to generate an active and stable population of Myo2p motors.
PMID:24247430	GO:0031139	(comment: I think this is real i.e. downregulation of growth to allow differentiation)
PMID:24291789	GO:0003690	(Fig. 2a,b; Extended Data Fig. 2a)
PMID:24291789	GO:0032116	(Fig. 1a)
PMID:24291789	GO:0032116	(Fig. 1a)
PMID:24291789	PBO:0114852	(Fig. 1c,d)
PMID:24291789	GO:0030892	(Fig. 2a,b; Extended Data Fig. 2a)
PMID:24291789	GO:0030892	(Fig. 2a,b; Extended Data Fig. 2a)
PMID:24291789	GO:0030892	(Fig. 2a,b; Extended Data Fig. 2a)
PMID:24291789	GO:0030892	(Fig. 2a,b; Extended Data Fig. 2a)
PMID:24291789	GO:0003690	(Fig. 2a,b; Extended Data Fig. 2a)
PMID:24291789	GO:0003690	(Fig. 2a,b; Extended Data Fig. 2a)
PMID:24291789	GO:0003690	(Fig. 2a,b; Extended Data Fig. 2a)
PMID:24291789	GO:0007064	(Fig. 2E,F; Fig. 3a,b)
PMID:24291789	PBO:0114852	(Fig. 1c,d)
PMID:24291789	GO:0007064	(Fig. 3b), suggesting that cohesin in principle achieves topological loading onto DNA independently of a cohesin loader, albeit inefficiently.
PMID:24291789	GO:0007064	(Fig. 2e) Fig. 2f) Fig. 3a,b).
PMID:24291789	GO:0007064	(Fig. 3b), suggesting that cohesin in principle achieves topological loading onto DNA independently of a cohesin loader, albeit inefficiently.
PMID:24291789	GO:0007064	(Fig. 3b), suggesting that cohesin in principle achieves topological loading onto DNA independently of a cohesin loader, albeit inefficiently.
PMID:24291789	GO:0007064	(Fig. 3b), suggesting that cohesin in principle achieves topological loading onto DNA independently of a cohesin loader, albeit inefficiently.
PMID:24291789	PBO:0114853	(Fig. 4b)
PMID:24297439	GO:0005515	(comment: Two hybrid interaction using Gpa2K270E activated protein with Sck1.)
PMID:24297439	PBO:0120233	(comment: it's a bit indirect, but they show this via consensus site mutations....I think it is borderline ok)
PMID:24297439	GO:0005515	(comment: Two hybrid interaction using Gpa2K270E activated protein with Sck1.)
PMID:24297439	FYPO:0006822	Effect of sck1 deletion to increase cell length in git3 delete cells depends on Gpa2 activity. Otherwise, Sck1 acts in parallel with Pka1 to increase cell length.
PMID:24313451	GO:0101005	(comment: assayed using cell extract, overexpressed protien and synthetic UB conjugate)
PMID:24314397	GO:0030378	(comment: inhibited by α-(hydroxymethyl)serine CHEBI:28187)
PMID:24316795	FYPO:0001124	(comment: moderate overexpression)
PMID:24316795	GO:0010971	Negatively regulated by Pom1 via phosphorylation of C-ter
PMID:24316795	FYPO:0006822	(comment: CONDITION low concentration (<0.25 uM) 3MB-PP1)
PMID:24316795	FYPO:0006822	(comment: CONDITION low concentration (<0.25 uM) 3MB-PP1)
PMID:24316795	FYPO:0006822	(comment: CONDITION high concentration (1 uM) 3MB-PP1)
PMID:24316795	PBO:0107141	(comment: CONDITION low concentration (<0.25 uM) 3MB-PP1)
PMID:24316795	FYPO:0003150	(comment: CONDITION low concentration (<0.25 uM) 3MB-PP1)
PMID:24316795	FYPO:0001018	(comment: CONDITION high concentration (1 uM) 3MB-PP1)
PMID:24316795	FYPO:0003481	(comment: high overexpression)
PMID:24316795	FYPO:0000339	(comment: CONDITION high concentration (1 uM) 3MB-PP1)
PMID:24316795	PBO:0103729	(comment: CONDITION high concentration (1 uM) 3MB-PP1)
PMID:24316795	PBO:0103727	(comment: CHECK Phosphorylates cdr2 at S755 in vitro)
PMID:24316795	GO:0031569	Cdr2 phosphorylated by Pom1 at the CTD negatively regulates its activity
PMID:24316795	PBO:0094966	(comment: same as cdr2-S755A-758A alone)
PMID:24316795	PBO:0094966	(comment: same as cdr2-S755A-758A alone)
PMID:24316795	PBO:0096622	Pom1-as1 protein may preferentially localize to non-growing end.
PMID:24327658	PBO:0096022	(comment: CHECK in vitro kinase assay using recombinant Sre1 aa 1-440)
PMID:24327658	GO:0005515	Binds specifically to active Sre1 transcription factor and not full-length precursor
PMID:24327658	GO:0000122	accelerates degradation of active Sre1 transcription factor
PMID:24327658	GO:0010895	hhp2 deletion increases steady-state ergosterol
PMID:24327658	FYPO:0003251	(comment: Ok as a single mutant despite sre1-N mutant?)
PMID:24327658	PBO:0096021	(comment: CHECK in vitro kinase assay using recombinant Sre1 aa 1-440)
PMID:24327658	PBO:0108902	(comment: CHECK in vitro kinase assay using recombinant Sre1 aa 1-440)
PMID:24344203	PBO:0101640	same as isp7+ overexpression alone
PMID:24344203	PBO:0101640	same as isp7+ overexpression alone
PMID:24344203	PBO:0101636	isp7+ overexpression decreases Gad8's kinase activity towards substrate Fkh2
PMID:24475199	FYPO:0002827	(comment: Expression level up 8 times.)
PMID:24475199	FYPO:0002827	(comment: Expression level up 35 times)
PMID:24475199	FYPO:0002834	(comment: Expression level up 2 times)
PMID:24475199	FYPO:0002827	(comment: Expression level up 22 times)
PMID:24475199	FYPO:0002827	(comment: Expression level up 43 times)
PMID:24475199	FYPO:0002834	(comment: Expression level up 3 times)
PMID:24475199	FYPO:0002834	(comment: Expression level up 2 times)
PMID:24475199	FYPO:0002834	(comment: Expression level up 2.5 times)
PMID:24475199	FYPO:0002834	(comment: Expression level up 2 times)
PMID:24475199	FYPO:0002827	(comment: Expression level up 25 times)
PMID:24475199	FYPO:0002827	(comment: Expression level up 38 times)
PMID:24475199	FYPO:0002827	(comment: Expression level up 23 times)
PMID:24475199	FYPO:0002834	(comment: Expression level up 2 times)
PMID:24475199	FYPO:0002827	(comment: Expression level up 31 times)
PMID:24477934	FYPO:0005781	(Fig. S4a)
PMID:24477934	PBO:0096319	(Fig. S4a)
PMID:24477934	PBO:0096319	(Fig. S4a)
PMID:24477934	PBO:0096319	(Fig. S4a)
PMID:24477934	PBO:0096319	(Fig. S4a)
PMID:24477934	PBO:0096319	(Fig. S4a)
PMID:24477934	PBO:0096319	(Fig. S4a)
PMID:24477934	PBO:0116189	A complex between the checkpoint proteins Mad1 and Mad2 provides a platform for Mad2:Mad2 dimerization at unattached kinetochores, which enables Mad2 to delay anaphase. Here, we show that mutations in Bub1 and within the Mad1 C-terminal domain impair the kinetochore localization of Mad1:Mad2 and abrogate checkpoint activity. Artificial kinetochore recruitment of Mad1 in these mutants co-recruits Mad2; however, the checkpoint remains non-functional. We identify specific mutations within the C-terminal head of Mad1 that impair checkpoint activity without affecting the kinetochore localization of Bub1, Mad1 or Mad2. Hence, Mad1 potentially in conjunction with Bub1 has a crucial role in checkpoint signalling in addition to presenting Mad2.
PMID:24477934	PBO:0104995	(Fig. 3F)
PMID:24477934	FYPO:0004318	(Fig 2D and E) (comment: (mad1 localized did not rescue)
PMID:24477934	FYPO:0004318	(Figure 2B)
PMID:24477934	PBO:0104994	(Figure 1H)
PMID:24477934	PBO:0104993	(Figure 1H)
PMID:24477934	PBO:0095479	(Figure 1H)
PMID:24477934	PBO:0104992	(Fig. 1A, C-D)
PMID:24477934	PBO:0104992	(Fig. 1A, C-E)
PMID:24477934	PBO:0095479	(Fig. S1A and D)
PMID:24477934	PBO:0104991	(Fig. S2F)
PMID:24477934	PBO:0104990	(Fig. S2F)
PMID:24477934	FYPO:0003762	(Fig. S4a)
PMID:24477934	FYPO:0003762	(Fig. S4a)
PMID:24477934	PBO:0096319	(Fig. S2C,D,E)
PMID:24477934	PBO:0104989	(Fig. S2C,D,E)
PMID:24477934	PBO:0104982	(Fig. S2C,D,E)
PMID:24477934	PBO:0104982	(Fig. S2C,D,E)
PMID:24477934	FYPO:0004318	(Fig. S2F)
PMID:24477934	FYPO:0004318	(Fig. S2F)
PMID:24477934	PBO:0104988	(Fig. S1I)
PMID:24477934	PBO:0104987	(Fig. S1I)
PMID:24477934	PBO:0104986	(Fig. S1I)
PMID:24477934	PBO:0104985	(Fig. S1B)
PMID:24477934	PBO:0096320	(Fig. S1B)
PMID:24477934	FYPO:0003762	(Fig. S4a)
PMID:24477934	FYPO:0003762	(Fig. S4a)
PMID:24477934	PBO:0095474	(Fig. 3D)
PMID:24477934	PBO:0095474	(Fig. 3D)
PMID:24477934	FYPO:0003762	(Fig. S4a)
PMID:24477934	PBO:0104984	(Fig. 3B,C)
PMID:24477934	PBO:0104984	(Fig. 3B,C)
PMID:24477934	PBO:0104982	(Fig. 1I-L)
PMID:24477934	PBO:0104983	(Fig. 1I-L)
PMID:24477934	FYPO:0004318	(Fig. 1I-L)
PMID:24477934	PBO:0104982	(Fig. 1 C,D)
PMID:24477934	PBO:0104982	(Fig. S4A)
PMID:24477934	PBO:0104982	(Fig. S4A)
PMID:24477934	PBO:0096316	(Fig. 1A, C-E)
PMID:24477934	PBO:0096315	(Fig. 1A, C-E)
PMID:24477934	FYPO:0004318	(Fig. 1F)
PMID:24477934	FYPO:0004318	(Fig. 1F)
PMID:24477934	FYPO:0004318	(Fig. 1F)
PMID:24477934	FYPO:0004318	(Fig 1F)
PMID:24477934	FYPO:0005781	(Fig. S4a)
PMID:24477934	FYPO:0003762	(Fig. S4a)
PMID:24477934	PBO:0096319	(Fig. S4a)
PMID:24477934	FYPO:0005781	(Fig. S4a)
PMID:24478458	PBO:0108730	(comment: phosphorylates rgf1 during HU response, to maintain of protein lcoation in nucleus)
PMID:24493644	PBO:0096066	(Fig. 5)
PMID:24498240	PBO:0103053	As seen in Figure 1E, rho2D cells showed a partial VIC phenotype in medium supplemented with 0.2 M MgCl2 and became VIC negative in the presence of 0.3 M MgCl2.
PMID:24498240	PBO:0103053	As seen in Figure 1E, rho2D cells showed a partial VIC phenotype in medium supplemented with 0.2 M MgCl2 and became VIC negative in the presence of 0.3 M MgCl2.
PMID:24498240	PBO:0113635	However, a careful examination of these experiments revealed that Pmk1 basal phosphorylation in rho1-596 rho2D cells was actually lower than in rho2D cells, and this difference was statistically significant (P,0.04; Figure 1C). On the contrary, basal Pmk1 activity was nearly identical in pck2D and rho1-596 pck2D cells (Figure 1D), strongly suggesting that enhanced Pmk1 activation in rho1-596 cells is transmitted to the MAPK cascade mainly through Pck2.
PMID:24498240	PBO:0113634	Rho1 GTPase might modulate the activity Pmk1 by acting upstream of Pck2 because it has been described that overexpression of wild type or a constitutively active allele of rho1+ (G15V mutant) induced a marked hyperactivation of Pmk1 (Figure 1B
PMID:24498240	PBO:0113981	Taken as a whole, these results support that Pck1 might act as a Rho1 target during signal transmission to the CIP, although its role within this pathway seems restricted to specific situations.
PMID:24498240	PBO:0113632	Also, Pmk1 hyperactivation triggered by rho2+ overexpression is fully attenuated in mutants lacking Pck2 (Figure 1A).
PMID:24498240	PBO:0113631	Also, Pmk1 hyperactivation triggered by rho2+ overexpression is fully attenuated in mutants lacking Pck2 (Figure 1A).
PMID:24498240	GO:1903139	In this study we show for the first time that Rho1 and Pck1 are true activators of this signalling cascade in addition to Rho2 and Pck2 under specific environmental contexts
PMID:24498240	PBO:0113980	In this study we show for the first time that Rho1 and Pck1 are true activators of this signalling cascade in addition to Rho2 and Pck2 under specific environmental contexts
PMID:24498240	PBO:0095577	Importantly, the VIC phenotype in rho1-596 rho2D double mutant was markedly enhanced as compared to that shown by rho2D cells (Figure 1E), which is in good agreement with basal Pmk1 phosphorylation data (Figure 1C).
PMID:24498240	PBO:0113636	As expected, both wild type and rho1- 596 cells were VIC negative under any condition (Figure 1D).
PMID:24498240	GO:1903139	Previous work demonstrated that Rho2 GTPase, one of the six Rho GTPases found in S. pombe proteome (Rho1 to Rho5, and Cdc42) which controls cell polarity and cell wall biosynthesis, is a positive regulator operating upstream of the CIP [13,14]
PMID:24498240	PBO:0113640	(comment: note in Figure 3B the robust growth of rho1-596 rho2D pck1D cells in medium supplemented with 0.2 M MgCl2 as compared to rho2D pck1D cells).
PMID:24498240	PBO:0113639	(Figure 3A) indicates that deletion of rho2+ gene alleviated the increased Pmk1 basal phosphorylation present in pck1D cells.
PMID:24498240	PBO:0113635	(Figure 3A) indicates that deletion of rho2+ gene alleviated the increased Pmk1 basal phosphorylation present in pck1D cells.
PMID:24498240	PBO:0113634	(Figure 3A) indicates that deletion of rho2+ gene alleviated the increased Pmk1 basal phosphorylation present in pck1D cells.
PMID:24498240	PBO:0113639	However, in comparison to either control or rho2D and rho1-596 single mutant cells, MAPK activation was severely compromised in cells from the rho2D rho1-596 double mutant treated with Caspofungin (Figure 2C).
PMID:24498240	PBO:0113638	(comment: CHECK in response to oxidative stress) As shown in Figure 2B, Pmk1 activation in rho2D cells subjected to oxidative stress was not affected by simultaneous expression of the rho1-596 hypoactive allele.
PMID:24498240	PBO:0113638	(comment: CHECK in response to oxidative stress) On the contrary, MAPK activation triggered by oxidative (hydrogen peroxide) and cell wall (Caspofungin) stresses is only partially dependent on this GTPase (Figure 2B and C)
PMID:24498240	PBO:0113637	Pmk1 activation induced by hypo- and hyper-osmotic stress totally depends upon the signaling mediated by Rho2 (Figure 2A)
PMID:24498240	PBO:0113981	As a whole, these results sustain that Rho1 GTPase is a true positive regulator of the cell integrity pathway which operates during vegetative growth in an alternative fashion to Rho2 and using Pck2 as a main target.
PMID:24514900	PBO:0105619	(comment: CHECK low expressivity)
PMID:24514900	GO:0032220	Required for phosphatydil serine reorganization at the inner leaflet of plasma membrande during cell fusion
PMID:24514900	PBO:0102728	(comment: CHECK high penetrance)
PMID:24521463	FYPO:0002060	(comment: decreased cell pop is not a child of this term)
PMID:24554432	GO:0030010	(comment: CHECK sufficient to trigger cell shape change when targeted to cell sides by fusion with Cdr2; tea1/pom1 double mutant phenotype shows that Tea4 role is independent of Pom1)
PMID:24554432	GO:2000784	(comment: CHECK sufficient to trigger cell shape change when targeted to cell sides by fusion with Cdr2)
PMID:24554432	GO:2000114	(comment: CHECK sufficient to trigger cell shape change when targeted to cell sides by fusion with Cdr2)
PMID:24554432	GO:2000114	(comment: CHECK necessary to trigger cell shape change upon Tea4 targeting to cell sides by fusion with Cdr2)
PMID:24554432	GO:2000784	(comment: CHECK necessary to trigger cell shape change upon Tea4 targeting to cell sides by fusion with Cdr2)
PMID:24569997	PBO:0105209	(comment: CHECK *******during copper excess******) fig2
PMID:24569997	PBO:0025347	Observed at this location during spore maturation by indirect immunofluorescence
PMID:24569997	PBO:0105211	(Fig. 2)
PMID:24569997	PBO:0105204	(Figure 5B)
PMID:24569997	PBO:0105206	(fig 1)
PMID:24569997	PBO:0105207	(fig 1)
PMID:24569997	PBO:0105208	(fig 1)
PMID:24569997	PBO:0105209	(comment: CHECK *******during copper excess******) fig2
PMID:24569997	PBO:0105204	(Figure 5B)
PMID:24583014	PBO:0105367	(Fig. 3A, 3B, 3C) securin abnormally stabilized during anaphase
PMID:24583014	PBO:0105365	(Fig. 1B)
PMID:24583014	PBO:0105364	(Fig. 1A)
PMID:24583014	PBO:0105363	(Fig. 1A)
PMID:24583014	FYPO:0000274	(Fig. S1B, S1C)
PMID:24583014	FYPO:0004301	(Figure S1B)
PMID:24583014	PBO:0105362	(Fig. 1A) indicating that CDK1 activity remained high
PMID:24583014	FYPO:0006646	(Fig. 2B, 2C)
PMID:24583014	FYPO:0005684	(Fig. 2B, 2C)
PMID:24583014	FYPO:0007403	(Fig. 2A) (comment: complex seen here in anaphase although it normally forms in prometaphase and disassembles before anaphase)
PMID:24583014	PBO:0101464	(Fig. 1D, 1E)
PMID:24583014	PBO:0105366	(Fig. 1A)
PMID:24637836	GO:0005737	Fluorescence microscopy of Sec13 tagged with GFP at either its N-terminal or C-terminal end.
PMID:24637836	PBO:0093579	(comment: CHECK weak sensitivity)
PMID:24637836	PBO:0093579	(comment: CHECK weak sensitivity)
PMID:24637836	FYPO:0001355	Our strains expressing GFP-tagged nucleoporins were all viable, but four of them (spNup45-GFP, spNup184-GFP, GFP-spRae1, and spNup189n-GFP) showed growth deficiencies
PMID:24637836	PBO:0093563	(comment: CHECK weak sensitivity)
PMID:24637836	PBO:0093563	(comment: CHECK weak sensitivity)
PMID:24637836	PBO:0093563	(comment: CHECK weak sensitivity)
PMID:24652833	GO:0009262	(comment: it affects suc22 binding to cdc22. There is no evidence thta it is involved in catabolism and I dont think I can make a MF from it.)
PMID:24652833	PBO:0102211	(comment: no MF possible)
PMID:24662054	PBO:0097229	(comment: binds both DNA and histone. Not sure if the H3 preference is an artefact of in vitro system)
PMID:24662054	GO:0140750	(comment: binds both DNA and histone. Not sure if the H3 preference is an artefact of in vitro system)
PMID:24663817	PBO:0093581	(Fig. 1D)
PMID:24663817	PBO:0100323	(comment: CHECK phosphorylated rad9)
PMID:24663817	MOD:00696	(comment: CHECK affected by rad4)
PMID:24663817	PBO:0100321	(Fig. 3a,b)
PMID:24663817	PBO:0100320	(Fig. 3a,b) (comment: CHECK cds1-T11)
PMID:24663817	PBO:0100319	(Fig. 3a, b)
PMID:24663817	PBO:0100318	(Fig. 5A and B)
PMID:24663817	PBO:0100317	Consistent with the previous report [58], the interaction between Rad9 and Rad4 was dependent on Rad9 phosphorylation because the phosphorylation site mutant Rad9-T412A could not pull-down Rad4 (Fig. 5A, first lane on the left) and the interaction between Rad9 and Rad4 was sensitive to l-phosphatase treatment (Fig. S5A).
PMID:24663817	PBO:0100318	C13Y-K56R mutation abolished the interaction with Crb2 (Fig. 5C), not Rad9 (Fig. 5A and B).
PMID:24663817	PBO:0100317	E368K mutation abolished the binding to Rad9 as previously reported [47] (Fig. 5A and B)
PMID:24663817	PBO:0100316	C13Y-K56R mutation abolished the interaction with Crb2 (Fig. 5C), not Rad9 (Fig. 5A and B).
PMID:24663817	PBO:0093581	(Fig. 1D)
PMID:24663817	PBO:0100313	C13Y and K56R mutations completely eliminated the phosphorylation of Chk1 in MMS-treated cells (Fig. 3A)
PMID:24663817	PBO:0100314	C13Y and K56R mutations completely eliminated the phosphorylation of Chk1 in MMS-treated cells (Fig. 3A)
PMID:24663817	PBO:0100314	C13Y and K56R mutations completely eliminated the phosphorylation of Chk1 in MMS-treated cells (Fig. 3A)The slight decrease in Cds1 phosphorylation may be caused indirectly by a minor defect in DNA replication
PMID:24663817	PBO:0100315	The C13Y and K56R mutations abolished the scaffolding function of Rad4 required for the activation of Chk1 but not Rad3
PMID:24663817	PBO:0093617	(Fig. 3)
PMID:24663817	PBO:0093617	(Fig. 3)
PMID:24663817	PBO:0093580	(Fig. 3D)
PMID:24663817	PBO:0093580	(Fig. 3D)
PMID:24663817	PBO:0093616	(Fig. 3D)
PMID:24663817	PBO:0093616	(Fig. 3D)
PMID:24663817	FYPO:0000725	Interestingly, the DC mutant with the deletion of the whole C-terminus between amino acid 498 and 648 was resistant to HU and MMS almost like the wild type cells (Fig. 1D and 2B). The only difference we could readily find for the DC mutant was that the protein level was higher than in the wild type cells (Fig. 2C), suggesting that the C-terminus may not contain a robust AAD (see below).
PMID:24663817	PBO:0093617	(Fig. 1D, Fig. 2B)
PMID:24663817	PBO:0093617	(Fig. 1D,2B)
PMID:24663817	PBO:0093617	(Fig. 1D)
PMID:24663817	FYPO:0002061	We found that combinations of the previously reported E368K mutation [47] with K56R or F303S were lethal suggesting a defect in DNA replication.
PMID:24663817	FYPO:0002061	We found that combinations of the previously reported E368K mutation [47] with K56R or F303S were lethal suggesting a defect in DNA replication.
PMID:24663817	PBO:0093617	(Fig. 1D, Fig. 2B)
PMID:24663817	PBO:0093581	(Fig. 1D, Fig. 2B)
PMID:24663817	PBO:0093581	(Fig. 1D,2B)
PMID:24663817	PBO:0093581	(Fig. 1D,2B)
PMID:24663817	PBO:0100313	C13Y and K56R mutations completely eliminated the phosphorylation of Chk1 in MMS-treated cells (Fig. 3A)
PMID:24696293	FYPO:0000087	supp fig?
PMID:24710126	FYPO:0003410	(comment: CHECK convert to double mutant (cnp1 overexpression))
PMID:24710126	FYPO:0005071	(comment: central core)
PMID:24710126	FYPO:0005071	(comment: central core)
PMID:24713849	PBO:0094862	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	PBO:0094861	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	PBO:0094862	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	PBO:0095160	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	PBO:0101243	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	PBO:0101245	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	PBO:0095143	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	PBO:0094860	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	PBO:0094859	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	GO:1990477	(comment: Observed in cells undergoing vegetative growth)
PMID:24713849	PBO:0094861	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	PBO:0095143	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	PBO:0094860	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	PBO:0094859	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	GO:1990477	(comment: Observed in cells undergoing vegetative growth)
PMID:24713849	GO:1990477	(comment: Observed in cells undergoing vegetative growth)
PMID:24713849	GO:1990477	(comment: Observed in cells undergoing vegetative growth)
PMID:24713849	GO:1990477	(comment: Observed in cells undergoing vegetative growth)
PMID:24713849	PBO:0101244	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	PBO:0095161	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	GO:1990477	(comment: Observed in cells undergoing vegetative growth)
PMID:24741065	PBO:0097925	tor2 phosphorylates mei2. Phosphorylated mei2 is ubiquitylated which targets it for degradation via the proteasome.
PMID:24741065	PBO:0097921	(comment: CHECK phosphorylation of mei2 targets it for degradation via the proteasome)
PMID:24755092	GO:0010494	Exo2-GFP localizes to stress granules
PMID:24755092	GO:0010494	SPAC12G12.09-mCherry localizes to stress granules
PMID:24758716	GO:0019172	(comment: major)
PMID:24758716	GO:0019172	(comment: minor Hsp3106 has a lower in vitro glyoxalase III activity than Hsp3101 and Hsp3102)
PMID:24758716	GO:0019172	(comment: major)
PMID:24768994	GO:0005515	(Figure 2B)
PMID:24768994	FYPO:0000684	(Figure 5)
PMID:24768994	FYPO:0001407	(Figure 5)
PMID:24768994	GO:0005515	(Figure 2B)
PMID:24768994	GO:0005737	(Figure 3)
PMID:24768994	GO:0005634	(Figure 3)
PMID:24768994	FYPO:0000684	(Figure 5)
PMID:24768994	GO:0005635	(Figure 2A)
PMID:24768994	PBO:0104274	(Figure 2C)
PMID:24774534	FYPO:0002060	(Fig. 6)
PMID:24774534	FYPO:0002061	(Fig. 6)
PMID:24774534	FYPO:0002060	(Fig. 6)
PMID:24774534	FYPO:0002060	(Fig. 6)
PMID:24774534	FYPO:0002061	(Fig. 6)
PMID:24774534	FYPO:0002060	(Fig. 6)
PMID:24774534	FYPO:0002060	(Fig. 6)
PMID:24774534	FYPO:0002060	(Fig. 6)
PMID:24774534	FYPO:0002060	(Fig. 6)
PMID:24774534	FYPO:0002060	(Fig. 6)
PMID:24774534	FYPO:0002060	(Fig. 6)
PMID:24787148	PBO:0103362	(comment: ubiquitin monmomer inhibits sst2)
PMID:24790093	PBO:0108213	(comment: Yeast two hybrid)
PMID:24790095	PBO:0024047	(comment: CHECK mitotic interphase)
PMID:24790095	GO:0110085	(comment: CHECK exists_during( metaphase? anaphase A????))
PMID:24790095	GO:0110085	(comment: CHECK exists_during( metaphase? anaphase A????))
PMID:24806815	GO:0035861	This localisation requires phosphorylated histone H2A.
PMID:24806815	PBO:0111551	Mdb1 binds to Hta1 phosphorylated on Ser-129. (comment: CHECK PR:000027566 = H2A phosphorylated on S129)
PMID:24815688	FYPO:0003743	"(comment: CHECK transferres from term suggestion to allow approval decreased growth under low-glucose conditions Definition: ""decreased growth under low-glucose conditions"" is an ""decreased cell population growth"" that occurs specifically on media supplied with a lower concentration of glucose than regular media. ditto all the others)"
PMID:24818994	GO:0016929	(Figure 1A)
PMID:24818994	PBO:0099111	(Figure 1A)
PMID:24818994	FYPO:0002061	(Figure 1D)
PMID:24818994	GO:0070139	(Figure 1A)
PMID:24818994	PBO:0101445	(Figures 3 and 6)
PMID:24818994	FYPO:0000104	(Figure 1D)
PMID:24818994	PBO:0101445	(Figures 3 and 6)
PMID:24818994	GO:0005737	(comment: minor)
PMID:24818994	FYPO:0000088	(Figure 1D)
PMID:24818994	PBO:0101444	(Figure 5A)
PMID:24818994	GO:0005634	(Figures 3 and 6)
PMID:24818994	PBO:0101443	(Figure 1A)
PMID:24818994	GO:0005737	(Figures 3 and 6)
PMID:24831008	PBO:0099224	(Figure 7) the goal of the experiments in this figure is to map the minimal region of loz1 that is required for zinc-responsiveness by generating gene fusion with MtfA, a transcription factor from Aspergillus nidulans that contains a double zinc finger domain with high similarity to Loz1 from S. pombe, but contains no other similarity. When expressed in S. pombe this gene fusion was regulated by zinc, suggesting that the region necessary for zinc responsiveness in S. pombe, maps to the zinc finger domains and an upstream accessory domain
PMID:24831008	PBO:0099222	(Fig. 2)
PMID:24831008	PBO:0099222	(Fig. 2)
PMID:24831008	PBO:0099222	(Fig. 2)
PMID:24831008	PBO:0099222	(Fig. 2)
PMID:24831008	PBO:0099223	(Fig. 4)
PMID:24831008	PBO:0099223	(Fig. 4)
PMID:24831008	PBO:0099224	(Fig. 1)
PMID:24831008	PBO:0099224	(Fig. 1)
PMID:24831008	PBO:0099225	(Fig. 4g)
PMID:24831008	PBO:0099226	(Fig. 2)
PMID:24831008	PBO:0099228	RNA transcript expression is increased during the stress response to zinc ions, but the increase is less than the transcript levels seen with full de-repression
PMID:24831008	PBO:0099228	RNA transcript expression is increased during the stress response to zinc ions, but the increase is less than the transcript levels seen with full de-repression
PMID:24831008	PBO:0099228	RNA transcript expression is increased during the stress response to zinc ions, but the increase is less than the transcript levels seen with full de-repression
PMID:24831008	PBO:0099231	(Figure 7) the goal of the experiments in this figure is to map the minimal region of loz1 that is required for zinc-responsiveness by generating gene fusion with MtfA, a transcription factor from Aspergillus nidulans that contains a double zinc finger domain with high similarity to Loz1 from S. pombe, but contains no other similarity. When expressed in S. pombe this gene fusion was regulated by zinc, suggesting that the region necessary for zinc responsiveness in S. pombe, maps to the zinc finger domains
PMID:24831008	PBO:0099227	(Figure 7) the goal of the experiments in this figure is to map the minimal region of loz1 that is required for zinc-responsiveness by generating gene fusion with MtfA, a transcription factor from Aspergillus nidulans that contains a double zinc finger domain with high similarity to Loz1 from S. pombe, but contains no other similarity. When expressed in S. pombe this gene fusion was regulated by zinc, suggesting that the region necessary for zinc responsiveness in S. pombe, maps to the zinc finger domains and an upstream accessory domain
PMID:24838944	PBO:0119938	(Fig. 7C)
PMID:24838944	PBO:0119938	(Fig. 7B)
PMID:24838944	PBO:0092202	(Fig. 7A)
PMID:24838944	PBO:0119937	(Fig. 6C)
PMID:24838944	PBO:0119936	(Fig. 6B)
PMID:24838944	PBO:0119935	(Fig. 6A)
PMID:24838944	PBO:0119934	(Fig. 5C)
PMID:24838944	PBO:0119934	(Fig. 5D)
PMID:24838944	PBO:0119934	(Fig. 4E)
PMID:24838944	PBO:0119933	(Fig. 4D)
PMID:24838944	PBO:0092202	(Fig. 4C)
PMID:24838944	PBO:0092202	(Fig. 4B)
PMID:24838944	PBO:0092202	(Fig. 4A)
PMID:24838944	PBO:0119932	(Fig. 3B)
PMID:24838944	PBO:0092202	(Fig. 3A)
PMID:24838944	PBO:0119930	(Fig. 2G)
PMID:24838944	PBO:0119931	(Fig. 2F)
PMID:24838944	PBO:0119930	(Fig. 2F)
PMID:24838944	PBO:0114366	(Fig. 2E)
PMID:24838944	PBO:0114354	(Fig. S1D)
PMID:24838944	PBO:0114365	(Fig. 2E)
PMID:24838944	PBO:0119929	(Fig. 2C)
PMID:24838944	PBO:0119928	(Fig. 2C)
PMID:24838944	PBO:0114365	(Fig. 2A)
PMID:24838944	PBO:0119927	(Fig. 2A)
PMID:24838944	PBO:0119926	(Fig. 1D)
PMID:24838944	PBO:0023321	(Fig. 1D)
PMID:24838944	PBO:0035493	(Fig. 1D)
PMID:24838944	PBO:0119926	(Fig. 1C)
PMID:24838944	PBO:0023321	(Fig. 1C)
PMID:24838944	PBO:0035493	(Fig. 1C)
PMID:24838944	PBO:0114354	(Fig. 1A,1 B)
PMID:24847916	FYPO:0003928	The phenotype is assessed by the high-throughput sequencing.
PMID:24876389	PBO:0096275	(comment: CHECK internalization abolished)
PMID:24876389	PBO:0096275	(comment: CHECK internalization abolished)
PMID:24876389	PBO:0096283	(comment: CHECK have guessed at deleted residues)
PMID:24876389	PBO:0096275	(comment: CHECK internalization abolished)
PMID:24876389	PBO:0096271	(comment: ubiquitinated probably at K263)
PMID:24876389	PBO:0096275	(comment: CHECK internalization abolished)
PMID:24920274	PBO:0104608	(comment: at sme2 locus -one of several exosome foci in nucleus during vegetative growth)
PMID:24920274	PBO:0104594	(Figure S1)
PMID:24920274	PBO:0104603	(Figure 3)
PMID:24920274	PBO:0104602	(Figure 3)
PMID:24920274	PBO:0104603	(Figure 3)
PMID:24920274	PBO:0104602	(Figure 3)
PMID:24920274	PBO:0094908	(comment: CHECK abnormal RNA localization to chromatin)
PMID:24920274	PBO:0095590	(Figure S1)
PMID:24920274	PBO:0104600	(Figure S1)
PMID:24920274	FYPO:0000583	(Figure S1)
PMID:24920274	FYPO:0000583	(Figure S1)
PMID:24920274	PBO:0104597	(Figure S1)
PMID:24920274	PBO:0104596	(Figure S1)
PMID:24920274	PBO:0104595	(Figure S1)
PMID:24920274	PBO:0104608	(comment: at sme2 locus -one of several exosome foci in nucleus during vegetative growth)
PMID:24920274	PBO:0104599	(Figure S1)
PMID:24920274	PBO:0104598	(Figure S1)
PMID:24920274	PBO:0104597	(Figure S1)
PMID:24920274	PBO:0104596	(Figure S1)
PMID:24920274	PBO:0104595	(Figure S1)
PMID:24920274	PBO:0104594	(Figure S1)
PMID:24920823	PBO:0094078	(comment: CHECK medium penetrance)
PMID:24920823	PBO:0093476	(comment: CHECK S326, T429, S499: added by cyclin-dependent kinase (Cdk1))
PMID:24920823	PBO:0093476	(comment: CHECK S326, T429, S499: added by cyclin-dependent kinase (Cdk1))
PMID:24920823	PBO:0093475	(comment: CHECK S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1))
PMID:24920823	PBO:0093475	(comment: CHECK S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1))
PMID:24920823	PBO:0093475	(comment: CHECK S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1))
PMID:24920823	PBO:0093475	(comment: CHECK S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1))
PMID:24920823	GO:0031031	(comment: CHECK Term name: supports establishment of SIN asymmetry Definition: characterized by asymmetric localization of the SIN initiator kinase Cdc7 in anaphase)
PMID:24920823	PBO:0113865	(comment: CHECK affecting Cdc7)
PMID:24920823	PBO:0103495	(comment: CHECK targets Byr4 at S248A, S326A, T412A, T429A, S499A, T502A, S533A, results in Byr4 removal from metaphase spindle pole bodies)
PMID:24920823	PBO:0103496	(comment: CHECK Cdk1-dependent, Cdk1 non-phosphorylatable Byr4 localizes to one or both SPBs in >90% of metaphase cells)
PMID:24920823	PBO:0019669	(comment: CHECK low penetrance)
PMID:24920823	FYPO:0004562	results from collapse of actomyosin contractile ring
PMID:24920823	PBO:0019671	(comment: CHECK anaphase B)
PMID:24925530	FYPO:0003107	starts with longer telomeres than wild type, which then shorten
PMID:24928430	FYPO:0006103	(Fig. 4) (comment: CHECK minor rescue)
PMID:24928430	FYPO:0009001	(Fig. 3) (comment: CHECK minor rescue)
PMID:24928430	FYPO:0009001	(Fig. 3) (comment: CHECK minor rescue)
PMID:24928430	FYPO:0008008	(Fig. 1)
PMID:24928430	FYPO:0006103	(Fig. 3) (comment: CHECK minor rescue)
PMID:24928430	FYPO:0006103	(Fig. 3) (comment: CHECK minor rescue)
PMID:24928430	FYPO:0009001	(Fig. 3)
PMID:24928430	FYPO:0009000	(Fig. 1)
PMID:24928430	FYPO:0000899	(Fig. 2)
PMID:24928430	FYPO:0006103	(Fig. 4) (comment: CHECK minor rescue)
PMID:24928430	FYPO:0006103	(Fig. 3)
PMID:24928510	PBO:0106579	(comment: CHECK protein phosphorylation assayed in vitro)
PMID:24928510	PBO:0106579	(comment: CHECK protein phosphorylation assayed in vitro)
PMID:24928510	PBO:0106580	(comment: CHECK protein phosphorylation assayed in vitro)
PMID:24928510	PBO:0106579	(comment: CHECK protein phosphorylation assayed in vitro)
PMID:24928510	PBO:0096003	(comment: CHECK Phosphorylation assayed in vitro)
PMID:24928510	PBO:0106582	(comment: CHECK protein phosphorylation assayed in vitro)
PMID:24928510	PBO:0106563	(comment: CHECK protein phosphorylation assayed in vitro)
PMID:24928510	PBO:0096003	(comment: CHECK Phosphorylation assayed in vitro)
PMID:24928510	PBO:0101351	(comment: CHECK Phosphorylation assayed in vitro)
PMID:24928510	PBO:0096003	(comment: CHECK Phosphorylation assayed in vitro)
PMID:24928510	PBO:0106561	(comment: CHECK Protein phosphorylation assayed in vitro)
PMID:24928510	PBO:0106561	(comment: CHECK Protein phosphorylation assayed in vitro)
PMID:24928510	PBO:0096003	(comment: CHECK Phosphorylation assayed in vitro)
PMID:24928510	PBO:0096003	(comment: CHECK Phosphorylation assayed in vitro)
PMID:24928510	PBO:0096003	(comment: CHECK protein phosphorylation assayed in vitro)
PMID:24928510	PBO:0106563	(comment: CHECK protein phosphorylation assayed in vitro)
PMID:24928510	PBO:0096003	(comment: CHECK protein phosphorylation assayed in vitro)
PMID:24936793	GO:0071218	(comment: also inferrable (IC) from GO:0051787)
PMID:24939935	PBO:0111611	We report crystal structures of Pce1 bound to Pol2 CTD and Spt5 CTD ligands. Key findings are that (1) the CTDs of Pol2 and Spt5 interact with completely distinct sites on the NTase and OB domains of the fission yeast GTase, respectively, and (2) whereas the interface of GTase with the Pol2 CTD is dependent on Ser5 phosphorylation, GTase binding to Spt5 CTD is antagonized by Thr1 phosphorylation.
PMID:24939935	PBO:0093560	(Fig. 4D)
PMID:24939935	FYPO:0004481	(Fig. 4D)
PMID:24939935	PBO:0093557	(Fig. 1D)
PMID:24939935	PBO:0093558	(Fig. 1D)
PMID:24939935	PBO:0093561	(Fig. 1D)
PMID:24939935	PBO:0093559	(Fig. 1D)
PMID:24939935	PBO:0093558	(Fig. 1D)
PMID:24939935	FYPO:0002061	(Fig. 1D)
PMID:24939935	FYPO:0002061	(Fig. 1D)
PMID:24939935	FYPO:0002061	(Fig. 1D)
PMID:24939935	FYPO:0008181	(Fig. 1G)
PMID:24939935	FYPO:0008181	(Fig. 1G)
PMID:24939935	FYPO:0008181	(Fig. 1G)
PMID:24939935	FYPO:0008181	(Fig. 1G)
PMID:24939935	FYPO:0008181	(Fig. 1G)
PMID:24939935	PBO:0093561	(Fig. 4D)
PMID:24939935	PBO:0093557	(Fig. 4D)
PMID:24939935	FYPO:0008181	(Fig. 1G)
PMID:24939935	PBO:0093561	(Fig. 1D)
PMID:24939935	PBO:0093558	(Fig. 1D)
PMID:24939935	PBO:0093557	(Fig. 1D)
PMID:24939935	PBO:0093556	(Fig. 1D)
PMID:24939935	PBO:0111611	We report crystal structures of Pce1 bound to Pol2 CTD and Spt5 CTD ligands. Key findings are that (1) the CTDs of Pol2 and Spt5 interact with completely distinct sites on the NTase and OB domains of the fission yeast GTase, respectively, and (2) whereas the interface of GTase with the Pol2 CTD is dependent on Ser5 phosphorylation, GTase binding to Spt5 CTD is antagonized by Thr1 phosphorylation.
PMID:24939935	FYPO:0008182	(Fig. 4E)
PMID:24939935	FYPO:0002061	(Fig. 4D)
PMID:24939935	FYPO:0002061	(Fig. 4D)
PMID:24939935	FYPO:0002061	(Fig. 4D)
PMID:24945319	GO:0005847	(comment: I don't really know how to do this: I would like to say that SPAC824.04, Ppn1 and Dis2 are part of a protein module associated with the CPF. We have named this module the DPS module. Lack of this module does not affect the formation of the core CPF (all other CPF sub-units remain associated as a complex). )
PMID:24945319	GO:0005847	(comment: I don't really know how to do this: I would like to say that SPAC824.04, Ppn1 and Dis2 are part of a protein module associated with the CPF. We have named this module the DPS module. Lack of this module does not affect the formation of the core CPF (all other CPF sub-units remain associated as a complex). )
PMID:24945319	GO:0005847	(comment: I don't really know how to do this: I would like to say that SPAC824.04, Ppn1 and Dis2 are part of a protein module associated with the CPF. We have named this module the DPS module. Lack of this module does not affect the formation of the core CPF (all other CPF sub-units remain associated as a complex). )
PMID:24947517	PBO:0098141	(Fig. 1F)
PMID:24947517	PBO:0092529	(Fig. 4A)
PMID:24947517	PBO:0098145	(Fig. 3F)
PMID:24947517	PBO:0098144	Data not shown
PMID:24947517	PBO:0098143	Data not shown
PMID:24947517	PBO:0098142	(Figure 3C)
PMID:24947517	PBO:0098142	(Figure 3C)
PMID:24947517	PBO:0019669	(Fig. 1F)
PMID:24947517	PBO:0035615	(Fig. 1F)
PMID:24947517	PBO:0097059	(Fig. 1F)
PMID:24947517	PBO:0098140	(Fig. 1E)
PMID:24947517	PBO:0098140	(Fig. 1E)
PMID:24947517	FYPO:0000673	(Fig. 1D)
PMID:24947517	FYPO:0005628	(Fig. 1D) (comment: decreased rate of cell separation)
PMID:24947517	FYPO:0000650	(Fig. 1C)
PMID:24947517	FYPO:0001315	(Fig. 1B)
PMID:24947517	FYPO:0001357	(Fig. 1B)
PMID:24947517	FYPO:0001357	(Fig. 1B)
PMID:24947517	PBO:0098149	(Fig. 4A)
PMID:24947517	GO:0005515	(Fig. 4C, 4D, 4E)
PMID:24947517	GO:0005886	(Fig. 5A)
PMID:24947517	PBO:0098150	(Fig. 5A)
PMID:24947517	PBO:0098151	(Fig. 5B)
PMID:24947517	FYPO:0002061	(Fig. 6A)
PMID:24947517	FYPO:0002061	(Fig. 6A)
PMID:24947517	FYPO:0002061	(Fig. 6B)
PMID:24947517	FYPO:0002060	(Fig. 6B)
PMID:24947517	FYPO:0002060	(Fig. 6B)
PMID:24947517	PBO:0098152	(Fig. 6B)
PMID:24947517	PBO:0098153	(Fig. 6B)
PMID:24947517	PBO:0098154	(Fig. 6B)
PMID:24947517	FYPO:0002061	(Fig. 6C)
PMID:24947517	PBO:0095634	(Fig. 6C, 6D)
PMID:24947517	PBO:0098155	(Fig. 6D)
PMID:24947517	GO:0016192	(Fig. 6D)
PMID:24947517	GO:0032153	(Fig. 5A)
PMID:24947517	PBO:0035611	(Fig. 3A)
PMID:24947517	PBO:0098148	(Fig. 4A)
PMID:24947517	PBO:0098148	(Fig. 4A)
PMID:24947517	PBO:0035620	(Fig. 4A)
PMID:24947517	PBO:0098148	(Fig. 4A)
PMID:24947517	PBO:0098147	Data not shown
PMID:24947517	PBO:0098146	Data not shown
PMID:24947517	PBO:0098145	(Fig. 3F)
PMID:24947517	PBO:0098145	(Fig. 3F)
PMID:24954111	FYPO:0006366	(comment: never observed 54/54)
PMID:24954111	PBO:0102133	(Fig. 1) In wild-type cells, monopolar or nonpolar spindles were not observed (Fig. 4C).
PMID:24954111	PBO:0102137	bipolar spindle defects caused by the loss of telomere clustering were rescued by stopping nuclear movement.
PMID:24954111	FYPO:0006366	(comment: never observed 37/37)
PMID:24954111	PBO:0102138	spindle defects caused by the loss of telomere clustering were rescued by stopping nuclear movement.
PMID:24954111	PBO:0102137	bipolar/spindle defects caused by the loss of telomere clustering were rescued by stopping nuclear movement.
PMID:24954111	PBO:0102131	(Fig. 1)
PMID:24954111	PBO:0102132	(Fig. 1)
PMID:24954111	FYPO:0000678	(Fig. 6A,B) even in the presence of the bipolar spindle
PMID:24957674	GO:0006325	xap5 genetically interacts with pht1 to repress antisense transcripts. In the ∆xap5∆pht1 double mutants the level of antisense transcription is exacerbated as observed using RNA-seq. Selected loci also showed antisense RNA production in histone deacetylase (HDACs) gene mutants.
PMID:24957674	PBO:0100330	(comment: CHECK SO:0000141 = The sequence of DNA located either at the end of the transcript that causes RNA polymerase to terminate transcription. SO:0000186 - LTR SO:0000101 - transposable element)
PMID:24957674	PBO:0098752	(comment: CHECK SO:0000141 = The sequence of DNA located either at the end of the transcript that causes RNA polymerase to terminate transcription. SO:0000186 - LTR SO:0000101 - transposable element)
PMID:24957674	PBO:0100331	(comment: CHECK SO:0000141 = The sequence of DNA located either at the end of the transcript that causes RNA polymerase to terminate transcription. SO:0000186 - LTR SO:0000101 - transposable element)
PMID:24963130	FYPO:0002636	(comment: 2 sub populations spindle elongation delayed during anaphase. A spindle elongation delayed during anaphase B)
PMID:24972934	PBO:0119918	(Fig. 1)
PMID:24972934	PBO:0119923	(Fig. 4D)
PMID:24972934	PBO:0119923	(Fig. 4D)
PMID:24972934	FYPO:0003440	(Fig. 5D and E)
PMID:24972934	PBO:0119922	(Fig. 4D)
PMID:24972934	PBO:0119922	(Fig. 4D)
PMID:24972934	PBO:0119921	(Fig. 4D)
PMID:24972934	PBO:0119924	Here we identified an additional mechanism of MOR inhibition by the SIN through Sid2 phosphorylation of Sog2.
PMID:24972934	PBO:0119920	(Fig. 4B)
PMID:24972934	PBO:0119920	(Fig. 4B)
PMID:24972934	PBO:0107404	(Fig. 4B)
PMID:24972934	PBO:0107404	(Fig. 4B)
PMID:24972934	PBO:0107404	(Fig. 4B)
PMID:24972934	PBO:0107404	(Fig. 4B)
PMID:24972934	PBO:0119925	(Fig. 5)
PMID:24972934	FYPO:0008401	(Fig. 3)
PMID:24972934	PBO:0119919	(Fig. 1)
PMID:24972934	FYPO:0003440	(Fig. 5D and E)
PMID:24972934	PBO:0098709	(Fig. 5C)
PMID:24972934	PBO:0099929	(Fig. 5C)
PMID:24972934	PBO:0099929	(Fig. 5C)
PMID:24997422	FYPO:0001164	). Interestingly, growth of transformants overexpressing truncated Fxn1 with a disrupted mitochondrial localization sequence (Fxn1Δ2-11) is similar to pREP3X at all concentrations of thiamine (Fig. 1A). These observations demonstrate that the growth inhibition resulting from Fxn1 overexpression is related to mitochondrial levels or improper processing of Fxn1.
PMID:25002536	PBO:0097281	(comment: LTR and ncRNA)
PMID:25002536	GO:0000785	(comment: occurs at LTR and ncRNA)
PMID:25002536	GO:0000785	(comment: occurs at LTR and ncRNA)
PMID:25002536	PBO:0097280	(comment: LTR and ncRNA)
PMID:25002536	PBO:0097281	(comment: occurs at LTR and ncRNA)
PMID:25002536	PBO:0097280	(comment: occurs at LTR and ncRNA)
PMID:25009287	GO:1990463	Skb1 and Slf1 (SPAC821.03C) mutually depend to form node-like structures on the plasma membrane.
PMID:25009287	GO:1990463	Skb1 and Slf1 (SPAC821.03C) mutually depend to form node-like structures on the plasma membrane.
PMID:25015293	PBO:0102762	multinucleate inferred from DNA content
PMID:25015293	PBO:0102774	multinucleate inferred from DNA content
PMID:25015293	PBO:0102762	multinucleate inferred from DNA content
PMID:25015293	PBO:0102762	multinucleate inferred from DNA content
PMID:25015293	PBO:0102768	same as spt20delta alone
PMID:25015293	PBO:0102774	multinucleate inferred from DNA content
PMID:25015293	GO:0005737	(comment: CHECK punctate)
PMID:25015293	PBO:0102768	same as spt20delta alone
PMID:25015293	PBO:0102768	same as spt20delta alone
PMID:25040903	PBO:0099500	(Figure S1E)
PMID:25040903	PBO:0099499	(Figure S1E)
PMID:25040903	FYPO:0001492	(Figure S1C)
PMID:25040903	FYPO:0000024	(Figure S1C)
PMID:25057016	PBO:0109496	(Fig. 3)
PMID:25057016	PBO:0109497	(Fig. 4)
PMID:25057016	PBO:0109497	(Fig. 4)
PMID:25057016	PBO:0109497	(Fig. 4) (comment: BiFC)
PMID:25057016	PBO:0109494	(Fig. 4)
PMID:25057016	FYPO:0009114	(Fig. 4)
PMID:25057016	FYPO:0003566	(Fig. 4)
PMID:25057016	FYPO:0003840	(Fig. 4)
PMID:25057016	FYPO:0003840	(Fig. 4)
PMID:25057016	FYPO:0000228	(Fig. 6)
PMID:25057016	FYPO:0000228	(Fig. 6)
PMID:25057016	FYPO:0000228	(Fig. 6)
PMID:25057016	PBO:0092631	Good evidence for this is the colocalisation with cnp3 in Fig. 3A in the csi1D background, where alp7 does not go to the spindle, or nda3 mutant where the spindle does not form, but alp7 still goes to the kinetochore, as seen by cnp3
PMID:25057016	PBO:0109492	Thorough experiments throughout using both full deletions as well as phospho mutants. Direct physical interaction is confirmed by Y2H
PMID:25057016	FYPO:0003840	(Fig. 1)
PMID:25057016	PBO:0093565	(Fig. 1)
PMID:25057016	PBO:0093565	(Fig. 1)
PMID:25057016	FYPO:0003840	(Fig. 1)
PMID:25057016	FYPO:0003566	(Fig. 2)
PMID:25057016	FYPO:0003566	(Fig. 2)
PMID:25057016	PBO:0109493	(Fig. S1D)
PMID:25057016	PBO:0109494	(Fig. 3)
PMID:25057016	PBO:0109495	(Fig. 3)
PMID:25057016	PBO:0109494	(Fig. 4)
PMID:25057016	PBO:0109495	(Fig. 4)
PMID:25057016	FYPO:0009114	(Fig. 4)
PMID:25057016	FYPO:0003566	(Fig. 4)
PMID:25057016	PBO:0109498	(Fig. S5D)
PMID:25057016	PBO:0109497	(Fig. 4) (comment: BiFC)
PMID:25057016	PBO:0109495	(Fig. 4)
PMID:25081204	GO:0106057	(comment: prz1 is the pombe equivalent to NFAT -functional equivalent rather than ortholog)
PMID:25081204	GO:0106057	(comment: prz1 is the pombe equivalent to NFAT -functional equivalent rather than ortholog)
PMID:25102102	PBO:0116553	Among the four predicted genes for pyruvate decarboxylase, only the Phx1-dependent genes (pdc201+ and pdc202+) contributed to long-term survival as judged by mutation and overexpression studies. These findings indicate that the Phx1-mediated long-term survival is achieved primarily through increasing the synthesis and activity of pyruvate decarboxylase. Consistent with this hypothesis, we observed that Phx1 curtailed respiration when cells entered stationary phase.
PMID:25102102	PBO:0116554	Among the four predicted genes for pyruvate decarboxylase, only the Phx1-dependent genes (pdc201+ and pdc202+) contributed to long-term survival as judged by mutation and overexpression studies. These findings indicate that the Phx1-mediated long-term survival is achieved primarily through increasing the synthesis and activity of pyruvate decarboxylase. Consistent with this hypothesis, we observed that Phx1 curtailed respiration when cells entered stationary phase.
PMID:25103238	GO:0140480	Failure of NE fenestration during mitosis in the double tts1del cut1-6 mutant
PMID:25106870	GO:0042276	Tolerance of the 8oxoguanine lesion during DNA gap-filling inserting the ribonucleotide ATP. This acitivity can be coupled to the non-homologous end joining (NHEJ) of double strand breaks (DSBs). (comment: changed from dna repair to translesion synthesis. /AL)
PMID:25106870	GO:0070716	(comment: RER should probably be a child of this)
PMID:25106870	GO:0004523	(Fig. 5)
PMID:25106870	GO:0003887	(Fig. 1)
PMID:25106870	GO:1990516	Incision of ribonucleotides paired to 8oxoguanine in the DNA
PMID:25109267	GO:1990748	(comment: CONDITION Ricinoleic acid, RA moieties from phospholipids)
PMID:25122751	FYPO:0003908	(comment: At stress response genes)
PMID:25195688	GO:1990536	(comment: CHECK transmembrane import into Golgi lumen)
PMID:25195688	GO:1990536	(comment: CHECK transmembrane import into Golgi lumen)
PMID:25203555	GO:0005515	(comment: not sure)
PMID:25203555	PBO:0100996	(comment: CHECK regulator of structure-specific DNA nuclease)
PMID:25204792	PBO:0117222	(comment: CHECK defect in sexual development in response to zinc or iron limitation)
PMID:25204792	PBO:0117223	(comment: CHECK defect in sexual development in response to zinc or iron limitation)
PMID:25245948	PBO:0102504	(comment: cDNA; no introns)
PMID:25245948	GO:0031509	(Fig. 1)
PMID:25245948	PBO:0094688	(comment: cDNA; no introns)
PMID:25245948	PBO:0102503	(comment: cDNA; no introns)
PMID:25245948	PBO:0102504	(comment: cDNA; no introns)
PMID:25245948	PBO:0102503	(comment: cDNA; no introns)
PMID:25245948	FYPO:0003555	(comment: cDNA; no introns)
PMID:25254656	FYPO:0003328	(Figure S15)
PMID:25254656	GO:0000828	(comment: CHECK in vitro) Figure S1A, right pane
PMID:25254656	PBO:0096502	(Figure 4E)
PMID:25254656	PBO:0096501	(Figure 4E)
PMID:25254656	GO:0052843	(comment: CHECK in vitro) Figure S1A, right pane
PMID:25254656	FYPO:0006892	(Figure 3C)
PMID:25254656	FYPO:0005485	(Figure 3C)
PMID:25254656	FYPO:0006893	(Figure 3C) (comment: the N erminal domain has a dominent -ve effect in in vitro assay (not expression should ne n/a))
PMID:25254656	FYPO:0005682	(Figure 4A)
PMID:25254656	FYPO:0003328	(Figure 3A)
PMID:25254656	FYPO:0000091	(Figure S2A)
PMID:25254656	FYPO:0005799	(Figure 3B, Figure 3C)
PMID:25313826	GO:1990426	the CAF-1 complex promotes Replication-coupled homologous recombination at blocked replication forks.
PMID:25313826	GO:1990426	the CAF-1 complex promotes Replication-coupled homologous recombination at blocked replication forks.
PMID:25313826	GO:1990426	the CAF-1 complex promotes Replication-coupled homologous recombination at blocked replication forks.
PMID:25318672	FYPO:0000674	(comment: Mutant cells grow normally in liquid minimal medium supplemented with ethanolamine.)
PMID:25318672	FYPO:0006934	(comment: Determined by thin layer chromatography TLC)
PMID:25318672	FYPO:0006934	(comment: Determined by thin layer chromatography TLC)
PMID:25318672	FYPO:0000674	(comment: Mutant cells grow normally in liquid minimal medium supplemented with choline.)
PMID:25318672	PBO:0096383	(comment: Determined by thin layer chromatography, TLC)
PMID:25318672	PBO:0096381	(comment: The endoplasmic reticulum is wrapped around the abnormally large lipid droplets)
PMID:25318672	FYPO:0000674	(comment: Mutant cells grow normally in liquid rich medium)
PMID:25318672	PBO:0095634	Slow population growth rate can be rescued by supplementing the minimal medium with choline or ethanolamine, the precursors required for phospholipid biosynthesis through the de novo Kennedy pathway
PMID:25318672	PBO:0096380	At the restrictive temperature of 36C, cells accumulate very large lipid droplets surrounded by the endoplasmic reticulum. These lipid droplets arise from persistent growth rather than fusion.
PMID:25318672	FYPO:0001357	(comment: restrictive temperature for bbl1-9)
PMID:25318672	FYPO:0002061	(comment: restrictive temperature for bbl1-9)
PMID:25318672	PBO:0096379	At high temperature (36C), the mutant protein appeared to bind PA nearly as well as the wild-type enzyme but exhibited a strongly decreased rate of catalysis.
PMID:25318672	FYPO:0001355	(comment: permissive temperature for bbl1-9)
PMID:25318672	FYPO:0006934	(comment: Determined by thin layer chromatography TLC)
PMID:25318672	PBO:0095685	(comment: restrictive temperature for bbl1-9)
PMID:25330395	FYPO:0003107	Tpz1-L439R,L445R disrupts interaction with Ccq1 but retain interactions with Pot1 and Poz1 based on co-IP experiments.
PMID:25330395	FYPO:0003107	Tpz1-L449R disrupts interaction with Ccq1 but retain interactions with Pot1 and Poz1 based on co-IP experiments. In combination with poz1 deletion, telomeres become unprotected and cells survive by circularizing chromosomes. Telomerase cannot be recruited to telomeres since Rad3/Tel1-dependent phosphorylation of Ccq1 Thr93, essential for promoting Ccq1-Est1 interaction and telomerase recruitment, is eliminated by tpz1-L449R.
PMID:25330395	FYPO:0002019	Tpz1-[1-485] disrupts interaction with Poz1 but retain interactions with Pot1 and Ccq1 based on co-IP experiments. In combination with ccq1 deletion, telomeres become unprotected and cells survive by circularizing chromosomes. Telomerase recruitment to telomeres is increased since Rad3/Tel1-dependent phosphorylation of Ccq1 Thr93, essential for promoting Ccq1-Est1 interaction and telomerase recruitment, is increased in tpz1-[1-485] cells.
PMID:25330395	FYPO:0002019	Tpz1-W498R,I501R disrupts interaction with Poz1 but retain interactions with Pot1 and Ccq1 based on co-IP experiments. In combination with ccq1 deletion, telomeres become unprotected and cells survive by circularizing chromosomes. Telomerase recruitment to telomeres is increased since Rad3/Tel1-dependent phosphorylation of Ccq1 Thr93, essential for promoting Ccq1-Est1 interaction and telomerase recruitment, is increased in tpz1-W498R,I501R cells.
PMID:25332400	PBO:0092711	Importantly,CK2-mediated phosphorylation had a similar effect on the nucleosome-binding specificities of fly HP1a and S.pombe Swi6. (Figure 6A)
PMID:25348260	PBO:0110013	(Fig. 3)
PMID:25348260	PBO:0110014	(Fig. 3)
PMID:25348260	PBO:0110012	(Fig. 3)
PMID:25348260	PBO:0110012	(Fig. 3)
PMID:25348260	PBO:0110015	(Fig. 3)
PMID:25348260	PBO:0110015	(Fig. 3)
PMID:25348260	PBO:0110012	(Fig. 3)
PMID:25348260	PBO:0110013	(Fig. 3)
PMID:25348260	PBO:0110014	(Fig. 3)
PMID:25356590	PBO:0113703	(Fig. 3B)
PMID:25356590	FYPO:0008252	(Fig. 3B)
PMID:25356590	PBO:0113703	(Fig. 3B)
PMID:25356590	FYPO:0005311	(Fig. 3A)
PMID:25356590	FYPO:0005311	(Fig. 3A)
PMID:25356590	PBO:0113710	(Fig. 3A)
PMID:25356590	FYPO:0004126	(Fig. 3A)
PMID:25356590	FYPO:0002917	(Fig. 3A)
PMID:25356590	FYPO:0002917	(Fig. 1B)
PMID:25356590	FYPO:0002917	(Fig. 3A)
PMID:25356590	FYPO:0002917	(Fig. 3A)
PMID:25356590	FYPO:0004126	(Fig. 3A)
PMID:25356590	PBO:0113709	(Fig. 2C)
PMID:25356590	PBO:0113709	(Fig. 2C)
PMID:25356590	PBO:0113708	(Fig. 2C)
PMID:25356590	PBO:0113708	(Fig. 2C)
PMID:25356590	PBO:0113722	(Fig. S5)
PMID:25356590	PBO:0113722	(Fig. S5)
PMID:25356590	PBO:0113722	(Fig. S5)
PMID:25356590	PBO:0113722	(Fig. S5)
PMID:25356590	PBO:0113722	(Fig. S5)
PMID:25356590	PBO:0113718	(Fig. 4B)
PMID:25356590	PBO:0113721	(Fig. 4B)
PMID:25356590	PBO:0113718	(Fig. 4C)
PMID:25356590	PBO:0113718	(Fig. 4C)
PMID:25356590	PBO:0113718	(Fig. 4C)
PMID:25356590	PBO:0113720	(Fig. 4C)
PMID:25356590	PBO:0113723	(Fig. 4C)
PMID:25356590	PBO:0113808	(Fig. 6B)
PMID:25356590	PBO:0113717	(Fig. 3E)
PMID:25356590	FYPO:0005311	(Fig. 1B)
PMID:25356590	PBO:0113692	(Fig. 1B)
PMID:25356590	PBO:0113718	(Fig. 4A)
PMID:25356590	FYPO:0002917	(Fig. 1B)
PMID:25356590	PBO:0113722	(Fig. S5)
PMID:25356590	PBO:0113722	(Fig. S5)
PMID:25356590	PBO:0113700	(Fig. 1F)
PMID:25356590	PBO:0113699	(Fig. 1F)
PMID:25356590	PBO:0113699	(Fig. 1F)
PMID:25356590	PBO:0113699	(Fig. 1F)
PMID:25356590	PBO:0113699	(Fig. 1F)
PMID:25356590	PBO:0113719	(Fig. 4A)
PMID:25356590	PBO:0113719	(Fig. 4A)
PMID:25356590	PBO:0113719	(Fig. 4A)
PMID:25356590	PBO:0113721	(Fig. 4A)
PMID:25356590	PBO:0113720	(Fig. 4A)
PMID:25356590	PBO:0113718	(Fig. 4A)
PMID:25356590	PBO:0113693	(Fig. 1D)
PMID:25356590	PBO:0113693	(Fig. 1D)
PMID:25356590	PBO:0113694	(Fig. 1D)
PMID:25356590	PBO:0113695	(Fig. 1D)
PMID:25356590	PBO:0113696	(Fig. 1D)
PMID:25356590	PBO:0113697	(Fig. 1D)
PMID:25356590	PBO:0113716	(Fig. 3E)
PMID:25356590	PBO:0113716	(Fig. 3E)
PMID:25356590	PBO:0113716	(Fig. 3E)
PMID:25356590	PBO:0113697	(Fig. 1D)
PMID:25356590	PBO:0113698	(Fig. 1E)
PMID:25356590	PBO:0113698	(Fig. 1E)
PMID:25356590	PBO:0113698	(Fig. 1E)
PMID:25356590	PBO:0113698	(Fig. 1E)
PMID:25356590	PBO:0113698	(Fig. 1E)
PMID:25356590	PBO:0102526	(Fig. 1E)
PMID:25356590	FYPO:0002917	(Fig. 1B)
PMID:25356590	FYPO:0008246	(Fig. 1E)
PMID:25356590	PBO:0113699	(Fig. 1F)
PMID:25356590	PBO:0113699	(Fig. 3E)
PMID:25356590	PBO:0113715	(Fig. 3E)
PMID:25356590	PBO:0113699	(Fig. 3E)
PMID:25356590	PBO:0113714	(Fig. 3D)
PMID:25356590	PBO:0102526	(Fig. 3D)
PMID:25356590	PBO:0113698	(Fig. 3D)
PMID:25356590	PBO:0113698	(Fig. 3D)
PMID:25356590	PBO:0120505	(Fig. 3D)
PMID:25356590	PBO:0102526	(Fig. 3D)
PMID:25356590	PBO:0113698	(Fig. 3D)
PMID:25356590	PBO:0113696	(Fig. 3C)
PMID:25356590	PBO:0113697	(Fig. 3C)
PMID:25356590	PBO:0113712	(Fig. 3C)
PMID:25356590	PBO:0113712	(Fig. 3C)
PMID:25356590	PBO:0113696	(Fig. 3C)
PMID:25356590	PBO:0113697	(Fig. 3C)
PMID:25356590	PBO:0113712	(Fig. 3C)
PMID:25356590	FYPO:0008252	(Fig. 3B)
PMID:25356590	FYPO:0008252	(Fig. 3B)
PMID:25356590	FYPO:0008252	(Fig. 3B)
PMID:25356590	PBO:0113711	(Fig. 3B)
PMID:25356590	PBO:0113810	(Fig. 6B)
PMID:25356590	PBO:0113811	(Fig. 6B)
PMID:25356590	PBO:0113811	(Fig. 6B)
PMID:25356590	PBO:0113727	(Fig. 6C)
PMID:25356590	PBO:0113728	(Fig. 6C)
PMID:25356590	PBO:0113729	(Fig. 6C)
PMID:25356590	PBO:0113730	at the mat locus and subtelomeric repeats Set1-mediated H3K4me contributes to repression.
PMID:25356590	PBO:0113731	at the mat locus and subtelomeric repeats Set1-mediated H3K4me contributes to repression.
PMID:25356590	GO:0141005	Thus, H3K4me catalyzed by Set1C could compete with Mst1- mediated H3K4ac at Tf2s to maintain the integrity of Tf bodies.
PMID:25356590	FYPO:0002917	(Fig. 1B)
PMID:25356590	PBO:0113707	(Fig. 2C)
PMID:25356590	PBO:0113699	(Fig. 1F)
PMID:25356590	PBO:0113706	(Fig. 2A)
PMID:25356590	PBO:0113706	(Fig. 2A)
PMID:25356590	FYPO:0008252	(Fig. 1C)
PMID:25356590	PBO:0113704	(Fig. 2A)
PMID:25356590	PBO:0113705	(Fig. 2A)
PMID:25356590	PBO:0113705	(Fig. 2A)
PMID:25356590	PBO:0113703	(Fig. 1C)
PMID:25356590	PBO:0113703	(Fig. 1C)
PMID:25356590	PBO:0113703	(Fig. 1C)
PMID:25356590	PBO:0113702	(Fig. 1C)
PMID:25356590	PBO:0113701	(Fig. 1C)
PMID:25356590	PBO:0113701	(Fig. 1C)
PMID:25356590	FYPO:0002917	(Fig. 1B)
PMID:25375240	PBO:0095416	(Figure 5E)
PMID:25375240	PBO:0095418	(Figure 7D)
PMID:25375240	FYPO:0002060	(Figure 7D)
PMID:25375240	PBO:0095421	indicated by increased mad2 on unattached kinetochores
PMID:25375240	FYPO:0004396	Tracking of the inter-SPB distance indicated that the kinetics of spindle elongation in the kis1-1 mad2D double mutant was ameliorated compared with the kis1-1 single mutant (Figure S9).
PMID:25375240	FYPO:0001270	(Figure 4G)
PMID:25378562	FYPO:0000116	(comment: Sensitive to 3 mM ZnCl2. Suppressed by overexpression of budding yeast VAM7.)
PMID:25378562	GO:0006896	Vsl1p is a partner of Pep12p, and mainly functions on the prevacuolar and vacuolar membrane.
PMID:25378562	GO:0006896	Vsl1p is a partner of Pep12p, and mainly functions on the prevacuolar and vacuolar membrane.
PMID:25378562	FYPO:0001945	mutants defective in vacuolar sorting do not deliver SpCPY to the vacuole but rather to the outside of the cells.
PMID:25378562	FYPO:0001423	mutants defective in vacuolar sorting do not deliver SpCPY to the vacuole but rather to the outside of the cells.
PMID:25378562	FYPO:0000116	(comment: Sensitive to 3 mM ZnCl2)
PMID:25392932	PBO:0098562	(comment: CHECK SO:0001272 = tRNA gene)
PMID:25392932	PBO:0098562	(comment: CHECK SO:0001272 = tRNA gene)
PMID:25392932	GO:0006386	Our data only demonstrate that this true for RNA Polymerase III(comment: // MOVED UP TO 'REGULATION' FROM NEG REG BASED ON NEW PUBLICATION)
PMID:25402480	PBO:0116533	"(comment: SO:0000407 = 18s rRNA, the genes are the 18s genes of the ""correct length"" so I guess we want them in there if we want to be able to make the ""connections"" from the info in the database? Though I guess this regions isnt properly sequenced..)"
PMID:25402480	PBO:0116536	"(comment: SO:0000407 = 18s rRNA, the genes are the 18s genes of the ""correct length"" so I guess we want them in there if we want to be able to make the ""connections"" from the info in the database? Though I guess this regions isnt properly sequenced..)"
PMID:25402480	PBO:0116535	"(comment: SO:0000407 = 18s rRNA, the genes are the 18s genes of the ""correct length"" so I guess we want them in there if we want to be able to make the ""connections"" from the info in the database? Though I guess this regions isnt properly sequenced..)"
PMID:25402480	FYPO:0002061	"(comment: They couldn't make the knockout in haploid, and diploid inviable, hence inferring inviable vegetative rather than more general ""inviable cell pop"" or inviable spore pop)"
PMID:25402480	PBO:0116534	"(comment: SO:0000407 = 18s rRNA, the genes are the 18s genes of the ""correct length"" so I guess we want them in there if we want to be able to make the ""connections"" from the info in the database? Though I guess this regions isnt properly sequenced..)"
PMID:25404562	PBO:0106686	(Table 2)
PMID:25404562	FYPO:0001357	(Fig. 3A)
PMID:25404562	PBO:0106681	diploid lacked detectable Cm in its tRNAPhe and had normal levels of Gm compared with that from wild type (0.88 versus 0.90 moles/mole) (Table 3; Fig. 4A)
PMID:25404562	PBO:0106681	(Table 2)
PMID:25404562	PBO:0106691	strain lacked Gm34 in its tRNAPhe, and had Cm levels comparable to those of wild type (0.86 versus 0.91 moles/mole) (Table 3; Fig. 4A).
PMID:25404562	PBO:0106690	diploid lacked detectable Cm in its tRNAPhe and had normal levels of Gm compared with that from wild type (0.88 versus 0.90 moles/mole) (Table 3; Fig. 4A)
PMID:25404562	PBO:0106689	(Table 2)
PMID:25404562	PBO:0106681	(Table 2)
PMID:25404562	PBO:0106690	(Table 2)
PMID:25404562	PBO:0106687	(Table 2)
PMID:25404562	PBO:0106686	(Table 2)
PMID:25404562	PBO:0106681	(Table 2)
PMID:25404562	PBO:0106692	(Table 2)
PMID:25404562	PBO:0106691	(Table 2)
PMID:25404562	PBO:0106690	(Table 2)
PMID:25404562	PBO:0106689	(Table 2)
PMID:25404562	PBO:0106688	(Table 2)
PMID:25404562	PBO:0106687	(Table 2)
PMID:25404562	PBO:0106686	(Table 2)
PMID:25404562	PBO:0106682	(Table 2)
PMID:25404562	PBO:0106683	yW formation was impaired in the Sp trm734△ mutant (44% of wild-type levels) and to a lesser extent in the Sp trm732△ mutant (73%) (Fig. 4F), consistent with the increased m1G levels (Table 3; Fig. 4A)
PMID:25404562	PBO:0106683	yW formation was impaired in the Sp trm734△ mutant (44% of wild-type levels) and to a lesser extent in the Sp trm732△ mutant (73%) (Fig. 4F), consistent with the increased m1G levels (Table 3; Fig. 4A)
PMID:25404562	PBO:0106682	strain lacked Gm34 in its tRNAPhe, and had Cm levels comparable to those of wild type (0.86 versus 0.91 moles/mole) (Table 3; Fig. 4A).
PMID:25404562	FYPO:0001234	(Fig. 2A) (comment: 11 days for visible colonies)
PMID:25404562	PBO:0106688	(Table 2)
PMID:25404562	PBO:0106687	(Table 2)
PMID:25410910	PBO:0098171	(comment: yes it looks like pol II?! (val: changed to DNA binding term))
PMID:25411334	FYPO:0000026	(Fig. S2A)
PMID:25411334	FYPO:0000026	(Fig. S2A)
PMID:25411334	FYPO:0000026	(Fig. S2A)
PMID:25411338	GO:0031520	(comment: CHECK during cellular response to glucose starvation)
PMID:25411338	PBO:0094264	(comment: CHECK strong phenotype = has_severity(FYPO_EXT:0000001))
PMID:25411338	PBO:0106536	The ght5 gene, the transcription of which is repressed in the WT cells, is transcribed at a high level in the presence of 111 mM glucose in the scr1 delta cells.
PMID:25411338	PBO:0106537	the level of ght5 transcription, which increases in the WT during glucose limitation, fails to increase in this mutant cells in low-glucose medium.
PMID:25411338	GO:0031520	(comment: CHECK during cellular response to glucose starvation)
PMID:25411338	PBO:0106537	the level of ght5 transcription, which increases in the WT during glucose limitation, fails to increase in this mutant cells in low-glucose medium.
PMID:25411338	PBO:0106538	The Ght5 protein, which is localized on the plasma membrane in the WT, fails to be localized on the plasma membrane, accumulating in the cytoplasm.
PMID:25411338	PBO:0106538	The Ght5 protein, which is localized on the plasma membrane in the WT, fails to be localized on the plasma membrane, accumulating in the cytoplasm.
PMID:25411338	PBO:0106538	The Ght5 protein, which is localized on the plasma membrane in the WT, fails to be localized on the plasma membrane, accumulating in the cytoplasm.
PMID:25411338	PBO:0094264	(comment: CHECK strong phenotype = has_severity(FYPO_EXT:0000001))
PMID:25411338	PBO:0024683	(comment: CHECK during cellular response to glucose starvation)
PMID:25411338	GO:0031520	(comment: CHECK during cellular response to glucose starvation)
PMID:25411338	PBO:0106538	The Ght5 protein, which is localized on the plasma membrane in the WT, fails to be localized on the plasma membrane, accumulating in the cytoplasm.
PMID:25414342	FYPO:0003179	(comment: CHECK 7.4% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2A, Table S6)
PMID:25414342	FYPO:0000581	(comment: CHECK 13.87% of wild-type spore viability) (Table S6)
PMID:25414342	FYPO:0005659	(comment: CHECK 111.2% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim; skewed recombinant classes) (Figs. 5E, 7A, Table S6)
PMID:25414342	FYPO:0003179	(comment: CHECK 6.87% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2E, Table S6)
PMID:25414342	FYPO:0002485	(comment: CHECK 20.15% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Table S6)
PMID:25414342	FYPO:0000581	(comment: CHECK 31.18% of wild-type spore viability) (Table S6)
PMID:25414342	FYPO:0005658	(comment: CHECK 101.76% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim; skewed recombinant categories) (Figs. 5E, 7A, Table S6)
PMID:25414342	FYPO:0003179	(comment: CHECK 9.88% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2E, Table S6)
PMID:25414342	FYPO:0002485	(comment: CHECK 30.92% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0000581	(comment: CHECK 7.8% of wild-type spore viability, synergistic relationship) (Table S6)
PMID:25414342	FYPO:0005660	(comment: CHECK 79.92% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim; skewed recombinant categories) (Figs. 5E, 7A, Table S6)
PMID:25414342	FYPO:0003179	(comment: CHECK 37.89% of wild-type recombination assayed between ade6-3083 and ade6-469, similar to dmc1Δ-12 and rlp1Δ single mutants, but higher than dmc1Δ-12 rlp1Δ double mutant) (Fig. 2E, Table S6)
PMID:25414342	FYPO:0002485	(comment: CHECK 55.49% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0000581	(comment: CHECK 20.24% of wild-type spore viability) (Table S6)
PMID:25414342	FYPO:0005659	(comment: CHECK 114.54% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim; skewed recombinant categories) (Fig. 5D, Table S6)
PMID:25414342	FYPO:0003179	(comment: CHECK 15.59% of wild-type recombination assayed between ade6-3083 and ade6-469) (Fig. 2D, Table S6)
PMID:25414342	FYPO:0002485	(comment: CHECK 45.45% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0000581	(comment: CHECK 21.46% of wild-type spore viability, synergistic relationship) (Table S6)
PMID:25414342	FYPO:0005658	(comment: CHECK 101.4% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim; skewed recombinant categories) (Fig. 5D, Table S6)
PMID:25414342	FYPO:0003179	(comment: CHECK 10.34% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2D, Table S6)
PMID:25414342	FYPO:0002485	(comment: CHECK 38.89% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0004993	(comment: CHECK 91.68% of wild-type spore viability, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0005659	(comment: CHECK 122.65% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship) (Fig. 5D, Table S6)
PMID:25414342	FYPO:0003179	(comment: CHECK 27.08% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2D, Table S6)
PMID:25414342	FYPO:0002485	(comment: CHECK 49.8% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0000581	(comment: CHECK 21.45% of wild-type spore viability, synergistic relationship) (Table S6)
PMID:25414342	FYPO:0005659	(comment: CHECK 130.25% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship) (Fig. 5C, Table S6)
PMID:25414342	FYPO:0003179	(comment: CHECK 7.33% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2C, Table S6)
PMID:25414342	FYPO:0002485	(comment: CHECK 59.57% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0000581	(comment: CHECK 37.75% of wild-type spore viability, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0005659	(comment: CHECK 116.19% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship) (Fig. 5C, Table S6)
PMID:25414342	FYPO:0003179	(comment: CHECK 8.33% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2C, Table S6)
PMID:25414342	FYPO:0002485	(comment: CHECK 32.13% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0000581	(comment: CHECK 73.46% of wild-type spore viability, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0005658	(comment: CHECK 102.17% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, higher than rdl1Δ-25, lower than fml1Δ, skewed recombinant categories) (Fig. S3, Table S6)
PMID:25414342	FYPO:0003179	(comment: CHECK 52.08% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0002485	(comment: CHECK 46.52% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0005658	(comment: CHECK 101.33% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim; higher than rlp1Δ-7, lower than fml1Δ, skewed recombinant categories) (Figs. 5C, 7A, Table S6)
PMID:25414342	FYPO:0003179	(comment: CHECK 36.88% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2C, Table S6)
PMID:25414342	FYPO:0002485	(comment: CHECK 69.41% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0000581	(comment: CHECK 4.11% of wild-type spore viability) (Table S6)
PMID:25414342	FYPO:0005659	(comment: CHECK 136.75% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship) (Fig. 5B, Table S6)
PMID:25414342	FYPO:0003179	(comment: CHECK 12.19% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2B, Table S6)
PMID:25414342	FYPO:0002485	(comment: CHECK 15.53% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0000581	(comment: CHECK 3.68% of wild-type spore viability, synergistic relationship) (Table S6)
PMID:25414342	FYPO:0005659	(comment: CHECK 127.22% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship) (Fig. 5B, Table S6)
PMID:25414342	FYPO:0003179	(comment: CHECK 8.87% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2B, Table S6)
PMID:25414342	FYPO:0002485	(comment: CHECK 15.19% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0000581	(comment: CHECK 53.76% of wild-type spore viability, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0005659	(comment: CHECK 111.64% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship) (Fig. 5B, Table S6)
PMID:25414342	FYPO:0003179	(comment: CHECK 35.42% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2B, Table S6)
PMID:25414342	FYPO:0002485	(comment: CHECK 55.62% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, partial rescue from rad55Δ levels) (Table S6)
PMID:25414342	FYPO:0005659	(comment: CHECK 119.91% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship) (Fig. 5A, Table S6)
PMID:25414342	FYPO:0003179	(comment: CHECK 3.55% of wild-type recombination assayed between ade6-3083 and ade6-469) (Fig. 2A, Table S6)
PMID:25414342	FYPO:0002485	(comment: CHECK 28.85% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0000581	(comment: CHECK 54.78% of wild-type spore viability, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0005659	(comment: CHECK 115.12% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship) (Fig. 5A, Table S6)
PMID:25414342	FYPO:0003179	(comment: CHECK 2.55% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship) (Fig. 2A, Table S6)
PMID:25414342	FYPO:0002485	(comment: CHECK 25.9% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0005659	(comment: CHECK 115.17% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship) (Fig. 5A, Table S6)
PMID:25414342	FYPO:0002485	(comment: CHECK 24.3% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0000581	(comment: CHECK 60.64% of wild-type spore viability, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0005659	(comment: CHECK 124.3% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship - similar to fml1delta) (Fig. 5, Table S6)
PMID:25414342	FYPO:0003179	(comment: CHECK 7.2% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship - similar to rqh1delta) (Fig. 6, Table S6)
PMID:25414342	FYPO:0002485	(comment: CHECK 76.1% of wild-type recombination assayed between ade6-3083 and ade6-469) (Table S6)
PMID:25414342	FYPO:0000581	(comment: CHECK 15.4% of wild-type spore viability, synergistic relationship) (Table S6)
PMID:25414342	FYPO:0000581	(comment: CHECK 50.7% of wild-type spore viability, synergistic relationship) (Table S5)
PMID:25414342	FYPO:0005660	(comment: CHECK 75.2% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship) (Fig. S2, Table S5)
PMID:25414342	FYPO:0003179	(comment: CHECK 31.1% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Table S5)
PMID:25414342	FYPO:0002485	(comment: CHECK 54.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S5)
PMID:25414342	FYPO:0000581	(comment: CHECK 55.5% of wild-type spore viability, synergistic relationship) (Fig. 4D, Table S5)
PMID:25414342	FYPO:0005660	(comment: CHECK 76.7% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship; skewed recombinant classes) (Figs. 4C, 7A, Table S5)
PMID:25414342	FYPO:0003179	(comment: CHECK 21.1% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	(comment: CHECK 65.3% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Fig. 4B, Table S5)
PMID:25414342	FYPO:0000581	(comment: CHECK 9.9% of wild-type spore viability, synergistic relationship) (Fig. 4D, Table S5)
PMID:25414342	FYPO:0005657	(comment: CHECK 106.7% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship) (Fig. 4C, Table S5)
PMID:25414342	FYPO:0003179	(comment: CHECK 2.1% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship) (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	(comment: CHECK 0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, synergistic relationship) (Fig. 4B, Table S5)
PMID:25414342	FYPO:0000581	(comment: CHECK 76.9% of wild-type spore viability, epistatic relationship) (Fig. 4D, Table S5)
PMID:25414342	FYPO:0005660	(comment: CHECK 91.4% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship) (Fig. 4C, Table S5)
PMID:25414342	FYPO:0003179	(comment: CHECK 25.7% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	(comment: CHECK 26.4% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Fig. 4B, Table S5)
PMID:25414342	FYPO:0000581	(comment: CHECK 93.8% of wild-type spore viability, epistatic relationship) (Fig. 4D, Table S5)
PMID:25414342	FYPO:0005660	(comment: CHECK 84.1% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship) (Fig. 4C, Table S5)
PMID:25414342	FYPO:0003179	(comment: CHECK 14.2% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	(comment: CHECK 33.5% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Fig. 4B, Table S5)
PMID:25414342	FYPO:0000581	(comment: CHECK 13.0% of wild-type spore viability, synergistic relationship) (Fig. 4D, Table S5)
PMID:25414342	FYPO:0005660	(comment: CHECK 18.5% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship) (Fig. 4C, Table S5)
PMID:25414342	FYPO:0003179	(comment: CHECK 2.5% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship) (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	(comment: CHECK 4.5% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, synergistic relationship) (Fig. 4B, Table S5)
PMID:25414342	FYPO:0000581	(comment: CHECK 3.7% of wild-type spore viability, synergistic relationship) (Fig. 4D, Table S5)
PMID:25414342	FYPO:0003179	(comment: CHECK 0.42% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship) (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	(comment: CHECK 0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, synergistic relationship) (Fig. 4B, Table S5)
PMID:25414342	FYPO:0004993	(comment: CHECK 104.8% of wild-type spore viability) (Fig. 3D, Table S4)
PMID:25414342	FYPO:0005660	(comment: CHECK 78.6% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship) (Fig. 3C, Table S4)
PMID:25414342	FYPO:0003179	(comment: CHECK 44.4% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 3A, Table S4)
PMID:25414342	FYPO:0002485	(comment: CHECK 55.5% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Fig. 3B, Table S4)
PMID:25414342	FYPO:0004993	(comment: CHECK 117.1% of wild-type spore viability) (Fig. 3D, Table S4)
PMID:25414342	FYPO:0005660	(comment: CHECK 85.8% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship) (Fig. 3C, Table S4)
PMID:25414342	FYPO:0003179	(comment: CHECK 32.3% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 3A, Table S4)
PMID:25414342	FYPO:0002485	(comment: CHECK 48.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Fig. 2B, Table S4)
PMID:25414342	FYPO:0000581	(comment: CHECK 44.7% of wild-type spore viability, 17.4-fold higher spore viability than mus81 single mutant) (Fig. 2A, Table S3)
PMID:25414342	FYPO:0005660	(comment: CHECK 6.9% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 2B, Table S3)
PMID:25414342	FYPO:0003179	(comment: CHECK 36.3% of wild-type recombination assayed between ade6-3083 and ade6-469) (Table S3)
PMID:25414342	FYPO:0002485	(comment: CHECK 58.1% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Table S3)
PMID:25414342	FYPO:0000581	(comment: CHECK 28.9% of wild-type spore viability, 11.3-fold higher spore viability than mus81 single mutant) (Fig. 2A, Table S3)
PMID:25414342	FYPO:0005660	(comment: CHECK 7.8% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 2B, Table S3)
PMID:25414342	FYPO:0003179	(comment: CHECK 57.9% of wild-type recombination assayed between ade6-3083 and ade6-469) (Table S3)
PMID:25414342	FYPO:0002485	(comment: CHECK 6.4% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Table S3)
PMID:25414342	FYPO:0000581	(comment: CHECK 21.2% of wild-type spore viability, 8.3-fold higher spore viability than mus81 single mutant) (Fig. 2A, Table S3)
PMID:25414342	FYPO:0005660	(comment: CHECK 9.9% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 2B, Table S3)
PMID:25414342	FYPO:0003179	(comment: CHECK 30.1% of wild-type recombination assayed between ade6-3083 and ade6-469) (Table S3)
PMID:25414342	FYPO:0002485	(comment: CHECK 26.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Table S3)
PMID:25414342	FYPO:0000581	(comment: CHECK 42.9% of wild-type spore viability, 16.7-fold higher spore viability than mus81 single mutant) (Fig. 2A, Table S3)
PMID:25414342	FYPO:0005660	(comment: CHECK 10.5% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 2B, Table S3)
PMID:25414342	FYPO:0003179	(comment: CHECK 2.2% of wild-type recombination assayed between ade6-3083 and ade6-469) (Table S3)
PMID:25414342	FYPO:0002485	(comment: CHECK 19.1% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Table S3)
PMID:25414342	FYPO:0000581	(comment: CHECK 47% of wild-type spore viability) (Fig. 2A, Table S3), (comment: 18.3-fold higher spore viability than mus81 single mutant)
PMID:25414342	FYPO:0005660	(comment: CHECK 1.7% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 2B, Table S3)
PMID:25414342	FYPO:0003179	(comment: CHECK 12.3% of wild-type recombination assayed between ade6-3083 and ade6-469) (Table S3)
PMID:25414342	FYPO:0002485	(comment: CHECK 0.9% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Table S3)
PMID:25414342	FYPO:0000581	(comment: CHECK 43.6% of wild-type spore viability) (Table S6)
PMID:25414342	FYPO:0005657	(Fig. 5, Table S6)
PMID:25414342	FYPO:0003179	(comment: CHECK 8.0% of wild-type recombination assayed between ade6-3083 and ade6-469) (Fig. 6, Table S6)
PMID:25414342	FYPO:0002485	(comment: CHECK 31.4% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Table S6)
PMID:25414342	FYPO:0000581	(comment: CHECK 77.7% of wild-type spore viability) (Fig. 4D, Table S5)
PMID:25414342	FYPO:0005660	(comment: CHECK 87.6% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 4C, Table S5)
PMID:25414342	FYPO:0003179	(comment: CHECK 9.7% of wild-type recombination assayed between ade6-3083 and ade6-469) (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	(comment: CHECK 16.3% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Fig. 4B, Table S5)
PMID:25414342	FYPO:0004993	(comment: CHECK 133.5% of wild-type spore viability) (Fig. 3D, Table S4)
PMID:25414342	FYPO:0005660	(comment: CHECK 90.5% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 3C, Table S4)
PMID:25414342	FYPO:0003179	(comment: CHECK 49.2% of wild-type recombination assayed between ade6-3083 and ade6-469) (Fig. 3A, Table S4)
PMID:25414342	FYPO:0002485	(comment: CHECK 49.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Fig. 3B, Table S4)
PMID:25414342	FYPO:0004993	(comment: CHECK 108.5% of wild-type spore viability) (Fig. 3D, Table S4)
PMID:25414342	FYPO:0005660	(comment: CHECK 82.2% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 3C, Table S4)
PMID:25414342	FYPO:0003179	(comment: CHECK 27.7% of wild-type recombination assayed between ade6-3083 and ade6-469) (Fig. 3A, Table S4)
PMID:25414342	FYPO:0002485	(comment: CHECK 48.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Fig. 3B, Table S4)
PMID:25414342	FYPO:0004993	(comment: CHECK 95.2% of wild-type spore viability) (Fig. 3D, Table S4)
PMID:25414342	FYPO:0005660	(comment: CHECK 82.9% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 4C, Table S5)
PMID:25414342	FYPO:0003179	(comment: CHECK 42.4% of wild-type recombination assayed between ade6-3083 and ade6-469) (Fig. 3A, Table S4)
PMID:25414342	FYPO:0002485	(comment: CHECK 61.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Fig. 3B, Table S4)
PMID:25414342	FYPO:0000581	(comment: CHECK 61.1% of wild-type spore viability) (Fig. 4D, Table S5)
PMID:25414342	FYPO:0005660	(comment: CHECK 85.9% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 4C, Table S5)
PMID:25414342	FYPO:0003179	(comment: CHECK 39.7% of wild-type recombination assayed between ade6-3083 and ade6-469) (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	(comment: CHECK 28.9% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Fig. 4B, Table S5)
PMID:25414342	FYPO:0000581	(comment: CHECK 78.4% of wild-type spore viability) (Table S2)
PMID:25414342	FYPO:0005659	(comment: CHECK 117% of wild-type recombination assayed at various loci) (Fig. 1, Table S2)
PMID:25414342	FYPO:0003891	(Table S2)
PMID:25414342	FYPO:0005578	(Table S2)
PMID:25414342	FYPO:0000581	(comment: CHECK 83.9% of wild-type spore viability) (Fig. 4D, Table S5)
PMID:25414342	FYPO:0005657	(Fig. 4C, Table S5)
PMID:25414342	FYPO:0003179	33.7% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	38.5% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Fig. 4B, Table S5)
PMID:25417108	FYPO:0004819	(comment: Affecting Rad52 enrichment at rDNA)
PMID:25417108	FYPO:0003103	(comment: Affecting Dcr1-terminated genes)
PMID:25417108	FYPO:0004812	(comment: affecting highly transcribed genes, antisense transcription of tDNA and rDNA)
PMID:25417108	FYPO:0004818	(comment: affecting antisense transcription at tDNA)
PMID:25417108	FYPO:0004813	(comment: affecting highly transcribed genes, antisense transcription of tDNA and rDNA)
PMID:25417108	GO:0006369	(comment: occurs at rDNA, tRNA gene, protein coding gene)
PMID:25417108	FYPO:0004817	(comment: affecting antisense transcription at rDNA)
PMID:25417108	FYPO:0004814	(comment: affecting highly transcribed genes, antisense transcription of tDNA and rDNA)
PMID:25417108	PBO:0095377	(comment: occurs at tDNA)
PMID:25417108	GO:0006363	(comment: occurs at rDNA, tRNA gene, protein coding gene)
PMID:25417108	GO:0006386	(comment: occurs at rDNA, tRNA gene, protein coding gene)
PMID:25417108	FYPO:0004820	(comment: Affecting Rad52 enrichment at rDNA)
PMID:25428589	PBO:0096774	We identified a consensus DSR motif for Mmi1 binding at position þ820 nt within the nc-tgp1 transcript and RNA IP (RIP) experiments confirmed a direct interaction between Mmi1 and the nc-tgp1 RNA (Supplementary Fig. 5).
PMID:25428589	PBO:0096776	In addition, the transcript levels of tgp1þ, nc-tgp1, nc-1343, pho1þ and nc-pho1 were unaffected by loss of RNAi (for example, ago1D or dcr1D) or heterochromatin components (for example, clr4D or swi6D) (Fig. 5b; Supplementary Fig. 7a
PMID:25428589	PBO:0096778	In addition, the transcript levels of tgp1þ, nc-tgp1, nc-1343, pho1þ and nc-pho1 were unaffected by loss of RNAi (for example, ago1D or dcr1D) or heterochromatin components (for example, clr4D or swi6D) (Fig. 5b; Supplementary Fig. 7a
PMID:25428589	PBO:0096772	The size and levels of the nc-1343 transcript increased in exosome defective (rrp6D) cells, but not cells lacking Mmi1 or Red1 (Fig. 2c,d; Supplementary Fig. 4). T
PMID:25428589	FYPO:0004161	In agreement with this, significantly less RNAPII associates with the nc-tgp1 transcription unit in both phosphate-starved wild-type cells and phosphate-replete 1343D cells, which do not transcribe nc-tgp1 (Fig. 4c).
PMID:25428589	PBO:0093562	prevented nc-tgp1 transcription, induced tgp1þ expression to levels observed in 1343D levels and increased sensitivity of these cells to TBZ, HU and caffeine (Fig. 3b,c). These analyses demonstrate that it is nc-tgp1, not nc-1343, that is critical for repressing tgp1þ in the presence of phosphate.
PMID:25428589	FYPO:0000964	Truncations of nc-1343 (that is, AD and BD) that retain its 50 end did not result in the drug-sensitivity phenotype presented by 1343D cells (Fig. 3b) and, similarly, did not induce tgp1þ expression (Fig. 3c)
PMID:25428589	PBO:0096775	Northern analysis identified that an B1.9kb nc-tgp1 RNA accumulates in rrp6D, mmi1D and red1D, but not in wild-type cells (Fig. 2e,f; Supplementary Fig. 4).
PMID:25428589	PBO:0096775	Northern analysis identified that an B1.9kb nc-tgp1 RNA accumulates in rrp6D, mmi1D and red1D, but not in wild-type cells (Fig. 2e,f; Supplementary Fig. 4).
PMID:25428589	FYPO:0000964	Truncations of nc-1343 (that is, AD and BD) that retain its 50 end did not result in the drug-sensitivity phenotype presented by 1343D cells (Fig. 3b) and, similarly, did not induce tgp1þ expression (Fig. 3c)
PMID:25428589	PBO:0096775	Northern analysis identified that an B1.9kb nc-tgp1 RNA accumulates in rrp6D, mmi1D and red1D, but not in wild-type cells (Fig. 2e,f; Supplementary Fig. 4).
PMID:25428589	PBO:0111000	We therefore conclude that tgp1(+) is regulated by transcriptional interference.
PMID:25428589	PBO:0096780	Our ChIP analyses confirmed that Pho7-green fluorescent protein (Pho7-GFP) accumulates on the pho1 þ promoter in phosphate- depleted cells (Supplementary Fig. 8). In addition, Pho7-GFP levels accumulate over the region upstream of tgp1þ when activated (Fig. 6a
PMID:25428589	PBO:0096779	In contrast, nc-tgp1, nc-pho1 and sme2þ RNA levels were clearly elevated in cells lacking Mmi1-mediated exosome degradation (mmi1D and rrp6D). Th
PMID:25428589	PBO:0096776	In addition, the transcript levels of tgp1þ, nc-tgp1, nc-1343, pho1þ and nc-pho1 were unaffected by loss of RNAi (for example, ago1D or dcr1D) or heterochromatin components (for example, clr4D or swi6D) (Fig. 5b; Supplementary Fig. 7a
PMID:25428589	PBO:0096776	In addition, the transcript levels of tgp1þ, nc-tgp1, nc-1343, pho1þ and nc-pho1 were unaffected by loss of RNAi (for example, ago1D or dcr1D) or heterochromatin components (for example, clr4D or swi6D) (Fig. 5b; Supplementary Fig. 7a
PMID:25428589	PBO:0096776	In addition, the transcript levels of tgp1þ, nc-tgp1, nc-1343, pho1þ and nc-pho1 were unaffected by loss of RNAi (for example, ago1D or dcr1D) or heterochromatin components (for example, clr4D or swi6D) (Fig. 5b; Supplementary Fig. 7a
PMID:25428589	PBO:0093562	Cells lacking SPNCRNA.1343 (ncRNA.1343 for short) displayed a phenotype: hypersensitivity to TBZ, HU and caffeine but not to temperature extremities, ultraviolet-irradiation or oxidative stress (Supplementary Fig. 1c and Supplementary Fig. 2).
PMID:25428589	PBO:0096769	(repressed condition; Fig. 1c)
PMID:25428589	PBO:0096770	To determine whether the drug sensitivity of 1343D cells is a direct result of increased tgp1þ expression, the tgp1þ gene was deleted from 1343D cells (tgp1D1343D). This manipulation restored TBZ, HU and caffeine tolerance to levels comparable with wild-type cells (Fig. 1d). We conclude that increased tgp1þ expression is directly responsible for the drug-sensitivity phenotype of cells lacking ncRNA.1343.
PMID:25428589	PBO:0096772	The size and levels of the nc-1343 transcript increased in exosome defective (rrp6D) cells, but not cells lacking Mmi1 or Red1 (Fig. 2c,d; Supplementary Fig. 4). T
PMID:25428589	PBO:0096773	The size and levels of the nc-1343 transcript increased in exosome defective (rrp6D) cells, but not cells lacking Mmi1 or Red1 (Fig. 2c,d; Supplementary Fig. 4). T
PMID:25428987	PBO:0020227	(comment: CHECK mitotic interphase)
PMID:25451933	FYPO:0007573	As a result, ring constriction in Δaip1 cells takes ∼ 5 min less than in wild type cells (Table 3). Overall, cytokinesis was ∼16 min (24%) faster in Δaip1 cells than wild type cells, because the maturation period was shorter and the rings constricted faster.
PMID:25451933	FYPO:0007573	Surprisingly, contractile rings began to constrict earlier in Δaip1 cells than wild type cells (Fig. 7, A and B, and Table 3), foreshortening the maturation period before constriction
PMID:25451933	FYPO:0006187	(Figs. 6B and C, Table 3)
PMID:25451933	FYPO:0001366	The fission yeast lacking Aip1 have normal appearing actin patches, cables, and contractile rings (Fig. 5B).
PMID:25451933	GO:0051014	SpAip1 dramatically stimulated severing by 100 nM cofilin, with a maximum rate at 1.5 μM SpAip1 and lower rates at higher concentrations (Fig. 3C).At all SpAip1 concentrations tested ∼80% of new barbed ends created by severing events depolymerized (Fig. 3D) at rates that decreased insignificantly with SpAip1 concentration (Fig. 3E). These depolymerization rates were higher than published values (2), likely because severing near barbed ends was difficult to distinguish from filament depolymerization.
PMID:25451933	GO:0003786	(comment: competatively with cofilin)
PMID:25471935	FYPO:0005764	(comment: assayed Cdc20 recruitment)
PMID:25472718	PBO:0101240	In any case, the results shown here imply that Klp5-Klp6 localises to the kinetochores through interaction with the Alp7-Alp14 complex.
PMID:25472718	PBO:0101233	(Fig. 4E) reduced by >70%
PMID:25472718	FYPO:0001905	(Fig. 4C,D)
PMID:25472718	PBO:0101234	(Fig. 4A,B)
PMID:25472718	PBO:0101235	(Fig. 4A,B)
PMID:25472718	FYPO:0000674	(Fig. 1A)
PMID:25472718	PBO:0093561	(Fig. 1A)
PMID:25472718	PBO:0101236	(Fig. 1C-E) (comment: Type I)
PMID:25472718	PBO:0101232	(Fig. 3d)
PMID:25472718	FYPO:0001387	(Fig. 2A)
PMID:25472718	PBO:0101231	(Fig. 2C,D)
PMID:25472718	PBO:0101237	(Fig. 1C-E) (comment: Type I)
PMID:25472718	PBO:0101238	(Fig. 1C-E) (comment: Type I)
PMID:25472718	PBO:0037884	(Fig. 1A)
PMID:25472718	FYPO:0002061	(supplementary material Fig. S1A
PMID:25472718	FYPO:0000674	(Fig. 2A)
PMID:25472718	PBO:0093556	(Fig. 2A)
PMID:25472718	FYPO:0001387	(Fig. S2B)
PMID:25472718	FYPO:0001387	(Fig. S2B)
PMID:25472718	PBO:0101239	Overall, our data suggest that Klp5-Klp6 delivers PP1 to the attached kinetochores, thereby promoting SAC silencing.
PMID:25472718	PBO:0101239	Overall, our data suggest that Klp5-Klp6 delivers PP1 to the attached kinetochores, thereby promoting SAC silencing.
PMID:25472718	PBO:0101240	In any case, the results shown here imply that Klp5-Klp6 localises to the kinetochores through interaction with the Alp7-Alp14 complex.
PMID:25472718	PBO:0035594	(Fig. 1C; Fig. 3D)
PMID:25472718	FYPO:0000674	(Fig. 3A)
PMID:25472718	FYPO:0000674	(Fig. 3A)
PMID:25472718	FYPO:0000674	(Fig. 3A)
PMID:25472718	PBO:0097264	(Fig. 3A)
PMID:25472718	PBO:0097264	(Fig. 3C)
PMID:25472718	FYPO:0006259	(Fig. 5D)
PMID:25472718	FYPO:0004307	(Fig. 5D)
PMID:25472718	PBO:0101242	(Fig. 5A)
PMID:25472718	FYPO:0004310	(Fig. 5A)
PMID:25472718	FYPO:0001387	(Fig. 5A)
PMID:25472718	PBO:0101233	(Fig. 4E) reduced by >70%
PMID:25472718	PBO:0094476	(Fig. 1C; Fig. 3D)
PMID:25473118	PBO:0018576	(comment: independent of actin)
PMID:25473118	FYPO:0003339	the ring seems to start off forming normally but maturation is delayed, this leads to delayed constriction.
PMID:25473118	PBO:0102105	(Fig. 6)
PMID:25473118	PBO:0102181	(Fig. 6)
PMID:25487150	GO:0005515	(comment: unphosphorylated form)
PMID:25500221	PBO:0099955	(comment: secretion of acid phosphatase)
PMID:25500221	PBO:0099955	(comment: secretion of acid phosphatase)
PMID:25501814	PBO:0107513	Cdc7p-GFP never disappeared from the old SPB (Sohrmann et al., 1998) and the type 1 nodes did not reform (Fig. 3B; supplementary material Movie 3)
PMID:25501814	PBO:0107512	(Fig. 2g)
PMID:25501814	PBO:0099316	(Fig. 1)
PMID:25501814	PBO:0018634	(Fig. 1)
PMID:25501814	PBO:0023023	(Fig. 1)
PMID:25501814	PBO:0107514	(Fig. 3C).
PMID:25501814	PBO:0018845	(Fig. 1)
PMID:25501814	PBO:0018845	(Fig. 1)
PMID:25501814	PBO:0107511	(Fig. 1c)
PMID:25501814	PBO:0107510	(Fig. 1)
PMID:25519804	PBO:0106417	(comment: CHECK high suppression of phenotype)
PMID:25519804	PBO:0106418	(comment: low suppression of phenotype)
PMID:25519804	FYPO:0003911	(comment: suppresses ade6-M26 efficiently; suppresses ade6-M375 weakly)
PMID:25519804	FYPO:0003911	(comment: efficient suppression of ade6-M26; very poor suppression of ade6-M375)
PMID:25519804	PBO:0106417	(comment: CHECK high suppression of phenotype)
PMID:25520186	MOD:00047	(comment: Auto-phosphorylation occurred in the presence of ATP in vitro)
PMID:25520186	MOD:00046	(comment: Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro)
PMID:25520186	PBO:0097184	(comment: CHECK full-length Cut14 present; not sure how to interpret this)
PMID:25520186	PBO:0097184	(comment: CHECK full-length Cut14 present; not sure how to interpret this)
PMID:25520186	FYPO:0002060	(comment: only captured the OEX Experiment)
PMID:25520186	PBO:0097183	(comment: of condensin complex)
PMID:25520186	FYPO:0002061	(comment: only captured the OEX experiment)
PMID:25520186	PBO:0097182	(comment: of condensin complex)
PMID:25520186	MOD:00047	(comment: Auto-phosphorylation occurred in the presence of ATP in vitro)
PMID:25520186	MOD:00046	(comment: Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro)
PMID:25520186	MOD:00047	(comment: Auto-phosphorylation occurred in the presence of ATP in vitro)
PMID:25520186	PBO:0097184	(comment: CHECK full-length Cut14 present; not sure how to interpret this)
PMID:25520186	MOD:00047	(comment: Auto-phosphorylation occurred in the presence of ATP in vitro)
PMID:25520186	MOD:00047	(comment: Auto-phosphorylation occurred in the presence of ATP in vitro)
PMID:25520186	MOD:00583	(comment: Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro)
PMID:25520186	MOD:00046	(comment: Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro)
PMID:25520186	MOD:00046	(comment: Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro)
PMID:25520186	MOD:00046	(comment: Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro)
PMID:25520186	MOD:00046	(comment: Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro)
PMID:25520186	MOD:00046	(comment: Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro)
PMID:25533340	PBO:0103465	(comment: CHECK phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining T180)
PMID:25533340	PBO:0022125	(comment: This looks like direct regulation because it phosphorylates xlf1)
PMID:25533340	FYPO:0003584	(comment: CHECK increased end-joining activity in vegetative cells)
PMID:25533340	FYPO:0000482	(comment: leu1)
PMID:25533340	PBO:0103462	(comment: CHECK phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining S192)
PMID:25533340	PBO:0103463	(comment: CHECK phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining S192)
PMID:25533340	PBO:0103464	(comment: CHECK phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining T180)
PMID:25533348	PBO:0098717	(Fig. 3A)
PMID:25533348	PBO:0033097	(comment: WT 3%)
PMID:25533348	PBO:0098707	(comment: greater range of lengths)
PMID:25533348	PBO:0098708	(comment: greater range of lengths)
PMID:25533348	PBO:0098707	(comment: greater range of lengths)
PMID:25533348	PBO:0098727	(Fig. 3A)
PMID:25533348	PBO:0098726	(Fig. 3A)
PMID:25533348	PBO:0098725	(Fig. 3A)
PMID:25533348	PBO:0098724	(Fig. 3A)
PMID:25533348	PBO:0098723	(Fig. 3A)
PMID:25533348	PBO:0098722	(Fig. 3A)
PMID:25533348	PBO:0098721	(Fig. 3A)
PMID:25533348	PBO:0098720	(Fig. 3A)
PMID:25533348	PBO:0098719	(Fig. 3A)
PMID:25533348	PBO:0098718	(Fig. 3A)
PMID:25533348	PBO:0098715	(comment: WT 3%)
PMID:25533348	PBO:0033099	(comment: WT 3%)
PMID:25533348	PBO:0033098	(comment: WT 3%)
PMID:25533956	PBO:0105398	(Fig. 5e)
PMID:25533956	PBO:0105397	(Fig. 5e)
PMID:25533956	PBO:0105399	(comment: RECRUITS)
PMID:25543137	PBO:0023812	Cytoplasmic localisation in electron-dense inclusions at 37°C
PMID:25543137	GO:0042026	hsp104 refolds dicer and is required for robust centromeric silencing at 37°C
PMID:25543137	PBO:0104383	Dcr1 represses hsp104 levels
PMID:25543137	GO:0005737	Diffuse cytoplasmic localisation at 37°C, no stress granules
PMID:25543137	FYPO:0004808	A prionogenic reporter (S. cerevisiae Sup35 prion domain) aggregates in cytoplasmic inclusions in dcr1Δ
PMID:25543137	GO:0005634	Nuclear localization at 30°C
PMID:25543137	GO:0005634	Nuclear localization at 30°C
PMID:25543137	PBO:0023812	Dcr1 localizes in electron-dense cytoplasmic inclusions at 37°C together with hsp104. Hsp104 is required for dissolution of these inclusions.
PMID:25543137	PBO:0104384	Dcr1 is not released from cytoplasmic inclusions at 37°C in hsp104Δ
PMID:25590601	PBO:0023217	(comment: CHECK removed during nitrogen starvation) (comment: T415)
PMID:25590601	PBO:0023218	(comment: in the presence of glucose)
PMID:25590601	PBO:0023215	(comment: CHECK removed during glucose starvation) (comment: CHECK observed during nitrogen starvation) (comment: CHECK S546)
PMID:25590601	PBO:0101537	(comment: decreased during glucose starvation)
PMID:25590601	PBO:0101539	(comment: CHECK strong phenotype = has_severity(FYPO_EXT:0000001))
PMID:25590601	PBO:0023214	(comment: CHECK removed during glucose starvation) (comment: CHECK observed during nitrogen starvation) (comment: CHECK S546)
PMID:25590601	PBO:0023216	(comment: CHECK removed during glucose starvation) (comment: CHECK observed during nitrogen starvation) (comment: CHECK S546)
PMID:25619765	FYPO:0000227	(comment: cen2-lacO)
PMID:25619765	FYPO:0000227	(comment: pNBg was used)
PMID:25619998	GO:1990189	(Figure S2)
PMID:25619998	PBO:0116841	(Figure S2)
PMID:25619998	PBO:0116840	(Figure S2)
PMID:25639242	PBO:0101663	(comment: CHECK causally upstream of ssp2)
PMID:25639242	FYPO:0007434	(Fig. 3C)
PMID:25639242	FYPO:0007434	(Figure 4D)
PMID:25639242	PBO:0101653	(Figure 2D,4B)
PMID:25639242	PBO:0101653	(Fig. 4C)
PMID:25639242	FYPO:0007434	(Figure 2a)
PMID:25639242	FYPO:0007434	(Figure 3B)
PMID:25639242	PBO:0101659	However, no difference in CaMKKSsp1 protein levels or phos- ppk34 phorylation status was observed in CaMKK .D mutants compared with wild-type cells (Figures S4A and S4B
PMID:25639242	PBO:0101657	(Figure 5a)
PMID:25639242	FYPO:0002673	(Figure S3A)
PMID:25639242	PBO:0101653	(Figure 4C)
PMID:25639242	FYPO:0007434	(Fig. 3G)
PMID:25639242	FYPO:0007434	(Figure 3d)
PMID:25639242	FYPO:0007434	(Figure 4E)
PMID:25639242	FYPO:0007434	(Figure 4D)
PMID:25639242	PBO:0101661	An increase in AMPKaSsp2 Thr189 phosphorylation was also observed in the cbs2 .D AMPKg .D double mutant (Figure S2F).
PMID:25639242	FYPO:0007434	(Figure 3F) (comment: DECOUPLED CELL GROWTH AND DIVISION)
PMID:25639242	FYPO:0005206	(Figure 3F)
PMID:25639242	PBO:0101656	(Figure S2)
PMID:25639242	PBO:0101654	(Figure S2B)
PMID:25639242	PBO:0101660	(Fig. 6A)
PMID:25639242	FYPO:0007434	(Figure 6E)
PMID:25639242	PBO:0037529	(comment: CHECK causally upstream of ssp2)
PMID:25639242	FYPO:0007434	(Figure 6E)
PMID:25639242	FYPO:0007434	(Figure 2a)
PMID:25639242	PBO:0093770	(Figure 2b) (comment: 9% longer)
PMID:25639242	PBO:0101662	However, no difference in CaMKKSsp1 protein levels or phos- ppk34 phorylation status was observed in CaMKK .D mutants compared with wild-type cells (Figures S4A and S4B
PMID:25639242	PBO:0101659	(Fig. S4C,D)
PMID:25639242	PBO:0101660	(Fig. 6G)
PMID:25688133	PBO:0108656	(comment: residues 20â€-40 in synthetic peptide/ dissociation constant of 1.1 nM)
PMID:25688133	PBO:0096493	(comment: smears as does not self associate, but localizes to medial cortex)
PMID:25688133	GO:1990808	(comment: residues 20â€-40 in synthetic peptide/ dissociation constant of 1.1 nM)
PMID:25688133	FYPO:0000729	(comment: 23% slower)
PMID:25688133	FYPO:0000729	(comment: 26% slower)
PMID:25736293	PBO:0107632	(Fig. S1B)
PMID:25736293	FYPO:0000927	(Fig. 5c)
PMID:25736293	PBO:0107634	(Fig. 1C; supplementary material Fig. S1C)
PMID:25736293	PBO:0107634	(Fig. 1C; supplementary material Fig. S1C)
PMID:25736293	GO:0005515	(Figure S2)
PMID:25736293	GO:0005515	(Figure S2)
PMID:25736293	PBO:0107635	(Figure S2C)
PMID:25736293	PBO:0107635	(Figure S2C)
PMID:25736293	PBO:0107641	(Fig. S4B)
PMID:25736293	PBO:0107640	(Fig. S4B)
PMID:25736293	FYPO:0002177	(Fig. S1B)
PMID:25736293	PBO:0107639	(Fig. S4A)
PMID:25736293	PBO:0107644	(Fig. 6a)
PMID:25736293	PBO:0107639	(Fig. S4A)
PMID:25736293	PBO:0107645	abnormal movement of dynein
PMID:25736293	PBO:0107644	(Fig. 6a)
PMID:25736293	PBO:0107634	(Fig. 1C; supplementary material Fig. S1C)
PMID:25736293	FYPO:0005988	(Fig. 5c)
PMID:25736293	PBO:0107643	(Fig. S4B)
PMID:25736293	PBO:0107646	abnormal movement of dynein
PMID:25736293	PBO:0107647	(Fig. 7a)
PMID:25736293	PBO:0107632	(Fig. 7a)
PMID:25736293	PBO:0107642	(Fig. S4B)
PMID:25736293	GO:1903754	(Fig. 5C)
PMID:25736293	FYPO:0000964	(Fig. S1B)
PMID:25736293	FYPO:0000964	(Fig. S1B)
PMID:25736293	FYPO:0000964	(Fig. S1B)
PMID:25736293	FYPO:0002177	(Fig. S1B)
PMID:25736293	FYPO:0002177	(Fig. S1B)
PMID:25736293	GO:0035974	(Fig. 5C)
PMID:25736293	FYPO:0005988	(comment: CHECK 3B?)
PMID:25736293	PBO:0107637	(comment: CHECK microtubule cortical anchor (microtubule site clamp) add to other dynactin complex)
PMID:25736293	PBO:0107637	(comment: CHECK microtubule cortical anchor (microtubule site clamp) add to other dynactin complex)
PMID:25736293	PBO:0107637	(comment: CHECK microtubule cortical anchor (microtubule site clamp) add to other dynactin complex)
PMID:25736293	FYPO:0000903	(Fig. 7F; supplementary material Table S1)
PMID:25736293	FYPO:0000903	(Fig. 7F; supplementary material Table S1)
PMID:25736293	FYPO:0000903	(Fig. 7F; supplementary material Table S1)
PMID:25736293	FYPO:0000964	(Fig. S1B)
PMID:25736293	PBO:0107632	(Fig. S1B)
PMID:25736293	PBO:0107633	(Fig. S1B)
PMID:25736293	GO:0005938	(comment: accumulates on shrinking microtubules) (Fig. 2B)
PMID:25736293	GO:0035974	accumulates on shrinking microtubules (Fig. 2B)
PMID:25736293	PBO:0107633	(Fig. S1B)
PMID:25736293	GO:1903754	accumulates on shrinking microtubules (Fig. 2B)
PMID:25736293	PBO:0107636	(Fig. 7A)
PMID:25736293	FYPO:0000903	(Fig. 7F; supplementary material Table S1)
PMID:25736293	FYPO:0000903	(Fig. 7F; supplementary material Table S1)
PMID:25736293	PBO:0107638	(Fig. S4A)
PMID:25736293	PBO:0107638	(Fig. S4A)
PMID:25736293	GO:0051285	(Fig. 4A)
PMID:25736293	FYPO:0005990	(Fig. 3B, Fig. S3B) abolished microtubule cortical anchoring
PMID:25736293	PBO:0107637	(comment: CHECK microtubule cortical anchor (microtubule site clamp) add to other dynactin complex)
PMID:25736293	PBO:0107636	(Fig. 3B, Fig. S3B)
PMID:25763975	FYPO:0003302	To test these theoretical predictions, we measured the movements of the nucleus and of the SPB in a klp5Δ strain, which lacks the kinesin-8 motor Klp5 [Fig. 2(d)]. We observed that the nucleus is typically found farther away from the cell center in klp5Δ than in wild-type cells, as shown by the 1.7-fold larger standard deviation of the distribution of the nuclear position in klp5Δ cells, which is consistent with the prediction of the model [Figs. 2(b)
PMID:25763975	FYPO:0005872	Similarly, the division plane was positioned more asymmetrically in klp5Δ cells than in wild-type cells [Fig. 2(g)].
PMID:25778919	PBO:0108458	(Fig. 3D)
PMID:25778919	PBO:0108453	(Fig. 2A, 0-3 min, arrows)
PMID:25778919	PBO:0108462	(Fig. 7)
PMID:25778919	PBO:0108461	(Fig. 6)
PMID:25778919	FYPO:0005343	(Fig. 2D)
PMID:25778919	PBO:0108462	(Fig. 6)
PMID:25778919	FYPO:0004330	(Fig. S4A)
PMID:25778919	FYPO:0006267	(Fig. 4) (comment: decreased telomere dispersion)
PMID:25778919	PBO:0108456	(Fig. 2C, 2D) (comment: decreased telomere dispersion)
PMID:25778919	PBO:0108457	(Fig. 3)
PMID:25778919	FYPO:0005442	(Fig. 2C, 2D)
PMID:25778919	PBO:0108455	(Fig.S2A)
PMID:25778919	PBO:0108454	(comment: telomere disjunction)
PMID:25778919	GO:0120110	(comment: CHECK (requested negative regulation of) synonym mitotic telomere dispersion during metaphase)
PMID:25778919	FYPO:0006267	(Fig. 4) (comment: decreased telomere dispersion)
PMID:25778919	PBO:0108459	(Fig. 3)
PMID:25778919	PBO:0108460	(Fig. 5A)
PMID:25778919	GO:0044820	Together, these experiments suggest that Aurora-dependent removal of Swi6/HP1 and consequently cohesin Rad21 from telomeres in early mitosis contributes to telomere dispersion.
PMID:25778919	GO:0044820	Together, these experiments suggest that Aurora-dependent removal of Swi6/HP1 and consequently cohesin Rad21 from telomeres in early mitosis contributes to telomere dispersion.
PMID:25778919	FYPO:0006264	(Fig. 4)
PMID:25793410	FYPO:0002344	(comment: CONDITION Sensitivity was rescued less efficiently than for the wt by 150 - 600 mM KCl)
PMID:25793410	FYPO:0004752	(comment: CONDITION 10 ug/ml phleomycin for 4 h followed by recovery on YES)
PMID:25793410	FYPO:0001719	(comment: CONDITION Sensitivity was rescued by 0.6 M KCl 4 mM lithium for 4 h followed by recovery on YES)
PMID:25793410	FYPO:0002344	(comment: CONDITION Sensitivity was rescued by 0.6 M KCl, 10 ug/ml phleomycin for 4 h followed by recovery on YES)
PMID:25793410	FYPO:0000633	(comment: CONDITION 10 ug/ml G418 for 4 h followed by recovery on YES)
PMID:25793410	FYPO:0003559	(comment: CONDITION Sensitivity was rescued by 0.6 M KCl, 40 ug/ml doxorubicin for 4 h followed by recovery on YES)
PMID:25793410	FYPO:0003559	(comment: CONDITION Sensitivity was rescued by 0.6 M, but not 60 mM KCl, 40 ug/ml doxorubicin for 4 h followed by recovery on YES)
PMID:25793410	FYPO:0002344	(comment: CONDITION Sensitivity was rescued by 150 mM, but not 70 mM KCl, 10 ug/ml phleomycin for 4 h followed by recovery on YES)
PMID:25793410	PBO:0024650	Rad3-dependent phosphorylation of Chk1 is observed in the presence of phleomycin, but this is suppressed by KCl concentrations above 0.3 M
PMID:25793410	FYPO:0002344	(comment: CONDITION Sensitivity was rescued by 0.6 M KCl but not 60 mM KCl, 10 ug/ml phleomycin for 4 h followed by recovery on YES)
PMID:25793410	FYPO:0004751	(comment: CONDITION 100 ug/ml G418 for 4 h followed by recovery on YES)
PMID:25795664	PBO:0093617	spd1 deletion suppresses brc1delta csn1delta sensitivity to DNA damage agents
PMID:25795664	PBO:0093618	spd1 deletion suppresses brc1delta ddb1delta sensitivity to DNA damage agents
PMID:25795664	PBO:0093614	spd1 deletion suppresses brc1delta ddb1delta sensitivity to DNA damage agents
PMID:25795664	PBO:0093581	spd1 deletion suppresses brc1delta csn1delta sensitivity to DNA damage agents
PMID:25795664	PBO:0093630	spd1 deletion suppresses brc1delta csn1delta sensitivity to DNA damage agents
PMID:25795664	PBO:0093581	spd1 deletion suppresses brc1delta ddb1delta sensitivity to DNA damage agents
PMID:25795664	PBO:0093614	spd1 deletion suppresses brc1delta csn1delta sensitivity to DNA damage agents
PMID:25795664	PBO:0093631	spd1 deletion suppresses brc1delta ddb1delta sensitivity to DNA damage agents
PMID:25795664	FYPO:0001234	A spd1 deletion partially suppresses the synthetic growth defect in a brc1 ddb1 double mutant background
PMID:25795664	FYPO:0001234	A spd1 deletion partially suppresses the synthetic growth defect in a brc1 csn1 double mutant background
PMID:25798942	GO:0006338	ATPase domain mutant phenotype fig 5 and S6
PMID:25831549	FYPO:0004544	(Fig. 3D)
PMID:25831549	FYPO:0004544	(Fig. 3D)
PMID:25831549	FYPO:0004745	(Fig. 7E)
PMID:25831549	PBO:0098773	(Fig. 7E)
PMID:25831549	FYPO:0000887	(Fig. 7E)
PMID:25831549	FYPO:0004745	(Fig. 7D)
PMID:25831549	FYPO:0004745	(Fig. 7D)
PMID:25831549	FYPO:0007479	(Fig. 2)
PMID:25831549	FYPO:0004745	(Fig. 7D)
PMID:25831549	FYPO:0004544	(Fig. 3B)
PMID:25831549	GO:0031507	The deletion of epe1+, which encodes a putative histone H3K9 demethylase, did not affect the establishment of silencing. Fig. 2
PMID:25831549	FYPO:0004544	(Fig. 2A)
PMID:25831549	FYPO:0004544	(Fig. 3C)
PMID:25831549	GO:0033696	(Fig. 2)
PMID:25831549	FYPO:0007479	(Fig. 3E)
PMID:25837586	PBO:0103556	(comment: CHECK more severe in presence of LatA)
PMID:25837586	PBO:0103551	Increased levels of Cdc42 and Cdc42-GTP (CRIB)
PMID:25837586	PBO:0099084	Decreased levels of Cdc42 and Cdc42-GTP
PMID:25837586	PBO:0099084	Decreased levels of Cdc42 and Cdc42-GTP (CRIB)
PMID:25837586	PBO:0097265	Normal levels of Cdc42 and Cdc42-GTP (CRIB)
PMID:25837586	PBO:0103551	Increased levels of Cdc42 and Cdc42-GTP (CRIB)
PMID:25837586	PBO:0097265	Normal levels of Cdc42 and Cdc42-GTP (CRIB)
PMID:25837586	FYPO:0000672	(comment: Internally tagged functional allele, allowing live-imaging of Cdc42)
PMID:25837586	GO:0030427	(comment: CHECK Not affected by short-term actin cytoskeleton depolymerization by Latrunculin A)
PMID:25838386	FYPO:0002335	(Fig. S5)
PMID:25838386	FYPO:0002335	(Fig. S5)
PMID:25838386	FYPO:0002335	(Fig. S5)
PMID:25838386	FYPO:0004544	Catalytically inactivating mutations in the Fe(II) or 2-oxyglutarate binding sites of the Epe1 putative demethylase (epe1-H297A and epe1-K314A) had a similar phenotype (Fig. 4A, fig. S6, and table S3)
PMID:25838386	FYPO:0004544	Catalytically inactivating mutations in the Fe(II) or 2-oxyglutarate binding sites of the Epe1 putative demethylase (epe1-H297A and epe1-K314A) had a similar phenotype (Fig. 4A, fig. S6, and table S3)
PMID:25838386	FYPO:0004544	Of the eight tested mutants, only epe1D consistently formed red-pink colonies on +AHT plates, indicating that 4xtetO-ade6+ can remain repressed without bound TetR-Clr4* (Fig. 4A and figs. S5 and S6).
PMID:25838386	FYPO:0002335	(Fig. S5)
PMID:25838386	PBO:0112971	The analyses presented here are consistent with Epe1 normally acting as an H3K9 demethylase that removes H3K9 methylation from ectopic sites of heterochromatin formation.
PMID:25838386	FYPO:0002335	(Fig. S5)
PMID:25838386	FYPO:0002335	(Fig. S5)
PMID:25838386	FYPO:0002335	(Fig. S5)
PMID:25869666	PBO:0098123	(Fig. 4)
PMID:25869666	PBO:0098123	(Fig. 1)
PMID:25869666	PBO:0098123	(Fig. 4)
PMID:25869666	GO:0008569	Single deletion slows down nuclear congression (minus-end diretcted), double deletion with klp2 inhibits it.
PMID:25869666	PBO:0098121	(Fig. S3A)
PMID:25869666	GO:0000743	(comment: Phenocopies dhc1)
PMID:25869666	GO:0000743	Delayed nuclear congresion in klp2D (Fig. 1) and double deletion dhc1D klp2D completely abolishes nuclear congression (Fig. 1))
PMID:25869666	GO:0000743	Delayed nuclear congresion in dhc1D (Fig. 1) and double deletion dhc1D klp2D completely abolishes nuclear congression (Fig. 1))
PMID:25869666	PBO:0098122	(Fig. 1)
PMID:25869666	PBO:0098122	(Fig. 1)
PMID:25869666	GO:0008569	Single deletion slows down nuclear congression (minus-end diretcted), double deletion with dhc1 inhibits it.
PMID:25869666	PBO:0098123	(Fig. 1)
PMID:25869666	PBO:0098127	(Fig. 4)
PMID:25869666	PBO:0098124	(Fig. 1)
PMID:25869666	FYPO:0007162	(Fig. S1)
PMID:25869666	PBO:0098126	(Fig. 1)
PMID:25869666	PBO:0098125	(Fig. 1)
PMID:25891897	PBO:0033404	(comment: zygotic)
PMID:25891897	PBO:0033405	(comment: zygotic)
PMID:25891897	PBO:0033406	(comment: zygotic)
PMID:25891897	PBO:0033407	(comment: zygotic)
PMID:25891897	PBO:0033408	(comment: zygotic)
PMID:25891897	PBO:0033389	zygotic meiosis random spore analysis
PMID:25891897	FYPO:0003378	(comment: azygotic meiotic cell cyle)
PMID:25891897	PBO:0033390	zygotic meiosis random spore analysis
PMID:25891897	FYPO:0003379	azygotic meiotic cell cycle/timing of pre-meiotic DNA replication is normal
PMID:25891897	PBO:0033397	zygotic meiosis random spore analysis
PMID:25891897	PBO:0033399	zygotic random spore analysis
PMID:25891897	PBO:0033398	(comment: zygotic)
PMID:25891897	PBO:0033400	(comment: zygotic)
PMID:25891897	FYPO:0000478	zygotic / >80% of asci have 4 spores
PMID:25891897	PBO:0033401	zygotic/ random spore analysis
PMID:25891897	FYPO:0000478	azygotic/ slight advance in the timing of MI and MII
PMID:25891897	FYPO:0000478	zygotic//presence of 4x fusion protein restores the ability of cig1 cig2 puc1 rem1 quadruple deletion strain to undergo pre meiotic DNA replication
PMID:25891897	FYPO:0000478	azygotic// presence of 4x fusion protein restores the ability of cig1 cig2 puc1 rem1 quadruple deletion strain to undergo pre meiotic DNA replication
PMID:25891897	FYPO:0000478	(comment: azygotic)
PMID:25891897	PBO:0033402	(comment: zygotic meiosis)
PMID:25891897	PBO:0033403	zygotic meiosis/ Random spore analysis
PMID:25891897	FYPO:0000478	azygotic meiosis, rem1 and crs1 do not have a major role in azygotic meiosis
PMID:25891897	FYPO:0000478	(comment: zygotic)
PMID:25891897	FYPO:0003563	azygotic/ slight advance in the timing of MI and MII
PMID:25891897	PBO:0033332	(comment: zygotic)
PMID:25891897	PBO:0033391	zygotic meiosis random spore analysis
PMID:25891897	PBO:0033392	(comment: This phenotype is not seen when cells undergo azygotic meiosis)
PMID:25891897	FYPO:0004608	presence of more than 2 SPBs dots after meiotic nuclear divisions 19.6% zygotes exhibit abnormal meiotic division during zygotic meiosis
PMID:25891897	PBO:0033394	zygotic meiosis random spore analysis
PMID:25891897	PBO:0033395	(comment: zygotic)
PMID:25891897	PBO:0033396	(comment: zygotic)
PMID:25959226	PBO:0098839	Mutations of the hydrophobic C2-C2 interface shifted Mid1 into monomeric state (Figure 6A)
PMID:25959226	FYPO:0006005	Indeed, the morphology and positioning of the contractile ring marked with myosin regulatory light chain Rlc1 were normal in mid13A cells (Figure S6, C-D)
PMID:25959226	PBO:0098841	In contrast, monomerization only slightly reduced the affinity to PS.
PMID:25959226	PBO:0098840	which showed > 10-fold lower affinity to PI(4,5)P2 (Figure 3D).
PMID:25959226	FYPO:0000339	which interacts with the N-terminus of Mid1 and stabilizes Mid1 at the division plane (Ye et al., 2012; Zhu et al., 2013). As expected, mid13A gef2Δ double mutants had strong synthetic defects in division-plane placement and septum formation at 36°C (Figure 6, F-H).
PMID:25959226	FYPO:0006186	However, contractile ring assembly was significantly faster in mid13A than in mid1+ cells (Figure S6, C-F)
PMID:25959226	FYPO:0004456	In contrast, the monomeric Mid13A remained concentrated in the nucleus and its signals on the plasma membrane were more widespread, even reached the cell poles (Figure 6E
PMID:25959226	FYPO:0000339	which interacts with the N-terminus of Mid1 and stabilizes Mid1 at the division plane (Ye et al., 2012; Zhu et al., 2013). As expected, mid13A gef2Δ double mutants had strong synthetic defects in division-plane placement and septum formation at 36°C (Figure 6, F-H).
PMID:25959226	GO:0005546	Interestingly, it binds to PI(4,5)P2 strongly, with a Kd up to 0.12 μM (Figure 3C, 3D).
PMID:25965521	FYPO:0000085	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000089	(comment: same as brc1delta alone; brc1 epistatic)
PMID:25965521	PBO:0093579	(comment: same as brc1delta alone; brc1 epistatic)
PMID:25965521	PBO:0093615	(comment: same as brc1delta alone; brc1 epistatic
PMID:25965521	PBO:0093618	(comment: same as brc1delta alone; brc1 epistatic)
PMID:25965521	PBO:0093631	(comment: same as brc1delta alone; brc1 epistatic)
PMID:25965521	FYPO:0000088	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000085	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000089	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000268	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000088	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000085	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000089	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000268	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000088	same as mus81delta alone; mus81 epistatic
PMID:25965521	FYPO:0000089	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000268	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000088	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000085	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000089	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000268	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0002573	(comment: same as either single mutant)
PMID:25965521	FYPO:0002573	(comment: same as either single mutant)
PMID:25965521	PBO:0093579	(comment: same as brc1delta alone; brc1 epistatic)
PMID:25965521	PBO:0093615	(comment: same as brc1delta alone; brc1 epistatic)
PMID:25965521	PBO:0093631	(comment: same as brc1delta alone; brc1 epistatic)
PMID:25965521	PBO:0093618	(comment: same as brc1delta alone; brc1 epistatic)
PMID:25977474	FYPO:0000032	(comment: abnormal cleavage furrow disc formation) Fig 3
PMID:25977474	FYPO:0000032	(comment: abnormal cleavage furrow disc formation) Fig 3
PMID:25977474	FYPO:0000032	(comment: abnormal cleavage furrow disc formation) Fig 3
PMID:25977474	FYPO:0000032	(comment: abnormal cleavage furrow disc formation) Fig 3
PMID:25977474	FYPO:0000032	(comment: abnormal cleavage furrow disc formation) Fig 3
PMID:25987607	PBO:0018346	(comment: CHECK during mitotic M phase)
PMID:25987607	PBO:0018346	(comment: CHECK during mitotic M phase)
PMID:25987607	FYPO:0003787	(comment: non additive)
PMID:25987607	FYPO:0006173	(Fig. 5B and Videos 1-4)
PMID:25987607	PBO:0108312	(Fig. 5B and Videos 1-4)
PMID:25987607	PBO:0108308	(comment: I want to represent the microtubule based-transporter function and cargo)
PMID:25987607	FYPO:0004396	(comment: I think the pkl rigor is spb tethered here?)
PMID:25987607	PBO:0108309	(comment: I want to represent the microtubule based-transporter function and cargo)
PMID:25987607	FYPO:0002636	(Fig. 5B and Videos 1-4)
PMID:25987607	PBO:0108310	(Fig. 5B and Videos 1-4)
PMID:25987607	PBO:0018346	(comment: CHECK during mitotic M phase)
PMID:25989903	FYPO:0008152	Surprisingly, deletion of the S. pombe Trf4/5 orthologue, cid14, showed only a minor effect on CUTs at a genome-wide level (Fig. 2a,b)
PMID:25989903	FYPO:0002960	Deletion of iss10 or mmi1 only affects meiotic mRNAs
PMID:25989903	GO:0071031	meiotic genes ....Overall, our experiments show that the MTREC complex is specifically recruited to CUTs and meiotic mRNAs, and it plays a key role in their degradation by the nuclear exosome.
PMID:25989903	GO:0071039	(comment: exosome dependent)
PMID:25989903	FYPO:0008113	Similar to previous reports, we detected significantly increased intronic reads in the exosome mutant rrp6D strain (Fig. 4a,b).
PMID:25989903	FYPO:0002960	In contrast, deletion or mutation alleles of the MTREC complex lead to significant accumulation of all types of CUTs and also meiotic mRNAs. This effect is comparable to the level of CUT accumulation in the nuclear exosome subunit rrp6 deletion (Fig. 2a,b)
PMID:25989903	FYPO:0002960	In contrast, deletion or mutation alleles of the MTREC complex lead to significant accumulation of all types of CUTs and also meiotic mRNAs. This effect is comparable to the level of CUT accumulation in the nuclear exosome subunit rrp6 deletion (Fig. 2a,b)
PMID:25989903	FYPO:0008113	Similar to previous reports, we detected significantly increased intronic reads in the exosome mutant rrp6D strain (Fig. 4a,b).
PMID:25989903	FYPO:0008113	Similar to previous reports, we detected significantly increased intronic reads in the exosome mutant rrp6D strain (Fig. 4a,b).
PMID:25989903	PBO:0110921	Similar to previous reports, we detected significantly increased intronic reads in the exosome mutant rrp6D strain (Fig. 4a,b).
PMID:25989903	GO:0071030	This analysis revealed that in the ctr1D or nrl1D mutant strains, both the intronic and also the surrounding exonic sequence coverage showed similar increases, while the expression of genes without introns was unaffected (Supplementary Fig. 4c,d). This result strongly suggests that the elevated level of intronic reads in the mutant strains is the consequence of the inefficient degradation of unspliced or mis-
PMID:25989903	GO:0071030	(comment: exosome dependent)
PMID:25989903	PBO:0110921	Similar to previous reports, we detected significantly increased intronic reads in the exosome mutant rrp6D strain (Fig. 4a,b).
PMID:25989903	FYPO:0008113	Similar to previous reports, we detected significantly increased intronic reads in the exosome mutant rrp6D strain (Fig. 4a,b).
PMID:25989903	GO:0071030	(comment: exosome dependent)
PMID:25989903	FYPO:0002960	As previously reported, deletion of rrp6 leads to strong accumulation of CUTs and a small group of mRNAs that are mostly involved in meiosis16,23,25,29,30,35.
PMID:25989903	FYPO:0008148	As previously reported, deletion of rrp6 leads to strong accumulation of CUTs and a small group of mRNAs that are mostly involved in meiosis16,23,25,29,30,35.
PMID:25989903	GO:0071030	(comment: exosome dependent)
PMID:25989903	FYPO:0008148	In contrast, deletion or mutation alleles of the MTREC complex lead to significant accumulation of all types of CUTs and also meiotic mRNAs. This effect is comparable to the level of CUT accumulation in the nuclear exosome subunit rrp6 deletion (Fig. 2a,b)
PMID:25989903	FYPO:0008148	In contrast, deletion or mutation alleles of the MTREC complex lead to significant accumulation of all types of CUTs and also meiotic mRNAs. This effect is comparable to the level of CUT accumulation in the nuclear exosome subunit rrp6 deletion (Fig. 2a,b)
PMID:25989903	FYPO:0002960	In contrast, deletion or mutation alleles of the MTREC complex lead to significant accumulation of all types of CUTs and also meiotic mRNAs. This effect is comparable to the level of CUT accumulation in the nuclear exosome subunit rrp6 deletion (Fig. 2a,b)
PMID:25989903	FYPO:0008148	In contrast, deletion or mutation alleles of the MTREC complex lead to significant accumulation of all types of CUTs and also meiotic mRNAs. This effect is comparable to the level of CUT accumulation in the nuclear exosome subunit rrp6 deletion (Fig. 2a,b)
PMID:25989903	FYPO:0002960	Deletion of iss10 or mmi1 only affects meiotic mRNAs
PMID:25993311	FYPO:0005986	(Fig. 3)
PMID:25993311	FYPO:0005986	(Fig. 3)
PMID:25993311	FYPO:0004585	(Fig. 3)
PMID:25993311	FYPO:0004585	(Fig. 3)
PMID:25993311	FYPO:0000488	(Table 3)
PMID:25993311	FYPO:0000488	(Table 3)
PMID:25993311	PBO:0106061	(Table 3)
PMID:25993311	PBO:0106060	(Fig. 2a)
PMID:25993311	PBO:0106060	(Fig. 2a)
PMID:25993311	PBO:0112555	Table2
PMID:25993311	PBO:0101665	(Table 1)
PMID:25993311	PBO:0101138	(Table 1)
PMID:25993311	PBO:0101138	(Table 1)
PMID:25993311	PBO:0101138	(Table 2)
PMID:25993311	PBO:0099293	Table2
PMID:25993311	PBO:0106056	Table2
PMID:25993311	PBO:0106057	Table2
PMID:25993311	PBO:0106058	Table2
PMID:25993311	PBO:0106059	Table2
PMID:25993311	GO:0090006	(Table 1)
PMID:25993311	GO:0090006	(Table 1)
PMID:25993311	PBO:0101138	(Table 1)
PMID:25993311	FYPO:0001033	(Table 2)
PMID:25993311	FYPO:0000488	Table S3
PMID:25993311	FYPO:0000488	Table S3
PMID:25993311	FYPO:0000488	Table S3
PMID:25993311	FYPO:0000488	Table S3
PMID:25993311	PBO:0106060	(Fig. 2a)
PMID:25993311	PBO:0101138	(Table 2)
PMID:25993311	PBO:0105331	(Fig. 2)
PMID:25993311	PBO:0105331	(Fig. 2)
PMID:25993311	PBO:0106054	Table2
PMID:26031557	PBO:0098186	(Fig. 4)
PMID:26031557	PBO:0098181	(Fig. 2)
PMID:26031557	FYPO:0005709	(Fig. S2) Pkl1md-GFP localized primarily to the spindle poles
PMID:26031557	FYPO:0000324	(Fig. 3)
PMID:26031557	FYPO:0000324	(Fig. 3) This is important as it indicates that the delay in pkl1D is likely not due to a delay in chromosome capture, but rather spindle formation in prophase.
PMID:26031557	PBO:0098185	(Fig. 3) MT buckling during prolonged contact with the cell tip cortex—its associated chromosome mass to the medial cell division site (Fig. 3c). Subsequent cytokinesis appeared to cut through the chromosome mass, resulting in aneuploidy in 12% of mitotic cells.
PMID:26031557	PBO:0098187	(Fig. S4)
PMID:26031557	PBO:0098179	(Fig. 1)
PMID:26031557	PBO:0098180	(Fig. 2)
PMID:26031557	PBO:0098182	(Fig. 2) (comment: CHECK It's only a bit worse (+3% chromosome loss). Not sure if worth including)
PMID:26031557	PBO:0098183	(Fig. S2) Pkl1md-GFP localized primarily to the spindle poles and almost completely rescued the protrusion phenotype
PMID:26031557	PBO:0098184	(Fig. S2) In contrast, in pkl1D msd1D cells, Pkl1md-GFP localized primarily to the spindle and only partially rescued the protrusion phenotype
PMID:26088418	PBO:0107810	Mutant proteins were expressed at a comparable level as wild-type Taz1 (data not shown).
PMID:26088418	PBO:0107810	Mutant proteins were expressed at a comparable level as wild-type Taz1 (data not shown).
PMID:26088418	PBO:0107811	(comment: increased length hererogeneity*****************) Indeed, yeast cells expressing the L431R and L445R mutants exhibited significant loss of function in telomere length regulation and showed long and highly heterogenous telomeres that were as severe as that in taz1Δ cells (Figure 1K)
PMID:26088418	FYPO:0006464	(comment: increased length hererogeneity) taz1-4A cells still exhibited extremely heterogeneous telomeres similar to taz1Δ and taz1-4R cells (Figure 1E).
PMID:26088418	PBO:0107811	(comment: increased length hererogeneity)
PMID:26088418	GO:0042162	While wild-type Taz1 bound to DNA with an equilibrium dissociation constant (Kd) of ~600 nM (Figure 1I), the L445R mutation caused a 10-fold decrease in DNA binding with a Kd of ~7 μM (Figure 1I), suggesting that Taz1 homodimerization is required for its efficient association with the telomeric DNA in vitro.
PMID:26088418	PBO:0107810	Both mutant proteins were expressed at near wild-type levels, suggesting that these acidic residues are not required for protein stability (data not shown).
PMID:26088418	PBO:0107810	Both mutant proteins were expressed at near wild-type levels, suggesting that these acidic residues are not required for protein stability (data not shown).
PMID:26088418	PBO:0107811	(comment: increased length hererogeneity*****************) Indeed, yeast cells expressing the L431R and L445R mutants exhibited significant loss of function in telomere length regulation and showed long and highly heterogenous telomeres that were as severe as that in taz1Δ cells (Figure 1K)
PMID:26088418	PBO:0107811	(comment: increased length hererogeneity)
PMID:26088418	PBO:0107814	The L445R mutation caused a 10-fold decrease in DNA binding with a Kd of ~7 μM (Figure 1I), suggesting that Taz1 homodimerization is
PMID:26092938	PBO:0104502	decreased local concentration of the myosin-II
PMID:26092938	PBO:0096672	large portion of the mutant forms cytoplasmic dots
PMID:26092938	PBO:0104503	localization of the myosin-II is abolished
PMID:26092938	PBO:0104504	increased local concentration of the myosin-II
PMID:26092938	PBO:0104502	decreased local concentration of the myosin-II
PMID:26098872	PBO:0101262	(Figure 8c)
PMID:26098872	FYPO:0001357	(Figure 8a)
PMID:26098872	PBO:0093560	(Figure 8a)
PMID:26098872	PBO:0093559	(Figure 8a)
PMID:26098872	PBO:0093560	(Figure 8b)
PMID:26108447	FYPO:0003860	(Figure 6)
PMID:26108447	FYPO:0002766	(Figure 6)
PMID:26108447	FYPO:0002766	(Figure 6)
PMID:26108447	FYPO:0002766	(Figure 6)
PMID:26108447	FYPO:0002766	(Figure 6)
PMID:26108447	FYPO:0003860	(Figure 6)
PMID:26108447	FYPO:0003860	(Figure 6)
PMID:26108447	FYPO:0002766	(Figure 6)
PMID:26108447	FYPO:0002640	(Figure 6)
PMID:26108447	FYPO:0002766	(Figure 6)
PMID:26108447	FYPO:0003358	(Figure 6)
PMID:26108447	FYPO:0003860	(Figure 6)
PMID:26108447	FYPO:0003860	(Figure 6)
PMID:26108447	FYPO:0003860	(Figure 6)
PMID:26108447	FYPO:0002766	(Figure 6)
PMID:26122634	FYPO:0004688	(comment: polysomal profiling)
PMID:26122634	FYPO:0004688	(comment: polysomal profiling)
PMID:26124291	PBO:0035552	(Fig. 4 C)
PMID:26124291	PBO:0035552	(Fig. 4 C)
PMID:26124291	PBO:0035552	(Fig. 4 C)
PMID:26124291	GO:0099079	(Fig. 6C)
PMID:26124291	PBO:0095574	(Fig. S5E)
PMID:26124291	FYPO:0005565	(Fig. 7E)
PMID:26124291	PBO:0035552	(Fig. 4 C)
PMID:26124291	PBO:0035552	(Fig. 4 C)
PMID:26124291	GO:0099079	(Fig. 6C)
PMID:26124291	GO:0099079	(Fig. S5A,C)
PMID:26124291	FYPO:0004614	(Fig. 7 CD) (comment: abnormal Q-MT bundle elongation upon G1 re-entry/interphase bundle reassembly)
PMID:26124291	PBO:0095573	(Fig. S5E)
PMID:26124291	PBO:0035555	(Fig. 7E,F)
PMID:26124291	PBO:0035552	(Fig. 4 C)
PMID:26131711	PBO:0098160	modified forms of Cdc2 present differ from wild type
PMID:26131711	PBO:0098160	modified forms of Cdc2 present differ from wild type, but are same as in cdc2-1w alone
PMID:26131711	PBO:0098160	modified forms of Cdc2 differ from both wild type and cdc2-1w alone
PMID:26131711	GO:0072435	Chk1 binds to the unphosphorylated form of Cdc2 kinase
PMID:26131711	GO:0005515	Chk1 binds to the unphosphorylated form of Cdc2 kinase
PMID:26131711	GO:0005515	Chk1 binds to the unphosphorylated form of Cdc2 kinase
PMID:26131711	GO:0005515	Chk1 binds to the unphosphorylated form of Cdc2 kinase
PMID:26131711	GO:0005515	Chk1 binds to the unphosphorylated form of Cdc2 kinase
PMID:26131711	GO:0005515	Chk1 binds to the unphosphorylated form of Cdc2 kinase
PMID:26131711	PBO:0098160	modified forms of Cdc2 present differ from wild type, but are same as in cdc2-1w alone
PMID:26132084	FYPO:0003210	(Figure 1)
PMID:26132084	FYPO:0005871	(Fig. 4C)
PMID:26132084	FYPO:0005873	(Figure 4B)
PMID:26132084	FYPO:0004495	(Fig. 3C)
PMID:26132084	PBO:0097179	(Figure 3)
PMID:26132084	PBO:0097178	(Fig. 2D,2E)
PMID:26132084	PBO:0097172	(commentL P.P. Bgs4 and Ags1 abnormal localization in the septum membrane)
PMID:26132084	PBO:0097173	(commentL P.P. Bgs4 and Ags1 abnormal localization in the septum membrane)
PMID:26132084	FYPO:0005289	(Figure 1c)
PMID:26132084	PBO:0097174	(Figure 1A,B)
PMID:26132084	PBO:0097175	(Fig. 3C,D)
PMID:26132084	PBO:0097177	(Fig. 5) (comment: SH3 domain of Cdc15 is required for the proper concentration of Pxl1 at the CAR)
PMID:26132084	FYPO:0000117	(Fig. 6)
PMID:26132084	FYPO:0003890	(Fig. 6) Coupling of the Actomyosin ring contraction and septation onsetRing sliding even after the onset of septum synthesis, causing a longitudinal deposition along the plasma membrane of linear β-glucan as detected by CW staining until septum ingression started
PMID:26132084	FYPO:0003338	(Fig. 2A,B) fragmented with RLC strands
PMID:26137436	FYPO:0002060	(Table 1)
PMID:26137436	PBO:0101077	we failed to detect a band corresponding to the full-length Nup189 fused with GFP (Nup98-Nup96-GFP), indicating that autocleavage occurs with no remains of the joint molecule. The same bands corresponding to Nup98 and Nup96-GFP were also detected in the splicing-defective mutant, as expected (Fig. 2B and C
PMID:26150232	GO:1903077	(comment: of cell tip)
PMID:26152587	FYPO:0001355	(Fig. 1a)
PMID:26152587	PBO:0100231	(comment: CHECK a mild phenotype)
PMID:26152587	PBO:0020040	(comment: Gaf1-GFP is found in the nucleus following nitrogen starvation but not glucose starvation)
PMID:26152587	PBO:0020038	(comment: Gaf1-GFP is found in the nucleus following nitrogen starvation but not glucose starvation)
PMID:26152587	FYPO:0001357	(Fig. 1a)
PMID:26152587	FYPO:0001357	(Fig. 1a)
PMID:26152587	FYPO:0001357	(Fig. 1a)
PMID:26152587	FYPO:0001357	(Fig. 1a)
PMID:26152587	FYPO:0001357	(Fig. 1a)
PMID:26152587	FYPO:0001357	(Fig. 1a)
PMID:26152587	FYPO:0001357	(Fig. 1a)
PMID:26152587	PBO:0100232	(Fig. 1a)
PMID:26152587	PBO:0100231	(comment: CHECK a mild phenotype)
PMID:26152587	PBO:0100230	(comment: CONDITION 1h in proline medium) (comment: CHECK a mild phenotype)
PMID:26152587	PBO:0100230	(comment: CONDITION 1h in proline medium) (comment: CHECK a mild phenotype)
PMID:26152587	PBO:0100226	(comment: CONDITION 1h in proline medium) (comment: CHECK a mild phenotype)
PMID:26152587	PBO:0100226	(comment: CONDITION 1h in proline medium)
PMID:26152587	PBO:0018647	(comment: Gaf1-GFP is found in the nucleus following nitrogen starvation but not glucose starvation)
PMID:26152728	PBO:0106610	Interestingly, a few proteins were found to specifically interact with Sdj1-L169P (supplemental File S2). Among these were Ssa1 and Ssa2, two highly similar cytosolic Hsp70-type chaperones. To independently validate the data from mass spectrometry, we subsequently performed immunoprecipitation experiments with wild type Sdj1 and Sdj1-L169P. Indeed, we found that Hsp70 (Ssa1 and Ssa2) was specifically associated with Sdj1-L169P and not wild type Sdj1 (Fig. 4A).
PMID:26152728	GO:0030163	(comment: vw: this pathway appears to be proteasome independent, likely autohagy mediated)
PMID:26152728	GO:0030163	(comment: vw: this pathway appears to be proteasome independent, likely autophagy mediated)
PMID:26152728	PBO:0106612	Indeed, the Sdj1-L169P level was increased in ssa1, ssa2, and hsp104 null mutants, with the most marked effect observed in the ssa2Δ and hsp104Δ strains (Fig. 4B).
PMID:26152728	PBO:0106609	First, we observed that the steady-state level of Sdj1-L169P was reduced compared with wild type Sdj1 (Fig. 3A). In cultures where protein synthesis was blocked by addition of cycloheximide, we found that wild type Sdj1 appeared stable, whereas the Sdj1-L169P protein was rapidly degraded (Fig. 3B). However, when the proteasome inhibitor bortezomib was added to the culture, the degradation was blocked (Fig. 3B), suggesting that the reduced Sdj1-L169P steady-state level was primarily caused by proteasomal degradation of the protein
PMID:26152728	PBO:0106612	only in the ltn1Δ strain did we observe an increased level of Sdj1-L169P (Fig. 5A).
PMID:26152728	PBO:0106612	Indeed, Sdj1-L169P was more stable in both ltn1 and rqc1 deletion strains (Fig. 5B). Although degradation was still observed in the ltn1Δ and rqc1Δ strains, Sdj1-L169P was significantly stabilized in these mutants compared with the wild type control (Fig. 5C).
PMID:26152728	GO:0005829	Sdj1, carrying a C-terminal YFP, FLAG, and His6 (YFH) tag, was evenly distributed throughout the cytosol and nucleus, and did not markedly co-localize with the mitochondrial marker protein, Cox4 (Fig. 2A).
PMID:26152728	GO:0005634	Sdj1, carrying a C-terminal YFP, FLAG, and His6 (YFH) tag, was evenly distributed throughout the cytosol and nucleus, and did not markedly co-localize with the mitochondrial marker protein, Cox4 (Fig. 2A).
PMID:26152728	PBO:0106613	Indeed, the Sdj1-L169P level was increased in ssa1, ssa2, and hsp104 null mutants, with the most marked effect observed in the ssa2Δ and hsp104Δ strains (Fig. 4B).
PMID:26152728	PBO:0106612	Indeed, the Sdj1-L169P level was increased in ssa1, ssa2, and hsp104 null mutants, with the most marked effect observed in the ssa2Δ and hsp104Δ strains (Fig. 4B).
PMID:26152728	GO:1990116	(comment: =)
PMID:26152728	PBO:0106611	Interestingly, a few proteins were found to specifically interact with Sdj1-L169P (supplemental File S2). Among these were Ssa1 and Ssa2, two highly similar cytosolic Hsp70-type chaperones. To independently validate the data from mass spectrometry, we subsequently performed immunoprecipitation experiments with wild type Sdj1 and Sdj1-L169P. Indeed, we found that Hsp70 (Ssa1 and Ssa2) was specifically associated with Sdj1-L169P and not wild type Sdj1 (Fig. 4A).
PMID:26152728	PBO:0106608	As expected, we found that GST-tagged Sdj1 was able to co-precipitate wild type His6- tagged Sdj1, but not His6-tagged Sdj1-L169P (Fig. 1B). In agreement with this, we observe that the Leu-169 residue is located in the proximity of the subunit-subunit interface in the published crystal structure of Sdj1 (33) (Fig. 1C).
PMID:26160178	PBO:0096388	(comment: CHECK affecting binding to histone H2A (hta1))
PMID:26160178	PBO:0096385	(comment: CHECK affecting binding to Mdb1)
PMID:26167880	PBO:0104838	Dsk1 readily phosphorylated WT Bpb1 in vitro, and mutation of Bpb1 at either S131 or S133 to alanine did not abolish phosphorylation (Fig. 5a). However, mutation of both S131 and S133 did, thus indicating that these two residues are the major sites of Bpb1 phosphorylation by Dsk1 (Fig. 5a).
PMID:26167880	PBO:0092747	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	PBO:0113596	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	PBO:0113597	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	PBO:0113596	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	FYPO:0003029	Inhibition of Dsk1 and Prp4 caused a significant increase of intron retention in 1,945 (~42%) and 2,148 splicing events (~47%), respectively, thus indicating broad defects in RNA splicing (Fig. 1b). I
PMID:26167880	PBO:0113595	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	PBO:0113595	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	PBO:0113594	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	FYPO:0003029	Inhibition of Dsk1 and Prp4 caused a significant increase of intron retention in 1,945 (~42%) and 2,148 splicing events (~47%), respectively, thus indicating broad defects in RNA splicing (Fig. 1b). I
PMID:26167880	PBO:0113593	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	PBO:0113592	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	PBO:0092728	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	PBO:0113598	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	PBO:0113599	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	PBO:0113600	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	PBO:0113601	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	PBO:0113603	We conclude that phosphorylation of the Dsk1 substrate Bpb1 has a major effect on the genome-wide splicing pattern.
PMID:26167880	FYPO:0003029	However, mutation of the conserved S131 and S133 residues to alanine in Bpb1 (denoted Bpb1-2A) caused significant intron retention in 1,598 introns (~35%) (Fig. 3b) and thus produces a defect quantitatively and qualitatively similar to inhibition of either Dsk1 (ρ = 0.62 ± 0.02; P < 10−6, two sided) or Prp4 (ρ = 0.63 ± 0.02; P < 10−6, two sided).
PMID:26167880	FYPO:0003029	Importantly, introns retained in a temperature-sensitive mutant of the S. pombe U2AF65 ortholog prp2 (prp2-1) (2,873 introns retained, ~62%) (Supplementary Fig. 3b) did not result in a consistent positive correlation with suboptimal cis-regulatory sequences (Fig. 4a and Supplementary Fig. 3a).
PMID:26167880	PBO:0104838	Dsk1 readily phosphorylated WT Bpb1 in vitro, and mutation of Bpb1 at either S131 or S133 to alanine did not abolish phosphorylation (Fig. 5a). However, mutation of both S131 and S133 did, thus indicating that these two residues are the major sites of Bpb1 phosphorylation by Dsk1 (Fig. 5a).
PMID:26221037	PBO:0099745	(comment: modification(s) not identified)
PMID:26221037	PBO:0099745	(comment: modification(s) not identified)
PMID:26221037	PBO:0099741	(comment: higher than without nup132d)
PMID:26221037	PBO:0099739	(comment: higher than without nup132d)
PMID:26258632	PBO:0093562	(Fig. 1a)
PMID:26258632	PBO:0093564	(Fig. 1a)
PMID:26258632	PBO:0033345	(Fig. 3c)
PMID:26258632	FYPO:0005220	(comment: ABOLISHED tetermerization)
PMID:26258632	FYPO:0005220	(comment: ABOLISHED tetermerization) fig 4f
PMID:26258632	PBO:0093562	(Fig. 1a)
PMID:26258632	PBO:0093562	(Fig. 1a)
PMID:26258632	PBO:0093562	(Fig. 1a)
PMID:26258632	FYPO:0000030	"(Fig. 5c) (comment: CHECK ""gliding"" new GO term requested)"
PMID:26258632	PBO:0097990	(Fig. 1e)
PMID:26258632	PBO:0033343	(Fig. 1b)
PMID:26258632	PBO:0033342	(Fig. 1b)
PMID:26258632	PBO:0033342	(Fig. 1b)
PMID:26258632	PBO:0033341	(Fig. 1b)
PMID:26258632	PBO:0097989	(comment: kinetochore localization of Cut7 is unaffected)
PMID:26258632	PBO:0097988	(Fig. 2a) (comment:diminished relocation from kinetochore)
PMID:26258632	PBO:0033340	(Fig. 5C)
PMID:26258632	FYPO:0003762	(Fig. 2b) (comment: mad1 localizes to unattached kinetochores) and fig 3a
PMID:26258632	PBO:0112052	(Fig. 2d)
PMID:26258632	PBO:0093562	(Fig. 3b)
PMID:26258632	FYPO:0004318	(Fig. 3A,B)
PMID:26258632	PBO:0023853	(Fig. 2D) (comment: CHECK unattached kinetochore nda3-KM311 arrested cell)
PMID:26258632	FYPO:0004318	(Fig. 3 a,b)
PMID:26258632	PBO:0097992	(Fig. 2a)
PMID:26258632	PBO:0096319	(Fig. 2a)
PMID:26258632	PBO:0018845	(Figure 2a)
PMID:26258632	FYPO:0004318	(Fig. 3 a,b)
PMID:26258632	PBO:0097991	(Figure 2a)
PMID:26258632	PBO:0097990	(Fig. 1e)
PMID:26258632	PBO:0093564	(Fig. 1a)
PMID:26264592	PBO:0094777	(Fig. S1)
PMID:26264592	PBO:0101499	(Fig. 1)
PMID:26264592	PBO:0101499	(Fig. 1)
PMID:26264592	PBO:0101499	(Fig. 1)
PMID:26264592	PBO:0101499	(Fig. 1)
PMID:26264592	PBO:0101499	(Fig. 1)
PMID:26264592	PBO:0101499	(Fig. 1)
PMID:26264592	PBO:0094771	(Fig. 2)
PMID:26264592	PBO:0094771	(Fig. 2)
PMID:26264592	PBO:0094771	(Fig. 2)
PMID:26264592	PBO:0101499	(Fig. 1)
PMID:26264592	PBO:0094738	(Fig. 2)
PMID:26264592	PBO:0094738	(Fig. 2)
PMID:26264592	PBO:0094738	(Fig. 2)
PMID:26264592	PBO:0094738	(Fig. 2)
PMID:26264592	PBO:0094738	(Fig. 2)
PMID:26264592	PBO:0094738	(Fig. 2)
PMID:26264592	PBO:0094738	(Fig. 2)
PMID:26264592	PBO:0111634	(comment: CHECK negative extracellular phosphate aquisition (S5P,P6?,S7P))
PMID:26264592	GO:0030643	(comment: CHECK negative extracellular phosphate aquisition)
PMID:26264592	PBO:0111672	(comment: CHECK negative extracellular phosphate aquisition (S5P,P6?,S7P))
PMID:26264592	PBO:0111671	(comment: CHECK negative extracellular phosphate aquisition (S5P,P6?,S7P))
PMID:26264592	GO:0030643	(comment: CHECK negative regulation of extracellular phosphate aquisition)
PMID:26264592	GO:0030643	(comment: CHECK negative regulation of extracellular phosphate aquisition)
PMID:26264592	PBO:0094738	(Fig. 2)
PMID:26264592	PBO:0094738	(Fig. 2)
PMID:26264592	PBO:0094772	(Fig. S4)
PMID:26264592	PBO:0094773	(Fig. S4)
PMID:26264592	PBO:0111504	(Fig. S3)
PMID:26264592	PBO:0111504	(Fig. S3)
PMID:26264592	PBO:0111504	(Fig. S3)
PMID:26264592	PBO:0111504	(Fig. S3)
PMID:26264592	PBO:0111509	(Fig. S2)
PMID:26264592	PBO:0111508	(Fig. S2)
PMID:26264592	PBO:0111508	(Fig. S2)
PMID:26264592	PBO:0111508	(Fig. S2)
PMID:26264592	PBO:0094777	(Fig. S1)
PMID:26264592	PBO:0094777	(Fig. S1)
PMID:26264592	PBO:0094777	(Fig. S1)
PMID:26264592	PBO:0094777	(Fig. S1)
PMID:26264592	PBO:0093556	(Fig. 7A)
PMID:26264592	PBO:0093557	(Fig. 7A)
PMID:26264592	FYPO:0002061	(Fig. 7A)
PMID:26264592	FYPO:0002061	(Fig. 7A)
PMID:26264592	FYPO:0002061	(Fig. 7A)
PMID:26264592	FYPO:0002061	(Fig. 7A)
PMID:26264592	FYPO:0002061	(Fig. 7A)
PMID:26264592	FYPO:0002061	(Fig. 7A)
PMID:26264592	PBO:0093554	(Fig. 7A)
PMID:26264592	PBO:0093560	(Fig. 7A)
PMID:26264592	PBO:0093559	(Fig. 7A)
PMID:26264592	PBO:0093559	(Fig. 7A)
PMID:26264592	PBO:0093553	(Fig. 7A)
PMID:26264592	PBO:0093553	(Fig. 7A)
PMID:26264592	PBO:0101499	(Fig. 7B)
PMID:26264592	PBO:0094771	(Fig. 6)
PMID:26264592	PBO:0101499	(Fig. 6)
PMID:26264592	PBO:0094738	(Fig. 2)
PMID:26264592	PBO:0094771	(Fig. 6)
PMID:26264592	PBO:0094738	(Fig. 2)
PMID:26264592	PBO:0094738	(Fig. 2)
PMID:26264592	PBO:0111501	(Fig. 3C)
PMID:26264592	PBO:0111502	(Fig. 3C)
PMID:26264592	PBO:0111503	(Fig. 3C)
PMID:26264592	PBO:0094772	(Fig. 4C)
PMID:26264592	PBO:0094772	(Fig. 4C)
PMID:26264592	PBO:0094775	(Fig. 4C)
PMID:26264592	PBO:0094772	(Fig. 4C)
PMID:26264592	PBO:0094775	(Fig. 4C)
PMID:26264592	PBO:0094775	(Fig. 4C)
PMID:26264592	PBO:0094773	(Fig. 4A)
PMID:26264592	PBO:0094773	(Fig. 4A)
PMID:26264592	PBO:0094773	(Fig. 4A)
PMID:26264592	PBO:0094738	(Fig. 6)
PMID:26264592	PBO:0094738	(Fig. 6)
PMID:26264592	PBO:0094738	(Fig. 6)
PMID:26264592	PBO:0098248	(Fig. 6)
PMID:26264592	PBO:0098248	(Fig. 6)
PMID:26264592	PBO:0098248	(Fig. 6)
PMID:26264592	PBO:0111507	(Fig. 5C)
PMID:26264592	PBO:0111506	(Fig. 5B)
PMID:26264592	PBO:0111505	(Fig. 5B)
PMID:26264592	PBO:0111504	(Fig. 5A)
PMID:26264592	PBO:0098250	(Fig. 4A)
PMID:26264592	PBO:0098250	(Fig. 4A)
PMID:26264592	PBO:0098250	(Fig. 4A)
PMID:26275423	GO:0000775	Chromatin immunoprecipitation of this protein is highly enriched for centromeric sequences.
PMID:26275423	GO:0000775	Chromatin immunoprecipitation of this protein is highly enriched for centromeric sequences.
PMID:26275423	GO:0000775	Chromatin immunoprecipitation of this protein is highly enriched for centromeric sequences.
PMID:26275423	GO:0000775	Chromatin immunoprecipitation of this protein is highly enriched in centromeric DNA
PMID:26275423	GO:0000939	Chromatin immunoprecipitation of this protein is highly enriched for centromeric sequences.
PMID:26275423	GO:0000775	Chromatin immunoprecipitation of this protein is highly enriched in centromeric DNA
PMID:26365378	PBO:0110838	(comment: Indirect evidence, could be upstream)
PMID:26365378	PBO:0098887	"(comment: CHECK microscopy shows ""protein localization to vacuole with protein mislocalized to cytosol"" but with additional vacuolar processing phenotypes I think we can make the BP phenotypes /AL)"
PMID:26365378	GO:0005515	(Fig. S3)
PMID:26365378	GO:0005515	(Fig. S3)
PMID:26365378	FYPO:0006294	(comment: CHECK macroautophagy? - selective autophagy is a child of macroautophagy)
PMID:26365378	PBO:0098887	(comment: 4h)
PMID:26365378	PBO:0110838	(comment: Indirect evidence, could be upstream)
PMID:26365378	PBO:0110838	(comment: Indirect evidence, could be upstream)
PMID:26366556	PBO:0018467	(comment: CHECK low penetrance)
PMID:26366556	PBO:0101185	determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c
PMID:26366556	FYPO:0006822	(comment: CHECK low penetrance)
PMID:26366556	GO:0019216	ChIP-seq and microarray data indicate that Cbf11 regulates lipid metabolism genes.
PMID:26366556	FYPO:0001122	large fractions of both abnormally long and abnormally short cells are present in the population
PMID:26366556	PBO:0101182	determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c
PMID:26366556	PBO:0101183	determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c
PMID:26366556	PBO:0101184	determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c
PMID:26366556	PBO:0101187	determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c
PMID:26366556	PBO:0101186	determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c
PMID:26366556	PBO:0101181	(comment: CHECK low penetrance)
PMID:26366556	PBO:0021323	determined by EMSA. Substrate: dsDNA oligonucleotide derived from promoters of cut6 and ptl1 genes (contain the CSL_response_element)
PMID:26401015	PBO:0094446	(comment: abolishes preference for K4-trimethylated H3)
PMID:26401015	PBO:0094447	(comment: acetyltransferase normally processive in presence of K4-trimethylated H3 -bound by Sgf29)
PMID:26401015	PBO:0094446	(comment:abolishes preference for K4-trimethylated H3)
PMID:26401015	PBO:0094447	(comment: acetyltransferase normally processive in presence of K4-trimethylated H3 -bound by Sgf29)
PMID:26412298	GO:0061578	Inferred from in vitro biochemical assay using K63-linked di-ubiquitinase
PMID:26422458	GO:0051537	Biochemical and mutagenic studies demonstrated that the [2Fe-2S]2+ cluster substantially inhibits the phosphatase activity of Asp1, thereby increasing its net kinase activity.
PMID:26424849	PBO:0035522	(comment: CHECK waiting for go-ontology/issues/12536)
PMID:26424849	GO:0016428	(comment: in response to queuosine incorporation into tRNA-Asp)
PMID:26436826	PBO:0103248	(comment: alkaline DNA preparation)
PMID:26436826	PBO:0103249	(comment: alkaline DNA preparation)
PMID:26438724	FYPO:0005286	(Figure 4a)
PMID:26438724	PBO:0104237	(Fig. 5)
PMID:26438724	GO:0031507	(comment: changed from: heterochromatin organization involved in chromatin silencing)
PMID:26438724	FYPO:0000220	Supp 1b
PMID:26438724	PBO:0104236	(Fig. 5)
PMID:26438724	PBO:0104237	(Fig. 5)
PMID:26438724	FYPO:0004201	(Fig. 6)
PMID:26438724	PBO:0104234	(comment: EV3)
PMID:26438724	PBO:0104233	Supp 1b
PMID:26438724	FYPO:0004137	(comment: EV3)
PMID:26438724	FYPO:0002355	(comment: EV3)
PMID:26438724	FYPO:0004743	(comment: EV3)
PMID:26438724	PBO:0104235	(comment: EV3)
PMID:26438724	FYPO:0006362	(Fig. 6)
PMID:26438724	PBO:0098760	(comment: EV3)
PMID:26438724	PBO:0098773	(comment: EV3)
PMID:26438724	PBO:0104236	(Fig. 5)
PMID:26438724	PBO:0104237	(Fig. 5)
PMID:26438724	PBO:0104231	Supp 1b
PMID:26438724	PBO:0104236	(Fig. 5)
PMID:26438724	GO:0033696	(comment: changed from: heterochromatin organization involved in chromatin silencing)
PMID:26438724	FYPO:0003045	(Figure 4a)
PMID:26438724	PBO:0104232	Supp 1b
PMID:26438724	FYPO:0004749	(Figure 4a)
PMID:26443059	FYPO:0005053	(comment: inferred from protein binding phenotypes)
PMID:26443059	FYPO:0005053	(comment: inferred from protein binding phenotypes)
PMID:26443240	GO:0005634	absent when glucose limited
PMID:26443240	PBO:0095326	Pom1 does not relocalize to cell sides
PMID:26443240	PBO:0095326	Pom1 does not relocalize to cell sides
PMID:26443240	PBO:0095327	Tea4 does not relocalize to cell sides
PMID:26443240	GO:0031117	(comment: CHECK through negative regulation of Cls1)
PMID:26443240	PBO:0095330	Pom1 relocalizes to cell sides
PMID:26443240	PBO:0095330	Pom1 relocalizes to cell sides
PMID:26443240	PBO:0095330	Pom1 relocalizes to cell sides
PMID:26443240	PBO:0095330	Pom1 relocalizes to cell sides
PMID:26443240	PBO:0095330	Pom1 relocalizes to cell sides
PMID:26443240	PBO:0095332	Pom1 relocalization to cell sides
PMID:26443240	PBO:0095326	Pom1 does not relocalize to cell sides
PMID:26443240	PBO:0095326	Pom1 does not relocalize to cell sides
PMID:26443240	PBO:0095330	Pom1 does not relocalize to cell sides
PMID:26443240	PBO:0095326	Pom1 does not relocalize to cell sides
PMID:26443240	PBO:0095326	Pom1 does not relocalize to cell sides
PMID:26483559	PBO:0104214	(Fig. 6) (comment: CHECK increased or premature)
PMID:26483559	PBO:0104219	(Fig. 7C)
PMID:26483559	FYPO:0005634	(Fig. 9A)
PMID:26483559	FYPO:0005634	(Fig. 9A)
PMID:26483559	FYPO:0005634	(Fig. 9A)
PMID:26483559	FYPO:0005634	(Fig. 9A)
PMID:26483559	FYPO:0005634	(Fig. 9A)
PMID:26483559	FYPO:0005634	(Fig. 9A)
PMID:26483559	FYPO:0005634	(Fig. 9A)
PMID:26483559	FYPO:0000579	(Fig. 9A)
PMID:26483559	PBO:0036880	(Fig. 9A)
PMID:26483559	PBO:0036881	(Fig. 9A)
PMID:26483559	PBO:0036882	(Fig. 9A)
PMID:26483559	PBO:0036883	(Fig. 9A)
PMID:26483559	PBO:0036882	(Fig. 9A)
PMID:26483559	PBO:0036884	(Fig. 9A)
PMID:26483559	GO:1905318	(Fig. 9a,) there other evidence elsewhere but we don't have this annotation on mad2 at present...
PMID:26483559	FYPO:0005510	(Fig. 1B)
PMID:26483559	PBO:0104218	(Fig. 7, B and C)
PMID:26483559	FYPO:0005509	(Fig. 1b)
PMID:26483559	PBO:0104215	(Fig. 6) (comment: CHECK increased or premature)
PMID:26483559	PBO:0104216	(Fig. 8, B and C) (comment: CHECK increased or premature)
PMID:26483559	PBO:0035153	(Fig. 2)
PMID:26483559	FYPO:0004093	(Fig. 3A,B, S5)
PMID:26483559	FYPO:0004667	(Fig. 4, C and D)
PMID:26483559	FYPO:0005384	(Fig. 1B)
PMID:26483559	FYPO:0005512	(Fig. S1) (comment: Assayed by assaying depletion of securin from spindle)
PMID:26483559	FYPO:0005574	(Fig. S2)
PMID:26483559	FYPO:0005383	(Fig. 1D)
PMID:26483559	PBO:0104217	(Fig. 1D)
PMID:26499799	GO:0030295	(comment: cerevisiae substrate)
PMID:26518661	PBO:0095645	ev4
PMID:26518661	FYPO:0006995	(Figure 5)
PMID:26518661	PBO:0095641	(Figure 4)
PMID:26518661	FYPO:0006995	(Figure 5)
PMID:26518661	PBO:0094679	(Figure 5)
PMID:26518661	PBO:0095640	(Figure 4)
PMID:26518661	FYPO:0006988	(Figure 4)
PMID:26518661	FYPO:0006989	(Figure 4)
PMID:26518661	FYPO:0006989	(Figure 4)
PMID:26518661	PBO:0095642	(Figure 4)
PMID:26518661	PBO:0095639	(Figure 4)
PMID:26518661	PBO:0095638	(Figure 4)
PMID:26518661	PBO:0095643	(Figure 4)
PMID:26518661	PBO:0095644	(Figure 4)
PMID:26518661	PBO:0095644	(Figure 4)
PMID:26518661	PBO:0093562	(Figure 5)
PMID:26518661	PBO:0093564	(Figure 5)
PMID:26518661	PBO:0093564	(Figure 5)
PMID:26518661	FYPO:0001839	(Figure 5)
PMID:26518661	FYPO:0001839	(Figure 5)
PMID:26518661	FYPO:0005371	(Figure 5)
PMID:26518661	FYPO:0003411	(Figure 5)
PMID:26518661	FYPO:0003411	(Figure 5)
PMID:26518661	FYPO:0003411	(Figure 5)
PMID:26518661	FYPO:0003411	(Figure 5)
PMID:26518661	FYPO:0003411	(Figure 5)
PMID:26518661	FYPO:0003411	(Figure 5)
PMID:26518661	PBO:0095637	(Figure 4)
PMID:26518661	FYPO:0000862	(Figure 4)
PMID:26518661	FYPO:0004138	(Figure 4)
PMID:26518661	FYPO:0006987	(Figure 4)
PMID:26518661	FYPO:0006986	(Figure 2)
PMID:26518661	FYPO:0006986	(Figure 2)
PMID:26518661	FYPO:0006986	(Figure 2)
PMID:26518661	FYPO:0006986	(Figure 2)
PMID:26518661	FYPO:0006985	(Figure 2)
PMID:26518661	FYPO:0001355	(Figure 2)
PMID:26518661	FYPO:0006986	(Figure 2)
PMID:26518661	FYPO:0006986	(Figure 2)
PMID:26518661	FYPO:0006985	(Figure 2)
PMID:26518661	FYPO:0001125	(Figure 1)
PMID:26518661	PBO:0095646	ev4
PMID:26518661	FYPO:0004748	(Figure 7)
PMID:26518661	FYPO:0006997	(Figure 7)
PMID:26518661	FYPO:0006998	(Figure 7)
PMID:26518661	FYPO:0007000	(Figure 7)
PMID:26518661	FYPO:0007001	(Figure 7)
PMID:26518661	FYPO:0006986	(Figure 2)
PMID:26518661	FYPO:0003094	(Figure 5)
PMID:26518661	FYPO:0006986	(Figure 2)
PMID:26518661	FYPO:0007002	(Figure 7)
PMID:26518661	FYPO:0007000	(Figure 7)
PMID:26518661	FYPO:0007001	(Figure 7)
PMID:26518661	FYPO:0007002	(Figure 7)
PMID:26518661	FYPO:0007003	(Figure 7)
PMID:26518661	PBO:0120507	(Figure 7)
PMID:26518661	PBO:0120508	(Figure 7)
PMID:26518661	PBO:0120509	(Figure 7)
PMID:26518661	PBO:0120510	(Figure 7)
PMID:26518661	PBO:0095651	(Figure 7)
PMID:26518661	PBO:0095652	(Figure 7)
PMID:26518661	PBO:0095653	(Figure 7)
PMID:26518661	FYPO:0004376	(Figure 7)
PMID:26518661	FYPO:0002336	(Figure 7)
PMID:26518661	FYPO:0002336	(Figure 7)
PMID:26518661	FYPO:0002336	ev4,ef
PMID:26518661	FYPO:0003411	(Figure 5)
PMID:26518661	FYPO:0006995	(Figure 5)
PMID:26518661	FYPO:0000024	(Figure 1)
PMID:26518661	PBO:0095634	(Figure 1)
PMID:26518661	FYPO:0006985	(Figure 1)
PMID:26518661	FYPO:0006995	(Figure 5)
PMID:26518661	FYPO:0006992	(Figure 5)
PMID:26518661	FYPO:0006992	(Figure 5)
PMID:26518661	FYPO:0006993	(Figure 5)
PMID:26518661	FYPO:0006993	(Figure 5)
PMID:26518661	FYPO:0006993	(Figure 5)
PMID:26518661	FYPO:0004742	(Figure 5)
PMID:26518661	FYPO:0006994	(Figure 5)
PMID:26527280	PBO:0102439	(Fig. S6D)
PMID:26527280	PBO:0097773	(Fig. 3A, 3B)
PMID:26527280	PBO:0097772	(Fig. 3E, 3F)
PMID:26527280	PBO:0102434	(Fig. 5C)
PMID:26527280	FYPO:0001357	(Fig. 1J)
PMID:26527280	FYPO:0001357	(Fig. 1I)
PMID:26527280	PBO:0097773	(Figure 2A) Plo1 to SPBs persisted for more than 20 min
PMID:26527280	PBO:0102442	In contrast, there was only a very slight delay in sister chromatid separation (Figures 2A and 2B).
PMID:26527280	FYPO:0001946	chromosomes failed to split, but Plo1 was removed from SPBs with timing similar to that in wild-type cells (Figures 2A and 2C).
PMID:26527280	PBO:0101464	(Fig. S3G, S3H)
PMID:26527280	PBO:0101464	(Fig. S3D)
PMID:26527280	PBO:0102437	(Fig. S3A, S3C)
PMID:26527280	PBO:0102436	(Fig. S3A, S3B) (comment: control for increased proteasome in nucleus)
PMID:26527280	PBO:0097772	(Fig. S2B)
PMID:26527280	FYPO:0004310	chromosomes failed to split, but Plo1 was removed from SPBs with timing similar to that in wild-type cells (Figures 2A and 2C).
PMID:26527280	PBO:0038176	(comment: tetrad dioscection) Fig. 7C, 7E
PMID:26527280	PBO:0102434	(Fig. 4D, 4E)
PMID:26527280	FYPO:0004705	(Figures 3B, 3D). sister chromatid separation (which depends on securin degradation, not on cyclin B degradation) was delayed as well
PMID:26527280	PBO:0102443	(Figure S2F export of CDK1 from the nucleus, which depends on cyclin B degradation ,, was delayed
PMID:26527280	PBO:0038172	(comment: tetrad disection) Fig. 7D, 7E
PMID:26527280	FYPO:0002151	(Fig. 7D, 7E) (comment: tetrad dissection)
PMID:26527280	PBO:0102435	(Fig. 6G, S7F, S7G) (comment: TUBE pull-down)
PMID:26527280	PBO:0102438	(Fig. S3I, S3J)
PMID:26527280	PBO:0102440	(Fig. S6L, S6M)
PMID:26527280	PBO:0102441	(Fig. 4G, 4H)
PMID:26536126	PBO:0107662	(comment: inability to take up 14-C uracil in fur4 deletion mutant)
PMID:26536126	FYPO:0000647	(comment: CHECK cell lysis on uracil depleted medium)
PMID:26536126	FYPO:0001012	(comment: CHECK auxotrophic for cytosine, uridine and UMP)
PMID:26536126	GO:0005783	(comment: CONDITION grown in EMM or YES medium)
PMID:26536126	GO:0000139	(comment: CONDITION nitrogen rich)
PMID:26536126	FYPO:0005173	(comment: CHECK assayed_using(PomBase:fur4))
PMID:26536126	GO:0000324	(comment: CONDITION nitrogen rich)
PMID:26536126	GO:1905530	(comment: uracil uptake enhancement in pub1 deletion)
PMID:26545917	PBO:0099158	they don't actually use pombe isu1 because they couldn't purify it, but they try both C. thermophilum and S. cerevisiae Isu1 and get similar results & sequence conservation is good to pombe.
PMID:26545917	FYPO:0002060	(Fig. 2c)
PMID:26545917	PBO:0099158	they don't actually use pombe isu1 because they couldn't purify it, but they try both C. thermophilum and S. cerevisiae Isu1 and get similar results & sequence conservation is good to pombe.
PMID:26582768	FYPO:0000089	(comment: CHECK Increased MMS sensitivity)
PMID:26582768	FYPO:0000089	(comment: CHECK Increased MMS sensitivity)
PMID:26652183	PBO:0035668	(comment: CONDITION 5 J/m2 UV) Fig 1A, Fig. S2
PMID:26652183	PBO:0097360	(comment: CONDITION 5 J/m2 UV) Fig. 1B
PMID:26652183	PBO:0097361	(comment: CONDITION 5 J/m2 UV) Fig. 1B, Fig. 3E
PMID:26652183	PBO:0097362	(comment: CONDITION 5 or 10 J/m2 UV) Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	FYPO:0005625	(comment: CONDITION 5 or 10 J/m2 UV) Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	PBO:0093629	(comment: CONDITION 5 J/m2 UV) Sensitivity is greater than rad51delta or eso1-D147N single mutants (see Fig. S7)
PMID:26652183	PBO:0097363	(comment: CONDITION 5 J/m2 UV) Fig. S3
PMID:26652183	PBO:0097363	(comment: CONDITION 5 J/m2 UV) sensitivity similar to rad8delta and rhp18delta single mutants (Fig. 3G)
PMID:26652183	PBO:0097363	(comment: CONDITION 5 J/m2 UV) similar sensitivity to eso1-D147N single mutant (Fig. 3H)
PMID:26652183	PBO:0097362	(comment: CONDITION 5 or 10 J/m2 UV) Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	PBO:0097363	(comment: CONDITION 5 J/m2 UV) Fig. 3C
PMID:26652183	PBO:0097362	(comment: CONDITION 5 or 10 J/m2 UV) similar sensitivity to rev1delta and rev3delta single mutants (Fig. 3I, Fig. 4A, Fig. S6)
PMID:26652183	PBO:0097363	(comment: CONDITION 2 or 5 J/m2 UV) Fig. 3F, Fig. S6
PMID:26652183	PBO:0097360	(comment: CONDITION 5 J/m2 UV) Delay is greater than rad51delta alone (see Fig. S7)
PMID:26652183	PBO:0097359	(comment: CONDITION 5 J/m2 UV) duration is similar to rad8delta or rhp18delta single mutants (see Fig. 3G)
PMID:26652183	PBO:0097359	(comment: CONDITION 5 J/m2 UV) duration is similar to eso1-D147N alone (see Fig. 3H)
PMID:26652183	PBO:0097365	(comment: CONDITION 2 or 5 J/m2 UV) Fig. 3F, Fig. S6
PMID:26652183	PBO:0097364	(comment: CONDITION 5 J/m2 UV) Fig. 3C
PMID:26652183	PBO:0035673	(comment: CONDITION 5 J/m2 UV) Fig. 3B
PMID:26652183	PBO:0035673	(comment: CONDITION 5 J/m2 UV) Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	PBO:0035673	(comment: CONDITION 5 J/m2 UV) Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	PBO:0097363	(comment: CONDITION 5 J/m2 UV) Fig. 3E
PMID:26652183	PBO:0097363	(comment: CONDITION 5 J/m2 UV) Fig. 3D
PMID:26652183	FYPO:0005625	(comment: CONDITION 5 or 10 J/m2 UV) Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	PBO:0097360	(comment: CONDITION 25 J/m2 UV) delay is greater than rad51delta alone (Fig. 5A)
PMID:26652183	PBO:0097359	(comment: CONDITION 5 J/m2 UV) Figure 1B, Figure 3D, Figure S6
PMID:26670050	PBO:0111164	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111134	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111135	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0106222	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0099654	(comment: affects unspliced pre-mRNA)
PMID:26670050	PBO:0099655	(comment: CHECK gene locus: rps2202)
PMID:26670050	PBO:0111137	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111138	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111139	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111140	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111141	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111142	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111143	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111144	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111145	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111146	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111147	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111148	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111149	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111150	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111151	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111152	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111153	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111154	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111155	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0099655	(comment: CHECK gene locus affected: rps2202)
PMID:26670050	PBO:0099656	(comment: CHECK increase > 50-fold)
PMID:26670050	PBO:0099657	(comment: CHECK increase > 10-fold)
PMID:26670050	PBO:0099658	(comment: CHECK increase > 10-fold)
PMID:26670050	PBO:0099659	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099660	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099661	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099662	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099663	(comment: CHECK increase > 10-fold)
PMID:26670050	PBO:0097114	(comment: CHECK increase > 10-fold)
PMID:26670050	PBO:0099664	(comment: CHECK increase > 10-fold)
PMID:26670050	PBO:0099665	(comment: CHECK increase > 10-fold)
PMID:26670050	PBO:0099666	(comment: CHECK increase > 10-fold)
PMID:26670050	PBO:0099667	(comment: CHECK increase > 10-fold)
PMID:26670050	PBO:0099668	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099669	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099670	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099671	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099672	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099673	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099674	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099675	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099676	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099677	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099678	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099679	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099680	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099681	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099682	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099683	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099684	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099685	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099686	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099687	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099688	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099689	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099690	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099691	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0111157	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111158	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111159	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111160	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111161	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111162	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111163	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111165	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111166	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111167	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0005515	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111169	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111170	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111171	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111172	(comment: CHECK SPCC1235.04c)
PMID:26670050	PBO:0111173	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111174	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111175	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111176	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111177	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111178	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111179	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111180	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0106222	(comment: enrichment in CRAC > 10-fold; Mmi1 binds the 5' extended region of the overlapping regulatory lncRNA prt)
PMID:26670050	PBO:0111181	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111182	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111183	(comment: CHECK SPBC1289.13c)
PMID:26670050	PBO:0111184	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111185	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111186	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111187	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111188	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111189	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111190	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111191	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111192	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111193	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111194	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111195	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111196	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111197	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111198	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111199	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111200	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111201	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111202	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111203	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111204	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111360	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111361	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111207	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111208	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111209	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111210	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111211	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111212	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111213	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111214	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111215	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111216	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111217	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111218	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111219	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111220	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111221	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111222	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111223	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111224	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111225	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111226	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111227	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111228	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111229	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111230	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0111055	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	PBO:0099693	(comment: CHECK increase > 40-fold)
PMID:26670050	PBO:0099694	(comment: CHECK increase > 10-fold)
PMID:26670050	PBO:0099695	(comment: CHECK increase > 10-fold)
PMID:26670050	PBO:0109063	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099697	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099698	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099699	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099700	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099701	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099702	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099703	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099704	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099705	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099706	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099707	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099708	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099709	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099710	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0099655	(comment: CHECK gene locus affected: dbp2)
PMID:26670050	PBO:0099655	(comment: CHECK gene affected: rps2202)
PMID:26670050	PBO:0099652	(Fig. S4B)
PMID:26670050	PBO:0099711	(Fig. S5e)
PMID:26670050	PBO:0099712	(comment: CHECK increase > 5-fold)
PMID:26670050	PBO:0111326	(comment: enrichment in CRAC > 10-fold (vw changed dpp2->dbp2))
PMID:26687354	GO:0007064	(fig 2)
PMID:26687354	GO:0030892	(Figure 1C)
PMID:26687354	GO:0030892	(Figure 1C)
PMID:26687354	GO:0007064	(Figure 2B) (comment: dependent on pds5)
PMID:26687354	GO:0007064	(fig 2)
PMID:26687354	FYPO:0005557	(Figure 6C)
PMID:26687354	PBO:0035232	(Figure 6B) (comment: CHECK acetylated form acts as a DNA sensor)
PMID:26687354	FYPO:0005556	(Figure 6A)
PMID:26687354	FYPO:0005555	(Figure 6A)
PMID:26687354	PBO:0114865	(Figure S4C)
PMID:26687354	PBO:0035230	(Figure 3B)
PMID:26687354	FYPO:0005557	(Figure 3B)
PMID:26687354	PBO:0034924	(Figure 3B)
PMID:26687354	PBO:0034924	(Figure 3B)
PMID:26687354	PBO:0034924	(Figure 3B)
PMID:26687354	GO:0007064	(Figure 2B)
PMID:26697368	FYPO:0004490	(comment: CHECK link to GEO dataset- GSE71820)
PMID:26697368	FYPO:0005301	(comment: CHECK link to GEO dataset- GSE71820)
PMID:26730850	PBO:0106551	(Fig. 4)
PMID:26730850	PBO:0106550	(Fig. 3)
PMID:26730850	PBO:0106551	(Fig. 4)
PMID:26730850	PBO:0106550	(Fig. 3)
PMID:26730850	PBO:0106554	(Fig. 3)
PMID:26730850	PBO:0106556	(Fig. 4)
PMID:26730850	PBO:0106555	(Fig. 3)
PMID:26730850	PBO:0106550	(Fig. 3)
PMID:26730850	PBO:0106554	(Fig. 3)
PMID:26730850	PBO:0106555	(Fig. 3)
PMID:26730850	PBO:0106554	(Fig. 3)
PMID:26730850	GO:1905746	(comment: regulation of efficiency at weak donor)
PMID:26730850	FYPO:0000561	(Fig. S1)
PMID:26730850	PBO:0106553	(Figure 1D)
PMID:26730850	PBO:0106552	(Figure 1D)
PMID:26730850	PBO:0106551	(Figure 4) (comment: efficiency of introns displaying weak splice sites)
PMID:26730850	PBO:0106554	(Fig. 3)
PMID:26730850	PBO:0106554	(Fig. 3)
PMID:26730850	PBO:0106554	(Fig. 3)
PMID:26730850	PBO:0106557	(Fig. 4)
PMID:26730850	PBO:0106557	(Fig. 4)
PMID:26730850	FYPO:0000012	(Figure 1A-C) (comment: transient growth arrest)
PMID:26730850	PBO:0095406	(Figure 1D) (comment: efficiency/ of introns displaying weak splice sites)
PMID:26730850	PBO:0106550	(Figure 1D) (comment: efficiency/ of introns displaying weak splice sites)
PMID:26730850	FYPO:0000333	(Figure 1C) (comment: transient)
PMID:26730850	PBO:0106550	(Figure 3, 5) (comment: efficiency/ of introns displaying weak splice sites)
PMID:26730850	PBO:0106556	(Fig. 4)
PMID:26730850	PBO:0106555	(Fig. 5)
PMID:26730850	PBO:0106554	(Fig. 5)
PMID:26730850	PBO:0106555	(Fig. 5)
PMID:26730850	PBO:0106554	(Fig. 5)
PMID:26730850	PBO:0106555	(Fig. 5)
PMID:26730850	PBO:0106555	(Fig. 5)
PMID:26730850	PBO:0109724	(Figure 1D, 2D) (comment: - examined via RT-PCR) (Figure 2A) (comment: examined via RNA-Seq)
PMID:26730850	PBO:0106550	(Fig. 5)
PMID:26730850	PBO:0106555	(Fig. 5)
PMID:26730850	PBO:0106551	(Fig. 4)
PMID:26730850	PBO:0106551	(Fig. 4)
PMID:26744419	PBO:0094679	(Fig. S10)
PMID:26744419	PBO:0094679	(Fig. S10)
PMID:26744419	PBO:0094679	(Fig. 1c)
PMID:26744419	PBO:0094282	(Fig. S10)
PMID:26744419	PBO:0111257	(Fig. 1c)
PMID:26744419	PBO:0098783	(Fig. 5c) (comment: CHECK parent GO:0003682?)
PMID:26744419	PBO:0098784	(Fig. 5c) (comment: CHECK parent GO:0003682?)
PMID:26744419	PBO:0093559	(Fig. 1b)
PMID:26744419	PBO:0098766	(Fig. 5b)
PMID:26744419	PBO:0098766	(Fig. 5b)
PMID:26744419	FYPO:0004342	(Fig. 1c)
PMID:26744419	PBO:0095834	(Fig. S2)
PMID:26744419	PBO:0095834	(Fig. S2)
PMID:26744419	PBO:0095834	(Fig. 1b)
PMID:26744419	PBO:0093563	(Fig. S1c)
PMID:26744419	PBO:0098779	(Fig. 7b)
PMID:26744419	PBO:0094679	(Fig. 1c)
PMID:26744419	PBO:0098755	(Fig. 5c)
PMID:26744419	PBO:0098756	(Fig. 5c)
PMID:26744419	FYPO:0004742	(Fig. 1d)
PMID:26744419	GO:0072766	(Fig. 4b, c)
PMID:26744419	GO:0140698	(Fig. 1c, Fig 4e)
PMID:26744419	PBO:0098757	pericentric Fig 1c, In conclusion, while other tethering mechanisms in S. pombe could be functionally coupled to heterochromatin, the LEM-mediated centromere recruitment and the MSC-dependent silencing are independent mechanisms, although they are mediated by the same protein.
PMID:26744419	PBO:0098758	(Fig. 1c) (comment: CHECK SHOULD BRE ORGANIZATION)
PMID:26744419	PBO:0095652	(Fig. 1c)
PMID:26744419	FYPO:0002360	(Fig. 1d)
PMID:26744419	PBO:0097950	(Fig. 1c)
PMID:26744419	PBO:0095834	(Fig. 6d)
PMID:26744419	PBO:0098777	(Fig. 4e)
PMID:26744419	PBO:0098776	(Fig. 4e)
PMID:26744419	PBO:0098776	(Fig. 4e)
PMID:26744419	PBO:0098774	(Fig. 4)
PMID:26744419	PBO:0098775	(Fig. 4)
PMID:26744419	FYPO:0006429	(Fig. 3d)
PMID:26744419	PBO:0098773	(Fig. 3c)
PMID:26744419	PBO:0098772	(Fig. 3c)
PMID:26744419	PBO:0111258	(Fig. 3b)
PMID:26744419	PBO:0111255	(Fig. 3b)
PMID:26744419	PBO:0111255	(Fig. 3b)
PMID:26744419	PBO:0098767	(Fig. 1d)
PMID:26744419	PBO:0098767	(Fig. 1d)
PMID:26744419	FYPO:0002360	(Fig. S4)
PMID:26744419	PBO:0095834	(Fig. S2)
PMID:26744419	PBO:0096188	(Fig. S2)
PMID:26744419	PBO:0096189	(Fig. S2)
PMID:26744419	PBO:0111255	(Fig. 1c)
PMID:26744419	PBO:0111256	(Fig. S2)
PMID:26744419	PBO:0094679	(Fig. S2)
PMID:26744419	PBO:0111257	(Fig. 3b)
PMID:26744419	PBO:0098769	(Fig. S5A)
PMID:26744419	PBO:0094283	(Fig. 3)
PMID:26744419	PBO:0094679	(Fig. S2)
PMID:26744419	PBO:0113582	(Fig. 3)
PMID:26744419	PBO:0094282	(Fig. 3)
PMID:26744419	PBO:0111256	(Fig. 3)
PMID:26744419	FYPO:0003411	(Fig. 3)
PMID:26744419	PBO:0111256	(Fig. 3)
PMID:26744419	PBO:0111256	(Fig. 3)
PMID:26744419	PBO:0097950	(Fig. 6e)
PMID:26744419	PBO:0098759	(Fig. 6c)
PMID:26744419	FYPO:0004924	(Fig. 6c)
PMID:26744419	FYPO:0003555	(Fig. 6e)
PMID:26744419	FYPO:0002360	(Fig. 6d)
PMID:26744419	PBO:0095834	(Fig. 6d)
PMID:26744419	PBO:0095834	(Fig. 6d)
PMID:26744419	PBO:0097950	(Fig. 6e)
PMID:26744419	PBO:0097950	(Fig. 6e)
PMID:26744419	PBO:0098760	(Fig. 3c)
PMID:26744419	PBO:0098761	(Fig. 6a) (comment: CHECK in combination with csi1∆; phenocopies lem2∆ csi1∆)
PMID:26744419	PBO:0098762	(Fig. 7b)
PMID:26744419	PBO:0098763	(Fig. 7b)
PMID:26744419	PBO:0098764	(Fig. 5c)
PMID:26744419	PBO:0098765	(Fig. 5b)
PMID:26744419	PBO:0098765	(Fig. 5b)
PMID:26744419	PBO:0098780	(Fig. 7b)
PMID:26744419	PBO:0120517	(Fig. 7b)
PMID:26744419	PBO:0098778	(Fig. 5)
PMID:26744419	GO:0005635	(Fig. 5)
PMID:26744419	PBO:0098782	(Fig. 7b)
PMID:26744419	PBO:0097950	(Fig. 7)
PMID:26744419	PBO:0097950	(Fig. 7)
PMID:26744419	PBO:0097950	(Fig. 7)
PMID:26744419	PBO:0097950	(Fig. 7)
PMID:26744419	PBO:0111257	(Fig. 7)
PMID:26744419	PBO:0111257	(Fig. 7)
PMID:26744419	PBO:0111257	(Fig. 7)
PMID:26744419	PBO:0094681	(Fig. 7)
PMID:26744419	PBO:0113582	(Fig. 7)
PMID:26746798	PBO:0093618	(Fig. 2A)
PMID:26746798	PBO:0100920	(Fig. 2C)
PMID:26746798	PBO:0023560	(Fig. 7B)
PMID:26746798	PBO:0033073	(Fig. 7B)
PMID:26746798	FYPO:0000229	(Fig. 7A)
PMID:26746798	FYPO:0000963	(Fig. 6)
PMID:26746798	FYPO:0000963	(Fig. 6)
PMID:26746798	FYPO:0000963	(Fig. 6)
PMID:26746798	FYPO:0000963	(Fig. 6)
PMID:26746798	PBO:0100926	(Fig. 3C)
PMID:26746798	PBO:0094254	(Fig. 3C)
PMID:26746798	PBO:0094254	(Fig. 3C)
PMID:26746798	PBO:0094255	(Fig. 3C)
PMID:26746798	PBO:0100924	(Fig. 3B)
PMID:26746798	PBO:0100925	(Fig. 3B)
PMID:26746798	PBO:0100924	(Fig. 3B)
PMID:26746798	PBO:0100923	(Fig. 3A)
PMID:26746798	PBO:0100922	(Fig. 3A)
PMID:26746798	PBO:0100922	(Fig. 3A)
PMID:26746798	PBO:0100921	(Fig. 2C)
PMID:26746798	PBO:0100920	(Fig. 2C)
PMID:26746798	PBO:0100919	(Fig. 2C)
PMID:26746798	PBO:0100918	(Fig. 2C)
PMID:26746798	PBO:0097986	(Fig. 2B)
PMID:26746798	PBO:0097986	(Fig. 2B)
PMID:26746798	PBO:0100313	(Fig. 2B)
PMID:26746798	PBO:0093616	(Fig. 2A)
PMID:26746798	PBO:0093618	(Fig. 2A)
PMID:26746798	PBO:0093581	(Fig. 1A)
PMID:26746798	PBO:0093581	(Fig. 1A)
PMID:26746798	PBO:0093579	(Fig. 1A)
PMID:26746798	PBO:0093579	(Fig. 1A)
PMID:26746798	PBO:0093581	(Fig. 1A)
PMID:26746798	PBO:0093579	(Fig. 1A)
PMID:26746798	PBO:0093580	(Fig. 1A)
PMID:26746798	PBO:0093580	(Fig. 1A)
PMID:26746798	PBO:0093579	(Fig. 1A) Defect in Checkpoint Signaling.
PMID:26749213	PBO:0100971	(Figure 1a)
PMID:26749213	PBO:0100970	(comment: moved down to new term from :protein mislocalized to cytoplasm during vegetative growth)
PMID:26749213	PBO:0100969	(comment: moved down to new term from :protein mislocalized to cytoplasm during vegetative growth)
PMID:26749213	PBO:0035049	(Fig. 3B-D) (Fig. 4A and movies 3 and 4) slow dynamics of actin patch components: Sla1, wsc1, arc5, Crn1
PMID:26749213	PBO:0100968	(comment: moved down from abnormal protein localization to cell tip (new term))
PMID:26749213	PBO:0035047	(Fig. 6D); evidence: filipin staining
PMID:26749213	GO:0072583	(comment: moved down drom endocytosis.) Delayed FM4-64 uptake when in combination with a clathrin mutationSlow dynamics of endocytic patch markers
PMID:26749213	PBO:0100972	(Figure 1a)
PMID:26749213	PBO:0100973	(Figure 1a)
PMID:26749213	GO:0032153	(Fig. 1B)
PMID:26749213	GO:0032153	(Fig. 1B)
PMID:26749213	GO:0032153	(Fig. 1B)
PMID:26749213	GO:0051285	(Fig. 1B)
PMID:26749213	GO:0051285	(Fig. 1B)
PMID:26749213	GO:0051285	(Fig. 1B)
PMID:26749213	FYPO:0002061	(Fig. 2d)
PMID:26749213	FYPO:0001235	(Fig. 2D)
PMID:26749213	PBO:0035059	(Supporting Information Fig. S4A)
PMID:26749213	PBO:0035060	(comment: FM4-64 uptake (I made Henars original annotation into a double mutant so the attribution has changed))
PMID:26749213	FYPO:0004247	(Fig. S2A, B)
PMID:26749213	PBO:0100976	(Fig. S2C)
PMID:26749213	PBO:0098628	(Fig. 1c)
PMID:26749213	PBO:0100966	(Fig. 7b)
PMID:26776736	PBO:0095954	(comment: MOVE EXTENSION DOWN TO NITROGEN) (comment: This can be inferred from all of the proposed EXP and is part of the proposed model we can delete if we can make in a better way)
PMID:26776736	PBO:0095952	again confirms other systems Endosulfines are small phosphoproteins, highly conserved from yeasts to humans, that specifically bind to and inhibit the PP2A$B55 protein phosphatase subcomplex [8, 9]. PP2A$B55 has been shown to be cell-cycle-regulated in Xenopus, following the opposite pattern of activity to Cdk1$Cyclin B (high in interphase and low in mitosis) [15]. To determine whether Ser64-phosphorylated Igo1 inhibits the PP2A$B55 (PP2A$Pab1 in fission yeast) phosphatase activity, we purified PP2A$Pab1 phosphatase from cells expressing GST- Pab1 using glutathione sepharose beads and assayed them for phosphatase activity. Wild-type Igo1 thiophosphorylated in vitro at Ser64 by Xenopus Greatwall, but not Igo1-S64A, inhibited more than 90% the phosphatase activity of PP2A$Pab1 (B55) (Figures S4B and S4C). This result indicates that Ser64- phosphorylated Igo1 inhibits the activity of PP2A$B55, analogous to the situation in budding yeast [27, 28, 35] and animal cells [8, 9].
PMID:26776736	PBO:0035246	important when growing on poor nitrogen sources
PMID:26776736	PBO:0095951	(comment: vw: changed to directly activates and added part_of They are deomstrating that the system is conserved...In Xenopus and mammalian cells, phosphorylation of ENSA by greatwall at serine 67 promotes its binding to and inhibition of PP2A$B55 phosphatase [8, 9]. enough evidence for function by IMP ALSO Our genetic and physiological data is in agreement with published work in budding yeast, Drosophila, Xenopus, and mammalian cells indicating that greatwall phosphorylates endo- sulfine to inhibit PP2A$B55 [8, 9, 27, 28, 35]. To test whether Igo1 is a direct target of Ppk18, we performed Ppk18 in vitro kinase assays using purified recombinant Igo1 and Igo1-S64A, as substrates. Extracts from wild-type (ppk18+) and Myc-tagged (ppk18-13myc) Ppk18 cells, treated for 1 hr with rapamycin in order to activate Ppk18, were immunoprecipitated with anti-c-Myc monoclonal antibodies. Ppk18-13myc immunoprecipitates were able to phosphorylate in vitro wild-type Igo1, but not Igo1-S64A Our genetic and physiological data is in agreement with published work in budding yeast, Drosophila, Xenopus, and mammalian cells indicating that greatwall phosphorylates endo- sulfine to inhibit PP2A$B55 [8, 9, 27, 28, 35]. To test whether Igo1 is a direct target of Ppk18, we performed Ppk18 in vitro kinase assays using purified recombinant Igo1 and Igo1-S64A, as substrates. Extracts from wild-type (ppk18+) and Myc-tagged (ppk18-13myc) Ppk18 cells, treated for 1 hr with rapamycin in order to activate Ppk18, were immunoprecipitated with anti-c-Myc monoclonal antibodies. Ppk18-13myc immunoprecipitates were able to phosphorylate in vitro wild-type Igo1, but not Igo1-S64A Our genetic and physiological data is in agreement with published work in budding yeast, Drosophila, Xenopus, and mammalian cells indicating that greatwall phosphorylates endo- sulfine to inhibit PP2A$B55 [8, 9, 27, 28, 35]. To test whether Igo1 is a direct target of Ppk18, we performed Ppk18 in vitro kinase assays using purified recombinant Igo1 and Igo1-S64A, as substrates. Extracts from wild-type (ppk18+) and Myc-tagged (ppk18-13myc) Ppk18 cells, treated for 1 hr with rapamycin in order to activate Ppk18, were immunoprecipitated with anti-c-Myc monoclonal antibodies. Ppk18-13myc immunoprecipitates were able to phosphorylate in vitro wild-type Igo1 but not Igo1-S64A (Figure S4A), indicating that fission yeast Ppk18 can act as a greatwall kinase.) Phosphorylation of Igo1 was severely impaired in cells deleted for ppk18 or expressing a kinase-dead version of ppk18 (ppk18- K595A or ppk18-KD) but was still present in cek1-deleted cells (Figure 4B), consistent with the idea that Ppk18 is the main greatwall kinase that phosphorylates Igo1 in medium with low nitrogen.
PMID:26804021	FYPO:0006272	(Fig. 7b) (comment, CHECK increased occurance)
PMID:26804021	FYPO:0005758	(Fig. 7a)
PMID:26804021	PBO:0101334	(Fig. 5)
PMID:26804021	PBO:0101333	(Fig. 5)
PMID:26804021	PBO:0101333	(Fig. 5)
PMID:26804021	PBO:0101333	(Fig. 5)
PMID:26804021	FYPO:0005917	(Fig. 5A)
PMID:26804021	FYPO:0005917	(Fig. 5A)
PMID:26804021	FYPO:0005917	(Fig. 5C)
PMID:26804021	FYPO:0005917	(Fig. 5A)
PMID:26804021	FYPO:0006260	(Fig. 4c)
PMID:26804021	FYPO:0006260	(Fig. 4)
PMID:26804021	PBO:0101332	(Fig. 3B)
PMID:26804021	PBO:0101332	(Fig. 3B)
PMID:26804021	PBO:0101331	(Fig. S6) check allele????
PMID:26804021	PBO:0101330	(Fig. 3D)
PMID:26804021	PBO:0101330	(Fig. 3B)
PMID:26804021	GO:0000775	(Fig. 1a)
PMID:26804021	PBO:0101329	(Fig. 1a, 4) (knob)
PMID:26804021	PBO:0101328	(Fig. 4c)
PMID:26804021	PBO:0101334	(Fig. 5)
PMID:26804021	PBO:0101334	(Fig. 5)
PMID:26804917	PBO:0102847	Serine 481 is phosphorylated by Cig2/Cdc2 during meiosis I. Phosphorylation decreases Fkh2 DNA binding affinity
PMID:26804917	PBO:0102857	EMSA fig4
PMID:26804917	PBO:0112058	EMSA fig4
PMID:2682257	PBO:0094620	(Fig. 6C) (comment: Cells contain cdc2-F19 mutant on multi copy LEU2+ plasmid.)
PMID:2682257	FYPO:0002085	(Fig. 6B) (comment: Cells contain cdc2-F19 mutant on multi copy LEU2+ plasmid.)
PMID:2682257	PBO:0106437	(Fig. 6B) (comment: Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid.)
PMID:2682257	PBO:0106435	(Figs 1, 2, 3, 4, 5) (comment: cells blocked in late G2 and in mid mitosis)
PMID:2682257	PBO:0093712	(Fig. 6b,C-F) (comment: Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid.)
PMID:2682257	PBO:0037727	(Fig. 6b,C-F) (comment: Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid.)
PMID:2682257	PBO:0106436	(Fig. 6b,C-F) (comment: Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid.)
PMID:2682257	PBO:0037729	(Fig. 6b,C-F) (comment: Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid.)
PMID:2682257	PBO:0093560	Data not shown, assayed by colony growth on plates
PMID:2682257	PBO:0023760	(Figs 1,2,3,4,5) (comment: cells blocked in late G2 and in mid mitosis)
PMID:26832414	PBO:0112009	(Fig. 4F)
PMID:26832414	FYPO:0006299	(Fig. 4C)
PMID:26832414	PBO:0120530	(Fig. 4D)
PMID:26832414	PBO:0108388	(Fig. 4B)
PMID:26832414	PBO:0104710	(Fig. 4A)
PMID:26832414	PBO:0094283	(Fig. 3B)
PMID:26832414	PBO:0094283	(Fig. 3B)
PMID:26869222	PBO:0100993	(comment: The size of the nucleus is not actually abnormal, it is the right size for the cell size but is variable because of the variable cell size at division)
PMID:26869222	PBO:0100994	(comment: the resistance to Cutin-1 is dependent on nuclear size. Longer cells have a larger nucleus and are more resistant compared to smaller cells with a smaller nucleus)
PMID:26869222	PBO:0037350	Cells show increased mitotic chromosome segregation defects in presence of Cutin-1
PMID:26869222	PBO:0035594	(comment: CONDITION cells grown at 29°C for 6 hours in 30µM Cutin-1)
PMID:26869222	PBO:0035594	(comment: CONDITION cells grown at 29°C for 6 hours in 30µM Cutin-1)
PMID:26869222	PBO:0100991	(comment: CONDITION cells grown at 29°C for 6 hours in 30µM Cutin-1)
PMID:26869222	PBO:0037342	(comment: This is in presence of 30µM Cutin-1 for 6 hours. Wild type cells show 36.3% abnormal chromosome segregation in same conditions)
PMID:26869222	PBO:0037351	(comment: CONDITION cells grown at 29°C)
PMID:26869222	PBO:0037352	(comment: CONDITION Cells grown at 29°C)
PMID:26869222	PBO:0099529	(comment: CONDITION cells grown at 29°C for 6 hours in 30µM Cutin-1)
PMID:26869222	PBO:0037348	(comment: CONDITION cells grown at 29°C for 6 hours in 30µM Cutin-1)
PMID:26869222	PBO:0100995	(comment: Cells show partial resistance to 30µM Cutin-1 for 6 hours.)
PMID:26869222	PBO:0100991	(comment: CONDITION cells grown at 29°C for 6 hours in 30µM Cutin-1)
PMID:26869222	PBO:0100991	(comment: CONDITION Growth was assayed in presence of 10µM Cutin-1.)
PMID:26869222	PBO:0100991	shows no chromosome defects or cell length defects growth in presence of 10-100µM Cutin-1 for 15 hours at 100µM Cutin-1 reduced to 70% compared to ~10% in wild type
PMID:26869222	PBO:0100991	(comment: CONDITION +10µM Cutin-1)
PMID:26869222	PBO:0100991	growth in presence of 10-100µM Cutin-1 for 15 hours at 100µM Cutin-1 reduced to 70% compared to ~10% in wild type; assayed in presence of 30µM Cutin-1 for 6 hours shows no chromosome defects or cell length defects
PMID:26869222	PBO:0037344	(comment: This is in presence of 30µM Cutin-1 for 6 hours. Wild type cells show 36.3% abnormal chromosome segregation in same conditions)
PMID:26869222	PBO:0100992	(comment: CONDITION cells grown at 29°C for 6 hours in 30µM Cutin-1)
PMID:26877082	PBO:0038070	(Figure 2C)
PMID:26877082	FYPO:0002872	(Figures 1A, S1A, S1B, 1D, S1E)
PMID:26877082	FYPO:0000419	(Figures 1A, S1A, S1B, 1D, S1E)
PMID:26877082	PBO:0038073	(Figure S4C)
PMID:26877082	PBO:0099935	(Figure 2D)
PMID:26877082	FYPO:0000134	(Figure 4A)
PMID:26877082	PBO:0099936	(Figure 2D) (comment: CHECK abnormal cable clustering)
PMID:26877082	PBO:0099935	(Figure 2D)
PMID:26877082	PBO:0020891	(Figure 2)
PMID:26882497	PBO:0100113	(Figure 5a)
PMID:26882497	PBO:0100112	(Figure 5a)
PMID:26882497	FYPO:0004318	(Figure 2b)
PMID:26882497	FYPO:0003762	(Figure 2b)
PMID:26882497	FYPO:0005781	(Figure 2b,c)
PMID:26882497	PBO:0095476	(Figure 2bc,5)
PMID:26882497	FYPO:0001687	(Figure S3)
PMID:26882497	FYPO:0001687	(Figure S3)
PMID:26882497	FYPO:0001687	(Figure S3)
PMID:26882497	FYPO:0000094	(Figure S3)
PMID:26882497	PBO:0100103	(Figure 2a) (comment: 20 mins after synchronized released into mitosis. I wouldn't want to guess exactly what stage of mitosis this is)
PMID:26882497	PBO:0100111	(Figure 5a)
PMID:26882497	PBO:0100111	(Figure 4a)
PMID:26882497	PBO:0100110	(Figure 4a)
PMID:26882497	PBO:0095474	(Figure 2bc,5)
PMID:26882497	PBO:0037610	(Figure 2b,c)
PMID:26882497	PBO:0095476	(Figure 2bc,5)
PMID:26882497	PBO:0100096	"(comment: they don't show the ""added during"" data so this is a bit anecdotal from the text)"
PMID:26882497	PBO:0100096	"(comment: they don't show the ""added during"" data so this is a bit anecdotal from the text)"
PMID:26882497	PBO:0100096	"(comment: they don't show the ""added during"" data so this is a bit anecdotal from the text)"
PMID:26882497	PBO:0100096	"(comment: they don't show the ""added during"" data so this is a bit anecdotal from the text)"
PMID:26882497	PBO:0100097	"(comment: they don't show the ""added during"" data so this is a bit anecdotal from the text)"
PMID:26882497	PBO:0100098	"(comment: they don't show the ""added during"" data so this is a bit anecdotal from the text)"
PMID:26882497	PBO:0100101	(Figure 1d)
PMID:26882497	PBO:0100100	(Figure 1d)
PMID:26882497	PBO:0100099	(Figure 1b)
PMID:26882497	MOD:00047	in text relevant to fig1
PMID:26882497	PBO:0100104	text to fig2
PMID:26882497	PBO:0100105	text to fig2
PMID:26882497	GO:0007094	(comment: it looks like it is involved in MAINTAINING the checkpoint) fig S4A and 2C
PMID:26882497	GO:0007094	(Fig. S4A and 2C)
PMID:26882497	MOD:00046	in text relevant to fig1)
PMID:26882497	MOD:00046	in text relevant to fig1)
PMID:26882497	GO:0007094	(Fig. S4A and 2C)
PMID:26882497	PBO:0100098	"(comment: they don't show the ""added during"" data so this is a bit anecdotal from the text)"
PMID:26882497	MOD:00046	in text relevant to fig1)
PMID:26882497	PBO:0100096	"(comment: they don't show the ""added during"" data so this is a bit anecdotal from the text)"
PMID:26882497	PBO:0109101	(Figure 1b)
PMID:26882497	PBO:0100094	(Figure 1a) (comment: they don't really show that the modification is phosphorylation, but considering the rest of the data this annotation seems ok)
PMID:26882497	PBO:0100102	(Figure 1d)
PMID:26882497	GO:1990757	(comment: 3 E2s mixed in the same assay so can't specify a substrate)
PMID:26882497	PBO:0100114	(Fig. 6) (comment: they incubate with 3 different E2s so can't specify a substrate)
PMID:26882497	FYPO:0005781	(Figure 2bc,5)
PMID:26882497	PBO:0100113	(Figure 5a)
PMID:26882497	PBO:0100112	(Figure 5a)
PMID:26882497	PBO:0100110	(Figure 5a)
PMID:26891792	PBO:0093678	(Fig. 4)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000098	(Fig. 1)
PMID:26891792	FYPO:0000021	(Fig. 3)
PMID:26891792	FYPO:0003559	(Fig. 4)
PMID:26891792	FYPO:0003559	(Fig. 4)
PMID:26891792	FYPO:0003559	(Fig. 4)
PMID:26891792	FYPO:0003559	(Fig. 4)
PMID:26891792	FYPO:0003559	(Fig. 4)
PMID:26891792	PBO:0093678	(Fig. 4)
PMID:26891792	PBO:0093678	(Fig. 4)
PMID:26891792	PBO:0093680	(Fig. 5)
PMID:26891792	PBO:0093680	(Fig. 5)
PMID:26891792	PBO:0093678	(Fig. 4)
PMID:26891792	PBO:0093679	(Fig. 5)
PMID:26891792	PBO:0093679	(Fig. 5)
PMID:26891792	PBO:0093679	(Fig. 5)
PMID:26900649	PBO:0108072	"(comment: chromatin recruiter) Together, we concluded that the primary defects observed in the ndc80-AK01 mutant can be attributed to impaired Mph1 recruitment to kinetochores, which leads to failure in recruitment of the other SAC components and abortive mitotic arrest. (comment: COUld also get 'upstream of/affects SAC"")"
PMID:26912660	PBO:0097545	(comment: exists during veg growth & glucose starv & HU stress)
PMID:26912660	PBO:0100552	(comment: exists during veg growth & glucose starv & HU stress)
PMID:26912660	PBO:0100551	(comment: exists during veg growth & glucose starv & HU stress)
PMID:26941334	GO:0110085	(comment: localization dependent on actin cytoskeleton)
PMID:26942678	FYPO:0000877	(comment: author statement)
PMID:26942678	GO:1990251	(comment: Erh1 localizes with Mmi1 both during mitotic cell cycle and meiosis)
PMID:26942678	FYPO:0005857	(comment: some up some down)
PMID:26942678	FYPO:0005858	(comment: some up some down)
PMID:26960792	PBO:0108232	(comment: RhoGAP, GTPase activating protein for Cdc42 and Rho2)
PMID:26960792	PBO:0108437	(comment: hard to be more specific when cell shape is also abnormal (Rga6 normally goes to lateral cortex & non-growing tip))
PMID:26960792	PBO:0108438	(comment: can't assess viability)
PMID:26960792	PBO:0108438	(comment: can't assess viability)
PMID:26960792	PBO:0108438	(comment: can't assess viability)
PMID:26960792	PBO:0108438	(comment: can't assess viability)
PMID:26960792	PBO:0108426	growing tips were longer and thinner than those of wild-type cells. This morphology is similar to the one caused by overexpression of Rga4.
PMID:26960792	PBO:0108438	(comment: can't assess viability)
PMID:26960792	PBO:0023536	(comment: can't assess viability)
PMID:26960792	PBO:0108438	(comment: can't assess viability)
PMID:26990381	GO:0032541	This was especially true in the case of Are1p. mYFP-Are1p and mYFP-Are2p were both localized throughout the nuclear and cortical/peripheral ER (Figure 2A,B). We repeated these experiments in wild-type genetic backgrounds and saw qualitatively similar YFP signal patterns (Figure 2C,D). Thus, the localizations of these two enzymes do not provide evidence to explain polarized lipid droplet formation in either cdc25-22 or wild-type fission yeast cells
PMID:26990381	FYPO:0005585	analysis revealed that both strains had reduced whole-cell and lipid droplet TAG levels (Figure 3F,I).
PMID:26990381	FYPO:0005585	analysis revealed that both strains had reduced whole-cell and lipid droplet TAG levels (Figure 3F,I).
PMID:26990381	FYPO:0007343	Yeast cells lacking both genes (plh1Δdga1Δ) had no droplets but instead showed vesicle-shaped BODIPY 493/503-stained structures when grown in YE5S (Figure 3J).
PMID:26990381	FYPO:0002061	The same cells were not viable when grown in YPO (Figure S2B,C).
PMID:26990381	FYPO:0007342	analysis revealed that both strains had reduced whole-cell and lipid droplet TAG levels (Figure 3F,I).
PMID:26990381	GO:0097038	This was especially true in the case of Are1p. mYFP-Are1p and mYFP-Are2p were both localized throughout the nuclear and cortical/peripheral ER (Figure 2A,B). We repeated these experiments in wild-type genetic backgrounds and saw qualitatively similar YFP signal patterns (Figure 2C,D). Thus, the localizations of these two enzymes do not provide evidence to explain polarized lipid droplet formation in either cdc25-22 or wild-type fission yeast cells
PMID:26990381	GO:0097038	This was especially true in the case of Are1p. mYFP-Are1p and mYFP-Are2p were both localized throughout the nuclear and cortical/peripheral ER (Figure 2A,B). We repeated these experiments in wild-type genetic backgrounds and saw qualitatively similar YFP signal patterns (Figure 2C,D). Thus, the localizations of these two enzymes do not provide evidence to explain polarized lipid droplet formation in either cdc25-22 or wild-type fission yeast cells
PMID:26990381	GO:0140042	Thus, plh1Δdga1Δ double knockouts appear to have hampered droplet biogenesis events and it is probable that TAG plays a crucial role in the ER escape hatch mechanism with minimal amounts needed even for SE lipid droplet formation [40].
PMID:26990381	GO:0097038	mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B).
PMID:26990381	GO:0097038	mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B).
PMID:26990381	GO:0097038	mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B).
PMID:26990381	GO:0032541	mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B).
PMID:26990381	GO:0032541	mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B).
PMID:26990381	GO:0032541	This was especially true in the case of Are1p. mYFP-Are1p and mYFP-Are2p were both localized throughout the nuclear and cortical/peripheral ER (Figure 2A,B). We repeated these experiments in wild-type genetic backgrounds and saw qualitatively similar YFP signal patterns (Figure 2C,D). Thus, the localizations of these two enzymes do not provide evidence to explain polarized lipid droplet formation in either cdc25-22 or wild-type fission yeast cells
PMID:26990381	PBO:0096874	There were a negligible number of BODIPY 493/503-stained droplets throughout those elongated double knockout cells compared to positive controls (Figure 1F,G).
PMID:26990381	GO:0140042	Thus, plh1Δdga1Δ double knockouts appear to have hampered droplet biogenesis events and it is probable that TAG plays a crucial role in the ER escape hatch mechanism with minimal amounts needed even for SE lipid droplet formation [40].
PMID:26990381	PBO:0098222	As expected, these cells contained negligible amounts of TAG after lysis and TLC analysis (Figure 3K).
PMID:26990381	FYPO:0007342	analysis revealed that both strains had reduced whole-cell and lipid droplet TAG levels (Figure 3F,I).
PMID:27023709	GO:0002183	(Fig. 2H) (comment: cell free system)
PMID:27023709	GO:0002183	(Fig. 2H) (comment: cell free system)
PMID:27023709	GO:0002183	(Fig. 2H) (comment: cell free system)
PMID:27023709	GO:0002183	(Fig. 2H) (comment: cell free system)
PMID:27023709	GO:0002183	(Fig. 2H) (comment: cell free system)
PMID:27023709	FYPO:0005387	(Fig. 2i)
PMID:27023709	FYPO:0005387	(Fig. 2i)
PMID:27023709	FYPO:0005387	(Fig. 2i)
PMID:27069798	GO:0051015	Bundling activity inferred from pull-down experiments as well as from fluorescence microscopy
PMID:27075176	GO:0051017	(comment: mixed orientations)
PMID:27075176	PBO:0097850	(Fig. 6C)
PMID:27075176	PBO:0097851	(Fig. 6C)
PMID:27075176	PBO:0097852	(Fig. 6C)
PMID:27075176	PBO:0097849	(Fig. 6C)
PMID:27075176	PBO:0097848	(Fig. 6C)
PMID:27075176	PBO:0097847	(Fig. 6C)
PMID:27075176	GO:0032432	(Figure 3A and Supplemental Video 3).
PMID:27075176	PBO:0097845	(Figure 1, C and D).
PMID:27082518	FYPO:0002087	(Fig. 7C,D)
PMID:27082518	FYPO:0002086	(Fig. 7D)
PMID:27082518	PBO:0097576	(Fig. 7E)
PMID:27082518	PBO:0097577	(Fig. 7E)
PMID:27082518	PBO:0097577	(Fig. 7E)
PMID:27082518	PBO:0097578	(Fig. S6A)
PMID:27082518	PBO:0097579	(Fig. S6A)
PMID:27082518	PBO:0097580	(Fig. S6 B) (comment: probably due to delayed fusion of TRAPP containing vesicles with PM)
PMID:27082518	PBO:0097581	(Fig. S6 C) (comment: probably due to delayed fusion of TRAPP containing vesicles with PM)
PMID:27082518	FYPO:0003440	Fiig 6AB
PMID:27082518	FYPO:0003440	(Fig. 6c)
PMID:27082518	FYPO:0001364	(Fig. 6A,B)
PMID:27082518	PBO:0019716	(Fig. 1 C-E)
PMID:27082518	PBO:0019716	(Fig. 1 C-E)
PMID:27082518	PBO:0019716	(Fig. 1B)
PMID:27082518	FYPO:0002088	(Fig. 2H, 7A)
PMID:27082518	PBO:0097572	(Fig. 3B)
PMID:27082518	PBO:0097573	(Fig. 3B)
PMID:27082518	FYPO:0005543	(Fig. S3B)
PMID:27082518	PBO:0022838	(Fig. 5a)
PMID:27082518	FYPO:0001368	(Fig. 6A,B)
PMID:27082518	FYPO:0001904	(Fig. 6A,B)
PMID:27082518	FYPO:0002061	(Figure S4D)
PMID:27082518	FYPO:0002060	(Fig. 6E)
PMID:27082518	PBO:0035171	(Fig. 6E)
PMID:27082518	PBO:0035172	(Fig. 6E)
PMID:27082518	PBO:0097574	(Fig. S4E)
PMID:27082518	PBO:0097575	(Fig. S4F and S4G)
PMID:27082518	FYPO:0002088	(Fig. 7A)
PMID:27082518	FYPO:0002088	(Fig. 7C,D)
PMID:27098497	PBO:0098835	(comment: same as without exo1+ overexpression)
PMID:27098497	PBO:0099553	(comment: distal to break point)
PMID:27098497	PBO:0099568	(comment: same as without htb1-K119R)
PMID:27098497	FYPO:0002553	(comment: same as without csn1delta)
PMID:27098497	FYPO:0002553	(comment: same as without csn5delt)
PMID:27098497	FYPO:0002553	(comment: worse than without rqh1delta)
PMID:27098497	PBO:0093617	(comment: same as rhp6delta alone)
PMID:27098497	PBO:0093617	(comment: same as rhp6delta alone)
PMID:27098497	PBO:0098835	(comment: same as without exo1delta)
PMID:27098497	FYPO:0002553	(comment: same as without exo1delta)
PMID:27101289	PBO:0034987	binds with high affinity to diverged S. pombe telomeric repeats)
PMID:27101289	GO:0043565	binds with high affinity to mammalian-type 5'-TTAGGG-3' telomeric repeats, and with very low affinity to diverged S. pombe telomeric repeats
PMID:27146110	FYPO:0003779	(Figure 2)
PMID:27146110	FYPO:0006084	(Table 1)
PMID:27146110	FYPO:0006084	(Table 1)
PMID:27146110	FYPO:0006084	(Table 1)
PMID:27146110	FYPO:0006084	(Table 1)
PMID:27146110	PBO:0107270	(Figure 1, 2)
PMID:27146110	PBO:0107271	(Figure 1, 2)
PMID:27146110	PBO:0107272	(Figure 1, 2)
PMID:27146110	PBO:0107273	(Figure 1, 2)
PMID:27146110	PBO:0107274	(Figure 1, 2)
PMID:27146110	FYPO:0006041	(Figure 2)
PMID:27146110	FYPO:0006041	(Figure 2)
PMID:27146110	FYPO:0006041	(Figure 2)
PMID:27146110	FYPO:0004021	(comment: *****The definition of this term is not right) Figure 2
PMID:27146110	FYPO:0004021	(comment: *****The definition of this term is not right) Figure 2
PMID:27146110	FYPO:0005364	(Figure 2)
PMID:27146110	FYPO:0005364	(Figure 2)
PMID:27146110	FYPO:0006043	(Figure 2)
PMID:27146110	FYPO:0005960	(Figure 3)
PMID:27146110	PBO:0107270	(Figure 3)
PMID:27146110	PBO:0107275	(Figure 4)
PMID:27146110	PBO:0107276	(Figure 4)
PMID:27146110	FYPO:0006045	(Figure 5)
PMID:27146110	FYPO:0006045	(Figure 5)
PMID:27146110	FYPO:0006046	(Figure 5)
PMID:27146110	FYPO:0006047	(Figure 5)
PMID:27146110	FYPO:0006049	(Figure 6)
PMID:27146110	FYPO:0006049	(Figure 6)
PMID:27146110	FYPO:0006049	(Figure 6)
PMID:27146110	FYPO:0006049	(Figure 6)
PMID:27146110	FYPO:0004101	(Figure 7, 1)
PMID:27146110	FYPO:0004101	(Figure 7)
PMID:27146110	FYPO:0004101	(Figure 7)
PMID:27146110	FYPO:0004101	(Figure 7)
PMID:27146110	FYPO:0004705	(comment: ***DELAYED) Figure 7
PMID:27146110	FYPO:0004705	(comment: DELAYED) Figure 7
PMID:27146110	FYPO:0004705	(Figure 7)
PMID:27146110	FYPO:0005342	(Figure 8)
PMID:27146110	FYPO:0005342	(Figure 8)
PMID:27146110	FYPO:0006044	(Figure 8) (comment: anaphase B)
PMID:27151298	PBO:0105108	(comment: K63-ubiquitin chain from 3 to 8 ubiquitin molecules)
PMID:27151298	PBO:0105082	(comment: Delete K63-ubiquitin chains from 3 to 8 ubiquitins)
PMID:27151298	PBO:0108725	(comment: K63-diubiquitin chain)
PMID:27151298	PBO:0105079	(comment: K63-ubiquitin chain from 3 to 8 ubiquitin molecules)
PMID:27151298	PBO:0105109	(comment: K63-diubiquitin chain)
PMID:27168121	FYPO:0000972	(Figure 3C)
PMID:27168121	FYPO:0001919	(Figure 3C)
PMID:27168121	PBO:0018421	(Fig. 1b)
PMID:27168121	PBO:0018576	(Fig. 1b)
PMID:27168121	FYPO:0001861	(Figure 3D)
PMID:27168121	FYPO:0001492	(Figure 3B)
PMID:27168121	FYPO:0001492	(Figure 3B)
PMID:27168121	FYPO:0000324	(Figure 3E)
PMID:27168121	GO:0005515	(Fig. 1C)
PMID:27183912	PBO:0113582	(comment: can't distinguish tlh1 and tlh2 as identical sequences)
PMID:27183912	PBO:0111256	(comment: can't distinguish tlh1 and tlh2 as identical sequences)
PMID:27188733	PBO:0099545	(comment: says increased proportion, which is a synonym)
PMID:27191590	FYPO:0001501	(Fig. 4E)
PMID:27191590	FYPO:0001501	(Fig. 4D)
PMID:27191590	FYPO:0000123	(Fig. 5A)
PMID:27191590	FYPO:0005193	(Fig. 1C, 6C, 7C, S5)
PMID:27191590	FYPO:0001501	(Fig. 1C, 4)
PMID:27191590	PBO:0108881	happens during cellular resposne to BFA Fig 3A, Fig 4A-B, Fig 5B, Fig S3
PMID:27191590	MOD:00696	(Fig. 6E-G)
PMID:27191590	GO:0005737	(Fig. 1B)
PMID:27191590	FYPO:0001501	(Fig. 6C)
PMID:27191590	PBO:0108130	(Fig. 6B)
PMID:27191590	PBO:0108131	(Fig. 6D)
PMID:27191590	FYPO:0005193	(Fig. 7C)
PMID:27191590	FYPO:0001501	(Fig. 7C)
PMID:27191590	FYPO:0001164	(Fig. 1C, 4)
PMID:27191590	FYPO:0005193	(Fig. 6C)
PMID:27191590	FYPO:0001501	(Fig. 6C)
PMID:27191590	PBO:0108129	(Fig. 6B)
PMID:27191590	FYPO:0005193	(Fig. 6C)
PMID:27194449	FYPO:0003347	(comment: CHECK of human pyruvyltransferase activity for the LacNAc-pNP)
PMID:27194449	FYPO:0003347	(comment: CHECK of human pyruvyltransferase activity for the LacNAc-pNP)
PMID:27268234	FYPO:0008221	(Fig. S5A)
PMID:27268234	FYPO:0007472	(Fig. S6)
PMID:27268234	PBO:0112815	(Fig. 3B)
PMID:27268234	PBO:0112814	(Fig. 3A)
PMID:27268234	FYPO:0007472	(Fig. S6)
PMID:27268234	FYPO:0003557	(Fig. S6)
PMID:27268234	FYPO:0008221	(Fig. S5A)
PMID:27268234	FYPO:0008222	(Fig. S5B)
PMID:27268234	FYPO:0008222	(Fig. S5B)
PMID:27268234	FYPO:0008223	(Fig. S5B)
PMID:27268234	FYPO:0008224	(Fig. S5B)
PMID:27268234	PBO:0112813	(Fig. 3B)
PMID:27268234	PBO:0112812	(Fig. 3A)
PMID:27268234	FYPO:0003557	(Fig. S6)
PMID:27325741	FYPO:0002061	(comment: temperature permissive for ts cdc17-K42)
PMID:27325741	FYPO:0002061	(comment: temperature permissive for ts cdc17-K42)
PMID:27325741	FYPO:0002061	(comment: temperature permissive for ts cdc17-K42)
PMID:27327046	FYPO:0002177	(Fig. S2, 3)
PMID:27327046	FYPO:0001357	(Fig. S2, 3)
PMID:27327046	FYPO:0001357	(Fig. S2, 3)
PMID:27327046	PBO:0097059	(Figures 2 and 3A, B)
PMID:27327046	PBO:0097060	(Fig. S2, 3)
PMID:27327046	PBO:0097058	(comment: I changed the evidence from IDA to IMP /AL)
PMID:27327046	GO:0140116	Deletion of both homologues fex1 and fex2 make cells highly sensitive to fluoride. Expression of fex1 from a plasmid in fex1Del/fex2Del double deletion mutant rescues fluoride sensitivity.
PMID:27327046	PBO:0097058	(comment: I changed the evidence from IDA to IMP /AL)
PMID:27327046	GO:0140116	Expression of fex1 from a plasmid in fex1Del/fex2Del double deletion mutant rescues fluoride sensitivity.
PMID:27334362	PBO:0037733	(Fig. 8B; Table B)
PMID:27334362	PBO:0037732	(Fig. 3C)
PMID:27334362	FYPO:0005554	(Fig. 3C)
PMID:27334362	FYPO:0000888	(Fig. 3C)
PMID:27334362	FYPO:0004745	(Fig. 3C)
PMID:27334362	FYPO:0005554	(Fig. 3C)
PMID:27334362	PBO:0105899	(Fig. 3D)
PMID:27334362	PBO:0105898	(Fig. 3D)
PMID:27334362	FYPO:0005554	(Fig. 3C)
PMID:27334362	PBO:0105897	(Fig. 3D)
PMID:27334362	FYPO:0000878	(Fig. 3C)
PMID:27334362	GO:0061638	(Fig. 3A,B)
PMID:27334362	GO:0005637	(Fig. 1a)
PMID:27334362	GO:0005637	(Fig. 1A)
PMID:27334362	FYPO:0001357	(Fig. 2C)
PMID:27334362	FYPO:0001234	(Fig. 2B)
PMID:27334362	PBO:0035015	(Fig. 2a)
PMID:27334362	PBO:0035014	(Fig. 2D)
PMID:27334362	PBO:0035014	(Fig. 2D) (comment: additive)
PMID:27334362	FYPO:0005371	(Fig. 2D)
PMID:27334362	FYPO:0005371	(Fig. 2D)
PMID:27334362	PBO:0035021	(Fig. 8B; Table B)
PMID:27334362	FYPO:0001839	(Fig. 8B; Table B)
PMID:27334362	FYPO:0002060	(Fig. 9D)
PMID:27334362	FYPO:0002060	(Fig. 9D)
PMID:27334362	FYPO:0002061	(Fig. 9D)
PMID:27334362	FYPO:0002061	(Fig. 9D)
PMID:27334362	FYPO:0000887	(Fig. 7B)
PMID:27334362	FYPO:0000887	(Fig. 7B)
PMID:27334362	FYPO:0001357	(Fig. 6b)
PMID:27334362	FYPO:0002430	(Fig. 9A)
PMID:27334362	FYPO:0000888	(Fig. 3C)
PMID:27350684	PBO:0105964	(comment: splicing of rad21, nda3 and mad2 is also affected)
PMID:27350684	FYPO:0001387	(comment: CHECK conditional synthetic lethal with rna14-11)
PMID:27350684	PBO:0105963	(comment: splicing of rad21, nda3 and mad2 is also affected)
PMID:27350684	PBO:0098383	(comment: splicing of rad21, nda3 and mad2 is also affected)
PMID:27350684	PBO:0105965	(comment: splicing of rad21, nda3 and mad2 is also affected)
PMID:27365210	PBO:0108636	We chose to study mei4 + and ssm4 + transcripts because they both contain a DSR region (.........we observed an increase in mei4 + and ssm4 + transcripts during vegetative growth in cells containing red5-2 (Fig. 1D).
PMID:27365210	PBO:0110962	We chose to study mei4 + and ssm4 + transcripts because they both contain a DSR region (.........we observed an increase in mei4 + and ssm4 + transcripts during vegetative growth in cells containing red5-2 (Fig. 1D).
PMID:27365210	PBO:0110963	Diploid pfal1Δ−/− cells show a decreased sporulation efficiency compared to wild-type cells (Fig. 2B). Less than 5% of pfal1Δ−/− cells sporulated, and ∼20% form misshapen asci on SPA medium (Fig. 2C), suggesting a meiotic defect.
PMID:27365210	PBO:0110964	Diploid red5-2 cells show severe sporulation defects, with <1% of cells producing asci.
PMID:27365210	PBO:0110965	qRT-PCR results show a large increase in rec8+ transcript levels during meiosis in wild-type cells, but no increase in pfal1Δ and red5-2 mutants (Fig. 3A).
PMID:27365210	PBO:0110965	qRT-PCR results show a large increase in rec8+ transcript levels during meiosis in wild-type cells, but no increase in pfal1Δ and red5-2 mutants (Fig. 3A).
PMID:27365210	PBO:0110962	We chose to study mei4 + and ssm4 + transcripts because they both contain a DSR region (.........we observed an increase in mei4 + and ssm4 + transcripts during vegetative growth in cells containing red5-2 (Fig. 1D).
PMID:27365210	PBO:0110966	These results demonstrate that pFal1, Red5, and Red1 are required to generate spliced rec8+ mRNA during starvation-induced meiosis.
PMID:27365210	PBO:0110966	These results demonstrate that pFal1, Red5, and Red1 are required to generate spliced rec8+ mRNA during starvation-induced meiosis.
PMID:27365210	PBO:0110966	These results demonstrate that pFal1, Red5, and Red1 are required to generate spliced rec8+ mRNA during starvation-induced meiosis.
PMID:27365210	FYPO:0008147	Consistent with the meiotic defects, this shift did not occur efficiently in diploid homozygous pfal1 and red1 mutants, reflected by a decreased splicing index (Fig. 3).
PMID:27365210	FYPO:0008147	Consistent with the meiotic defects, this shift did not occur efficiently in diploid homozygous pfal1 and red1 mutants, reflected by a decreased splicing index (Fig. 3).
PMID:27365210	FYPO:0008147	Consistent with the meiotic defects, this shift did not occur efficiently in diploid homozygous pfal1 and red1 mutants, reflected by a decreased splicing index (Fig. 3).
PMID:27365210	GO:0035145	We can easily detect interaction between pFal1- Myc and Mnh1-FTP (Fig. 4A).
PMID:27365210	GO:0035145	We can easily detect interaction between pFal1- Myc and Mnh1-FTP (Fig. 4A).
PMID:27365210	GO:0035145	We also observed interactions of pFal1-Myc with Rnps1-GFP and Y14-HA (Fig. 4B,D).
PMID:27365210	GO:0035145	We also observed interactions of pFal1-Myc with Rnps1-GFP and Y14-HA (Fig. 4B,D).
PMID:27365210	PBO:0110967	loss of mnh1 causes severe sporulation defects (Fig. 4F)
PMID:27365210	FYPO:0008147	Using qRT- PCR, we found a reduction in spliced meiotic transcripts of rec8+ in mnhΔ1−/− but not y14Δ−/− or rnps1Δ−/− (Fig. 5A)
PMID:27365210	PBO:0110966	These results demonstrate that pFal1, Red5, and Red1 are required to generate spliced rec8+ mRNA during starvation-induced meiosis.
PMID:27365210	GO:0000785	S. pombe, pFal1 localizes to chromatin-containing regions of the nucleus and is not restricted to the nucleolus.
PMID:27365210	GO:0030874	S. pombe, pFal1 localizes to chromatin-containing regions of the nucleus and is not restricted to the nucleolus.
PMID:27365210	FYPO:0001355	While viable, pfal1Δ showed a strong growth defect at all three temperatures tested (Fig. 1A).
PMID:27365210	FYPO:0001355	While viable, pfal1Δ showed a strong growth defect at all three temperatures tested (Fig. 1A).
PMID:27365210	FYPO:0001355	While viable, pfal1Δ showed a strong growth defect at all three temperatures tested (Fig. 1A).
PMID:27365210	PBO:0108651	We chose to study mei4 + and ssm4 + transcripts because they both contain a DSR region (.........we observed an increase in mei4 + and ssm4 + transcripts during vegetative growth in cells containing red5-2 (Fig. 1D).
PMID:27385337	PBO:0096604	(Table 1)
PMID:27385337	PBO:0038151	(Figure 3F)
PMID:27385337	PBO:0038152	(Figure 3F)
PMID:27385337	PBO:0038153	(Figure 3F)
PMID:27385337	PBO:0038154	(Figure 3F)
PMID:27385337	PBO:0038155	(Figure 3F)
PMID:27385337	PBO:0038155	(Figure 3F)
PMID:27385337	PBO:0096602	(Table 1)
PMID:27385337	PBO:0096603	(Table 1)
PMID:27385337	PBO:0096604	(Table 1)
PMID:27385337	PBO:0096603	(Table 1)
PMID:27385337	PBO:0096603	(Table 1)
PMID:27385337	PBO:0096603	(Table 1)
PMID:27385337	PBO:0096605	(Table 1)
PMID:27385337	PBO:0096603	(Table 1)
PMID:27385337	PBO:0096606	(Table 1)
PMID:27385337	PBO:0096607	(Fig. 5a)
PMID:27385337	PBO:0096603	(Figure 4F)
PMID:27385337	PBO:0096607	(Fig. 5a)
PMID:27385337	PBO:0096611	(Figure 4G)
PMID:27385337	PBO:0095095	(Figure 1F)
PMID:27385337	PBO:0096612	(Fig. 3C)
PMID:27385337	PBO:0096612	(Fig. 3C)
PMID:27385337	PBO:0096613	(Figure 4 G) (comment: localizes as a dot rather than a disk)
PMID:27385337	PBO:0096614	Supplemental Figure S4B
PMID:27385337	PBO:0034985	Supplemental Figure S4F and Table 2
PMID:27385337	PBO:0096601	Table 1, fig 3 C
PMID:27385337	FYPO:0002023	(Figure 5D,6)
PMID:27385337	PBO:0038150	(Figure 3F)
PMID:27385337	PBO:0096601	(Fig. 3C)
PMID:27385337	FYPO:0002023	(Figure 5D, Figure 6)
PMID:27388936	PBO:0101262	(Fig. 8c)
PMID:27388936	PBO:0093561	(Fig. 8a)
PMID:27388936	FYPO:0005440	(Fig. 5b)
PMID:27388936	PBO:0093560	(Fig. 8a)
PMID:27388936	PBO:0093560	(Fig. 5a)
PMID:27388936	PBO:0093561	(Fig. 5a)
PMID:27388936	PBO:0096314	(Fig. 8c)
PMID:27398807	FYPO:0000088	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0000089	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0000088	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0000088	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	PBO:0093559	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	PBO:0093579	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0001357	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0000963	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0001357	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	PBO:0099747	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	PBO:0093560	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	PBO:0093579	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0001357	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	PBO:0093561	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0006822	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	PBO:0093613	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0000963	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	PBO:0099741	(comment: CONDITION 30 degrees C)
PMID:27398807	PBO:0107296	(comment: CONDITION 30 degrees C)
PMID:27398807	PBO:0093614	(comment: CONDITION 30 degrees C)
PMID:27398807	PBO:0093580	(comment: CONDITION 30 degrees C)
PMID:27444384	GO:0051536	(comment: through conserved cysteines)
PMID:27451393	GO:0061638	(Fig. 2B and C, Fig. 2D and E)
PMID:27451393	FYPO:0000877	(Fig. 5A)
PMID:27451393	PBO:0103721	(Fig. 5C and D)
PMID:27451393	PBO:0112084	(Fig. 5C and D)
PMID:27451393	PBO:0103720	(comment: DNS)
PMID:27451393	GO:0005515	(Fig. 1A)
PMID:27451393	GO:0005515	(Fig. 1A)
PMID:27451393	GO:0033553	(Fig. 3A-D)
PMID:27451393	GO:0099115	(Fig. 3A-D)
PMID:27451393	FYPO:0004604	(Fig. 3E)
PMID:27451393	FYPO:0004604	(Fig. 3E)
PMID:27451393	PBO:0103718	(Fig. 4A and B)
PMID:27451393	FYPO:0003411	(Fig. 1B, D, E)
PMID:27451393	FYPO:0003411	(Fig. 1B, D, E)
PMID:27451393	FYPO:0000091	(Fig. G)
PMID:27451393	FYPO:0000091	(Fig. G)
PMID:27451393	GO:0061638	(Fig. 2, F and G)
PMID:27451393	FYPO:0000877	(Fig. 5A)
PMID:27451393	PBO:0103719	(comment: DNS)
PMID:27538348	FYPO:0004742	(Fig. 2)
PMID:27538348	FYPO:0004742	(Fig. 2)
PMID:27538348	FYPO:0004742	(Fig. 2)
PMID:27538348	PBO:0094282	(Fig. 2)
PMID:27538348	PBO:0109208	(Fig. 1G)
PMID:27538348	PBO:0095653	(Fig. 1F)
PMID:27538348	PBO:0101104	(Fig. 1G)
PMID:27538348	PBO:0107598	(Fig. 1F)
PMID:27538348	PBO:0113938	(Fig. 3C)
PMID:27538348	PBO:0113942	(Fig. 3C)
PMID:27538348	PBO:0113950	(Fig. 3C)
PMID:27538348	PBO:0113949	(Fig. 3C)
PMID:27538348	PBO:0112656	(Fig. 5A)
PMID:27538348	PBO:0113959	(Fig. 5A)
PMID:27538348	PBO:0113960	(Fig. 5A)
PMID:27538348	PBO:0113961	(Fig. 5A)
PMID:27538348	FYPO:0004742	(Fig. 5B and C)
PMID:27538348	FYPO:0004742	(Fig. 5B and C)
PMID:27538348	FYPO:0004743	(Fig. 5D)
PMID:27538348	FYPO:0004743	(Fig. 5D)
PMID:27538348	FYPO:0004742	(Fig. 5B and C)
PMID:27538348	FYPO:0004742	(Fig. 5B and C)
PMID:27538348	FYPO:0004742	(Fig. 5B and C)
PMID:27538348	FYPO:0004742	(Fig. 5B and C)
PMID:27538348	FYPO:0004743	(Fig. 5D)
PMID:27538348	PBO:0112526	(Fig. 3C)
PMID:27538348	PBO:0112530	(Fig. 3C)
PMID:27538348	PBO:0113948	(Fig. 3C)
PMID:27538348	PBO:0112521	(Fig. 3C)
PMID:27538348	PBO:0113947	(Fig. 3C)
PMID:27538348	PBO:0113946	(Fig. 3C)
PMID:27538348	PBO:0112528	(Fig. 3C)
PMID:27538348	PBO:0112527	(Fig. 3C)
PMID:27538348	PBO:0113945	(Fig. 3C)
PMID:27538348	PBO:0113944	(Fig. 3C)
PMID:27538348	PBO:0113943	(Fig. 3C)
PMID:27538348	PBO:0113942	(Fig. 3C)
PMID:27538348	PBO:0113941	(Fig. 3C)
PMID:27538348	PBO:0113940	(Fig. 3C)
PMID:27538348	PBO:0113939	(Fig. 3C)
PMID:27538348	PBO:0112521	(Fig. 3C)
PMID:27538348	PBO:0113937	(Fig. 3C)
PMID:27538348	PBO:0113936	(Fig. 3C)
PMID:27538348	PBO:0113935	(Fig. 3C)
PMID:27538348	PBO:0113934	(Fig. 3C)
PMID:27538348	PBO:0113933	(Fig. 3C)
PMID:27538348	PBO:0112525	(Fig. 3C)
PMID:27538348	PBO:0113932	(Fig. 3C)
PMID:27538348	PBO:0113931	(Fig. 3B and 4B)
PMID:27538348	PBO:0113930	(Fig. 3B and 4B)
PMID:27538348	PBO:0113929	(Fig. 3B and 4B)
PMID:27538348	PBO:0113928	(Fig. 3B and 4B)
PMID:27538348	PBO:0113927	(Fig. 3B and 4B)
PMID:27538348	GO:0005721	(Fig. 3B)
PMID:27538348	PBO:0094691	(Fig. 3A)
PMID:27538348	FYPO:0004742	(Fig. 2)
PMID:27538348	FYPO:0004743	(Fig. 5D)
PMID:27538348	FYPO:0004743	(Fig. 5D)
PMID:27538348	FYPO:0004743	(Fig. 5D)
PMID:27538348	PBO:0094282	(Fig. 5B and C)
PMID:27538348	PBO:0098772	(Fig. 5D)
PMID:27538348	PBO:0113962	Set3 is targeted to the promoters of clr4+ and rik1+, probably through its PHD finger. Set3 promotes transcription of clr4+ and rik1+.
PMID:27538348	PBO:0098772	(Fig. 1E)
PMID:27538348	FYPO:0006112	(Fig. 1G)
PMID:27538348	PBO:0095651	(Fig. 1F)
PMID:27538348	FYPO:0006111	(Fig. 1G)
PMID:27538348	PBO:0113926	(Fig. 1F)
PMID:27538348	PBO:0098773	(Fig. 1E)
PMID:27538348	PBO:0094282	(Fig. 1)
PMID:27538348	PBO:0094283	(Fig. 1)
PMID:27538348	PBO:0113955	(Fig. 4D)
PMID:27538348	PBO:0113954	(Fig. 4D)
PMID:27538348	PBO:0113953	(Fig. 4D)
PMID:27538348	PBO:0113958	(Fig. 4D)
PMID:27538348	PBO:0113957	(Fig. 4D)
PMID:27538348	PBO:0113955	(Fig. 4D)
PMID:27538348	PBO:0113956	(Fig. 4C)
PMID:27538348	PBO:0113930	(Fig. 4C)
PMID:27538348	PBO:0113929	(Fig. 4C)
PMID:27538348	PBO:0113931	(Fig. 4C)
PMID:27538348	PBO:0113955	(Fig. 4B)
PMID:27538348	PBO:0113954	(Fig. 4B)
PMID:27538348	PBO:0113953	(Fig. 4B)
PMID:27538348	PBO:0113945	(Fig. 3C)
PMID:27538348	PBO:0113952	(Fig. 3C)
PMID:27538348	PBO:0113951	(Fig. 3C)
PMID:27548313	FYPO:0000141	(comment: Kenichi comment mitotic defects mitotic defects caused by ace2 deletion)
PMID:27548313	FYPO:0000141	(comment: Kenichi comment mitotic defects mitotic defects caused by eng1 deletion)
PMID:27548313	FYPO:0000141	(comment: Kenichi comment mitotic defects mitotic defects caused by 343.20 deletion)
PMID:27558664	PBO:0097285	(comment: CHECK affecting sua1 affecting cys11 affecting met14)
PMID:27558664	PBO:0097286	(comment: CHECK affecting sua1 affecting cys11 affecting met14)
PMID:27558664	PBO:0097287	(comment: CHECK affecting sua1 affecting cys11 affecting met14)
PMID:27558664	PBO:0116834	A requirement for Mms19 is explained by its role in directing iron-sulfur cluster assembly into sulfite reductase as opposed to promoting DNA repair
PMID:27558664	PBO:0097286	(comment: CHECK affecting sua1 affecting cys11 affecting met14)
PMID:27558664	PBO:0097285	(comment: CHECK affecting sua1 affecting cys11 affecting met14)
PMID:27558664	PBO:0097287	(comment: CHECK affecting sua1 affecting cys11 affecting met14)
PMID:27558664	GO:0006535	Cys2 is a serine O-acetyltransferase required for cysteine biosynthesis Functional profiling revealed that Cys2 is essential for As/Cd tolerance (Table S5). Cys2 has greatest sequence homology to homoserine O-acetyltransferases, predicting that it should be involved with methionine biosynthesis. However, as noted previously, Met6 is also predicted to be a homoserine O-acetyltransferase (Ma et al. 2007). S. cerevisiae homoserine O-acetyltransferase Met2 is significantly more similar to Met6 than Cys2 in S. pombe, suggesting that in S. pombe Met6 is more likely the authentic homoserine O-acetyltransferase (Figure 3). Furthermore, met6D mutants require methionine supplementation for growth on defined minimal medium whereas cys2D cells require cysteine supplementation (Ma et al. 2007). Thus our data showing that cys2D but not met6D cells are highly sensitive to As/Cd toxicity, as well as our data indicating that methionine biosynthesis is not required for cadmium or arsenic resistance, support the notion that Cys2 is actually a serine O-acetyltransferase that is specifically essential for cysteine biosynthesis (Figure 3).
PMID:27558664	PBO:0116583	Cys2 is a serine O-acetyltransferase required for cysteine biosynthesis Functional profiling revealed that Cys2 is essential for As/Cd tolerance (Table S5). Cys2 has greatest sequence homology to homoserine O-acetyltransferases, predicting that it should be involved with methionine biosynthesis. However, as noted previously, Met6 is also predicted to be a homoserine O-acetyltransferase (Ma et al. 2007). S. cerevisiae homoserine O-acetyltransferase Met2 is significantly more similar to Met6 than Cys2 in S. pombe, suggesting that in S. pombe Met6 is more likely the authentic homoserine O-acetyltransferase (Figure 3). Furthermore, met6D mutants require methionine supplementation for growth on defined minimal medium whereas cys2D cells require cysteine supplementation (Ma et al. 2007). Thus our data showing that cys2D but not met6D cells are highly sensitive to As/Cd toxicity, as well as our data indicating that methionine biosynthesis is not required for cadmium or arsenic resistance, support the notion that Cys2 is actually a serine O-acetyltransferase that is specifically essential for cysteine biosynthesis (Figure 3).
PMID:27558664	PBO:0097285	(comment: CHECK affecting sua1 affecting cys11 affecting met14)
PMID:27558664	PBO:0097286	(comment: CHECK affecting sua1 affecting cys11 affecting met14)
PMID:27558664	PBO:0097287	(comment: CHECK affecting sua1 affecting cys11 affecting met14)
PMID:27558664	PBO:0097288	(comment: CHECK affecting gst2)
PMID:27558664	PBO:0097288	(comment: CHECK affecting gst2)
PMID:27558664	PBO:0097288	(comment: CHECK affecting gst2)
PMID:27587357	FYPO:0005760	(Fig. 3)
PMID:27587357	FYPO:0002061	(Fig. 3)
PMID:27587357	FYPO:0003333	(Fig. 1d)
PMID:27587357	FYPO:0006273	(comment: CHECK see ttps://github.com/pombase/fypo/issues/3152#issuecomment-340506554) A reduced UDP-glucose transport is a decreased transporter activity that produces an abnormal lower level of UDP-glucose in the endoplasmic reticulum lumen
PMID:27587357	FYPO:0002482	(Fig. 1d)
PMID:27587357	FYPO:0002061	(Fig. 1)
PMID:27587357	GO:0006491	endoplasmic reticulum quality control of glycoprotein folding The quality control of glycoprotein folding is a process that facilitates glycoprotein folding and retains in the endoplasmic reticulum folding intermediates.
PMID:27587357	GO:0005458	(comment: inferred from cell wall galactomannan defects)
PMID:27587357	PBO:0105973	(comment: inferred from cell wall galactomannan defects)
PMID:27587357	FYPO:0002196	(Fig. 3)
PMID:27587357	FYPO:0002196	(Fig. 3)
PMID:27587357	FYPO:0002196	(Fig. 3)
PMID:27587357	PBO:0105976	(Fig. 3)
PMID:27587357	FYPO:0003333	(Fig. 3)
PMID:27587357	FYPO:0003333	(Fig. 3)
PMID:27587357	FYPO:0005760	(Fig. 3)
PMID:27587357	FYPO:0002061	(Fig. 3)
PMID:27587357	FYPO:0002196	(Fig. 3)
PMID:27611590	FYPO:0005766	(comment: assayed Cdc20 recruitment)
PMID:27611590	FYPO:0005767	(comment: assayed Cdc20 recruitment)
PMID:27611590	FYPO:0005768	(comment: assayed Cdc20 recruitment)
PMID:27611590	FYPO:0005765	(comment: assayed Cdc20 recruitment)
PMID:27613427	PBO:0094268	AA medium (Rose et al 1990 Methods in Yeast Genetics)
PMID:27613427	PBO:0093612	AA medium (Rose et al 1990 Methods in Yeast Genetics)
PMID:27618268	PBO:0104641	(Figures 4C, S4B). (comment: non kinetochore bound)
PMID:27618268	PBO:0104629	(Fig. 1A)
PMID:27618268	PBO:0104630	(Fig. 1A)
PMID:27618268	PBO:0104630	(Fig. 1A)
PMID:27618268	PBO:0104631	(Fig. 1A)
PMID:27618268	PBO:0104632	(Fig. 1A)
PMID:27618268	PBO:0104632	(Fig. 1A)
PMID:27618268	FYPO:0005781	(Fig. 1B)
PMID:27618268	FYPO:0005781	(Fig. 1B)
PMID:27618268	FYPO:0003762	(Fig. 1B)
PMID:27618268	FYPO:0003762	(Fig. 1B)
PMID:27618268	FYPO:0003762	(Fig. 1B)
PMID:27618268	FYPO:0003762	(Fig. 1B)
PMID:27618268	PBO:0095476	(Fig. 1D)
PMID:27618268	PBO:0095476	(Fig. 1D)
PMID:27618268	PBO:0104633	(Figure 2A)
PMID:27618268	PBO:0101454	(Figure 2A)
PMID:27618268	PBO:0104634	(Figure 2B)
PMID:27618268	PBO:0095476	(Fig. 2D)
PMID:27618268	PBO:0104635	(Fig. 2E)
PMID:27618268	FYPO:0000168	(Figure 2E) (comment: how is this abnormal? i got confused here)
PMID:27618268	FYPO:0000168	(Figure 2D)
PMID:27618268	PBO:0104636	(Fig. 3C)
PMID:27618268	PBO:0104637	(Fig. 3C)
PMID:27618268	PBO:0104638	(Fig. 3C)
PMID:27618268	PBO:0104639	(Figure S3E)
PMID:27618268	PBO:0104640	(Figure S3E)
PMID:27618268	PBO:0101483	(Figure S3E)
PMID:27618268	PBO:0104640	(Figures 4B, S4A)
PMID:27618268	PBO:0104636	(Figures 4B, S4A)
PMID:27618268	PBO:0101480	(Figures 4C, S4B). (comment: non kinetochore bound)
PMID:27618268	PBO:0104638	((Figure S4C)). (comment: non kinetochore bound)
PMID:27618268	PBO:0104642	Together, these data indicate that Mph1 (Mps1) kinase and Dis2 (PP1) phosphatase antagonistically regulate the interaction of Mad1 and Mad2 with Bub1 in fission yeast, most likely through phosphorylation of the conserved central motif of Bub1.
PMID:27618268	PBO:0104643	Together, these data indicate that Mph1 (Mps1) kinase and Dis2 (PP1) phosphatase antagonistically regulate the interaction of Mad1 and Mad2 with Bub1 in fission yeast, most likely through phosphorylation of the conserved central motif of Bub1.
PMID:27627185	PBO:0095935	((comment: unphosphorylated form of tif211) inhibited by stress-inducedphosphorylation of Ser51 in the a subunit of eIF2(tif211)
PMID:27627185	PBO:0108748	(comment: unphosphorylated form of tif211)
PMID:27630265	PBO:0097861	(comment: CHECK during meiosis) (Figure 5, Supplemental Figure S4)
PMID:27630265	PBO:0097869	(Supplemental Figure S11B)
PMID:27630265	PBO:0097872	(Supplemental Figure S10A)
PMID:27630265	PBO:0097871	(Supplemental Figure S10A)
PMID:27630265	PBO:0097870	(Supplemental Figure S10A)
PMID:27630265	PBO:0097873	(comment: CHECK localizations at spindle poles during meiotic anaphase I) (Figure 6, Supplemental Figure S6)
PMID:27630265	PBO:0097873	(comment: CHECK localizations at spindle poles during meiotic anaphase I) (Figure 6, Supplemental Figure S6)
PMID:27630265	PBO:0097869	(Supplemental Figure S11B)
PMID:27630265	GO:0005628	(Figure 8A)
PMID:27630265	PBO:0097862	(comment: CHECK localizations at spindle poles during meiotic anaphase I) (Figure 6, Supplemental Figure S3)
PMID:27630265	PBO:0097860	(comment: CHECK localizations at spindle poles during meiotic anaphase I) (Figure 6, Supplemental Figure S6)
PMID:27630265	PBO:0037641	(Figure 6, S6)
PMID:27630265	PBO:0037648	Supplemental Figure S11
PMID:27630265	PBO:0097863	Supplemental Figure S11
PMID:27630265	PBO:0037650	(Supplemental Figure S11)
PMID:27630265	PBO:0035494	(Figure 8, S9)
PMID:27630265	PBO:0037651	(comment: CHECK initiation of forespore membrane delayed )(Figure 3, Table 2)
PMID:27630265	GO:0051285	(Figure 8A)
PMID:27630265	GO:0071341	(Figure 8A)
PMID:27630265	PBO:0035494	(Figure 4, 5, S4)
PMID:27630265	PBO:0037653	(Figure 4, 5)
PMID:27630265	GO:0005085	Sec2 interacted with specifically with GTP- bound forms of Ypt3 (Figure 7, Supplemental Figure S8).
PMID:27630265	PBO:0097869	Supplemental Figure S5A
PMID:27630265	PBO:0097868	(Figure 6A, S3)
PMID:27630265	PBO:0097867	Supplemental Figure S5A
PMID:27630265	PBO:0097866	(Figure 6A, S3)
PMID:27630265	PBO:0097865	Supplemental Figure S5A
PMID:27630265	GO:0005515	Spo13 interacted with both GTP- and GDP-bound forms of Ypt3 (Figure 7, Supplemental Figure S8).
PMID:27630265	GO:0032120	(Figure 1, S1)
PMID:27630265	PBO:0025347	(comment: from metaphase II to postmeiosis) (Figure 2)
PMID:27630265	PBO:0037641	(Figure 2)
PMID:27630265	FYPO:0002061	(Figure 1)
PMID:27630265	PBO:0097859	(comment: CHECK in vegetative cells) (Supplemental Figure S10)
PMID:27630265	PBO:0037642	(Figure 1, S1)
PMID:27630265	PBO:0097860	(comment: CHECK in sporulating cells) (Figure 9, Supplemental Figure S9, Supplemental Figure S10)
PMID:27630265	FYPO:0002061	(Figure 1)
PMID:27630265	FYPO:0002060	(Figure 1)
PMID:27630265	FYPO:0004609	Supplemental Figure S12
PMID:27630265	PBO:0097864	(Figure 5C, S4B)
PMID:27648579	PBO:0103243	(comment: substrate: bulk histone octamers)
PMID:27648579	PBO:0103241	(comment: CHECK not increased (relative to wild type Hht3+/Clr4+) as with hht3-K9M alone)
PMID:27648579	PBO:0103241	(comment: CHECK not increased (relative to wild type Hht3+/Clr4+) as with hht3-K9M alone)
PMID:27648579	PBO:0103234	(comment: substrate: recombinant mono-nucleosomes)
PMID:27655872	PBO:0095816	Western blot analysis show Sre1 cleavage defect under low oxygen
PMID:27655872	PBO:0095816	Western blot analysis show Sre1 cleavage defect under low oxygen
PMID:27655872	PBO:0095816	Western blot analysis show Sre1 cleavage defect under low oxygen
PMID:27655872	PBO:0095816	(Fig. 2C)
PMID:27655872	PBO:0095816	(Fig. 2C)
PMID:27655872	PBO:0096888	(Fig. 2G, lanes 10- 12)
PMID:27655872	GO:0000139	(Fig. 1E)
PMID:27655872	PBO:0095816	"(Fig. 2B) ""Sre1 cleavage defect under low oxygen"""
PMID:27655872	PBO:0103858	(Fig. 2D, lane 3)
PMID:27655872	PBO:0096888	(Fig. 2G, lanes 6-8)
PMID:27655872	PBO:0103859	(Fig. 3A, lane 4) both cleavage products
PMID:27655872	PBO:0103859	(Fig. 3A, lane 3)
PMID:27655872	PBO:0103860	(Fig. 3A, lane 3)
PMID:27655872	PBO:0103861	(Fig. 3D, compare lanes 3 and 4)
PMID:27655872	PBO:0103861	(Fig. 3D)
PMID:27655872	PBO:0103861	(Fig. 3D)
PMID:27655872	PBO:0103861	(Fig. 3D)
PMID:27655872	PBO:0103859	(Fig. 3D) compare lanes 3 and 4
PMID:27655872	PBO:0103862	(Figure 3E) precursor
PMID:27655872	PBO:0110516	(Fig. 3E, 3D)
PMID:27655872	PBO:0108957	(Fig. 3E, 3D)
PMID:27655872	PBO:0103865	(Fig. 5D, 5F) (comment: 4.5 fold) precursor)
PMID:27655872	PBO:0103866	PRECURSOR Fig 5E and F
PMID:27655872	PBO:0103866	(Fig. 5E,F) precursor
PMID:27655872	PBO:0103866	(Fig. 5E,F) precursor
PMID:27655872	PBO:0103866	(Fig. 5E,F) precursor
PMID:27655872	PBO:0103866	(Fig. 5E,F) precursor
PMID:27655872	PBO:0103867	(Fig. 5E,F) precursor
PMID:27655872	PBO:0103866	(Fig. 5E,F) precursor
PMID:27655872	PBO:0103868	(Fig. 5E and F)
PMID:27655872	PBO:0103869	(Fig. 6B)
PMID:27655872	PBO:0103869	(Fig. 6B)
PMID:27655872	PBO:0103857	(Fig. 2B, lanes 5-13)
PMID:27655872	PBO:0095816	"(Fig. 2B) ""Sre1 cleavage defect under low oxygen"""
PMID:27655872	PBO:0094110	(Fig. 2A)
PMID:27655872	FYPO:0002061	(Fig. 2A)
PMID:27655872	FYPO:0001245	(Fig. 2A)
PMID:27655872	PBO:0103870	(Fig. 6B)
PMID:27655872	PBO:0103870	(Fig. 6B)
PMID:27655872	GO:0005515	(Fig. 7A, lanes 4-6)
PMID:27655872	PBO:0103871	(Fig. 7A, lanes 4-6)
PMID:27655872	FYPO:0001245	(Fig. 8A)
PMID:27655872	PBO:0103872	(Fig. 8)
PMID:27655872	FYPO:0001245	(Fig. 8A)
PMID:27655872	PBO:0103872	(Fig. 8)
PMID:27655872	PBO:0095816	(Fig. 9A)
PMID:27655872	PBO:0095816	(Fig. 9A)
PMID:27655872	PBO:0099029	(Fig. 9A)
PMID:27655872	PBO:0103873	(Fig. 9A)
PMID:27655872	PBO:0103875	(Fig. 3A, lane 4) both cleavage products
PMID:27655872	FYPO:0001422	(Fig. 8C, 8D) Western blot analysis show decreased Sre1 cleavage activation under low oxygen
PMID:27655872	PBO:0095816	(Fig. 8C, 8D) Western blot analysis show Sre1 cleavage defect under low oxygen
PMID:27664110	FYPO:0003004	(Fig. 3)
PMID:27664110	FYPO:0000256	(Fig. 3)
PMID:27664110	FYPO:0000078	(Fig. 3)
PMID:27664110	PBO:0100417	(Fig. 2)
PMID:27664110	FYPO:0000256	(comment: text)
PMID:27664110	FYPO:0000256	(comment: text)
PMID:27664110	FYPO:0000256	(comment: text)
PMID:27664110	FYPO:0002009	(Fig. 1c)
PMID:27664110	PBO:0100416	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive temperature
PMID:27664110	PBO:0100416	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive temperature
PMID:27664110	PBO:0094264	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive temperature
PMID:27664110	PBO:0094264	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive temperature
PMID:27664110	PBO:0094264	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive temperature
PMID:27664110	PBO:0093558	(Fig. 1b) severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive temperature
PMID:27664110	PBO:0100415	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive temperature
PMID:27664110	PBO:0100416	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive temperature
PMID:27664110	FYPO:0003810	(Fig. 2)
PMID:27664222	PBO:0094996	(Figure 3A)
PMID:27664222	FYPO:0002693	(Figure 2A)
PMID:27664222	FYPO:0000763	(Figure 2A)
PMID:27664222	FYPO:0000962	Supplementary Figure S3A
PMID:27664222	FYPO:0001037	Supplementary Figure S3A NaCl or KCl)
PMID:27664222	FYPO:0000799	Supplementary Figure S1B
PMID:27664222	FYPO:0000096	Supplementary Figure S1B
PMID:27664222	FYPO:0000726	subcategory of oxidative stress known as GSH or disulfide stress (4). Indeed, a lower GSH/GSSG ratio was found after treatment with diamide or Cd (Supplementary Figure S4) in WT and in the SPBC29A10.12Δ strain
PMID:27664222	GO:0034599	(comment: CHECK detoxification of thiol disulphide (in response to disulphide stress))
PMID:27664222	GO:0034599	(comment: CHECK detoxification of thiol disulphide (in response to disulphide stress))
PMID:27664222	PBO:0094983	(Figure 3A)
PMID:27664222	PBO:0094984	(Figure 3A)
PMID:27664222	PBO:0094985	(Figure 3A)
PMID:27664222	PBO:0094986	(Figure 3A)
PMID:27664222	PBO:0094987	(Figure 3A)
PMID:27664222	PBO:0094988	(Figure 3A)
PMID:27664222	PBO:0094989	(Figure 3A)
PMID:27664222	PBO:0094990	(Figure 3A)
PMID:27664222	PBO:0094991	(Figure 3A)
PMID:27664222	PBO:0094992	(Figure 3A)
PMID:27664222	PBO:0094993	(Figure 3A)
PMID:27664222	GO:0001228	(Figure 3A)
PMID:27664222	PBO:0094994	(Figure 3A)
PMID:27664222	GO:0006366	(comment: CHECK detoxification of thiol disulphide (in response to disulphide stress))
PMID:27664222	PBO:0095000	(Figure 5A)
PMID:27664222	PBO:0022693	(Figure 5A)
PMID:27664222	GO:0005737	(Figure 5A)
PMID:27664222	PBO:0094999	(comment: diamide-induced promoters)
PMID:27664222	PBO:0094998	(Figure 3A)
PMID:27664222	PBO:0094997	(Figure 3A)
PMID:27664222	PBO:0094995	(Figure 3A)
PMID:27666591	FYPO:0005887	(Figure 1B, Figure S1F)
PMID:27666591	FYPO:0002061	(Figure 3A)
PMID:27666591	GO:0140898	(comment: not sure if this is quite right)
PMID:27666591	PBO:0095876	(Figure S5B)
PMID:27666591	PBO:0093564	(Figures 2B and 2C)
PMID:27666591	PBO:0110819	(Figure 5B)
PMID:27666591	PBO:0095880	(Figure 5C)
PMID:27666591	PBO:0093562	(Figure 5C)
PMID:27666591	PBO:0095871	(Figure 1B, Figure S1F)
PMID:27666591	FYPO:0000091	(Figure S1F)
PMID:27666591	FYPO:0000228	(Figure S1G)
PMID:27666591	PBO:0095870	(comment: VW: added exists_during..)
PMID:27666591	FYPO:0001234	(Figures 1F and S2B)
PMID:27666591	PBO:0095873	(Figures S2A and S2B)
PMID:27666591	GO:0140898	(Figure 5A)
PMID:27666591	PBO:0095877	(Figure 4D)
PMID:27666591	PBO:0095874	(Figures 2D and S3B)
PMID:27666591	FYPO:0001870	(Figures S1A and S1B)
PMID:27666591	PBO:0095871	(Figure 1A, S1C-S1E)
PMID:27666591	PBO:0095871	(Figure 7D)
PMID:27666591	PBO:0095875	(Figure 4C)
PMID:27666591	PBO:0093564	(Figure 5C)
PMID:27666591	FYPO:0005887	(Figure 2D)
PMID:27666591	PBO:0095881	(Figure 7B)
PMID:27666591	PBO:0095882	(Fig. 7e)
PMID:27666591	PBO:0095883	(Fig. 7F)
PMID:27666591	FYPO:0000091	(Figure 7C)
PMID:27666591	PBO:0095878	(Figure 5A)
PMID:27666591	PBO:0095872	(Figure 2A)
PMID:27687771	GO:0045944	(comment: target genes: cut6, vht1, bio2)
PMID:27687866	FYPO:0000972	(comment: CHECK acetaldehyde sensitivity)
PMID:27687866	FYPO:0000972	(comment: acetaldehyde absent)
PMID:27687866	FYPO:0000972	(comment: CHECK acetaldehyde sensitivity)
PMID:27697865	FYPO:0005976	(Fig. 5)
PMID:27697865	FYPO:0000228	(Fig. 6E)
PMID:27697865	PBO:0098846	(Fig. 6E)
PMID:27697865	FYPO:0001513	(comment: CHECK Fig.)
PMID:27697865	FYPO:0006476	(Fig. S4)
PMID:27697865	PBO:0098849	(Fig. 6E)
PMID:27697865	FYPO:0001355	(Fig. 6A)
PMID:27697865	FYPO:0004236	(Fig. 1A)
PMID:27697865	PBO:0098848	(Fig. 6, 7)
PMID:27697865	FYPO:0000324	(Fig. 5c)
PMID:27697865	FYPO:0005342	(Fig. 4E)
PMID:27697865	FYPO:0002638	(comment: vw: changed to increased activation, and D333A allele)
PMID:27697865	FYPO:0000274	(Fig. 5c)
PMID:27697865	FYPO:0004438	(Fig. 4)
PMID:27736299	PBO:0094266	(Fig. 1) (comment: CHECK 19.29% longer than control mean)
PMID:27736299	PBO:0106451	(Fig. 3) (comment: CHECK Nup189 level reduced to ~50% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	PBO:0095711	(Fig. 1) (comment: CHECK 16.50% shorter than control mean)
PMID:27736299	PBO:0094967	(Fig. 3) (comment: CHECK Wee1 level reduced to ~32% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	PBO:0095711	(Fig. 1) (comment: CHECK 11.15% shorter than control mean)
PMID:27736299	PBO:0106450	(Fig. 3) (comment: CHECK Pom1 level reduced to ~55% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	PBO:0095711	(Fig. 1) (comment: CHECK 10.86% shorter than control mean)
PMID:27736299	PBO:0106449	(Fig. 3) (comment: CHECK Suc1 level reduced to ~60% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	PBO:0097393	(Fig. 3) (comment: CHECK Ppa2 reduced to~45% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	PBO:0095712	(Fig. 1) (comment: CHECK 9.10% shorter than control mean)
PMID:27736299	PBO:0093767	(Fig. 1) (comment: CHECK 8.74% longer than control mean)
PMID:27736299	PBO:0106448	(Fig. 3) (comment: CHECK Cpc2 level reduced to about 55% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	PBO:0093767	(Fig. 1) (comment: CHECK 8.78% longer than control mean)
PMID:27736299	PBO:0106447	(Fig. 3) (comment: CHECK nup45 level reduced to ~45% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	PBO:0093767	(Fig. 1) (comment: CHECK 8.80% longer than control mean)
PMID:27736299	PBO:0106446	(Fig. 3) (comment: CHECK Sal3 level reduced to ~48% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	PBO:0094266	(Fig. 1) (comment: CHECK 10.81% longer than control mean)
PMID:27736299	PBO:0106445	(Fig. 3) (comment: CHECK Cdr1 level reduced to ~55% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	PBO:0094266	(Fig. 1) (comment: CHECK 11.63% longer than control mean)
PMID:27736299	PBO:0106444	(Fig. 3) (comment: CHECK Cdc2 level reduced to about 48% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	PBO:0094266	(Fig. 1) (comment: CHECK 14.43% longer than control mean)
PMID:27736299	PBO:0106443	(Fig. 3) (comment: CHECK cdc25 level reduced to ~48% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	PBO:0094266	(Fig. 1) (comment: CHECK 15.55% longer than control mean)
PMID:27736299	PBO:0106442	(Fig. 3) (comment: CHECK Nup186 level reduced to ~45% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	PBO:0094266	(Fig. 1) (comment: CHECK 15.82% longer than control mean)
PMID:27736299	PBO:0097048	(Fig. 3) (comment: CHECK cdc13 level reduced to ~44% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	PBO:0094266	(Fig. 1) (comment: CHECK 16.78% longer than control mean)
PMID:27736299	PBO:0106441	(Fig. 3) (comment: CHECK Nup97 level reduced to ~55% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	PBO:0094266	(Fig. 1) (comment: CHECK 18.92% longer than control mean)
PMID:27736299	PBO:0106440	(Fig. 3) (comment: CHECK Nsp1 level reduced to ~45% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	PBO:0019143	(Fig. 1) (comment: CHECK 31.94% longer than control mean)
PMID:27736299	PBO:0106438	(Fig. 3) (comment: CHECK Dea2 level reduced to 50%)
PMID:27736299	PBO:0094266	(Fig. 1) (comment: CHECK 23.46% longer than control mean)
PMID:27736299	PBO:0106439	(Fig. 3) (comment: CHECK Nup184 level reduced to 30% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27737912	PBO:0104260	(Fig. 6)
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007553	24h G0 cell microscopy
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27738016	FYPO:0007553	24h G0 cell microscopy
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27738016	FYPO:0007553	24h G0 cell microscopy
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27738016	FYPO:0007553	24h G0 cell microscopy
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27738016	FYPO:0007553	24h G0 cell microscopy
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27738016	FYPO:0007553	24h G0 cell microscopy
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27738016	FYPO:0007553	24h G0 cell microscopy
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27738016	FYPO:0007553	24h G0 cell microscopy
PMID:27738016	FYPO:0007553	24h G0 cell microscopy
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27738016	FYPO:0006935	24h G0 cell microscopy
PMID:27738016	PBO:0101386	G0 viability assay
PMID:27738016	PBO:0101386	G0 viability assay
PMID:27738016	PBO:0101386	G0 viability assay
PMID:27738016	PBO:0101386	G0 viability assay
PMID:27738016	PBO:0101381	24h G0 cell microscopy
PMID:27738016	FYPO:0006660	G0 viability assay
PMID:27738016	FYPO:0006518	G0 viability assay
PMID:27738016	FYPO:0000091	15 ug/ml thiabendazole
PMID:27738016	FYPO:0000091	15 ug/ml thiabendazole
PMID:27738016	FYPO:0000091	15 ug/ml thiabendazole
PMID:27738016	FYPO:0000091	15 ug/ml thiabendazole
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27738016	FYPO:0006518	G0 viability assay
PMID:27738016	FYPO:0006660	G0 viability assay
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27738016	PBO:0094072	G0 viability assay
PMID:27738016	FYPO:0006079	2 day G0 ChIP
PMID:27738016	PBO:0101387	2 day G0 ChIP
PMID:27738016	FYPO:0006518	G0 viability assay
PMID:27738016	FYPO:0006660	G0 viability assay
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27738016	PBO:0101388	S13; Tetrad dissection
PMID:27738016	PBO:0101388	S13; Tetrad dissection
PMID:27738016	PBO:0101389	S13; Tetrad dissection
PMID:27738016	PBO:0101386	G0 viability assay
PMID:27738016	PBO:0101386	G0 viability assay
PMID:27738016	FYPO:0006660	G0 viability assay
PMID:27738016	PBO:0101386	G0 viability assay
PMID:27738016	FYPO:0000964	15 ug/ml thiabendazole
PMID:27738016	FYPO:0000091	15 ug/ml thiabendazole
PMID:27738016	FYPO:0000091	15 ug/ml thiabendazole
PMID:27738016	FYPO:0000091	15 ug/ml thiabendazole
PMID:27738016	FYPO:0000091	15 ug/ml thiabendazole
PMID:27738016	FYPO:0000091	15 ug/ml thiabendazole
PMID:27738016	PBO:0101381	24h G0 cell microscopy
PMID:27738016	FYPO:0006518	G0 viability assay
PMID:27738016	PBO:0101381	24h G0 cell microscopy
PMID:27738016	FYPO:0006518	G0 viability assay
PMID:27738016	PBO:0101381	24h G0 cell microscopy
PMID:27738016	FYPO:0006518	G0 viability assay
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27738016	FYPO:0007553	24h G0 cell microscopy
PMID:27738016	FYPO:0000091	15 ug/ml thiabendazole
PMID:27738016	GO:0070317	mutant defective in maintenance of quiescence
PMID:27738016	GO:0070317	mutant defective in maintenance of quiescence
PMID:27738016	FYPO:0000069	(Fig. S6) (comment: CHECK 15 ug/ml or 20 ug/ml thiabendazole)
PMID:27738016	FYPO:0000069	(Fig. S6) (comment: CHECK 15 ug/ml or 20 ug/ml thiabendazole)
PMID:27738016	FYPO:0000069	(Fig. S6) (comment: CHECK 15 ug/ml or 20 ug/ml thiabendazole)
PMID:27738016	FYPO:0000069	(Fig. S6) (comment: CHECK 15 ug/ml or 20 ug/ml thiabendazole
PMID:27738016	FYPO:0007553	24h G0 cell microscopy
PMID:27738016	GO:0070317	mutant defective in maintenance of quiescence
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0000091	15 ug/ml thiabendazole
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	PBO:0101391	Decreased RNA polymerase I at rDNA during vegetative growth; nuc1-FLAG
PMID:27738016	PBO:0101392	Increase of stalled RNA polymerase I at rDNA during G0 phase; nuc1-FLAG
PMID:27738016	PBO:0101392	Increase of stalled RNA polymerase I at rDNA during G0 phase; nuc1-FLAG
PMID:27738016	PBO:0101393	Increase of stalled RNA polymerase I at rDNA during G0 phase; nuc1-FLAG
PMID:27738016	PBO:0101393	Increase of stalled RNA polymerase I at rDNA during G0 phase; nuc1-FLAG
PMID:27738016	FYPO:0004032	Increased RNA polymerase II at rDNA during vegetative growth
PMID:27738016	FYPO:0007639	Increased gH2AX/H2A ratio (marker of DNA damage) at rDNA during G0; 2 day G0 ChIP
PMID:27738016	FYPO:0007639	Increased gH2AX/H2A ratio (marker of DNA damage) at rDNA during G0; 2 day G0 ChIP
PMID:27738016	FYPO:0007639	Increased gH2AX/H2A ratio (marker of DNA damage) at rDNA during G0; 2 day G0 ChIP
PMID:27738016	FYPO:0007639	Increased gH2AX/H2A ratio (marker of DNA damage) at rDNA during G0; 2 day G0 ChIP
PMID:27738016	FYPO:0000429	(comment: CHECK G0-exit)
PMID:27738016	PBO:0101396	(comment: CHECK Rad22-YFP, G0-exit)
PMID:27738016	FYPO:0002835	small-RNA-seq
PMID:27738016	FYPO:0004817	small-RNA-seq
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	PBO:0101386	G0 viability assay
PMID:27738016	FYPO:0007629	G0 viability assay
PMID:27738016	PBO:0101386	G0 viability assay
PMID:27738016	PBO:0098933	G0 viability assay
PMID:27738016	PBO:0098933	G0 viability assay
PMID:27738016	FYPO:0007553	24h G0 cell microscopy
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27738016	FYPO:0007553	24h G0 cell microscopy
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27738016	PBO:0098933	G0 viability assay
PMID:27738016	PBO:0098933	G0 viability assay
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27738016	FYPO:0007553	24h G0 cell microscopy
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27738016	FYPO:0007553	24h G0 cell microscopy
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27738016	FYPO:0007553	24h G0 cell microscopy
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27738016	FYPO:0007553	24h G0 cell microscopy
PMID:27738016	FYPO:0007553	G0 viability assay
PMID:27746023	PBO:0105075	(Figure 2C)
PMID:27746023	PBO:0105074	(Figure 2C)
PMID:27746023	PBO:0105074	(Figure 2D)
PMID:27746023	PBO:0105077	Movie S4. Sty1 activity is critical for maintaining a non-polarized Cdc42 module in N-starved quiescent cells.
PMID:27746023	PBO:0105074	(Figures 2A, S1A; Movie S1)
PMID:27746023	PBO:0105074	Movie S4. Sty1 activity is critical for maintaining a non-polarized Cdc42 module in N-starved quiescent cells.
PMID:27746023	FYPO:0000646	(comment: arrested)
PMID:27746023	PBO:0105074	(Figures S1C, S1D)
PMID:27746023	PBO:0105074	(Figures S1C, S1D)
PMID:27746023	PBO:0105076	(comment: CHECK during nitrogen starvation). Although many mutants in the SAPK pathway have defects in mating and meiosis, this result may help to explain why sty1D and wis1D mutants in particular continue to elongate upon N starvation, unlike other mutants in the pathway
PMID:27746023	PBO:0105075	(Figure S1B)
PMID:27746023	FYPO:0006634	unlike WT cell elongation continued after actin depolymerization, (Figures 2A and 2B; Movie S1) conclusions. 1. the SAPK pathway is required for CRIB dispersal after LatA treatment. 2 the actin cytoskeleton per se is not required for stability of the Cdc42 polarity module at cell tips. 3. cell elongation can occur in the complete absence of the actin cytoskeleton.
PMID:27746023	FYPO:0006634	unlike WT cell elongation continued after actin depolymerization, (Figures 2A and 2B; Movie S1) conclusions. 1. the SAPK pathway is required for CRIB dispersal after LatA treatment. 2 the actin cytoskeleton per se is not required for stability of the Cdc42 polarity module at cell tips. 3. cell elongation can occur in the complete absence of the actin cytoskeleton.
PMID:27811944	PBO:0099388	deletion of Sre1 aa 877-900 also destabilized Sre1 and prevented proteolytic activation
PMID:27811944	PBO:0099388	mutation destabilized Sre1 precursor and prevented Sre1 proteolytic cleavage
PMID:27811944	PBO:0099389	mutation destabilized Sre1 precursor and prevented Sre1 proteolytic cleavage
PMID:27851962	GO:0030014	(Figure 1)
PMID:27851962	GO:0030014	(Figure 1)
PMID:27851962	GO:0030014	(Figure 1)
PMID:27851962	GO:0030014	(Figure 1)
PMID:27851962	GO:0030014	(Figure 1)
PMID:27851962	GO:0030014	(Figure 1)
PMID:27851962	GO:0030014	(Figure 1)
PMID:27852900	PBO:0097768	(Fig. 4) (comment: GFP-LactC2 probe expressed from pREP3X)
PMID:27852900	PBO:0097763	(Figure 8e)
PMID:27852900	PBO:0097762	(Fig. 8a)
PMID:27852900	PBO:0019132	(Fig. 8a)
PMID:27852900	PBO:0097762	(Fig. 8a)
PMID:27852900	FYPO:0004963	(Figure 5D)
PMID:27852900	PBO:0097771	(Fig. 7)
PMID:27852900	PBO:0097770	(Fig. 7)
PMID:27852900	FYPO:0006547	(Figure 3, A and E)
PMID:27852900	FYPO:0006547	(Figure 3, A and E)
PMID:27852900	PBO:0097767	(Fig. 4) (comment: GFP-LactC2 probe expressed from pREP3X)
PMID:27852900	FYPO:0002297	(Fig. 8d)
PMID:27852900	FYPO:0004964	(Fig. 8d)
PMID:27852900	PBO:0097769	(comment: GFP-LactC2 probe expressed from pREP3X)
PMID:27852900	PBO:0097769	(comment: GFP-LactC2 probe expressed from pREP3X)
PMID:27852900	PBO:0097769	(comment: GFP-LactC2 probe expressed from pREP3X)
PMID:27852900	PBO:0097768	(Fig. 4B) (comment: GFP-LactC2 probe expressed from pREP3X)
PMID:27852900	PBO:0097767	(comment: GFP-LactC2 probe expressed from pREP3X)
PMID:27871365	GO:0006281	(comment: from later paper: We speculate that SPRTN is able to degrade DPCs to peptide adducts that are sufficiently small for efficient TLS. https://www.sciencedirect.com/science/article/pii/S1097276518309948)
PMID:27871365	GO:0003690	(Fig. 3H)
PMID:27871365	GO:0003697	(Fig. 3H)
PMID:27872152	PBO:0093562	(Fig. 7D)
PMID:27872152	PBO:0093562	(Fig. 7D)
PMID:27872152	FYPO:0002061	(Fig. 7B,C)
PMID:27872152	PBO:0108498	(comment: 2.0% versus <0.1%) (Fig. 7F)
PMID:27872152	PBO:0093562	(Fig. 7D)
PMID:27872152	PBO:0108497	(Fig. 7E)
PMID:27872152	PBO:0108496	(comment: CHECK adaptor for dis1-microtubule)
PMID:27872152	GO:0005515	(Fig. 2A) (Fig. 2B; Fig. S2B).
PMID:27886462	PBO:0094532	(Table 2)
PMID:27886462	PBO:0094530	(Table 2)
PMID:27886462	PBO:0094523	(Table 2)
PMID:27886462	PBO:0109849	(Figure 3A)
PMID:27886462	FYPO:0003004	(Figure 3C)
PMID:27886462	PBO:0094194	(Figure 3C)
PMID:27886462	FYPO:0003004	(Figure 3C)
PMID:27886462	FYPO:0003004	(Figure 3C)
PMID:27886462	PBO:0094524	(Table 2)
PMID:27886462	PBO:0094527	(Table 2)
PMID:27886462	PBO:0094526	(Table 2)
PMID:27886462	PBO:0109849	(Figure 3A)
PMID:27886462	PBO:0100387	(Table 4)
PMID:27886462	PBO:0100386	(Table 4)
PMID:27886462	PBO:0100385	(Table 4)
PMID:27886462	FYPO:0000245	(Figure 1A)
PMID:27886462	FYPO:0001357	(Figure 1A)
PMID:27886462	FYPO:0001357	(Figure 1A)
PMID:27886462	FYPO:0001357	(Figure 1A)
PMID:27886462	FYPO:0001357	(Figure 1A)
PMID:27886462	FYPO:0000245	(Figure 1A)
PMID:27886462	FYPO:0000245	(Figure 1A)
PMID:27886462	FYPO:0000245	(Figure 1A)
PMID:27886462	FYPO:0000245	(Figure 1A)
PMID:27886462	FYPO:0005760	(Figure 1B)
PMID:27886462	PBO:0100384	(Table 4)
PMID:27886462	PBO:0100383	(Table 4)
PMID:27886462	FYPO:0005760	(Figure 1B)
PMID:27886462	FYPO:0005760	(Figure 1B)
PMID:27886462	FYPO:0005760	(Figure 1B)
PMID:27886462	FYPO:0003730	(Figure 1C)
PMID:27886462	FYPO:0003730	(Figure 1C)
PMID:27886462	FYPO:0003730	(Figure 1C)
PMID:27886462	FYPO:0003730	(Figure 1C)
PMID:27886462	FYPO:0003730	(Figure 1C)
PMID:27886462	FYPO:0003730	(Figure 1C)
PMID:27886462	FYPO:0003730	(Figure 1C)
PMID:27886462	FYPO:0003730	(Figure 1C)
PMID:27886462	PBO:0100365	(Figure 2A)
PMID:27886462	PBO:0100365	(Figure 2A)
PMID:27886462	PBO:0100365	(Figure 2A)
PMID:27886462	PBO:0100365	(Figure 2A)
PMID:27886462	PBO:0109849	(Figure 3A)
PMID:27886462	PBO:0109849	(Figure 3A)
PMID:27886462	PBO:0100382	(Table 3)
PMID:27886462	PBO:0100381	(Table 3)
PMID:27886462	PBO:0100380	(Table 3)
PMID:27886462	PBO:0100379	(Table 3)
PMID:27886462	PBO:0100378	(Table 3)
PMID:27886462	PBO:0100377	(Table 3)
PMID:27886462	PBO:0100376	(Table 3)
PMID:27886462	PBO:0100375	(Table 3)
PMID:27886462	PBO:0099519	(Figure 4)
PMID:27886462	PBO:0100374	(Figure 4, Table 3)
PMID:27886462	PBO:0100373	(Figure 4, Table 3)
PMID:27886462	PBO:0100372	(Figure 4, Table 3)
PMID:27886462	PBO:0100371	(Figure 4, Table 3)
PMID:27886462	PBO:0100370	(Figure 4, Table 3)
PMID:27886462	PBO:0100369	(Figure 4, Table 3)
PMID:27886462	PBO:0100368	(Figure 4, Table 3)
PMID:27886462	PBO:0100367	(Table 2)
PMID:27886462	PBO:0100366	(Table 2)
PMID:27886462	PBO:0094529	(Table 2)
PMID:27889481	FYPO:0000737	(comment: CHECK abolished)
PMID:27889481	PBO:0098189	(Figure 1C) In contrast, in the absence of the bouquet, the duplicated SPBs often fail to separate . Indeed, 75.5% of bqt1Δ cells with defective meiosis show problems in SPB separation at MI
PMID:27889481	PBO:0098188	(Figure 1C) In contrast, in the absence of the bouquet, the duplicated SPBs often fail to separate. Indeed, 75.5% of bqt1Δ cells with defective meiosis show problems in SPB separation at MI
PMID:27889481	PBO:0035493	(Figure 1B)
PMID:27889481	PBO:0035494	(Figure 1B)
PMID:27889481	PBO:0098202	(Figure 3D, E)
PMID:27889481	PBO:0098203	(Figure 4B)
PMID:27889481	PBO:0098204	(Figures 4D-E, S5B, S5D) sad1.2 cells exhibiting total centromere dissociation not only fail to insert but also appear to separate from the NE, dislodging into the cytoplasm
PMID:27889481	PBO:0098205	(Fig. 5C)
PMID:27889481	PBO:0098206	(Figure 5B) (comment: centromeres are also released from LINC in bouquet-defective cells)
PMID:27889481	FYPO:0004160	(Figure 5C) spindle formation occurs normally at both MI and MII in sad1.2 meiosis
PMID:27889481	FYPO:0004367	(Fig. 6)
PMID:27889481	FYPO:0002060	(Fig. 6)
PMID:27889481	PBO:0035494	(Figure 1D)
PMID:27889481	PBO:0035493	(Figure 1D)
PMID:27889481	PBO:0098190	(Figure 1E) In contrast, Alp4 localization is defective (ie one or both SPB signals lack any detectable Alp4 colocalization at MI onset) in 59% of bqt1Δ meiocytes (n= 100, p<0.01) from the onset of MI onwards
PMID:27889481	PBO:0098191	(Figure 1E) and all (n=50, p<0.01) those SPBs failing to recruit Alp4 show SPB separation problems and failed spindle nucleation (Figure 1E).
PMID:27889481	PBO:0098192	(comment: Figure) In 100% of the bqt1Δ cells that show monopolar spindles (n=11), those spindles are nucleated specifically from the old SPB (Figure S1I). Hence, failed spindle nucleation in the absence of the bouquet is specific to the new SPB.
PMID:27889481	FYPO:0007487	(Figure 1C, 1F, 1G) We previously observed a tendency for the SPB to dissociate from the NE just prior to meiotic spindle formation in the bqt1Δ setting (Fennell et al., 2015; Tomita and Cooper, 2007); indeed, SPBs showing problems in separation typically appear to dislodge into the cytoplasm (Figure 1C, yellow arrowheads
PMID:27889481	FYPO:0005736	(Figure 1)
PMID:27889481	FYPO:0006363	(Figure 1)
PMID:27889481	FYPO:0002060	(Fig. 2c)
PMID:27889481	FYPO:0002061	(Fig. 2c)
PMID:27889481	FYPO:0001234	(Fig. 2c)
PMID:27889481	FYPO:0002061	(Fig. 2c)
PMID:27889481	PBO:0098193	(Figure 3A) Sad1.2-GFP remains stably associated with the SPB throughout interphase, in contrast to Sad1.1-GFP, which is destabilized at 36°C
PMID:27889481	PBO:0098194	(Figure 3A) Sad1.2-GFP remains stably associated with the SPB throughout interphase, in contrast to Sad1.1-GFP, which is destabilized at 36°C
PMID:27889481	PBO:0098195	(Figures 3B-C, S4A)
PMID:27889481	PBO:0098196	(Figures 3B-C, S4A)
PMID:27889481	PBO:0098197	(Figure S4B)
PMID:27889481	PBO:0098198	(Figure S4B)
PMID:27889481	PBO:0098199	(Fig. 3DE) sad1.2 cells often show extra Mis6-GFP foci unassociated with the SPB, even at permissive temperature
PMID:27889481	PBO:0098200	(Figure 3D, E) At restrictive temperature, a population of sad1.2 cells emerges in which all three centromeres are clearly dissociated from the SPB
PMID:27889481	PBO:0098201	(Fig. 3D, E)
PMID:27889481	FYPO:0007486	(Figure 1)
PMID:27898700	FYPO:0001369	(Fig. 1F,G) slides along axis from midpoint
PMID:27898700	FYPO:0001365	(Fig. 1F,G)
PMID:27898700	FYPO:0001035	(Fig. 2 A) (comment: 3x WT)
PMID:27898700	FYPO:0005873	(Fig. 2 A) (comment: 2x WT)
PMID:27898700	FYPO:0004653	(Fig. 1F,G)
PMID:27898700	FYPO:0001368	(Fig. 1F,G)
PMID:27898700	PBO:0037854	(Fig. 1C)
PMID:27898700	PBO:0037853	(Fig. 1C)
PMID:27898700	PBO:0096854	(Fig. 4)
PMID:27898700	PBO:0095928	(Fig. 4)
PMID:27898700	PBO:0037852	(Fig. 1C)
PMID:27898700	FYPO:0002423	(Fig. 1B) (comment: CHECK swollen multiseptate elongated)
PMID:27898700	PBO:0096857	(Fig. 4)
PMID:27898700	FYPO:0005469	(Fig. 1A) (comment: CHECK during cytokinesis)
PMID:27898700	PBO:0096856	(Fig. 4)
PMID:27898700	FYPO:0005872	(Fig. 2A)
PMID:27898700	FYPO:0005871	(Fig. 2A)
PMID:27898700	FYPO:0003205	(Fig. 2A)
PMID:27898700	PBO:0096855	(Fig. S4D, S4E)
PMID:27898700	PBO:0096854	(Fig. 4)
PMID:27898700	PBO:0095928	(Fig. 4)
PMID:27898700	PBO:0096853	(Fig. S3B)
PMID:27898700	PBO:0096852	(Fig. S3B)
PMID:27898700	PBO:0037851	(Fig. 1A)
PMID:27898700	PBO:0096858	(Fig. 4)
PMID:27901072	PBO:0099062	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099067	(Fig. 6)
PMID:27901072	PBO:0099063	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099061	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099060	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099059	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099058	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099057	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099056	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099063	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099061	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099060	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099059	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099058	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099057	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099055	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099054	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099053	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099052	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099051	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099050	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099049	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099048	(comment: asynchronous) fig 3a
PMID:27901072	PBO:0099047	(Fig. 1d)
PMID:27901072	PBO:0099056	(comment: asynchronous) fig 3a
PMID:27902423	FYPO:0001407	(comment: Promoter analysis)
PMID:27902423	FYPO:0002061	(comment: Promoter analysis)
PMID:27902423	FYPO:0002061	(comment: Promoter analysis)
PMID:27966061	FYPO:0005886	(comment: indicates Hsf1 activation)
PMID:27984744	FYPO:0006518	(Fig. 1A)
PMID:27984744	FYPO:0006518	(Fig. S2)
PMID:27984744	FYPO:0006518	(Fig. 1B)
PMID:27984744	FYPO:0006518	(Fig. 1A)
PMID:27984744	PBO:0101377	(Fig. 2A, 2B)
PMID:27984744	PBO:0101377	(Fig. 2E, 2F)
PMID:27984744	PBO:0101377	(Fig. 2E, 2F)
PMID:27984744	PBO:0101377	(Fig. 2E, 2F)
PMID:27984744	FYPO:0007629	(Fig. 1A)
PMID:27984744	FYPO:0006518	(Fig. 1B)
PMID:27984744	FYPO:0004276	(comment: ChIP-seq); Fig. 1C, 1D
PMID:27984744	FYPO:0007629	(Fig. 1B)
PMID:27984744	FYPO:0006518	(Fig. 1B)
PMID:27984744	FYPO:0006518	(Fig. 1A)
PMID:27984744	FYPO:0007629	(Fig. 1B)
PMID:27984744	FYPO:0006518	(Fig. 1A)
PMID:27984744	FYPO:0006518	(Fig. 1B)
PMID:27984744	FYPO:0007629	(Fig. 1A)
PMID:28011631	PBO:0105894	(Figure S2)
PMID:28011631	GO:0140043	(Fig. 1H, Fig. 3B)
PMID:28011631	GO:0140043	(Fig. 3B)
PMID:28011631	GO:0030476	(Fig. 4F) Assembly of Isp3-GFP onto the spore surface was defective in the dga1Δplh1Δ mutant.
PMID:28011631	GO:0019915	(Fig. 4B) The dga1Δplh1Δ mutant possessed few lipid droplets.
PMID:28011631	PBO:0105892	(Fig. 4A, 4C, and 4D) Using spore colony formation assay and microscopic observation, most of the dga1Δplh1Δ mutant spores failed to form colonies showed no sign of germination.
PMID:28011631	FYPO:0006003	(Fig. 3B) normal lipid droplet localization to FSM leading edge
PMID:28011631	FYPO:0006053	(Fig. 2C) (comment: also in lantrunculin treated sceels indicating actin dependeny)
PMID:28011631	FYPO:0000808	(Fig. 2C)
PMID:28011631	GO:0019915	(Fig. 4B) The dga1Δplh1Δ mutant possessed few lipid droplets.
PMID:28011631	FYPO:0006051	(Figure S3) LP clustering at nucleus
PMID:28011631	FYPO:0006053	(Fig. 3B) (comment: also in lantrunculin treated sceels indicating actin dependeny)
PMID:28011631	PBO:0105896	(Fig. 4A,C)
PMID:28011631	GO:0140042	(Fig. 4B)
PMID:28011631	GO:0140042	(Fig. 4B)
PMID:28011631	FYPO:0006054	(Fig. 3B) (comment: also in lantrunculin treated sceels indicating actin dependeny)
PMID:28011631	FYPO:0004993	(Fig. 4A)
PMID:28011631	FYPO:0006051	(Fig. 2C) (comment: also in lantrunculin treated sceels indicating actin dependeny)
PMID:28011631	PBO:0105895	(Fig. 2C) (comment: also in lantrunculin treated sceels indicating actin dependeny)
PMID:28011631	FYPO:0004925	(Fig. 4F) Isp3-GFP was improperly assembled in the dga1Δplh1Δ mutant.
PMID:28011631	PBO:0105893	(Figure S2)
PMID:28011631	GO:0140043	(Fig. 1F, Fig. 2C)
PMID:28017606	PBO:0097624	(Figures 1D and 1E) / ectopic. show a very striking result: co-expression of TetR-Spc7-9TE with TetR-D(1-302)Mph1 was sufficient to arrest cells in mitosis.
PMID:28017606	PBO:0097625	Spc7-wt arrested significantly faster than Spc7-9TE, with $60% mitotic arrest after 12 hr compared to 16 hr for Spc7-9TE.
PMID:28017606	PBO:0097627	Strains co-expressing Spc7 and Mph1 do not accumulate Mad2-GFP at spindle poles in strains containing the mad1-KAKA mutation that disrupts the Mad1-Cut7 kinesin motor interaction.
PMID:28017606	PBO:0097628	136 amino acids of Mad1 containing a coiled-coil region (CC) were removed, preventing Mad1-Mad2 interaction with Mlps and the nuclear envelope and also removing the Cut7 interaction site. These mad1-DCC cells were also able to arrest efficiently when TetR-Spc7-9TE and TetR-D(1-302)Mph1 were co-expressed (Figure 3E). We conclude that the Mad and Bub proteins do not need to be enriched at kinetochores, spindle poles, or the nuclear periphery for a robust checkpoint arrest to be generated in fission yeast. Most likely a diffuse, soluble pool of Spc7
PMID:28017606	FYPO:0007438	advance (by ∼4 hr) in the timing of arrest in bub3DΔ cells arresting due to Spc7-9TE cells (although there is no effect with Spc7-wt, see Figure S4C).
PMID:28017606	GO:0007094	This demonstrates that the ‘‘activated’’ Spc7-9TE binding platform is sufficient to recruit these three checkpoint proteins constitutively, and that this works ectopically and thus does not require additional kinetochore factors. and Figure 1C. thus, we believe that this Spc7-Bub-Mad3 complex likely acts as an independent signaling module
PMID:28031482	PBO:0094672	(Fig. 6C)
PMID:28031482	PBO:0094671	(Fig. 6C)
PMID:28031482	PBO:0094670	(Fig. 6C)
PMID:28031482	PBO:0094669	(Fig. 6C)
PMID:28031482	PBO:0094668	(Fig. 6C)
PMID:28031482	PBO:0094667	(Fig. 6C)
PMID:28031482	PBO:0094666	(Fig. 6C)
PMID:28031482	PBO:0094665	(Fig. 6C)
PMID:28031482	FYPO:0002061	(Figure 7A)
PMID:28031482	PBO:0094664	(Fig. 6D)
PMID:28031482	PBO:0094664	(Fig. 6D)
PMID:28031482	PBO:0094664	(Fig. 6D)
PMID:28031482	PBO:0094664	(Fig. 6D)
PMID:28031482	PBO:0094664	(Fig. 6D)
PMID:28031482	PBO:0094663	(Figure 6C)
PMID:28031482	PBO:0094663	(Figure 6C)
PMID:28031482	PBO:0094662	(Figure 6A)
PMID:28031482	PBO:0094661	(Fig. 5G, left panel)
PMID:28031482	FYPO:0000784	(Fig. 5G, left panel)
PMID:28031482	GO:0005737	(Fig. 5G, left panel)
PMID:28031482	PBO:0094660	(Fig. 5D)
PMID:28031482	PBO:0094659	(Fig. 5B)
PMID:28031482	PBO:0094658	(Fig. 5C)
PMID:28031482	PBO:0094657	(Fig. 5A)
PMID:28031482	PBO:0094656	(Fig. 4H, right panel)
PMID:28031482	PBO:0094655	(Fig. 4D)
PMID:28031482	FYPO:0001896	(Fig. 4B,4D)
PMID:28031482	FYPO:0001895	(Fig. 2B)
PMID:28031482	FYPO:0005993	(Figure 2D)
PMID:28031482	PBO:0094654	(Figure 2D)
PMID:28031482	PBO:0094653	(Figure 2B)
PMID:28031482	PBO:0094652	(Figure 1E)
PMID:28031482	PBO:0094651	(Figure 1D)
PMID:28031482	PBO:0094650	(Figure 1E)
PMID:28031482	PBO:0094649	(Figure 1E)
PMID:28031482	FYPO:0001234	(Fig. 6D)
PMID:28031482	FYPO:0001234	(Fig. 6D)
PMID:28031482	FYPO:0001234	(Fig. 6D)
PMID:28031482	PBO:0094648	(Fig. 6D)
PMID:28031482	PBO:0094648	(Fig. 6D)
PMID:28031482	GO:0000290	pdc2 is required for mRNA decapping. Fig. 2A 2B
PMID:28031482	GO:0000932	(Fig. 1D)
PMID:28103117	PBO:0111514	(Fig. 2a)
PMID:28103117	PBO:0111513	(Fig. 2a) For example, in the second cell cycle, Wee1 phosphorylation was initiated at the end of G2 (180 minutes) and reached a maximum level at metaphase (200 minutes), just before Cdc13 degradation in anaphase (220 minutes).
PMID:28103117	PBO:0099448	(Fig. 2a)
PMID:28103117	PBO:0099449	(Fig. 2a)
PMID:28103117	PBO:0101618	(Fig. 2a)
PMID:28103117	PBO:0099453	changes in phosphorylation level Figs. 5A, B and S2)
PMID:28103117	PBO:0099454	changes in phosphorylation level Figs. 5A, B and S2)
PMID:28103117	FYPO:0005955	The cell cycle was 20 min longer in clp1D cells compared with wild type cells.
PMID:28103117	PBO:0099454	changes in phosphrylation level fig4 Wee1 to remain in the partially phosphorylated form throughout the cell cycle (Fig. S2)
PMID:28103117	PBO:0099453	changes in phosphrylation level fig4 Wee1 to remain in the partially phosphorylated form throughout the cell cycle (Fig. S2)
PMID:28103117	PBO:0099452	(Fig. 3a) (comment: Cdk1 consensus sites)
PMID:28103117	PBO:0111515	(Fig. 2a)
PMID:28103117	PBO:0101618	(Fig. 2a)
PMID:28160081	FYPO:0006331	(Fig. 2B)
PMID:28160081	FYPO:0000245	(Fig. 5)
PMID:28160081	FYPO:0001309	(Fig. 4c)
PMID:28160081	FYPO:0006333	(Fig. 2B)
PMID:28160081	FYPO:0000245	(Fig. 2A)
PMID:28160081	FYPO:0000245	(Fig. 2A)
PMID:28160081	FYPO:0000245	(Fig. 2A)
PMID:28160081	FYPO:0000245	(Fig. 2A)
PMID:28160081	FYPO:0006331	(Fig. 2B)
PMID:28160081	FYPO:0006331	(Fig. 2B)
PMID:28160081	FYPO:0006331	(Fig. 2B)
PMID:28178520	FYPO:0006646	(Fig. 4A)
PMID:28178520	FYPO:0005684	(Fig. 4A)
PMID:28178520	FYPO:0005684	(Fig. 4D)
PMID:28178520	FYPO:0005684	(Fig. 4D)
PMID:28178520	FYPO:0006646	(Fig. 4D)
PMID:28178520	FYPO:0005684	(Fig. 5)
PMID:28178520	FYPO:0006646	(Fig. 5)
PMID:28178520	PBO:0107470	(Figure 2B)
PMID:28178520	PBO:0107471	(Figure S3C,D)
PMID:28178520	PBO:0107472	(Figure S4C)
PMID:28178520	PBO:0107473	(Figure S4C)
PMID:28178520	PBO:0107474	(Figure S4C)
PMID:28178520	FYPO:0006475	(Figures S2B)
PMID:28178520	PBO:0107464	(Figures S2B)
PMID:28178520	PBO:0097932	(Figures S2A)
PMID:28178520	PBO:0097932	(Figures S2A)
PMID:28178520	PBO:0097610	(Figures 1J)
PMID:28178520	PBO:0107463	(Figures 1J)
PMID:28178520	PBO:0107463	(Figures 1J)
PMID:28178520	PBO:0097610	(Figures 1J)
PMID:28178520	PBO:0107462	(Figures 1J)
PMID:28178520	PBO:0107461	(Figures 1J)
PMID:28178520	PBO:0107460	(Figures 1J)
PMID:28178520	PBO:0101201	(Figures 1J)
PMID:28178520	PBO:0095694	(Figures 1J)
PMID:28178520	PBO:0095694	(Figures 1J)
PMID:28178520	PBO:0107459	(Figure 1I)
PMID:28178520	PBO:0107458	(Figure 1I)
PMID:28178520	PBO:0107454	(Figures 1H)
PMID:28178520	PBO:0097607	(Figures 1H)
PMID:28178520	PBO:0107446	(Figure 1H)
PMID:28178520	PBO:0022963	(Fig. 1) (comment: requires Clp1 activity)
PMID:28178520	PBO:0022963	(Fig. 1) (comment: requires Klp9, Clp1 activity)
PMID:28178520	GO:0000022	(comment: requires motor activity)
PMID:28178520	FYPO:0005343	(Fig. 3)
PMID:28178520	PBO:0095694	(Figures 1G and 1I; Figure S1F)
PMID:28178520	PBO:0107457	(Figures 1G and 1I; Figure S1F)
PMID:28178520	PBO:0107456	(Figure 1E)
PMID:28178520	PBO:0107446	(Figure 1B and S1B,C)
PMID:28178520	PBO:0101952	(Figure 1B and S1B,C)
PMID:28178520	PBO:0107454	(Figure 1D)
PMID:28178520	PBO:0022963	(Fig. 1)
PMID:28178520	PBO:0107453	(Figure 1D)
PMID:28178520	PBO:0107455	(Figures S1D and S1E)
PMID:28178520	PBO:0018645	(Figure 1C)
PMID:28178520	PBO:0107454	(Figure 1B and S1B,C)
PMID:28178520	PBO:0107453	(Figure 1B and S1B,C)
PMID:28178520	PBO:0107452	(Figure 1B and S1B,C)
PMID:28178520	PBO:0107451	(Figure 1B and S1B,C)
PMID:28178520	PBO:0107450	(Figure 1B and S1B,C)
PMID:28178520	PBO:0107446	(Figure 1B and S1B,C)
PMID:28178520	PBO:0105361	(Figure 1B and S1B,C)
PMID:28178520	PBO:0107447	(Figure 1B and S1B,C)
PMID:28178520	PBO:0107448	(Figure 1B and S1B,C)
PMID:28178520	PBO:0107449	(Figure 1B and S1B,C)
PMID:28178520	FYPO:0006646	(Fig. 4A)
PMID:28178520	FYPO:0006646	(Fig. 4A)
PMID:28178520	PBO:0107479	(Figure 5B)
PMID:28178520	PBO:0107478	(Figure 5B)
PMID:28178520	FYPO:0006257	(Fig. 5)
PMID:28178520	FYPO:0005683	(Fig. 5)
PMID:28178520	PBO:0107477	(Figure 4E)
PMID:28178520	FYPO:0004833	(Fig. 4D)
PMID:28178520	PBO:0107476	(Figure 4E)
PMID:28178520	FYPO:0006257	(Fig. 4D)
PMID:28178520	FYPO:0005683	(Fig. 4D)
PMID:28178520	FYPO:0005683	(Fig. 4D)
PMID:28178520	FYPO:0005683	(Fig. 4A)
PMID:28178520	PBO:0107475	(Figure S4C)
PMID:28178520	FYPO:0005684	(Figure 4A)
PMID:28178520	FYPO:0005684	(Fig. 4A)
PMID:28178520	FYPO:0006257	(Fig. 4A)
PMID:28178520	FYPO:0006257	(Fig. 4A)
PMID:28178520	FYPO:0006257	(Fig. 4A)
PMID:28178520	FYPO:0005684	(Fig. 4A)
PMID:28178520	FYPO:0005684	(Fig. 4A)
PMID:28178520	PBO:0101954	(Figure 2A)
PMID:28178520	PBO:0107467	(Figure 2A; Figure S3A)
PMID:28178520	FYPO:0000324	(Figure 2A; Figure S3A)
PMID:28178520	PBO:0107468	(Figure S3B)
PMID:28178520	PBO:0095920	(Figure S3B)
PMID:28178520	PBO:0107469	(Figure 2B)
PMID:28191457	PBO:0107140	(comment: Phenotype is inherited in non-Mendelian manner, via protein aggregates (prion-like))
PMID:28191457	PBO:0107139	(comment: SDS-PAGE followed by western blotting and proteinase K treatment. Dot plots with extracts for pellet, soluble and total cell fractions with and without pre-treatment with 2% SDS. SDD-AGE gels of samples treated at room temperature and at 95°C, both with and without curing with GdnHCl.)
PMID:28193844	FYPO:0006890	(Fig. 9)
PMID:28193844	MOD:00171	(comment: they show it is GPI anchored, the specified residue is predicted)
PMID:28193844	GO:0000329	(Fig. 4)
PMID:28193844	PBO:0094472	(Fig. 8b)
PMID:28193844	GO:0015886	(Fig. 6)
PMID:28193844	GO:0000324	(Fig. 4)
PMID:28193844	GO:0140357	(Fig. 6a)
PMID:28202541	PBO:0106195	(comment: Ost1-mCherry, mCherry antibody)
PMID:28202541	PBO:0106191	(comment: Scp1-13xMyc used for Scp1, pulled on Myc)
PMID:28202541	FYPO:0002448	(comment: pulled on Dsc2)
PMID:28202541	PBO:0106196	improved relative to WT Sre1
PMID:28202541	PBO:0106193	Ost1-mCherry increased signal in ER
PMID:28202541	PBO:0106192	Anp1-GFP mislocalized from Golgi puncta to ER and vacuole
PMID:28202541	PBO:0106194	Anp1-GFP degradation as assayed by appearance of free GFP
PMID:28218250	PBO:0096565	(comment: ChIP-seq)
PMID:28218250	FYPO:0005952	(comment: ChIP-seq)
PMID:28218250	PBO:0096565	(comment: ChIP-seq)
PMID:28218250	PBO:0096563	(comment: ChIP-seq)
PMID:28218250	FYPO:0005951	(comment: ChIP-seq)
PMID:28218250	FYPO:0005950	(comment: ChIP-seq)
PMID:28218250	PBO:0096564	(comment: ChIP-seq; same severity as spt16-1 alone)
PMID:28218250	FYPO:0005950	(comment: ChIP-seq)
PMID:28218250	PBO:0096564	(comment: ChIP-seq)
PMID:28218250	PBO:0096562	(comment: ChIP-seq)
PMID:28218250	PBO:0096562	(comment: ChIP-seq)
PMID:28218250	PBO:0096562	(comment: ChIP-seq)
PMID:28218250	PBO:0096563	(comment: ChIP-seq)
PMID:28218250	PBO:0096562	(comment: ChIP-seq)
PMID:28218250	PBO:0096562	(comment: ChIP-seq)
PMID:28218250	FYPO:0005950	(comment: ChIP-seq)
PMID:28218250	PBO:0096563	(comment: ChIP-seq)
PMID:28218250	PBO:0096562	(comment: ChIP-seq)
PMID:28242692	PBO:0097304	(comment: partial leaking) Fig. 3B, arrow; Fig. 3 C and D, quantification
PMID:28242692	PBO:0097302	(Fig. 1C)
PMID:28242692	FYPO:0003973	and the NPCs that were present were localized to regions that were largely free of karmellae and tubulo-vesicular structures (Fig. 4D).
PMID:28242692	PBO:0097305	cells with abnormal NE morphology at the beginning of the experiment, by contrast, lost nuclear GFP completely over the time course (Fig. S3B). Thus, cytoplasmic GFP resulted from loss of nuclear integrity rather than from defects in nuclear import.
PMID:28242692	FYPO:0006018	(Fig. 4B) asterisk
PMID:28242692	PBO:0097302	(Fig. 1C)
PMID:28242692	PBO:0097303	(Fig. S1C)
PMID:28242692	FYPO:0002085	(Fig. 1B, supp table S1)
PMID:28242692	FYPO:0002085	(Fig. 1B, supp table S1)
PMID:28242692	PBO:0097302	(Fig. 1C)
PMID:28242692	FYPO:0000772	(comment: severe leaking) Fig. 3B, arrow; Fig. 3 C and D, quantification, Figure 4 B
PMID:28242692	PBO:0097300	(Fig. 1D-F)
PMID:28242692	PBO:0097304	(comment: partial leaking) Fig. 3B, arrow; Fig. 3 C and D, quantification
PMID:28242692	PBO:0097304	(comment: partial leaking) Fig. 3B, arrow; Fig. 3 C and D, quantification
PMID:28242692	FYPO:0006019	4B, arrowheads, and Fig. 5B
PMID:28242692	FYPO:0003751	Remarkably, double-mutant cells displayed WT-like nuclei, although a few examples of probable nuclear fenestrations were observed in lem2Δ single-mutant cells (Fig. 5G).
PMID:28242692	FYPO:0001420	(Fig. 1C)
PMID:28242692	PBO:0097303	(Fig. S1C)
PMID:28242692	FYPO:0003751	Remarkably, double-mutant cells displayed WT-like nuclei, although a few examples of probable nuclear fenestrations were observed in lem2Δ single-mutant cells (Fig. 5G).
PMID:28242692	FYPO:0001513	(comment: CHECK rescue)
PMID:28242692	PBO:0097024	(Fig. S1A,B)
PMID:28242692	PBO:0097301	(Fig. 1A)
PMID:28242692	FYPO:0001733	(Fig. 2B)
PMID:28264193	PBO:0100360	(comment: CHECK Supp)
PMID:28264193	PBO:0114477	(Fig. 5) (comment: CHECK fusion mutant not currently capturable)
PMID:28264193	PBO:0100361	(Fig. S2)
PMID:28264193	PBO:0100361	(Fig. S2)
PMID:28264193	PBO:0100361	(Fig. S2)
PMID:28264193	PBO:0100361	(Fig. S2)
PMID:28264193	PBO:0100361	(Fig. S2)
PMID:2827111	GO:0003917	(Fig. 7B)
PMID:2827111	FYPO:0002061	(Table 1)
PMID:2827111	FYPO:0001234	(Table 1)
PMID:2827111	FYPO:0002061	Table1
PMID:2827111	FYPO:0002061	Table1
PMID:28281664	PBO:0103667	(Figure 2)
PMID:28281664	PBO:0103667	(Figure 1a)
PMID:28281664	PBO:0093606	(Figure 1B)
PMID:28281664	PBO:0103667	(Figure 2)
PMID:28281664	PBO:0103668	(Figure 2)
PMID:28281664	PBO:0103669	(Figure 1d)
PMID:28281664	PBO:0103670	(Figure 1c, 1d)
PMID:28281664	FYPO:0001122	(Figure 1b) divides longer than WT in the same conditions
PMID:28281664	PBO:0103678	(Figure 3)
PMID:28281664	FYPO:0001122	(Figure 3)
PMID:28281664	PBO:0093578	(Figure 3)
PMID:28281664	PBO:0095677	(Figure 3)
PMID:28281664	PBO:0103676	(Figure 2)
PMID:28281664	PBO:0103675	(Figure 2)
PMID:28281664	PBO:0093606	(Figure 2)
PMID:28281664	PBO:0103675	(Figure 2)
PMID:28281664	PBO:0095677	(Figure 1D)
PMID:28281664	PBO:0103674	(Figure 1)
PMID:28281664	PBO:0103672	(Figure 3)
PMID:28281664	PBO:0097116	(Figure 3)
PMID:28281664	PBO:0096662	(Figure 3)
PMID:28281664	PBO:0093605	(Figure 3)
PMID:28281664	PBO:0103671	(Figure 2)
PMID:28281664	PBO:0103667	(Figure 2)
PMID:28281664	PBO:0100665	(Figure 1D)
PMID:28282432	PBO:0114464	(Fig. 4)
PMID:28282432	FYPO:0008288	(Fig. 5)
PMID:28282432	FYPO:0004695	(Fig. 5)
PMID:28282432	PBO:0114465	(Fig. 4)
PMID:28282432	FYPO:0004695	(Fig. 5)
PMID:28282432	FYPO:0005663	(Fig. 2)
PMID:28282432	FYPO:0006974	(Fig. 4)
PMID:28282432	FYPO:0006974	(Fig. 4)
PMID:28282432	FYPO:0006974	(Fig. 4)
PMID:28282432	FYPO:0008288	(Fig. 5)
PMID:28282432	PBO:0114465	(Fig. 4)
PMID:28282432	PBO:0098222	(Fig. 4)
PMID:28282432	FYPO:0005663	(Fig. 2)
PMID:28292899	FYPO:0003835	(Fig. 5B)
PMID:28292899	FYPO:0002674	(Fig. 5B,A) (comment: ALSO FOR THE myo-1TH3 domain deletion - need genotype description)
PMID:28292899	PBO:0100312	(Fig. 6)
PMID:28292899	FYPO:0003835	(Fig. 5B)
PMID:28292899	PBO:0100311	(Fig. 5B)
PMID:28292899	PBO:0100311	(Fig. 4 D-F)
PMID:28292899	FYPO:0000927	(Fig. 7)
PMID:28292899	GO:0005546	(Fig. 2, 3C)
PMID:28292899	PBO:0100310	(Fig. 1A) Inset and Movie S1/ number of Mcp5 molecules per cluster 10 ± 2 ( Fig. 1D)
PMID:28292899	FYPO:0000927	(Fig. 7)
PMID:28334955	PBO:0096229	(Fig. 1B)
PMID:28334955	PBO:0093796	(Fig. 1C)
PMID:28334955	PBO:0093793	(Fig. 1C)
PMID:28334955	PBO:0096247	(Figure Supp S8)
PMID:28334955	PBO:0096248	(Figure 9d)
PMID:28334955	PBO:0096237	(Figure 9F)
PMID:28334955	PBO:0096238	(Figure 9F)
PMID:28334955	PBO:0096239	(Figure 9F)
PMID:28334955	PBO:0096240	(Figure 9F)
PMID:28334955	PBO:0096226	(Fig. 7A)
PMID:28334955	PBO:0096227	(Fig. 7B)
PMID:28334955	PBO:0096229	(Fig. 1B)
PMID:28334955	PBO:0096235	(Figure 2B,8B,8C)
PMID:28334955	PBO:0096234	(Figure 2B)
PMID:28334955	PBO:0096244	(Figure 8A)
PMID:28334955	PBO:0096233	(Figure 2B)
PMID:28334955	PBO:0096232	(Figure 2B) (comment: barely detectable level )
PMID:28334955	PBO:0096240	(Figure 9F)
PMID:28334955	PBO:0096239	(Figure 9F)
PMID:28334955	PBO:0096238	(Figure 9F)
PMID:28334955	PBO:0096237	(Figure 9F)
PMID:28334955	GO:0035694	(comment: Based on what we know about lon in other species, i think the rescue of mpa1 phenotype is enough to predict a catabolic role)
PMID:28334955	PBO:0096231	Supp. S3
PMID:28334955	FYPO:0002380	Supp. S3
PMID:28334955	FYPO:0002106	Supp. S3
PMID:28334955	FYPO:0003335	Supplementary Figure S3B ((comment: abolished by galactose addition)
PMID:28334955	PBO:0093796	(Fig. 7A)
PMID:28334955	FYPO:0002582	(Figure 2C)
PMID:28334955	GO:0005759	(Figure 6c)
PMID:28334955	GO:0005739	(Figure 6a)
PMID:28334955	GO:0005759	(Figure 6c)
PMID:28334955	GO:0005739	(Figure 6a)
PMID:28334955	PBO:0096232	(Figure 8B,8C) (comment: barely detectable level )
PMID:28334955	PBO:0096233	(Figure 8B,8C)
PMID:28334955	PBO:0096234	(Figure 8B,8C)
PMID:28334955	FYPO:0004153	Supplementary Figure S3B
PMID:28334955	PBO:0096236	(Figure 8D)
PMID:28334955	PBO:0096237	(Figure 8D)
PMID:28334955	PBO:0096238	(Figure 8D)
PMID:28334955	PBO:0096239	(Figure 8D)
PMID:28334955	PBO:0096240	(Figure 8D)
PMID:28334955	PBO:0096241	(Figure 8D)
PMID:28334955	PBO:0096245	(Figure 9A)
PMID:28334955	PBO:0093605	(Fig. 1 E,F)
PMID:28334955	PBO:0096246	(Fig. 9C)
PMID:28334955	FYPO:0004153	Supplementary Figure S7
PMID:28334955	PBO:0093605	(Fig. 7c)
PMID:28334955	PBO:0093793	(Fig. 1A)
PMID:28334955	PBO:0093796	(Fig. 1A)
PMID:28334955	PBO:0096226	(Fig. 1A)
PMID:28334955	PBO:0096227	(Fig. 1B)
PMID:28334955	PBO:0096227	(Fig. 1B)
PMID:28334955	PBO:0096228	(Fig. 1B)
PMID:28343969	PBO:0098610	(Fig. 2B)
PMID:28343969	PBO:0114894	Here we identify a conserved Hrk1-interacting motif (HIM) in Pds5 and a Pds5-interacting motif (PIM) in Hrk1 in fission yeast. Mutations in either motif result in the displacement of Hrk1 from centromeres. We also show that the mechanism of Pds5-dependent Hrk1 recruitment is conserved in human cells | (Figure 1 E) Thus, although Eso1, Wpl1, and Hrk1 all bind to the same surface of Pds5, we assume that they do not always compete for binding because of the excess amounts of Pds5 in the cells. Thus, HIM in Pds5 and PIM in Hrk1 are required solely for centromeric Hrk1 localization and its function, at least in the context of targeting the CPC to centromeres.
PMID:28343969	GO:0051456	(comment: CHECK specifically, biorientation)
PMID:28343969	GO:0051456	(comment: CHECK specifically, biorientation)
PMID:28343969	PBO:0098619	(Fig. S4A)
PMID:28343969	PBO:0098619	(Fig. S4A)
PMID:28343969	GO:0140463	(Figures S4D and S4E)
PMID:28343969	PBO:0114951	(Figures S4D and S4E)
PMID:28343969	PBO:0098619	(Fig. S4A)
PMID:28343969	FYPO:0002060	(Fig. S4A)
PMID:28343969	FYPO:0002061	(Fig. S4A)
PMID:28343969	PBO:0095072	(Fig. 4G)
PMID:28343969	PBO:0095072	(Fig. 4G)
PMID:28343969	PBO:0093564	(Fig. 4f)
PMID:28343969	PBO:0093562	(Fig. 4f)
PMID:28343969	PBO:0093557	(Fig. 4f)
PMID:28343969	PBO:0093558	(Fig. 4f)
PMID:28343969	PBO:0098618	(Fig. 4E)
PMID:28343969	PBO:0098618	(Fig. 4E)
PMID:28343969	FYPO:0002061	(Fig. 4C)
PMID:28343969	FYPO:0002061	(Fig. 4C)
PMID:28343969	PBO:0098617	(Fig. 4b)
PMID:28343969	PBO:0098617	(Fig. 4b)
PMID:28343969	FYPO:0006521	(Fig. S4A)
PMID:28343969	FYPO:0006521	(Fig. S4A)
PMID:28343969	PBO:0098616	(Fig. S4B)
PMID:28343969	PBO:0098615	(Fig. 2F)
PMID:28343969	PBO:0098614	(Fig. 2E)
PMID:28343969	PBO:0098614	(Fig. 2E)
PMID:28343969	PBO:0098613	(Fig. 2F)
PMID:28343969	PBO:0098613	(Fig. 2F)
PMID:28343969	PBO:0098612	"(Fig. 2C) (comment: this represents Yoshi's suggestion"" An Ark1 reduction can become a reason of merotelic attachment, which is also caused by a defect in kinetochore structures.)"" (comment: CHECK has_penetrance high , assayed_using ark1)"
PMID:28343969	PBO:0098612	"(Fig. 2C) (comment: vw: this represents Yoshi's suggestion"" An Ark1 reduction can become a reason of merotelic attachment, which is also caused by a defect in kinetochore structures.)"""
PMID:28343969	PBO:0098611	(Fig. 2A,B)
PMID:28343969	PBO:0098611	(Fig. 2A,B)
PMID:28343969	PBO:0098610	(Fig. 2B)
PMID:28343969	PBO:0098609	(Fig. 2A,B)
PMID:28343969	PBO:0098609	(Fig. 2A,B)
PMID:28343969	PBO:0098606	(Fig. 1B)
PMID:28343969	PBO:0098605	(Fig. S2A, S2C)
PMID:28343969	PBO:0098604	(Fig. 4F, 4H)
PMID:28343969	PBO:0098604	(Fig. 4H)
PMID:28343969	PBO:0098603	(Fig. 2C, 2D, 2G)
PMID:28343969	PBO:0098602	(Fig. 2C, 2D, 2G)
PMID:28345447	FYPO:0002865	(comment: CHECK restored by depletion of ammonium)
PMID:28345447	FYPO:0002865	(comment: CHECK restored by depletion of ammonium)
PMID:28345447	FYPO:0002865	(comment: CHECK restored by depletion of ammonium)
PMID:28345447	FYPO:0002865	(comment: CHECK restored by depletion of ammonium)
PMID:28345447	FYPO:0002865	(comment: CHECK restored by depletion of ammonium)
PMID:28366743	PBO:0095476	(Fig. 1B)
PMID:28366743	PBO:0096928	(comment: synchronous mitotic cells) fig 1c
PMID:28366743	PBO:0095476	(Fig. S1G)
PMID:28366743	PBO:0096924	(Fig. 3B)
PMID:28366743	PBO:0096925	(Fig. 3B)
PMID:28366743	PBO:0096921	(Fig. 4D)
PMID:28366743	PBO:0096926	(Fig. 4C)
PMID:28366743	PBO:0096922	(Figure 3A)
PMID:28366743	PBO:0096923	(Figure 3A)
PMID:28366743	PBO:0096926	(Figure 4C) (comment: synchronous mitotic cells)
PMID:28366743	FYPO:0004318	(Fig. S1h)
PMID:28366743	FYPO:0004318	(Figure 1F
PMID:28366743	PBO:0095475	(Figures 1F, S1H)
PMID:28366743	PBO:0096921	(Figure 4D)
PMID:28366743	PBO:0095475	(Fig. 4A)
PMID:28366743	PBO:0096926	(Fig. 4C)
PMID:28366743	PBO:0096920	(Figure 4D)
PMID:28366743	FYPO:0004318	(Fig. 1B)
PMID:28366743	PBO:0096921	(Figure 4D)
PMID:28366743	PBO:0096930	(Figure S1e)
PMID:28366743	PBO:0096933	(Figure S3B)
PMID:28366743	PBO:0096934	(Figure S3B)
PMID:28366743	PBO:0096927	(Fig. 4C)
PMID:28366743	PBO:0096931	(Fig. S3B)
PMID:28366743	PBO:0096932	(Figure S3B)
PMID:28366743	PBO:0096932	(Figure S3B)
PMID:28366743	PBO:0096922	(Fig. 3a)
PMID:28366743	PBO:0096923	(Fig. 3a)
PMID:28366743	PBO:0096924	(Fig. 3A, B) (comment: CHECK: present in interphase cells)
PMID:28366743	PBO:0096925	(Fig. 3A, B) (comment: CHECK: present in interphase cells)
PMID:28366743	PBO:0096935	(Figure S3B)
PMID:28366743	PBO:0096929	(Fig. 1C) (comment: synchronous mitotic cells)
PMID:28366743	PBO:0096933	(Figure S3B)
PMID:28366743	PBO:0095476	(Fig. 2C, D, S2B)
PMID:28366743	FYPO:0004367	(Fig. 4A)
PMID:28366743	FYPO:0003762	(Fig. 2C, D, S2B)
PMID:28366743	PBO:0095474	(Fig. 1B)
PMID:28366743	PBO:0095474	(Fig. 1B)
PMID:28366743	PBO:0095474	(Fig. 1B)
PMID:28366743	PBO:0095475	(Fig. 1b)
PMID:28366744	PBO:0105660	(Fig. 2a)
PMID:28366744	GO:0031145	Deletion increases levels of mitotic checkpoint complex associated with the anaphase promoting complex in mitosis.
PMID:28366744	GO:0031145	Required for mitotic checkpoint complex binding to the anaphase promoting complex.
PMID:28366744	FYPO:0004318	(comment: vw I changed the genotype/) Fig 1A (comment: checkpoint assay)
PMID:28366744	FYPO:0005727	(comment: vw; I changed the genotype here)
PMID:28366744	PBO:0105657	"(comment: vw changed term from ""reduced ubiquitin ligase activity"")"
PMID:28366744	FYPO:0004318	(Fig. 1A) (comment: checkpoint assay)
PMID:28366744	FYPO:0004318	(Fig. 1A) (comment: checkpoint assay)
PMID:28366744	FYPO:0004318	(Fig. 1A) (comment: checkpoint assay)
PMID:28366744	FYPO:0004318	(Fig. 1A) (comment: checkpoint assay)
PMID:28366744	FYPO:0005783	(Fig. 1c)
PMID:28366744	FYPO:0004318	(Fig. 1A) (comment: checkpoint assay)
PMID:28366744	PBO:0105663	(Figure 3A).
PMID:28366744	FYPO:0005783	(Fig. 1c)
PMID:28366744	PBO:0105658	(Fig. S1)
PMID:28366744	PBO:0105659	(Fig. 2a)
PMID:28366744	FYPO:0007173	(Fig. 1c)
PMID:28366744	PBO:0095469	(Fig. 2a)
PMID:28366744	PBO:0095469	(Fig. 2a)
PMID:28366744	PBO:0095924	(Figure 2b)
PMID:28366744	PBO:0105661	(Figures 3A, 3B)
PMID:28366744	PBO:0105662	(Figure 3B).
PMID:28366744	PBO:0105663	(Figure 3A).
PMID:28366744	PBO:0105664	(Figure 3A)
PMID:28366744	PBO:0105665	(Figure 3B).
PMID:28367989	PBO:0111620	(comment: S2P form)
PMID:28377506	FYPO:0000963	"(Fig. 7) ""unlike the hem13-1 mutant, the hem12 and hem14 null mutants of the heme biosynthesis pathway are insensitive to HU"""
PMID:28377506	FYPO:0001934	(Fig. 4)
PMID:28377506	FYPO:0001934	(Fig. 4)
PMID:28377506	FYPO:0000726	(Fig. 4D)
PMID:28377506	FYPO:0000963	"(Fig. 7) ""unlike the hem13-1 mutant, the hem12 and hem14 null mutants of the heme biosynthesis pathway are insensitive to HU"""
PMID:2837764	GO:0005786	(comment: assayed using mammalian proteins)
PMID:28388826	FYPO:0006566	data not shown
PMID:28388826	FYPO:0006566	data not shown
PMID:28404620	PBO:0097041	(comment: also uses Pol ii-RNA immunoprecipitation)
PMID:28404620	FYPO:0006109	(comment: sequencing of Ago1-bound siRNA)
PMID:28404620	FYPO:0006109	(comment: sequencing of Ago1-bound siRNA)
PMID:28404620	PBO:0097042	(comment: uses Pol ii-RNA immunoprecipitation)
PMID:28404620	FYPO:0006109	(comment: sequencing of Ago1-bound siRNA)
PMID:28404620	FYPO:0006110	(comment: sequencing of Ago1-bound siRNA)
PMID:28404620	FYPO:0006109	(comment: sequencing of Ago1-bound siRNA)
PMID:28404620	PBO:0111231	(comment: uses histone H3 RNA immunoprecipitation)
PMID:28404620	FYPO:0006109	(comment: sequencing of Ago1-bound siRNA)
PMID:28404620	PBO:0097039	(comment: also uses Pol ii-RNA immunoprecipitation)
PMID:28404620	FYPO:0002827	(comment: uses Pol ii-RNA immunoprecipitation)
PMID:28404620	FYPO:0006109	(comment: sequencing of Ago1-bound siRNA)
PMID:28410370	PBO:0102726	(comment: stronger phenotype when crossed to fus1∆)
PMID:28410370	PBO:0102726	(comment: phenotype more severe when crossed to fus1∆)
PMID:28410370	FYPO:0004806	(comment: Strong phenotype in crosses with fus1∆)
PMID:28410370	PBO:0102727	(comment: more severe phenotype when crossed to fus1delta)
PMID:28410370	PBO:0105710	(comment: wider localization)
PMID:28410370	PBO:0105712	(comment: wider localization)
PMID:28410370	PBO:0105713	(comment: wider localization)
PMID:28410370	PBO:0105710	(comment: wider localization)
PMID:28410370	PBO:0105710	(comment: wider localization)
PMID:28410370	PBO:0105712	wider localization at the shmoo tip
PMID:28410370	PBO:0102726	(comment: more severe phenotype when crossed to fus1∆)
PMID:28410370	FYPO:0006108	(comment: wider distribution along shmoo tip)
PMID:28410370	PBO:0105710	(comment: Wider localization at shmoo tip)
PMID:28432181	PBO:0100750	(comment: snRNA/ complementation of yeast pus1)
PMID:28438891	FYPO:0002061	(Figure 5 B) (comment: exacerbates )
PMID:28438891	GO:0000785	(Fig. EV5)
PMID:28438891	MOD:00046	(Fig. 3C)
PMID:28438891	GO:0045875	(comment: MIOTOTIC)
PMID:28438891	GO:0045875	(comment: type 2 cohesion (still bound) MITOTIC)
PMID:28438891	GO:0005515	(Fig. 7)
PMID:28438891	FYPO:0001357	(Fig. 4)
PMID:28438891	PBO:0099135	(Fig. 3C)
PMID:28438891	PBO:0095073	(Fig. 3C)
PMID:28438891	PBO:0095073	(Fig. 3C)
PMID:28438891	PBO:0099134	(Fig. 3C)
PMID:28438891	PBO:0096226	(Fig. 1C)
PMID:28438891	PBO:0096226	(Fig. 1C)
PMID:28438891	PBO:0096226	(Fig. 1C)
PMID:28438891	FYPO:0001357	(Fig. 1D)
PMID:28438891	FYPO:0001357	(Fig. 1D)
PMID:28438891	FYPO:0001357	(Fig. 1C)
PMID:28438891	FYPO:0001357	(Fig. 1C)
PMID:28438891	PBO:0096226	(Fig. 1C)
PMID:28438891	PBO:0096226	(Fig. 1C)
PMID:28438891	PBO:0096226	(Fig. 1C)
PMID:28438891	FYPO:0002061	(Fig. 1C)
PMID:28438891	FYPO:0002061	(Fig. 1C)
PMID:28438891	FYPO:0001357	(Fig. 1C)
PMID:28438891	FYPO:0002061	(Fig. 1C)
PMID:28438891	PBO:0099133	(comment: type 2 cohesion (still bound))
PMID:28438891	PBO:0099132	(comment: required for Rad21 dephosphorylation)
PMID:28438891	FYPO:0002060	(Fig. 5A)
PMID:28438891	FYPO:0002060	(Fig. 4E)
PMID:28467824	FYPO:0000826	Mutations that are predicted to impair middle module sta- bility also lead to a general decrease in RNA synthesis (Extended Data Fig. 4d), showing that the middle module is globally required for transcription. (comment: used txn rather than RNA level because we know it is transcription)
PMID:28467824	FYPO:0000826	Mutations that are predicted to impair middle module sta- bility also lead to a general decrease in RNA synthesis (Extended Data Fig. 4d), showing that the middle module is globally required for transcription. (comment: used txn rather than RNA level because we know it is transcription)
PMID:28469148	PBO:0102481	(comment: CHECK ura1 met5)
PMID:28469148	PBO:0102473	(comment: CHECK ade6 arg1)
PMID:28469148	PBO:0102481	(comment: CHECK ura1 met5)
PMID:28469148	PBO:0102480	(comment: CHECK lys3 ura1)
PMID:28469148	PBO:0102479	(comment: CHECK lys3 ura1)
PMID:28469148	PBO:0102480	(comment: CHECK lys3 ura1)
PMID:28469148	PBO:0102480	(comment: CHECK lys3 ura1)
PMID:28469148	PBO:0102481	(comment: CHECK ura1 met5)
PMID:28469148	PBO:0102480	(comment: CHECK lys3 ura1)
PMID:28469148	PBO:0102481	(comment: CHECK ura1 met5)
PMID:28469148	PBO:0102480	(comment: CHECK lys3 ura1)
PMID:28469148	PBO:0102481	(comment: CHECK ura1 met5)
PMID:28475874	FYPO:0003589	(comment: in response to a single blocked replisome)
PMID:28475874	FYPO:0003589	(comment: in response to a single blocked replisome)
PMID:28475874	FYPO:0004251	(comment: in response to a single blocked replisome)
PMID:28475874	FYPO:0005236	(comment: in response to a single blocked replisome)
PMID:28475874	FYPO:0003589	(comment: in response to a single blocked replisome)
PMID:28475874	FYPO:0006086	(comment: in response to a single blocked replisome)
PMID:28475874	GO:0031297	In the absence of Rad51, newly replicated strands are extensively resected at dysfunctional replication forks thus generating mitotic sister chromatid bridging
PMID:28475874	GO:0031297	In the absence of Rad52, newly replicated strands are extensively resected at dysfunctional replication forks thus generating mitotic sister chromatid bridging.
PMID:28476936	FYPO:0007786	(Fig. 2)
PMID:28476936	FYPO:0007786	(Fig. 2)
PMID:28476936	FYPO:0007786	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	(Fig. 2)
PMID:28476936	FYPO:0007786	(Fig. 2)
PMID:28476936	FYPO:0007786	(Fig. 2)
PMID:28476936	PBO:0098321	(Fig. S1A, 1)
PMID:28476936	FYPO:0007785	(Fig. S1A,1B,1C)
PMID:28476936	FYPO:0007786	(Fig. 2, 3, 4B)
PMID:28476936	FYPO:0007786	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	(Fig. 5) (comment: supplements added)
PMID:28476936	PBO:0098323	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	(Fig. S5) in this situation gad8 overexpression is unable to promote growth i. This show that Sck2 is the main S6 kinase effector of promoting growth in this situation
PMID:28476936	FYPO:0007786	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	(Fig. S5) in this situation psk1 only causes a small increase in cell length increase compared to Sck2 . This show that Sck2 is the main S6 kinase effector of promoting growth in this situation
PMID:28476936	FYPO:0007786	(Fig. S5) in this situation Sck1 only causes a small increase in cell length increase compared to Sck2 . This show that Sck2 is the main S6 kinase effector of promoting growth in this situation
PMID:28476936	FYPO:0001235	(Fig. S4A) cell growth at G2/M1 arrest is dependent on transcription. (comment: no supplements added)
PMID:28476936	PBO:0098322	(Fig. 4D) (comment: no supplements added)
PMID:28476936	FYPO:0007787	(Fig. 4A, C, E, F) (comment: no supplements added)
PMID:28476936	FYPO:0007786	(Fig. 2)
PMID:28476936	FYPO:0007786	(Fig. 2)
PMID:28479325	FYPO:0001124	(comment: CHECK normal cell size homeostasis)
PMID:28479325	PBO:0092427	During G2, the concentration of Cdc25 increases about 2 fold (Figure 1A)
PMID:28479325	PBO:0097937	relatively constant concentration during G2, as previously observed
PMID:28479325	GO:0031569	We propose that the size-dependent expression of the cdc25 transcript is the mechanism that allows cells to divide at a particular size, but it is not the mechanism which regulates what that size is.
PMID:28479325	FYPO:0001317	We find that the size dependent expression of Cdc25 does not require the 5′ UTR of its transcript, showing that this mechanism of translational regulation is not necessary for size dependent expression (Figure S3A).
PMID:28481910	PBO:0093559	(comment: same as cdc20-M10 alone)
PMID:28497540	PBO:0112493	(Fig. 1E)
PMID:28497540	GO:1990813	(Fig. 1E,F)
PMID:28497540	PBO:0109676	(Fig. 1B)
PMID:28497540	PBO:0112495	(Fig. 1F)
PMID:28497540	GO:1990813	(Fig. 1B)
PMID:28497540	PBO:0095117	(Fig. S5)
PMID:28497540	PBO:0095115	(Fig. 4A)
PMID:28497540	PBO:0095101	(Fig. 4A)
PMID:28497540	PBO:0095114	(comment: check during interphase)
PMID:28497540	PBO:0095113	(Fig. 3C)
PMID:28497540	PBO:0095113	(Fig. 3C)
PMID:28497540	FYPO:0003606	(Fig. S4)
PMID:28497540	FYPO:0003606	(Fig. 2B)
PMID:28497540	PBO:0095112	(Fig. S4)
PMID:28497540	PBO:0095111	(Fig. 2B)
PMID:28497540	PBO:0095110	(Fig. 2B)
PMID:28497540	PBO:0112495	(Fig. 5)
PMID:28497540	PBO:0095118	(Fig. 5C)
PMID:28497540	PBO:0095110	(Fig. S5)
PMID:28497540	PBO:0095111	(Fig. S2A)
PMID:28497540	PBO:0109340	(Fig. E)
PMID:28497540	PBO:0112491	(Fig. 5C)
PMID:28497540	PBO:0109340	(Fig. 3A,B)
PMID:28497540	PBO:0095100	(Fig. 2b)
PMID:28497540	PBO:0095101	(Fig. 2b)
PMID:28497540	PBO:0109670	(Fig. 1B)
PMID:28497540	PBO:0112490	(Fig. 1B, 1D)
PMID:28497540	FYPO:0006423	(Fig. 1B)
PMID:28497540	PBO:0112491	(Fig. 1C)
PMID:28497540	PBO:0112491	(Fig. 5)
PMID:28497540	PBO:0095120	4B
PMID:28497540	PBO:0112490	(Fig. 5)
PMID:28497540	PBO:0095119	(Fig. 5C)
PMID:28497540	FYPO:0006424	(Fig. 1C)
PMID:28497540	PBO:0112492	(Fig. 1D)
PMID:28497540	PBO:0112494	(Fig. 1F)
PMID:28513584	FYPO:0002085	(Fig. S4)
PMID:28513584	FYPO:0000049	(Fig. S3E)
PMID:28513584	FYPO:0001053	(Fig. 2) (comment: main text)
PMID:28513584	FYPO:0004395	(Fig. 2)
PMID:28513584	FYPO:0005342	(Fig. 2)
PMID:28513584	FYPO:0000049	(comment: Main text (Figure S2 seems wrongly labelled))
PMID:28513584	PBO:0103048	(Fig. S3D) and the fact that is required for bipolar spindle formation
PMID:28513584	GO:0061804	(comment: CHECK cut7D pkl1D ase1D lethal)
PMID:28513584	GO:0061804	(comment: CHECK cut7D pkl1D cls1off lethal)
PMID:28513584	GO:0061805	(comment: CHECK cut7D pkl1D klp9off does not elongate during anaphase B, cut7D pkl1D klp9D lethal, deleting all other kinesins except klp9 did not affect elongation after removing cut7)
PMID:28513584	PBO:0097932	(Fig. 1)
PMID:28513584	FYPO:0005343	(Fig. S4)
PMID:28513584	PBO:0103047	(Fig. 3)
PMID:28513584	PBO:0103046	(Fig. 3)
PMID:28513584	PBO:0103045	(Fig. 3)
PMID:28513584	PBO:0103044	(Fig. 3)
PMID:28513584	FYPO:0000049	(Fig. 3)
PMID:28513584	FYPO:0000049	(Fig. 2)
PMID:28513584	FYPO:0006174	(Fig. 2)
PMID:28513584	FYPO:0000324	(Fig. 2)
PMID:28513584	FYPO:0004395	(Fig. 2)
PMID:28513584	FYPO:0000276	(Fig. S1)
PMID:28513584	FYPO:0004085	(Fig. 1)
PMID:28513584	FYPO:0001574	(Fig. S1) (comment: Not really abnormal, should be just bipolar)
PMID:28515144	PBO:0096810	Increased duration of ssp2-T189 phosphorylation under osmotic stress
PMID:28515144	PBO:0096810	Increased duration of ssp2-T189 phosphorylation under osmotic stress
PMID:28515144	PBO:0096810	Increased duration of ssp2-T189 phosphorylation under osmotic stress
PMID:28515144	PBO:0096808	Reduced ssp2-T189 phosphorylation under osmotic stress
PMID:28515144	PBO:0096810	Increased duration of ssp2-T189 phosphorylation under osmotic stress
PMID:28515144	PBO:0096809	Abolished ssp2-T189 phosphorylation under osmotic stress
PMID:28515144	PBO:0096808	Reduced ssp2-T189 phosphorylation under osmotic stress
PMID:28533364	GO:0170008	Second, Dcp1 stabilizes the fold of the Dcp2 RD, especially around the split active site, as revealed by hydrogen deuterium exchange rates (SI Appendix, Fig. S13). Finally, Edc1 enforces the active orientation in Dcp2 (Fig. 1 B–D) through specific interaction between its YAG activation motif and Dcp2.
PMID:28533364	GO:0170008	Second, Dcp1 stabilizes the fold of the Dcp2 RD, especially around the split active site, as revealed by hydrogen deuterium exchange rates (SI Appendix, Fig. S13). Finally, Edc1 enforces the active orientation in Dcp2 (Fig. 1 B-D) through specific interaction between its YAG activation motif and Dcp2. ------ COMMENT: 0927ffeae1602f26 6 920Q9A21F/+7Ic0Fevc8Buw9Caw Second, Dcp1 stabilizes the fold of the Dcp2 RD, especially around the split active site, as revealed by hydrogen deuterium exchange rates (SI Appendix, Fig. S13). Finally, Edc1 enforces the active orientation in Dcp2 (Fig. 1 B-D) through specific interaction between its YAG activation motif and Dcp2.
PMID:28541282	GO:0140746	(Fig. 5d,e) Only in presence of cid14/16 does rrp6 degrade ago1 bound rnas. This mechanism protects the genome from uncontrolled small RNAs
PMID:28541282	GO:0140746	(comment: CHECK see comment on cid14)
PMID:28545058	FYPO:0006926	(Fig. 1A, 1B)
PMID:28545058	FYPO:0000836	(Fig. 3B, Table S4) mass spec used to show that there is bulk accumulation of nuclear localised protein rather than a few specific proteins
PMID:28545058	FYPO:0001221	(Fig. 2A, 2B)
PMID:28545058	FYPO:0003286	(Fig. 3A)
PMID:28545058	FYPO:0000911	Table S5
PMID:28545058	PBO:0097188	(Fig. 2A)
PMID:28545058	PBO:0097188	(Fig. 2A)
PMID:28545058	FYPO:0001221	(Fig. 2A)
PMID:28545058	FYPO:0001221	(Fig. 4A, 4B)
PMID:28545058	FYPO:0001673	(Fig. 4A, 4B)
PMID:28545058	FYPO:0001221	(Fig. 4A)
PMID:28545058	PBO:0097188	(Fig. 4C, 4D)
PMID:28545058	PBO:0097191	(Fig. 4c)
PMID:28545058	PBO:0097191	(Fig. 4C) (comment: cut6-621 partial suppresses the increased NC ratio of rae1-167 so not sure whether increased NC ration is the correct term)
PMID:28545058	PBO:0097192	(Fig. 4D)
PMID:28545058	PBO:0097193	(Fig. 4D)
PMID:28545058	FYPO:0006926	(Fig. 1D)
PMID:28545058	FYPO:0006926	(Fig. 1D)
PMID:28545058	FYPO:0006926	(Fig. 1D)
PMID:28545058	FYPO:0006926	(Fig. 1D)
PMID:28545058	FYPO:0006926	(Fig. 1D)
PMID:28545058	FYPO:0006926	(Fig. 1D)
PMID:28545058	FYPO:0001221	(Fig. 1D)
PMID:28545058	FYPO:0001221	(Fig. 1D)
PMID:28545058	FYPO:0001221	(Fig. 1D)
PMID:28545058	FYPO:0001221	(Fig. 1D)
PMID:28545058	FYPO:0001221	(Fig. 1D)
PMID:28545058	FYPO:0001221	(Fig. 1D)
PMID:28545058	FYPO:0006926	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	(Fig. 1D)
PMID:28545058	FYPO:0002061	data not shown
PMID:28545058	FYPO:0000769	(Fig. 1C)
PMID:28545058	FYPO:0006926	(Fig. 1D)
PMID:28545058	FYPO:0000836	(Fig. 3A, 3B)
PMID:28545058	PBO:0097188	(Fig. 2A)
PMID:28545058	PBO:0097190	(Fig. S1C, S1D)
PMID:28545058	PBO:0097189	(Fig. 2A, 2B)
PMID:28545058	PBO:0097188	(Fig. 2A, 2B)
PMID:28545058	FYPO:0000769	(Fig. 1C)
PMID:28552615	FYPO:0000963	(Fig. S1B)
PMID:28552615	GO:0003918	(Figure 3F and G)
PMID:28552615	PBO:0112756	(comment: vw edited based on https://github.com/geneontology/go-annotation/issues/5239)
PMID:28552615	GO:0061995	(Fig. 5) (comment: vw, added substrate top2, this term will probably merge into displacement activity)
PMID:28552615	PBO:0112756	(comment: vw edited based on https://github.com/geneontology/go-annotation/issues/5239)
PMID:28552615	FYPO:0002775	(Fig. S1C)
PMID:28552615	FYPO:0002775	(Fig. S1C)
PMID:28552615	PBO:0098740	(Fig. S1C, 3A)
PMID:28552615	PBO:0098733	(Fig. S1E)
PMID:28552615	FYPO:0001690	(Fig. S1B)
PMID:28552615	FYPO:0000957	(Fig. S1B)
PMID:28552615	GO:0005515	(Figure S2E)
PMID:28552615	PBO:0098735	(Fig. 2h)
PMID:28552615	PBO:0098737	(Fig. 2i)
PMID:28552615	PBO:0098739	(Fig. 3a)
PMID:28552615	PBO:0098736	(Fig. 2h)
PMID:28552615	FYPO:0002775	(Fig. S1C)
PMID:28552615	PBO:0098735	(Fig. 2h)
PMID:28552615	FYPO:0000969	(Fig. S1B)
PMID:28552615	FYPO:0002775	(Fig. S1C)
PMID:28552615	FYPO:0002775	(Fig. S1C)
PMID:28552615	FYPO:0002775	(Fig. S1C)
PMID:28552615	FYPO:0002775	(Fig. S1C)
PMID:28572514	PBO:0105204	(Fig. 7)
PMID:28572514	PBO:0107770	(Fig. 7)
PMID:28572514	PBO:0107770	(Fig. 7)
PMID:28572514	PBO:0107770	(Fig. 7)
PMID:28572514	PBO:0019744	(Fig. 6)
PMID:28572514	GO:0005628	(Fig. 6)
PMID:28572514	PBO:0107767	(comment: vw: changed to match previous session terms RNA ...from cuf1Δ mutant spores showed loss of copper starvation-dependent induction of ctr4+ and ctr5+ gene expression, indicating that the copper-dependent reg ulation of ctr4+ and ctr5+ mRNAs required Cuf1 during germination and outgrowth.)
PMID:28572514	PBO:0105204	(Fig. 7)
PMID:28572514	PBO:0107766	(comment: vw: changed to match previous session terms RNA ...from cuf1Δ mutant spores showed loss of copper starvation-dependent induction of ctr4+ and ctr5+ gene expression, indicating that the copper-dependent reg ulation of ctr4+ and ctr5+ mRNAs required Cuf1 during germination and outgrowth.)
PMID:28572514	GO:0005886	(Fig. 5)
PMID:28572514	PBO:0107769	(Fig. 9)
PMID:28572514	PBO:0107768	(comment: vw: changed to match previous session terms RNA ...from cuf1Δ mutant spores showed loss of copper starvation-dependent induction of ctr4+ and ctr5+ gene expression, indicating that the copper-dependent reg ulation of ctr4+ and ctr5+ mRNAs required Cuf1 during germination and outgrowth.)
PMID:28586299	FYPO:0006920	(Figure 4B) decreased frequency of deletions at direct repeat recombination reporter
PMID:28586299	FYPO:0006920	(Figure 4C) decreased frequency of gene conversions at direct repeat recombination reporter
PMID:28586299	FYPO:0006921	(Figure 2) decreased frequency of gene conversions but unaltered frequency of deletions at direct repeat recombination reporter; deletions in a rad51∆ mutant depend on Rad52
PMID:28586299	FYPO:0000167	(Figure 4C) increased frequency of deletions at direct repeat recombination reporter
PMID:28586299	FYPO:0006920	(Figure 4A) decreased frequency of deletions and gene conversions at direct repeat recombination reporter
PMID:28600551	FYPO:0005968	(Fig. 1)
PMID:28600551	FYPO:0005968	(Fig. 1)
PMID:28600551	FYPO:0005968	(comment: I can never remember why e.g. sodium chloride isn't a child to salt stress)
PMID:28600551	FYPO:0000852	(Fig. 1c)
PMID:28600551	FYPO:0000852	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	FYPO:0000852	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	FYPO:0003743	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	FYPO:0003743	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	FYPO:0003743	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	FYPO:0003743	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	FYPO:0003743	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	PBO:0103776	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	PBO:0103778	(Fig. 4)
PMID:28600551	FYPO:0000584	(Fig. 5)
PMID:28600551	FYPO:0000584	(Fig. 5)
PMID:28600551	PBO:0103789	(Fig. 5)
PMID:28600551	FYPO:0006712	(Fig. 5)
PMID:28600551	FYPO:0006712	(Fig. 5)
PMID:28600551	PBO:0103790	(Fig. 5)
PMID:28600551	FYPO:0006713	(Fig. 5)
PMID:28600551	FYPO:0006713	(Fig. 5)
PMID:28600551	FYPO:0006714	(Fig. 5)
PMID:28600551	FYPO:0006714	(Fig. 5)
PMID:28600551	FYPO:0006714	(Fig. 5)
PMID:28600551	PBO:0101662	(Fig. 5)
PMID:28600551	FYPO:0000584	(Fig. 5)
PMID:28600551	PBO:0103778	(Fig. 4)
PMID:28600551	PBO:0103776	(Fig. 4)
PMID:28600551	PBO:0103776	(Fig. 4)
PMID:28600551	PBO:0103776	(Fig. 4)
PMID:28600551	PBO:0103776	(Fig. 4)
PMID:28600551	FYPO:0004765	(Fig. 4)
PMID:28600551	FYPO:0004765	(Fig. 4)
PMID:28600551	PBO:0103786	(Fig. 2a)
PMID:28600551	FYPO:0004765	(Fig. 3c)
PMID:28600551	PBO:0103778	(Fig. 2a)
PMID:28600551	PBO:0103778	(Fig. 2a)
PMID:28600551	FYPO:0003743	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	FYPO:0003743	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	PBO:0103785	(Fig. 3d)
PMID:28600551	PBO:0103785	(Fig. 3d)
PMID:28600551	PBO:0103784	(Fig. 2e)
PMID:28600551	PBO:0103783	(Fig. 2e)
PMID:28600551	PBO:0103782	(Fig. 2d)
PMID:28600551	PBO:0103781	(Fig. 2d)
PMID:28600551	PBO:0103780	(Fig. 2c)
PMID:28600551	PBO:0103779	(Fig. 2c)
PMID:28600551	PBO:0103778	(Fig. 2a)
PMID:28600551	PBO:0103777	(Fig. 2a)
PMID:28600551	FYPO:0001987	(Fig. 1d)
PMID:28600551	FYPO:0001987	(Fig. 1d)
PMID:28600551	FYPO:0001987	(Fig. 1d)
PMID:28600551	PBO:0101662	(Fig. 5)
PMID:28600551	PBO:0103787	(Fig. 5)
PMID:28600551	PBO:0103788	(Fig. 5)
PMID:28600551	FYPO:0000303	(Fig. 5)
PMID:28600551	FYPO:0000303	(Fig. 5)
PMID:28600551	PBO:0100647	(Fig. 5)
PMID:28619713	FYPO:0001791	(Fig. 6C)
PMID:28619713	PBO:0103586	(Fig. 6C)
PMID:28619713	GO:0061496	(Fig. S1B)
PMID:28619713	GO:0140480	Our data suggest that Sad1 is present at the SPB early to set up structures that will trigger SPB insertion before the cell even enters mitosis.fig6
PMID:28619713	GO:0140480	(comment: rename CHECK term https://github.com/geneontology/go-ontology/issues/14887) Our data suggest that Sad1 is present at the SPB early to set up structures that will trigger SPB insertion before the cell even enters mitosis.fig6
PMID:28619713	GO:0061496	(Fig. S1B)
PMID:28631612	PBO:0092298	"(comment: ""antidote"" product of longer alternative transcript; assayed by expressing S.k. ortholog in S.p.)"
PMID:28631612	GO:0072324	"(comment: ""poison"" product of shorter alternative transcript;assayed by expressing S.k. ortholog in S.p.)"
PMID:28640807	PBO:0093559	(comment: CHECK aerobic conditions)
PMID:28640807	PBO:0093559	(comment: CHECK aerobic conditions)
PMID:28640807	PBO:0093560	(comment: CHECK aerobic conditions)
PMID:28640807	PBO:0093560	(comment: CHECK aerobic conditions)
PMID:28640807	PBO:0093560	(comment: CHECK aerobic conditions)
PMID:28640807	PBO:0093560	(comment: CHECK aerobic conditions)
PMID:28640807	PBO:0099137	Increased Cdc22 oxidation attenuated by 2 mM Glutathione. Increased Cdc22 oxidation attenuated by deleting tpx1.
PMID:28640807	PBO:0099137	Increased Cdc22 oxidation attenuated by 2 mM Glutathione. Increased Cdc22 oxidation attenuated by deleting tpx1.
PMID:28640807	FYPO:0003238	(comment: CHECK 2 mM Glutathione restores aerobic growth.)
PMID:28640807	PBO:0097692	(comment: CHECK 2 mM Glutathione restores aerobic growth.)
PMID:28640807	PBO:0093560	(comment: CHECK aerobic conditions)
PMID:28652406	FYPO:0000087	Δatf1 expressing the mutant named HA-Atf1.6M, lacking sites 5 to 10 in Atf1, was as sensitive to growth on peroxide-containing plates as cells lacking Atf1.
PMID:28652406	FYPO:0000087	the HA-Atf1.1M mutant was fully able to suppress the sensitivity to peroxides of strain Δatf1, expression of the HA-Atf1.10M and 11M mutants did not alleviate this phenotype (supplemental Fig. S1C).
PMID:28652406	PBO:0105244	whereas the expression of all stress genes in cells expressing HAAtf1.10D was not altered by sty1 deletion. Concomitantly
PMID:28652406	PBO:0105834	whereas the expression of all stress genes in cells expressing HAAtf1.10D was not altered by sty1 deletion. Concomitantly
PMID:28652406	FYPO:0000962	expression of HA-Atf1.10D fully suppressed all stress defects of cells lacking Sty1 (Fig. 2C).
PMID:28652406	PBO:0105836	whereas the expression of all stress genes in cells expressing HAAtf1.10D was not altered by sty1 deletion. Concomitantly
PMID:28652406	PBO:0100901	2A,cells expressing the hypophosphorylation mutant HA-Atf1.10M are not able to fully trigger the ctt1 and srx1 genes after H2O2 stress
PMID:28652406	FYPO:0000087	the HA-Atf1.1M mutant was fully able to suppress the sensitivity to peroxides of strain Δatf1, expression of the HA-Atf1.10M and 11M mutants did not alleviate this phenotype (supplemental Fig. S1C).
PMID:28652406	PBO:0094384	expression of the Sty1-independent Atf1.7D-HA mutant cannot bypass the absence of Pcr1, as shown by the lack of transcription of stress genes (Fig. 4C).
PMID:28652406	PBO:0097079	(comment: CHECK ditto)
PMID:28652406	PBO:0105838	whether Atf1 binding to DNA is dependent on the presence of Pcr1; as shown in Fig. 4D, Atf1-GFP is not recruited to DNA in Δpcr1 cells, with the only exception of srx1
PMID:28652406	PBO:0105837	(comment: CHECK ditto)
PMID:28652406	PBO:0097080	(comment: CHECK ditto)
PMID:28652406	PBO:0105840	that Pap1 is dispensable for the activation of gpd1 and hsp9 but required for ctt1 and srx1 (Fig. 5A)
PMID:28652406	FYPO:0001485	the HA-Atf1.1M mutant was fully able to suppress the sensitivity to peroxides of strain Δatf1, expression of the HA-Atf1.10M and 11M mutants did not alleviate this phenotype (supplemental Fig. S1C).
PMID:28652406	PBO:0105841	(comment: CHECK ditto)
PMID:28652406	PBO:0105838	Regarding the role of Pap1 and Atf1 at these genes, ChIP analysis indicates that the stress-dependent recruitment of Atf1 to ctt1 and srx1 promoters is dependent on Pap1 (Fig. 5C).
PMID:28652406	FYPO:0000962	(comment: vw, I deleted Caludias annotation by mistake when comparing to the older partially completed session by Laura, so adding back !)
PMID:28652406	PBO:0105845	As shown in Fig. 2B, the capacity of HA-Atf1.10M to activate hsp9 and gpd1 after stress imposition was abolished in the absence of Sty1
PMID:28652406	PBO:0105844	As shown in Fig. 2B, the capacity of HA-Atf1.10M to activate hsp9 and gpd1 after stress imposition was abolished in the absence of Sty1
PMID:28652406	PBO:0105838	....whereas it is never recruited to these promoters in cells expressing Pap1.C523D (Fig. 5D).
PMID:28652406	PBO:0105842	Atf1 is constitutively bound to srx1 and ctt1 in strain Δtrr1....
PMID:28652406	PBO:0105835	whereas the expression of all stress genes in cells expressing HAAtf1.10D was not altered by sty1 deletion. Concomitantly
PMID:28652406	PBO:0105837	Atf1.7M-HA are constitutively bound to the gpd1 and hsp9 promoters both before and after stress
PMID:28652406	PBO:0094384	(comment: CHECK ditto)
PMID:28652406	PBO:0100901	(comment: CHECK ditto)
PMID:28652406	PBO:0105835	allows stress-dependent activation of ctt1 and srx1 to the same extent as wild-type cells; however, it constitutively induces expression of gpd1 and hsp9 (Fig. 2A).
PMID:28652406	PBO:0105836	allows stress-dependent activation of ctt1 and srx1 to the same extent as wild-type cells; however, it constitutively induces expression of gpd1 and hsp9 (Fig. 2A).
PMID:28652406	FYPO:0000087	(comment: CHECK ditto)
PMID:28652406	PBO:0105836	(comment: CHECK ditto)
PMID:28652406	PBO:0105835	Strains expressing wild-type Atf1 or Atf1.7M or Atf1.7D mutants displayed the same patterns of tolerance to peroxides and activation of stress genes as the constitutive amino-terminally tagged versions (supplemental Fig S4, B and C).
PMID:28652406	PBO:0105835	Importantly, expression of the phospho-mimicking HA-Atf1.10D (Fig. 2B) or HA-Atf1.6D (Fig S3, C and D) bypasses the requirement for a MAP kinase in the transcription process, which questions the direct participation of the kinase in Pol II initiation and/or elongation.
PMID:28652406	FYPO:0000962	Concomitantly, although expression of HA-Atf1.10M was not able to suppress the sensitivity to peroxides of strain Δatf1 (supplemental Fig. S1C and Fig. 1G), expression of HAAtf1.10D alleviated this phenotype (Fig. 1G).
PMID:28656962	PBO:0099985	These data suggest that Bhd1 and Ypt71 (but not Ypt7) functionally interact and, in agreement with the mammalian cell data, negatively regulate TORC1 activity in response to amino-acid deprivation.
PMID:28656962	FYPO:0001357	(Figure 5b)
PMID:28656962	FYPO:0001357	(Figure 5b)
PMID:28656962	FYPO:0001357	(Figure 5b)
PMID:28656962	PBO:0099985	These data suggest that Bhd1 and Ypt71 (but not Ypt7) functionally interact and, in agreement with the mammalian cell data, negatively regulate TORC1 activity in response to amino-acid deprivation.
PMID:28656962	FYPO:0000077	To determine whether these proteins are related to TORC1 signalling, we treated bhd1Δ, ypt71Δ, ypt7Δ and double deletion strains with 200 ng ml−1 of rapamycin and found that all of the strains grew better than WT cells (Fig. 5b).
PMID:28656962	FYPO:0000077	To determine whether these proteins are related to TORC1 signalling, we treated bhd1Δ, ypt71Δ, ypt7Δ and double deletion strains with 200 ng ml−1 of rapamycin and found that all of the strains grew better than WT cells (Fig. 5b).
PMID:28656962	FYPO:0000077	To determine whether these proteins are related to TORC1 signalling, we treated bhd1Δ, ypt71Δ, ypt7Δ and double deletion strains with 200 ng ml−1 of rapamycin and found that all of the strains grew better than WT cells (Fig. 5b).
PMID:28656962	FYPO:0001355	Strains lacking Ypt7 (ypt7Δ, bhd1Δ ypt7Δ, ypt71Δ ypt7Δ) displayed a significant growth defect in the low amino-acid condition (EMM plates supplemented with low concentration of amino acids) compared to WT strains, or bhd1Δ and ypt71Δ strains (Fig. 5b).
PMID:28656962	FYPO:0001355	Strains lacking Ypt7 (ypt7Δ, bhd1Δ ypt7Δ, ypt71Δ ypt7Δ) displayed a significant growth defect in the low amino-acid condition (EMM plates supplemented with low concentration of amino acids) compared to WT strains, or bhd1Δ and ypt71Δ strains (Fig. 5b).
PMID:28656962	FYPO:0001355	Strains lacking Ypt7 (ypt7Δ, bhd1Δ ypt7Δ, ypt71Δ ypt7Δ) displayed a significant growth defect in the low amino-acid condition (EMM plates supplemented with low concentration of amino acids) compared to WT strains, or bhd1Δ and ypt71Δ strains (Fig. 5b).
PMID:28656962	FYPO:0001355	Strains lacking Ypt7 (ypt7Δ, bhd1Δ ypt7Δ, ypt71Δ ypt7Δ) displayed a significant growth defect in the low amino-acid condition (EMM plates supplemented with low concentration of amino acids) compared to WT strains, or bhd1Δ and ypt71Δ strains (Fig. 5b).
PMID:28656962	FYPO:0001355	Strains lacking Ypt7 (ypt7Δ, bhd1Δ ypt7Δ, ypt71Δ ypt7Δ) displayed a significant growth defect in the low amino-acid condition (EMM plates supplemented with low concentration of amino acids) compared to WT strains, or bhd1Δ and ypt71Δ strains (Fig. 5b).
PMID:28656962	PBO:0109157	We observed that loss of Bhd1 and Ypt71, but not Ypt7, resulted in increased TORC1 activity, as determined by an increase in Rps6 and p70 S6K phosphorylation levels when cells were deprived of amino acids (Fig. 5a, compare lanes 1, 3, 5 and 7).
PMID:28656962	PBO:0109156	We observed that loss of Bhd1 and Ypt71, but not Ypt7, resulted in increased TORC1 activity, as determined by an increase in Rps6 and p70 S6K phosphorylation levels when cells were deprived of amino acids (Fig. 5a, compare lanes 1, 3, 5 and 7).
PMID:28659415	GO:0036286	(comment: Pil1p form filaments. Pil1 exchanges rapidly at the ends of these filaments in vivo)
PMID:28659415	GO:0070941	(comment: Pil1p form filaments. Pil1 exchanges rapidly at the ends of these filaments in vivo)
PMID:28674280	PBO:0103012	(comment: CHECK same as snf22delta alone)
PMID:28674280	PBO:0103012	(comment: CHECK same as snf22delta alone)
PMID:28674280	PBO:0103012	same as snf22delta alone
PMID:28765164	PBO:0099881	(Fig. 2e)
PMID:28765280	FYPO:0002060	(Fig. 6A)
PMID:28765280	FYPO:0002060	(Fig. 1A)
PMID:28765280	FYPO:0002061	(Figure 1B)
PMID:28765280	PBO:0095311	(Fig. 1E,F)
PMID:28765280	FYPO:0002060	(Fig. 2A)
PMID:28765280	PBO:0095315	(Figure 6E,F)
PMID:28765280	PBO:0095314	(Fig. 6C)
PMID:28765280	FYPO:0000673	(Fig. 6C)
PMID:28765280	PBO:0095314	(Fig. 6G).
PMID:28765280	PBO:0095313	(Figure 3b)
PMID:28765280	FYPO:0002060	(Figure 1D)
PMID:28765280	PBO:0095316	(Fig. 7A)
PMID:28765280	PBO:0095316	(Fig. 7A)
PMID:28765280	PBO:0038207	(Figure 2)
PMID:28765280	FYPO:0002060	(Fig. 7A)
PMID:28765280	FYPO:0002060	(Fig. 7A)
PMID:28765280	PBO:0095312	(Figure 3b)
PMID:28765280	FYPO:0002060	(Fig. 1B)
PMID:28765280	FYPO:0000673	(Fig. 1B)
PMID:28771613	PBO:0108423	The preRC- loading delay was abolished in the irradiated gcn1Δ cells (Fig 3C)
PMID:28771613	PBO:0108419	(Figure 1E)
PMID:28771613	PBO:0108423	The preRC- loading delay was abolished in the irradiated gcn1Δ cells (Fig 3C)
PMID:28771613	PBO:0108420	(Figure 1E)
PMID:28771613	PBO:0108417	(Figure 1E)
PMID:28771613	PBO:0108424	(comment: unfortunately no direct binding data, but physical interactions have been shown in other organisms)
PMID:28771613	PBO:0108418	(Figure 2B)
PMID:28775153	FYPO:0000229	(Fig. 4D) DAPI staining. (comment: CHECK I have requested a new term and included response to streptonigrin but should it be more general e.g. response to DNA damaging agent (if this is known))
PMID:28775153	FYPO:0000229	(Fig. 4B) DAPI staining. (comment: CHECK I have requested a new term and included response to streptonigrin but should it be more general e.g. response to DNA damaging agent (if this is known))
PMID:28775153	FYPO:0006865	(Fig. 4C) DAPI staining. (comment: CHECK I have requested a new term and included response to streptonigrin but should it be more general e.g. response to DNA damaging agent (if this is known))
PMID:28784611	PBO:0102564	(Fig. 2A-C)
PMID:28784611	GO:1903475	(comment: naintenence)
PMID:28784611	GO:0005886	(Figure 1B)
PMID:28784611	PBO:0102565	(Fig. 3A) (in table, data not shown)
PMID:28784611	PBO:0102562	(Fig. 2A-C)
PMID:28784611	PBO:0102561	(Fig. 2A-C)
PMID:28784611	FYPO:0002061	(Fig. S1C, S1D)
PMID:28784611	FYPO:0002061	(Fig. S1C, S1D)
PMID:28784611	PBO:0102560	(Figure 1C)
PMID:28784611	PBO:0102559	(Figure 1C)
PMID:28784611	PBO:0102558	(Figure S2E)
PMID:28784611	FYPO:0005020	(Figure S2A, S2B)
PMID:28784611	FYPO:0005905	(Figure S2A, S2B)
PMID:28784611	FYPO:0002061	(Figure S1C)
PMID:28784611	FYPO:0001489	(Figure S1D)
PMID:28784611	PBO:0102557	(Figure 3D)
PMID:28784611	PBO:0098955	(Figure 3B)
PMID:28784611	PBO:0102556	(Figure 3C)
PMID:28784611	PBO:0098958	(Figure 3E)
PMID:28784611	FYPO:0003278	"(comment: CHECK i requested reduced plasma membrane PIP issues/3117 GFP-2xPH(Plc delta)) ""localization The PI(4,5)P2 sensor GFP-2×PH(PLCδ) (Stefan et al., 2002) was reduced at the cell cortex and the division site in efr3Δ compared with WT (Fig. 1 D), indicating that PIP PM abundance is reduced in efr3Δ"""
PMID:28784611	GO:0005886	(Figure 1B)
PMID:28784611	GO:0005886	(Fig. 1B)
PMID:28784611	FYPO:0002253	(Fig. S2C)
PMID:28784611	FYPO:0002253	(Fig. 5A)
PMID:28784611	FYPO:0004293	(Fig. 1A, 1B)
PMID:28784611	FYPO:0000339	(Figure 1A)
PMID:28784611	FYPO:0002061	(Fig. S2D)
PMID:28784611	FYPO:0006005	(Fig. 5B) CR sliding events no longer occurred in myo51Δ efr3Δ
PMID:28784611	GO:0007009	(comment: phospholipid biosynthesis?)
PMID:28784611	FYPO:0006005	(Fig. 5B) CR sliding events no longer occurred in myo51Δ efr3Δ
PMID:28806726	FYPO:0006242	replication forks stall with partial dependence on intra-S checkpoint (fig. 6)
PMID:28806726	FYPO:0006241	inhibition of origin firing requires intra-S checkpoint (fig. 5)
PMID:28806726	FYPO:0006242	replication forks stall with partial dependence on intra-S checkpoint (fig. 6)
PMID:28806726	FYPO:0006241	inhibition of origin firing requires intra-S checkpoint (fig. 5)
PMID:28806726	FYPO:0006240	replication forks slow independently of intra-S checkpoint (fig. 6)
PMID:28806726	FYPO:0003923	(table S1)
PMID:28806726	FYPO:0006242	replication forks stall with partial dependence on intra-S checkpoint (fig. 6)
PMID:28806726	FYPO:0006241	inhibition of origin firing requires intra-S checkpoint (fig. 5)
PMID:28811350	PBO:0096424	(comment: consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA)
PMID:28811350	PBO:0096420	(comment: consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA)
PMID:28811350	PBO:0096423	(comment: consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA)
PMID:28811350	PBO:0096422	(comment: consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated from MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	(comment: generated by MMS mutagenesis)
PMID:28825727	FYPO:0006302	(comment: Cnd3 depletion following promoter shut-off and auxin-induced degron activation)
PMID:28825727	FYPO:0006302	(Fig. 2b) (comment: hi-C difference assay)
PMID:28825727	FYPO:0006302	(Fig. 3) (comment: hi-C)
PMID:28825727	FYPO:0000214	(comment: Cnd3 depletion following promoter shut-off and auxin-induced degron activation)
PMID:28825727	FYPO:0006248	(comment: hic and) Fig. 3C (comment: pcr ) fig 2d increased mitotic intra centromere connection
PMID:28825727	FYPO:0000214	Supplementary Figs. 1b, 1f, 4a-c (comment: Cnd3 depletion following promoter shut-off and auxin-induced degron activation)
PMID:28825727	FYPO:0006302	(comment: (vw made more specific) Hi-C) Supplementary Figs. 1b, 1f, 4a-c
PMID:28825727	FYPO:0000214	(comment: hi C????? ) Supplementary Figs. 1b, 1f, 4a-c
PMID:28827290	FYPO:0001357	(Fig. 6)
PMID:28827290	FYPO:0001355	(Fig. 5)
PMID:28827290	FYPO:0001355	(Fig. 5)
PMID:28827290	FYPO:0002060	(Fig. 4)
PMID:28827290	FYPO:0002060	(Fig. 4)
PMID:28827290	FYPO:0002060	(Fig. 4)
PMID:28827290	FYPO:0002061	(Fig. 3)
PMID:28827290	FYPO:0002061	(Fig. 3)
PMID:28827290	FYPO:0002061	(Fig. 3)
PMID:28827290	FYPO:0002061	(Fig. 3)
PMID:28827290	FYPO:0002061	(Fig. 3)
PMID:28827290	FYPO:0002061	(Fig. 3)
PMID:28827290	FYPO:0002061	(Fig. 3)
PMID:28827290	PBO:0101837	(Fig. 2D)
PMID:28827290	PBO:0101836	(comment: CHECK wt 68%) (Fig. 2C)
PMID:28827290	GO:0000775	(Fig. 2C)
PMID:28827290	PBO:0101835	(Fig. 2B)
PMID:28827290	PBO:0094554	(Figure 2B)
PMID:28827290	FYPO:0002061	(Fig. 2)
PMID:28827290	FYPO:0002061	(Fig. 2)
PMID:28827290	PBO:0101834	(Fig. 1B)
PMID:28827290	PBO:0101833	(Fig. 1B)
PMID:28827290	FYPO:0002061	(Fig. 3)
PMID:28827290	FYPO:0002061	(Fig. 3)
PMID:28827290	FYPO:0002061	(Fig. 3)
PMID:28827290	FYPO:0001357	(Fig. 8)
PMID:28827290	PBO:0101838	(Fig. 7)
PMID:28827290	FYPO:0001357	(Fig. 6)
PMID:28827290	FYPO:0001357	(Fig. 6)
PMID:28827290	FYPO:0001357	(Fig. 6)
PMID:28827290	FYPO:0001357	(Fig. 6)
PMID:28827290	FYPO:0001357	(Fig. 6)
PMID:28827290	PBO:0094438	(Fig. 5)
PMID:28841135	PBO:0108111	(comment: mRNA co-immunoprecipitated with ribosomes)
PMID:28882432	FYPO:0001157	(Fig. 3)
PMID:28904333	FYPO:0006843	especially at centromere; also at other regions where Ino80 complex normally binds
PMID:28904333	PBO:0100463	(comment: CONDITION 25 degrees)
PMID:28904333	FYPO:0006843	(comment: especially at centromere; also at other regions where Ino80 complex normally binds)
PMID:28904333	PBO:0100463	(comment: CONDITION 30 degrees)
PMID:28924043	PBO:0107344	Cdr1-K41A remains in nodes; Cdr1+ not tagged
PMID:28924043	PBO:0107336	combination of in vitro kinase assay and mutant phenotypes
PMID:28924043	PBO:0107333	(comment: Cdr2 does not exit nodes (unlike Cdr1) upon osmotic stress)
PMID:28924043	PBO:0107341	Cdr1-K41A remains unphosphorylated; Cdr1+ not tagged
PMID:28934464	PBO:0107970	(Fig. 3C)
PMID:28934464	PBO:0107976	(Fig. 3E)
PMID:28934464	GO:0003714	(Fig. 5D) (comment: a bit tenuous but we don't have this annotated..)
PMID:28934464	GO:0003714	(Fig. 5D) (comment: a bit tenuous but we don't have this annotated..)
PMID:28934464	GO:0140585	(comment: I replaced GO:0090579 dsDNA loop formation as per https://github.com/geneontology/go-annotation/issues/3610)
PMID:28934464	PBO:0107969	(Fig. 3B)
PMID:28934464	PBO:0107969	(Fig. S2D)
PMID:28934464	PBO:0107972	(Fig. 3C)
PMID:28934464	PBO:0107970	(Fig. 3C)
PMID:28934464	PBO:0107971	(Fig. 3C)
PMID:28934464	PBO:0107969	(Fig. 3B)
PMID:28934464	PBO:0107975	(Fig. 3E)
PMID:28934464	PBO:0107974	(Fig. 3D)
PMID:28934464	PBO:0107973	(Fig. 3D)
PMID:28944093	FYPO:0000271	(comment: can't disambiguate salt from specific calcium sensitivity in these experiments)
PMID:28944093	FYPO:0000271	(comment: can't disambiguate salt from specific calcium sensitivity in these experiments)
PMID:28944093	FYPO:0000098	(comment: can't disambiguate salt from specific calcium sensitivity in these experiments)
PMID:28944093	FYPO:0000098	(comment: can't disambiguate salt from specific calcium sensitivity in these experiments)
PMID:28947618	PBO:0109713	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	(comment: CHECK does not grow at high temperature, defective pre-mRNA splicing, assayed_using SPBC1778.02 | assayed_using SPAC227.16C | assayed_using SPBP16F5.02
PMID:28947618	GO:0005634	(comment: CHECK column_17 Sde2UBL)
PMID:28947618	GO:0045292	(comment: CHECK Intron-Specific pre-mRNA Splicing)
PMID:28947618	PBO:0109678	(comment: CHECK decreased cell population growth at high temperature)
PMID:28947618	FYPO:0003244	does not complement sde2Δ, defective in telomeric silencing and genome stability
PMID:28947618	FYPO:0001355	normal processing, protein very stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, complements partially sde2Δ
PMID:28947618	FYPO:0001355	processing defective, does not complement sde2Δ
PMID:28947618	FYPO:0001575	(Fig. 1D) does not complement sde2Δ
PMID:28947618	FYPO:0001355	(Fig. 1D) complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, protein very stable, does not complement sde2Δ
PMID:28947618	FYPO:0001355	normal processing, protein unstable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, protein unstable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, protein stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, protein very stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, protein stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, protein very stable, complements partially sde2Δ
PMID:28947618	FYPO:0003244	(Fig. 3C) decreased cell growth, normal processing, protein very stable, complements partially sde2Δ; over expression causes growth defect in hub1-1 strain, defective in telomeric silencing and genome stability
PMID:28947618	FYPO:0001355	normal processing, complements partially sde2Δ
PMID:28947618	FYPO:0001575	processing defective, does not complement sde2Δ
PMID:28947618	FYPO:0001355	normal processing, protein very stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, protein unstable,complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, protein stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, protein very stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, complements partially sde2Δ
PMID:28947618	FYPO:0001355	reduced processing, complements partially sde2Δ
PMID:28947618	FYPO:0001355	processing defective, does not complement sde2Δ
PMID:28947618	FYPO:0001357	(Fig. EV2B) normal processing, complements sde2Δ
PMID:28947618	FYPO:0001357	(Fig. EV2B) normal processing, complements sde2Δ
PMID:28947618	FYPO:0001355	(Fig. EV2B) processing defective, does not complement sde2Δ
PMID:28947618	FYPO:0001355	(Fig. EV2B) processing defective, does not complement sde2Δ
PMID:28947618	FYPO:0001355	(Fig. EV2B) processing defective, does not complement sde2Δ
PMID:28947618	FYPO:0001355	(Fig. EV2B) processing defective, does not complement sde2Δ
PMID:28947618	PBO:0109679	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109680	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109681	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109682	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109683	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109684	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109685	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109686	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109687	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109688	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109689	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109690	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109691	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109692	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109693	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109694	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109695	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109696	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109697	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109698	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109699	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109700	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109701	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109702	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109703	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109704	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109705	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109706	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109707	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109708	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109709	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109710	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109711	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0109712	(Fig. 5B,S5A,S5B)
PMID:28947618	PBO:0106830	(comment: CHECK endo mutant does not cleave Sde2 precursor)
PMID:28947618	PBO:0106831	(comment: CHECK endo mutant does not cleave Sde2 precursor)
PMID:28947618	FYPO:0003244	(comment: CHECK assayed_using SPBC1778.02 | assayed_using SPAC227.16C | assayed_using SPBP16F5.02)
PMID:28947618	PBO:0106832	(Fig. 1B)
PMID:28947618	PBO:0106832	(Fig. 1B)
PMID:28947618	PBO:0106833	Appendix Fig S2A
PMID:28947618	PBO:0106832	(Fig. 2A,B)
PMID:28947618	PBO:0106834	(Fig. 2D)
PMID:28947618	PBO:0106834	(Fig. 2D)
PMID:28947618	PBO:0106835	(Fig. 3E) (comment: CHECK N-end rule pathway substrate assayed using LysSde2-C N-end rule substrate pro-obo/term-requests/119/ )
PMID:28947618	PBO:0106836	(Fig. 3E) (comment: CHECK N-end rule pathway substrate assayed using LysSde2-C N-end rule substrate pro-obo/term-requests/119/ )
PMID:28947618	GO:0005681	(Fig. 4A)
PMID:28947618	PBO:0106837	(Fig 7A)
PMID:28947618	PBO:0106838	(Fig 7A)
PMID:28947618	PBO:0106839	(Fig 7A)
PMID:28947618	PBO:0106840	(Fig. 8B) (comment: CHECK in spliceosome)
PMID:28947618	GO:0045292	(comment: CHECK Intron-Specific pre-mRNA Splicing)
PMID:28974540	FYPO:0002061	(Fig. 2E)
PMID:28974540	FYPO:0002061	(Fig. 2E)
PMID:28974540	FYPO:0002061	(Fig. 2E)
PMID:28974540	FYPO:0000324	(Fig. S2B)
PMID:28974540	PBO:0104444	(comment: added affected genes as extensions) fig 3A-C
PMID:28974540	FYPO:0000227	(Fig. 1)
PMID:28974540	GO:0005635	(Fig. 5A)
PMID:28974540	MOD:01148	(Fig. 4G and see the Ubiquitin pull-down section of Materials and methods).
PMID:28974540	GO:0005635	(Fig. 5A)
PMID:28974540	PBO:0104456	(Fig. 5b) (comment: nuclear envelope)
PMID:28974540	PBO:0104457	(Fig. 5b)
PMID:28974540	PBO:0104458	(Fig. 5D-G) (comment: nuclear envelope)
PMID:28974540	PBO:0104445	(comment: added affected genes as extensions) fig 3A-C
PMID:28974540	PBO:0104446	(comment: added affected genes as extensions) fig 3A-C
PMID:28974540	PBO:0104459	(Fig. 5D-G) (comment: nuclear envelope)
PMID:28974540	PBO:0104446	(Fig. 6)
PMID:28974540	PBO:0104460	(Fig. 6)
PMID:28974540	PBO:0104461	(Fig. 6)
PMID:28974540	FYPO:0002061	(Fig. 2E)
PMID:28974540	PBO:0104446	(Fig. 4a)
PMID:28974540	PBO:0104455	(Fig. 4c)
PMID:28974540	PBO:0104446	(Fig. 4e)
PMID:28974540	FYPO:0002061	(Fig. 2E)
PMID:28974540	PBO:0104443	(comment: added affected genes as extensions) fig 3A-C
PMID:28974540	PBO:0104442	(comment: added affected genes as extensions) fig 3A-C
PMID:28974540	FYPO:0002638	(Fig. S3)
PMID:28974540	PBO:0104441	(Fig. 1b)
PMID:28974540	FYPO:0002061	(Fig. 2E)
PMID:28974540	FYPO:0002061	(Fig. 2E)
PMID:28974540	FYPO:0002061	(Fig. 2E)
PMID:28974540	PBO:0104447	(comment: added affected genes as extensions) fig 3A-C
PMID:28974540	PBO:0104448	(comment: added affected genes as extensions) fig 3A-C
PMID:28974540	PBO:0104449	(comment: added affected genes as extensions) fig 3A-C
PMID:28974540	PBO:0033477	(Fig. S2A, S1E)
PMID:28974540	FYPO:0002649	(comment: vw: moved down to elongated (update fypo?)) fig 1e
PMID:28974540	GO:0017056	(Fig. 1a) (comment: + others)
PMID:28974540	FYPO:0000284	(Fig. 1C)
PMID:28974540	PBO:0104450	(Fig. 1)
PMID:28974540	PBO:0104451	(Fig. S2)
PMID:28974540	PBO:0104452	(Fig. S3C)
PMID:28974540	PBO:0100719	(Fig. S3E)
PMID:28974540	PBO:0095380	(Fig. S3G, S3H)
PMID:28974540	PBO:0104453	(Fig. S3I) (comment: additive, do we know %?)
PMID:28974540	PBO:0099862	(comment: added affected genes as extensions) fig 3E
PMID:28974540	PBO:0104454	(comment: added affected genes as extensions) fig 3E
PMID:28974540	FYPO:0003094	(Fig. 3)
PMID:28974540	FYPO:0006353	(Fig. 3)
PMID:28974540	FYPO:0004314	(Fig. 3G)
PMID:28976798	GO:0005515	(Fig. 1)
PMID:28976798	PBO:0099345	(Fig. 1D)
PMID:28976798	GO:0005515	(Fig. 1)
PMID:28976798	GO:0005515	(Fig. 1)
PMID:28976798	GO:0005515	(Fig. 1)
PMID:28977643	GO:0045003	(comment: CHECK mhf1-L78R)
PMID:28977649	PBO:0107497	(comment: Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU)
PMID:28977649	PBO:0107498	(comment: Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU)
PMID:28977649	PBO:0107495	(comment: Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA)
PMID:28977649	PBO:0107496	(comment: Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA)
PMID:28977649	PBO:0107497	(comment: Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA)
PMID:28977649	PBO:0107498	(comment: Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA)
PMID:28977649	PBO:0107507	(comment: tRNA-Ser GCU and tRNA-Ser AGA unaffected)
PMID:28977649	PBO:0107499	(comment: Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA)
PMID:28977649	PBO:0107500	(comment: Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA)
PMID:28977649	PBO:0107501	(comment: Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA)
PMID:28977649	PBO:0107502	(comment: Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA)
PMID:28977649	PBO:0107503	affects tRNA-Ser UGA/CGA; suggests tRNA-Ser UGA/CGA misfolding due to decreased dimethylation of G26, but modification not assayed directly for this tRNA
PMID:28977649	PBO:0107503	affects tRNA-Ser UGA/CGA; suggests tRNA-Ser UGA/CGA misfolding due to decreased dimethylation of G26, but modification not assayed directly for this tRNA
PMID:28977649	PBO:0107508	(comment: tRNA-Ser GCU and tRNA-Ser AGA unaffected)
PMID:28977649	PBO:0107509	(comment: tRNA-Ser GCU and tRNA-Ser AGA unaffected)
PMID:28977649	PBO:0107504	(comment: tRNA-Ser GCU and tRNA-Ser AGA unaffected)
PMID:28977649	PBO:0107505	(comment: tRNA-Ser GCU and tRNA-Ser AGA unaffected)
PMID:28977649	PBO:0107506	(comment: tRNA-Ser GCU and tRNA-Ser AGA unaffected)
PMID:28977649	PBO:0107495	(comment: Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU)
PMID:28977649	PBO:0107496	(comment: Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU)
PMID:28982178	FYPO:0000249	(comment: CHECK 40 fold less)
PMID:29021344	PBO:0095235	(Figure S5D)
PMID:29021344	FYPO:0003241	(Fig. 3C)
PMID:29021344	PBO:0095235	(Figure S5D)
PMID:29021344	FYPO:0002061	(Figure 4B)
PMID:29021344	PBO:0095234	(Figure 2E)
PMID:29021344	FYPO:0002060	(Supplemental Figure S1A).
PMID:29021344	FYPO:0005343	(Figure 2G)
PMID:29021344	FYPO:0005343	(Figure 1F)
PMID:29021344	FYPO:0002061	(Figure 4A and Supplemental Figure S4)
PMID:29021344	FYPO:0002061	(Figure 4A and Supplemental Figure S4)
PMID:29021344	FYPO:0002061	(Figure 4A and Supplemental Figure S4)
PMID:29021344	FYPO:0002061	(Figure 4A and Supplemental Figure S4)
PMID:29032152	FYPO:0001689	(Fig. 2)
PMID:29032152	GO:0005515	(Fig. 4)
PMID:29032152	PBO:0101314	(Fig. 4)
PMID:29032152	PBO:0101315	inferred from combined experiments
PMID:29032152	PBO:0101314	(Fig. 4)
PMID:29032152	PBO:0101314	(Fig. 4)
PMID:29032152	PBO:0101316	(Table 3)
PMID:29032152	PBO:0094648	(Fig. 1, 3b)
PMID:29032152	FYPO:0001926	(Fig. 2)
PMID:29032152	FYPO:0001021	(Fig. 2a)
PMID:29032152	FYPO:0000089	(Fig. 2b, c)
PMID:29032152	FYPO:0002550	(Fig. 2)
PMID:29032152	FYPO:0001234	(Fig. 1)
PMID:29032152	FYPO:0001357	(Fig. 3b)
PMID:29032152	PBO:0095685	(Fig. 3b)
PMID:29032152	PBO:0095685	(Fig. 3b)
PMID:29032152	PBO:0101316	(Table 3)
PMID:29032152	PBO:0101316	(Table 3)
PMID:29032152	FYPO:0000957	(Fig. 3e)
PMID:29032152	PBO:0095685	(Fig. 3b)
PMID:29032152	PBO:0094648	(Fig. 3b)
PMID:29032152	PBO:0101316	(Table 3)
PMID:29032152	PBO:0101317	(Table 3)
PMID:29032152	FYPO:0001689	(Fig. 3e)
PMID:29032152	FYPO:0000969	(Fig. 3e)
PMID:29079657	PBO:0097753	(Fig. 2 and supp table)
PMID:29079657	PBO:0097754	(Fig. 6)
PMID:29079657	PBO:0097753	(Fig. 2 and supp table)
PMID:29079657	PBO:0097752	(Fig. 2 and supp table)
PMID:29079657	PBO:0097753	(Fig. 2 and supp table)
PMID:29079657	PBO:0097752	(Fig. 2 and supp table)
PMID:29079657	PBO:0097753	(Fig. 2 and supp table)
PMID:29079657	PBO:0097752	(Fig. 2 and supp table)
PMID:29079657	PBO:0097753	(Fig. 2 and supp table)
PMID:29079657	PBO:0097752	(Fig. 2 and supp table)
PMID:29079657	PBO:0097753	(Fig. 2 and supp table)
PMID:29079657	PBO:0097752	(Fig. 2 and supp table)
PMID:29079657	PBO:0097753	(Fig. 2 and supp table)
PMID:29079657	PBO:0097752	(Fig. 2 and supp table)
PMID:29079657	PBO:0097753	(Fig. 2 and supp table)
PMID:29079657	PBO:0097752	(Fig. 2 and supp table)
PMID:29079657	PBO:0097753	(Fig. 2 and supp table)
PMID:29079657	PBO:0097752	(Fig. 2 and supp table)
PMID:29079657	PBO:0097753	(Fig. 2 and supp table)
PMID:29079657	PBO:0097752	(Fig. 2 and supp table)
PMID:29079657	PBO:0097753	(Fig. 2 and supp table)
PMID:29079657	PBO:0097752	(Fig. 2 and supp table)
PMID:29079657	PBO:0097753	(Fig. 2 and supp table)
PMID:29079657	PBO:0097752	(Fig. 2 and supp table)
PMID:29079657	PBO:0097753	(Fig. 2 and supp table)
PMID:29079657	PBO:0097752	(Fig. 2 and supp table)
PMID:29079657	PBO:0097753	(Fig. 2 and supp table)
PMID:29079657	PBO:0097752	(Fig. 2 and supp table)
PMID:29079657	PBO:0097753	(Fig. 2 and supp table)
PMID:29079657	PBO:0097752	(Fig. 2 and supp table)
PMID:29079657	PBO:0097753	(Fig. 2 and supp table)
PMID:29079657	PBO:0097752	(Fig. 2 and supp table)
PMID:29079657	PBO:0097753	(Fig. 2 and supp table)
PMID:29079657	PBO:0097752	(Fig. 2 and supp table)
PMID:29079657	PBO:0097753	(Fig. 2 and supp table)
PMID:29079657	GO:1900237	To conclude, upon nutrient starvation, TORC2 functions as both an activator and an inhibitor of sexual differentiation, the latter being mediated by Taf12 phosphorylation.
PMID:29079657	PBO:0097752	(Fig. 2 and supp table)
PMID:29079657	PBO:0097753	(Fig. 2 and supp table)
PMID:29079657	PBO:0097752	(Fig. 2 and supp table)
PMID:29079657	PBO:0097752	(Fig. 2 and supp table)
PMID:29079657	GO:0010515	(Fig. 1)
PMID:2908246	PBO:0099003	(Fig. 3)
PMID:2908246	PBO:0038194	mild over expression of cdc2+ on multi copy plasmid rescues the cdc13-117 ts phenotype
PMID:2908246	FYPO:0001234	mild over expression of cdc13+ on multi copy plasmid pYep13 causes slow growth
PMID:2908246	PBO:0099005	mild over expression of cdc13+ on multi copy plasmid pYep13 rescues the cdc13-117 ts phenotype. .
PMID:2908246	PBO:0099004	(Fig. 3)
PMID:29084823	PBO:0104936	(Fig. 3C)
PMID:29084823	PBO:0104952	(comment: RNA)
PMID:29084823	PBO:0099114	(Fig. 7A) shows that puc1delta shows increased mating efficiency at nitrogen levels which suppress mating in wild type cells
PMID:29084823	PBO:0104951	(Fig. 6A, 6B)
PMID:29084823	FYPO:0001147	(Fig. 3A) deletion of puc1 increases mating efficiency of zfs1 delta to WT
PMID:29084823	PBO:0093825	(Fig. 3B) varying the copy number of pJKpuc1+ leads to varying levels of sporulation efficiency in wild type cells increased puc1 mRNA causes reduced mating efficiency
PMID:29084823	PBO:0104935	(Fig. 2D, 2E, S2)
PMID:29084823	PBO:0104934	(Fig. 2B, 2C, 6A)
PMID:29084823	PBO:0104933	(Figure 1C)
PMID:29084823	PBO:0104932	(Figure 1C)
PMID:29084823	PBO:0104946	(Fig. 6A)
PMID:29084823	FYPO:0001890	"(comment: jack suggested ""up regulation of protein binding RNAs because normally bound by zfs1"" I'm using this to make the sequestering GO annotation.)"
PMID:29084823	PBO:0104945	(Fig. 6A)
PMID:29084823	PBO:0104944	(Fig. 5E)
PMID:29084823	PBO:0104943	(Fig. 5E)
PMID:29084823	PBO:0104942	(Fig. 5C, 5D)
PMID:29084823	PBO:0104942	(Fig. 5C, 5D)
PMID:29084823	PBO:0104941	(Fig. 5B)
PMID:29084823	PBO:0020460	(Fig. 4A, 4B) (comment: about 10%? of Zfs1 is phosphorylated during vegetative growth)
PMID:29084823	PBO:0104940	(Fig. 4D, S3) the hyperphosphoryated zfs1 (3rd band higest). Gad8 is required to hyperphosphorylate zfs1. In Fig4C they also show that TOR inhibition by Torin stimulates hyerphosphorylation of Zfs1
PMID:29084823	PBO:0104939	(Fig. 4A, 4B) Zfs is hyperphosphorylated in response to nitrogen depletion
PMID:29084823	PBO:0104938	(Fig. 3C, 7A) shows that zfs1delta shows high mating efficiency at nitrogen levels which suppress mating in wild type cells wild type cells
PMID:29084823	PBO:0104937	(Fig. 3C)
PMID:29084823	PBO:0104947	(Fig. 6A, 6B)
PMID:29084823	PBO:0104950	(Fig. 6A, 6B)
PMID:29084823	PBO:0104935	(Fig. 6A, 6B)
PMID:29084823	PBO:0104950	(Fig. 6A, 6B)
PMID:29084823	PBO:0104945	(Fig. 6A)
PMID:29084823	PBO:0104945	(Fig. 6A)
PMID:29084823	PBO:0104949	(Fig. 5E)
PMID:29084823	PBO:0104948	(Fig. 5E)
PMID:29084823	PBO:0093825	(Fig. 3A) deletion of cig2 does not rescue mating efficiency zfs1delta
PMID:29084823	PBO:0093825	(Fig. 3A) deletion of cig1 does not rescue mating efficiency of zfs1 delta
PMID:29084823	PBO:0104947	(Fig. 6A, 6B)
PMID:29084823	PBO:0104946	(Fig. 6A)
PMID:29084823	PBO:0104931	(Figure 1A, S1)
PMID:29084823	PBO:0093825	(Fig. 3A)
PMID:29109278	PBO:0094282	(comment: otr1R(SphI)::ura4+)
PMID:29109278	PBO:0094283	(comment: otr1R(SphI)::ura4+)
PMID:29109278	PBO:0105309	(comment: otr1R(SphI)::ura4+)
PMID:29109278	FYPO:0002827	(comment: mat3M::ura4+)
PMID:29109278	PBO:0105308	(comment: otr1R(SphI)::ura4+)
PMID:29109278	PBO:0094283	(comment: otr1R(SphI)::ura4+)
PMID:29109278	FYPO:0004742	(comment: otr1R(SphI)::ura4+)
PMID:29109278	PBO:0094679	(comment: otr1R(SphI)::ura4+)
PMID:29109278	PBO:0094679	(comment: otr1R(SphI)::ura4+)
PMID:29109278	PBO:0094679	(comment: otr1R(SphI)::ura4+)
PMID:29109278	FYPO:0003412	(comment: otr1R(SphI)::ura4+)
PMID:29109278	FYPO:0004604	(comment: tel2L::ura4+)
PMID:29123917	PBO:0102320	(comment: Later stage of meiotic prophase, observed by co-localisation with Taz1)
PMID:29123917	FYPO:0006372	S10 E and F
PMID:29123917	PBO:0102320	(comment: Later stage of meiotic prophase, observed by co-localisation with Taz1)
PMID:29123917	PBO:0102323	(Fig. 6)
PMID:29134248	GO:0070867	(comment: CHECK Fusion domain)
PMID:29134248	GO:0032220	(comment: CHECK plasma membrane fusion during conjugation)
PMID:29134248	GO:0032220	(comment: CHECK plasma membrane fusion during conjugation)
PMID:29136238	PBO:0097950	(Fig. 2)
PMID:29136238	PBO:0101106	(Fig. 1)
PMID:29136238	PBO:0107682	(Fig. 1)
PMID:29136238	PBO:0107683	(Fig. 2)
PMID:29136238	PBO:0094283	(Fig. 2)
PMID:29136238	PBO:0094681	(Fig. 2)
PMID:29136238	PBO:0094282	(Fig. 2)
PMID:29136238	FYPO:0004743	(Fig. 3)
PMID:29136238	FYPO:0006429	(Fig. 3)
PMID:29136238	FYPO:0003575	(Fig. 3)
PMID:29136238	FYPO:0006395	(Fig. 3)
PMID:29136238	PBO:0107684	and observed a preferential association of Swi6 with Y41F over Y41p peptide, suggesting that phosphorylation of H3Y41 counteracts the interaction of Swi6 with histone H3 (Supplementary Figure S6A).
PMID:29136238	PBO:0107685	and observed a preferential association of Swi6 with Y41F over Y41p peptide, suggesting that phosphorylation of H3Y41 counteracts the interaction of Swi6 with histone H3 (Supplementary Figure S6A).
PMID:29136238	PBO:0107686	and observed a preferential association of Swi6 with Y41F over Y41p peptide, suggesting that phosphorylation of H3Y41 counteracts the interaction of Swi6 with histone H3 (Supplementary Figure S6A).
PMID:29136238	PBO:0094682	(Fig. 4)
PMID:29136238	PBO:0107687	(Fig. 4)
PMID:29136238	PBO:0107688	(Fig. 4, 5)
PMID:29136238	PBO:0120494	(Fig. 4, 5)
PMID:29136238	FYPO:0000088	(Fig. 7)
PMID:29149597	PBO:0095032	The localization of Poz1, Tpz1 and Rap1 proteins are assayed.
PMID:29149597	PBO:0095032	The localization of Poz1, Tpz1 and Rap1 proteins are assayed.
PMID:29149597	PBO:0095033	The localization of Poz1, Tpz1 and Rap1 proteins are assayed.
PMID:29149597	PBO:0095034	The localization of Poz1, Tpz1 and Rap1 proteins are assayed.
PMID:29149597	PBO:0095034	The localization of Poz1, Tpz1 and Rap1 proteins are assayed.
PMID:29149597	PBO:0095033	The localization of Poz1, Tpz1 and Rap1 proteins are assayed.
PMID:29160296	PBO:0093637	(Fig. 5D)
PMID:29160296	PBO:0093636	(Fig. 5A)
PMID:29160296	PBO:0093636	(Fig. 5A)
PMID:29160296	PBO:0093636	(Fig. 5A)
PMID:29160296	PBO:0093636	(Fig. 5A)
PMID:29160296	PBO:0114404	(Fig. 4F)
PMID:29160296	PBO:0114403	(Fig. 4F)
PMID:29160296	PBO:0114403	(Fig. 4F)
PMID:29160296	PBO:0114402	(Fig. 4F)
PMID:29160296	PBO:0114402	(Fig. 4F)
PMID:29160296	PBO:0114402	(Fig. 4F)
PMID:29160296	PBO:0114402	(Fig. 4F)
PMID:29160296	PBO:0114402	(Fig. 4F)
PMID:29160296	PBO:0114402	(Fig. 4F)
PMID:29160296	PBO:0114402	(Fig. 4F)
PMID:29160296	PBO:0114401	(Fig. 3D)
PMID:29160296	PBO:0114400	(Fig. 3D)
PMID:29160296	PBO:0114399	(Fig. 3D)
PMID:29160296	PBO:0114398	(Fig. 3D)
PMID:29160296	PBO:0114398	(Fig. 3D)
PMID:29160296	PBO:0114397	(Fig. 3E)
PMID:29160296	PBO:0114397	(Fig. 3E)
PMID:29160296	PBO:0114397	(Fig. 3E)
PMID:29160296	PBO:0114397	(Fig. 3E)
PMID:29160296	PBO:0114396	(Fig. 2C)
PMID:29160296	PBO:0114396	(Fig. 2C)
PMID:29160296	PBO:0114396	(Fig. 2C)
PMID:29160296	PBO:0114396	(Fig. 2C)
PMID:29160296	PBO:0114395	(Fig. 2C)
PMID:29160296	PBO:0093637	(Fig. 5D)
PMID:29160296	PBO:0093637	(Fig. 5D)
PMID:29160296	PBO:0093637	(Fig. 5D)
PMID:29160296	PBO:0093637	(Fig. 5D)
PMID:29160296	PBO:0114409	(Fig. 5E)
PMID:29160296	PBO:0114408	(Fig. 5E)
PMID:29160296	PBO:0114408	(Fig. 5E)
PMID:29160296	PBO:0114408	(Fig. 5E)
PMID:29160296	PBO:0114408	(Fig. 5E)
PMID:29160296	PBO:0114408	(Fig. 5E)
PMID:29160296	PBO:0114408	(Fig. 5E)
PMID:29160296	PBO:0114407	(Fig. 5B)
PMID:29160296	PBO:0114407	(Fig. 5B)
PMID:29160296	PBO:0114406	(Fig. 5B)
PMID:29160296	PBO:0114405	(Fig. 5B)
PMID:29160296	PBO:0114405	(Fig. 5B)
PMID:29160296	PBO:0114405	(Fig. 5B)
PMID:29160296	PBO:0114405	(Fig. 5B)
PMID:29160296	PBO:0114405	(Fig. 5B)
PMID:29160296	PBO:0114405	(Fig. 5B)
PMID:29160296	PBO:0093634	(Fig. 5A)
PMID:29160296	PBO:0093632	(Fig. 5A)
PMID:29167352	FYPO:0002060	(Fig. 1C
PMID:29167352	PBO:0101442	~30% of the double mutant cells exhibited the monopolar spindle phenotype.
PMID:29167352	GO:1990810	(Fig. 4) Klp2 is not required, but acts collaboratively with Pkl1, in anchoring the spindle microtubule to the mitotic SPB
PMID:29167352	GO:0072686	(comment: often in a punctate manner)
PMID:29167352	FYPO:0002060	(Fig. 1C
PMID:29167352	FYPO:0001489	(comment: CONDITION 28 celcius)
PMID:29167352	FYPO:0002060	(Fig. 1C
PMID:29167352	FYPO:0002060	(Fig. 1C
PMID:29167352	FYPO:0002060	(Fig. 1C (comment: CONDITION 28 Celcius)
PMID:29167352	FYPO:0002060	(Fig. 1C
PMID:29167439	FYPO:0006507	increase with telomere shortening and time in quiescence
PMID:29167439	PBO:0102675	increase with telomere shortening and time in quiescence
PMID:29167439	PBO:0102676	limit subtelomeric DNA amplification in G0
PMID:29167439	FYPO:0006507	Require for subtelomeric DNA amplification in G0
PMID:29167439	FYPO:0006507	require for subtelomeric DNA amplification in G0
PMID:29180432	PBO:0108186	(Fig. 2G)
PMID:29180432	PBO:0108186	(Fig. 4)
PMID:29180432	PBO:0098308	(Fig. 5) (measured at 4 um spindle. WT has 6%)
PMID:29180432	FYPO:0006800	(Fig. 5B and D)
PMID:29180432	PBO:0108191	increased duration of metaphase Fig. 5E
PMID:29180432	FYPO:0002638	(Fig. 5f)
PMID:29180432	PBO:0108188	(Fig. 6)
PMID:29180432	PBO:0108185	(Fig. 2G)
PMID:29180432	PBO:0108185	(Fig. 2G)
PMID:29180432	PBO:0108192	(Figure 3)
PMID:29180432	PBO:0109271	(Fig. 3)
PMID:29180432	PBO:0108189	(Figure 3)
PMID:29180432	PBO:0108188	(Fig. 3)
PMID:29180432	PBO:0108187	(Fig. 6)
PMID:29194511	FYPO:0003241	(Figure S1A and B)
PMID:29194511	PBO:0102787	(Figure 3E-F, Supplementary Figure 8 C-D)
PMID:29194511	PBO:0102787	(Figure 3C-D, Supplementary Figure 8A-B)
PMID:29194511	FYPO:0001234	(Figure 2A, B, C)
PMID:29194511	PBO:0101834	(Figure 2E-F, supplementary Figure 5)
PMID:29194511	PBO:0102788	(Figure 2G, supplementary Figure 4)
PMID:29194511	FYPO:0003241	(Figure S1A and B)
PMID:29194511	FYPO:0003241	(Figure S1A and B)
PMID:29194511	FYPO:0003241	(Figure S1A and B)
PMID:29194511	PBO:0102789	(Fig. 1b, C)
PMID:29194511	PBO:0102790	(Fig. 1b, C, 3H)
PMID:29194511	PBO:0102791	(Fig. 1b, C, 3H)
PMID:29194511	PBO:0102792	(Fig. 1b, C)
PMID:29194511	PBO:0102793	(Fig. 1b, C)
PMID:29194511	PBO:0102794	(Fig. 1b, C)
PMID:29194511	PBO:0102795	(Fig. 1b, C)
PMID:29194511	PBO:0102793	(Fig. 1b, C)
PMID:29194511	PBO:0102796	(Fig. 1b, C)
PMID:29194511	FYPO:0003241	(Fig. 4a)
PMID:29194511	FYPO:0003241	(Fig. 4a)
PMID:29194511	FYPO:0006353	(Fig. 4b)
PMID:29194511	FYPO:0006353	(Fig. 4b)
PMID:29194511	GO:0005515	(Fig. 5)
PMID:29214404	PBO:0094683	(comment: at telomeres 1L, 1R, 2L, 2R)
PMID:29214404	PBO:0100489	(comment: greater decrease at telomeres 1R and 2L than at 1L and 2R)
PMID:29214404	FYPO:0004137	(comment: at telomere 1R)
PMID:29214404	FYPO:0000873	(comment: at telomeres 1L, 2R)
PMID:29215009	FYPO:0003589	(comment: CHECK same as either single mutant)
PMID:29215009	FYPO:0006320	(comment: upstream reporter)
PMID:29215009	FYPO:0006318	(comment: CHECK same as exo1delta alone)
PMID:29215009	FYPO:0006320	(comment: upstream reporter)
PMID:29216371	PBO:0095218	(comment: IMP evidence for part_of extension)
PMID:29216371	PBO:0095218	(comment: IMP evidence for part_of extension)
PMID:29249658	GO:0005515	(Fig. 3h)
PMID:29249658	PBO:0103099	(Fig. 3D)
PMID:29249658	PBO:0103102	(Figure 3D)
PMID:29249658	PBO:0103103	(Figure S3F)
PMID:29249658	PBO:0103103	(Figure S3F)
PMID:29249658	PBO:0103101	(Figure S3F)
PMID:29249658	PBO:0103102	(Figure S3F)
PMID:29249658	PBO:0103102	(Figure S3F)
PMID:29249658	PBO:0103101	(Figure S3F)
PMID:29249658	PBO:0103100	(Fig. 3)
PMID:29249658	PBO:0103099	(Fig. 3)
PMID:29249658	PBO:0103098	(Fig. 3D)
PMID:29249658	PBO:0103097	(Fig. S3A)
PMID:29249658	PBO:0103097	(Fig. 3c)
PMID:29249658	PBO:0103096	(Fig. 3B)
PMID:29249658	PBO:0103096	(Fig. 3A)
PMID:29249658	FYPO:0000224	(Fig. 2A)
PMID:29249658	PBO:0103095	(Figure 2)
PMID:29249658	PBO:0103094	(Figure 2)
PMID:29249658	PBO:0103093	(Figure 2)
PMID:29249658	PBO:0103092	(Fig. 2)
PMID:29249658	PBO:0103084	(Fig. 1B)
PMID:29249658	PBO:0103084	(Fig. 1B)
PMID:29249658	PBO:0103085	(Figure 1c)
PMID:29249658	PBO:0099941	(Fig. 1D, 1E) (comment: CHECK ~55%)
PMID:29249658	FYPO:0002021	(Fig. 1)
PMID:29249658	PBO:0103086	(Fig. 1)
PMID:29249658	PBO:0103087	(Fig. 1)
PMID:29249658	PBO:0103088	(comment: CHeCK phenotypes)
PMID:29249658	PBO:0103089	(Fig. 2A)
PMID:29249658	PBO:0103089	(Fig. 2A)
PMID:29249658	PBO:0103090	(Figure 2D)
PMID:29249658	PBO:0103091	(Fig. 2A)
PMID:29249658	PBO:0103091	(Fig. 2A)
PMID:29249658	PBO:0103089	(Fig. 2A)
PMID:29249658	FYPO:0000223	(Fig. 2A)
PMID:29249658	PBO:0103108	(Fig. 4F) (comment: lasso)
PMID:29249658	PBO:0103107	(Fig. 4F)
PMID:29249658	PBO:0103106	(Figure S4C)
PMID:29249658	PBO:0103106	(Figure S4C)
PMID:29249658	PBO:0103105	(Figure S4C)
PMID:29249658	PBO:0103105	(Figure S4C)
PMID:29249658	FYPO:0000118	(Fig. 4C, 4D)
PMID:29249658	FYPO:0000013	(Fig. 4C, 4D)
PMID:29249658	PBO:0103104	(Figure 3H)
PMID:29259000	FYPO:0000583	(Fig. 2) (comment: abolished asci formation)
PMID:29259000	FYPO:0000280	(Fig. 2A)
PMID:29259000	FYPO:0006313	(Fig. 2A) (comment: CHECK abolished entry into meiosis (at pre meiosis?))
PMID:29259000	FYPO:0006313	(Fig. 2A) (comment: CHECK abolished entry into meiosis (at pre meiosis?))
PMID:29259000	FYPO:0006314	(Fig. 2)
PMID:29259000	PBO:0102144	(Fig. 3D)
PMID:29259000	PBO:0102145	(Fig. 3D)
PMID:29259000	FYPO:0000485	(Figure 3F)
PMID:29259000	PBO:0102146	(Figure S3C-E)
PMID:29259000	PBO:0102147	(Figure S3C-E)
PMID:29259000	PBO:0102148	(Figure 4A and B) (comment: MI NDJ)
PMID:29259000	PBO:0102149	(Figure 4A and B) (comment: MI NDJ)
PMID:29259000	FYPO:0000485	(Figure 4)
PMID:29259000	PBO:0102150	(Fig. 5)
PMID:29259000	FYPO:0002222	(Fig. 5D)
PMID:29259000	FYPO:0006128	(Fig. S5A)
PMID:29259000	FYPO:0006316	(Fig. 5E)
PMID:29259000	PBO:0035494	(Figure 6)
PMID:29259000	PBO:0102151	(Fig. 7D, E, F)
PMID:29259000	PBO:0102152	(Fig. 5)
PMID:29290560	FYPO:0001945	(Fig. 3D)
PMID:29290560	FYPO:0000539	(Fig. 3D)
PMID:29290560	PBO:0019141	(Figure 3C)
PMID:29290560	PBO:0019141	(Figure 3C)
PMID:29290560	PBO:0019132	(Fig. 3C)
PMID:29290560	PBO:0096459	(Figure 2E)
PMID:29290560	PBO:0096458	(Fig. 2A)
PMID:29290560	FYPO:0006330	(Figure 1F) ER-PM uncoupling
PMID:29290560	PBO:0096457	(Figures 1D and S1F)
PMID:29290560	FYPO:0006330	(Figures 1D and S1F) ER-PM uncoupling (comment: *********lateral PM)
PMID:29290560	FYPO:0000537	(Fig. 3D)
PMID:29290560	PBO:0108726	(Fig. 1) ER plasma membrane tethering ER-PM contact removal OR abnormal ER-PM contact formation
PMID:29290560	GO:0140268	(Fig. 1)
PMID:29290560	FYPO:0006330	(Figures 1C and S1C) ER-PM contact removal
PMID:29292846	GO:0005635	(Fig. 4)
PMID:29292846	PBO:0104333	(Fig. 2)
PMID:29292846	PBO:0104333	(Fig. 2)
PMID:29292846	FYPO:0000655	(Fig. 3)
PMID:29292846	FYPO:0000659	(Fig. 3)
PMID:29292846	FYPO:0000655	(Fig. 3)
PMID:29292846	GO:0005635	(Fig. 4)
PMID:29292846	GO:0044732	(Fig. 4)
PMID:29292846	PBO:0104335	(Fig. 5)
PMID:29292846	PBO:0104336	(Fig. 5)
PMID:29292846	PBO:0104337	(Fig. 5)
PMID:29292846	PBO:0104339	(Fig. 5)
PMID:29292846	FYPO:0002967	(Fig. 5)
PMID:29292846	FYPO:0005612	(Fig. 5)
PMID:29292846	GO:0003690	(comment: DNA binding site: 1-60 a.a.)
PMID:29292846	PBO:0104332	(Fig. 5)
PMID:29292846	GO:0019237	Deletion of LEM domain decreases the association of Lem2 at the centromere
PMID:29292846	GO:0005515	(Fig. 1a) (comment: residues 200-307)
PMID:29292846	PBO:0104333	(Fig. 2)
PMID:29292846	PBO:0104334	(Fig. 2)
PMID:29292846	PBO:0104333	(Fig. 2)
PMID:29319508	FYPO:0000064	An increased resistance to cell lysis induced by the presence of higher concentration of 2-deoxyglucose in the vegetative growth phase of cell
PMID:29319508	FYPO:0000064	An increased resistance to cell lysis induced by the presence of higher concentration of 2-deoxyglucose in the vegetative growth phase of cell
PMID:29319508	PBO:0093822	A phenotype in which a cell lyses, i.e. the plasma membrane ruptures and cytoplasm is lost, in presence of higher concentration of 2-deoxyglucose.
PMID:29319508	FYPO:0000064	An increased resistance to cell lysis induced by the presence of higher concentration of 2-deoxyglucose in the vegetative growth phase of cell
PMID:29319508	PBO:0097995	An increased resistance to cell lysis induced by the presence of higher concentration of 2-deoxyglucose in the vegetative growth phase of life cycle of cell
PMID:29319508	FYPO:0000064	An increased resistance to cell lysis induced by the presence of higher concentration of 2-deoxyglucose in the vegetative growth phase of cell
PMID:29343550	PBO:0099724	(Figure 4)
PMID:29343550	FYPO:0002177	(Figure 2C)
PMID:29343550	FYPO:0004737	(Figure 4A)
PMID:29343550	PBO:0106492	(Figure 3A)
PMID:29343550	PBO:0099724	(Figure 4C)
PMID:29343550	PBO:0106949	(Figure 4E-F)
PMID:29343550	FYPO:0004741	(Figure 4A)
PMID:29343550	FYPO:0004740	(Figure 4A)
PMID:29343550	FYPO:0003339	(Figure 5)
PMID:29343550	FYPO:0005020	(Figure 5)
PMID:29343550	FYPO:0003339	(Figure 5)
PMID:29343550	FYPO:0001365	(Figure 5)
PMID:29343550	FYPO:0004741	(Figure 4A)
PMID:29343550	PBO:0106951	(Figure 1A-B)
PMID:29343550	PBO:0106952	(Figure 1C)
PMID:29343550	FYPO:0002060	(Figure 2C)
PMID:29343550	PBO:0106492	(Figure 3A)
PMID:29343550	PBO:0106948	(Figure 4E)
PMID:29352077	FYPO:0002060	(Figure 4)
PMID:29352077	FYPO:0002060	(Figure 3)
PMID:29352077	FYPO:0001513	(Figure 3)
PMID:29352077	FYPO:0002060	(Figure 4)
PMID:29352077	FYPO:0001513	(Figure 3)
PMID:29352077	FYPO:0001513	(Figure 3)
PMID:29352077	FYPO:0001513	(Figure 3)
PMID:29352077	FYPO:0002060	(Figure 3)
PMID:29352077	FYPO:0001513	(Figure 3)
PMID:29352077	FYPO:0002060	(Figure 4)
PMID:29352077	FYPO:0002060	(Figure 4)
PMID:29352077	FYPO:0002060	(Figure 3)
PMID:29352077	FYPO:0001513	(Figure 3)
PMID:29352077	FYPO:0001513	(Figure 3)
PMID:29352077	FYPO:0002060	(Figure 4)
PMID:29352077	FYPO:0002060	(Figure 4)
PMID:29352077	FYPO:0002060	(Figure 4)
PMID:29352077	PBO:0107889	(Figure 4F)
PMID:29352077	FYPO:0002060	(Figure 3)
PMID:29352077	FYPO:0002060	(Figure 2)
PMID:29352077	FYPO:0001513	(Figure 2)
PMID:29352077	FYPO:0002060	(Figure 3)
PMID:29352077	FYPO:0002060	(Figure 3)
PMID:29352077	FYPO:0002060	(Figure 3)
PMID:29414789	PBO:0097330	(comment: Northern blot and primer extension analysis)
PMID:29414789	GO:0140256	(comment: CHECK GONEW: negative regulation of cellular response to phosphate starvation)
PMID:29414789	FYPO:0002243	(Fig. 8c)
PMID:29414789	PBO:0101897	(comment: Primer extension analysis)
PMID:29414789	PBO:0101897	(comment: Primer extension analysis)
PMID:29414789	PBO:0101897	(comment: Primer extension analysis)
PMID:29414789	PBO:0097322	(comment: Northern blot and primer extension analysis)
PMID:29414789	PBO:0096175	(comment: Northern blot and primer extension analysis)
PMID:29414789	PBO:0096175	(comment: Northern blot and primer extension analysis)
PMID:29414789	PBO:0101896	(comment: Primer extension analysis)
PMID:29414789	PBO:0097322	(comment: Northern blot and primer extension analysis)
PMID:29414789	PBO:0096175	(comment: Primer extension analysis)
PMID:29414789	PBO:0094613	(comment: Primer extension analysis)
PMID:29414789	PBO:0101896	(comment: Primer Extension Analysis)
PMID:29414789	PBO:0096175	(comment: Primer extension analysis)
PMID:29414789	PBO:0094613	(comment: Primer extension analysis)
PMID:29422501	PBO:0101702	(Fig. 3a)
PMID:29422501	PBO:0101688	(Fig. 2)
PMID:29422501	PBO:0101688	(Fig. 1a)
PMID:29422501	PBO:0101695	(Fig. 1c)
PMID:29422501	PBO:0101696	(Fig. 1c)
PMID:29422501	PBO:0101696	(Fig. 1c)
PMID:29422501	PBO:0101688	(Fig. 2)
PMID:29422501	PBO:0101694	(Fig. 1c)
PMID:29422501	PBO:0101688	(Fig. 2)
PMID:29422503	FYPO:0003106	(Figure 1a)
PMID:29422503	PBO:0095753	Lsm3 binding was detected at ars2004, non-ARS, ade6+ and his1+ loci. In ter1∆ cells, Lsm3 binding to those non-telmeric sites were increased.
PMID:29422503	PBO:0095772	(Supplementary Fig. 4)
PMID:29422503	PBO:0095747	(Fig. 5)
PMID:29422503	GO:1904868	(Fig. 1-3)
PMID:29422503	PBO:0095772	Supplementary Fig. 4
PMID:29422503	PBO:0095773	Supplementary Fig. 4
PMID:29422503	PBO:0095772	Supplementary Fig. 4
PMID:29422503	GO:1904868	(Fig. 1-3)
PMID:29422503	PBO:0095768	(Fig. 3b)
PMID:29422503	PBO:0095768	(Fig. 3a)
PMID:29422503	PBO:0095767	(Fig. 1E)
PMID:29422503	PBO:0095767	(Fig. 1E)
PMID:29422503	PBO:0095767	(Fig. 1C,D)
PMID:29422503	PBO:0095766	(Fig. 1C,D)
PMID:29422503	PBO:0095765	(Fig. 1C,D)
PMID:29422503	PBO:0095764	(Fig. 1C,D)
PMID:29422503	GO:0140445	(Fig. 1e)
PMID:29422503	GO:0007004	(Fig. 1)
PMID:29422503	PBO:0095737	Trt1 binding is reduced to ~80% of pof8+ cells, but not as severely reduced as pof8∆ cells (~35%).
PMID:29422503	PBO:0095737	Trt1 binding is reduced to ~70% of pof8+ cells, but not as severely reduced as pof8∆ cells (~35%).
PMID:29422503	PBO:0095737	Trt1 binding is reduced to ~58% of pof8+ cells, but not as severely reduced as pof8∆ cells (~35%).
PMID:29422503	PBO:0095759	(Fig. 6b)
PMID:29422503	PBO:0095748	(Fig. 6)
PMID:29422503	PBO:0095759	(Fig. 6)
PMID:29422503	FYPO:0003106	(Fig. 6) pof8-∆[289-402] cells show as short telomere as pof8∆ cells.
PMID:29422503	FYPO:0003106	(Fig. 6) pof8-∆[390-402] cells show as short telomere as pof8∆ cells.
PMID:29422503	FYPO:0003106	(Fig. 6) pof8-R343A cells show as short telomere as pof8∆ cells.
PMID:29422503	FYPO:0003106	(Fig. 6) pof8-Y330A cells show as short telomere as pof8∆ cells.
PMID:29422503	PBO:0095758	Trt1 binding is reduced to ~69% of pof8+ cells, but not as severely reduced as pof8∆ cells (~35%).
PMID:29422503	PBO:0095757	(Fig. 5)
PMID:29422503	FYPO:0002687	(Fig. 5)
PMID:29422503	PBO:0095756	(Fig. 5)
PMID:29422503	FYPO:0002239	(Fig. 5)
PMID:29422503	PBO:0095755	(Fig. 4e)
PMID:29422503	PBO:0095754	(Fig. 4d)
PMID:29422503	PBO:0095751	Lsm3 protein level was not affected by est1∆.
PMID:29422503	PBO:0095750	(Fig. 4f) Lsm3 binding to telomeres was not affected by est1∆.
PMID:29422503	PBO:0095751	Lsm3 protein level was not affected by trt1∆.
PMID:29422503	PBO:0095750	(Fig. 4f) Lsm3 binding to telomeres was not affected by trt1∆.
PMID:29422503	PBO:0095751	Lsm3 protein level was not affected by ter1∆.
PMID:29422503	PBO:0095752	(Fig. 4f) Lsm3 binding at telomeres is increased by ter1∆.
PMID:29422503	PBO:0095751	Lsm3 protein level was not affected by pof8∆.
PMID:29422503	PBO:0095750	(Fig. 4f)
PMID:29422503	PBO:0095749	(Fig. 4c) Lsm3-TER1 interaction is abolished in pof8∆ cells.
PMID:29422503	PBO:0095748	(Fig. 4a) Expression level of telomerase RNA TER1 is reduced but not eliminated in pof8∆ cells. Expression level for telomerase RNA pre-cursor was not affected by pof8∆.
PMID:29422503	PBO:0095747	Trt1-TER1 interaction is reduced but not eliminated in pof8-∆[289-4020]. Extent of reduction in Trt1-TER1 is similar to pof8∆ cells.
PMID:29422503	PBO:0095746	(Fig. 3a) Pof8-TER1 interaction is not affected by est1∆.
PMID:29422503	PBO:0095745	(Fig. 3a) Pof8-TER1 interaction is reduced but not eliminated in trt1∆ cells.
PMID:29422503	PBO:0095745	(Fig. 3a) Pof8-TER1 interaction is reduced but not eliminated in ccq1∆.
PMID:29422503	PBO:0095744	Pof8 expression was not affected by est1∆.
PMID:29422503	PBO:0095743	(Fig. 1e) Localization of Pof8 at telomeres is reduced but not eliminated in est1∆.
PMID:29422503	PBO:0095744	Pof8 expression level is not affected by trt1∆.
PMID:29422503	PBO:0095743	(Fig. 1e) Localization of Pof8 at telomeres is reduced but not eliminated in trt1∆.
PMID:29422503	PBO:0095744	Pof8 expression level is not affected in ccq1∆.
PMID:29422503	PBO:0095743	(Fig. 1e) Localization of Pof8 at telomeres is reduced but not eliminated in ccq1∆.
PMID:29422503	PBO:0095744	Pof8 expression level was not altered in ter1∆ cells.
PMID:29422503	PBO:0095743	(Fig. 1e) Localization of Pof8 at telomeres is reduced but not eliminated in ter1∆.
PMID:29422503	PBO:0095740	Est1 expression level detected by western in ter1∆ cells was similar to Est1 level in ter1+ (wild-type) cells.
PMID:29422503	PBO:0095739	Est1 binding to telomeres is reduced to near no binding in ter1∆, based on ChIP assay.
PMID:29422503	PBO:0095742	(Fig. 3b)
PMID:29422503	PBO:0095741	(Fig. 3c) Interaction between Est1 and TER1 was not affected by pof8∆.
PMID:29422503	PBO:0095740	Est1 showed similar expression level in pof8∆ cells as wild-type cells.
PMID:29422503	PBO:0095739	Telomere binding of Est1 is reduced in pof8∆ cells.
PMID:29422503	PBO:0095738	moderately reduced less severe thanin ter1∆ cells.
PMID:29422503	PBO:0095738	Trt1 expression level detected by western blot is reduced in ter1∆ cells.
PMID:29422503	PBO:0095737	Based on ChIP, ter1∆ cause loss of telomerase (Trt1) localization at telomeres.
PMID:29422503	PBO:0095736	(Fig. 1C,D)
PMID:29422503	FYPO:0003106	pof8∆ rif1∆ cells showed short telomeres, very similar to pof8∆ cells.
PMID:29422503	PBO:0095735	pof8∆ poz1∆ cells showed very slightly shortend telomeres, rather than highly elongated telomeres in poz1∆ cells. (This strain showed longer telomere than pof8∆ cells.)
PMID:29422503	PBO:0095735	pof8∆ rap1∆ cells showed shortened telomeres, more similar to pof8∆, rather than highly elongated telomeres in rap1∆ cells.
PMID:29422503	PBO:0093634	pof8∆ taz1∆ showed much shorter telomere length (almost like wild-type cells) than taz1∆ cells, but showed some rearrangement in sub-telomeres.
PMID:29422503	FYPO:0003106	(Figure 1a) Telomere shortening is similar to pof8∆ cells.
PMID:29422503	FYPO:0003107	(Fig. 1) Lose telomere signal, much like trt1∆ cells.
PMID:29424342	PBO:0102649	(Fig. 6)
PMID:29424342	PBO:0099879	(Fig. 4B)
PMID:29424342	PBO:0102644	(Fig. 4)
PMID:29424342	PBO:0102645	(Fig. 4)
PMID:29424342	PBO:0102646	(Fig. 4)
PMID:29424342	PBO:0102647	(Fig. 4)
PMID:29424342	PBO:0102648	(Fig. 4)
PMID:29424342	PBO:0102642	(Fig. 5)
PMID:29424342	PBO:0102643	(Fig. 5)
PMID:29424342	PBO:0102643	(Fig. 5)
PMID:29424342	PBO:0102642	(Fig. 5)
PMID:29424342	PBO:0102651	(Fig. 6)
PMID:29424342	PBO:0102650	(Fig. 6)
PMID:29424342	GO:0006406	(Fig. 2)
PMID:29432178	PBO:0100856	(Fig. 3A)
PMID:29432178	FYPO:0006474	Ribosome profiling and matching RNA-seq in gcn2Δ cells treated or untreated with 3-AT revealed that the majority of the translationally induced genes did not respond to amino acid starvation (Fig. 2B)
PMID:29432178	FYPO:0006444	the expression of most genes induced by amino acid starvation in wild-type cells was not up-regulated, confirming that Gcn2 is the major mediator of this response
PMID:29432178	FYPO:0001234	(comment: CHECK Can we say somewhere - overexpresses genes involved by amino acid starvation, or something similar?)
PMID:29432178	PBO:0100857	(Fig. 3B) (comment: CHECK during normal growth)
PMID:29432178	FYPO:0006473	(Fig. 3E)
PMID:29432178	FYPO:0001357	(Fig. 3A)
PMID:29432178	PBO:0100854	(Fig. 3A)
PMID:29453312	PBO:0096695	In the absence of efc25 Ras1 is not activated at the cell cortex
PMID:29453312	PBO:0096701	In the absence of gap1 Ras activity increases and decorates the entire cortex of vegetative growing cells
PMID:29453312	PBO:0096697	In the absence of efc25 Ras1 is not activated at the cell cortex
PMID:29453312	GO:1902917	Ras activity increases during the mating process and is maximum at the fusion site just before the fusion event.
PMID:29453312	GO:1990819	Active Ras1 co-localizes with the actin fusion focus during the process of cell-cell fusion
PMID:29453312	PBO:0096692	ras1 mutant cells undergo precocious fusion resulting in cell lysis
PMID:29453312	PBO:0096693	ras1 mutant cells undergo precocious fusion resulting in cell lysis
PMID:29453312	PBO:0096694	Active Ras1 is localized to cell poles during mitotic growth
PMID:29453312	PBO:0092569	Ative Ras1 localizes to septa during mitotic growth
PMID:29453312	GO:1990819	Ste6 co-localizes with the actin fusion focus during the process of cell-cell fusion
PMID:29453312	PBO:0096694	Active Ras1 is localized to cell poles during mitotic growth
PMID:29453312	PBO:0092569	Active Ras1 is localized to cell poles during mitotic growth
PMID:29458562	FYPO:0004085	(Fig. 2)
PMID:29458562	FYPO:0002060	(Fig. 2)
PMID:29458562	PBO:0096251	(Fig. 3) (comment: CHECK abolished)
PMID:29458562	FYPO:0000562	(Fig. 2) (comment: likey due to intron encoded maturase)
PMID:29458562	PBO:0096256	(Fig. 4)
PMID:29458562	PBO:0096257	(Fig. 4)
PMID:29458562	PBO:0096258	(Fig. 4)
PMID:29458562	PBO:0096255	(Fig. 4)
PMID:29458562	PBO:0096254	(Fig. 3)
PMID:29458562	PBO:0096250	(Fig. 4)
PMID:29458562	PBO:0096253	(Fig. 3)
PMID:29458562	PBO:0096252	(Fig. 3)
PMID:29458562	FYPO:0004153	DNS
PMID:29458562	FYPO:0000245	(Fig. 2)
PMID:29458562	FYPO:0004085	(Fig. 2)
PMID:29514920	PBO:0107823	(Fig. 1A)
PMID:29514920	PBO:0101337	(Fig. 3A, 3B S2, A and B) IN TRANSIENT BURSTS & progressive increase in the number of Wee1 nodes as a function of cell size, ... 20X in Wee1 nodes in large cells versus small cells (Fig. 4 B).
PMID:29514920	PBO:0107816	fig 3D
PMID:29514920	PBO:0102684	Fig. S2, F and G
PMID:29514920	PBO:0023824	(Figure 2D) (commment: Epistatic to cdr2delta)
PMID:29514920	PBO:0107817	(Fig. 2C) (comment: protein localizes to cytoplasm, nucleus, and spindle-pole body)
PMID:29514920	PBO:0110564	(Fig. 1A)
PMID:29514920	PBO:0110565	(Fig. 1A)
PMID:29514920	PBO:0107821	(Fig. 1A)
PMID:29514920	PBO:0107822	(Fig. 1A)
PMID:29514920	PBO:0107822	(Fig. 1A)
PMID:29514920	PBO:0107431	(Fig. 1B)
PMID:29514920	PBO:0107823	(Fig. 1C)
PMID:29514920	PBO:0107824	(Fig. 2B)
PMID:29514920	PBO:0107824	(Fig. 2B)
PMID:29514920	PBO:0107825	(Fig. 2B)
PMID:29514920	PBO:0107825	(Fig. 2B)
PMID:29514920	PBO:0023824	(Fig. 2D) (comment: Epistatic to cdr2delta)
PMID:29529046	PBO:0102038	(Fig. 5A,B) In this paper we used a high affinity zinc-responsive FRET sensor (ZapCY1) to measure zinc ion availability in the cytosol under conditions of zinc deficiency. Thus, in addition to accumulating high levels of total cellular zinc - this manuscript shows that loz1D cells also accumulate higher levels of zinc in the cytosol. This accumulation is also dependent upon Zrt1 as this phenotype is not observed in a loz1 zrt1 double mutant
PMID:29529046	GO:0120127	A key finding of our work is that Zhf1 does NOT transport zinc out of the cytosol under conditions of zinc ion starvation
PMID:29529046	PBO:0111437	Zhf1 is required for the rapid transport of zinc ions out of the cytosol during a zinc shock (a condition where there is a rapid influx of zinc into a cell)
PMID:29529046	PBO:0102046	(Fig. 8)
PMID:29529046	PBO:0102047	(Fig. 8)
PMID:29529046	PBO:0102048	(Fig. 8)
PMID:29529046	PBO:0102049	(Fig. 8)
PMID:29529046	PBO:0102050	(Fig. 8)
PMID:29529046	PBO:0102051	(Fig. 8)
PMID:29529046	PBO:0102051	(Fig. 8)
PMID:29529046	PBO:0093559	(Figure 1) ((comment: CHECK EDTA, zinc chelator)
PMID:29529046	GO:0006882	Zrg17 also transports zinc out of the cytosol when zinc is available (as well as when it is limiting)
PMID:29529046	PBO:0102043	The reporter genes used were the ZapCY1 high affinity and ZapCY2 low affinity zinc-responsive FRET reporter. As this reporter is located in the cytosol and nucleus it measures zinc availability in these compartments (so the Term name should really be increased cytoplasm (not cellular) zinc level)
PMID:29529046	PBO:0102039	The reporter gene was the the ZapCY1 high affinity zinc-responsive FRET reporter. As this reporter is located in the cytosol and nucleus it measures zinc availability in these compartments (so the Term name should really be increased cytoplasm (not cellular) zinc level)
PMID:29529046	PBO:0102039	The reporter gene was the the ZapCY1 high affinity zinc-responsive FRET reporter. As this reporter is located in the cytosol and nucleus it measures zinc availability in these compartments (so the Term name should really be increased cytoplasm (not cellular) zinc level)
PMID:29529046	PBO:0102042	The reporter gene was the the ZapCY1 high affinity zinc-responsive FRET reporter. As this reporter is located in the cytosol and nucleus it measures zinc availability in these compartments (so the Term name should really be increased cytoplasm (not cellular) zinc level)
PMID:29529046	PBO:0102041	"We made the term ""zinc ion import into organelle""in GO becuse it fits better witht the descendants"
PMID:29529046	PBO:0102039	(Fig. 6)
PMID:29529046	PBO:0093561	(Figure 1) ((comment: CHECK EDTA, zinc chelator)
PMID:29529046	PBO:0102045	(Fig. 8)
PMID:29529046	PBO:0102040	"We made the term ""zinc ion import into organelle""in GO becuse it fits better witht the descendants"
PMID:29529046	FYPO:0001534	The experiment performed was to measure total cellular zinc ion levels in a zrt1D strain during a zinc shock (Figure 4A)
PMID:29529046	PBO:0102039	The reporter gene was the the ZapCY1 high affinity zinc-responsive FRET reporter. As this reporter is located in the cytosol and nucleus it measures zinc availability in these compartments (so the Term name should really be increased cytoplasm (not cellular) zinc level)
PMID:29529046	PBO:0102044	(Fig. 4B,E)
PMID:29549126	PBO:0106479	(comment: assayed using heme analog ZnMP)
PMID:29549126	FYPO:0007397	(comment: assayed using heme analog ZnMP)
PMID:29549126	PBO:0106478	(comment: assayed using heme analog ZnMP)
PMID:29549126	GO:0020037	(Fig. 6)
PMID:29549126	GO:0020037	(Fig. 6)
PMID:29549126	GO:1904334	(Fig. 3B, C) We therefore concluded that Shu1 is required for hemin acquisition when hemin is present at very low concentrations (0.075 ΔM), whereas its presence is dispensable under conditions of high hemin concentrations
PMID:29549126	GO:0140420	(Fig. 3B, C)
PMID:29549126	GO:0016020	(Fig. 7)
PMID:29549126	GO:0016020	(Fig. 7)
PMID:29596413	PBO:0095599	(Fig. 7)
PMID:29596413	PBO:0095606	(Fig. 7C) (comment: CHECK supression of trm7-delta)
PMID:29596413	PBO:0095608	(Fig. 7C) (comment: CHECK supression of trm7-delta)
PMID:29596413	PBO:0095607	(Fig. 7C)
PMID:29596413	PBO:0095608	(Fig. 7C) (comment: CHECK supression of trm7-delta)
PMID:29596413	PBO:0095606	(Fig. 7C) (comment: CHECK supression of trm7-delta)
PMID:29596413	PBO:0095605	(Fig. 7C)
PMID:29596413	PBO:0095604	(Fig. 7C)
PMID:29596413	PBO:0095603	(Fig. 7C)
PMID:29596413	PBO:0095602	(Fig. 7)
PMID:29596413	PBO:0095601	(Fig. 7)
PMID:29596413	PBO:0095600	(Fig. 7)
PMID:29596413	PBO:0095610	(Fig. 7C) (comment: CHECK supression of trm7-delta)
PMID:29596413	PBO:0095609	(Fig. 7C) (comment: CHECK supression of trm7-delta)
PMID:29610759	PBO:0105325	(Fig. 1)
PMID:29610759	PBO:0105327	(Fig. 5)
PMID:29610759	FYPO:0005353	(comment: at MPS1)
PMID:29610759	PBO:0105326	(Fig. 1)
PMID:29610759	PBO:0098985	(Fig 1, 4)
PMID:29610759	PBO:0098985	enriched at mat1 right border and cenH left border; fig 1
PMID:29610759	PBO:0105324	(Fig. 2)
PMID:29610759	PBO:0098985	(Fig. 1, 4)
PMID:29618061	PBO:0110989	as expected, northern blot analysis revealed no obvious additive effect compared to the ncproΔ single mutant (Figure 2E).
PMID:29618061	PBO:0110992	H3K14ac levels were also increased in this strain (Figure 2D), similar to that seen in clr3Δ (Figure 1E)
PMID:29618061	PBO:0110994	We found that, in the absence of non-coding transcription in a strain lacking the prt promoter (ncproΔ) (5), Clr3 recruitment to pho1 was reduced (Figure 2C).
PMID:29618061	PBO:0110993	Remarkably, this mutant showed an additive accumulation of pho1 mRNA levels (Figure 2A) and displayed a slow growth phenotype considerably more severe than either of the single mutants, clr3Δ or clr4Δ (Figure 2B).
PMID:29618061	PBO:0110993	Remarkably, this mutant showed an additive accumulation of pho1 mRNA levels (Figure 2A) and displayed a slow growth phenotype considerably more severe than either of the single mutants, clr3Δ or clr4Δ (Figure 2B).
PMID:29618061	PBO:0096776	No detectable increase in either tgp1 or nc-tgp1 was observed in sir2Δ, strains harbouring a clr6 mutation (Supplementary Figure S3A, lanes 6-8)
PMID:29618061	PBO:0096778	No detectable increase in either tgp1 or nc-tgp1 was observed in sir2Δ, strains harbouring a clr6 mutation (Supplementary Figure S3A, lanes 6-8)
PMID:29618061	PBO:0096776	No detectable increase in either tgp1 or nc-tgp1 was observed in sir2Δ, strains harbouring a clr6 mutation (Supplementary Figure S3A, lanes 6-8)
PMID:29618061	PBO:0096776	Unlike at pho1, we found that deletion of clr3 has no discernible induction effect on tgp1
PMID:29618061	PBO:0096777	Co-incident with Seb1 loss, tgp1 mRNA levels start to accrue (Supplementary Figure S3A, lane 13)
PMID:29618061	PBO:0096777	We found accumulation of tgp1 in the seb1-1 mutant compared to wild-type (Supplementary Figure S3A, compare lanes 1 and 2).
PMID:29618061	PBO:0110996	To test whether Clr3 recruitment depends on Set1 we performed ChIP-qPCR. In support of Set1 acting upstream of Clr3 we found the HDAC’s recruitment to the pho1 locus to be compromised in a set1Δ strain (Figure 3E).
PMID:29618061	PBO:0110989	. Interestingly, deletion of the H3K4 methyltransferase Set1 leads to derepression of pho1 (Figure 3C). In contrast, deletion of the H3K36 methyltransferase Set2 only had a minor effect on pho1 derepression, suggesting that the mechanism underlying pho1 silencing primarily relies on histone methylation by Set1
PMID:29618061	PBO:0110999	However, mug14 is not affected in this exosome mutant, suggesting that the gene is likely to be regulated only at the transcriptional level (Figure 5a).
PMID:29618061	PBO:0110995	In the case of prt-3Δ, this phenotype is likely a result of lost Mmi1 recruitment since this mutant lacks the DSR motifs we previously mapped ((5,37), Figure 3A, Mmi1 CRAC). We tested Mmi1 recruitment to the prt locus in this mutant and it is indeed defective (data not shown).
PMID:29618061	PBO:0110989	To directly assess whether this is the case and that the two proteins function as part of the same pathway we performed a Northern blot to compare a double mutant clr3Δset1Δ with the respective single mutants (Figure 3D). We found that the double mutant did not lead to higher pho1 derepression as compared to single set1Δ, indicating that both proteins do indeed function in the same pathway.
PMID:29618061	PBO:0110989	Of the TSA-sensitive HDACs, Clr3 was the only one that had an effect on pho1 expression, with its deletion resulting in increased pho1 mRNA levels (Figure 1B).
PMID:29618061	PBO:0110958	No change in pho1 expression could be detected for either prt-4Δ or prt-5Δ (Figure 3B, lanes 5 and 6).
PMID:29618061	PBO:0110958	No change in pho1 expression could be detected for either prt-4Δ or prt-5Δ (Figure 3B, lanes 5 and 6).
PMID:29618061	PBO:0096778	No detectable increase in either tgp1 or nc-tgp1 was observed in sir2Δ, strains harbouring a clr6 mutation (Supplementary Figure S3A, lanes 6-8)
PMID:29618061	PBO:0096776	clr4Δ, or the double mutant clr3Δclr4Δ (Supplementary Figure S3A, lane 4 and 5), also revealed no change in mRNA expression levels. These results indicate that unlike pho1, tgp1 repression
PMID:29618061	PBO:0096778	clr4Δ, or the double mutant clr3Δclr4Δ (Supplementary Figure S3A, lane 4 and 5), also revealed no change in mRNA expression levels. These results indicate that unlike pho1, tgp1 repression
PMID:29618061	PBO:0096776	clr4Δ, or the double mutant clr3Δclr4Δ (Supplementary Figure S3A, lane 4 and 5), also revealed no change in mRNA expression levels. These results indicate that unlike pho1, tgp1 repression
PMID:29618061	PBO:0096778	clr4Δ, or the double mutant clr3Δclr4Δ (Supplementary Figure S3A, lane 4 and 5), also revealed no change in mRNA expression levels. These results indicate that unlike pho1, tgp1 repression
PMID:29618061	PBO:0110997	In agreement with a previously demonstrated role for the nuclear exosome complex in the degradation of meiotic transcripts during mitosis, we observe increased levels of meu19 and meu31 in rrp6Δ (Figure 5B and C).
PMID:29618061	PBO:0110998	In agreement with a previously demonstrated role for the nuclear exosome complex in the degradation of meiotic transcripts during mitosis, we observe increased levels of meu19 and meu31 in rrp6Δ (Figure 5B and C).
PMID:29618061	PBO:0108864	Interestingly, elevated pho1 levels were observed in prt-1Δ, prt-2Δ, and prt-3Δ (Figure 3B, lanes 1- 4) suggesting that element(s) responsible for pho1 silencing are located within the 5′ part of prt.
PMID:29618061	PBO:0110989	Northern blot (Supplementary Figure S1A). Compared to wild-type pho1 mRNA levels, a slight accumulation was detected for all strains. However, this is less pronounced than in clr3Δ, indicating that Clr3 is unlikely to entirely depend on Clr2 or other components of SHREC for recruitment to pho1.
PMID:29618061	PBO:0110991	(Figure 1D). We found that loss of Clr3 leads to increased Pol II levels upstream of the pho1 promoter and particularly across the gene body.
PMID:29618061	PBO:0110958	In contrast, deletion of TSA- insensitive sir2, which contributes to transcriptional silencing at constitutive heterochromatin, had no effect on pho1 expression (Figure 1B, lane 5).
PMID:29618061	PBO:0110990	This revealed that Clr3 indeed localizes to the gene, particularly at the non-coding region (Figure 1C).
PMID:29618061	PBO:0110989	Northern blot (Supplementary Figure S1A). Compared to wild-type pho1 mRNA levels, a slight accumulation was detected for all strains. However, this is less pronounced than in clr3Δ, indicating that Clr3 is unlikely to entirely depend on Clr2 or other components of SHREC for recruitment to pho1.
PMID:29618061	PBO:0110989	Northern blot (Supplementary Figure S1A). Compared to wild-type pho1 mRNA levels, a slight accumulation was detected for all strains. However, this is less pronounced than in clr3Δ, indicating that Clr3 is unlikely to entirely depend on Clr2 or other components of SHREC for recruitment to pho1.
PMID:29618061	PBO:0110992	an increase in the levels of H3K14ac could be detected by ChIP-qPCR (Figure 1E)
PMID:29618061	PBO:0110993	Remarkably, this mutant showed an additive accumulation of pho1 mRNA levels (Figure 2A) and displayed a slow growth phenotype considerably more severe than either of the single mutants, clr3Δ or clr4Δ (Figure 2B).
PMID:29618061	PBO:0108864	Interestingly, elevated pho1 levels were observed in prt-1Δ, prt-2Δ, and prt-3Δ (Figure 3B, lanes 1- 4) suggesting that element(s) responsible for pho1 silencing are located within the 5′ part of prt.
PMID:29618061	PBO:0108864	Interestingly, elevated pho1 levels were observed in prt-1Δ, prt-2Δ, and prt-3Δ (Figure 3B, lanes 1- 4) suggesting that element(s) responsible for pho1 silencing are located within the 5′ part of prt.
PMID:29632066	PBO:0104930	(Fig. S1B)
PMID:29632066	PBO:0104930	(Fig. S1B)
PMID:29632066	PBO:0104930	(Fig. S1B)
PMID:29641590	GO:0000480	(comment: A0 cleavage)
PMID:29641590	GO:0000447	(comment: A2 cleavage)
PMID:29641590	GO:0000472	(comment: A1 cleavage)
PMID:29641590	FYPO:0007064	(Fig. 3)
PMID:29641590	FYPO:0007065	(Fig. 3)
PMID:29641590	FYPO:0007063	(Fig. 3)
PMID:29641590	FYPO:0001135	(Fig. 3)
PMID:29689193	FYPO:0006746	(Figure 2F)
PMID:29689193	GO:1903338	(comment: Promotes cell wall thickness hoemostasis)
PMID:29689193	GO:1903338	(comment: Promotes cell wall thickness hoemostasis)
PMID:29689193	GO:1903338	(comment: Promotes cell wall thickness hoemostasis)
PMID:29689193	FYPO:0006745	(comment: thicker and thinner, disrupted homeostasis)
PMID:29689193	FYPO:0006745	(comment: thicker and thinner, disrupted homeostasis)
PMID:29689193	FYPO:0006745	(comment: thicker and thinner, disrupted homeostasis)
PMID:29689193	FYPO:0003889	(Fig. 3C)
PMID:29689193	FYPO:0001035	(Figure 3B)
PMID:29689193	FYPO:0001035	(Figure 3B)
PMID:29735656	FYPO:0002060	(Fig. 4b)
PMID:29735656	FYPO:0002061	(Figure 2 AB) (comment: inactive separase, uncleavable kleisin)
PMID:29735656	FYPO:0002060	(Figure 2 AB) (comment: inactive separase, uncleavable kleisin)
PMID:29735656	FYPO:0002061	(Figure 2 AB) inactive separase, uncleavable kleisin
PMID:29735656	FYPO:0002060	(Figure 1A Supp S1A)
PMID:29735656	FYPO:0002060	(Figure 1A)
PMID:29735656	FYPO:0002060	(Figure 1A)
PMID:29735656	FYPO:0002060	(Figure 1A)
PMID:29735656	FYPO:0000268	(Figure 4d)
PMID:29735656	PBO:0098320	(Fig. 4e)
PMID:29735656	PBO:0098320	(Figure 3c)
PMID:29735656	FYPO:0000085	Supp. S4
PMID:29735656	FYPO:0000088	Supp. S4
PMID:29735656	FYPO:0002060	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	(Figure 1A)
PMID:29735656	FYPO:0002060	(Figure 1A)
PMID:29735656	FYPO:0002060	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	(Figure 1A Supp S1A)
PMID:29735656	FYPO:0002060	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	(Figure 1A)
PMID:29735656	FYPO:0002060	(Figure 1A)
PMID:29735656	FYPO:0002060	(Figure 1A)
PMID:29735656	FYPO:0002060	(Figure 1A)
PMID:29735656	FYPO:0002060	(Figure 1A)
PMID:29735656	FYPO:0002060	(Figure 1A)
PMID:29735656	FYPO:0002060	(Figure 2 AB) (comment: inactive separase, uncleavable kleisin)
PMID:29735656	FYPO:0002060	(Fig. 4b)
PMID:29735656	FYPO:0002060	(Fig. 4b)
PMID:29735745	FYPO:0004099	(Fig. S2D)
PMID:29735745	FYPO:0004099	(Fig. S2D)
PMID:29735745	PBO:0105516	(Fig. 7D)
PMID:29735745	PBO:0105514	(Fig. 7C)
PMID:29735745	FYPO:0001357	(Fig. 7B)
PMID:29735745	PBO:0096226	(Fig. 7B)
PMID:29735745	PBO:0105516	(Fig. 7C)
PMID:29735745	PBO:0105516	(Fig. 7C)
PMID:29735745	FYPO:0001357	(Fig. 7B)
PMID:29735745	FYPO:0002151	(Fig. 7B)
PMID:29735745	FYPO:0001234	(Fig. 7B)
PMID:29735745	FYPO:0002061	(Fig. 6B)
PMID:29735745	FYPO:0004099	(Fig. 6D)
PMID:29735745	FYPO:0001420	(Fig. 6B, 6C)
PMID:29735745	FYPO:0001420	(Fig. 6B, 6C)
PMID:29735745	FYPO:0001420	(Fig. 6B, 6C)
PMID:29735745	FYPO:0001420	(Fig. 6B, 6C)
PMID:29735745	FYPO:0001420	(Fig. 6B, 6C)
PMID:29735745	PBO:0105521	(Fig. 3D)
PMID:29735745	PBO:0105522	(Fig. 3D)
PMID:29735745	PBO:0105522	(Fig. 3D)
PMID:29735745	PBO:0105523	(Fig. 3D)
PMID:29735745	FYPO:0001420	(Fig. 6B, 6C)
PMID:29735745	FYPO:0001420	(Fig. 6B, 6C)
PMID:29735745	FYPO:0001420	(Fig. 6B, 6C)
PMID:29735745	PBO:0105523	(Fig. 3D)
PMID:29735745	PBO:0105524	(Fig. 3D)
PMID:29735745	PBO:0105524	(Fig. 3D)
PMID:29735745	PBO:0105525	(Fig. 3D)
PMID:29735745	PBO:0105525	(Fig. 3D)
PMID:29735745	PBO:0105526	(Fig. 3D)
PMID:29735745	PBO:0105526	(Fig. 3D)
PMID:29735745	PBO:0105527	(Fig. 3D)
PMID:29735745	FYPO:0001234	(Fig. 6B, 6C)
PMID:29735745	FYPO:0001234	(Fig. 6B, 6C)
PMID:29735745	PBO:0105516	(Fig. 5C)
PMID:29735745	PBO:0105516	(Fig. 5C)
PMID:29735745	PBO:0093732	(Fig. 5B)
PMID:29735745	PBO:0093732	(Fig. 5B)
PMID:29735745	PBO:0093733	(Fig. 5B)
PMID:29735745	PBO:0105355	(Fig. 5A)
PMID:29735745	PBO:0105515	(Fig. 5A)
PMID:29735745	PBO:0105354	(Fig. 5A)
PMID:29735745	PBO:0105514	(Fig. 5A, 5C)
PMID:29735745	PBO:0105513	(Fig. 3D)
PMID:29735745	PBO:0105512	(Fig. 3D)
PMID:29735745	PBO:0105511	(Fig. 3D)
PMID:29735745	PBO:0105510	(Fig. 3D)
PMID:29735745	PBO:0105509	(Fig. 3D)
PMID:29735745	PBO:0105508	(Fig. 3D)
PMID:29735745	PBO:0105507	(Fig. 3D)
PMID:29735745	PBO:0105506	(Fig. 3D)
PMID:29735745	PBO:0105505	(Fig. 3D)
PMID:29735745	PBO:0105504	(Fig. 3D)
PMID:29735745	PBO:0105503	(Fig. 3D)
PMID:29735745	PBO:0105502	(Fig. 3D)
PMID:29735745	PBO:0105501	(Fig. 2D)
PMID:29735745	FYPO:0002061	(Fig. 2D)
PMID:29735745	FYPO:0001357	(Fig. 2D)
PMID:29735745	PBO:0105500	(Fig. 2D)
PMID:29735745	FYPO:0004481	(Fig. 1C)
PMID:29735745	PBO:0033591	(Fig. 1E)
PMID:29735745	FYPO:0000159	(Fig. 1D)
PMID:29735745	PBO:0101242	(Fig. 1E)
PMID:29735745	PBO:0032915	(Fig. 1E)
PMID:29735745	FYPO:0004481	(Fig. 1C)
PMID:29735745	FYPO:0004481	(Fig. 1C)
PMID:29735745	FYPO:0000214	(Fig. 1D)
PMID:29735745	FYPO:0004099	(Fig. S2D)
PMID:29735745	FYPO:0004099	(Fig. S2D)
PMID:29735745	FYPO:0004099	(Fig. 7D)
PMID:29735745	FYPO:0001420	(Fig. 5G)
PMID:29735745	FYPO:0001420	(Fig. 5G)
PMID:29735745	PBO:0105518	(Fig. 3D)
PMID:29735745	PBO:0105518	(Fig. 3D)
PMID:29735745	PBO:0105527	(Fig. 3D)
PMID:29735745	FYPO:0001513	(Fig. 2B)
PMID:29735745	FYPO:0001357	(Fig. 2B)
PMID:29735745	FYPO:0002061	(Fig. 2D)
PMID:29735745	PBO:0105528	(comment: binds to the consensus sequence CCCCAY) (Fig. 4)
PMID:29735745	PBO:0105528	(comment: binds to the consensus sequence CCCCAY) (Fig. 4)
PMID:29735745	PBO:0105519	(Fig. 3D)
PMID:29735745	PBO:0105519	(Fig. 3D)
PMID:29735745	PBO:0105520	(Fig. 3D)
PMID:29735745	PBO:0105520	(Fig. 3D)
PMID:29735745	PBO:0105521	(Fig. 3D)
PMID:29735745	PBO:0105517	(Fig. 5A, 5B, 5C; Fig. 7C)
PMID:29735745	PBO:0105517	(Fig. 5A, 5B, 5C; Fig. 7C)
PMID:29735745	GO:0000977	(comment: binds to the consensus sequence CCCCAY) (Fig. 4)
PMID:29735745	GO:0000977	(comment: binds to the consensus sequence CCCCAY) (Fig. 4)
PMID:29735745	PBO:0018530	Video S2
PMID:29735745	PBO:0018530	Video S2
PMID:29735745	PBO:0018677	(Fig. 2C)
PMID:29735745	PBO:0018677	(Fig. 2C)
PMID:29735745	FYPO:0000214	(Fig. 5H)
PMID:29735745	FYPO:0004099	(Fig. S2D)
PMID:29735745	FYPO:0004099	(Fig. S2D)
PMID:29735745	FYPO:0004099	(Fig. S2D)
PMID:29735745	FYPO:0004099	(Fig. S2D)
PMID:29735745	FYPO:0004099	(Fig. S2D)
PMID:29742018	PBO:0106088	(comment: normal with and without spindle checkpoint activation)
PMID:29742018	PBO:0106091	(comment: CHECK in vitro)
PMID:29742018	PBO:0106092	(comment: normal with and without spindle checkpoint activation)
PMID:29742018	PBO:0106103	(comment: CHECK in vitro)
PMID:29742018	PBO:0106102	(comment: CHECK in vitro)
PMID:29742018	PBO:0106094	(comment: CHECK in vitro)
PMID:29742018	PBO:0106095	(comment: CHECK in vitro)
PMID:29742018	PBO:0106102	(comment: CHECK in vitro)
PMID:29742018	PBO:0106102	(comment: CHECK in vitro)
PMID:29742018	PBO:0106099	Hhp1 accumulates at SPB when spindle checkpoint activated
PMID:29742018	PBO:0106096	(comment: CHECK in vitro)
PMID:29769606	PBO:0112463	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	PBO:0112463	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	FYPO:0003182	Consistently, sister chromatid non-disjunction at meiosis II was signifcantly increased in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. S3D).
PMID:29769606	PBO:0112465	Te recombinant proteins of fssion yeast H2A (SpHta1) were also purifed. An in vitro kinase assay using these recombinant proteins showed that the H2A-K119D and the H2A-K119E mutants, as well as the H2A-S121A mutant, were not signifcantly phosphorylated by Bub1, whereas H2A-K119R mutant proteins were phosphorylated by Bub1 (Fig. 4B).
PMID:29769606	PBO:0112465	Te recombinant proteins of fssion yeast H2A (SpHta1) were also purifed. An in vitro kinase assay using these recombinant proteins showed that the H2A-K119D and the H2A-K119E mutants, as well as the H2A-S121A mutant, were not signifcantly phosphorylated by Bub1, whereas H2A-K119R mutant proteins were phosphorylated by Bub1 (Fig. 4B).
PMID:29769606	PBO:0112465	Te recombinant proteins of fssion yeast H2A (SpHta1) were also purifed. An in vitro kinase assay using these recombinant proteins showed that the H2A-K119D and the H2A-K119E mutants, as well as the H2A-S121A mutant, were not signifcantly phosphorylated by Bub1, whereas H2A-K119R mutant proteins were phosphorylated by Bub1 (Fig. 4B).
PMID:29769606	FYPO:0003182	Consistently, sister chromatid non-disjunction at meiosis II was signifcantly increased in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. S3D).
PMID:29769606	PBO:0112464	Te recombinant proteins of fssion yeast H2A (SpHta1) were also purifed. An in vitro kinase assay using these recombinant proteins showed that the H2A-K119D and the H2A-K119E mutants, as well as the H2A-S121A mutant, were not signifcantly phosphorylated by Bub1, whereas H2A-K119R mutant proteins were phosphorylated by Bub1 (Fig. 4B).
PMID:29769606	PBO:0112465	Te recombinant proteins of fssion yeast H2A (SpHta1) were also purifed. An in vitro kinase assay using these recombinant proteins showed that the H2A-K119D and the H2A-K119E mutants, as well as the H2A-S121A mutant, were not signifcantly phosphorylated by Bub1, whereas H2A-K119R mutant proteins were phosphorylated by Bub1 (Fig. 4B).
PMID:29769606	FYPO:0000091	We found that malonyl-mimetic K119D and K119E mutants showed sensitivity to a microtubule depolymerizing agent (TBZ) in the same way the H2A-S121A mutant had (Fig. S3B)
PMID:29769606	FYPO:0000091	We found that malonyl-mimetic K119D and K119E mutants showed sensitivity to a microtubule depolymerizing agent (TBZ) in the same way the H2A-S121A mutant had (Fig. S3B)
PMID:29769606	FYPO:0000091	We found that malonyl-mimetic K119D and K119E mutants showed sensitivity to a microtubule depolymerizing agent (TBZ) in the same way the H2A-S121A mutant had (Fig. S3B)
PMID:29769606	FYPO:0000091	We found that malonyl-mimetic K119D and K119E mutants showed sensitivity to a microtubule depolymerizing agent (TBZ) in the same way the H2A-S121A mutant had (Fig. S3B)
PMID:29769606	FYPO:0003182	Consistently, sister chromatid non-disjunction at meiosis II was signifcantly increased in the K119D and K119E mutants
PMID:29769606	PBO:0112466	An acetyl-mimetic H2A-K119Q mutation slightly inhibited Bub1-mediated H2A phosphorylation (Fig. 4B)
PMID:29769606	PBO:0112466	An acetyl-mimetic H2A-K119Q mutation slightly inhibited Bub1-mediated H2A phosphorylation (Fig. 4B)
PMID:29769606	PBO:0112465	Te recombinant proteins of fssion yeast H2A (SpHta1) were also purifed. An in vitro kinase assay using these recombinant proteins showed that the H2A-K119D and the H2A-K119E mutants, as well as the H2A-S121A mutant, were not signifcantly phosphorylated by Bub1, whereas H2A-K119R mutant proteins were phosphorylated by Bub1 (Fig. 4B).
PMID:29769606	PBO:0112465	Te recombinant proteins of fssion yeast H2A (SpHta1) were also purifed. An in vitro kinase assay using these recombinant proteins showed that the H2A-K119D and the H2A-K119E mutants, as well as the H2A-S121A mutant, were not signifcantly phosphorylated by Bub1, whereas H2A-K119R mutant proteins were phosphorylated by Bub1 (Fig. 4B).
PMID:29769606	PBO:0112463	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	PBO:0112463	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	PBO:0096739	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	PBO:0096739	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	PBO:0096739	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	PBO:0096739	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	PBO:0112463	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	PBO:0112463	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	PBO:0096739	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	PBO:0096739	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	FYPO:0005633	Consistently, sister chromatid non-disjunction at meiosis II was signifcantly increased in the K119D and K119E mutants
PMID:29769606	FYPO:0003182	Consistently, sister chromatid non-disjunction at meiosis II was signifcantly increased in the K119D and K119E mutants
PMID:29769606	FYPO:0003182	Consistently, sister chromatid non-disjunction at meiosis II was signifcantly increased in the K119D and K119E mutants
PMID:29774234	PBO:0093557	(comment: CHECK slightly better growth than stn1-226 alone)
PMID:29774234	PBO:0093557	(comment: CHECK same as stn1-226 alone)
PMID:29774234	PBO:0097405	(comment: Exacerbated at high temperature)
PMID:29774234	FYPO:0000266	(comment: CHECK Sensitive to HU, CPT and MMS)
PMID:29774234	FYPO:0000122	loss of telomeric and subtelomeric sequences at high temperature
PMID:29804820	FYPO:0001355	(Figure 4D)
PMID:29804820	PBO:0108723	However, the interaction is significantly diminished when either L32 (Mis16D1-32), or both L32 (Mis16D1-32) and L32/W33 (Mis16D1-33), are deleted (Figures 6A and 6B). In contrast, the Mis16-H4a1 interaction was only mildly affected in the context of the Mis16D1-33 truncation. These findings strongly suggest that Mis16 L32 and W33 participate in specific interactions with Eic1 but not histone H4. To verify these observations in vivo, we performed
PMID:29804820	PBO:0108722	However, the interaction is significantly diminished when either L32 (Mis16D1-32), or both L32 (Mis16D1-32) and L32/W33 (Mis16D1-33), are deleted (Figures 6A and 6B). In contrast, the Mis16-H4a1 interaction was only mildly affected in the context of the Mis16D1-33 truncation. These findings strongly suggest that Mis16 L32 and W33 participate in specific interactions with Eic1 but not histone H4. To verify these observations in vivo, we performed
PMID:29804820	PBO:0108721	However, the interaction is significantly diminished when either L32 (Mis16D1-32), or both L32 (Mis16D1-32) and L32/W33 (Mis16D1-33), are deleted (Figures 6A and 6B). In contrast, the Mis16-H4a1 interaction was only mildly affected in the context of the Mis16D1-33 truncation. These findings strongly suggest that Mis16 L32 and W33 participate in specific interactions with Eic1 but not histone H4. To verify these observations in vivo, we performed
PMID:29804820	PBO:0108720	However, the interaction is significantly diminished when either L32 (Mis16D1-32), or both L32 (Mis16D1-32) and L32/W33 (Mis16D1-33), are deleted (Figures 6A and 6B). In contrast, the Mis16-H4a1 interaction was only mildly affected in the context of the Mis16D1-33 truncation. These findings strongly suggest that Mis16 L32 and W33 participate in specific interactions with Eic1 but not histone H4. To verify these observations in vivo, we performed
PMID:29804820	PBO:0108720	However, the interaction is significantly diminished when either L32 (Mis16D1-32), or both L32 (Mis16D1-32) and L32/W33 (Mis16D1-33), are deleted (Figures 6A and 6B). In contrast, the Mis16-H4a1 interaction was only mildly affected in the context of the Mis16D1-33 truncation. These findings strongly suggest that Mis16 L32 and W33 participate in specific interactions with Eic1 but not histone H4. To verify these observations in vivo, we performed
PMID:29804820	PBO:0108719	(Figures 6A, 6B).
PMID:29804820	GO:0005515	A Homodimer of the Mis18 C-Terminal Domain Interacts with a Mis16-Eic1 Heterodimer
PMID:29804820	GO:0098654	The Stoichiometry of the S. pombe Mis18 Holo-Complex Is (Mis16)2:(Eic1)2:(Mis18)4 T
PMID:29804820	GO:0098654	The Stoichiometry of the S. pombe Mis18 Holo-Complex Is (Mis16)2:(Eic1)2:(Mis18)4 T
PMID:29804820	GO:0098654	The Stoichiometry of the S. pombe Mis18 Holo-Complex Is (Mis16)2:(Eic1)2:(Mis18)4 T
PMID:29813053	FYPO:0006831	(Fig. S3E) The timing of septation onset depends on the AR function. The start of septation is delayed when the function of the AR F-BAR protein Cdc15 is compromised.
PMID:29813053	FYPO:0006831	(Fig. S3D) The timing of septation onset depends on the AR function. The start of septation is delayed when the function of the AR unconventional type II myosin Myp2 is compromised.
PMID:29813053	FYPO:0006832	(Fig. 4E and F) Inactivation of Cdc2 kinase in early mitosis induces a very premature septation onset. ATP-analogue sensitive cdc2-asM17 mutant cells carrying Cdc13-GFP were G2-arrested by growth in the presence of 1 μM1-NP-PP1 for 3.5 h at 32C. Then, the cells were G2-released by transfer to a fresh medium and imaged to detect the entry into mitosis. Cdc2 was inactivated during early mitosis transferring the cells to a fresh medium containing either DMSO or 10 μM1-NP-PP1.
PMID:29813053	FYPO:0006832	(Fig. 2) The start of septation scales with anaphase B progression and correlates linearly with the cell length.
PMID:29813053	FYPO:0006832	(Fig. 2) The start of septation scales with anaphase B progression and cell size in fission yeast and correlates linearly with the cell length.
PMID:29813053	FYPO:0006831	(Fig. 5B) Septation start is delayed when the function of Sid2 is compromised. Cells were grown in YES at 25C shifted to 28C for 4 h and imaged as in Fig 1. The data are developed in Table 1 and Table 3.
PMID:29813053	FYPO:0006833	(Fig. 5E) Timely activation of septum synthesis does not depend on SIN asymmetry. Defective SIN-Inhibitory Phosphatase (SIP) complex csc2Δ cells were examined. The data of cells of C, D and E are developed in S2 Table.
PMID:29813053	FYPO:0006831	(Fig. 6) The levels of Etd1 and Rho1 regulate the timing of septation start. (A) The timing of septum deposition onset correlates with the start of increase of Etd1 in the cell middle. Cells were grown inMMwithout thiamine (GFP-etd1+ induced) at 25ÊC for 24 h and imaged as in Fig 1. (B) The increase of Etd1 in the cell middle and concomitant initiation of septation are delayed in long cells. Cells were analyzed as in A after 3.5 h of cell cycle arrest at 36ÊC. Graphs to the right show the total fluorescence of GFP-Etd1 at the cell poles and middle in the series to the left. A.U., arbitrary units. Arrow, cortical localization of Etd1 in the cell middle. Dashed outlines indicate the ROIs used to measure the total fluorescence of GFP-Etd1 in the corresponding regions of the cell. (C) The timing of septation onset is dependent on the level of etd1+. Cells expressing endogenous etd1+ and 41X-GFP-etd1+ grown at 32ÊC for 24 h either in the absence (ON, high etd1+ level; n = 4, 34 cells) or in the presence of thiamine (OFF, wild-type etd1+ level; n = 2, 11 cells), and cells expressing etd1Δ 81X-etd1+ grown for 15 h with thiamine (OFF, very low etd1+ level; n = 3, 23 cells), just before the emergence of SIN phenotype were analyzed as in A.
PMID:29813053	FYPO:0006832	(Fig. 6) The levels of Etd1 and Rho1 regulate the timing of septation start. (A) The timing of septum deposition onset correlates with the start of increase of Etd1 in the cell middle. Cells were grown inMMwithout thiamine (GFP-etd1+ induced) at 25ÊC for 24 h and imaged as in Fig 1. (B) The increase of Etd1 in the cell middle and concomitant initiation of septation are delayed in long cells. Cells were analyzed as in A after 3.5 h of cell cycle arrest at 36ÊC. Graphs to the right show the total fluorescence of GFP-Etd1 at the cell poles and middle in the series to the left. A.U., arbitrary units. Arrow, cortical localization of Etd1 in the cell middle. Dashed outlines indicate the ROIs used to measure the total fluorescence of GFP-Etd1 in the corresponding regions of the cell. (C) The timing of septation onset is dependent on the level of etd1+. Cells expressing endogenous etd1+ and 41X-GFP-etd1+ grown at 32ÊC for 24 h either in the absence (ON, high etd1+ level; n = 4, 34 cells) or in the presence of thiamine (OFF, wild-type etd1+ level; n = 2, 11 cells), and cells expressing etd1Δ 81X-etd1+ grown for 15 h with thiamine (OFF, very low etd1+ level; n = 3, 23 cells), just before the emergence of SIN phenotype were analyzed as in A.
PMID:29813053	FYPO:0006832	(Fig. 6) The levels of Etd1 and Rho1 regulate the timing of septation start. (F) The start of septum deposition is dependent on the level of rho1+. Cells expressing endogenous rho1+ and 3Xrho1+ grown at 32ÊC for 16 h either without (ON, high rho1+ level; n = 2, 14 cells) or with thiamine (OFF, wild-type rho1+ level; n = 2, 16 cells) were analyzed.
PMID:29813053	FYPO:0006832	(Fig. 7) The spindle and the proximity of the nucleus to the division site are required for proper septum synthesis activation in fission yeast. (A) Scheme of the steps required to prevent nuclear separation and to maintain or separate the undivided nucleus from the cell middle and/or from the division site. (A-1 and C) Nucleus and division site are maintained in the cell middle; cells were treated for 90 min and imaged with methyl 2-benzimidazolecarbamate (or carbendazim, MBC, 50 μg ml-1) to avoid spindle assembly and nuclear separation. (A-2 and D) Nucleus and division site are relocated to a cell end; cells were treated for 45 min, centrifuged to displace the nucleus, treated 45 more min and visualized with MBC. (A-3 and E) The nucleus is relocated and separated from the division plane; cells were treated for 90 min, centrifuged and examined with MBC. (B) mad2Δ cells were grown and imaged without MBC as in Fig 1. The mad2Δ cells were used to avoid a delay caused by the activation of the spindle assembly checkpoint. (C-E) The premature and uncoupled septation start caused by the absence of the spindle depends on the position of the nucleus. mad2Δ cells were processed as in A to prevent nuclear separation and to maintain or separate the undivided nucleus from the cell middle and/or the division site. (C) The nucleus and division site are maintained in the cell middle. (F) The nucleus and division site are relocated to a cell end. (E) The nucleus is relocated and separated from the division plane. MBC-treated cells were imaged as in B. Anaphase A onset was considered as time zero. Graphs to the right are as in Fig 4. Dashed lines and arrowheads: green, anaphase A onset; dark blue, septum synthesis start; light blue, septum ingression onset. White arrowhead: first CW-stained septum synthesis detection. White arrow: first CW-staining increase showing septum ingression. A.U., arbitrary units. (F) Uncoupled septum synthesis and ingression timing with MBC is restored to wild-type levels when the undivided nucleus is separated from the division site. Table showing the time between anaphase A (green) and septum synthesis start (dark blue) or septum ingression onset (light blue) in the indicated cells. Parenthesis: n, number of experiments and cells; T, delay in septum synthesis and ingression start with respect to control cells with MBC as in C.
PMID:29813053	FYPO:0000639	(Fig. 7) The spindle and the proximity of the nucleus to the division site are required for proper septum synthesis activation in fission yeast. (A) Scheme of the steps required to prevent nuclear separation and to maintain or separate the undivided nucleus from the cell middle and/or from the division site. (A-1 and C) Nucleus and division site are maintained in the cell middle; cells were treated for 90 min and imaged with methyl 2-benzimidazolecarbamate (or carbendazim, MBC, 50 μg ml-1) to avoid spindle assembly and nuclear separation. (A-2 and D) Nucleus and division site are relocated to a cell end; cells were treated for 45 min, centrifuged to displace the nucleus, treated 45 more min and visualized with MBC. (A-3 and E) The nucleus is relocated and separated from the division plane; cells were treated for 90 min, centrifuged and examined with MBC. (B) mad2Δ cells were grown and imaged without MBC as in Fig 1. The mad2Δ cells were used to avoid a delay caused by the activation of the spindle assembly checkpoint. (C-E) The premature and uncoupled septation start caused by the absence of the spindle depends on the position of the nucleus. mad2Δ cells were processed as in A to prevent nuclear separation and to maintain or separate the undivided nucleus from the cell middle and/or the division site. (C) The nucleus and division site are maintained in the cell middle. (F) The nucleus and division site are relocated to a cell end. (E) The nucleus is relocated and separated from the division plane. MBC-treated cells were imaged as in B. Anaphase A onset was considered as time zero. Graphs to the right are as in Fig 4. Dashed lines and arrowheads: green, anaphase A onset; dark blue, septum synthesis start; light blue septum ingression onset. White arrowhead: first CW-stained septum synthesis detection. White arrow: first CW-staining increase showing septum ingression. A.U., arbitrary units. (F) Uncoupled septum synthesis and ingression timing with MBC is restored to wild-type levels when the undivided nucleus is separated from the division site. Table showing the time between anaphase A (green) and septum synthesis start (dark blue) or septum ingression onset (light blue) in the indicated cells. Parenthesis: n, number of experiments and cells; T, delay in septum synthesis and ingression start with respect to control cells with MBC as in C.
PMID:29813053	FYPO:0006831	S5 Fig. The establishment of SIN asymmetry and the timely activation of septum synthesis do not depend on each other. (A, B) Early log-phase wild-type and thermosensitive cps1-191 (Bgs1) mutant cells were grown in YES at 25ÊC, shifted to 28ÊC for 1 h (A) or 32ÊC for 30 min (B) to produce a gradual delay in the onset of septum synthesis of cps1-191 mutant, and imaged as in Fig 5C. Anaphase B onset is considered as time zero (T = 0). White arrow: first CWstained detection of septum synthesis. Arrowheads: green, anaphase B onset; blue, septum deposition start (time immediately before septum detection with CW); red, complete asymmetry of SIN Cdc7, being Cdc7-GFP completely lost from one SPB. The data of this figure are developed in S2 Table. (C) The timing of septation onset is not related to the asymmetry of SIN. Early log-phase wild-type cells were grown in YES at 25ÊC, 28ÊC or 32ÊC, imaged as in Fig 5C and the timings of SIN asymmetry and of septation onset were determined with respect to the anaphase B onset (see also the data in S2 Table).
PMID:29813053	FYPO:0006834	(Fig. 3)
PMID:29813053	FYPO:0003201	(Fig. 3)
PMID:29813053	GO:1905757	(Fig. 4D, E)
PMID:29813053	GO:1905758	(Fig. 5B, Table 1) (comment: also inferred from localization timing)
PMID:29813053	GO:1905758	(Fig. 5,6A-D) (comment: also inferred from localization timing)
PMID:29813053	GO:1905758	(Fig. 56E) (comment: also inferred from localization timing)
PMID:29813053	FYPO:0006831	(Fig. 2) The start of septation scales with anaphase B progression and cell size in fission yeast. and correlates linearly with the cell length.
PMID:29813053	FYPO:0006831	(Fig. 2) The start of septation scales with anaphase B progression and cell size in fission yeast and correlates linearly with the cell length.
PMID:29844133	PBO:0094265	(comment: Beware using aged colonies, cell size recovery observed.)
PMID:29844133	FYPO:0001407	(comment: beware using old strains, phenotypic changes observed.)
PMID:29851556	GO:0035861	(comment: CHECK in the presence or absence of Nbs1)
PMID:29851556	PBO:0100532	(comment: localization of mutated protein assayed)
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	GO:0007535	In summary, our observations suggest that the factors, Clr4, Sir2, Swd1 and Clr3 probably work in the same pathway as Swi6, but Brl2, Pof3, Cbp1 and Swi2 have an effect on donor selection through Swi6-dependent and -independent mechanisms.
PMID:29852001	GO:0007535	In summary, our observations suggest that the factors, Clr4, Sir2, Swd1 and Clr3 probably work in the same pathway as Swi6, but Brl2, Pof3, Cbp1 and Swi2 have an effect on donor selection through Swi6-dependent and -independent mechanisms.
PMID:29852001	GO:0007535	In summary, our observations suggest that the factors, Clr4, Sir2, Swd1 and Clr3 probably work in the same pathway as Swi6, but Brl2, Pof3, Cbp1 and Swi2 have an effect on donor selection through Swi6-dependent and -independent mechanisms.
PMID:29852001	GO:0007535	In summary, our observations suggest that the factors, Clr4, Sir2, Swd1 and Clr3 probably work in the same pathway as Swi6, but Brl2, Pof3, Cbp1 and Swi2 have an effect on donor selection through Swi6-dependent and -independent mechanisms.
PMID:29852001	FYPO:0003659	(Fig. 3)
PMID:29852001	FYPO:0003659	(Fig. 3)
PMID:29852001	FYPO:0003659	(Fig. 3)
PMID:29852001	FYPO:0003659	(Fig. 3)
PMID:29852001	FYPO:0003659	(Fig. 3)
PMID:29852001	FYPO:0003659	(Fig. 3)
PMID:29852001	FYPO:0003659	(Fig. 3)
PMID:29852001	FYPO:0003659	(Fig. 3)
PMID:29852001	FYPO:0003659	(Fig. 3)
PMID:29852001	FYPO:0003659	(Fig. 3)
PMID:29852001	FYPO:0003659	(Fig. 3)
PMID:29852001	FYPO:0003659	(Fig. 3)
PMID:29852001	FYPO:0003659	(Fig. 3)
PMID:29852001	FYPO:0003659	(Fig. 3)
PMID:29852001	FYPO:0003659	(Fig. 3)
PMID:29852001	FYPO:0003659	(Fig. 3)
PMID:29852001	PBO:0113773	(Fig. 3)
PMID:29852001	PBO:0113772	(Fig. 3)
PMID:29852001	PBO:0113772	(Fig. 3)
PMID:29852001	PBO:0113772	(Fig. 3)
PMID:29852001	PBO:0112930	(Fig. 3)
PMID:29852001	PBO:0112930	(Fig. 3)
PMID:29852001	PBO:0112930	(Fig. 3)
PMID:29852001	PBO:0112930	(Fig. 3)
PMID:29852001	PBO:0112930	(Fig. 3)
PMID:29852001	PBO:0112930	(Fig. 3)
PMID:29852001	PBO:0112930	(Fig. 3)
PMID:29852001	PBO:0112930	(Fig. 3)
PMID:29852001	PBO:0112930	(Fig. 3)
PMID:29852001	PBO:0112930	(Fig. 3)
PMID:29852001	PBO:0112930	(Fig. 3)
PMID:29852001	PBO:0112930	(Fig. 3)
PMID:29852001	PBO:0112930	(Fig. 3)
PMID:29852001	PBO:0112930	(Fig. 3)
PMID:29852001	PBO:0112930	(Fig. 3)
PMID:29852001	PBO:0112930	(Fig. 3)
PMID:29852001	PBO:0112930	(Fig. 3)
PMID:29852001	PBO:0112930	(Fig. 3)
PMID:29852001	PBO:0112930	(Fig. 3)
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S3
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29852001	FYPO:0000470	Table S2
PMID:29866182	PBO:0098372	(comment: Myc-Ago1)
PMID:29866182	PBO:0098372	(comment: Myc-Ago1)
PMID:29866182	PBO:0098371	(comment: FLAG-Ago1)
PMID:29866182	PBO:0098375	(comment: FLAG-Ago1, Arb1-Myc)
PMID:29866182	PBO:0098375	(comment: FLAG-Ago1, Arb1-Myc)
PMID:29866182	PBO:0098376	(comment: Tas3-Myc)
PMID:29866182	PBO:0098371	(comment: FLAG-Ago1)
PMID:29898918	PBO:0111500	(comment: CHECK present in cycling cells and meiosis I cells. Required for cellular resistance to MMS and CPT.)
PMID:29898918	PBO:0093617	(comment: CHECK slightly worse than srs2delta alone)
PMID:29898918	FYPO:0000085	(comment: CHECK Epistatic genetic interaction, same as mus81delta alone)
PMID:29898918	PBO:0093559	(comment: CHECK Epistatic genetic interaction, same as eme1delta alone)
PMID:29898918	PBO:0093617	(comment: CHECK slightly worse than srs2delta alone)
PMID:29898918	PBO:0093559	(comment: CHECK Epistatic genetic interaction,same as mus81delta alone)
PMID:29898918	FYPO:0000085	(comment: CHECK Epistatic genetic interaction, same as mus81delta alone)
PMID:29898918	PBO:0093617	(comment: CHECK Epistatic genetic interaction, same as eme1delta alone)
PMID:29898918	PBO:0093617	(comment: CHECK Epistatic genetic interaction, same as mus81delta alone)
PMID:29898918	MOD:00085	(comment: CHECK Required for cellular resistance to MMS and CPT)
PMID:29898918	PBO:0111499	(comment: CHECK present in cycling cells and meiosis I cells. Required for cellular resistance to MMS and CPT.)
PMID:29899453	PBO:0107365	(Fig. 6a, b)
PMID:29899453	FYPO:0005260	(Figure 3d, Extended fig 8d) (comment: (vw: some suppression?))
PMID:29899453	PBO:0107366	extended data Figure 9 decreased RNA pol2 localization to chromatin (occurs at termination sites)
PMID:29899453	GO:1904595	Extended data Figure 9
PMID:29899453	FYPO:0006613	Extended Data Fig 3a, Fig. 2c, Extended Data Fig. 3b-d)
PMID:29899453	FYPO:0006614	(Figure 3e) Also increased termination index Fig. 4e
PMID:29899453	FYPO:0002061	(Figure 3e)
PMID:29899453	PBO:0107367	(Fig. 1d)
PMID:29899453	PBO:0107368	(Fig. 1d)
PMID:29899453	PBO:0107368	(Fig. 1d)
PMID:29899453	PBO:0107358	(Fig. 5c)
PMID:29899453	PBO:0107369	Extended Data Fig 10
PMID:29899453	PBO:0107369	Extended Data Fig 10
PMID:29899453	PBO:0107369	Extended Data Fig 10
PMID:29899453	PBO:0107358	Extended Data Fig 5a (comment: vw: based on EXP and comment changed allele from psf2 to cdk9 (P.P. Core CPF recruitment to chromatin is unaffected by Cdk9 inhibition). pfs2 pla1 cft1)
PMID:29899453	PBO:0093559	(Fig. 3e)
PMID:29899453	PBO:0099591	(Fig. 1c)
PMID:29899453	FYPO:0000080	(Fig. 3e)
PMID:29899453	PBO:0107350	(Fig. 1b)
PMID:29899453	PBO:0107356	Extended Data Fig 5a (comment: vw: fixed allele and target)
PMID:29899453	PBO:0107355	Extended Data Fig 4d (comment: (vw: fixed allele))
PMID:29899453	PBO:0107355	Extended Data Fig 4d (comment: Added Dis2 extension)
PMID:29899453	PBO:0107355	Extended Data Fig 4a Cdk9 inhibition increased chromatin recruitment of Dis2
PMID:29899453	PBO:0107354	Extended Data Fig 6e Cdk9 does not restrict chromatin recruitment of Sds21.
PMID:29899453	PBO:0092258	(Fig. 1B) vw: corrected back to dis2 not cdk9!
PMID:29899453	PBO:0107349	(Fig. 1b)
PMID:29899453	PBO:0107353	Extended Data Fig 6a,b ChIP-qPCR analysis at the rps17a+ gene. Comparison of pSpt5:Spt5 ratio in the indicated strains upstream and downstream of the CPS at 30 °C (left) and comparison of the ratio between dis2+ and dis2-11 cells at 18 °C (right). Extended Data Fig 6a,b
PMID:29899453	PBO:0107353	Extended Data Fig 5d .
PMID:29899453	PBO:0107352	Extended Data Fig 2f .(comment: CHECK (cdk9as, cdk9as ssu72C13S, ssu72C13S))
PMID:29899453	PBO:0107351	(comment: vw: I changed the allele to the multi gene genotype to reflect the comment.) Extended Data Fig 2c Fcp1 inactivation stabilizes Rpb1 Ser2 phosphorylation after Lsk1 inhibition. Fission-yeast strains, lsk1as or lsk1as fcp1-452, were grown at 30 °C and shifted to 37 °C (or not shifted), treated for the indicated time with 20 μM 3-MB-PP1, and analysed by immunoblotting for Pol II Ser2 phosphorylation
PMID:29899453	PBO:0099591	(Fig. 1b)
PMID:29899453	PBO:0107357	Extended Data Fig 5a (comment: vw: fixed allele and target)
PMID:29899453	PBO:0107350	(Fig. 1c, Extended Data Fig 2a)
PMID:29899453	PBO:0099591	(Fig. 1c)
PMID:29899453	PBO:0107359	(Fig. 1d, Extended Data Fig. 1d)
PMID:29899453	PBO:0107359	(Fig. 1d, Extended Data Fig. 1d)
PMID:29899453	PBO:0107360	(comment: check this addition) Fig. 2a, Extended Data Fig. 2a
PMID:29899453	PBO:0099622	(Fig. S2, Extended Data Fig. 2c)
PMID:29899453	PBO:0094008	(Fig. S2, Extended Data Fig. 2d)
PMID:29899453	PBO:0107361	(Fig. 2d)
PMID:29899453	PBO:0107361	(Extended Data Fig 2f)
PMID:29899453	PBO:0107361	(Extended Data Fig 2f)
PMID:29899453	PBO:0107362	(Extended Data Fig 3a, Fig. 2c, Extended Data Fig. 3b-d)
PMID:29899453	PBO:0107363	(Fig. 2e, Extended Data Fig. 4b)
PMID:29899453	PBO:0107363	(Fig. 2e, Extended Data Fig. 4c)
PMID:29899453	PBO:0107365	(Fig. 6a, b)
PMID:29914874	FYPO:0001234	Supplementary Table S3
PMID:29914874	FYPO:0001234	Supplementary Fig. S3
PMID:29914874	FYPO:0000017	Supplementary Fig. S3
PMID:29914874	FYPO:0004750	Supplementary Figure S3
PMID:29914874	FYPO:0001234	Supplementary Fig. S3
PMID:29914874	FYPO:0001234	Supplementary Fig. S3
PMID:29914874	FYPO:0000005	Supplementary Fig. S3
PMID:29914874	FYPO:0001234	Supplementary Fig. S3
PMID:29930085	GO:0110085	(Figure 5, Figure S4, Movie 5)
PMID:29930085	PBO:0103570	(Figure 1) (comment: CHECK interphase arrest)
PMID:29930085	FYPO:0005465	(Figure 2, Movei 1)
PMID:29930085	FYPO:0005465	(Figure 1) (comment: CHECK interphase arrest)
PMID:29930085	PBO:0096676	(Figure 1) (comment: CHECK interphase arrest requested during interphase)
PMID:29930085	PBO:0094706	(Figure 1) (comment: CHECK interphase arrest requested during interphase)
PMID:29930085	PBO:0103569	(Figure 1) (comment: CHECK interphase arrest requested during interphase)
PMID:29930085	PBO:0103568	(Figure 6, Figure S6, Movie 7)
PMID:29930085	PBO:0103568	(Figure 7, Movie 9)
PMID:29930085	FYPO:0002060	(Figure 5B)
PMID:29930085	FYPO:0002104	(Figure 4, Movie 4)
PMID:29930085	GO:0005737	(Figure 5, Figure S4, Movie 5)
PMID:29930085	PBO:0103568	(Figure S6, Movie 8)
PMID:29930085	GO:1902716	(Figure 1)
PMID:29930085	FYPO:0002150	(Figure S3)
PMID:29930085	FYPO:0002150	(Figure S3)
PMID:29930085	PBO:0103572	(comment: PORTLI GROWTH) fig 2 (comment: CHECK interphase arrest https://github.com/pombase/fypo/issues/3339)
PMID:29930085	PBO:0103571	(Figure 1) (comment: CHECK interphase arrest)
PMID:29930085	PBO:0103574	(Figure S3)
PMID:29930085	PBO:0103577	(comment: PORTLI Growth) Figure 6, Figure S6, Movie 7 (comment: CHECK https://github.com/pombase/fypo/issues/3339)
PMID:29930085	PBO:0103576	(comment: PORTLI GROWTH) Figure 6C (comment: CHECK https://github.com/pombase/fypo/issues/3339)
PMID:29930085	PBO:0103575	(comment: PORTLI GROWTH) Figure S6 (comment: CHECK https://github.com/pombase/fypo/issues/3339)
PMID:29930085	PBO:0103572	(comment: PORTLI GROWTH) Figure S6 (comment: CHECK https://github.com/pombase/fypo/issues/3339)
PMID:29930085	FYPO:0005465	(Figure 5B)
PMID:29930085	FYPO:0003316	(Figure 4,AB)
PMID:29930085	PBO:0103572	(comment: PORTLI GROWTH) (Figs 3B and 4B; Movie 2) (comment: CHECK https://github.com/pombase/fypo/issues/3339)
PMID:29930085	PBO:0097442	(Figure 1) (comment: CHECK interphase arrest requested during interphase)
PMID:29930085	PBO:0103572	(Figure 7, Movie 9) (comment: CHECK https://github.com/pombase/fypo/issues/3339)
PMID:29930085	PBO:0093708	(Figure 7D)
PMID:29930085	FYPO:0006639	(Figure 7C)
PMID:29930085	PBO:0103573	(Figure 3)
PMID:29930085	PBO:0103573	(Figure 3)
PMID:29930085	PBO:0103572	(comment: PORTLI GROWTH) (Figs 3B and 4B; Movie 2) (comment: CHECK https://github.com/pombase/fypo/issues/3339)
PMID:29930085	PBO:0103578	(Figure 7D)
PMID:29930085	GO:0110085	(Figure 1)
PMID:29930085	PBO:0020227	(Figure 1)
PMID:29930085	GO:0110085	(Figure 1)
PMID:29930085	PBO:0018345	(Figure 1)
PMID:29930085	PBO:0018345	(Figure 1)
PMID:29930085	GO:0005938	(Figure 1)
PMID:29930085	GO:0110085	(Figure 1)
PMID:29930085	PBO:0103568	(Figure 2)
PMID:29930085	PBO:0103568	(Figure 3, Figure 4, Figure S2, Movie 2, Movie 3, Movie 4)
PMID:29930085	PBO:0103568	(Figure 3, Movie 2)
PMID:29930085	FYPO:0002104	(Figure 4, Movie 4)
PMID:29930085	FYPO:0002104	(Figure 4, Figure S3, Movie 4)
PMID:29930085	FYPO:0002104	(Figure 4, Movie 4)
PMID:29930085	FYPO:0005465	(Figure 2) (comment: CHECK interphase arrest)
PMID:29930085	PBO:0019153	(Figure S6, Movie 8)
PMID:29930085	PBO:0019141	(Figure 7, Figure S8)
PMID:29930085	FYPO:0002104	(Figure 7, Figure S8)
PMID:29930085	FYPO:0006617	(Figure S1)
PMID:29975113	GO:0071341	(Figure 1B and S1B)
PMID:29975113	PBO:0113859	(DNS) Dma1-I194A constitutively localizes to SPB throughout the cell cycle. Dma1-I194A localizes more intensely at one of the two SPBs for most of mitosis
PMID:29975113	PBO:0023023	(Figures 1B and S1A) Dma1-mNeonGreen became enriched at SPBs prior to SPB separation. It appeared to transiently leave SPBs during anaphase B, returning before telophase and then leaving again after cell division. Dma1 SPB transient loss happens before the development of Cdc7 SPB localiztion asymmetry. Dma1 failed to return to SPBs in late anaphase in cdc7-24 cells at restrictive temperature. Dma1 could be detected on majority SPBs in cdc16-116 cells at restrictive temperature, suggesting high SIN activity promote Dma1 SPB re-accumulation at the end of anaphase.
PMID:29975113	PBO:0096158	(Figure 2G)
PMID:29975113	FYPO:0001491	(Figure S2D) dma1-GFP sid4-GBP-mCherry cells are very sick, if not die. ppc89-DUB rescued the synthetic sick phenotype of dma1-GFP sid4-GBP-mCherry. The cells have reduced levels of multi-nucleate and kissing nuclei compared with dma1-GFP sid4-GBP-mCherry.
PMID:29975113	PBO:0096156	(Figure S2A)
PMID:29975113	PBO:0096153	(comment: Vw, because mutants are related to WT, I changed this to 'normal'), Dma1-I194A-mNeonGreen displays transient loss from SPB during anaphase, just like wild-type Dma1.
PMID:29975113	FYPO:0002060	(Figure S2D)
PMID:29975113	PBO:0096159	(comment: CHECK These data are consistent with auto-ubiquitination triggering Dma1 destruction.)
PMID:29975113	PBO:0096158	(Figure 2D)
PMID:29975113	PBO:0096151	(Figure S2B)
PMID:29975113	PBO:0096154	(Figure 2D) (comment: CHECK in vivo)
PMID:29975113	PBO:0096157	(comment: temporal localization pattern) Figure S2B
PMID:29975113	PBO:0019716	(Figure 1B and S1B) Dma1-mNeonGreen forms a ring at cell division site during early mitosis. Then it leaves and returns to cell division site during mitosis. Dma1 transiently leaves cell division site before Sid2 appears at the cell division site.
PMID:29975113	PBO:0096150	(Figure 2B and C)
PMID:29975113	GO:0031030	(comment: [ dma1 unubiquitinated, sid4 phosphorylated]) When Dma1-GFP is permanently tethered to SPBs by Sid4-GBP-mCherry, cells displayed multi-nucleate and kissing nuclei indicative of SIN and cytokinesis failure.
PMID:29975157	PBO:0098955	(Fig. 4A)
PMID:29975157	FYPO:0000123	(Fig. S2A)
PMID:29975157	FYPO:0002253	(Fig. S1F)
PMID:29975157	FYPO:0002253	(Fig. S1F)
PMID:29975157	PBO:0098959	(Fig. S1F)
PMID:29975157	PBO:0098954	(Fig. 1B)
PMID:29975157	FYPO:0002253	(Fig. S1F)
PMID:29975157	FYPO:0006628	(Fig. 5A)
PMID:29975157	FYPO:0006628	(Fig. 5A)
PMID:29975157	FYPO:0006628	(Fig. 5A)
PMID:29975157	FYPO:0006629	(Fig. 5A)
PMID:29975157	FYPO:0006628	(Fig. 5A)
PMID:29975157	FYPO:0006626	(Fig. 5C)
PMID:29975157	FYPO:0006625	(Fig. 5C)
PMID:29975157	FYPO:0006627	(Fig. 5C)
PMID:29975157	FYPO:0006625	(Fig. 5C)
PMID:29975157	FYPO:0006623	(Fig. 5B)
PMID:29975157	FYPO:0006624	(Fig. 5B)
PMID:29975157	FYPO:0006623	(Fig. 5B)
PMID:29975157	FYPO:0006623	(Fig. 5B)
PMID:29975157	FYPO:0006624	(Fig. 5B)
PMID:29975157	PBO:0098958	(Fig. 4D)
PMID:29975157	PBO:0098957	(Fig. 4C)
PMID:29975157	PBO:0098956	(Fig. 4B)
PMID:29975157	FYPO:0005289	(Fig. 3)
PMID:29975157	FYPO:0002071	(Fig. 2D)
PMID:29975157	FYPO:0001369	(Fig. 2A-C)
PMID:29975157	FYPO:0001369	(Fig. 2A-C)
PMID:29975157	FYPO:0000339	(Fig. 1B)
PMID:29975157	FYPO:0002253	(Fig. 1B)
PMID:29975157	FYPO:0002253	(Fig. 1B)
PMID:29975157	FYPO:0000339	(Fig. 1B)
PMID:29975157	FYPO:0002253	(Fig. 1B)
PMID:29975157	PBO:0098954	(Fig. 1B)
PMID:29975157	FYPO:0000339	(Fig. 1B)
PMID:29975157	FYPO:0002253	(Fig. 1B)
PMID:29975157	FYPO:0002253	(Fig. 1B)
PMID:29975157	FYPO:0002253	(Fig. 1B)
PMID:29975157	FYPO:0002253	(Fig. 1B)
PMID:29975157	FYPO:0002253	(Fig. 1B)
PMID:29975157	FYPO:0002253	(Fig. 1B)
PMID:29975157	FYPO:0002253	(Fig. 1B)
PMID:29975157	FYPO:0000339	(Fig. S2E)
PMID:29975157	FYPO:0002253	(Fig. 1B)
PMID:29975157	FYPO:0001369	(Fig. S2C,D)
PMID:29975157	FYPO:0000339	(Fig. S2A-D)
PMID:30003614	FYPO:0004695	(Fig. 4)
PMID:30003614	FYPO:0002227	(Fig. 4)
PMID:30003614	FYPO:0006632	(Fig. 4)
PMID:30003614	FYPO:0002061	(Fig. 5) (comment: cerulenin)
PMID:30003614	FYPO:0000808	increased number of lipid droples/cell fig 3b,c
PMID:30003614	FYPO:0002236	(Fig. 4)
PMID:30044717	FYPO:0001494	(Fig. 5b)
PMID:30044717	FYPO:0002061	(Fig. 5B)
PMID:30044717	PBO:0107419	(Fig. S2,E)
PMID:30044717	PBO:0107420	(Fig. S4E)
PMID:30044717	PBO:0105130	(Fig. S4E)
PMID:30044717	FYPO:0001355	(Fig. 2b)
PMID:30044717	FYPO:0002061	(Fig. 2a)
PMID:30044717	GO:0001786	(Fig. S3 DE)
PMID:30044717	GO:0005546	(Fig. S3 DE)
PMID:30044717	PBO:0107419	(Fig. S2,E)
PMID:30044717	PBO:0107419	(Fig. S2C,E)
PMID:30044717	PBO:0107418	(Fig. S2)
PMID:30044717	PBO:0107418	(Fig. S2)
PMID:30044717	FYPO:0004653	(Fig. 5)
PMID:30044717	FYPO:0002061	(Fig. 5B)
PMID:30044717	FYPO:0001581	(Fig. 5B)
PMID:30044717	PBO:0108998	(Figure 7)
PMID:30044717	PBO:0107417	Supp S1G
PMID:30044717	PBO:0107417	Supp S1F
PMID:30044717	PBO:0107416	(Figure 1)
PMID:30044717	PBO:0107413	(Fig. 4)
PMID:30044717	PBO:0107410	(Fig. 5C)
PMID:30044717	PBO:0107408	(Fig. 6A)
PMID:30044717	PBO:0107407	(Fig. 5C)
PMID:30044717	PBO:0019669	(Fig. S4C)
PMID:30044717	PBO:0107404	(Fig. S4C)
PMID:30044717	PBO:0107403	(Fig. S4C)
PMID:30044717	PBO:0018421	(Fig. 1)
PMID:30044717	PBO:0018576	(Figure 1)
PMID:30044717	PBO:0019669	(Fig. 2B)
PMID:30044717	PBO:0107401	(Fig. 2a) (comment: vw: average survival ~ 7 cell cycles)
PMID:30044717	PBO:0035615	(Fig. S4C)
PMID:30044717	GO:0032153	(Fig. 7E)
PMID:30044717	GO:0035838	(Fig. 7E)
PMID:30044717	GO:0090689	(Figure 6E)
PMID:30044717	PBO:0107422	(Fig. S6B)
PMID:30044717	PBO:0108997	(Fig. 5D and Movie 5)
PMID:30053106	GO:0070336	(comment: requires long flap (binding affinity much higher with 27-nt than 15-nt flap))
PMID:30053106	GO:0070336	(comment: requires long flap (binding affinity much higher with 27-nt than 15-nt flap))
PMID:30053106	GO:0160225	(comment: requires long flap (binding affinity much higher with 27-nt than 15-nt flap))
PMID:30053106	GO:0160225	(comment: requires long flap (binding affinity much higher with 27-nt than 15-nt flap))
PMID:30072377	PBO:0103668	(Fig. 3C, D; Fig. 4A,B)
PMID:30072377	PBO:0103668	(Fig. 3B, Fig. 4A,B)
PMID:30072377	PBO:0103668	(Fig. 4A,B)
PMID:30072377	FYPO:0006779	(Fig. 4C) Resistant to 1mM spermidine at 37C.
PMID:30072377	FYPO:0006779	(Fig. 4C) Resistant to 1 mM spermidine at 37C.
PMID:30072439	PBO:0093556	Suppression of temperature sensitivity by 1.2M sorbitol
PMID:30072439	PBO:0093557	(comment: CHECK Partial suppression of growth defect in the presence of sorbitol)
PMID:30072439	FYPO:0004165	(comment: Normal glucose consumption, but cell division is sensitive to low glucose condition)
PMID:30072439	PBO:0093558	Synthetic growth defect between cwh43-G753R mutant and dga1Δ plh1Δ double deletion mutant.
PMID:30072439	FYPO:0006970	(comment: CHECK decreased cellular diphosphoglycerate level)
PMID:30072439	FYPO:0006951	(comment: CHECK increased cellular dimethyl-histidine level during vegetative growth)
PMID:30072439	GO:1990578	However, in scs2Δ scs22Δ double deletion mutant cells, localization of both Cwh43-GFP and AHDL- mCherry at the plasma membrane disappeared, and, instead, accumulated in the cytoplasm
PMID:30072439	PBO:0093561	Partial suppression of growth defect in the presence of sorbitol
PMID:30072439	PBO:0096875	Sorbitol addition partly suppresses beta-glucan accumulation in cwh43-G753R mutant cells
PMID:30072439	PBO:0093556	Suppression of temperature sensitivity by 1.2M sorbitol
PMID:30072439	PBO:0093556	Suppression of temperature sensitivity by 1.2M sorbitol
PMID:30072439	PBO:0093556	Suppression of temperature sensitivity by 1.2M sorbitol
PMID:30072439	PBO:0093560	Synthetic growth defect between cwh43-G753R mutant and dga1Δ plh1Δ double deletion mutant.
PMID:30072439	FYPO:0003516	Drastic changes in antioxidants, sugar derivatives, amino acid derivatives, organic acids, coenzyme A (CoA), and nucleotide derivatives. Most of these compounds are biomarkers for nutritional starvation (low-glucose or nitrogen-starvation).
PMID:30076928	PBO:0106501	(comment: transcription read through by PCR)
PMID:30076928	PBO:0106502	(comment: CHECK RT-PCR)
PMID:30076928	PBO:0106503	(comment: CHECK RT-PCR)
PMID:30076928	PBO:0106504	(comment: transcription read through by PCR)
PMID:30089114	MOD:01148	(comment: CHECK polyubiquitylated)
PMID:30089114	GO:0034080	Heterochromatin structure protects native CENP-A from ubiquitin-mediated degradation.
PMID:30089908	FYPO:0006669	(Fig. 1a) type IIIa
PMID:30089908	PBO:0096714	(Fig. 1g)
PMID:30089908	PBO:0096713	Extended data figure 1F (comment: dominant over shk2 downstream sporulation phenotypes)
PMID:30089908	FYPO:0006673	(Figure 1c)
PMID:30089908	FYPO:0000678	(comment: CHECK abolished karyogamy with transient cytogamy -this is a bit like twin haploid meiosis? should be siblings? also looks like karyogamy failure)
PMID:30089908	FYPO:0006672	(comment: CHECK abolished karyogamy with transient cytogamy -this is a bit like twin haploid meiosis? should be siblings? also looks like karyogamy failure)
PMID:30089908	GO:0005737	(comment: M-cells)
PMID:30089908	GO:0005634	(comment: CHECK P-cells (rapid) M-cells (delayed))
PMID:30089908	GO:0005634	Extended Data Fig. 3b, Supplementary Video 5a
PMID:30089908	PBO:0096715	(Fig. 1a) type IIIb
PMID:30089908	PBO:0096712	(Fig. 1a) type IIIb
PMID:30089908	GO:0032220	Homothalic pak2∆ partners exhibit fusion efficiency decrease of ~20% as compared to wild-type partner fusion. Homothalic pak2∆ cells undergo transient fusion with frequency of ~10%, which is absent in wild-type matings.
PMID:30089908	FYPO:0000413	(Fig. 1 II)
PMID:30089908	PBO:0112050	(comment: Regulation of asymmetric gene expression from parental genomes Factor that regulates differential gene expression of homologous parental gene copies)
PMID:30089908	PBO:0112050	(comment: Regulation of asymmetric gene expression from parental genomes Factor that regulates differential gene expression of homologous parental gene copies)
PMID:30089908	PBO:0112056	(comment: Regulation of asymmetric gene expression from parental genomes)
PMID:30089908	PBO:0112056	(comment: Regulation of asymmetric gene expression from parental genomes)
PMID:30089908	PBO:0096720	Extended Data Fig. 5e, f, Supplementary Video 9; see also ref. 1
PMID:30089908	PBO:0096719	Extended Data Fig. 5e, f, Supplementary Video 9; see also ref. 1
PMID:30089908	FYPO:0001886	(comment: in M-cell)
PMID:30089908	FYPO:0006014	(comment: never ending search for mating partner by P cell)
PMID:30089908	FYPO:0006014	(Fig. 2c) (comment: never ending search for mating partner)
PMID:30089908	FYPO:0002052	(Fig. 4a, Extended Data Fig. 4c, Supplementary Video 7b)
PMID:30089908	FYPO:0001147	(Fig. 4a, Extended Data Fig. 4c, Supplementary Video 7b)
PMID:30089908	FYPO:0006014	(Fig. 4a, Extended Data Fig. 4c, Supplementary Video 7b)
PMID:30089908	PBO:0096718	(Fig. 3d, Supplementary Video 5b)
PMID:30089908	PBO:0096717	(comment: CHECK *******to nucleus of opposite mating type cell******)
PMID:30089908	GO:0062071	(comment: CHECK go-ontology/issues/16327)
PMID:30089908	PBO:0096716	(comment: CHECK ******abolished in M cells) Fig. 2a, Supplementary Video 5, Fig. 2b, Supplementary Video 2a Importantly, mei3 was also asymmetrically expressed in WT...zygotes first express the meiotic inducer Mei3 from the P genome.
PMID:30089908	GO:0140538	(comment: CHECK GO:0140538 +name: negative regulation of conjugation with zygote https://github.com/geneontology/go-ontology/issues/16329)
PMID:30089908	GO:0140538	(comment: CHECK GO:0140538 +name: negative regulation of conjugation with zygote https://github.com/geneontology/go-ontology/issues/16329)
PMID:30102332	GO:0006368	also inferred from orthology, interactions, and chromatin localization (ChIP)
PMID:30102332	FYPO:0004903	(Figures 4, 5)
PMID:30102332	FYPO:0000650	(Figure 5)
PMID:30102332	GO:0006368	also inferred from orthology, interactions, and chromatin localization (ChIP)
PMID:30102332	GO:0006368	also inferred from orthology, interactions, and chromatin localization (ChIP)
PMID:30102332	FYPO:0004903	(Figures 4, 5)
PMID:30102332	FYPO:0004903	(Figures 4, 5)
PMID:30102332	FYPO:0000650	(Figure 5)
PMID:30102332	FYPO:0000650	(Figure 5)
PMID:30104346	PBO:0107548	(comment: evidence is combination of ChIP in this paper plus data in other publications showing that Rad52 binds DNA directly)
PMID:30104346	PBO:0107547	(comment: evidence is combination of ChIP in this paper plus data in other publications showing that Ctp1 binds DNA directly)
PMID:30104346	PBO:0107547	(comment: evidence is combination of ChIP in this paper plus data in other publications showing that Rad50 orthologs (and therefore almost certainly Sc Rad50) binds DNA directl)
PMID:30110338	PBO:0103520	(comment: CHECK H3 K9me3)
PMID:30110338	PBO:0119957	(comment: CHECK H3 K9me3 https://github.com/geneontology/go-ontology/issues/16331)
PMID:30110338	PBO:0119872	(comment: CHECK H3 K9me3 https://github.com/geneontology/go-ontology/issues/16331)
PMID:30110338	PBO:0119871	(comment: CHECK H3 K9me3 https://github.com/geneontology/go-ontology/issues/16331)
PMID:30116786	PBO:0107390	(Fig. 4E)
PMID:30116786	PBO:0107380	(Fig. 4E)
PMID:30116786	PBO:0112759	(Fig. 4E)
PMID:30116786	PBO:0107394	(Fig. 4E)
PMID:30116786	PBO:0107395	(Fig. 4E)
PMID:30116786	FYPO:0000238	(Fig. 3F) (comment: loss of mitotic competence)
PMID:30116786	PBO:0018802	(Fig. 3B)
PMID:30116786	FYPO:0006667	(Fig. 3C)
PMID:30116786	FYPO:0006660	(Fig. 3F) (comment: loss of mitotic competence)
PMID:30116786	PBO:0107378	(Fig. 3)
PMID:30116786	PBO:0107378	(Fig. 3)
PMID:30116786	PBO:0107377	(Fig. 3B)
PMID:30116786	PBO:0107391	(Fig. 4E)
PMID:30116786	PBO:0107392	(Fig. 4E)
PMID:30116786	FYPO:0006662	(Fig. S3)
PMID:30116786	PBO:0107379	(Fig. 4A,E)
PMID:30116786	PBO:0107381	(Fig. 4C)
PMID:30116786	PBO:0107382	(Fig. 4E)
PMID:30116786	FYPO:0002552	(Fig. 3)
PMID:30116786	PBO:0107383	(Fig. 4E)
PMID:30116786	PBO:0107384	(Fig. 4E)
PMID:30116786	PBO:0107385	(Fig. 4E)
PMID:30116786	PBO:0107386	(Fig. 4E)
PMID:30116786	PBO:0107387	(Fig. 4E)
PMID:30116786	PBO:0107388	(Fig. 4E)
PMID:30116786	FYPO:0002552	(Fig. 3)
PMID:30116786	PBO:0107389	(Fig. 4E)
PMID:30134042	PBO:0094696	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	PBO:0094701	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	PBO:0094700	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	PBO:0094700	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	PBO:0094697	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	PBO:0094697	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	PBO:0094697	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	PBO:0094697	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	PBO:0094697	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	PBO:0094697	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	PBO:0094697	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	PBO:0094696	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30201262	PBO:0107958	(Fig. 6)
PMID:30201262	FYPO:0002061	SFig5
PMID:30201262	PBO:0107957	(Fig. 6)
PMID:30201262	FYPO:0001904	(comment: Temperature was shifted at anaphase B.)
PMID:30201262	FYPO:0000161	(comment: Temperature was shifted at prophase or metaphase.)
PMID:30201262	FYPO:0007200	(Fig. 1)
PMID:30201262	FYPO:0007201	(Fig. 6)
PMID:30212894	PBO:0101499	correlation with gel shift assays
PMID:30212894	PBO:0094771	correlation with gel shift assays
PMID:30212894	PBO:0101499	correlation with gel shift assays
PMID:30212894	PBO:0094771	correlation with gel shift assays
PMID:30212894	PBO:0101499	correlation with gel shift assays
PMID:30212894	PBO:0094771	correlation with gel shift assays
PMID:30212894	PBO:0101499	correlation with gel shift assays
PMID:30212894	FYPO:0001045	correlation with gel shift assays
PMID:30212894	PBO:0101499	correlation with gel shift assays
PMID:30212894	PBO:0094771	correlation with gel shift assays
PMID:30212894	FYPO:0006658	correlation with gel shift assays
PMID:30212894	FYPO:0001045	correlation with gel shift assays
PMID:30212894	PBO:0104166	correlation with gel shift assays
PMID:30212894	PBO:0094771	correlation with gel shift assays
PMID:30212894	PBO:0101499	correlation with gel shift assays
PMID:30212894	PBO:0094771	correlation with gel shift assays
PMID:30212894	PBO:0101499	correlation with gel shift assays
PMID:30212894	PBO:0094771	correlation with gel shift assays
PMID:30212894	PBO:0101499	correlation with gel shift assays
PMID:30212894	PBO:0094771	correlation with gel shift assays
PMID:30212894	PBO:0101499	correlation with gel shift assays
PMID:30212894	PBO:0094771	correlation with gel shift assays
PMID:30212894	PBO:0104165	correlation with gel shift assays
PMID:30212894	PBO:0098248	correlation with gel shift assays
PMID:30217891	FYPO:0004602	(Supp S14)
PMID:30217891	PBO:0103043	(Fig. 3)
PMID:30217891	PBO:0103042	(Fig. 3)
PMID:30228203	PBO:0119661	the levels of Sen2-mECitrine and Sen54-mECitrine are reduced in tom70Δ cells compared with wild type (Fig. 5B; Supplemental Fig. S9). We interpret these results to support the hypothesis that S. pombe Tom70 functions in the mitochondrial localization of SEN subunits; when mitochondrial localization is not achieved, the SEN subunits become unstable, although it is possible that SEN subunits are poorly expressed in tom70Δ cells.
PMID:30228203	GO:0032473	Sen2, Sen34, and Sen54 endogenously tagged at their C termini locate to mitochondria, as indicated by the overlapping signal with the mitochondrion stain MitoView Blue (Fig. 5A). H
PMID:30228203	GO:0032473	Sen2, Sen34, and Sen54 endogenously tagged at their C termini locate to mitochondria, as indicated by the overlapping signal with the mitochondrion stain MitoView Blue (Fig. 5A). H
PMID:30228203	GO:0032473	Sen2, Sen34, and Sen54 endogenously tagged at their C termini locate to mitochondria, as indicated by the overlapping signal with the mitochondrion stain MitoView Blue (Fig. 5A). H
PMID:30228203	FYPO:0008394	If S. pombe Tom70 is important for function and/or stability of the SEN complex, then deletion of S. pombe TOM70 would be expected to cause defects in pre- tRNA splicing. We used Northern analysis with probes complementary to the 5′ exons or introns of S. pombe tRNALeuCAA and tRNAProCGG. tom70Δ cells accumulate more intron-containing tRNALeuCAA and tRNAProCGG than wild-type cells (Fig. 5C), documenting a role for S. pombe Tom70 in pre-tRNA splicing.
PMID:30228203	FYPO:0008113	If S. pombe Tom70 is important for function and/or stability of the SEN complex, then deletion of S. pombe TOM70 would be expected to cause defects in pre- tRNA splicing. We used Northern analysis with probes complementary to the 5′ exons or introns of S. pombe tRNALeuCAA and tRNAProCGG. tom70Δ cells accumulate more intron-containing tRNALeuCAA and tRNAProCGG than wild-type cells (Fig. 5C), documenting a role for S. pombe Tom70 in pre-tRNA splicing.
PMID:30228203	PBO:0119660	By confocal microscopy, Sen2-mECitrine and Sen54- mECitrine signals were very weak in tom70Δ cells, with the residual signals located in the cytoplasm and some located on mitochondria (Fig. 5A).
PMID:30279276	PBO:0100645	(comment: Cdc42-GTP assayed with CRIB- broad zones of activity)
PMID:30280012	PBO:0093577	(Fig. 6)
PMID:30280012	PBO:0093577	(Fig. 6)
PMID:30280012	PBO:0093576	(Fig. 6)
PMID:30280012	PBO:0093576	(Fig. 6)
PMID:30280012	PBO:0093577	(Fig. 6)
PMID:30280012	FYPO:0000082	(Figure S5A, S5B)
PMID:30280012	FYPO:0002177	(Fig. S5C, S6)
PMID:30280012	PBO:0093577	(Fig. 6)
PMID:30282034	PBO:0095888	(comment: CHECK at transcription_termination_signal)
PMID:30282034	PBO:0100141	(comment: CHECK at transcription_termination_signal)
PMID:30282034	PBO:0100139	(comment: CHECK at transcription_termination_signal)
PMID:30282034	PBO:0100139	(comment: CHECK at transcription_termination_signal)
PMID:30332655	PBO:0107863	(comment: inferred from phenotypes and from direct assay using human calcineurin)
PMID:30348841	PBO:0094936	deletion of Brc1 significantly reduced Nse4 residence at binding sites tested under normal and genotoxic stress
PMID:30348841	PBO:0094936	deletion of Nse6 strongly reduced Nse4 residence at binding sites tested under normal and genotoxic stress
PMID:30348841	PBO:0094933	(Fig. 1 a) brc1 mutant abolishes Nse4 nuclear foci in HU/MMS treated cells
PMID:30348841	PBO:0094932	(Fig. 1) brc1 mutant cells expressing brc1-T672A are deficient in Nse4 foci formation
PMID:30348841	PBO:0094940	mutations in brc1 weaken interaction with nse6
PMID:30348841	PBO:0094939	Nse4 sumoylation at wild type level
PMID:30348841	PBO:0094938	Nse4 sumoylation reduced in brc1Δ
PMID:30348841	PBO:0093580	nse2-SA brc1Δ cells are more sensitive to genotoxins than either single mutant (Fig. 4C).
PMID:30348841	PBO:0094942	Notably, however, deletion of either Nse5 or Nse6 strongly reduced Nse4 residence at all binding sites tested, which was most evident under conditions of genotoxic stress that stimulate de novo Smc5-Smc6 loading
PMID:30348841	PBO:0094943	Notably, however, deletion of either Nse5 or Nse6 strongly reduced Nse4 residence at all binding sites tested, which was most evident under conditions of genotoxic stress that stimulate de novo Smc5-Smc6 loading
PMID:30348841	PBO:0094944	As anticipated, the MMS-induced SUMOylation of Nse4-TAP in wild-type cells was detectable upon immunoprecipitation (IP) of Nse4 without overexpression or initial enrichment of SUMO (Fig. 4A)
PMID:30348841	PBO:0094945	MMS-induced Nse4 SUMOylation was also reduced in brc1Δ cells but was similar to wild-type in rhp18Δ cells, which support normal Nse4-GFP focus formation (Fig. 4B)
PMID:30348841	PBO:0094933	Nse4 foci gone in nse6 mutant cells
PMID:30348841	PBO:0094937	Nse4 sumoylation undetectable in nse6Δ
PMID:30348841	PBO:0094936	deletion of Nse5 strongly reduced Nse4 residence at binding sites tested under normal and genotoxic stress
PMID:30355493	PBO:0105005	(Fig. 4)
PMID:30355493	PBO:0105009	(Fig. 3c)
PMID:30355493	PBO:0105003	(Fig. 2d)
PMID:30355493	PBO:0105002	(Fig. 2d)
PMID:30355493	PBO:0105008	(Fig. 2d)
PMID:30355493	PBO:0105007	(Fig. 2d)
PMID:30355493	PBO:0105006	(Fig. 2d)
PMID:30355493	PBO:0105005	(Fig. 2d)
PMID:30355493	PBO:0105004	(Fig. 2d)
PMID:30355493	PBO:0105003	(Fig. 2d)
PMID:30355493	PBO:0105002	(Fig. 2d)
PMID:30355493	PBO:0105001	(Fig. S3C)
PMID:30355770	FYPO:0001045	(Fig. 2A)
PMID:30355770	FYPO:0001045	(Fig. 2A)
PMID:30355770	FYPO:0001045	(Fig. 2A)
PMID:30355770	FYPO:0001045	(Fig. 2A)
PMID:30355770	FYPO:0001045	(Fig. 2A)
PMID:30355770	FYPO:0001045	(Fig. 2A)
PMID:30355770	FYPO:0003267	(Fig. 2A)
PMID:30355770	FYPO:0003267	(Fig. 2A)
PMID:30355770	FYPO:0001045	(Fig. 2A)
PMID:30355770	FYPO:0001045	(Fig. 2A)
PMID:30355770	FYPO:0001045	(Fig. 2A)
PMID:30355770	PBO:0108846	(Fig. 2B)
PMID:30355770	PBO:0108845	(Fig. 2B)
PMID:30355770	PBO:0108844	(Fig. 2B)
PMID:30355770	PBO:0108843	(Fig. 2B)
PMID:30355770	PBO:0108843	(Fig. 2B)
PMID:30355770	FYPO:0001045	(Fig. 2A)
PMID:30355770	FYPO:0001045	(Fig. 2A)
PMID:30355770	FYPO:0001045	(Fig. 2A)
PMID:30355770	FYPO:0001045	(Fig. 2A)
PMID:30355770	FYPO:0001045	(Fig. 2A)
PMID:30355770	FYPO:0001045	(Fig. 2A)
PMID:30355770	FYPO:0002243	(Fig. 2A)
PMID:30355770	FYPO:0001045	(Fig. 7D)
PMID:30355770	FYPO:0001045	(Fig. 7D)
PMID:30355770	FYPO:0003267	(Fig. 7D)
PMID:30355770	FYPO:0003267	(Fig. 7D)
PMID:30355770	FYPO:0003267	(Fig. 7D)
PMID:30355770	FYPO:0003267	(Fig. 7D)
PMID:30355770	FYPO:0002060	(Fig. S8)
PMID:30355770	FYPO:0002061	(Fig. S8)
PMID:30355770	FYPO:0002061	(Fig. S8)
PMID:30355770	FYPO:0001045	(Fig. 4B)
PMID:30355770	PBO:0108849	(Fig. 4B)
PMID:30355770	PBO:0108849	(Fig. 4B)
PMID:30355770	FYPO:0002243	(Fig. 4B)
PMID:30355770	PBO:0108848	(Fig. S5)
PMID:30355770	FYPO:0002243	(Fig. S5)
PMID:30355770	FYPO:0001045	(Fig. S5)
PMID:30355770	PBO:0108847	(Fig. S6)
PMID:30355770	PBO:0108847	(Fig. S6)
PMID:30355770	PBO:0108847	(Fig. S6)
PMID:30355770	FYPO:0001045	(Fig. 2A)
PMID:30389790	PBO:0093561	(Fig. 2b)
PMID:30389790	PBO:0093561	(Fig. 5b)
PMID:30389790	PBO:0095685	(Fig. 5b)
PMID:30389790	PBO:0095685	(Fig. 5b)
PMID:30389790	FYPO:0001211	(Fig. 6)
PMID:30389790	FYPO:0001124	(Figure 5c)
PMID:30389790	FYPO:0000672	(Figure 5c)
PMID:30389790	FYPO:0001910	(Figure 5c) (comment: CHECK hypoglycosylation)
PMID:30389790	FYPO:0001211	(Fig. 6)
PMID:30389790	FYPO:0002060	(Figure 5 and 11) (comment: no loss of viability )
PMID:30389790	PBO:0093560	(Fig. 2b)
PMID:30389790	FYPO:0001357	(Figure 5b and S2)
PMID:30389790	FYPO:0000805	(Fig. 10)
PMID:30389790	FYPO:0007030	(Fig. S4)
PMID:30389790	FYPO:0001211	(Fig. 6)
PMID:30389790	PBO:0095634	(Fig. 5b)
PMID:30389790	PBO:0095685	(Fig. 5b)
PMID:30389790	GO:0004573	Glucosidase 1, a type II membrane protein with a luminal hydrolytic domain, removes the outermost glucose from protein-linked Glc3Man9GlcNAc2 in the endoplasmic reticulum
PMID:30389790	FYPO:0006980	(Fig. 3b)
PMID:30389790	FYPO:0001035	(Fig. 10)
PMID:30389790	FYPO:0006982	(Fig. 10)
PMID:30389790	FYPO:0006981	(Fig. S4)
PMID:30393157	PBO:0094535	Table2
PMID:30393157	FYPO:0002061	(Fig. 2B)
PMID:30393157	FYPO:0002061	(Fig. 2B)
PMID:30393157	FYPO:0005823	(Fig. 1A)
PMID:30393157	PBO:0094522	(Fig. 1C,D)
PMID:30393157	FYPO:0002061	(Fig. 2B)
PMID:30393157	FYPO:0005823	(Fig. 2C,D)
PMID:30393157	FYPO:0005823	(Fig. 2C,D)
PMID:30393157	PBO:0094526	Table2
PMID:30393157	PBO:0094525	Table2
PMID:30393157	PBO:0094524	Table2
PMID:30393157	PBO:0094523	Table2
PMID:30393157	FYPO:0003004	(Fig. 4)
PMID:30393157	FYPO:0004944	(Fig. 4)
PMID:30393157	FYPO:0003810	(Fig. 4)
PMID:30393157	FYPO:0000375	(Figure 3D)
PMID:30393157	FYPO:0005823	(Fig. 2C,D)
PMID:30393157	FYPO:0001673	(Figure 3D)
PMID:30393157	FYPO:0006661	(Fig. 2E,F)
PMID:30393157	FYPO:0006661	(Fig. 2E,F)
PMID:30393157	PBO:0094527	Table2
PMID:30393157	FYPO:0006661	(Fig. 2E,F)
PMID:30393157	FYPO:0006661	(Fig. 2E,F)
PMID:30393157	FYPO:0005823	(Fig. 2C,D)
PMID:30393157	FYPO:0005823	(Fig. 2C,D)
PMID:30393157	PBO:0094528	Table2
PMID:30393157	PBO:0094529	Table2
PMID:30393157	PBO:0094530	Table2
PMID:30393157	PBO:0094531	Table2
PMID:30393157	PBO:0094532	Table2
PMID:30393157	PBO:0094533	Table2
PMID:30393157	PBO:0094534	Table2
PMID:30393157	FYPO:0002061	(Fig. 2B)
PMID:30393157	PBO:0094536	Table2
PMID:30393157	PBO:0094537	Table2
PMID:30393157	PBO:0094538	Table2
PMID:30393157	PBO:0094539	Table2
PMID:30393157	PBO:0094540	Table2
PMID:30393157	PBO:0094541	(Fig. 5A)
PMID:30393157	PBO:0094542	(Fig. 5A)
PMID:30393157	PBO:0094543	(Fig. 5A)
PMID:30393157	PBO:0094544	(Fig. 5A)
PMID:30393157	PBO:0094545	(Fig. 5A)
PMID:30393157	PBO:0094546	(Fig. 5A)
PMID:30393157	PBO:0094547	(Fig. 5A)
PMID:3040264	PBO:0037115	Table1
PMID:3040264	PBO:0037116	Table1
PMID:3040264	PBO:0037114	Table1
PMID:3040264	PBO:0037113	(Fig. 2b) (comment: CHECK uncondensed chromosomes)
PMID:3040264	GO:0007076	(Fig. 2B)
PMID:3040264	FYPO:0003145	(Fig. 2b) ((comment: CHECK uncondensed chromosomes)
PMID:3040264	FYPO:0001683	(Fig. 2a) (comment: CHECK no spindle rod like chromsomes)
PMID:3040264	FYPO:0001683	(Fig. 2b)
PMID:3040264	FYPO:0002071	(Fig. 2a)
PMID:3040264	FYPO:0000620	(Fig. 2a) (comment: CHECK no spindle rod like chromsomes)
PMID:3040264	FYPO:0002018	(Fig. 2a) (comment: no spindle rod like chromsomes)
PMID:30427751	PBO:0107999	Therefore, we concluded that Rsp1 is required to prevent excessive accumulation of Mto1
PMID:30427751	FYPO:0005558	(Figure 1)
PMID:30427751	FYPO:0000234	(Figure 1G,H) (comment: from preexisting microtubules)
PMID:30427751	PBO:0107994	(Figure 2A) (comment:CHECK with increased localization to SPB)
PMID:30427751	PBO:0107995	(Figure 2B)
PMID:30427751	PBO:0107996	(Figure 2A) (comment:CHECK with increased localization to SPB)
PMID:30427751	PBO:0107997	(Figure 2B)
PMID:30427751	PBO:0107998	(Figure 2B)
PMID:30427751	PBO:0107999	Therefore, we concluded that Rsp1 is required to prevent excessive accumulation of Mto1
PMID:30427751	PBO:0108000	(Figure 5A)
PMID:30427751	PBO:0108001	(Figure 5A)
PMID:30427751	GO:0005515	(Fig. 5A) (comment:CHECK recruitment)
PMID:30427751	PBO:0108002	(Figure 5G,H)
PMID:30427751	PBO:0108003	(Figure 5I)
PMID:30427751	FYPO:0004511	(Figure 6D)
PMID:30427751	FYPO:0005686	(Figure 6A,C)
PMID:30427751	PBO:0108004	(Figure 6A,C)
PMID:30451685	GO:0007033	(Figure 2; Figure S1)
PMID:30451685	FYPO:0006784	(Figure 3—Figure supplement 1B, 2B)
PMID:30451685	FYPO:0006784	(Figure 3—Figure supplement 1B, 2B)
PMID:30451685	PBO:0108012	(Figure 3—Figure supplement 2)
PMID:30451685	PBO:0108012	(Figure 3—Figure supplement 2)
PMID:30451685	PBO:0108012	(Figure 3—Figure supplement 2)
PMID:30451685	PBO:0108013	(Figure 4A)
PMID:30451685	PBO:0108013	(Figure 4—Figure supplement 1C)
PMID:30451685	PBO:0108014	(Figure 4A)
PMID:30451685	PBO:0108015	(Figure 4—Figure supplement 1B)
PMID:30451685	PBO:0108015	(Figure 4—Figure supplement 1B)
PMID:30451685	PBO:0108015	(Figure 4A)
PMID:30451685	PBO:0108015	(Figure 4—Figure supplement 1B)
PMID:30451685	PBO:0108015	(Figure 4—Figure supplement 1B)
PMID:30451685	PBO:0108010	(Figure 4B)
PMID:30451685	PBO:0108010	(Figure 4B)
PMID:30451685	PBO:0108010	(Figure 4B)
PMID:30451685	FYPO:0006784	(Figure 3—Figure supplement 1B, 2B)
PMID:30451685	PBO:0108008	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	PBO:0108008	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	PBO:0108008	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	PBO:0108008	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	PBO:0108011	(Figure 4—Figure supplement 1B)
PMID:30451685	PBO:0108011	(Figure 3—Figure supplement 2)
PMID:30451685	PBO:0108011	(Figure 3—Figure supplement 2)
PMID:30451685	FYPO:0004247	(Figure 3—Figure supplement 1B)
PMID:30451685	PBO:0108010	(Figure 3—Figure supplement 1A)
PMID:30451685	PBO:0108009	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	PBO:0108009	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	PBO:0108009	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	PBO:0108009	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	PBO:0108009	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	FYPO:0006579	(Figures 2C, 2D, and Figure 2—Figure supplement 2) (comment: same as either single mutant)
PMID:30451685	FYPO:0001245	(Figures 2C, 2D, and Figure 2—Figure supplement 2) (comment: same as either single mutant)
PMID:30451685	FYPO:0000116	(Figures 2C, 2D, and Figure 2—Figure supplement 2) (comment: same as either single mutant)
PMID:30451685	FYPO:0000385	(Figure 2—Figure supplement 1A)
PMID:30451685	PBO:0108008	(Figure 3—Figure supplement 1)
PMID:30451685	FYPO:0004247	(Figure 4C,D)
PMID:30451685	FYPO:0004247	(Figure 4C,D)
PMID:30451685	FYPO:0004247	(Figure 4C,D)
PMID:30451685	FYPO:0004247	(Figure 4C,D)
PMID:30451685	FYPO:0004247	(Figure 4C,D)
PMID:30451685	FYPO:0004247	(Figure 4C,D)
PMID:30451685	FYPO:0006786	(Figure 2D and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0006785	(Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0004247	(Figure 4C,D)
PMID:30451685	PBO:0108009	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	PBO:0108008	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	FYPO:0006784	(Figure 3—Figure supplement 1B, 2B)
PMID:30451685	FYPO:0006784	(Figure 3—Figure supplement 1B, 2B)
PMID:30451685	FYPO:0006786	(Figure 2D and Figure 2—Figure supplement 2)
PMID:30451685	PBO:0108010	(Figure 4B)
PMID:30451685	PBO:0108016	(Figure 4B)
PMID:30451685	PBO:0108016	(Figure 4B)
PMID:30451685	FYPO:0003507	(Figure 2D and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0006785	(Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0003507	(Figure 2D and Figure 2—Figure supplement 2)
PMID:30451685	PBO:0108008	(Figure 4B)
PMID:30451685	FYPO:0006786	(Figure 2D and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0001245	(Figure 4E)
PMID:30451685	FYPO:0000116	(Figure 4E)
PMID:30451685	FYPO:0006784	(Figures 4C and 4D)
PMID:30451685	FYPO:0006785	(Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0003507	(Figure 2D and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0004247	(Figure 2—Figure supplement 1D)
PMID:30451685	FYPO:0006579	(Figures 2C, 2D, and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0001245	(Figures 2C, 2D, and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0000116	(Figures 2C, 2D, and Figure 2—Figure supplement 2)
PMID:30451685	PBO:0108006	(Figures 2A and 2B)
PMID:30451685	FYPO:0006579	(Figures 2C, 2D, and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0001245	(Figures 2C, 2D, and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0000116	(Figures 2C, 2D, and Figure 2—Figure supplement 2)
PMID:30451685	PBO:0108005	(Figures 2A and 2B)
PMID:30451685	GO:0000329	(Figure 1) (direct assay for vacuolar membrane) and Figure 1-Figure supplement 1 (sequence feature evidence for transmembrane)
PMID:30451685	GO:0000329	when SpHfl1 was overexpressed from a strong nmt1 promoter, the cytosolic signal of mYFP-SpAtg8 disappeared and the vacuole membrane localization of mYFP-SpAtg8 became much more conspicuous (Figure 1F).
PMID:30451685	GO:0007033	(Figure 2)
PMID:30462301	PBO:0103855	(Figure 6B and Supplementary Figure S8B)
PMID:30462301	PBO:0100093	(comment: suggested by Junko)
PMID:30462301	PBO:0100089	(Figure 6B and Supplementary Figure S8C)
PMID:30462301	PBO:0103856	(Figure 6B and Supplementary Figure S8B)
PMID:30462301	PBO:0103856	(Figure 6B and Supplementary Figure S8B)
PMID:30462301	PBO:0103856	(Figure 6B and Supplementary Figure S8C))
PMID:30462301	PBO:0103855	(Figure 6B and Supplementary Figure S8B)
PMID:30462301	PBO:0103855	(Figure 6B and Supplementary Figure S8B)
PMID:30462301	GO:0005515	(comment: competatively with lem2)
PMID:30462301	PBO:0103854	(Figure 4F and Supplementary Figure S7F)
PMID:30462301	PBO:0103853	Supplementary Figure S7E
PMID:30462301	PBO:0103853	Supplementary Figure S7E
PMID:30462301	PBO:0103853	(Figure 4A)
PMID:30462301	PBO:0103853	Supplementary Figure S7E
PMID:30462301	PBO:0103852	(Figure 4A)
PMID:30462301	PBO:0103852	(Figure 4A)
PMID:30462301	PBO:0103852	(Figure 4A)
PMID:30462301	GO:0005515	(comment: competatively with sad1)
PMID:30462301	PBO:0103851	(Supplementary Figure S7A-D)
PMID:30462301	FYPO:0001894	(Figure 3)
PMID:30462301	FYPO:0001894	(Figure 3)
PMID:30462301	FYPO:0001894	(Figure 3)
PMID:30462301	FYPO:0001894	(Figure 3)
PMID:30462301	FYPO:0000172	(Figure 3B and Supplementary Figure S6)
PMID:30462301	FYPO:0006366	(Figure 3B and Supplementary Figure S6)
PMID:30462301	FYPO:0000172	(Figure 3B and Supplementary Figure S6)
PMID:30462301	FYPO:0006366	(Figure 3B and Supplementary Figure S6)
PMID:30462301	FYPO:0004791	(Figure 3A)
PMID:30462301	FYPO:0004791	(Figure 3A)
PMID:30462301	FYPO:0004791	(Figure 3A)
PMID:30462301	FYPO:0004791	(Figure 3A)
PMID:30462301	FYPO:0006515	(Supplementary Figure S5B)
PMID:30462301	FYPO:0006515	(Supplementary Figure S5B)
PMID:30462301	FYPO:0006515	(Supplementary Figure S5B)
PMID:30462301	FYPO:0006515	(Supplementary Figure S5B)
PMID:30462301	FYPO:0006515	(Supplementary Figure S5B)
PMID:30462301	PBO:0103848	(Supplementary Figure S4A)
PMID:30462301	PBO:0103848	(Figure 2E and Supplementary Figure S4B)
PMID:30462301	PBO:0103847	Supplementary Figure S4A)
PMID:30462301	PBO:0103847	(Figure S4A)
PMID:30462301	PBO:0103847	(Figure S4A)
PMID:30462301	PBO:0100089	(Figure 2C,D S3A,C)
PMID:30462301	PBO:0100089	(Figure 2C,D S3A,C)
PMID:30462301	PBO:0100089	(Figure 2D S3B,C)
PMID:30462301	PBO:0100089	(Figure 2D S3B,C)
PMID:30462301	PBO:0103846	(Figure 2C S3A,C)
PMID:30462301	PBO:0100089	(Figure 2C S3A,C)
PMID:30462301	PBO:0100089	(Figure 2C S3A,C)
PMID:30462301	PBO:0100088	Supplementary Figure S1A-E
PMID:30463883	FYPO:0002060	(comment: CONDITION at 33 degrees Celsius)
PMID:30463883	FYPO:0002060	(comment: CONDITION at 36 degrees Celsius)
PMID:30463883	FYPO:0006884	The mitotic spindle has two poles but is thicker than normal.
PMID:30463883	PBO:0102981	(Figure 2A,B)
PMID:30463883	FYPO:0002060	(comment: at 36 degrees Celsius)
PMID:30463883	FYPO:0002060	(comment: CONDITION at 36 degrees Celsius)
PMID:30463883	FYPO:0002060	(comment: CONDITION at 36 degrees Celsius)
PMID:30463883	FYPO:0002060	(comment: CONDITION at 36 degrees Celsius)
PMID:30463883	FYPO:0002060	(comment: CONDITION at 33 degrees Celsius)
PMID:30463883	FYPO:0002060	(comment: CONDITION at 33 degrees Celsius)
PMID:30463883	PBO:0102980	(Figure 2A,B)
PMID:30463883	PBO:0102980	(Figure 2A,B)
PMID:30463883	PBO:0102980	(Figure 2A,B)
PMID:30463883	FYPO:0002060	(comment: CONDITION at 33 degrees Celsius)
PMID:30463883	PBO:0102980	(Figure 2A,B)
PMID:30463883	FYPO:0006884	The mitotic spindle has two poles but is thicker than normal.
PMID:30463883	FYPO:0002060	(comment: CONDITION at 36 degrees Celsius)
PMID:30471998	GO:0034314	Dip1 activates Arp2/3 complex to nucleate linear actin filaments analogous to branched actin filaments created by Wsp1-mediated Arp2/3 complex activation. These Dip1-Arp2/3 complex nucleated filaments act as seeds for Wsp1-mediated Arp2/3 complex branching nucleation.
PMID:30475921	FYPO:0006790	(comment: suppresses wtf13 drive)
PMID:30475921	FYPO:0006793	(comment: wtf13 driver, wtf18 suppressor)
PMID:30475921	FYPO:0006793	(comment: wtf13 driver, wtf18 suppressor)
PMID:30475921	FYPO:0006793	(comment: wtf13 driver, wtf18 suppressor)
PMID:30475921	PBO:0092298	(comment: wtf18-2 allele assayed)
PMID:30475921	PBO:0019133	when wtf13 antidote not present (homozygous, wtf13poison/wtf13+, or wtf13poison/wtf13Δ
PMID:30475921	FYPO:0006793	(comment: wtf13 driver, wtf18 suppressor)
PMID:30503780	FYPO:0002687	(Fig. S5B)
PMID:30503780	PBO:0100088	(Fig. 2D)
PMID:30503780	FYPO:0004791	(Figures 5A and 5B)
PMID:30503780	PBO:0100089	(Figure 2D)
PMID:30503780	PBO:0100089	(Figure 2D)
PMID:30503780	PBO:0100089	(Figure 2D)
PMID:30503780	GO:0003677	(Figure 3) (comment: incompatible with rap1 binding)
PMID:30503780	FYPO:0000658	(Fig. 4)
PMID:30503780	FYPO:0000658	(Fig. 4)
PMID:30503780	GO:0005515	(comment: incompatible with DNA binding)
PMID:30503780	FYPO:0005612	(Fig. S5B)
PMID:30503780	FYPO:0005612	(Fig. S5B)
PMID:30503780	FYPO:0002687	(Fig. S5B)
PMID:30503780	FYPO:0004093	(Fig. S5B)
PMID:30503780	FYPO:0004093	(Fig. S5B)
PMID:30503780	FYPO:0004791	(Figures 5A and 5B)
PMID:30503780	FYPO:0004791	(Figures 5A and 5B)
PMID:30503780	PBO:0100090	(Figures 5C)
PMID:30503780	PBO:0100091	(Figures 5C)
PMID:30503780	FYPO:0000590	(comment: transeferred from Junkos session PMID:30462301)
PMID:30503780	FYPO:0000590	((comment: transeferred from Junkos session PMID:30462301)
PMID:30503780	PBO:0100092	((comment: transeferred from Junkos session PMID:30462301)
PMID:30503780	PBO:0100093	((comment: transeferred from Junkos session PMID:30462301)
PMID:30528393	GO:0005829	(comment: although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA)
PMID:30528393	GO:0005739	(comment: although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA)
PMID:30528393	GO:0005829	(comment: although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA)
PMID:30528393	GO:0005739	(comment: although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA)
PMID:30530492	FYPO:0000464	(comment: CHECK glycosphingolipid transport)
PMID:30530492	GO:0140351	(comment: glucosylceramide, galactosylceramide)
PMID:30573453	PBO:0096302	(Fig. 6)
PMID:30573453	FYPO:0003575	(Fig. 5)
PMID:30573453	PBO:0094679	(Figure 2c)
PMID:30573453	PBO:0095652	(Figure 2c)
PMID:30573453	FYPO:0000833	(Figure 2d)
PMID:30573453	FYPO:0000703	(Figure 2d)
PMID:30573453	PBO:0095652	(Figure 3a)
PMID:30573453	FYPO:0002336	(Figure 3a)
PMID:30573453	FYPO:0002336	(Figure 3a)
PMID:30573453	PBO:0094282	(Figure S4)
PMID:30573453	PBO:0094679	(Figure 2c)
PMID:30573453	PBO:0096292	(Figure 4C)
PMID:30573453	PBO:0094679	(Figure 4d)
PMID:30573453	PBO:0096294	(Figure 4c)
PMID:30573453	FYPO:0006814	(Figure 5)
PMID:30573453	FYPO:0003575	(Figure 5)
PMID:30573453	PBO:0096295	(Figure 5)
PMID:30573453	FYPO:0000966	(Figure 5)
PMID:30573453	FYPO:0003574	(Figure 5)
PMID:30573453	PBO:0096296	(Figure 6)
PMID:30573453	PBO:0096297	(Figure 6)
PMID:30573453	FYPO:0003411	(Figure 6)
PMID:30573453	PBO:0095834	(Figure 6)
PMID:30573453	FYPO:0000966	(Figure 6)
PMID:30573453	FYPO:0006814	(Figure 6)
PMID:30573453	FYPO:0000967	(Figure 6)
PMID:30573453	FYPO:0006814	(Figure 6)
PMID:30573453	PBO:0096298	(Figure S8)
PMID:30573453	PBO:0096299	(Figure S8)
PMID:30573453	PBO:0096300	(Figure S8)
PMID:30573453	PBO:0096301	(Figure S8)
PMID:30573453	PBO:0095834	(Fig. 6)
PMID:30573453	PBO:0096189	(Figure S7)
PMID:30573453	PBO:0096189	(Figure S7)
PMID:30573453	PBO:0096188	(Figure S7)
PMID:30573453	PBO:0120551	(Figure 2c)
PMID:30601114	PBO:0101038	(Figure 2B)
PMID:30601114	PBO:0101038	(Figure 2)
PMID:30601114	PBO:0101039	(Figure 2B)
PMID:30601114	GO:1905762	(Figure 1; Figure supplement 1A)
PMID:30601114	PBO:0101033	(Figure 1; Figure supplement 1B,1C)
PMID:30601114	FYPO:0006809	(Figure 2A and Figure 2-Figure supplement 1B-E)
PMID:30601114	FYPO:0006809	(Figure 2A and Figure 2-Figure supplement 1B-E)
PMID:30601114	FYPO:0002134	ADD DOMAIN WHEN SO TERM AVAILABLE Figure 2A and Figure 2-Figure supplement 1B-E
PMID:30601114	PBO:0101039	(Figure 2B)
PMID:30601114	GO:1905762	(Figure 1; Figure supplement 1A)
PMID:30601114	GO:0062104	(comment: PRE element) Figure 1-Figure supplement 1B/Figure 1-Figure supplement 1C
PMID:30601114	PBO:0101034	(Figure 1A and Figure 1-Figure supplement 1D- E)
PMID:30601114	PBO:0101034	(Figure 1A and Figure 1-Figure supplement 1D- E)
PMID:30601114	PBO:0101035	(Figure 1A and Figure 1-Figure supplement 1D- E) (I think it is correct to describe as an enzyme regulator (MF, because it increases processivity.)
PMID:30601114	PBO:0101036	(Figure 1B and Figure 1-Figure supplement 1D-E) (I think it is correct to describe as an enzyme regulator (MF, because it increases processivity.)
PMID:30601114	FYPO:0006809	(Figure 2B)
PMID:30601114	PBO:0101038	(Figure 2B)
PMID:30601114	PBO:0101038	(Figure 2B)
PMID:30601114	PBO:0101038	(Figure 2B)
PMID:30601114	FYPO:0006809	(Figure 2B)
PMID:30601114	FYPO:0006809	(Figure 2B)
PMID:30601114	FYPO:0006809	(Figure 2B)
PMID:30602572	PBO:0109849	We counted 23.3 + 1.4 (mean + S.E.) mitochondria in Klp5Δ/Klp6Δ cells lacking Mmb1Δ (Fig. 6C), which was not significantly different from Mmb1Δ cells
PMID:30602572	FYPO:0000895	(Fig. S5B) Furthermore, in Klp4Δ cells, which typically contain several short mitochondria (Fig. 1A), absence of Dnm1 results in a single large, fused mitochondrion
PMID:30602572	FYPO:0007196	Klp5Δ/Klp6Δ cells exhibited a fission frequency that was half that of WT
PMID:30602572	FYPO:0003820	(Fig. 1C) observed that Klp5Δ/Klp6Δ contained only 2.3 + 0.4 (mean + S.E.).
PMID:30602572	PBO:0096097	(Figure 2C) the mitochondria have a fission frequency that is almost double that of wild-type
PMID:30602572	PBO:0096096	(Figure 1B) the anti-parallel microtubule bundles are only about half the length of wild-type bundles
PMID:30602572	PBO:0096095	(Figure 6B)
PMID:30602572	PBO:0109848	(Figure 1C, 1D)
PMID:30602572	PBO:0109848	(Figure 6C, 6D) Increased mitochondrial numbers and decreased mitochondrial sizes with overall mitochondrial volume same as what is observed in wild-type cells
PMID:30602572	FYPO:0003810	WT cells highly overexpressing Dnm1 had 11.6 + 0.2 mitochondria (mean + S.E.), which is twice that of WT cells
PMID:30626735	PBO:0093630	(comment: CHECK 75 J/m^2; Andres SN et al. (2019))
PMID:30626735	PBO:0101188	(comment: CHECK Andres SN et al. (2019))
PMID:30626735	PBO:0093620	(comment: CHECK 200 Gy; Andres SN et al. (2019))
PMID:30635289	PBO:0092128	Consistent with the previous report (Takahashi et al. 2000), cnp1 mRNA peaks before the transcription of histone H3, $120 min after elutriation, showing an approximately twofold increase. This pattern of expression coincides with the expression of cdc18, a well-known cell cycle-regulated gene expressed specifically in G1 phase (Figure 1A).
PMID:30635289	PBO:0113858	ChIP analysis showed that Nrm1, Yox1, and Res2 bind to the cnp1 promoter (Figure 4B).
PMID:30635289	PBO:0113858	ChIP analysis showed that Nrm1, Yox1, and Res2 bind to the cnp1 promoter (Figure 4B).
PMID:30635289	PBO:0113858	ChIP analysis showed that Nrm1, Yox1, and Res2 bind to the cnp1 promoter (Figure 4B).
PMID:30635289	PBO:0113845	Deletion of nrm1 or yox1 resulted in a $5-6-fold increase in cnp1 mRNA levels, whereas res2 deletion led to a more modest twofold increase (Figure 3A).
PMID:30635289	PBO:0113857	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635289	PBO:0113856	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635289	PBO:0113855	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635289	PBO:0113854	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635289	PBO:0033884	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635289	PBO:0113853	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635289	PBO:0113852	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635289	PBO:0113851	Through the visual screen, we identified that three mutants, nrm1D, yox1D, and res2D, showed abnormal CENP-A distribution patterns (Figure 2A). In these mutants, Cnp1-GFP at centromeres tends to be brighter and also gives a high nucleoplasmic signal (Figure 2A), suggesting an increase in Cnp1-GFP levels.
PMID:30635289	PBO:0113851	Through the visual screen, we identified that three mutants, nrm1D, yox1D, and res2D, showed abnormal CENP-A distribution patterns (Figure 2A). In these mutants, Cnp1-GFP at centromeres tends to be brighter and also gives a high nucleoplasmic signal (Figure 2A), suggesting an increase in Cnp1-GFP levels.
PMID:30635289	PBO:0113851	Through the visual screen, we identified that three mutants, nrm1D, yox1D, and res2D, showed abnormal CENP-A distribution patterns (Figure 2A). In these mutants, Cnp1-GFP at centromeres tends to be brighter and also gives a high nucleoplasmic signal (Figure 2A), suggesting an increase in Cnp1-GFP levels.
PMID:30635289	PomGeneEx:0000018	Cnp1-GFP protein increases approximately twofold at 165-min postelutriation. This resulindicates that the mRNA increase in G1 results in augmentation of the Cnp1 protein level in S phase.
PMID:30635289	PBO:0092128	Consistent with the previous report (Takahashi et al. 2000), cnp1 mRNA peaks before the transcription of histone H3, $120 min after elutriation, showing an approximately twofold increase. This pattern of expression coincides with the expression of cdc18, a well-known cell cycle-regulated gene expressed specifically in G1 phase (Figure 1A).
PMID:30635289	PBO:0092131	Accordingly, the peak of septation matches with the peak of expression of the histone H3 (hht1 gene) as histones are highly expressed during S phase (Figure 1A).
PMID:30635289	PBO:0097102	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635289	PBO:0113847	Through the visual screen, we identified that three mutants, nrm1D, yox1D, and res2D, showed abnormal CENP-A distribution patterns (Figure 2A). In these mutants, Cnp1-GFP at centromeres tends to be brighter and also gives a high nucleoplasmic signal (Figure 2A), suggesting an increase in Cnp1-GFP levels.
PMID:30635289	PBO:0113848	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635289	PBO:0113847	Through the visual screen, we identified that three mutants, nrm1D, yox1D, and res2D, showed abnormal CENP-A distribution patterns (Figure 2A). In these mutants, Cnp1-GFP at centromeres tends to be brighter and also gives a high nucleoplasmic signal (Figure 2A), suggesting an increase in Cnp1-GFP levels.
PMID:30635289	PBO:0113848	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635289	PBO:0113845	Deletion of nrm1 or yox1 resulted in a $5-6-fold increase in cnp1 mRNA levels, whereas res2 deletion led to a more modest twofold increase (Figure 3A).
PMID:30635289	PBO:0113847	Through the visual screen, we identified that three mutants, nrm1D, yox1D, and res2D, showed abnormal CENP-A distribution patterns (Figure 2A). In these mutants, Cnp1-GFP at centromeres tends to be brighter and also gives a high nucleoplasmic signal (Figure 2A), suggesting an increase in Cnp1-GFP levels.
PMID:30635402	PBO:0106862	(comment: also assayed directly using human CKII)
PMID:30635402	FYPO:0000228	(comment: ICRF-193, a bisdioxopiperazine derivative [meso-4,4-(2,3-butanediyl)-bis (2,6-piperazinedione)], is a catalytic topo II inhibitor)
PMID:30635402	FYPO:0005739	This phenotype is observed in the presence of ICRF-193, a bisdioxopiperazine derivative [meso-4,4-(2,3-butanediyl)-bis (2,6-piperazinedione)], a catalytic topo II inhibitor.
PMID:30635402	PBO:0108715	These phosphorylation sites were identified by the phos-tag analysis, phospho-specific antibodies, and in vitro phosphorylation assay
PMID:30639107	FYPO:0001877	(Fig. 1B)
PMID:30639107	FYPO:0006616	(Fig. 1B)
PMID:30639107	PBO:0096314	(Fig. 1C)
PMID:30639107	PBO:0102525	(Fig. 1C)
PMID:30639107	PBO:0114674	(Fig. 1C)
PMID:30639107	PBO:0114675	(Fig. 1C)
PMID:30639107	PBO:0096311	(Fig. 1E)
PMID:30639107	PBO:0096312	(Fig. 1E)
PMID:30639107	PBO:0098148	(Fig. 1E)
PMID:30639107	PBO:0114676	(Fig. 1E)
PMID:30639107	PBO:0114676	(Fig. 1E)
PMID:30639107	PBO:0114676	(Fig. 1E)
PMID:30639107	PBO:0114676	(Fig. 1E)
PMID:30639107	PBO:0114677	(Fig. 1E)
PMID:30639107	PBO:0114678	(Fig. 1E)
PMID:30639107	PBO:0114679	(Fig. 1E)
PMID:30639107	FYPO:0001392	(Fig. 3)
PMID:30640914	PBO:0102476	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	PBO:0103591	(comment: Recombination assay; assayed region: leu1-his5 interval)
PMID:30640914	PBO:0103592	(comment: mbs1 hotspot quantification)
PMID:30640914	PBO:0103593	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	PBO:0103594	(comment: Recombination assay; assayed region: leu1-his5 interval)
PMID:30640914	PBO:0103592	(comment: mbs1 hotspot quantification)
PMID:30640914	PBO:0103595	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	PBO:0103596	(comment: Recombination assay; assayed region: leu1-his5 interval)
PMID:30640914	PBO:0103597	(comment: mbs1 hotspot quantification)
PMID:30640914	PBO:0103598	(comment: mbs1 hotspot quantification)
PMID:30640914	FYPO:0006838	(comment: Rec25 visualization)
PMID:30640914	FYPO:0006838	(comment: Rec25 visualization)
PMID:30640914	PBO:0103599	(comment: Cellular fractionation; affecting Rec25)
PMID:30640914	PBO:0103599	(comment: Cellular fractionation; affecting Rec25)
PMID:30640914	PBO:0103592	(comment: mbs1 hotspot quantification)
PMID:30640914	PBO:0103595	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	PBO:0103596	(comment: Recombination assay; assayed region: leu1-his5 interval)
PMID:30640914	PBO:0103598	(comment: mbs1 hotspot quantification)
PMID:30640914	FYPO:0006838	(comment: Rec25 visualization)
PMID:30640914	PBO:0103599	(comment: Cellular fractionation; affecting Rec25)
PMID:30640914	PBO:0103595	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	PBO:0103595	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	PBO:0103595	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	PBO:0102476	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	PBO:0102476	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	PBO:0103593	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	PBO:0103593	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	PBO:0103593	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	PBO:0102476	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	PBO:0102476	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	PBO:0102476	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	FYPO:0004993	(Figure S1A)
PMID:30640914	FYPO:0004993	(Figure S1A)
PMID:30640914	FYPO:0004993	(Figure S1A)
PMID:30640914	FYPO:0000581	(Figure S1A)
PMID:30640914	FYPO:0004628	(Figure S2)
PMID:30640914	FYPO:0004628	(Figure S2)
PMID:30640914	FYPO:0005650	(Figure S2)
PMID:30640914	PBO:0103598	(comment: mbs1 hotspot quantification
PMID:30640914	FYPO:0004610	(Fig. 8)
PMID:30640914	FYPO:0005650	(Figure S4)
PMID:30640914	FYPO:0004610	(Fig. 8)
PMID:30640914	FYPO:0005650	(Fig. S4)
PMID:30640914	FYPO:0006841	(Figure S2)
PMID:30640914	FYPO:0004993	(Figure S1)
PMID:30646830	PBO:0095187	Abolished tRNA cytosine-5 methylation of C49 and C50 (comment: tRNA bisulphite sequencing)
PMID:30646830	GO:0016428	trm402 (Trm4b) methylates C49 and C50 of tRNAs
PMID:30646830	PBO:0095187	abolished tRNA C34, C48 methylation (comment: trna bisulphite sequencing)
PMID:30646830	GO:0016428	trm401 (Trm4a) methylates C34 of tRNA-Leu (CAA) and tRNA-Pro (CGG) as well as all C48 tRNA methylation sites. Methylates C34 only on intron-containing tRNA.
PMID:30649994	FYPO:0006896	(Fig. 3E)
PMID:30649994	PBO:0108066	(Fig. 3E)
PMID:30649994	PBO:0108066	(Fig. 3E)
PMID:30649994	PBO:0108065	(Fig. S3)
PMID:30649994	GO:0070300	Supplemental Figure S2
PMID:30649994	GO:1901612	Supplemental Figure S2
PMID:30649994	FYPO:0006896	(Fig. 3E)
PMID:30649994	PBO:0018826	(Fig. 4b)
PMID:30652128	PBO:0103454	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0103454	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0103454	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0103455	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0103455	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0103455	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0103456	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096842	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096842	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096842	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096839	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096839	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096838	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096842	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096839	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096839	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096839	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096842	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096838	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0006811	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096842	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096842	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096842	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0006810	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0094685	tfs1∆ reduced centromere noncoding RNA in the clr4∆ strain. (comment: Northern blot assay)
PMID:30652128	PBO:0094685	rpd1-S7A reduced centromere noncoding RNA in the clr4∆ strain. (comment: Northern blot assay)
PMID:30652128	FYPO:0006811	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	rpd1-S7A increased the rate of gross chromosomal rearrangement in the otherwise wild-type background. (comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096838	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096839	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096838	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096838	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096838	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096838	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096838	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096838	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0006811	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096839	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096839	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096842	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096838	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096842	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001742	(comment: Pulse-field gel electrophoresis (PFGE), Polymerase chain reaction (PCR), Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001742	(comment: Pulse-field gel electrophoresis (PFGE), Polymerase chain reaction (PCR), Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001742	(comment: Pulse-field gel electrophoresis (PFGE), Polymerase chain reaction (PCR), Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096838	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0006811	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0006811	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0006811	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096839	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096842	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0006811	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0006811	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096842	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0006811	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0096839	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	PBO:0093563	(comment: Monitoring an extra-chromosome ChL)
PMID:30658998	FYPO:0006914	(Fig. 1B)
PMID:30658998	FYPO:0003810	(Fig. 1C)
PMID:30658998	FYPO:0003769	(Fig. 1D)
PMID:30658998	FYPO:0002061	(Fig. 1B)
PMID:30658998	FYPO:0006910	(Fig. 1B)
PMID:30658998	FYPO:0003810	(Fig. 1C) (comment: supressed by hexestrol)
PMID:30658998	FYPO:0003769	(Fig. 1D) (comment: supressed by hexestrol or clomifene)
PMID:30658998	FYPO:0006034	(comment: supressed dna fragmentation)
PMID:30658998	FYPO:0006034	(comment: supressed dna fragmentation)
PMID:30658998	FYPO:0006911	(Fig. 1B)
PMID:30658998	FYPO:0006913	(Fig. 1B)
PMID:30658998	FYPO:0001355	(Fig. 1B)
PMID:30659798	GO:0008017	(Fig. 2)
PMID:30659798	GO:0003777	(Fig. 2f)
PMID:30667359	FYPO:0007006	(Figure 6C)
PMID:30667359	FYPO:0007007	(Figure 6c)
PMID:30667359	FYPO:0006920	(Figure 6B)
PMID:30667359	FYPO:0007005	(Figure 6C)
PMID:30667359	FYPO:0006920	(Figure 6B)
PMID:30667359	FYPO:0007005	(Figure 6C)
PMID:30667359	FYPO:0000167	(Figure 2B)
PMID:30667359	FYPO:0006920	(Figure 2B)
PMID:30667359	FYPO:0007005	(Figure 2B)
PMID:30667359	FYPO:0007006	(Figure 6C)
PMID:30667359	FYPO:0007006	(Figure 6C)
PMID:30667359	FYPO:0007005	(Figure 2B)
PMID:30667359	FYPO:0007007	(Figure 6C)
PMID:30715423	PBO:0102225	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
PMID:30715423	PBO:0102227	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
PMID:30715423	PBO:0102221	(comment: No queuosine-mediated reduction of translational errors at GGC (Gly) and UGC (Tyr) codons)
PMID:30715423	PBO:0102222	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
PMID:30715423	PBO:0102223	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
PMID:30715423	PBO:0102224	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
PMID:30715423	GO:1990145	... Q-modification in tRNAs is to improve translation ofC-ending codons relative to U-ending codons in S. pombe.
PMID:30715423	PBO:0102226	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
PMID:30726745	PBO:0095263	(Figure S5)
PMID:30726745	FYPO:0001045	(Figure 7A)
PMID:30726745	FYPO:0001903	(Figure 7C, 7D)
PMID:30726745	FYPO:0001903	(Figure 7C, 7D)
PMID:30726745	FYPO:0003267	(Figure 7A)
PMID:30726745	PBO:0095262	(Figure 2, Figure 3)
PMID:30726745	PBO:0095261	(Figure 1)
PMID:30726745	PBO:0095262	(Figure 2, Figure 3)
PMID:30726745	GO:1902716	(Figure 6)
PMID:30726745	FYPO:0001045	(Figure 7A)
PMID:30726745	FYPO:0001903	(Figure 7C, 7D)
PMID:30726745	PBO:0095263	(Figure 7C, 7D)
PMID:30726745	FYPO:0001045	(Figure 7A)
PMID:30759079	FYPO:0002256	data not shown
PMID:30759079	FYPO:0006927	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006927	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006927	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006927	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006927	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006927	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006927	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006927	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006927	(Fig. 6) The nuclear envelope is marked with Cut11-GFP
PMID:30759079	FYPO:0002256	data not shown
PMID:30759079	FYPO:0002256	data not shown
PMID:30759079	FYPO:0006927	(Fig. 6) The nuclear envelope is marked with Cut11-GFP
PMID:30759079	FYPO:0006927	(Fig. 6) The nuclear envelope is marked with Cut11-GFP
PMID:30759079	FYPO:0006926	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759238	PBO:0112928	(Fig. S6B)
PMID:30759238	FYPO:0001357	(Fig. S6C)
PMID:30759238	FYPO:0001357	(Fig. S6C)
PMID:30759238	FYPO:0001357	(Fig. S6C)
PMID:30759238	FYPO:0001357	(Fig. S6C)
PMID:30759238	PBO:0093560	(Fig. S6C)
PMID:30759238	PBO:0093560	(Fig. S6C)
PMID:30759238	FYPO:0001357	(Fig. S6D)
PMID:30759238	FYPO:0001357	(Fig. S6D)
PMID:30759238	FYPO:0001357	(Fig. S6D)
PMID:30759238	FYPO:0001357	(Fig. S6D)
PMID:30759238	FYPO:0001357	(Fig. S6D)
PMID:30759238	FYPO:0001357	(Fig. S6D)
PMID:30759238	FYPO:0001357	(Fig. S6D)
PMID:30759238	FYPO:0001357	(Fig. S6D)
PMID:30759238	PBO:0112927	(Fig. S9B)
PMID:30759238	PBO:0112926	(Fig. S9B)
PMID:30759238	PBO:0112929	(Fig. S6B)
PMID:30759238	PBO:0112929	(Fig. S6B)
PMID:30759238	PBO:0112926	(Fig. 3B)
PMID:30759238	PBO:0112933	(Fig. 6)
PMID:30759238	PBO:0112932	(Fig. 6)
PMID:30759238	PBO:0093560	(Fig. S6D)
PMID:30759238	PBO:0093560	(Fig. S6D)
PMID:30759238	PBO:0093561	(Fig. S6D)
PMID:30759238	PBO:0093561	(Fig. S6D)
PMID:30759238	FYPO:0000472	(Fig. S9B)
PMID:30759238	PBO:0112927	(Fig. S9B)
PMID:30759238	PBO:0112929	(Fig. S6B)
PMID:30759238	PBO:0112929	(Fig. S6B)
PMID:30759238	PBO:0112928	(Fig. S6B)
PMID:30759238	PBO:0112928	(Fig. S6B)
PMID:30759238	PBO:0112928	(Fig. S6B)
PMID:30759238	PBO:0112928	(Fig. S6B)
PMID:30759238	FYPO:0001357	(Fig. S6C)
PMID:30759238	FYPO:0003353	(Fig. 3C)
PMID:30759238	PBO:0112927	(Fig. 4B)
PMID:30759238	PBO:0112927	(Fig. 4B)
PMID:30759238	FYPO:0001357	(Fig. S6D)
PMID:30759238	FYPO:0001357	(Fig. S6D)
PMID:30759238	FYPO:0001357	(Fig. S6D)
PMID:30759238	FYPO:0001357	(Fig. S6D)
PMID:30759238	PBO:0093560	(Fig. S6D)
PMID:30759238	PBO:0093560	(Fig. S6D)
PMID:30759238	FYPO:0003353	(Fig. 3C)
PMID:30759238	FYPO:0003353	(Fig. 3C)
PMID:30759238	FYPO:0003353	(Fig. 3C)
PMID:30759238	FYPO:0003353	(Fig. 3C)
PMID:30759238	PBO:0112928	(Fig. 4B)
PMID:30759238	PBO:0112930	(Fig. 4D)
PMID:30759238	FYPO:0003353	(Fig. 4D)
PMID:30759238	FYPO:0003353	(Fig. 4D)
PMID:30759238	PBO:0112928	(Fig. 4B)
PMID:30759238	PBO:0112928	(Fig. 4B)
PMID:30759238	PBO:0093560	(Fig. S6D)
PMID:30759238	PBO:0093560	(Fig. S6D)
PMID:30759238	PBO:0112929	(Fig. 4B)
PMID:30759238	PBO:0112930	(Fig. 4D)
PMID:30759238	PBO:0112930	(Fig. 4D)
PMID:30759238	PBO:0112930	(Fig. 4D)
PMID:30759238	PBO:0117199	(Fig. 5)
PMID:30759238	FYPO:0003353	(Fig. 3C)
PMID:30759238	PBO:0112929	(Fig. 3B)
PMID:30759238	PBO:0112929	(Fig. 3B)
PMID:30759238	PBO:0112928	(Fig. 3B)
PMID:30759238	PBO:0112927	(Fig. 3B)
PMID:30759238	PBO:0112926	(Fig. 3B)
PMID:30759238	PBO:0112926	(Fig. S6B)
PMID:30773398	PBO:0101843	(Figs 1B, 1D, 1F, S1, S2)
PMID:30773398	FYPO:0006858	(Figure S2)
PMID:30773398	PBO:0101842	(Figs 1B, 1D, 1F, S1, S2)
PMID:30773398	PBO:0101841	(Figs 1B, 1D, 1F, S1, S2)
PMID:30773398	GO:0005737	(Fig. 1a)
PMID:30773398	GO:0005634	(Fig. 1a)
PMID:30773398	FYPO:0006858	(Figure S2)
PMID:30773398	FYPO:0006857	(Figure 1E)
PMID:30773398	FYPO:0006857	(Figure 1E)
PMID:30773398	FYPO:0006858	(Figure S2)
PMID:30773398	FYPO:0006858	(Figure S2)
PMID:30773398	FYPO:0006858	(Figure S2)
PMID:30773398	FYPO:0002919	(Figure 1E)
PMID:30773398	GO:0046975	(Figs 1C, S1)
PMID:30773398	FYPO:0006858	(Figure S2)
PMID:30773398	FYPO:0002919	(Figure 1E)
PMID:30773398	PBO:0033658	(Fig. 3)
PMID:30773398	GO:0005515	(comment: CHECK homodimer)
PMID:30796050	PBO:0093632	(Fig. S2)
PMID:30796050	PBO:0104041	(comment: also inferred from orthology and various genetic interactions)
PMID:30796050	PBO:0093634	(Fig. EV3) restrictive temperature for cdc2-M68
PMID:30796050	PBO:0104039	(Fig. EV3)
PMID:30796050	PBO:0104037	(Fig. EV3)
PMID:30796050	PBO:0097410	(Fig. 3)
PMID:30796050	PBO:0093636	(Fig. 2)
PMID:30796050	PBO:0093636	(Fig. 1)
PMID:30796050	PBO:0093634	(Fig. 4)
PMID:30796050	PBO:0093634	(Fig. 1)
PMID:30796050	PBO:0093632	(Fig. S3)
PMID:30796050	PBO:0093632	(Fig. S3)
PMID:30796050	PBO:0093632	(Fig. S3)
PMID:30796050	PBO:0093632	(Fig. S3)
PMID:30796050	PBO:0093632	(Fig. S3)
PMID:30796050	PBO:0093632	(Fig. S3)
PMID:30796050	PBO:0093632	(Fig. 4)
PMID:30796050	PBO:0093632	(Fig. 4)
PMID:30796050	PBO:0093632	(Fig. 3)
PMID:30796050	PBO:0093632	(Fig. 2)
PMID:30796050	PBO:0093632	(Fig. 2)
PMID:30796050	PBO:0093632	(Fig. S2)
PMID:30796050	PBO:0102806	(Fig. EV2)
PMID:30796050	PBO:0102806	(Fig. S2)
PMID:30796050	PBO:0102806	(Fig. S2)
PMID:30796050	PBO:0102806	(Fig. S1)
PMID:30796050	PBO:0102806	(Fig. S1)
PMID:30796050	PBO:0102806	(Fig. 1)
PMID:30796050	PBO:0093632	(Fig. 1)
PMID:30796050	PBO:0104038	(Fig. 4)
PMID:30796050	PBO:0097407	(Fig. 4)
PMID:30796050	FYPO:0006860	(Fig. 3) (comment: less intense Y arc in 2D gel)
PMID:30796050	FYPO:0006859	(Fig. 3) (comment: less intense Y arc in 2D gel)
PMID:30796050	PBO:0104037	(Fig. 3)
PMID:30796050	FYPO:0005402	(Fig. 2, S2)
PMID:30796050	PBO:0104036	(Fig. 2)
PMID:30796050	PBO:0095229	(Fig. 1)
PMID:30796050	PBO:0104035	(Fig. 1)
PMID:30796050	PBO:0093632	(Fig. 1)
PMID:30806623	FYPO:0005342	(Fig. 6)
PMID:30806623	FYPO:0005343	(Fig. 3)
PMID:30806623	FYPO:0005706	(Fig. 3)
PMID:30806623	PBO:0097932	(Fig. 6)
PMID:30806623	FYPO:0007958	(Fig. 5)
PMID:30806623	FYPO:0007958	(Fig. 1)
PMID:30806623	FYPO:0003268	(Fig. 1)
PMID:30806623	FYPO:0001492	(Fig. 1)
PMID:30806623	FYPO:0000648	(Fig. 1)
PMID:30806623	FYPO:0004310	(Fig. 1)
PMID:30806623	FYPO:0004310	(Fig. 1)
PMID:30806623	FYPO:0005342	(Fig. 6)
PMID:30806623	FYPO:0005342	(Fig. 6)
PMID:30806623	FYPO:0005343	(Fig. 6)
PMID:30810475	PBO:0103147	(Fig. 6)
PMID:30810475	GO:0016887	In vitro RNA helicase activity using recombinant protein encoded by the helicase domain of Prp16
PMID:30810475	FYPO:0004742	(Fig. 7)
PMID:30810475	FYPO:0003412	(Fig. 7)
PMID:30810475	FYPO:0003412	(Fig. 7)
PMID:30810475	PBO:0103152	(Fig. 7)
PMID:30810475	PBO:0103151	(Fig. 7)
PMID:30810475	PBO:0103152	(Fig. S6, 7)
PMID:30810475	PBO:0103151	(Fig. S6, 7)
PMID:30810475	PBO:0103150	(Fig. S6, 7)
PMID:30810475	PBO:0103149	(Fig. S6, 7)
PMID:30810475	FYPO:0000091	(Fig. 7)
PMID:30810475	FYPO:0001919	(Fig. 7) (comment: CHECK they say fragmented nucleus but they stained chromosomes, not nuclear envelope)
PMID:30810475	FYPO:0000229	(Fig. 7)
PMID:30810475	FYPO:0001917	(Fig. 7)
PMID:30810475	PBO:0103148	(Fig. 6)
PMID:30810475	PBO:0103146	(Fig. 4)
PMID:30810475	PBO:0095406	(Fig. 4)
PMID:30810475	FYPO:0001355	(Fig. 4)
PMID:30810475	PBO:0100020	(Fig. 4)
PMID:30810475	PBO:0100020	(Fig. 4)
PMID:30810475	PBO:0093556	(Fig. 1)
PMID:30810475	PBO:0093557	(Fig. 1)
PMID:30810475	FYPO:0002061	(Fig. 1)
PMID:30810475	PBO:0103145	(Fig. 1b) for dga1 normal splicing of inton 3, abnormal intron 2, Fig. S4
PMID:30810475	PBO:0103144	(Fig. 1b) for dga1 normal splicing of inton 3, abnormal intron 2, Fig. S4
PMID:30810475	PBO:0095902	(Fig. 1b) for dga1 normal splicing of inton 3, abnormal intron 2, Fig. S4
PMID:30810475	PBO:0103143	(Fig. 1b) for dga1 normal splicing of inton 3, abnormal intron 2, Fig. S4
PMID:30810475	PBO:0095406	(Fig. 1b) for dga1 normal splicing of inton 3, abnormal intron 2, Fig. S4
PMID:30810475	PBO:0103142	(Fig. 1b)
PMID:30810475	PBO:0098392	(Fig. 1b)
PMID:30810475	PBO:0100020	(Fig. 1b)
PMID:30810475	PBO:0095406	(Fig. 1b)
PMID:30810475	FYPO:0000082	(Fig. 1)
PMID:30810475	FYPO:0000082	(Fig. 1)
PMID:30810475	FYPO:0000674	(Fig. 1)
PMID:30810475	FYPO:0001357	(Fig. 1)
PMID:30810475	FYPO:0002141	(Fig. 1)
PMID:30810475	PBO:0103141	(comment: Required for splicing of introns with strong 5' splice site - U6 snRNA and branch site - U2 snRNA interactions)
PMID:30810475	GO:0045292	Required for the splicing of several genome-wide transcripts. Inferred from transcriptome sequencing of the mutant strain prp16F528S. Splicing defects in transcripts validated by RT-PCR assays.
PMID:30810475	GO:0034458	In vitro RNA helicase activity using recombinant protein encoded by the helicase domain of Prp16
PMID:30840879	PBO:0097517	(Fig. 1B)
PMID:30840879	PBO:0096613	(Fig. 2A, Figure 2A)
PMID:30840879	PBO:0097517	(Fig. 1B)
PMID:30840879	PBO:0097518	(Figure 2A)
PMID:30840879	PBO:0096613	(Fig. 3e)
PMID:30840879	PBO:0097517	(Fig. 3e)
PMID:30840879	PBO:0097517	(Fig. 3e)
PMID:30840879	PBO:0097519	(Fig. 3c)
PMID:30840879	PBO:0097520	(Fig. 3c)
PMID:30840879	PBO:0097520	(Fig. 3c)
PMID:30840879	PBO:0097521	(Fig. 2b)
PMID:30840879	PBO:0097535	(comment: CHECK F-BAR/BAR domain adaptors) Rng10(751-950) interacts directly with the Rga7 F-BAR domain
PMID:30840879	GO:0005546	(comment: CHECK MEMBRANE LIPID BINDING) Rga7 F-BAR preferred membranes rich in PI(4)P and PI(4,5)P2 (Figure 3D)
PMID:30840879	GO:0070273	(comment: CHECK MEMBRANE LIPID BINDING) Rga7 F-BAR preferred membranes rich in PI(4)P and PI(4,5)P2 (Figure 3D)
PMID:30840879	PBO:0097538	(Figure 2A)
PMID:30840879	PBO:0097537	(Fig. 2b) (comment: CHECK normal lipid binding)
PMID:30840879	PBO:0097536	(Fig. 1F)
PMID:30840879	PBO:0097536	Defining the Rga7-binding motif within Rng10 further, we found that Rng10(751-950) bound Rga7(1-320) with a similar Kd of 0.69 μM (Figures 1F, 1G, and S2B)
PMID:30840879	PBO:0097536	To test for a direct interaction, we performed in vitro binding assays using recombinant Rng10 C terminus and the Rga7 F-BAR (Figures 1D and S2A). GST- Rng10(751-1,038) efficiently bound His6-Rga7(1-320) with a dissociation constant (Kd) of 0.43 μM (Figures 1D, 1E, and S2B).
PMID:30840879	PBO:0097534	GFP-Rga7(277-695) alone, lacking the majority of the F-BAR domain, could not localize to the PM, resulting in massive cell lysis
PMID:30840879	PBO:0097524	(Fig. 4)
PMID:30853434	FYPO:0003210	(Figure 4G) (comment: live cell DIC)
PMID:30853434	PBO:0094418	(Figure 4A, 4B) (comment: live cell imaging)
PMID:30853434	FYPO:0005905	(Figure 3A, 3B) (comment: Live-cell time-lapse imaging)
PMID:30853434	PBO:0094433	(Fig. 1D)
PMID:30853434	PBO:0024047	(Fig. 1D)
PMID:30853434	PBO:0018677	(Fig. 1D)
PMID:30853434	FYPO:0007474	(Figure 4E) ((comment: moved from wee) (skewed towards small, low severity))
PMID:30853434	PBO:0094414	increased binding by about 2 fold from Figure 4C, 4D
PMID:30853434	PBO:0094415	(Figure 3A, 3B) (comment: Live-cell time-lapse imaging)
PMID:30853434	PBO:0094416	(Figure 1D-G) (comment: live cell imaging)
PMID:30853434	PBO:0094417	(Figure 2A, 2B) ((comment: vw changed to cell division site during M-phase from septum) (live cell imaging))
PMID:30853434	FYPO:0002873	(Figure 3D) (comment: live cell DIC)
PMID:30853434	PBO:0094420	(Figure S4C, S4D)
PMID:30853434	FYPO:0003481	(Figure S4F, S4G) (comment: (vw move to FYPO:0006822 and requested parentage fix in FYPO) (live cell DIC))
PMID:30853434	FYPO:0003481	(Figure S4F, S4G) (comment: (vw move to FYPO:0006822 and requested parentage fix in FYPO) (live cell DIC))
PMID:30853434	FYPO:0006822	(Figure S4F, S4H) (comment: live cell DIC)
PMID:30853434	PBO:0094419	(Figure 2E, 2F) (comment: live cell imaging)
PMID:30853434	FYPO:0003210	(Figure 3C, 3D) (comment: live cell DIC)
PMID:30853434	PBO:0094431	(Figure 1H, 1I) (comment: live cell imaging)
PMID:30853434	PBO:0094432	(Figure S3C, S3D) (comment: live cell imaging)
PMID:30853434	PBO:0094432	(Figure S3A) (comment: live cell imaging)
PMID:30853434	PBO:0094431	(Figure S4A) (comment: live cell imaging)
PMID:30853434	PBO:0094431	(Figure S4A) (comment: live cell imaging)
PMID:30853434	FYPO:0006822	(Figure S4F, S4H) (comment: (vw move to FYPO:0006822 and requested parentage fix in FYPO) (live cell DIC))
PMID:30853434	FYPO:0003481	(Figure S4G) (comment: (vw moved down to FYPO:0003481) (live cell DIC))
PMID:30853434	PBO:0094435	(Figure S4A)
PMID:30853434	PBO:0094434	(Fig. 2E, 2F)
PMID:30853434	FYPO:0003481	(Figure 4H) (comment: (vw moved down to FYPO:0003481) (live cell DIC))
PMID:30853434	FYPO:0003439	(Figure 4G) (comment: live cell DIC)
PMID:30853434	FYPO:0001223	(Figure 4G) (comment: live cell DIC)
PMID:30853434	FYPO:0003210	(Figure 4G) (comment: live cell DIC)
PMID:30853434	FYPO:0003210	(Figure 4I) (comment: Live-cell time-lapse imaging)
PMID:30853434	FYPO:0001365	(Figure 3A, 3B) (comment: Live-cell time-lapse imaging)
PMID:30853434	PBO:0094430	(Figure S1)
PMID:30853434	PBO:0094430	(Figure S1)
PMID:30853434	PBO:0094430	(Figure S1)
PMID:30853434	PBO:0094430	(Figure S1)
PMID:30853434	PBO:0094430	(Figure S1)
PMID:30853434	PBO:0094430	(Figure S1)
PMID:30853434	PBO:0094429	(Figure S3C, S3D) (comment: live cell imaging)
PMID:30853434	PBO:0094428	(Figure S3A) (comment: live cell imaging)
PMID:30853434	PBO:0094427	(Figure S2C) (comment: live cell imaging)
PMID:30853434	PBO:0094426	(Figure S2A, S2B) (comment: live cell imaging)
PMID:30853434	PBO:0094425	(Figure S2A, S2B) (comment: (vw changed from FYPO:0001677 to FYPO:0002874 to match rlc1) (live cell imaging))
PMID:30853434	PBO:0094424	(Figure S2A, S2B) (comment: (vw changed from FYPO:0001677 to FYPO:0002874 to match rlc1) (live cell imaging))
PMID:30853434	PBO:0094423	(Figure S2A, S2B) (comment: (vw changed from FYPO:0001677 to FYPO:0002874 to match rlc1) (live cell imaging))
PMID:30853434	PBO:0094422	(Figure 1C)
PMID:30853434	PBO:0094421	(Figure 1H, 1I) (comment: live cell imaging)
PMID:30853434	FYPO:0002873	(Figure 3C,D)
PMID:30862564	FYPO:0003125	(comment: converted from bp by cc)
PMID:30862564	FYPO:0003125	(comment: converted from bp by cc)
PMID:30967422	PBO:0104187	(Figure 2b)
PMID:30967422	PBO:0104186	(Figure 2b)
PMID:30967422	PBO:0104185	(Figure 2b)
PMID:30967422	PBO:0104182	(Figure 2b)
PMID:30973898	PBO:0093562	(Figure 5A)
PMID:30973898	PBO:0095942	(Figure 5A)
PMID:30973898	PBO:0095942	(Figure 5A)
PMID:30973898	PBO:0105559	(Figure S2B)
PMID:30973898	PBO:0105558	(Figure S2A)
PMID:30973898	PBO:0095942	(Figure 5A)
PMID:30973898	PBO:0095942	(Figure 5A)
PMID:30973898	PBO:0095942	(Figure 5A)
PMID:30973898	PBO:0105564	(Figure 4C)
PMID:30973898	PBO:0105564	(Figure 4C)
PMID:30973898	FYPO:0002061	(Figure 3A)
PMID:30973898	FYPO:0002059	(Figure 3A)
PMID:30973898	PBO:0093562	(Figure 3A)
PMID:30973898	PBO:0095942	(Figure 3A)
PMID:30973898	PBO:0102086	(Figure 2D)
PMID:30973898	PBO:0105563	(Figure 2D)
PMID:30973898	PBO:0105562	(Figure 2D)
PMID:30973898	PBO:0022298	(Figure 2D)
PMID:30973898	FYPO:0002061	(Figure 2C)
PMID:30973898	PBO:0093562	(Figure 2C)
PMID:30973898	PBO:0095942	(Figure 2C)
PMID:30973898	PBO:0095942	(Figure 2C)
PMID:30973898	PBO:0105560	(Figure 2B) (comment: (two hybrid))
PMID:30973898	PBO:0105560	(Figure 2B) (comment: (two hybrid))
PMID:30973898	PBO:0105561	(Figure 2B) (comment: (two hybrid))
PMID:30973898	PBO:0105560	(Figure 2B) (comment: (two hybrid))
PMID:30973898	PBO:0105559	(Figure S2B)
PMID:30973898	PBO:0105558	(Figure S2A)
PMID:30973898	PBO:0095942	(Figure 3A)
PMID:30973898	PBO:0093562	(Fig. 1D)
PMID:30973898	PBO:0093562	(Fig. 1D)
PMID:30973898	FYPO:0000964	(Figure 1B)
PMID:30973898	PBO:0105557	mini-chromosome Ch16 loss assay
PMID:30973898	PBO:0105556	(Figure 4C) mini-chromosome Ch16 loss assay
PMID:30973898	FYPO:0000229	(Figure 4) DAPI staining
PMID:30973898	FYPO:0001214	(Figure 1A)
PMID:30973898	FYPO:0000107	(Figure 1A)
PMID:30973898	PBO:0093567	(Figure 1A)
PMID:30973898	PBO:0093564	(Figure 1A)
PMID:30973898	FYPO:0005947	(Figure 1A)
PMID:30973898	FYPO:0003809	(Figure 1A)
PMID:30973898	FYPO:0001686	(Figure 1A)
PMID:30973898	FYPO:0000964	(Figure 1A)
PMID:30973898	PBO:0093564	(Figure 1B)
PMID:30975915	FYPO:0002061	(Figure 3)
PMID:30975915	FYPO:0002061	(Figure 1)
PMID:30975915	FYPO:0002061	(Figure 3)
PMID:30975915	FYPO:0001234	(Fig. 4A)
PMID:30975915	FYPO:0000088	(Fig. 4B)
PMID:30975915	FYPO:0002061	(Fig. 2B)
PMID:30975915	FYPO:0002061	(Figure 3)
PMID:30975915	FYPO:0002061	(Figure 1A)
PMID:30975915	FYPO:0001357	(Figure 1)
PMID:30975915	FYPO:0002061	(Figure 1)
PMID:30975915	FYPO:0002061	(Figure 1)
PMID:30975915	FYPO:0002360	(Fig. 4)
PMID:30975915	FYPO:0001839	(Fig. 4)
PMID:30975915	FYPO:0000963	(Fig. 4B)
PMID:30975915	FYPO:0000088	(Fig. 4B)
PMID:30992049	PBO:0093615	(comment: hhf2 and hhf3 are wild-type. Only hhf2 is mutated)
PMID:30992049	PBO:0093615	(comment: hhf2 and hhf3 are wild-type. Only hhf2 is mutated)
PMID:30992049	PBO:0093615	(comment: hhf1 and hhf3 are wild-type. Only hhf2 is mutated)
PMID:30992049	PBO:0093617	(comment: hhf1 and hhf3 are wild-type. Only hhf2 is mutated)
PMID:30992049	FYPO:0002550	(comment: hhf1 and hhf3 are wild-type. Only hhf2 is mutated)
PMID:30992049	FYPO:0000095	(comment: hhf1 and hhf3 are wild-type. Only hhf2 is mutated)
PMID:30992049	FYPO:0000085	(comment: grows normally at 25 degrees but not at 30 degrees)
PMID:30992049	FYPO:0001355	grows normally at 25 degrees but not at 30 degrees
PMID:30992049	PBO:0093613	(comment: grows normally at 25 degrees but not at 30 degrees)
PMID:30992049	PBO:0093617	(comment: same as swi1delta alone)
PMID:30992049	PBO:0093614	(comment: grows normally at 25 degrees but not at 30 degrees)
PMID:30992049	PBO:0093615	(comment: CHECK same as nmt81-vid21 alone)
PMID:30992049	FYPO:0000085	(comment: 25 degrees; same as mst1-L344S alone)
PMID:30996236	FYPO:0002674	(Fig. 3)
PMID:30996236	FYPO:0001357	(Fig. 2)
PMID:30996236	FYPO:0001234	(Fig. 2)
PMID:30996236	FYPO:0001357	(Fig. 2)
PMID:30996236	FYPO:0001357	(Fig. 2)
PMID:30996236	FYPO:0002674	(Fig. 3)
PMID:30996236	FYPO:0002674	(Fig. 3)
PMID:30996236	FYPO:0002674	(Fig. 3)
PMID:30996236	FYPO:0002674	(Fig. 3)
PMID:30996236	FYPO:0002674	(Fig. 3)
PMID:30996236	FYPO:0002674	(Fig. 3)
PMID:30996236	FYPO:0002674	(Fig. 3)
PMID:30996236	FYPO:0002674	(Fig. 3)
PMID:30996236	FYPO:0002674	(Fig. 3)
PMID:30996236	FYPO:0002674	(Fig. 3)
PMID:30996236	FYPO:0002674	(Fig. 3)
PMID:30996236	FYPO:0002674	(Fig. 3)
PMID:30996236	FYPO:0001357	(Fig. 2)
PMID:30996236	PBO:0095685	(Fig. 2)
PMID:30996236	PBO:0095685	(Fig. 2)
PMID:30996236	PBO:0095634	(Fig. 2)
PMID:30996236	PBO:0095634	(Fig. 2)
PMID:30996236	PBO:0095634	(Fig. 2)
PMID:30996236	PBO:0095634	(Fig. 2)
PMID:30996236	PBO:0095634	(Fig. 2)
PMID:30996236	PBO:0095634	(Fig. 2)
PMID:30996236	PBO:0095634	(Fig. 2)
PMID:30996236	PBO:0094648	(Fig. 2)
PMID:31000521	FYPO:0004310	) Rad21 locates to centromere in dfp1-3A mutants.
PMID:31000521	FYPO:0000091	(Fig. S1)
PMID:31000521	PBO:0104284	(comment: (vw 3B? changed from normal to lagging, added penetrance)) dfp1-CFP-2CD rescues minichromosome loss in the absence of Swi6.
PMID:31000521	PBO:0104283	(Fig. 2A) (comment: Spindle pole-to-pole distance was measured based on the distance of duplicated SPBs revealed by Sad1-DsRed.)
PMID:31000521	FYPO:0004310	(comment: (VW changed to multi allele)) The delay of m-to-G1/S phase transition in swi6∆ and dfp1-3A was abolished after deleting mad2.
PMID:31000521	FYPO:0000634	(Fig. 5B) (comment: CHECK abolish Swi6 protein localization to centromere during vegetative growth)
PMID:31000521	FYPO:0004742	(Fig. 7B)
PMID:31000521	FYPO:0004742	(Fig. 7B)
PMID:31000521	FYPO:0003412	(Fig. 7B)
PMID:31000521	FYPO:0006811	(Fig. 7) (comment: using minichromosome)
PMID:31000521	PBO:0096838	(Fig. 7) (comment: using minichromosome)
PMID:31000521	PBO:0096842	(Fig. 7) (comment: using minichromosome)
PMID:31000521	PBO:0104282	(Figure 3B) (comment: vw changed more specific to lagging chromosmes) Increase the frequency of mitotic cells showing lagging chromosomes. Rad21 fails to accumulate at centromere in the absence of Swi6.
PMID:31000521	FYPO:0001513	(Figure 3B) Chp1 fails to accumulate at noncentromeric location in the absence of Chp2 and Swi6.
PMID:31000521	FYPO:0001007	(comment: (vw: changed genotype to add swi6 delt)) dfp1-CFP-2CD restores lagging chromosomes in the absence of Swi6. Rad21 locates to centromere in dfp1-CFP-2CD mutants.
PMID:31000521	PBO:0104292	(Fig. 5B)
PMID:31000521	PBO:0104291	(Figure 3B)
PMID:31000521	PBO:0104290	(Figure 3B)
PMID:31000521	PBO:0104289	(Figure 3B)
PMID:31000521	PBO:0104288	(Fig. 3B)
PMID:31000521	PBO:0104287	(Figure 3B)
PMID:31000521	PBO:0097772	(Fig. 2C)
PMID:31000521	PBO:0104286	(Fig. 2C)
PMID:31000521	PBO:0097773	(Fig. 2C)
PMID:31000521	PBO:0104285	(Fig. 2A) (comment: Spindle pole-to-pole distance was measured based on the distance of duplicated SPBs revealed by Sad1-DsRed.)
PMID:31000521	FYPO:0003412	(Fig. 7B)
PMID:31000521	FYPO:0003412	(Fig. 7B)
PMID:31000521	PBO:0104293	Rad21-GFP enrichment at the centromere is unaffected in swi6-sm1 (Figure S4C)
PMID:31000521	FYPO:0001513	The swi6-sm1 allele disrupts silencing without lagging chromosomes (Yamagishi et al. 2008) (Figure S4, A and B). We observed a similar frequency of lagging chromosomes in wild-type (1%) and swi6-sm1 mutants (1.03%).
PMID:31000521	PBO:0096838	(Fig. 7) (comment: using minichromosome)
PMID:31000521	PBO:0104293	(Fig. 5C)
PMID:31000521	PBO:0104292	(Fig. 5E)
PMID:31015410	PBO:0097189	supp Fig 7
PMID:31015410	FYPO:0001380	(Fig. 3c)
PMID:31015410	FYPO:0001380	(Fig. 3c)
PMID:31015410	PBO:0107674	(Fig. 3c)
PMID:31015410	PBO:0107671	(Fig. 3f)
PMID:31015410	PBO:0107673	(Fig. 4a,c)
PMID:31015410	PBO:0097188	(Fig. 4b,c) (comment: CHECK ENHANCER OF N/C ratio of lem2/rae1)
PMID:31015410	FYPO:0001221	(Fig. 4a,c)
PMID:31015410	GO:0031965	Supp Fig6
PMID:31015410	PBO:0107672	supp Fig6a
PMID:31015410	PBO:0107671	(Fig. 3f)
PMID:31015410	PBO:0107669	(Fig. 2d,e,f,g,h, S6B)
PMID:31015410	FYPO:0001221	(Fig. 1 supp data)
PMID:31015410	FYPO:0001221	(Fig. 1 supp data)
PMID:31015410	FYPO:0001221	(Fig. 1 supp data)
PMID:31015410	FYPO:0001221	(Fig. 1 supp data)
PMID:31015410	FYPO:0001221	(Fig. 1 supp data)
PMID:31015410	FYPO:0001221	(Fig. 1 supp data)
PMID:31015410	PBO:0097191	(Fig. 1)
PMID:31015410	PBO:0097191	(Fig. 1a,b,c)
PMID:31015410	PBO:0107670	(Fig. 3c,d)
PMID:31015410	PBO:0097191	(Fig. 1a) shows the lem2 chromatin binding domain is not required to restrict enhancement of the NC ratio of rae1-167
PMID:31015410	PBO:0107668	(Fig. 2a,b,c)
PMID:31015410	PBO:0107670	(Fig. 3c,d)
PMID:31015410	PBO:0097191	(Fig. 3c)
PMID:31015410	FYPO:0001221	(Fig. 3a,b)
PMID:31015410	FYPO:0001221	(Fig. 4a,c)
PMID:31015410	PBO:0107673	(Fig. 4a,c)
PMID:31015410	PBO:0107678	(Fig. 1) (comment: normal compaction)
PMID:31015410	PBO:0107677	(Fig. 3e)
PMID:31015410	PBO:0107677	(Fig. 3e)
PMID:31015410	PBO:0107676	(Fig. 3e)
PMID:31015410	PBO:0107676	(Fig. 3e)
PMID:31015410	PBO:0107675	(Fig. 3d)
PMID:31015410	FYPO:0001221	(Fig. 3d)
PMID:31015410	FYPO:0001221	(Fig. 1)
PMID:31015410	PBO:0097191	supp data Fig 1b,c
PMID:31015410	PBO:0097189	supp Fig 7
PMID:31030285	PBO:0105857	(Fig. S1)
PMID:31030285	PBO:0105860	(Fig. 7)
PMID:31030285	PBO:0105861	(Fig. 7)
PMID:31030285	PBO:0105862	(Fig. 7)
PMID:31030285	PBO:0105863	(Fig. 7)
PMID:31030285	PBO:0105861	(Fig. 7)
PMID:31030285	PBO:0105862	(Fig. 7)
PMID:31030285	PBO:0105863	(Fig. 7)
PMID:31030285	PBO:0105864	(Fig. 7)
PMID:31030285	PBO:0105865	not shown
PMID:31030285	FYPO:0001420	(Fig. 8)
PMID:31030285	FYPO:0000442	cell growth is slower than wild type in glycerol and ethanol medium
PMID:31030285	PBO:0105855	Coq4 protein is decreased but Dlp1, Coq3, Coq5 and Coq8 are not
PMID:31030285	PBO:0105856	Coq4 protein is increased but Dlp1, Coq3, Coq5, and Coq8 are not
PMID:31030285	FYPO:0004167	cell growth is faster than wild type in glycerol and ethanol medium
PMID:31030285	PBO:0105857	(Fig. S1)
PMID:31030285	PBO:0105857	(Fig. S1)
PMID:31030285	FYPO:0006978	(Fig. 6)
PMID:31030285	PBO:0105857	(Fig. S1)
PMID:31030285	PBO:0105857	(Fig. S1)
PMID:31030285	PBO:0105857	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105858	(Fig. S1)
PMID:31030285	PBO:0105859	(Fig. S1)
PMID:31041892	PBO:0019202	(Fig. 1)
PMID:31041892	PBO:0096766	(Figure 3) blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	PBO:0096764	(Figure 2)
PMID:31041892	PBO:0096764	(Figure 2)
PMID:31041892	PBO:0096767	(Figure 3)
PMID:31041892	PBO:0096767	(Figure 3)
PMID:31041892	FYPO:0005905	(Figure 4) blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	FYPO:0005905	(Figure 4) blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	PBO:0096768	(Figure 5)
PMID:31041892	PBO:0096761	(Figure 3)
PMID:31041892	PBO:0096761	(Figure 3)
PMID:31041892	PBO:0096762	(Figure 5)
PMID:31041892	FYPO:0004646	blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	PBO:0019202	(Fig. 1)
PMID:31041892	PBO:0019202	(Fig. 1)
PMID:31041892	PBO:0096760	(Figure 2) blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	PBO:0096763	(Figure 4)
PMID:31041892	PBO:0096763	(Figure 4)
PMID:31041892	PBO:0096763	(Figure 4) blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	PBO:0096760	(Figure 2)
PMID:31041892	PBO:0096760	(Figure 2)
PMID:31041892	FYPO:0005905	(Figure 4) blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	PBO:0096764	(Figure 2) blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	PBO:0096765	(Figure 3) blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31053915	GO:0008171	(comment: catechol O-methyltransferase activity)
PMID:31053915	GO:0010340	(comment: catechol O-methyltransferase activity (Vw I kept this as o-methytransferase since no report of catachols in fission yeast))
PMID:31053915	GO:1990748	(comment: detoxification)
PMID:31053915	GO:1990748	(comment: detoxification)
PMID:31072933	FYPO:0002061	(Figure 1c)
PMID:31072933	FYPO:0002061	(Figure 1c)
PMID:31072933	PBO:0099134	((comment: Rescued to WT level) Rad21 phosphorylation level in cohesin hinge cs mutants is rescued by Δwpl1, while the loss of the Rad21 protein level in cohesin hinge ts mutants cannot be rescued by Δwpl1
PMID:31072933	PBO:0100832	(Figure S7A)
PMID:31072933	FYPO:0001355	(Figure 5C)
PMID:31072933	FYPO:0002061	(Figure S8)
PMID:31072933	FYPO:0002061	(Figure S8)
PMID:31072933	PBO:0100832	(Figure 6c)
PMID:31072933	FYPO:0002060	(Figure 3A)
PMID:31072933	PBO:0100825	(Figure 1G)
PMID:31072933	PBO:0100825	(Figure 1G, Figure 2)
PMID:31072933	PBO:0098320	(Figure 6c)
PMID:31072933	PBO:0098320	(Figure 6c)
PMID:31072933	PBO:0098320	(Figure 6c)
PMID:31072933	PBO:0098320	(Figure 6c)
PMID:31072933	PBO:0100832	(Figure S7A)
PMID:31072933	PBO:0100832	(Figure S7A)
PMID:31072933	PBO:0100832	(Figure S7A)
PMID:31072933	FYPO:0002061	(Figure 5C)
PMID:31072933	FYPO:0001355	(Figure 5C)
PMID:31072933	FYPO:0002060	(Figure 4D-H)
PMID:31072933	FYPO:0002060	(Figure 4D-H)
PMID:31072933	FYPO:0002060	(Figure 4D-H)
PMID:31072933	FYPO:0001355	(Figure 1C)
PMID:31072933	FYPO:0002060	(Figure 4A,B)
PMID:31072933	FYPO:0002060	(Figure 4A,B)
PMID:31072933	FYPO:0002060	(Figure 4A,B)
PMID:31072933	FYPO:0002060	(Figure 4A,B)
PMID:31072933	FYPO:0002060	(Figure 4A,B)
PMID:31072933	FYPO:0002060	(Figure 3A)
PMID:31072933	FYPO:0002060	(Figure 3A)
PMID:31072933	FYPO:0002060	(Figure 3A)
PMID:31072933	FYPO:0001355	(Fig. 3B)
PMID:31072933	FYPO:0002060	(Figure S4)
PMID:31072933	FYPO:0002060	(Figure 3A)
PMID:31072933	FYPO:0002060	(Figure S4)
PMID:31072933	FYPO:0002060	(Figure S4)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure 3A)
PMID:31072933	FYPO:0002060	(Figure 3A)
PMID:31072933	FYPO:0002060	(Figure 3A)
PMID:31072933	PBO:0098320	(Figure 6c)
PMID:31072933	FYPO:0002060	(Figure 3F)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure S3)
PMID:31072933	FYPO:0002060	(Figure 2C)
PMID:31072933	PBO:0100827	(Figure 2)
PMID:31072933	FYPO:0002060	(Figure 1e)
PMID:31072933	FYPO:0002060	(Figure 1e)
PMID:31072933	FYPO:0002060	(Figure 1e)
PMID:31072933	FYPO:0002060	(Figure 1c)
PMID:31072933	FYPO:0002060	(Figure 1c)
PMID:31072933	FYPO:0002060	(Figure 1c)
PMID:31072933	FYPO:0002060	(Figure 1c)
PMID:31072933	FYPO:0002060	(Figure 1c)
PMID:31072933	FYPO:0002061	(Figure 1c)
PMID:31072933	FYPO:0002060	(Figure 1c)
PMID:31072933	FYPO:0002060	(Figure 1c)
PMID:31072933	FYPO:0002060	(Figure 1c)
PMID:31072933	FYPO:0002060	(Figure 1c)
PMID:31072933	FYPO:0002060	(Figure 1c)
PMID:31072933	FYPO:0002060	(Figure 1c)
PMID:31072933	FYPO:0002060	(Figure 1c)
PMID:31072933	FYPO:0002060	(Figure 1c)
PMID:31072933	FYPO:0002060	(Figure 1c)
PMID:31072933	FYPO:0002061	(Figure 1c)
PMID:31072933	FYPO:0002061	(Figure 1c)
PMID:31072933	FYPO:0001355	(Fig. 3B)
PMID:31072933	FYPO:0001355	(Fig. 3B)
PMID:31072933	PBO:0100832	(Figure 6c)
PMID:31072933	PBO:0098320	(Figure 6c)
PMID:31072933	PBO:0100831	(Figure 1G)
PMID:31072933	PBO:0100830	(Figure 1G)
PMID:31072933	PBO:0100829	(Figure 1G)
PMID:31072933	PBO:0100826	(Figure 2)
PMID:31072933	PBO:0100825	(Figure 1G)
PMID:31089172	FYPO:0006917	(Fig. 2E)
PMID:31089172	FYPO:0002061	(Figure 4A)
PMID:31089172	FYPO:0002061	(Figure 4A)
PMID:31089172	FYPO:0002061	(Figure 4A)
PMID:31089172	FYPO:0002061	(Figure 4A)
PMID:31089172	PBO:0033572	(Fig. 4A)
PMID:31089172	PBO:0021821	(Fig. 4A)
PMID:31089172	FYPO:0002061	(Fig. 3)
PMID:31089172	FYPO:0002061	(Fig. 3)
PMID:31089172	FYPO:0002061	(Fig. 2A top)
PMID:31089172	FYPO:0000324	(Fig. 2E)
PMID:31089172	FYPO:0006917	(Fig. 2E)
PMID:31089172	FYPO:0002061	(Figure 4A)
PMID:31089172	FYPO:0003268	(Fig. 2C, D)
PMID:31089172	FYPO:0003268	(Fig. 2C, D)
PMID:31089172	FYPO:0003268	(Fig. 2C, D)
PMID:31089172	PBO:0101948	(Fig. 2A, B)
PMID:31089172	PBO:0101948	(Fig. 2A, B)
PMID:31089172	PBO:0097932	(Figure 5E)
PMID:31089172	PBO:0097932	(Figure 5E)
PMID:31089172	PBO:0097932	(Figure 5E)
PMID:31089172	PBO:0097932	(Figure 6C-E)
PMID:31089172	PBO:0101954	(Figure 6C-E)
PMID:31089172	FYPO:0002061	(Figure 4A)
PMID:31089172	PBO:0095688	(Fig. 5B, C)
PMID:31089172	PBO:0095688	(Fig. 5B, C)
PMID:31089172	PBO:0101953	(Fig. 5B, C)
PMID:31089172	PBO:0101953	(Fig. 5B, C)
PMID:31089172	FYPO:0002061	(Fig. 5D and Supplementary Fig. S2A,C)
PMID:31089172	FYPO:0002061	(Fig. 5D and Supplementary Fig. S2A,C)
PMID:31089172	FYPO:0002061	(Fig. 5D and Supplementary Fig. S2A,C)
PMID:31089172	FYPO:0002061	(Fig. 5D and Supplementary Fig. S2A,C)
PMID:31089172	PBO:0097932	(Figure 5E)
PMID:31089172	FYPO:0002061	(Fig. 6)
PMID:31089172	FYPO:0002061	(Fig. 6)
PMID:31089172	FYPO:0002061	(Fig. 6)
PMID:31089172	FYPO:0006917	(Fig. 6)
PMID:31089172	PBO:0024749	(Fig. 4A)
PMID:31089172	FYPO:0004833	(Figure 4A, B)
PMID:31089172	FYPO:0006918	(Figure 4A, B)
PMID:31089172	PBO:0101949	(Figure 4A, B)
PMID:31089172	PBO:0101949	(Figure 4A, B)
PMID:31089172	PBO:0101949	(Figure 4A, B)
PMID:31089172	PBO:0101950	(Figure 4A, B)
PMID:31089172	PBO:0097932	(Figure 4A, B)
PMID:31089172	PBO:0097932	(Figure 4A, B)
PMID:31089172	PBO:0097932	(Figure 4A, B)
PMID:31089172	PBO:0097932	(Figure 4A, B)
PMID:31089172	PBO:0097932	(Figure 4A, B)
PMID:31089172	PBO:0101949	(Fig. 4)
PMID:31089172	PBO:0101951	(Fig. 4)
PMID:31089172	PBO:0101952	(Fig. 4)
PMID:31089172	FYPO:0002061	(Figure 4A)
PMID:31089172	FYPO:0002060	(Fig. 4A)
PMID:31089172	FYPO:0002061	(Fig. 3)
PMID:31089172	FYPO:0002060	(Fig. 3)
PMID:31089172	FYPO:0002060	(Fig. 3)
PMID:31116668	GO:0009992	(Fig. 5)
PMID:31116668	FYPO:0006005	(Fig. 4)
PMID:31116668	FYPO:0006899	(Fig. 5c)
PMID:31116668	GO:0031520	(Fig. 1d) (comment: vw: localized by the secretory pathway)
PMID:31116668	PBO:0098990	(Fig. 1e)
PMID:31131414	FYPO:0002019	(comment: CONDITION Southern blot) (comment: same as rap1-7A single mutant)
PMID:31149897	FYPO:0006922	PCNA foci persist longer than normal, and form large bright patches before disappearing (Fig 2).
PMID:31149897	FYPO:0000167	(Fig. 4) (comment: very small difference from fbh1delta alone)
PMID:31149897	FYPO:0000167	(Fig. 4)
PMID:31149897	PBO:0097857	(Fig. 4)
PMID:31149897	FYPO:0006920	elg1∆ exhibits reduced direct repeat recombination associated with replication fork collapse at the RTS1 replication fork barrier
PMID:31149897	FYPO:0000167	(Fig. 4)
PMID:31149897	FYPO:0000473	(Figure 3A) (comment: CHECK increased spontaneous direct repeat recombination)
PMID:31149897	FYPO:0006921	(Fig. 6)
PMID:31149897	FYPO:0006921	(Fig. 6)
PMID:31149897	FYPO:0006925	(Fig. 5)
PMID:31149897	FYPO:0006924	(Fig. 5)
PMID:31149897	FYPO:0006923	(Fig. 3)
PMID:31178220	GO:1901612	SpTam41 interacts strongly with cardiolipin
PMID:31201205	PBO:0102633	(Figure 4)
PMID:31201205	FYPO:0006660	(Figure 7B)
PMID:31201205	FYPO:0006935	(Figure 7B) small, viable
PMID:31201205	FYPO:0006660	(Figure 7B)
PMID:31201205	FYPO:0002048	(Figure 7B) small viable
PMID:31201205	GO:0005635	(Fig. 2)
PMID:31201205	GO:0005635	(Fig. 2)
PMID:31201205	GO:0005783	(Fig. 2)
PMID:31201205	GO:0005783	(Fig. 2)
PMID:31201205	FYPO:0001234	The resulting cwh43 pdt1Δ 201 double mutant partly recovered colony formation capacity at 36°C, compared to that of the 202 cwh43 single mutant (Fig. 2D).
PMID:31201205	FYPO:0002061	(Fig. 2B,C)
PMID:31201205	FYPO:0002061	(Fig. 2B,C)
PMID:31201205	FYPO:0002061	(Fig. 2B,C)
PMID:31201205	FYPO:0002061	(Fig. 2B,C)
PMID:31201205	FYPO:0002061	(Fig. 2B,C)
PMID:31201205	FYPO:0002903	(comment: CHECK small viable)
PMID:31201205	PBO:0096876	(Figure 6)
PMID:31201205	FYPO:0002060	(Figure 7)
PMID:31201205	PBO:0102635	(Figure 6)
PMID:31201205	PBO:0102634	(Figure 4)
PMID:31201205	PBO:0102634	(Figure 4)
PMID:31201205	PBO:0102633	(Figure 4)
PMID:31201205	PBO:0102633	(Figure 4)
PMID:31201205	GO:0005886	(Fig. 2)
PMID:31201205	GO:0005886	(Fig. 2)
PMID:31201205	PBO:0096875	(Figure 6)
PMID:31201205	FYPO:0002903	(Figure 5) (vw: changed to pear, descendent of spherical)
PMID:31201205	FYPO:0002251	(Figure 5)
PMID:31201205	PBO:0102632	(Figure 4)
PMID:31201205	PBO:0102632	(Figure 4)
PMID:31206516	FYPO:0007479	Loss of Clr4 abolished red-white variegation in the epe1Δ ade6-m210 background, indicating a requirement for the H3K9 methyltransferase Clr4. clr3 and sir2, which encode histone deacetylases, are required for self-propagation of heterochromatin [30-34]. The introduction of clr3Δ or sir2Δ into the epe1Δ background also induced a uniform red phenotype. Similarly, loss of Swi6 suppressed variegation.
PMID:31206516	FYPO:0007479	Loss of Clr4 abolished red-white variegation in the epe1Δ ade6-m210 background, indicating a requirement for the H3K9 methyltransferase Clr4. clr3 and sir2, which encode histone deacetylases, are required for self-propagation of heterochromatin [30-34]. The introduction of clr3Δ or sir2Δ into the epe1Δ background also induced a uniform red phenotype. Similarly, loss of Swi6 suppressed variegation.
PMID:31206516	FYPO:0007479	Loss of Clr4 abolished red-white variegation in the epe1Δ ade6-m210 background, indicating a requirement for the H3K9 methyltransferase Clr4. clr3 and sir2, which encode histone deacetylases, are required for self-propagation of heterochromatin [30-34]. The introduction of clr3Δ or sir2Δ into the epe1Δ background also induced a uniform red phenotype. Similarly, loss of Swi6 suppressed variegation.
PMID:31206516	FYPO:0007479	Loss of Clr4 abolished red-white variegation in the epe1Δ ade6-m210 background, indicating a requirement for the H3K9 methyltransferase Clr4. clr3 and sir2, which encode histone deacetylases, are required for self-propagation of heterochromatin [30-34]. The introduction of clr3Δ or sir2Δ into the epe1Δ background also induced a uniform red phenotype. Similarly, loss of Swi6 suppressed variegation.
PMID:31206516	GO:0033696	Thus, we concluded that ectopic heterochromatin-mediated repression of ade5 caused the white phenotype of the epe1Δ W70 strain.
PMID:31206516	PBO:0110798	Since loss of Epe1 increases H3K9me levels at subtel1L and 2L [23, 24], we hypothesized that the ade5 gene was silenced by ectopically deposited H3K9me, which arrested red pigment formation.
PMID:31206516	PBO:0110797	(comment: vw: variegated population) These results suggested that the white phenotype of W70 was not linked to otr1R::ade6+. The re-appearance of red colonies from epe1Δ W70 cells (Fig 1C) suggested that the white phenotype was due to epigenetic rather than genetic alterations.
PMID:31206516	PBO:0110796	The H297A substitution slightly impaired the interaction (S4G Fig), which was confirmed by the results of a bait-prey exchange experiment. We performed co-immunoprecipitation analysis of Swi6 with Epe1H297A. Consistent with the results of yeast two-hybrid assay, the Epe1H297A mutant interacted with Swi6 with a slightly lower efficiency than wild-type Epe1 (Fig 4H).
PMID:31206516	PBO:0120528	FLAG ChIP analysis revealed that H297A reduced appreciably Epe1 enrichment on centromeric dg repeats and IRC3 (Fig 4G), a centromeric boundary sequence where Epe1 accumulates to a high level [12, 14
PMID:31206516	PBO:0110802	However, consistent with the previous report [13], the C-terminal half of Epe1 (487-948 amino acids region) interacted with Swi6 in the yeast two-hybrid system, but the N-terminal half (1-486) did not (S4I Fig).
PMID:31206516	PBO:0110803	However, consistent with the previous report [13], the C-terminal half of Epe1 (487-948 amino acids region) interacted with Swi6 in the yeast two-hybrid system, but the N-terminal half (1-486) did not (S4I Fig).
PMID:31206516	PBO:0110801	We introduced Epe1ΔN into ade6-m210 cells to examine the effect of the ΔN mutation on the suppression of ectopic heterochromatin formation. Epe1ΔN cells formed pink/white colonies with a slightly lower frequency than epe1Δ cells (Fig 4K), indicating that the NTA domain contributed to the suppression of ectopic heterochromatin-mediated variegation.
PMID:31206516	FYPO:0002876	We found that deletion of the N-terminal 171 amino acids (Epe1ΔN) abolished transcriptional activation by Epe1 and the N-terminal 208 amino acids (Epe1N208) activated transcription of the HIS3 reporter independently of JmjC (Fig 4I), suggesting that the N-terminal 171 amino acids region is required for the transcriptional activation activity.
PMID:31206516	FYPO:0007479	However, how Epe1 finds target sites to prevent ectopic heterochromatin formation is unknown. Since Epe1 physically interacts with the bromodomain protein Bdf2, which is required for heterochromatin-euchromatin boundary formation [14], we predicted that Bdf2 would recruit Epe1 to the target sites. However, bdf2Δ cells showed an almost uniform red phenotype in the ade6-m210 background (S4H Fig), suggesting that Bdf2 was not related to suppression of variegation and ectopic heterochromatin formation.
PMID:31206516	PBO:0110800	Unlike loss of Epe1, the H297A mutation generated few pink/white colonies in the ade6-m210 background (Fig 4A); indeed, 96.2% of Epe1H297A cells formed WT-like red colonies, while 61.7% of epe1Δ cells did.
PMID:31206516	PBO:0110799	We next examined the requirement for Ago1 and Taz1 for epe1Δ-induced variegation, because both factors are involved in subtelomeric constitutive heterochromatin formation [5]. epe1Δ ago1Δ, epe1Δ taz1Δ, and epe1Δ ago1Δ taz1Δ strains displayed red-white variegated phenotypes (S2A and S2B Fig), indicating that neither RNAi nor Taz1 was essential for epe1Δ- induced variegation.
PMID:31206516	PBO:0110799	We next examined the requirement for Ago1 and Taz1 for epe1Δ-induced variegation, because both factors are involved in subtelomeric constitutive heterochromatin formation [5]. epe1Δ ago1Δ, epe1Δ taz1Δ, and epe1Δ ago1Δ taz1Δ strains displayed red-white variegated phenotypes (S2A and S2B Fig), indicating that neither RNAi nor Taz1 was essential for epe1Δ- induced variegation.
PMID:31206516	PBO:0110799	We next examined the requirement for Ago1 and Taz1 for epe1Δ-induced variegation, because both factors are involved in subtelomeric constitutive heterochromatin formation [5]. epe1Δ ago1Δ, epe1Δ taz1Δ, and epe1Δ ago1Δ taz1Δ strains displayed red-white variegated phenotypes (S2A and S2B Fig), indicating that neither RNAi nor Taz1 was essential for epe1Δ- induced variegation.
PMID:31206516	FYPO:0007479	Loss of Clr4 abolished red-white variegation in the epe1Δ ade6-m210 background, indicating a requirement for the H3K9 methyltransferase Clr4. clr3 and sir2, which encode histone deacetylases, are required for self-propagation of heterochromatin [30-34]. The introduction of clr3Δ or sir2Δ into the epe1Δ background also induced a uniform red phenotype. Similarly, loss of Swi6 suppressed variegation.
PMID:31206516	FYPO:0007479	Loss of Clr4 abolished red-white variegation in the epe1Δ ade6-m210 background, indicating a requirement for the H3K9 methyltransferase Clr4. clr3 and sir2, which encode histone deacetylases, are required for self-propagation of heterochromatin [30-34]. The introduction of clr3Δ or sir2Δ into the epe1Δ background also induced a uniform red phenotype. Similarly, loss of Swi6 suppressed variegation.
PMID:31206516	FYPO:0007479	Loss of Clr4 abolished red-white variegation in the epe1Δ ade6-m210 background, indicating a requirement for the H3K9 methyltransferase Clr4. clr3 and sir2, which encode histone deacetylases, are required for self-propagation of heterochromatin [30-34]. The introduction of clr3Δ or sir2Δ into the epe1Δ background also induced a uniform red phenotype. Similarly, loss of Swi6 suppressed variegation.
PMID:31206516	FYPO:0007479	Loss of Clr4 abolished red-white variegation in the epe1Δ ade6-m210 background, indicating a requirement for the H3K9 methyltransferase Clr4. clr3 and sir2, which encode histone deacetylases, are required for self-propagation of heterochromatin [30-34]. The introduction of clr3Δ or sir2Δ into the epe1Δ background also induced a uniform red phenotype. Similarly, loss of Swi6 suppressed variegation.
PMID:31217286	PBO:0112011	(Fig. S6)
PMID:31217286	FYPO:0008169	(Fig. 6A, 6B)
PMID:31217286	PBO:0112013	(Fig. S1C)
PMID:31217286	PBO:0112014	(Fig. S1E, S1F)
PMID:31217286	PBO:0112020	(Fig. 4C)
PMID:31217286	PBO:0112012	Phenotype of Erg25 overexpression is suppressed by Erg11 inhibition. Fig. 1E
PMID:31217286	PBO:0112011	(Fig. 1D)
PMID:31217286	FYPO:0007677	(Fig. 1C)
PMID:31217286	PBO:0112019	(Fig. 4B)
PMID:31217286	PBO:0112010	(Fig. 1)
PMID:31217286	GO:0005783	(Fig. S1D)
PMID:31217286	PBO:0112013	(Fig. S1C)
PMID:31217286	PBO:0112017	(Fig. 3)
PMID:31217286	PBO:0112016	(Fig. 2)
PMID:31217286	PBO:0112015	(Fig. 2)
PMID:31217286	PBO:0112018	(Fig. 4A)
PMID:31217286	PBO:0112024	(Fig. 6D)
PMID:31217286	PBO:0112012	(Fig. 6D)
PMID:31217286	PBO:0112023	(Fig. 5A)
PMID:31217286	PBO:0112022	(Fig. 6C)
PMID:31217286	PBO:0112021	(Fig. 6C)
PMID:31239353	FYPO:0007043	(Figure 5B)
PMID:31239353	GO:0004035	(comment: CHECK Figure 1A Zinc-dependent)
PMID:31239353	FYPO:0007044	(Fig. 1)
PMID:31239353	GO:0004035	(Figure 1A)
PMID:31239353	FYPO:0007044	(Fig. 1)
PMID:31239353	PBO:0095242	(comment: pho8 transcript and protein levels are increased in high zinc BUT ZINC DEPENDENT CHAnges are independent of transcript levels)
PMID:31239353	PBO:0095243	(Figure 1B and 1C)
PMID:31239353	PBO:0095244	(Figure 2B)
PMID:31239353	FYPO:0007043	(Figure 5B)
PMID:31239353	FYPO:0007042	reduced during conditions of zinc shock (Figure 8 and Figure 9). (comment: as Pho8 binds its zinc cofactors inside of the secretory pathway, it activity is dependent upon zinc transporters that supply zinc ions to the secretory pathway)
PMID:31239353	FYPO:0007047	(Figure 7)
PMID:31239353	FYPO:0007044	reduced alkaline phosphatase activity and Pho8 dimerization (Figures 6C and 6D)
PMID:31239353	FYPO:0007044	reduced alkaline phosphatase activity and Pho8 dimerization (Figures 6C and 6D)
PMID:31239353	FYPO:0007048	(Figure 7)
PMID:31239353	FYPO:0007048	(Figure 7)
PMID:31239353	PBO:0095245	consistent with Loz1 facilitating the repression of pho8 gene expression in high zinc (Figure 2A)
PMID:31239353	PBO:0095246	Pho8 abundance is increased in high zinc in a loz1 deletion strain (Figure 2B and 2C)
PMID:31239353	PBO:0095247	(Figure 4) hat although processing of Pho8 is dependent upon the growth phase of cells, zinc is the major factor that limits Pho8 activity in vivo
PMID:31239353	FYPO:0007045	(Fig. 1)
PMID:31239353	PBO:0095248	(Fig. 1) (comment: CHECK abolished?)
PMID:31239353	PBO:0095248	(comment: CHECK abolished ?)
PMID:31239353	PBO:0095249	(Figure 1B and 1C)
PMID:31239353	PBO:0095247	(Figure 4) ....although processing of Pho8 is dependent upon the growth phase of cells, zinc is the major factor that limits Pho8 activity in vivo
PMID:31239353	PBO:0095250	(Figure 5D)
PMID:31239353	PBO:0095251	(Figure 5D)
PMID:31239353	FYPO:0007041	(Figure 8)
PMID:31239353	GO:0106219	(comment: CHECK DIRECTLY_ACTIVATES pho8 GO:0004035) As zinc did not affect Pho8 stability, processing, or dimerization, we hypothesized that the activity of Pho8 is directly affected by cellular zinc status. .. .....Taken together these results are consistent with yeast maintaining an inactive 5 Zinc-dependent alkaline phosphatase activity pool of Pho8 in low zinc, which can be rapidly activated as soon as zinc is available.
PMID:31257143	PBO:0101482	(Figure S4)
PMID:31257143	FYPO:0002638	(Figures S3B and S3D)
PMID:31257143	FYPO:0002638	(Figures S3B and S3C)
PMID:31257143	PBO:0101478	3b (comment: 80% 12 hours)
PMID:31257143	FYPO:0002638	(Figure 2B) (comment: demonstrates robust arrest)
PMID:31257143	PBO:0101478	(Figure 2B) (comment: demonstrates robust arrest 3b 80% 12 hours)
PMID:31257143	FYPO:0004318	(Figure 2D)
PMID:31257143	FYPO:0004318	(Figure 2d)
PMID:31257143	FYPO:0004318	(Figure 2d)
PMID:31257143	PBO:0101483	(Figure S4)
PMID:31260531	PBO:0103435	(comment: Rep2 locates SAGA complex at MBF-regulated promoters.)
PMID:31260531	PBO:0103437	(comment: chromatin association at MCBs is part of positive regulation of G1/S transition of mitotic cell cycle)
PMID:31269446	FYPO:0003049	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0002173	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0002664	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0000080	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0000080	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0000080	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0003049	(comment: CONDITION 18 °C)
PMID:31269446	PBO:0111618	(comment: non-canonical termination sites)
PMID:31269446	FYPO:0007213	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0007213	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0002664	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0002173	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0003049	(comment: CONDITION 18 °C)
PMID:31269446	GO:0090052	(comment: si independent pericentric heterochromatin formation CPF and RNAi Act in Parallel to Assemble Centromeric Heterochromatin)
PMID:31269446	GO:0090052	(comment: si independent pericentric heterochromatin formation CPF and RNAi Act in Parallel to Assemble Centromeric Heterochromatin)
PMID:31269446	PBO:0111618	(comment: non-canonical termination sites)
PMID:31269446	FYPO:0007213	(comment: CONDITION 18 °C)
PMID:31269446	PBO:0111618	(comment: non-canonical termination sites)
PMID:31269446	FYPO:0002664	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0003049	(comment: CONDITION 18 °C)
PMID:31276301	FYPO:0003717	(Figure S1a)
PMID:31276301	FYPO:0004429	Furthermore, abnormally elongated cytoplasmic and spindle MTs were frequently observed in these cells (Figure 6).
PMID:31276301	FYPO:0002215	(Fig. 6)
PMID:31276301	FYPO:0004097	(Figure S1a)
PMID:31276301	FYPO:0004652	(Figure S1a)
PMID:31276301	FYPO:0003702	(Figure S1a)
PMID:31276301	FYPO:0002060	(Figure S1a)
PMID:31276301	PBO:0106675	(Fig. 4b)
PMID:31276301	FYPO:0003190	(Table 3)
PMID:31276301	PBO:0106674	(Fig. 4e)
PMID:31276301	PBO:0106673	(Fig. 4e)
PMID:31276301	PBO:0106672	(Fig. 4d)
PMID:31276301	PBO:0106671	(Fig. 4a)
PMID:31276301	FYPO:0000733	Furthermore, abnormally elongated cytoplasmic and spindle MTs were frequently observed in these cells (Figure 6).
PMID:31276301	FYPO:0005880	(Fig. 6)
PMID:31276301	FYPO:0005706	Table 2 Figures 5a-d and S2)
PMID:31276301	PBO:0106677	(Fig. 4e)
PMID:31276301	PBO:0106676	(Fig. 4a)
PMID:31276301	FYPO:0004622	(Figure 7b)
PMID:31276301	FYPO:0007182	(Table 3)
PMID:31276588	FYPO:0000080	(Figure 1B)
PMID:31276588	PBO:0094738	(Figure 1C)
PMID:31276588	FYPO:0000047	(Figure 1B)
PMID:31276588	PBO:0094738	(Figure 1C)
PMID:31276588	FYPO:0000047	(Figure 1B)
PMID:31276588	PBO:0094774	(Figure 1D)
PMID:31276588	PBO:0094773	(Figure 1D)
PMID:31276588	PBO:0111667	(comment: CHECK target genes repressing lncRNA)
PMID:31276588	PBO:0111666	(comment: CHECK target genes pho1, pho84, and tgp1)
PMID:31276588	GO:0180034	lncRNA. Specifically, it is hypothesized that loss of the Ser7-PO4 or Ser5-PO4 marks leads to precocious termination of prt lncRNA transcription prior to the pho1 promoter and loss of the Thr4-PO4 mark reduces termination and hence increases transcription across the pho1 promoter (8) (Figure 1A).
PMID:31276588	PBO:0098285	Octo phosphatase IP8 is a relevant substrate for the Aps1 pyrophosphatase with respect to phosphate homeostasis.
PMID:31276588	PBO:0094771	(Figure 2A)
PMID:31276588	FYPO:0000080	(Figure 2C)
PMID:31276588	FYPO:0000080	(Figure 2C)
PMID:31276588	FYPO:0002061	(Figure 2C)
PMID:31276588	FYPO:0002061	(Figure 2C)
PMID:31276588	FYPO:0002061	(Figure 2C)
PMID:31276588	FYPO:0002061	(Figure 2C)
PMID:31276588	FYPO:0002061	(Figure 2C)
PMID:31276588	FYPO:0002061	(Figure 2C)
PMID:31276588	FYPO:0002061	(Figure 2C)
PMID:31276588	FYPO:0002061	(Figure 2C)
PMID:31276588	FYPO:0002059	(Figure 1E)
PMID:31276588	FYPO:0002059	(Figure 1E)
PMID:31276588	PBO:0094771	(Figure 1F)
PMID:31276588	FYPO:0000080	(Figure 1B)
PMID:31276588	PBO:0094772	(Figure 1D)
PMID:31276588	PBO:0098248	(Figure 1C)
PMID:31276588	PBO:0094771	(Figure 1F)
PMID:31276588	PBO:0094774	(Figure 1D)
PMID:31276588	PBO:0094773	(Figure 1D)
PMID:31276588	PBO:0094772	(Figure 1D)
PMID:31276588	PBO:0098248	(Figure 1C)
PMID:31278118	PBO:0097430	cells revealed that H3K9me2 was notably decreased at centromeres and telomeres in pds5D (Figure 3, A and B).
PMID:31278118	FYPO:0002336	(Figure 6B)
PMID:31278118	FYPO:0002336	(Figure 6B)
PMID:31278118	FYPO:0002827	(Figure S5)
PMID:31278118	FYPO:0002827	(Figure S5) Moreover, when we deleted pds5 in cells lacking Eso1 and/or Wpl1, the levels of haploid meiosis displayed by double or triple mutants were comparable to that of single-mutant pds5D
PMID:31278118	PBO:0097432	ue to their antagonistic roles in cohesion establishment, the lethality of eso1D can be suppressed by deletion of wpl1 (Feytout et al. 2011; Kagami et al. 2011). Whereas wpl1D did not show defects in heterochromatic silencing, the eso1D wpl1D double mutant showed derepression of mat2P::ura4+ and haploid meiosis similar to pds5D cells (Figure 6A)
PMID:31278118	PBO:0097431	However, the localization of Pds5 to euchromatic locations was unaffected in heterochromatin-deficient cells (Figure 5E)
PMID:31278118	PBO:0097431	However, the localization of Pds5 to euchromatic locations was unaffected in heterochromatin-deficient cells (Figure 5E)
PMID:31278118	PBO:0095651	Compared to the single ago1D or pds5D deletion mutants, the ago1D pds5D double mutant showed severe loss-of-silencing of Kint2::ura4+ (Figure S2C).
PMID:31278118	FYPO:0007376	(Figure 4A) (comment: CHECK https://github.com/pombase/fypo/issues/3693)
PMID:31278118	PBO:0097429	cells revealed that H3K9me2 was notably decreased at centromeres and telomeres in pds5D (Figure 3, A and B).
PMID:31278118	PBO:0097427	(Fig. 1D, 1E)
PMID:31278118	PBO:0097426	(Fig. 1D, 1E)
PMID:31278118	PBO:0097425	(Fig. 1D, 1E)
PMID:31278118	PBO:0097423	(Fig. 1d)
PMID:31278118	FYPO:0002336	(Figure 6A)
PMID:31278118	PBO:0097422	(Fig. 5B) (comment: vw: moved pds5 to assayed target)
PMID:31278118	PBO:0097420	(Fig. 2B) (Figure S1B and Table S2). This variegated staining pattern is a characteristic of mutants that are known to be defective in the maintenance of heterochromatin and that show a reduction, but not loss, of H3K9me levels (Taneja et al. 2017). Indeed, ChIP analyses of H3K9 di- and trimethylation (H3K9me2/3) showed a reduction in heterochromatic H3K9 marks at or near mat2P in pds5D (Figure 2B).
PMID:31278118	FYPO:0002336	(Figure 6B)
PMID:31278118	PBO:0097416	ue to their antagonistic roles in cohesion establishment, the lethality of eso1D can be suppressed by deletion of wpl1 (Feytout et al. 2011; Kagami et al. 2011). Whereas wpl1D did not show defects in heterochromatic silencing, the eso1D wpl1D double mutant showed derepression of mat2P::ura4+ and haploid meiosis similar to pds5D cells (Figure 6A)
PMID:31278118	FYPO:0002336	(Fig. 7)
PMID:31278118	FYPO:0002336	(Fig. 7)
PMID:31278118	PBO:0097416	(Table 1)
PMID:31278118	PBO:0097416	Table1
PMID:31285271	PBO:0099576	(Figure 1e)
PMID:31285271	PBO:0099577	(Figure 2d)
PMID:31285271	PBO:0099578	(Figure 2d)
PMID:31285271	PBO:0099579	(Figure 2d)
PMID:31285271	PBO:0099580	(Figure 2d)
PMID:31285271	PBO:0099581	(Figure 2d)
PMID:31285271	PBO:0099582	(Figure 3a)
PMID:31285271	PBO:0099583	(Figure 3a)
PMID:31285271	PBO:0099584	(Figure 3e)
PMID:31285271	PBO:0037494	(Fig. 5) Asc1 colocalized with stress granule proteins in response to heat shock.
PMID:31285271	PBO:0099575	(Figure 1d)
PMID:31285271	GO:0016282	(Fig. 2) (comment: Asc1 associates with polysomes.)
PMID:31285271	FYPO:0003125	(Fig. 4)
PMID:31285271	FYPO:0001234	(Fig. 4h)
PMID:31285271	PBO:0099585	(Figure 3e)
PMID:31285271	GO:0001731	(comment: CHECK cytoplasmic translation is a parent to this term)
PMID:31285271	FYPO:0000046	(Fig. 4h)
PMID:31285271	PBO:0099251	COMMENT: 312c8af6293e302e 41 MB+WxZqtLoWkmNqZLfwtd2DBEh8 (Fig. 6)
PMID:31285271	PBO:0099586	COMMENT: 312c8af6293e302e 41 MB+WxZqtLoWkmNqZLfwtd2DBEh8 (Fig. 6f)
PMID:31289327	FYPO:0002019	(Fig. S2)
PMID:31289327	FYPO:0002019	(Fig. S2)
PMID:31289327	PBO:0100058	(Fig. 4a)
PMID:31289327	FYPO:0000012	(Fig. 5)
PMID:31289327	FYPO:0002019	(Fig. S2)
PMID:31289327	FYPO:0002019	(Fig. S2)
PMID:31289327	FYPO:0000012	(Fig. 5)
PMID:31294478	PBO:0106272	(Fig. 4)
PMID:31294478	FYPO:0007014	(Fig. 2b)
PMID:31294478	FYPO:0007013	(Fig. 2b)
PMID:31294478	PBO:0106269	(Fig. 4)
PMID:31294478	PBO:0106268	(Fig. 3)
PMID:31294478	PBO:0106267	(Fig. 3)
PMID:31294478	FYPO:0001134	(Fig. 2b)
PMID:31294478	FYPO:0007012	(Fig. 2b)
PMID:31294478	FYPO:0007013	(Fig. 2b)
PMID:31294478	PBO:0098170	(comment: CHECK coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472)
PMID:31294478	PBO:0106254	AL fig 4. (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	PBO:0106253	AL fig 4. (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	PBO:0098170	(comment: CHECK coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472)
PMID:31294478	PBO:0098170	(comment: CHECK coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472)
PMID:31294478	FYPO:0002061	(Figure 5B)
PMID:31294478	PBO:0098170	(comment: CHECK COINCIDENT WITH 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472)
PMID:31294478	PBO:0106247	(Fig. 1b) We have shown using ChIP-seq experiments that Sen1 associates with all types of RNA polymerase III-transcribed genes. This includes tRNA_genes, 5S rRNA_genes, snu6 and srp7 but not the TFIIIC-bound COC sites.
PMID:31294478	PBO:0098562	(Fig. 1A and F)
PMID:31294478	PBO:0106249	AL fig 4. and 5c (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	PBO:0106250	AL fig 4. and 5c (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	PBO:0106251	AL fig 4. and 5c (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	PBO:0106252	AL fig 4. and 5c (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	PBO:0106253	AL fig 4. and 5c (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	PBO:0106254	AL fig 4. and 5c (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	PBO:0106255	AL fig 4. and 5c (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	GO:0030874	ChIP-qPCR of Dbl8 indicates that Dbl8 is enriched at the rDNA and at highly-expressed RNAPII-transcribed genes
PMID:31294478	PBO:0106257	(Fig. 2c, 5d)
PMID:31294478	PBO:0106258	(Fig. 2c, 5d)
PMID:31294478	PBO:0106259	(Fig. 2c, 5d)
PMID:31294478	PBO:0106260	(Fig. 2c, 5d)
PMID:31294478	FYPO:0001134	(Fig. 2b)
PMID:31294478	FYPO:0007012	(Fig. 2b)
PMID:31294478	FYPO:0007013	(Fig. 2b)
PMID:31294478	PBO:0106270	(Fig. 4)
PMID:31294478	PBO:0106271	(Fig. 4)
PMID:31294478	PBO:0106252	AL fig 4. (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	PBO:0098170	(comment: CHECK coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472)
PMID:31294800	GO:0035925	(comment: UAAU motif)
PMID:31315658	FYPO:0007471	In sharp contrast, the H3K9me2 levels remained constant in leo1∆ cells throughout G0 phase (Fig. 2; Additional file 2: Fig. S2
PMID:31315658	FYPO:0006518	Additional file 1: Fig. S1b, c
PMID:31315658	FYPO:0006518	(Fig. 1c)
PMID:31315658	FYPO:0006518	Additional file 1: Fig. S1b, c
PMID:31315658	FYPO:0006518	Additional file 1: Fig. S1b, c
PMID:31332096	FYPO:0004372	(comment: reduced chk1 phosphorylation)
PMID:31332096	PBO:0101079	(comment: elimination of Rad3-specific phosphorylation)|
PMID:31341193	PBO:0107617	Increased co-localization with Cfr1
PMID:31341193	FYPO:0007055	Evaluated by measuring the size of Vps10-GFP foci
PMID:31341193	GO:0000328	(comment: Microscopy)
PMID:31341193	PBO:0107620	(comment: Dot-Blot test)
PMID:31341193	PBO:0107608	(Fig. 5)
PMID:31341193	PBO:0107609	(comment: Dot-Blot assay)
PMID:31341193	GO:0005802	Co-localization with TGN marker
PMID:31341193	PBO:0107607	(Fig. 1a-c)
PMID:31341193	PBO:0107613	(Fig. 3) Increased co-localization with Cfr1
PMID:31341193	PBO:0107614	Reduced co-localization with the PI3P probe Cherry-FYVE
PMID:31341193	PBO:0107611	Increased co-localization with Cfr1
PMID:31341193	PBO:0107616	Reduced co-localization with the PI3P probe Cherry-FYVE
PMID:31341193	PBO:0107631	(comment: this is in a mutant but I guess it occurs physiologicall?)
PMID:31341193	PBO:0107623	isp6 delta supresses the abnormal Vps10 processing detected in vps35 delta strain
PMID:31341193	PBO:0107621	(Fig. 7) Syb1 co-localizes with late endosome markers
PMID:31341193	GO:0031906	(comment: Microscopy)
PMID:31341193	PBO:0107623	isp6 delta supresses the abnormal Vps10 processing detected in ent3 delta gga21 delta gga22 delta strain
PMID:31341193	PBO:0107623	isp6 delta suppresses Vps10 abnormal processing observed in ent3 delta gga22 delta strain
PMID:31341193	PBO:0107623	isp6 delta supresses the abnormal Vps10 proessing detected in gga21 delta gga22 delta strain
PMID:31341193	FYPO:0001355	Reduced growth on 0.6M KCl plates
PMID:31341193	FYPO:0001355	Reduced growth at 37ºC on YES agar plates
PMID:31341193	PBO:0107622	(Fig. 7)
PMID:31341193	GO:0032588	(comment: Microscopy)
PMID:31341193	PBO:0107606	(Fig. 1a-c)
PMID:31341193	FYPO:0000674	(comment: CONDITION 37ºC)
PMID:31341193	FYPO:0005947	(comment: CONDITION 28ºC)
PMID:31341193	PBO:0107628	(Fig. 1)
PMID:31341193	GO:0005770	(Fig. 1) (comment: major)
PMID:31341193	GO:0005802	(Fig. 1) (comment: minor)
PMID:31341193	PBO:0107608	(Fig. 5)
PMID:31341193	PBO:0107629	(Fig. 1)
PMID:31341193	PBO:0107629	(Fig. 1)
PMID:31341193	PBO:0107611	(Fig. 1) Increased colocalization with Cfr1
PMID:31341193	PBO:0107612	Reduced co-localyzation with the PI3P probe Cherry-FYVE
PMID:31341193	PBO:0107628	(Fig. 1)
PMID:31341193	PBO:0107628	(Fig. 1)
PMID:31341193	PBO:0107606	(Fig. 1d)
PMID:31350787	FYPO:0007122	(Fig. 6)
PMID:31350787	FYPO:0004529	(Fig. 5)
PMID:31350787	FYPO:0002056	(Fig. 5)
PMID:31350787	PBO:0095092	(Fig. 4B)
PMID:31350787	GO:0005759	(Fig. 3)
PMID:31350787	GO:0005759	(Fig. 3)
PMID:31350787	PBO:0093578	(Fig. 1A)
PMID:31350787	PBO:0093797	"(Fig. 1A) (comment: they say it is dramatically reduced....between med/low severity... ""dramatically reduced on glycerol medium, which requires high mitochondrial respiratory activity at 30 °C"")"
PMID:31350787	FYPO:0001934	(Fig. 2A) The Dmti2 mutant was not able to grow at all on medium containing glycerol at the restrictive temperature of 37 °C
PMID:31350787	PBO:0094264	(Fig. 1A)
PMID:31350787	PBO:0095091	(Fig. 1A)
PMID:31350787	FYPO:0007121	(Fig. 1)
PMID:31350787	FYPO:0000962	(Fig. 1)
PMID:31350787	PBO:0093576	(Fig. 1)
PMID:31350787	FYPO:0001164	(Fig. 1)
PMID:31350787	FYPO:0001164	(Fig. 1)
PMID:31350787	FYPO:0001409	(Fig. 1)
PMID:31350787	FYPO:0001409	(Fig. 1)
PMID:31366733	PBO:0103309	(Fig. 7)
PMID:31366733	PBO:0103309	(Fig. 7)
PMID:31366733	PBO:0103309	(Fig. 7)
PMID:31366733	PBO:0103309	(Fig. 7)
PMID:31366733	PBO:0103309	(Fig. 7)
PMID:31371524	PBO:0107535	(Figure 6)
PMID:31371524	PBO:0107533	(Figure 4)
PMID:31371524	PBO:0107534	(Figure 2)
PMID:31371524	PBO:0107536	(Figure 6)
PMID:31371524	PBO:0107534	(Figure 2)
PMID:31371524	PBO:0107533	(Figure 2)
PMID:31371524	GO:0005515	(comment: inhibits hhf4 binding)
PMID:31427431	FYPO:0001357	(Figure 1b)
PMID:31427431	FYPO:0001357	(Figure 1b)
PMID:31427431	FYPO:0001357	(Figure 1b)
PMID:31427431	FYPO:0001357	(Figure 1b)
PMID:31427431	FYPO:0000674	(Figure 1b)
PMID:31427431	FYPO:0000080	(Figure 1b)
PMID:31427431	FYPO:0000082	(Figure 1b)
PMID:31427431	FYPO:0001357	(Figure S1)
PMID:31427431	FYPO:0000069	(Figure 1e)
PMID:31427431	FYPO:0000069	(Figure 1e)
PMID:31427431	PBO:0097927	(Figure 1f)
PMID:31427431	FYPO:0000030	(Figure 2)
PMID:31427431	FYPO:0000030	(Figure 2)
PMID:31427431	FYPO:0000324	(Figure 2)
PMID:31427431	FYPO:0000324	(Figure 2)
PMID:31427431	FYPO:0000228	(Figure 2)
PMID:31427431	FYPO:0000228	(Figure 2)
PMID:31427431	FYPO:0000069	(Figure 2f)
PMID:31427431	FYPO:0000069	(Figure 2f)
PMID:31427431	FYPO:0000069	(Figure 2f)
PMID:31427431	FYPO:0000069	(Figure 2f)
PMID:31427431	FYPO:0000733	(Figure S2)
PMID:31427431	FYPO:0000733	(Figure S2)
PMID:31427431	FYPO:0001943	(Figure 4)
PMID:31427431	FYPO:0000733	(Figure 5)
PMID:31427431	FYPO:0000324	(Figure 5)
PMID:31427431	FYPO:0000141	(Figure 5)
PMID:31427431	PBO:0019232	(Figure 7) (comment: type II cells)
PMID:31427431	PBO:0097933	(Figure 7)
PMID:31427431	PBO:0097933	(Figure 7)
PMID:31427431	PBO:0097933	(Figure 7)
PMID:31427431	PBO:0097932	(Figure 7)
PMID:31427431	FYPO:0005342	(Figure 7)
PMID:31427431	FYPO:0007071	(Figure 6)
PMID:31427431	FYPO:0007071	(Figure 6)
PMID:31427431	FYPO:0007071	(Figure 6)
PMID:31427431	FYPO:0000228	(Figure 6)
PMID:31427431	PBO:0097931	(Figure 6)
PMID:31427431	FYPO:0000228	(Figure 6)
PMID:31427431	FYPO:0001846	(Figure 6)
PMID:31427431	FYPO:0001846	(Figure 6)
PMID:31427431	FYPO:0001846	(Figure 6)
PMID:31427431	FYPO:0002059	(Figure 1)
PMID:31427431	FYPO:0000080	(Figure 1b)
PMID:31427431	FYPO:0002141	(Figure 1b)
PMID:31427431	FYPO:0002141	(Figure 1b)
PMID:31427431	FYPO:0000674	(Figure 1b)
PMID:31427431	FYPO:0000674	(Figure 1b)
PMID:31427431	FYPO:0005342	(Figure 7)
PMID:31468675	GO:0000792	colocalizes with H3K9me2
PMID:31468675	FYPO:0002827	partial derepression of marker gene at silent mating-type cassette; measured by cell growth spot assay
PMID:31468675	FYPO:0006993	measured by cell growth spot assay
PMID:31468675	PBO:0097202	spot assay
PMID:31468675	FYPO:0002827	measured by cell growth spot assay
PMID:31468675	FYPO:0002827	measured by cell growth spot assay
PMID:31468675	GO:0000792	colocalizes with H3K9me2
PMID:31468675	GO:0000792	colocalizes with H3K9me2
PMID:31477575	PBO:0101352	(Fig. S1)
PMID:31477575	GO:0005938	(Fig. 3c)
PMID:31477575	GO:0005829	(Fig. 3c)
PMID:31477575	PBO:0101352	(Fig. S3B)
PMID:31477575	PBO:0101352	(Fig. S3B)
PMID:31477575	PBO:0101370	(Fig. S3B)
PMID:31477575	PBO:0101352	(Fig. S1)
PMID:31477575	PBO:0101352	(Fig. S1)
PMID:31477575	PBO:0101352	(Fig. S1)
PMID:31477575	PBO:0101352	(Fig. S1)
PMID:31477575	PBO:0101352	(Fig. S1)
PMID:31477575	PBO:0101352	(Fig. S1)
PMID:31477575	PBO:0101352	(Fig. S1)
PMID:31477575	PBO:0101352	(Fig. S1)
PMID:31477575	GO:0005515	(Fig. 1)
PMID:31477575	PBO:0101369	(Fig. 2b)
PMID:31477575	PBO:0101368	(Fig. 2b)
PMID:31477575	PBO:0101367	(Fig. 2b)
PMID:31477575	PBO:0101366	(Fig. 2b)
PMID:31477575	PBO:0101365	(Fig. 2b)
PMID:31477575	PBO:0101363	(Fig. 1)
PMID:31477575	PBO:0101363	(Fig. 1)
PMID:31477575	PBO:0101363	(Fig. 1)
PMID:31483748	FYPO:0000089	(Figure 2A)
PMID:31483748	FYPO:0000267	(Fig. 2)
PMID:31483748	FYPO:0000085	(Fig. 2)
PMID:31483748	FYPO:0000957	(Fig. 2)
PMID:31483748	FYPO:0007209	(comment: CHECK issues/3588) Figure 5A-E
PMID:31483748	GO:0005634	We examined whether Mto1 localizes to DNA repair factories and found that Mto1-mCherry was not detectable within the nucleus, as previously shown (Sawin et al., 2004; Venkatram et al.)
PMID:31483748	FYPO:0007191	(Figure 3A, 3B)
PMID:31483748	PBO:0093616	(Figure 2C)
PMID:31483748	PBO:0093616	(Figure 2C)
PMID:31483748	FYPO:0000089	(Figure 2C) No increase in severity to mto1 delete
PMID:31483748	FYPO:0000957	(Fig. 2)
PMID:31483748	FYPO:0000957	(Fig. 2)
PMID:31483748	FYPO:0000957	(Fig. 2)
PMID:31483748	FYPO:0000957	(Fig. 2)
PMID:31483748	FYPO:0000963	(Fig. 2)
PMID:31483748	FYPO:0000969	(Fig. 2)
PMID:31483748	FYPO:0007192	(Fig. 1B-G)
PMID:31483748	FYPO:0007209	(comment: CHECK issues/3588 decreased)
PMID:31483748	PBO:0101859	Reduced Rad21 binding to chromosome arms
PMID:31483748	FYPO:0000185	Recombination rates were decreased by 10-fold in mto1∆ strains in both recombination substrates (Figure 4B)
PMID:31483748	FYPO:0006921	Recombination rates were decreased by 10-fold in mto1∆ strains in both recombination substrates (Figure 4B)
PMID:31483748	FYPO:0000972	(Figure 3A, 3B) (comment: number and intensity)
PMID:31483748	FYPO:0000089	(Figure S1A)
PMID:31483748	FYPO:0000089	(Figure S1A)
PMID:31495586	PBO:0102726	(Figure 2)
PMID:31495586	PBO:0102727	(Figure 2)
PMID:31495586	PBO:0102727	(Figure 2)
PMID:31495586	PBO:0102728	(Figure 2)
PMID:31495586	PBO:0102728	(Figure 2)
PMID:31495586	FYPO:0000413	(Figure 2)
PMID:31495586	FYPO:0000413	(Figure 2)
PMID:31495586	PBO:0102729	(Figure 5)
PMID:31495586	PBO:0102729	(Figure 5)
PMID:31495586	PBO:0102730	(Figure 4 and 6)
PMID:31495586	PBO:0102731	(Figure 5) (comment: assayed using Myo52)
PMID:31495586	PBO:0102732	(Figure 5) (comment: assayed using Myo52)
PMID:31495586	PBO:0102732	(Figure 5) (comment: assayed using Myo52)
PMID:31495586	PBO:0102716	(Figure 5)
PMID:31495586	PBO:0102731	(Figure 3) (comment: assayed using Myo52)
PMID:31495586	FYPO:0007095	(comment: assayed using CHD,) FigureS1
PMID:31495586	PBO:0102733	(Figure S3)
PMID:31495586	PBO:0102722	(Figure S3)
PMID:31495586	PBO:0102719	(Figure S3)
PMID:31495586	PBO:0102723	(Figure S3)
PMID:31495586	PBO:0102734	(Figure S5) (comment: assayed using LifeAct)
PMID:31495586	PBO:0102732	(Figure 3, S4) (comment: assayed using Myo52 and Fus1)
PMID:31495586	FYPO:0007095	(Figure S1) (comment: assayed using CHD)
PMID:31495586	PBO:0102733	(Figure S3)
PMID:31495586	PBO:0102739	(Figure 6)
PMID:31495586	PBO:0102738	(Figure 6)
PMID:31495586	PBO:0097695	(Figure 6)
PMID:31495586	PBO:0097695	(Figure 6)
PMID:31495586	PBO:0102737	(Figure 4)
PMID:31495586	PBO:0102733	(Figure 3)
PMID:31495586	FYPO:0007095	(Figure 2) (comment: Increased 1.5-fold, assayed using CHD)
PMID:31495586	FYPO:0006081	(Figure S5) (comment: assayed using LifeAct)
PMID:31495586	FYPO:0006081	(Figure S5) (comment: assayed using LifeAct)
PMID:31495586	PBO:0102736	(Figure S6)
PMID:31495586	PBO:0102711	(Figure S6)
PMID:31495586	PBO:0102711	(Figure S6)
PMID:31495586	PBO:0102722	(Figure S3)
PMID:31495586	PBO:0102719	(Figure S3)
PMID:31495586	PBO:0102723	(Figure S3)
PMID:31495586	PBO:0102711	(Figure S6)
PMID:31495586	PBO:0102735	(comment: 1.1 fold,) Figure S2
PMID:31495586	FYPO:0006108	(Figure 3)
PMID:31495586	FYPO:0002021	(Figure 6)
PMID:31495586	FYPO:0002030	(Figure 6)
PMID:31495586	PBO:0102710	(Figure 6)
PMID:31495586	PBO:0102711	(Figure 6)
PMID:31495586	PBO:0102712	(Figure 4)
PMID:31495586	PBO:0102713	(Figure 4 and 6)
PMID:31495586	PBO:0102714	(Figure 4 and 6)
PMID:31495586	PBO:0102715	(Figure 4 and 6)
PMID:31495586	PBO:0102716	(Figure 1)
PMID:31495586	PBO:0102716	(Figure 1)
PMID:31495586	PBO:0102717	(comment: Increased 4-fold,) Figure2
PMID:31495586	PBO:0102718	(Figure 3)
PMID:31495586	PBO:0102719	(Figure 3)
PMID:31495586	PBO:0102720	(Figure 1)
PMID:31495586	PBO:0102721	(Figure 2)
PMID:31495586	PBO:0102717	(comment: Increased 4-fold,) FigureS1
PMID:31495586	PBO:0102717	(comment: Increased 4-fold,) Figure2
PMID:31495586	PBO:0102722	(Figure 3)
PMID:31495586	PBO:0102723	(Figure 3)
PMID:31495586	PBO:0102724	(Figure 3)
PMID:31495586	PBO:0102725	(Figure 3) (comment: assayed using Myo52)
PMID:31495586	PBO:0102726	(Figure 2)
PMID:31509478	PBO:0099932	(Figure 6A)
PMID:31509478	PBO:0096673	(Fig. 6)
PMID:31509478	FYPO:0001904	(comment: synonym =ring collapse) fig3F
PMID:31509478	PBO:0099934	(Fig. S3C)
PMID:31509478	PBO:0099934	(Fig. S3C)
PMID:31509478	PBO:0099934	(Fig. S3C)
PMID:31509478	PBO:0099934	(Fig. S3C)
PMID:31509478	FYPO:0002177	(Fig. 3)
PMID:31509478	FYPO:0002059	(Fig. 2)
PMID:31509478	FYPO:0002060	(Fig. 1)
PMID:31509478	FYPO:0005543	(Figure 3E)
PMID:31509478	FYPO:0005840	(Fig. 3F)
PMID:31509478	FYPO:0000650	(Fig. 3)
PMID:31509478	FYPO:0003343	(Fig. 3)
PMID:31509478	FYPO:0005543	(Figure 3E)
PMID:31509478	FYPO:0003343	(Fig. 3)
PMID:31509478	FYPO:0000650	(Fig. 3)
PMID:31509478	FYPO:0002059	(Figure 1)
PMID:31509478	FYPO:0002059	(Fig. 1)
PMID:31515876	PBO:0102517	Loz1 represses gene expression when zinc is in excess and growth in zinc deficient media leads to de-repression of its target genes. Expression from the pgk1DTATA promoter leads to higher levels of Loz1 accumulating inside of cells, which in turn leads to higher levels of gene repression under low zinc conditions (Figure 1B)
PMID:31515876	PBO:0102518	When Loz1 is expressed at a constant level inside of cells, it binds to the adh4 promoter in high zinc conditions and not in low zinc conditions (consistent with its role in gene repression in high zinc conditions
PMID:31515876	PBO:0102512	ChIP-seq, RNA-seq and northern blot analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 3B and 3C)
PMID:31515876	PBO:0102513	ChIP-seq, RNA-seq and northern blot analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 3B and 3C)
PMID:31515876	PBO:0102511	ChIP-seq, RNA-seq and northern blot analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 3B and 3C)
PMID:31515876	PBO:0102510	ChIP-seq, RNA-seq and northern blot analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 3B and 3C)
PMID:31515876	PBO:0102509	deletion of loz1 leads to increased expression of this transcript in high zinc growth conditions (inferred from RNA seq analysis - see Table 1).
PMID:31515876	PBO:0102508	ChIP-seq, RNA-seq and reporter gene analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 4)
PMID:31515876	PBO:0102507	ChIP-seq, RNA-seq and northern blot analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 3B and 3C)
PMID:31515876	PBO:0102506	deletion of loz1 leads to increased expression of this transcript in high zinc growth conditions (inferred from RNA seq analysis - see Table 1).
PMID:31515876	PBO:0102505	deletion of loz1 leads to increased expression of this transcript in high zinc growth conditions (inferred from RNA seq analysis - see Table 1).
PMID:31515876	PBO:0102514	ChIP-seq, RNA-seq and northern blot analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 3B and 3C)
PMID:31515876	PBO:0102515	When Loz1 is expressed at a constant level inside of cells, it binds to the zrt1 promoter in high zinc conditions and not in low zinc conditions (comment: consistent with its role in gene repression in high zinc conditions)
PMID:31515876	PBO:0102516	(comment: CHECK ADD SO TERM WHEN AVAILABLE ) Mutagenesis of 3 Loz1 response elements in the SPBC1348.06c promoter resulted in the promoter no longer being repressed in high zinc in a manner that is dependent upon Loz1 (see Figure 4). The minimal Loz1 DNA binding domain (amino acids 426-522) also binds to this motif in vitro (supplemental Fig 2), and multiple copies of this element are able to confer Loz1-mediated gene repression in a minimal reporter system - see Figure 6)
PMID:31532702	FYPO:0004668	(Figure S5)
PMID:31532702	PBO:0095634	(Figure 5B)
PMID:31532702	PBO:0105601	(Figure 5C, D)
PMID:31532702	FYPO:0002060	(comment: I didn't check the supp, but probably can only make this annotation?)
PMID:31532702	FYPO:0004159	(Figure 1B)
PMID:31532702	PBO:0105592	(Figure 1B)
PMID:31532702	PBO:0105593	(comment: single nucleus)
PMID:31532702	PBO:0105595	(Figure 1D)(comment: E . monopolar?)
PMID:31532702	PBO:0105596	(Figure 1B, D)
PMID:31532702	PBO:0105597	(Figure 2A)
PMID:31532702	PBO:0105598	top, Figure 3B, C)
PMID:31532702	PBO:0105599	(comment: meiosis I inital ) Figure 3B, C
PMID:31532702	PBO:0105600	(Figure 2A)
PMID:31532702	FYPO:0007081	(Figure S3B, C) (comment: pentrance, frequently like quadruple)
PMID:31532702	GO:0000073	The Nuf2-containing kinetochore complex serves as a physical fulcrum for microtubule-dependent SPB separation
PMID:31532702	FYPO:0007083	28 ~ 32 min, Figure 3B; and 24 ~ 28 min, Figure S3B)
PMID:31532702	FYPO:0006475	28 ~ 32 min, Figure 3B; and 24 ~ 28 min, Figure S3B)
PMID:31532702	PBO:0105602	meiotic . The Nuf2-containing kinetochore complex serves as a physical fulcrum for microtubule-dependent SPB separation
PMID:31532702	FYPO:0007080	(Figure 6D, E)
PMID:31532702	FYPO:0003566	(Figure 6A)
PMID:31532702	FYPO:0002060	(Figure 5I)
PMID:31532702	FYPO:0002060	(Figure 5H)
PMID:31532702	PBO:0095634	(Figure 5E)
PMID:31532702	FYPO:0000732	(Figure 5E)
PMID:31532702	FYPO:0000732	(Figure S6)
PMID:31532702	FYPO:0003566	(Figure 5G) (comment: this term referes to initial)
PMID:31538680	PBO:0105152	Mutant proliferates faster and with shorter lag than wild-type in sublethal concentrations of hydroxyurea, phleomycin or doxorubicin
PMID:31538680	FYPO:0000006	Mutant proliferates faster and with shorter lag than wild-type in sublethal concentrations of hydroxyurea, phleomycin or doxorubicin
PMID:31538680	FYPO:0000006	Mutant proliferates faster and with shorter lag than wild-type in sublethal concentrations of hydroxyurea, phleomycin or doxorubicin
PMID:31562247	FYPO:0000056	(Fig. 3a)
PMID:31562247	PBO:0097036	(Figure 4c)
PMID:31562247	FYPO:0003896	Indeed, no noticeable change in mitochondrial morphology or altered mitochondrion numbers were found in the three mutant cells cultured in glucose-rich EMM (Fig. 5, C and D).
PMID:31562247	PBO:0097038	(Figure 4a, b)
PMID:31562247	PBO:0097038	(Figure 4a, b)
PMID:31562247	FYPO:0003896	As shown in Fig. 5A, the changes in mitochondrial morphology were similar within 40 min of glucose starvation in the three mutant and WT cells
PMID:31562247	PBO:0097037	(Figure 4c)
PMID:31562247	FYPO:0002780	As shown in Fig. 6, A and B, ROS production under glucose starvation was reduced, but not abolished, in the absence of Dnm1 because only 􏰆25% of dnm1􏰇 cells were DCDHF-DA- positive after glucose starvation.
PMID:31562247	FYPO:0007611	(comment: CHECK (with decreased total volume -. new term requested)) Throughout the period of glucose starvation, mitochondria in dnm1􏰇 cells did not appear to fragment but shrunk over time (Fig. 3A). mitochondrion numbers remained largely unchanged during glucose starvation (Fig. 3B)
PMID:31563844	PBO:0093629	The UV sensitivity of a rad13Δ mutant, the 3’-endonuclease that functions in nucleotide excision repair (ortholog of human XPG) is increased in the double mutant with exo5Δ, suggesting that Exo5 does not have a function in nucleotide excision repair.
PMID:31563844	PBO:0093630	However, the exo5Δ mutant is more sensitive than isogenic wild-type to UV-irradiation and alkylating agents (Fig. 5A).
PMID:31563844	GO:0032042	The results from these experiments establish a redundant function in mitochondria for Exo5 and FEN1, presumably operating during the final steps of DNA replication in order to generate ligatable nicks.
PMID:31563844	GO:0032042	The results from these experiments establish a redundant function in mitochondria for Exo5 and FEN1, presumably operating during the final steps of DNA replication in order to generate ligatable nicks.
PMID:31563844	PBO:0110209	We observed a severe loss of mitochondrial DNA from the exo5Δ rad2Δ strain compared to the wild-type and single mutants, suggesting that Exo5 and FEN1 are redundantly required for mitochondrial DNA maintenance (Fig. 2C).
PMID:31563844	PBO:0110209	We observed a severe loss of mitochondrial DNA from the exo5Δ rad2Δ strain compared to the wild-type and single mutants, suggesting that Exo5 and FEN1 are redundantly required for mitochondrial DNA maintenance (Fig. 2C).
PMID:31563844	PBO:0093559	The double mutant also showed a minor growth defect on rich media containing glucose (Fig. 5D)
PMID:31563844	PBO:0093559	The double mutant also showed a minor growth defect on rich media containing glucose (Fig. 5D)
PMID:31563844	FYPO:0002061	Interestingly, while neither the single exo5Δ nor rad2Δ mutant is associated with a detectable mitochondrial growth phenotype, the double mutant exo5Δ rad2Δ showed a failure to grow on media lacking a fermentable carbon source (Fig. 2B).
PMID:31563844	FYPO:0002060	S. pombe exo5Δ strains are viable, indicating that spExo5 is not essential for mitochondrial genome stability (Fig. 2B).
PMID:31563844	FYPO:0002061	However, while overexpression of exo5-D207A in a rad3Δ background eliminated the cell elongation phenotype, it did not suppress lethality (Fig. 4A,B)
PMID:31563844	FYPO:0003503	However, while overexpression of exo5-D207A in a rad3Δ background eliminated the cell elongation phenotype, it did not suppress lethality (Fig. 4A,B)
PMID:31563844	FYPO:0003503	However, while overexpression of exo5-D207A in a rad3Δ background eliminated the cell elongation phenotype, it did not suppress lethality (Fig. 4A,B)
PMID:31563844	PBO:0110207	Examination of the cell morphology revealed that the cells were elongated, indicative of checkpoint activation [17] (Fig. 4B
PMID:31563844	PBO:0102116	Examination of the cell morphology revealed that the cells were elongated, indicative of checkpoint activation [17] (Fig. 4B
PMID:31563844	FYPO:0002061	This lethality was not due to the nuclease activity of the protein, since overexpression of the nuclease-deficient mutant (exo5-D207A) showed similar lethality.
PMID:31563844	GO:0036298	The Fanconi branch of ICL repair is represented by fml1+ and fan1+. Exo5+ is epistatic with fml1+, i.e. the double mutant is not more sensitive than the single mutants (Fig. 5E). Likewise, the exo5Δfan1Δ double mutant is not more sensitive than the single mutants (Supplementary Fig. S5A). These data suggest that Exo5 functions in the Fanconi pathway of ICL repair.
PMID:31563844	FYPO:0000102	Exo5Δ and pli1Δ show synergistic interactions indicating that they operate in different, competing pathways (Fig. 5F).
PMID:31563844	PBO:0094311	Exo5Δ and pli1Δ show synergistic interactions indicating that they operate in different, competing pathways (Fig. 5F).
PMID:31563844	PBO:0094311	Exo5Δ and pli1Δ show synergistic interactions indicating that they operate in different, competing pathways (Fig. 5F).
PMID:31563844	PBO:0110229	spExo5 showed activity on either substrate, with a preference for the 5’-ended substrate (Supplementary Fig. S2B).
PMID:31563844	GO:0005634	Wild-type Exo5+ showed diffuse cytoplasmic fluorescence and both nuclear and punctate mitochondrial fluorescence. The Exo5-M58A mutant showed diffuse cytoplasmic/nuclear fluorescence, but lacked punctate fluorescence suggesting its exclusion from the mitochondria. The Δ(1-57) mutant showed only punctate staining suggesting that this truncated form of Exo5 is solely localized to the mitochondria (Supplementary Table 2). Therefore, both sets of data are consistent with a model in which mitochondrial localization of spExo5 proceeds through translational initiation at Met58, whereas initiation at Met1 yields predominantly the cytoplasmic and nuclear forms.
PMID:31563844	PBO:0110228	spExo5 showed activity on either substrate, with a preference for the 5’-ended substrate (Supplementary Fig. S2B).
PMID:31563844	GO:0005739	Wild-type Exo5+ showed diffuse cytoplasmic fluorescence and both nuclear and punctate mitochondrial fluorescence. The Exo5-M58A mutant showed diffuse cytoplasmic/nuclear fluorescence, but lacked punctate fluorescence suggesting its exclusion from the mitochondria. The Δ(1-57) mutant showed only punctate staining suggesting that this truncated form of Exo5 is solely localized to the mitochondria (Supplementary Table 2). Therefore, both sets of data are consistent with a model in which mitochondrial localization of spExo5 proceeds through translational initiation at Met58, whereas initiation at Met1 yields predominantly the cytoplasmic and nuclear forms.
PMID:31563844	GO:0005634	The affinity-purified wild-type Exo5-FLAG protein showed two prominent species by immunoblot blot analysis (Fig. 2A). The upper band is consistent with the predicted molecular weight of spExo5-3XFLAG protein (~50 kDa), while the lower band is consistent with that of a protein starting at Met58, followed by loss of a small signal peptide upon mitochondrial entry (~43 kDa). Importantly, the M58A mutant lacked the lower band, as one would expect if translation of the mitochondrial species started at Met58 with the M58A mutation eliminating this initiation. Conversely, the Δ(1-57) mutant showed only the lower band, further supporting our model.
PMID:31563844	GO:0005739	The affinity-purified wild-type Exo5-FLAG protein showed two prominent species by immunoblot blot analysis (Fig. 2A). The upper band is consistent with the predicted molecular weight of spExo5-3XFLAG protein (~50 kDa), while the lower band is consistent with that of a protein starting at Met58, followed by loss of a small signal peptide upon mitochondrial entry (~43 kDa). Importantly, the M58A mutant lacked the lower band, as one would expect if translation of the mitochondrial species started at Met58 with the M58A mutation eliminating this initiation. Conversely, the Δ(1-57) mutant showed only the lower band, further supporting our model.
PMID:31563844	FYPO:0002061	Under these highly inducing conditions, Exo5-FLAG levels were increased dramatically, and cells carrying the Exo5+ plasmid showed a negative growth phenotype (Supplementary Fig. S3B).
PMID:31563844	PBO:0110206	Consistent with these studies, mutation of either of the analogous active site aspartates to alanines (D176A, D207A), abrogated the nuclease activity of spExo5 (Supplementary Fig. S2A).
PMID:31563844	PBO:0110206	Consistent with these studies, mutation of either of the analogous active site aspartates to alanines (D176A, D207A), abrogated the nuclease activity of spExo5 (Supplementary Fig. S2A).
PMID:31563844	GO:0051539	The purified enzyme shows an absorption at 410 nm, characteristic of a [4Fe-4S] iron-sulfur cluster (Fig. 1B,C).
PMID:31563844	GO:0051539	The purified enzyme shows an absorption at 410 nm, characteristic of a [4Fe-4S] iron-sulfur cluster (Fig. 1B,C).
PMID:31563844	GO:0036298	The Fanconi branch of ICL repair is represented by fml1+ and fan1+. Exo5+ is epistatic with fml1+, i.e. the double mutant is not more sensitive than the single mutants (Fig. 5E). Likewise, the exo5Δfan1Δ double mutant is not more sensitive than the single mutants (Supplementary Fig. S5A). These data suggest that Exo5 functions in the Fanconi pathway of ICL repair.
PMID:31563844	PBO:0094311	The crosslink sensitivity of pso2Δ is substantially higher than that of exo5Δ (Fig. 5B, C), while the double mutant exo5Δ pso2Δ shows an increased sensitivity to cis-platin (Fig. 5C, Supplementary Fig. S5B
PMID:31563844	PBO:0094311	The crosslink sensitivity of pso2Δ is substantially higher than that of exo5Δ (Fig. 5B, C), while the double mutant exo5Δ pso2Δ shows an increased sensitivity to cis-platin (Fig. 5C, Supplementary Fig. S5B
PMID:31563844	PBO:0094312	Furthermore, the deletion is particularly hypersensitive to interstrand crosslinking (ICL) agents such as 8-methoxypsoralen (Fig. 5B) and cis-platin (Fig. 5C). 8- methoxypsoralen intercalates into the DNA and forms interstrand crosslinks upon irradiation with visible light [23].
PMID:31563844	PBO:0093629	The UV sensitivity of a rad13Δ mutant, the 3’-endonuclease that functions in nucleotide excision repair (ortholog of human XPG) is increased in the double mutant with exo5Δ, suggesting that Exo5 does not have a function in nucleotide excision repair.
PMID:31563844	FYPO:0000102	Furthermore, the deletion is particularly hypersensitive to interstrand crosslinking (ICL) agents such as 8-methoxypsoralen (Fig. 5B) and cis-platin (Fig. 5C). 8- methoxypsoralen intercalates into the DNA and forms interstrand crosslinks upon irradiation with visible light [23].
PMID:31563844	PBO:0093616	Fission yeast Exo1 exonuclease is involved in Okazaki fragment maturation, double-strand break repair, mismatch repair, and interstrand crosslink repair [27-29]. While the single exo1Δ and exo5Δ mutants showed a comparable sensitivity to UV, MMS and ICL agents, the double mutant exo1Δ exo5Δ showed an increased sensitivity to these agents, indicating that Exo1 and Exo5 repair these damages with partial redundancy (Fig. 5A, Supplementary Fig. S4E).
PMID:31563844	PBO:0093616	Fission yeast Exo1 exonuclease is involved in Okazaki fragment maturation, double-strand break repair, mismatch repair, and interstrand crosslink repair [27-29]. While the single exo1Δ and exo5Δ mutants showed a comparable sensitivity to UV, MMS and ICL agents, the double mutant exo1Δ exo5Δ showed an increased sensitivity to these agents, indicating that Exo1 and Exo5 repair these damages with partial redundancy (Fig. 5A, Supplementary Fig. S4E).
PMID:31575705	FYPO:0000089	(Fig. 1A) growth inhibited by 0.005% MMS after 4 days
PMID:31575705	FYPO:0006318	(Fig. 2C) (comment: RTS1-RFB assay)
PMID:31575705	FYPO:0000089	The fft3-K418R-myc strain exhibited similar sensitivity to CPT and MMS than fft3Δ cells, indicating that the ATPase activity is required to promote cell resistance to replication stress.
PMID:31575705	FYPO:0006318	(comment: RTS1-RFB assay)
PMID:31575705	FYPO:0000957	(Figure 1A)
PMID:31575705	FYPO:0000957	(Figure 1A)
PMID:31575705	FYPO:0006686	(Fig. 1)
PMID:31575705	GO:0000785	(comment: constitutive)
PMID:31575705	FYPO:0003586	decreased replciation restart fig1 indicating that only one-third of forks arrested at the RTS1-RFB are efficiently restarted in the absence of Fft3.
PMID:31575705	FYPO:0007254	normal replciation restart/ HR-mediated fork restart RTS1-RFB assay. urprisingly, the induction of downstream RS in fft3-K418R-myc strain was similar to the one observed in wild-type cells (Fig 4D, bottom panel). This finding indicates that the lack of the ATPase activity does not impact the efficiency of HR-mediated fork restart.
PMID:31582398	PBO:0104162	(Figure. 5C, D) normal (comment: CHECK increased mitochondrial segregation during meiosis)
PMID:31582398	PBO:0104164	"""in the absence of Mcp5 in rho+ parental strain (strain PHP4xVA074; see Table S1), only 31.3% of the tetrads dissected (n = 16 tetrads) exhibited mtDNA segregation similar to that observed in Fig. 6 D."""
PMID:31582398	PBO:0104161	(Figure. 3C, D, E, F and Video 5)
PMID:31582398	FYPO:0007276	To verify that the attachment to microtubules was not necessary for segregation during meiosis, we employed parental cells lacking the microtubule-mitochondrial linker protein Mmb1 (Fu et al., 2011). Additionally, one of the parental cells had its mitochondria fluorescently labeled. In zygotes and asci resulting from this cross, we observed that parental mitochondria continued to remain segregated (Fig. S2, C and D).
PMID:31582398	PBO:0104161	(Figure. 3C, D, E, F and Video 5)
PMID:31584934	FYPO:0000957	(Fig. 6)
PMID:31584934	FYPO:0000085	(Fig. 6)
PMID:31584934	FYPO:0007160	(Fig. 3)
PMID:31584934	GO:0006335	(Fig. 3,4)
PMID:31584934	FYPO:0000089	(Fig. 6)
PMID:31584934	PBO:0105882	(Fig. 3c)
PMID:31584934	FYPO:0000473	(Fig. 7)
PMID:31584934	FYPO:0000085	(Fig. 6)
PMID:31584934	FYPO:0001690	(Fig. 6)
PMID:31584934	FYPO:0000085	(Fig. 6)
PMID:31584934	FYPO:0001690	(Fig. 6)
PMID:31584934	FYPO:0000089	(Fig. 6)
PMID:31584934	FYPO:0000095	(Fig. 6)
PMID:31584934	FYPO:0000957	(Fig. 6)
PMID:31584934	FYPO:0003906	(Fig. 6)
PMID:31584934	FYPO:0003906	(Fig. 6)
PMID:31584934	PBO:0105875	"(comment: changed to decreased from abolished based on ""H3-FLAG association with H3-H113D-HA was severely reduced)"
PMID:31584934	PBO:0093560	(Fig. 2)
PMID:31584934	PBO:0105881	"""Reciprocally, H3-H113D-HA association with wt H3 and H4 were severely reduced"""
PMID:31584934	FYPO:0002151	"""Consistent with this, we found that the deletion of pcf1 is synthetic lethal with the deletion of hip1, the gene encoding one subunit of the fission yeast HIRA complex (S4A Fig). T"""
PMID:31584934	FYPO:0007160	(Fig. 3)
PMID:31615333	PBO:0097132	(Figure 2 and 3)
PMID:31615333	FYPO:0006613	(Figure S3)
PMID:31615333	FYPO:0003165	(Figure 1c)
PMID:31615333	FYPO:0006613	(Figure S3)
PMID:31615333	PBO:0097134	(Figure 2 and S3)
PMID:31615333	PBO:0097133	(Figure 2) (comment: detected by northern blot analysis)
PMID:31615333	PBO:0097133	(Figure S1)
PMID:31615333	FYPO:0006613	(Figure S3)
PMID:31615333	PBO:0097132	(Figure 2 and 3)
PMID:31615333	PBO:0097134	(Figure 2 and S3)
PMID:31615333	PBO:0097134	(Figure 2 and S3)
PMID:31615768	PBO:0094444	(Figure 1E) (comment: unbundled microtubules seen in early mitosis)
PMID:31615768	PBO:0094442	(Fig. 4)
PMID:31615768	PBO:0024749	S2A/4
PMID:31615768	GO:0000776	S2A
PMID:31615768	FYPO:0002061	(Fig. 3I)
PMID:31615768	FYPO:0003307	(Fig. 3)
PMID:31615768	FYPO:0002638	(Fig. 3)
PMID:31615768	PBO:0094441	(Fig. 3)
PMID:31615768	FYPO:0007126	(Fig. 1C)
PMID:31615768	FYPO:0005722	(Fig. 1C)
PMID:31615768	PBO:0094440	(Figure S4)
PMID:31615768	FYPO:0006174	(Figure 1A)
PMID:31615768	PBO:0094439	Supp S2
PMID:31615768	PBO:0037411	Supp S2A/4
PMID:31615768	FYPO:0002061	(Figure S1)
PMID:31615768	PBO:0094438	(Fig. 3a) (comment: by cen2-GFP observation)
PMID:31615768	PBO:0094437	(Figure 1E) (comment: unbundled microtubules seen in early mitosis)
PMID:31615768	PBO:0094443	(Fig. 4)
PMID:31618856	FYPO:0006475	(Fig. 4)
PMID:31618856	FYPO:0005694	(Figure 2D)
PMID:31618856	FYPO:0005681	(comment: CHECK defective in microtubule growth during both interphase and mitosis)
PMID:31618856	FYPO:0005699	appears to retain normal microtubule nucleation activity
PMID:31618856	FYPO:0002061	(Fig. 1)
PMID:31618856	PBO:0102760	(Fig. 4)
PMID:31618856	FYPO:0004315	(Fig. 3)
PMID:31618856	FYPO:0000131	(Fig. 4)
PMID:31641022	FYPO:0002060	(Fig. 2)
PMID:31644361	PBO:0102680	Cdr1 directly phosphorylated Wee1, but Cdr1(K41A) did not (Figure 1H).
PMID:31644361	PBO:0102681	(Figure 1H) (in vitro) Cdr1 directly phosphorylated Wee1, but Cdr1(K41A) did not ().
PMID:31644361	PBO:0094002	(Figure 3A) Consistent with this model, wee1(4A) phosphorylation was reduced when compared with wild type, and its phosphorylation was not altered by cdr1∆ or cdr2∆ (
PMID:31644361	PBO:0020446	deed, cdr1∆ wee1(4A) cells divided at the same size as cdr1∆ cells
PMID:31644361	FYPO:0002061	(Figure 3C) Both wee1(4A) and cdr1∆ were synthetically lethal with cdc25-dD
PMID:31644361	FYPO:0002061	(Figure 3C) Both wee1(4A) and cdr1∆ were synthetically lethal with cdc25-dD
PMID:31644361	PBO:0099234	Along with enhanced Wee1 hyperphosphorylation, these cells divided at a smaller size than wild-type cells. These results show that Cdr1 localization to nodes is a limiting factor for phosphorylation of Wee1 and cell size at division
PMID:31644361	PBO:0102684	(Figure 5B) We tested the effects of artificially recruiting mEGFP-cdr1(∆460-482) back to nodes using cdr2-GFPbinding peptide (GBP)-mCherry, which contains the GBP. In this system, mEGFP-cdr1(∆460-482) colocalized with cdr2-GBP-mCherry at nodes.
PMID:31644361	PBO:0102682	(Figure 3, A and D) We confirmed that wee1(4A) protein level does not increase and still localizes to cortical nodes
PMID:31644361	PBO:0102679	(Fig. 1B) Cdr1 overexpression induced hyperphosphorylation of Wee1 and loss of Cdk1-pY15, indicating inhibition of Wee1 kinase activity
PMID:31644361	PBO:0101181	Accordingly, the size of wee1(4A) cells was largely (but not entirely) insensitive to Cdr1 overexpression (Figure 3G).
PMID:31644361	PBO:0093712	(Fig. 1C) overexpression of Cdr1 but not of Cdr2 resulted in reduced cell size in cdr1∆cdr2∆ cells (Figure 1C
PMID:31644361	FYPO:0001124	(Fig. 1) In contrast, Cdr2 overexpression induced hyperphosphorylation of Wee1 but no change in Cdk1-pY15
PMID:31644361	PBO:0094002	(Figure 1D) Phosphorylation of Wee1 in fission yeast cells was reduced in the catalytically inactive mutant cdr1(K41A)
PMID:31644361	PBO:0020446	(Figure 3B)
PMID:31644361	PBO:0102677	(Fig. 1B) Cdr1 overexpression induced hyperphosphorylation of Wee1 and loss of Cdk1-pY15, indicating inhibition of Wee1 kinase activity
PMID:31644361	PBO:0102678	(Fig. 1B) Cdr1 overexpression induced hyperphosphorylation of Wee1 and loss of Cdk1-pY15, indicating inhibition of Wee1 kinase activity
PMID:31644361	PBO:0102677	(Fig. 1B) In contrast, Cdr2 overexpression induced hyperphosphorylation of Wee1 but no change in Cdk1-pY15
PMID:31644361	PBO:0111082	(Figure 4A) We confirmed that S. pombe Cdk1- asM17 directly thiophosphorylates Wee1 and Wee1(K596L)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?) ----- COMMENT: 61b5b08d53bec31b 11 BCT25wJvpLwsSnBDCDQXMVETx5s (comment: CHECK Table ?)
PMID:31657618	PBO:0109290	(Fig. 3)
PMID:31657618	PBO:0109290	(Fig. 3)
PMID:31657618	PBO:0109290	(Fig. 3)
PMID:31657618	PBO:0109290	(Fig. 3)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	PBO:0109290	(Fig. 3)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	PBO:0109290	(Fig. 3)
PMID:31657618	FYPO:0001122	(Fig. 4)
PMID:31657618	FYPO:0001122	(Fig. 4)
PMID:31657618	FYPO:0001122	(Fig. 4)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	(comment: CHECK Table ?)
PMID:31712578	FYPO:0003612	Table S3; spore viability similar to wild type
PMID:31712578	FYPO:0004993	Table S3
PMID:31712578	FYPO:0003612	Table S3; spore viability similar to wild type
PMID:31712578	FYPO:0003612	Table S3; spore viability similar to wild type
PMID:31712578	FYPO:0003612	Table S3; spore viability similar to wild type
PMID:31712578	FYPO:0003612	Table S3; spore viability similar to wild type
PMID:31712578	FYPO:0004993	Table S3
PMID:31712578	FYPO:0004993	Table S3
PMID:31712578	FYPO:0004993	Table S3
PMID:31712578	FYPO:0004993	Table S3
PMID:31712578	FYPO:0003612	Table S3
PMID:31712578	FYPO:0003612	Table S3; spore viability lower than wild type (~50% of wild-type viability)
PMID:31712578	FYPO:0004993	Table S3
PMID:31712578	FYPO:0003612	Table S3; spore viability similar to wild type
PMID:31719112	PBO:0103649	(comment: temperature permissive for mcm4/cdc21-M68)
PMID:31719112	PBO:0103649	(comment: temperature restrictive for cdc22-M45)
PMID:31719163	PBO:0019716	localizes to division site after Gef1 and Scd2, but before contractile ring constriction begins
PMID:31719163	PBO:0019716	localizes to division site before Scd1, and before contractile ring constriction begins
PMID:31719163	PBO:0019716	localizes to division site before Scd1, and before contractile ring constriction begins
PMID:31748520	FYPO:0008121	See Figure 4
PMID:31748520	FYPO:0008117	See Figure 3c, 3d
PMID:31748520	FYPO:0008117	See Figure 3a, 3b Describes the biogenesis of a multisubunit complex from nascent proteins. (comment: Could be linked to pombase ID of one or several components of the complex)
PMID:31748520	FYPO:0001216	Normal Tra1 interaction with SAGA complex
PMID:31748520	PBO:0109866	(comment: RNA-seq)
PMID:31748520	PBO:0093626	(Fig. 5d)
PMID:31748520	PBO:0109865	Decreased Tra1 interaction with SAGA complex
PMID:31748520	PBO:0109865	Abolished Tra1 interaction with SAGA complex
PMID:31748520	PBO:0109865	Abolished Tra1 interaction with SAGA complex
PMID:31748520	PBO:0109865	Abolished Tra1 interaction with SAGA complex
PMID:31748520	FYPO:0008120	Abolished Tra1 interaction with SAGA complex
PMID:31748520	PBO:0109864	Decreased levels of Tra1 and Tra2 in SAGA and NuA4 complexes, respectively (Figure 2)
PMID:31748520	PBO:0109854	(comment: RNA-seq)
PMID:31748520	PBO:0109851	. Similarly, we observed about a twofold reduction of Tra2 levels from NuA4 (Fig. 2b).
PMID:31748520	PBO:0109850	MS analyses revealed a tenfold reduction of Tra1 from SAGA when Tti2 is depleted, as compared with control conditions (Fig. 2a). Similarly, we observed about a twofold reduction of Tra2 levels from NuA4 (Fig. 2b). Both approaches showed decreased interaction between newly synthesised Tra1 and affinity purified Spt7 in cells partially depleted of Tel2. These results demonstrate that TTT contributes to the de novo incorporation of Tra1 into the SAGA complex.
PMID:31748520	PBO:0109863	(Fig. 2e, 1f) (comment: CHECK spt7/tra1 pho84 and mei2 promoters. and spt7/tras ssa2 promoter)
PMID:31748520	PBO:0109862	(Fig. 2e, 1f) (comment: CHECK spt7/tra1 pho84 and mei2 promoters. and spt7/tras ssa2 promoter)
PMID:31748520	PBO:0109865	Abolished Tra1 interaction with SAGA complex spt20Δ mutants, without any other visible changes in its overall migration profile (Fig. 6a). Spt20 is therefore essential for Tra1 incorporation into SAGA.
PMID:31748520	GO:0005198	Tra2 contributes to the scaffolding and stabilisation of the entire NuA4 complex.
PMID:31748520	PBO:0109868	Silver staining analysis showed that Hsp90 inactivation causes a specific decrease of Tra1 in Spt7 purification eluates (Supplementary Fig. 6). effect is modest in this hypomorphic mutant, this observation supports the conclusion that Hsp90, like TTT, contributes to the de novo assembly of Tra1 into SAGA.
PMID:31748520	PBO:0109867	(comment: RNA-seq)
PMID:31748520	GO:0140463	Such distinct architectural roles provide a functional validation of the recent structural studies of yeast SAGA and NuA4, which showed that Tra1 occupies a peripheral position within SAGA
PMID:31748520	PBO:0109861	(Fig. 2e, 1f) (comment: CHECK spt7/tra1 pho84 and mei2 promoters. and spt7/tras ssa2 promoter)
PMID:31748520	PBO:0101995	(comment: RNA-seq)
PMID:31748520	PBO:0101995	(comment: RNA-seq)
PMID:31748520	PBO:0109854	(comment: RNA-seq)
PMID:31748520	PBO:0093580	(Fig. 5d) Phenotypic analyses of tra1-Sptra2 and tra1-Sctra1 strains showed that tra1-Sptra2 mutants are sensitive to HU and caffeine, similar to tra1Δ mutants
PMID:31748520	PBO:0109869	Importantly, quantitative MS analyses show that both Tra1-SpTra2 and Tra1-ScTra1 hybrid mutant proteins efficiently copurify with Tti2 (Supplementary Fig. 9b).
PMID:31748520	FYPO:0000963	whereas tra1-Sctra1 strains show no growth defects, as compared with wild-type cells (Fig. 5d).
PMID:31748520	FYPO:0001522	whereas tra1-Sctra1 strains show no growth defects, as compared with wild-type cells (Fig. 5d).
PMID:31748520	FYPO:0001855	(comment: RNA-seq)
PMID:31748520	PBO:0109870	Decreased levels of Tra1 and Tra2 in SAGA and NuA4 complexes, respectively (Figure 2)
PMID:31777937	GO:0140432	A novel 5′-hydroxyl dinucleotide hydrolase activity for the DXO/Rai1 family of enzymes
PMID:31811152	PBO:0105417	(Figure 1b) (comment: live cell observation)
PMID:31811152	PBO:0105416	(Figure 1b,4b) (comment: live cell observation)
PMID:31811152	PBO:0105419	(Figure 4A)
PMID:31811152	PBO:0105420	(Figure 1b) (comment: live cell observation)
PMID:31811152	PBO:0105416	(Figure 1b) (comment: live cell observation)
PMID:31811152	PBO:0105417	(Figure 1b) (comment: live cell observation)
PMID:31811152	PBO:0105426	(Figure 1c)
PMID:31811152	PBO:0105428	(comment: C24 locus) fig2
PMID:31811152	PBO:0105432	(Figure 4b) (comment: live cell observation)
PMID:31811152	PBO:0105431	(Figure 4b) (comment: live cell observation)
PMID:31811152	PBO:0105430	(Figure 4b)
PMID:31811152	PBO:0105429	(comment: C24 locus) fig2
PMID:31811152	PBO:0105426	(Figure 1c)
PMID:31811152	PBO:0105427	(Fig. 2)
PMID:31811152	PBO:0105427	(Fig. 2)
PMID:31811152	PBO:0105418	(Figure 1b) (comment: live cell observation)
PMID:31811152	PBO:0105416	(Figure 1b) (comment: live cell observation)
PMID:31811152	PBO:0105421	(Figure 1b) (comment: live cell observation)
PMID:31811152	PBO:0105416	(Figure 1b) (comment: live cell observation)
PMID:31811152	PBO:0105422	(Figure 4a) (comment: homologous pairing examined at C24 locus)
PMID:31833215	FYPO:0000245	(comment: same as maf1delta alone)
PMID:31837996	FYPO:0000854	(comment: similar to pob3delta alone)
PMID:31837996	FYPO:0005917	(comment: RNA-seq)
PMID:31837996	PBO:0104317	(comment: RNA-seq)
PMID:31837996	FYPO:0005917	(comment: RNA-seq)
PMID:31837996	PBO:0104322	(comment: assayed using bulk histones)
PMID:31837996	PBO:0104317	(comment: RNA-seq)
PMID:31837996	PBO:0104317	(comment: RNA-seq)
PMID:31837996	PBO:0104321	(comment: assayed using bulk histones)
PMID:31837996	PBO:0104318	(comment: similar to pob3delta alone)
PMID:31883795	PBO:0095652	(Fig. S1B)
PMID:31883795	PBO:0095652	(Fig. S1E)
PMID:31883795	PBO:0095652	(Fig. S1E)
PMID:31883795	PBO:0095652	(Fig. S1E)
PMID:31883795	FYPO:0002336	(Fig. S2D)
PMID:31883795	FYPO:0002336	(Fig. S2D)
PMID:31883795	FYPO:0002336	(Fig. S2D)
PMID:31883795	PBO:0095652	(Fig. S1E)
PMID:31883795	PBO:0095652	(Fig. S1E)
PMID:31883795	PBO:0095652	(Fig. S1E)
PMID:31883795	PBO:0095653	(Fig. 1B)
PMID:31883795	PBO:0117335	(Fig. 1C)
PMID:31883795	GO:0034399	(Fig. 1E and F)
PMID:31883795	PBO:0095651	(Fig. 3F)
PMID:31883795	PBO:0095651	(Fig. 3F)
PMID:31883795	PBO:0117336	(Fig. 3G)
PMID:31883795	PBO:0117335	(Fig. 2G)
PMID:31883795	PBO:0117337	(Fig. 3H)
PMID:31883795	PBO:0117337	(Fig. 3H)
PMID:31883795	PBO:0117338	(Fig. 3C and D)
PMID:31883795	PBO:0117339	(Fig. 3C and D)
PMID:31883795	PBO:0117339	(Fig. 3C and D)
PMID:31883795	PBO:0117338	(Fig. 3C and D)
PMID:31883795	PBO:0117340	(Fig. 3C and D)
PMID:31883795	PBO:0117341	(Fig. 3C and D)
PMID:31883795	PBO:0117340	(Fig. 3C and D)
PMID:31883795	PBO:0117341	(Fig. 3C and D)
PMID:31883795	FYPO:0008369	(Fig. 4C and D)
PMID:31883795	FYPO:0008369	(Fig. 4C and D)
PMID:31883795	FYPO:0008369	(Fig. 4C and D)
PMID:31883795	PBO:0109209	(Fig. 5A and B)
PMID:31883795	PBO:0117342	(Fig. 5A and B)
PMID:31883795	PBO:0109209	(Fig. 5A and B)
PMID:31883795	PBO:0117342	(Fig. 5A and B)
PMID:31883795	PBO:0117342	(Fig. 5A and B)
PMID:31883795	GO:0140464	Our analyses show that RIXC bound to the H3K9me-Swi6 platform tethers heterochromatic regions to Amo1 at the nuclear periphery, which in turn stabilizes heterochromatin through suppression of histone turnover (Figure 7D).
PMID:31883795	PBO:0117346	Our analyses show that RIXC bound to the H3K9me-Swi6 platform tethers heterochromatic regions to Amo1 at the nuclear periphery, which in turn stabilizes heterochromatin through suppression of histone turnover (Figure 7D).
PMID:31883795	PBO:0095652	(Fig. S7C)
PMID:31883795	FYPO:0008364	(Fig. 5A and B)
PMID:31883795	PBO:0109215	(Fig. 5A and B)
PMID:31883795	PBO:0109215	(Fig. 5A and B)
PMID:31883795	FYPO:0008368	(Fig. 5A and B)
PMID:31883795	FYPO:0008368	(Fig. 5A and B)
PMID:31883795	PBO:0109215	(Fig. 5A and B)
PMID:31883795	PBO:0109215	(Fig. 5A and B)
PMID:31883795	FYPO:0008368	(Fig. 5A and B)
PMID:31883795	FYPO:0008368	(Fig. 5A and B)
PMID:31883795	FYPO:0008367	(Fig. 5D)
PMID:31883795	FYPO:0008367	(Fig. 5D)
PMID:31883795	PBO:0109209	(Fig. 6A and Fig. S6B)
PMID:31883795	PBO:0095652	(Fig. S7C)
PMID:31883795	FYPO:0008368	(Fig. 6A and Fig. S6B)
PMID:31883795	FYPO:0008368	(Fig. 6A and Fig. S6B)
PMID:31883795	PBO:0095653	(Fig. S2D)
PMID:31883795	PBO:0095652	(Fig. S2D)
PMID:31883795	PBO:0117343	(Fig. 6A and Fig. S6B)
PMID:31883795	PBO:0109215	(Fig. 6A and Fig. S6B)
PMID:31883795	PBO:0109215	(Fig. 6A and Fig. S6B)
PMID:31883795	PBO:0117344	(Fig. 6C)
PMID:31883795	PBO:0117345	(Fig. 6D)
PMID:31883795	PBO:0112767	(Fig. 6G)
PMID:31883795	PBO:0112331	(Fig. 6G)
PMID:31883795	PBO:0112331	(Fig. 6G)
PMID:31883795	PBO:0112331	(Fig. 6G)
PMID:31883795	PBO:0095652	(Fig. 7A)
PMID:31883795	PBO:0095652	(Fig. 7A)
PMID:31883795	PBO:0095651	(Fig. 7A)
PMID:31883795	PBO:0095651	(Fig. 7A)
PMID:31883795	PBO:0095652	(Fig. S1B)
PMID:31883795	PBO:0095652	(Fig. S1E)
PMID:31895039	PBO:0095067	(Fig. 2)
PMID:31895039	PBO:0095054	(Fig. 2)
PMID:31895039	PBO:0095070	(Fig. 2) (comment: CHECK Phenotype suppressed by the deletion of the pef1 gene)
PMID:31895039	PBO:0095071	(Fig. 2) (comment: CHECK Phenotype suppressed by the deletion of the pef1 gene)
PMID:31895039	FYPO:0002061	(Fig. 2b)
PMID:31895039	PBO:0095072	(Fig. 2 supp1)
PMID:31895039	FYPO:0000674	(Fig. 2)
PMID:31895039	FYPO:0002060	(Fig. 2) (comment: CONDITION 34°C)
PMID:31895039	FYPO:0000674	(Fig. 2)
PMID:31895039	FYPO:0002061	(Fig. 2)
PMID:31895039	PBO:0116188	Phosphorylates Rad21 on threonine 262. Fig. 2
PMID:31895039	PBO:0095060	(Fig. 2)
PMID:31895039	FYPO:0001234	"(Figure 1—Figure supplement 1) ""although colonies were tiny and grew very slowly"""
PMID:31895039	FYPO:0002061	(Figure 1—Figure supplement 1)
PMID:31895039	FYPO:0002060	(Figure 1—Figure supplement 1)
PMID:31895039	PBO:0095059	(Fig. 2)
PMID:31895039	PBO:0095058	(Fig. 2)
PMID:31895039	PBO:0095057	(Fig. 1c)
PMID:31895039	FYPO:0002060	(Fig. 1) (comment: CONDITION 36.5°C)
PMID:31895039	PBO:0095056	(Fig. 2)
PMID:31895039	FYPO:0002060	(Fig. 2) (comment: CONDITION 36.5°C)
PMID:31895039	FYPO:0002060	(comment: CONDITION 36.5°C)
PMID:31895039	PBO:0114608	(comment: antagonises pef1)
PMID:31895039	PBO:0095073	(Fig. 5g)
PMID:31895039	PBO:0095073	(Figure 5E, Figure 5—Figure supplement 1). Replacement of T262 by an alanine abolished in vitro Rad21 phosphorylation by Pef1-GFP
PMID:31895039	PBO:0095073	"(Figure 5D) ""In vitro Rad21 phosphorylation was abolished when Pef1 was purified from psl1 deleted cells"""
PMID:31895039	PBO:0114607	Pef1 ablation or chemical inactivation of its kinase activity stimulates Rad21 and Mis4 binding to their cognates sites on chromosomes. The effect in most prominent in the G1 phase of the mitotic cycle.
PMID:31895039	GO:0005634	Psm1 and Mis4 are found in Pef1 immunoprecipitates (Fig. 5AB)
PMID:31895039	PBO:0095054	(Fig. 7) The phenotype is exacerbated by pph3 deletion and rescued by pef1 deletion
PMID:31895039	PBO:0095055	(Figure 2, S1)
PMID:31895039	FYPO:0002060	(Fig. 2)
PMID:31895039	FYPO:0002060	(Fig. 2)
PMID:31895039	FYPO:0002060	(Fig. 2)
PMID:31895039	FYPO:0002060	(Fig. 2)
PMID:31895039	FYPO:0002060	(Fig. 2)
PMID:31895039	PBO:0095068	(Fig. 2)
PMID:31895039	PBO:0095054	(Fig. 2)
PMID:31895039	PBO:0033478	(Fig. 2)
PMID:31895039	PBO:0095069	(Fig. 2)
PMID:31895039	PBO:0095066	(Fig. 2)
PMID:31895039	PBO:0095065	(Fig. 2)
PMID:31895039	PBO:0095064	(Fig. 2)
PMID:31895039	FYPO:0002060	(Fig. 2)
PMID:31895039	FYPO:0002060	(comment: CONDITION 34°C), Fig. 2
PMID:31895039	FYPO:0002061	(comment: CONDITION 34°C), Fig. 2
PMID:31895039	PBO:0095063	(Fig. 2) Phenotype suppressed by the deletion of pef1
PMID:31895039	PBO:0095062	(Fig. 2) Phenotype suppressed by the deletion of pef1
PMID:31895039	PBO:0095069	(Fig. 2)
PMID:31911490	PBO:0106181	A nonphosphorylatable GST-Rnc1 fusion [GST-Rnc1(S/T6A)] expressed in fission yeast was several times less effective than the wild type (GST-Rnc1) in binding wak1Δ, wis1Δ , atf1Δ , pyp1Δ , and pyp2Δ mRNAs in vitro (Fig. 5A)
PMID:31911490	PBO:0106182	A nonphosphorylatable GST-Rnc1 fusion [GST-Rnc1(S/T6A)] expressed in fission yeast was several times less effective than the wild type (GST-Rnc1) in binding wak1Δ, wis1Δ , atf1Δ , pyp1Δ , and pyp2Δ mRNAs in vitro (Fig. 5A)
PMID:31911490	PBO:0106183	A nonphosphorylatable GST-Rnc1 fusion [GST-Rnc1(S/T6A)] expressed in fission yeast was several times less effective than the wild type (GST-Rnc1) in binding wak1Δ, wis1Δ , atf1Δ , pyp1Δ , and pyp2Δ mRNAs in vitro (Fig. 5A)
PMID:31911490	PBO:0106184	A nonphosphorylatable GST-Rnc1 fusion [GST-Rnc1(S/T6A)] expressed in fission yeast was several times less effective than the wild type (GST-Rnc1) in binding wak1Δ, wis1Δ , atf1Δ , pyp1Δ , and pyp2Δ mRNAs in vitro (Fig. 5A)
PMID:31911490	PBO:0106138	and enhanced expression of Wak1, Wis1, and Pyp1 proteins during unperturbed growth (Fig. 5C)
PMID:31911490	PBO:0106167	(Fig. 1B) cell length at division either of pmk1􏰂 cells or in a mutant strain lacking the dual-specificity phosphatase Pmp1 that dephosphorylates and inactivates Pmk1 in vivo (14), ... was similar to that of wild-type cells (Fig. 1B)
PMID:31911490	PBO:0106167	(Fig. 1B)
PMID:31911490	FYPO:0006822	(Fig. 1B)
PMID:31911490	FYPO:0006822	(Fig. 1B)
PMID:31911490	PBO:0092746	These results suggest that while T50 is a main phosphorylation site for Sty1 within Rnc1, other phosphosites are likely targeted by this kinase in vivo.
PMID:31911490	PBO:0093712	(Fig. 1B,1C) (14.04+0.25 versus 11.98+0.29μm, respectively)
PMID:31911490	PBO:0106138	(Fig. 2B)
PMID:31911490	PBO:0106144	(Fig. 1D). In addition, basal Sty1 activity was significantly higher in exponentially growing rnc1􏰂 cells expressing a genomic C-terminal hemagglutinin (HA)-tagged version of the MAP kinase, compared to wild-type cells or a pmk1􏰂 mutant
PMID:31911490	PBO:0101762	(Fig. 3f)
PMID:31911490	PBO:0106146	(Fig. 2)
PMID:31911490	PBO:0106155	Pyp2 protein levels increased +2 times in the mutant background (Fig. 5C), but they were of a lower magnitude than that in rnc1􏰂 versus wild-type cells (+8 to 9 times) (Fig. 2C
PMID:31911490	FYPO:0001122	(Fig. 1B)
PMID:31911490	PBO:0106180	A nonphosphorylatable GST-Rnc1 fusion [GST-Rnc1(S/T6A)] expressed in fission yeast was several times less effective than the wild type (GST-Rnc1) in binding wak1Δ, wis1Δ , atf1Δ , pyp1Δ , and pyp2Δ mRNAs in vitro (Fig. 5A)
PMID:31911490	PBO:0106160	(Fig. 2C)
PMID:31911490	FYPO:0006822	(comment:12.13 + 0.1)
PMID:31911490	PBO:0106164	(Fig. 4h)
PMID:31911490	PBO:0106170	(Fig. 5C)
PMID:31911490	PBO:0093712	(Fig. 5e)
PMID:31911490	PBO:0106157	(Fig. 5B)
PMID:31911490	PBO:0106176	(Fig. 4B)
PMID:31932483	FYPO:0000962	(Fig. 4B) (comment: CONDITION0.5 mM H2O2 in agar)
PMID:31932483	FYPO:0000962	(Fig. 4B) (comment: CONDITION0.5 mM H2O2 in agar)
PMID:31932483	FYPO:0000962	(Fig. 4B) (comment: CONDITION0.5 mM H2O2 in agar)
PMID:31932483	FYPO:0000087	(Fig. 4B) (comment: CONDITION0.5 mM H2O2 in agar)
PMID:31932483	FYPO:0000087	(Fig. 4B) (comment: CONDITION0.5 mM H2O2 in agar)
PMID:31932483	FYPO:0000087	(Fig. 4B) (comment: CONDITION 0.5 mM H2O2 in agar)
PMID:31932483	FYPO:0001214	(Fig. 4B) (comment: CONDITION 1M KCl in agar)
PMID:31932483	FYPO:0005947	(Fig. 4B) (comment: CONDITION 1M KCl in agar)
PMID:31932483	FYPO:0005947	(Fig. 4B) (comment: CONDITION 1M KCl in agar)
PMID:31932483	FYPO:0005947	(Fig. 4B) (comment: CONDITION 1M KCl in agar)
PMID:31932483	PBO:0101321	(Fig. 2)
PMID:31932483	MOD:00210	(Fig. 3)
PMID:31932483	PBO:0101320	(Fig. 4A)
PMID:31932483	PBO:0101319	(Fig. 7E)
PMID:31932483	PBO:0101318	(Fig. 6E)
PMID:31932483	FYPO:0007332	(Fig. 6F)
PMID:31932483	FYPO:0005947	(Fig. 4B) (comment: CONDITION 1M KCl in agar)
PMID:31932483	FYPO:0005947	(Fig. 4B) (comment: CONDITION 1M KCl in agar)
PMID:31932483	FYPO:0005947	(Fig. 4B) (comment: CONDITION 1M KCl in agar)
PMID:31932483	FYPO:0000962	(Fig. 4B) (comment: CONDITION0.5 mM H2O2 in agar)
PMID:31941401	PBO:0108221	(Figure 1E)
PMID:31941401	PBO:0105271	(comment: Pho8Δ60 assay) (Fig. S3A).
PMID:31941401	FYPO:0006295	(Figure 2A) (comment: Pho8Δ60 autophagy assay)
PMID:31941401	PBO:0108220	(Figure 3A, B)
PMID:31941401	PBO:0105271	In contrast, Pho8Δ60 activity was only restored to about half of the wild-type level when expressing Atg38[AIM mut]. AND Tdh1-YFP processing assay
PMID:31941401	FYPO:0006295	(Fig. S2)
PMID:31941401	PBO:0108221	(Figure 1G)
PMID:31941401	PBO:0108222	(Figure 1G)
PMID:31941401	PBO:0108228	(Figure 3A,B) but reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	PBO:0108227	(Figure 3A,B) but reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	PBO:0108226	(Figure 3A,B) but reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	PBO:0108225	(Figure 3A,B) but reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	PBO:0108224	(Figure 3A,B) but reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	PBO:0108223	(Figure 3A,B) but reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	PBO:0108222	(Figure 1G)
PMID:31941401	PBO:0108221	(Figure 1F)
PMID:31941401	PBO:0105271	(comment: Pho8Δ60 assay) (Fig. S3A).
PMID:31941401	FYPO:0000674	(Fig. S2)
PMID:31941401	FYPO:0006266	(Fig. S2)
PMID:31941401	FYPO:0006295	(Figure 1B)
PMID:31941401	PBO:0108221	(Figure 1G)
PMID:31941401	PBO:0108221	(Figure 1G)
PMID:31980821	FYPO:0007419	zoning of telomere foci within the nuclear envelope was severely impaired in bqt4Δ ter1Δ for vegetative and quiescent cells (Supplementary Figure S3D and E).
PMID:31980821	PBO:0094925	Indeed, in bqt4Δ ter1Δ cells the percentage of cells that are unable to form a colony increased in correlation with the massive accumulation of STEEx at D1 and D3 of senescence
PMID:31980821	PBO:0094922	TERRA level was higher in bqt4Δ than WT in vegetative cells and this difference was substantially intensified after 48H in quiescence (Figure 6A)
PMID:31980821	PBO:0094923	When ter1+ gene was deleted in bqt4Δ cells, we observed that the combination of telomere erosion and NE dissociation provokes a massive accumulation of TERRA in Vg cells and this robust increase in transcription is even stronger after 48H in quiescence
PMID:31980821	PBO:0094924	accumulation of TERRA depends on Cid14, a RNA poly adenyl-transferase, (Supplementary Figure S5)
PMID:31980821	FYPO:0002955	As previously shown, we observed that telomere erosion and STEEx formation in ter1Δ cells correlates with defects to exit properly from G0 (22)
PMID:31980821	FYPO:0006516	(Fig. 5A) bqt4delta/ telomerase + cells exhibited wild-type telomeres that were stable in post-mitotic cells
PMID:31980821	PBO:0038206	In contrast to ter1Δ cells in which the loss of growth capacity was progressive, the growth of bqt4Δ ter1Δ cells was severely impaired (Figure 4A and Supplementary Figure S2).
PMID:31980821	PBO:0094919	When ter1+ gene was deleted in bqt4Δ cells, we observed that the combination of telomere erosion and NE dissociation provokes a massive accumulation of TERRA in Vg cells and this robust increase in transcription is even stronger after 48H in quiescence
PMID:31980821	PBO:0094920	TERRA level was higher in bqt4Δ than WT in vegetative cells and this difference was substantially intensified after 48H in quiescence (Figure 6A)
PMID:31980821	FYPO:0007414	(Fig. 2B)
PMID:31980821	FYPO:0007269	(Figure 2D) We found that telomere attrition observed in the absence of telomerase did not significantly impair telomere hyperclusterization in quiescence. However, telomere clusterization did not reach WT level in ter1Δ cells after 3 days in G0.
PMID:31980821	FYPO:0007419	(Fig. 2D) althouh also the percentage of cells that contain a unique telomeric cluster in G0 after streaks 3 and 4 (Figure 2D). We found that telomere attrition observed in the absence of telomerase did not significantly impair telomere hyperclusterization in quiescence. However, telomere clusterization did not reach WT level in ter1Δ cells after 3 days in G0.
PMID:31980821	FYPO:0007419	(Fig. 3D) We confirmed that telomere foci moved from nuclear periphery to a more central area (zone 1 to zone 2 or 3) in bqt4Δ Vg cells
PMID:31980821	FYPO:0007419	zoning of telomere foci within the nuclear envelope was severely impaired in bqt4Δ ter1Δ for vegetative and quiescent cells (Supplementary Figure S3D and E).
PMID:31980821	PBO:0094921	STEEx were readily detected as two bands at 1500 and 900 bp, the highest one being prevalent (Figure 5A, right panel). Strikingly, we observed a massive accumulation of STEEx in quiescent bqt4Δ ter1Δ cells at early time points of quiescence (Figure 5A).
PMID:32012158	PBO:0094866	(Figure S3A)
PMID:32012158	PBO:0105681	(Figure S3A) COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED
PMID:32012158	PBO:0105682	(Figure S3A) COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED
PMID:32012158	PBO:0116215	The interaction between these proteins was abolished in the absence of red1 (Fig 3A), suggesting that Red1 physically links Mmi1 with the exosome. and Fig 4B The direct binding of Red1 with Rrp6 was also observed (Fig 4B).
PMID:32012158	PBO:0105684	(Figure 3A)
PMID:32012158	PBO:0105681	(Figure S3A) COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED
PMID:32012158	PBO:0105686	(Figure 5A)
PMID:32012158	PBO:0105687	(Figure 5B)
PMID:32012158	PBO:0095145	(Figure 5B)
PMID:32012158	PBO:0105688	(Figure 6A)
PMID:32012158	PBO:0105689	(Figure 1A)
PMID:32012158	PBO:0105690	(Figure 5A)
PMID:32012158	PBO:0094604	(Figure S3A)
PMID:32012158	PBO:0094605	(Figure S3A)
PMID:32012158	PBO:0094866	(Figure S3A)
PMID:32012158	FYPO:0006821	(Figure S3A)
PMID:32012158	FYPO:0002085	(Figure S3A)
PMID:32012158	PBO:0105680	(Figure 2)
PMID:32012158	PBO:0105679	(Figure 1A)
PMID:32012158	PBO:0095145	(Figure 2)
PMID:32012158	PBO:0105678	(Figure 1A)
PMID:32012158	PBO:0105677	(Figure 1A)
PMID:32012158	PBO:0105676	(Figure 1A)
PMID:32012158	PBO:0105675	(Figure 1A)
PMID:32012158	PBO:0094604	(Figure S3A)
PMID:32012158	PBO:0094605	(Figure S3A)
PMID:32012158	PBO:0105681	(Figure S3A) COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED IN GENOME
PMID:32023460	FYPO:0006330	(Figure 4, S4B).
PMID:32023460	PBO:0103693	(Figure 4, S4B).
PMID:32023460	PBO:0103691	Pil1 lacking the C terminus failed to interact with Scs2 (Figure S5F
PMID:32023460	GO:0007029	(comment: cortical)
PMID:32023460	PBO:0103690	decreased Pil1 protein abundance Figure S1F
PMID:32023460	FYPO:0007263	resulting in the formation of fewer punctate eisosomes (Figure S1B).
PMID:32023460	PBO:0103689	(Figure S1F). increased Pil1 phosphorylation was detected in these cells
PMID:32023460	FYPO:0007263	(comment: PMID:32023460) Of note, the PM coverage of eisosomes was also reduced in scs2Dscs22D cells (Figure S1B), implicating VAPs in the regulation of eisosome assembly.
PMID:32023460	FYPO:0002872	(Figures 1A, 1B) (EM) data also confirmed that eisosomes/MCC associated with the cER, especially with curved cER rims, over the lateral cell cortex in WT (Figures 1C and S1A). Such an association was abolished in scs2Dscs22D cells lacking ER-PM contacts.(comment: the Exp says more but I don't know how to capture that)
PMID:32023460	FYPO:0007268	the cortical tubular ER pattern changes slower than wild type
PMID:32023460	FYPO:0007268	the cortical tubular ER pattern changes slower than wild type
PMID:32023460	FYPO:0007273	increased cortical ER remodeling dynamics the cortical tubular ER pattern changes faster than wild type
PMID:32023460	FYPO:0007273	increased cortical ER remodeling dynamics
PMID:32023460	FYPO:0007273	increased cortical ER remodeling dynamics
PMID:32023460	FYPO:0007268	the cortical tubular ER pattern changes slower than wild type
PMID:32023460	FYPO:0007268	(Figure 3A) decreased cortical ER remodeling dynamics the cortical tubular ER pattern changes slower than wild type
PMID:32023460	FYPO:0007268	(Figure S3C). the cortical tubular ER pattern changes slower than wild type
PMID:32023460	FYPO:0007268	(Figure 3A) the cortical tubular ER pattern changes slower than wild type
PMID:32023460	FYPO:0007273	(Figure S5G). the cortical tubular ER pattern changes faster than wild type
PMID:32023460	FYPO:0007273	(Fig. 2) increased cortical ER remodeling dynamics
PMID:32023460	FYPO:0007273	(Fig. 2) increased cortical ER remodeling dynamics
PMID:32023460	FYPO:0007273	(Fig. 2) the cortical tubular ER pattern changes faster than wild type
PMID:32023460	FYPO:0007265	(Figure S1F). Pil1 mis-assembled into fewer and longer filaments
PMID:32023460	FYPO:0007268	(Figure S3D)
PMID:32023460	PBO:0103688	decreased Pil1 protein abundance Figure S1F
PMID:32023460	FYPO:0006330	(Figure 4, S4B).
PMID:32023460	FYPO:0006330	(Figure 4, S4B).
PMID:32023460	FYPO:0006330	(Figure 4, S4B).
PMID:32032353	PBO:0092298	(comment: S.p. wtf13 assayed; doesn't specify which isoform (or if it's both))
PMID:32032353	PBO:0092298	(comment: S.p. wtf13 assayed; doesn't specify which isoform (or if it's both))
PMID:32032353	FYPO:0000590	(comment: Both wtf21 alleles were found at equal frequency in the viable spores.)
PMID:32032353	GO:0110134	inferred from crosses involving hemizygous diploids
PMID:32032353	GO:0110134	inferred from crosses involving hemizygous diploids
PMID:32032353	GO:0005783	assayed by expressing S.k. ortholog in S.p.
PMID:32032353	PBO:0092298	assayed by expressing S.k. ortholog in S.p.
PMID:32032353	PBO:0092298	assayed by expressing S.k. ortholog in S.p.)
PMID:32047038	PBO:0095188	(Fig. 5G) The IP6-binding pocket formed between CSN2 and Rbx1 is remarkably conserved from yeasts to plants and humans (Figs. 2D and 3D). Deleting ipk1, the yeast IP6 synthase, abolishes Csn2 interaction with Cul1 in Schizosaccharomyces pombe
PMID:32047038	FYPO:0000268	(Fig. 5H) This defect in UV-resistance can be rescued by wild-type SpCsn2, but not its IP6 binding-deficient K70E mutant .
PMID:32047038	FYPO:0000969	(Fig. 5H) This defect in UV-resistance can be rescued by wild-type SpCsn2, but not its IP6 binding-deficient K70E mutant .
PMID:32047038	FYPO:0000268	(Fig. 5H) This defect in UV-resistance can be rescued by wild-type SpCsn2, but not its IP6 binding-deficient K70E mutant .
PMID:32053662	PBO:0105866	(Figure 5a-c)
PMID:32053662	PBO:0105866	(Figure 5a-c)
PMID:32053662	PBO:0105866	(Figure 5a-c)
PMID:32053662	PBO:0105866	(Figure 5a-c)
PMID:32053662	PBO:0105870	(Fig. 6b, c)
PMID:32053662	PBO:0105870	(Fig. 6b, c)
PMID:32053662	PBO:0105867	(Figure 5a-c)
PMID:32053662	PBO:0105868	(Fig. 6d)
PMID:32053662	PBO:0105869	(Fig. 6d)
PMID:32053662	PBO:0105870	(Fig. 6b, c)
PMID:32053662	PBO:0105870	(Fig. 6b, c)
PMID:32053662	PBO:0105870	(Fig. 6b, c)
PMID:32053662	PBO:0105866	(Figure 5a-c)
PMID:32053662	PBO:0105867	(Figure 5a-c)
PMID:32053662	PBO:0105869	(Fig. 6d)
PMID:32053662	PBO:0105866	(Figure 5a-c)
PMID:32062975	FYPO:0000091	(Figure 6B)
PMID:32062975	FYPO:0000141	(Figure 6A)
PMID:32062975	FYPO:0001903	(Figure 6A)
PMID:32062975	FYPO:0003736	(Figure 6A)
PMID:32071154	FYPO:0007323	(Fig. 4)
PMID:32071154	FYPO:0007321	(Fig. 4)
PMID:32071154	FYPO:0007321	(Fig. 4)
PMID:32071154	FYPO:0007321	(Fig. 4)
PMID:32071154	FYPO:0002061	(comment: polysome profile)
PMID:32071154	FYPO:0002061	(Fig. 7B)
PMID:32071154	FYPO:0002061	(Fig. 7B)
PMID:32071154	FYPO:0001357	(Fig. 7B)
PMID:32071154	FYPO:0002061	(Fig. 7B)
PMID:32071154	FYPO:0002061	(Fig. 7)
PMID:32071154	FYPO:0002061	(Fig. 7)
PMID:32071154	FYPO:0002061	(Fig. 7)
PMID:32071154	FYPO:0002061	(Fig. 7)
PMID:32071154	PBO:0106940	(Figure 6F)
PMID:32071154	PBO:0106940	(Figure 6F)
PMID:32071154	FYPO:0001897	(Figure 6E)
PMID:32071154	FYPO:0001897	(Figure 6E)
PMID:32071154	FYPO:0001896	(Fig. 6a)
PMID:32071154	FYPO:0001896	(Fig. 6a)
PMID:32071154	FYPO:0001896	(Fig. 6a)
PMID:32071154	FYPO:0001896	(Fig. 6a)
PMID:32071154	FYPO:0002348	(Fig. 5C)
PMID:32071154	FYPO:0007319	(Fig. 5C)
PMID:32071154	FYPO:0007319	(Fig. 5C)
PMID:32071154	FYPO:0007319	(Fig. 5C)
PMID:32071154	FYPO:0007323	(Fig. 4)
PMID:32071154	FYPO:0007323	(Fig. 4)
PMID:32071154	FYPO:0007321	(Fig. 4)
PMID:32071154	FYPO:0002350	(Figure 2C)
PMID:32071154	PBO:0106937	(Fig. 2B)
PMID:32071154	FYPO:0007317	(comment: polysome profile)
PMID:32075773	FYPO:0007301	(Fig. S2)
PMID:32075773	FYPO:0007301	(Fig. S2)
PMID:32075773	PBO:0108267	(Figure 1B)
PMID:32075773	FYPO:0007299	(Fig. 2B, S2B-D)
PMID:32075773	FYPO:0007301	(Fig. S2)
PMID:32075773	FYPO:0007299	(Fig. 2B, S2B-D)
PMID:32075773	FYPO:0007299	(Fig. 2B, S2B-D)
PMID:32075773	PBO:0100916	37C is a moderate heat shock for fission yeast, which does not slow growth nor exerts toxicity to wild-type cultures, but significantly affects the viability of cells lacking stress signaling components, such as the MAP kinase Sty1 (Figures 1E and S1B).
PMID:32075773	PBO:0108266	(Figure 1B)
PMID:32075773	FYPO:0007301	(Fig. S2A)
PMID:32075773	FYPO:0007299	(Fig. 2B, S2B-D)
PMID:32075773	FYPO:0007300	(Fig. 2B, S2B-D)
PMID:32075773	FYPO:0007299	(Fig. 2B, S2B-D)
PMID:32075773	FYPO:0007299	(Fig. 2B, S2B-D)
PMID:32075773	PBO:0108269	(Fig. 4D)
PMID:32075773	PBO:0108269	(Fig. 4D)
PMID:32075773	FYPO:0002348	(Fig. 3D) Lack of Mas5 abolishes both PAC formation and the assembly of stress granules.
PMID:32075773	FYPO:0007301	(Fig. S2)
PMID:32084401	PBO:0097957	(Fig. 2H) when plo1 kinase is inactivated at the restrictive temperature the HPM mutant does not bind to the SPB after release into mitosis
PMID:32084401	PBO:0097959	(Fig. 3A) when an integrated copy of cdc13HPM (at leu1 locus) is expressed from the cdc13 promoter the endogenous cdc13+ cells are advanced into mitosis. This suggests cdc13HPM can do some of events required for mitotic entry. This is independent of the G1/S cyclins
PMID:32084401	PBO:0097958	(Fig. 2H) cdc13HPM localisation to SPB in mitosis is dependent on plo1 activity
PMID:32084401	FYPO:0000776	FIGURE S1E Wee1-dependent CDK-Y15 phosphorylation was similar between Cdc13HPM-CDK and Cdc13WT-CDK
PMID:32084401	PBO:0097956	(Fig. 2G) when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced
PMID:32084401	PBO:0097955	(Fig. 2G) when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced
PMID:32084401	PBO:0097956	(Fig. 2G) when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced
PMID:32084401	PBO:0097955	(Fig. 2G) when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced
PMID:32084401	PBO:0018634	cdc13HPM mutant fails to localise to the SPB during G2
PMID:32084401	PBO:0097951	(Fig. 1B) cells blocked in G1 by nitrogen starvation and released in presence of nitrogen into S phase with cdc13+ switched off
PMID:32084401	FYPO:0001357	(Fig. S1A, S1C) cells arrested G1 in low nitrogen then released into S phase at restrictive temperature cells the tested for viability at 25°C after S phase with only ccdc13hpm
PMID:32084401	PBO:0097951	(Fig. S1D) cdc13+ and cdc13HPM are not differentially sensitive to rum1. S phase same in both strains in absence of rum1
PMID:32084401	PBO:0097952	(Fig. S1-E) cdc2 Y15 phosphorylation same in cdc13+ control and cdc13HPM strain endogenous cdc13+ is completely degraded so does not contribute in the HPM mutant
PMID:32084401	PBO:0097953	(Fig. 2B-D) Endogenous untagged nmt 41cdc13+ is expressed to allow cells to proceed into mitosis tagged exogenous cdc13HPM or cdc13+ control can be seen at SPB
PMID:32084401	PBO:0097954	(Fig. 2A) cells are unable to enter mitosis in absence of cdc13+ expression-no septated cells
PMID:32084401	FYPO:0002061	(Fig. 2A) cells expressing only cdc13HPM are unable to form colonies
PMID:32084401	PBO:0018346	cdc13HPM mutant can localise to SPB in mitosis
PMID:32084401	PBO:0097955	(Fig. 2G) when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced
PMID:32084401	PBO:0097956	(Fig. 2G) when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced
PMID:32084401	PBO:0097958	(Fig. 2H) cdc13HPM localisation to SPB in mitosis is dependent on plo1 activity
PMID:32101481	PBO:0100704	(Figure 6E)
PMID:32101481	PBO:0100702	(Figure 6D) Indeed, deleting components of the CR scaffolded by Cdc15 (e.g., pxl1 or fic1) suppressed tip septation in mid1Δ pom1as1cells to a similar degree as cdc15-22D (Figure 6, D and E).
PMID:32101481	PBO:0100695	(Figure 1A and 1B)
PMID:32101481	PBO:0100704	(Figure 2D)
PMID:32101481	FYPO:0007393	(Figure 2, C)
PMID:32101481	PBO:0100698	(comment: CHECK 4B?)
PMID:32101481	PBO:0100699	Though the length of CR formation (node appearance to complete ring) was similar in wild type, cdc15-22A, and cdc15-22D, the periods of maturation (interval between CR formation and constriction initiation) and constriction (start to end of CR diameter decrease) were shorter in cdc15-22A and longer in cdc15-22D (Figure 4F).
PMID:32101481	PBO:0100706	(Figure 6, A and B)
PMID:32101481	PBO:0100707	(Figure 6, A and B)
PMID:32101481	PBO:0100702	Indeed, the percentage of tip septa was significantly reduced in mid1Δ pom1as1 cdc15-22D cells (Figure 4G).
PMID:32101481	PBO:0100705	the slow-migrating, phosphorylated forms of Cdc15 were reduced in pom1Δ cells (Figure 3B), and recombinant Pom1 efficiently phosphorylated recombinant N-terminal (Cdc15N; amino acids [aa]1-460) ||||||. later....We conclude that Cdc15 is a key substrate in the Pom1-mediated tip occlusion pathway.
PMID:32101745	PBO:0099437	(Figure 4C,S3) Although the percentage of total reads was relatively small, the iss1-DC mutation caused a reproducible and statistically significant extension of the 30 end of transcripts by about 200 nt.
PMID:32101745	PBO:0094605	(Fig. 4g,S4, Figure 5A)
PMID:32101745	FYPO:0005420	(Fig. 4e) The 73 genes with increased expression in the iss1-DC mutant were evaluated for common functions and were strongly enriched for factors important for iron assimilation GO:0033212.
PMID:32101745	FYPO:0004170	(Figure 3F)
PMID:32101745	PBO:0094283	(Figure 3E)
PMID:32101745	PBO:0099436	(Figure 5B) the iss1-DC mutation significantly reduced H3K9me2 at both ssm4 and mei4).
PMID:32101745	PBO:0094679	(Figure 3A,B)
PMID:32101745	FYPO:0001357	(Figure 3A)
PMID:32101745	GO:1990251	(Figure 5H) We found that Iss1 assembles into nuclear dots, and these co-localized with Pla1, indicating that Iss1 also assembles in vivo with RNA elimination factors
PMID:32101745	PBO:0094604	(Fig. 4g,S4, Figure 5A)
PMID:32101745	PBO:0099438	(Figure 5B) the iss1-DC mutation significantly reduced H3K9me2 at both ssm4 and mei4).
PMID:32101745	PBO:0099439	(Figure 5F) the iss1-DC truncation did disrupt its interaction with Mmi1.
PMID:32101745	PBO:0099440	(Figure S5) However, the truncation did not reduce Iss1 interaction with Rrp6
PMID:32168916	PBO:0101607	(Figure 4) (comment: ALSO TFIIH but not sure which sunbunit)
PMID:32168916	FYPO:0004085	(Fig. 3)
PMID:32168916	FYPO:0004085	(Fig. 3)
PMID:32168916	PBO:0101610	(Figure 3,S4) (comment: ALSO TFIIH but not sure which sunbunit)
PMID:32168916	PBO:0101609	(Figure 3,S4) (comment: ALSO TFIIH but not sure which sunbunit)
PMID:32168916	PBO:0101609	(Figure 4) (comment: CHECK SAP155K700E restored splicing to prp10-1)
PMID:32168916	PBO:0101608	(Figure 4) (comment: ALSO TFIIH but not sure which sunbunit)
PMID:32168916	FYPO:0002060	(Figure S4)
PMID:32168916	FYPO:0002060	(Figure S4)
PMID:32168916	FYPO:0002060	(Figure S4)
PMID:32168916	FYPO:0002060	(Figure S4)
PMID:32204793	PBO:0105172	(comment: in complex with Sfr1) Figure 6
PMID:32204793	PBO:0105172	(comment: in complex with Swi5) Figure 6
PMID:32204793	PBO:0105170	(Figure 1; Figure supplement 1A)
PMID:32204793	PBO:0105170	(Figure 1; Figure supplement 1A)
PMID:32204793	PBO:0105170	(Figure 1; Figure supplement 1A; Figure 7C,D; Figure 7—Figure supplement 1A)
PMID:32204793	PBO:0105171	(Figure 7; Figure supplement 1B)
PMID:32204793	PBO:0105171	(Figure 7; Figure supplement 1B)
PMID:32204793	PBO:0105170	(Figure 7; Figure supplement 1B)
PMID:32204793	PBO:0105171	(Figure 7C,D)
PMID:32204793	PBO:0105171	(Figure 7C,D)
PMID:32204793	PBO:0105170	(Figure 7C,D)
PMID:32204793	FYPO:0000265	(Figure 1D; Figure 1—Figure supplement 1)
PMID:32204793	FYPO:0000265	(Figure 1D; Figure 1—Figure supplement 1)
PMID:32204793	PBO:0105169	(Figure 6—Figure supplement 1)
PMID:32204793	PBO:0105168	(Figure 5B; Figure 5—Figure supplement 1C)
PMID:32204793	PBO:0105169	(Figure 5B; Figure 5—Figure supplement 1C)
PMID:32204793	PBO:0105168	(Figure 5B; Figure 5—Figure supplement 1C)
PMID:32204793	PBO:0105167	(Figure 6—Figure supplement 1)
PMID:32204793	PBO:0105166	(Figure 5B) Figure 5—Figure supplement 1C
PMID:32204793	PBO:0110075	inferred from combination of in vitro assay and phenotypes; Figures 1 & 5, including supplements
PMID:32204793	PBO:0110075	inferred from combination of in vitro assay and phenotypes; Figures 1 & 5, including supplements
PMID:32204793	FYPO:0007346	(Figure 7A,B)
PMID:32204793	FYPO:0007346	(Figure 7A,B)
PMID:32204793	FYPO:0007346	(Figure 7A,B)
PMID:32269268	FYPO:0007531	(Fig. 5)
PMID:32269268	FYPO:0004573	(Fig. 4)
PMID:32269268	PBO:0107531	(Fig. 1)
PMID:32269268	PBO:0107525	"(comment: 25 degrees C; using ""low temperature"" to distinguish from 30 degrees C;) Fig 1"
PMID:32269268	PBO:0107530	(Fig. 1)
PMID:32269268	FYPO:0007226	(Fig. 5)
PMID:32269268	PBO:0107523	(Fig. 1)
PMID:32269268	FYPO:0000220	(Fig. S2)
PMID:32269268	FYPO:0000220	(Fig. 4)
PMID:32269268	PBO:0107529	(Fig. 1)
PMID:32269268	PBO:0033972	"(comment: 25 degrees C; using ""low temperature"" to distinguish from 30 degrees C;) Fig 1"
PMID:32269268	FYPO:0004573	(Fig. 2, S1)
PMID:32269268	FYPO:0004137	(Fig. 2)
PMID:32269268	GO:0140720	(comment: [vw added to cover missing EXP annotation based on localization phenotype below])
PMID:32269268	FYPO:0007654	(Fig. 5)
PMID:32269268	FYPO:0007653	(Fig. 5)
PMID:32269268	PBO:0107528	(Fig. 1)
PMID:32269268	PBO:0107526	(Fig. 1)
PMID:32269268	PBO:0107527	(Fig. 1)
PMID:32269268	PBO:0107524	"(comment: 25 degrees C; using ""low temperature"" to distinguish from 30 degrees C;) Fig 1"
PMID:32269268	PBO:0107526	(Fig. 1)
PMID:32269268	PBO:0107525	(Fig. 1)
PMID:32269268	PBO:0107524	"(comment: 25 degrees C; using ""low temperature"" to distinguish from 30 degrees C;) Fig 1"
PMID:32277274	FYPO:0000460	(Fig. a)
PMID:32277274	PBO:0106053	(Fig. 2)
PMID:32277274	FYPO:0007209	(Fig. b)
PMID:32282918	PBO:0094852	(Figure 11)
PMID:32282918	PBO:0094831	(Figure 11)
PMID:32282918	PBO:0094832	(Figure 11)
PMID:32282918	PBO:0094855	(Figure S1)
PMID:32282918	PBO:0094833	(Figure 11)
PMID:32282918	PBO:0094834	(Figure 11)
PMID:32282918	PBO:0094835	(Figure 11)
PMID:32282918	PBO:0094836	(Figure 11)
PMID:32282918	PBO:0094837	(Figure 11)
PMID:32282918	PBO:0094838	(Figure 11)
PMID:32282918	PBO:0094839	(Figure 11)
PMID:32282918	PBO:0094840	(Figure 11)
PMID:32282918	PBO:0094841	(Figure 11)
PMID:32282918	PBO:0094842	(Figure 11)
PMID:32282918	PBO:0094843	(Figure 11)
PMID:32282918	PBO:0094844	(Figure 11)
PMID:32282918	PBO:0094845	(Figure 11)
PMID:32282918	PBO:0094846	(Figure 11)
PMID:32282918	PBO:0094847	(Figure 11)
PMID:32282918	PBO:0094848	(Figure 11)
PMID:32282918	PBO:0094849	(Figure 11)
PMID:32282918	PBO:0094850	(Figure 11)
PMID:32282918	PBO:0094851	(Figure 11)
PMID:32282918	PBO:0094852	(Figure 11)
PMID:32282918	PBO:0094853	(Figure S1)
PMID:32282918	PBO:0094854	(Figure S1)
PMID:32282918	FYPO:0008034	(Figure S1)
PMID:32282918	PBO:0094856	(Figure S1)
PMID:32282918	PBO:0094856	(Figure S2)
PMID:32282918	PBO:0094856	(Figure S2)
PMID:32282918	PBO:0094856	(Figure S2)
PMID:32282918	PBO:0094856	(Figure S2)
PMID:32282918	PBO:0094856	(Figure S2)
PMID:32282918	PBO:0094857	(Figure S2)
PMID:32282918	PBO:0094857	(Figure S2)
PMID:32282918	PBO:0094857	(Figure S2)
PMID:32282918	PBO:0094857	(Figure S2)
PMID:32282918	PBO:0094857	(Figure S2)
PMID:32282918	FYPO:0001357	(Figure 1)
PMID:32282918	FYPO:0001357	(Figure 1)
PMID:32282918	FYPO:0001357	(Figure 1)
PMID:32282918	FYPO:0001357	(Figure S3)
PMID:32282918	FYPO:0001357	(Figure S3)
PMID:32282918	FYPO:0001357	(Figure 5C)
PMID:32282918	FYPO:0001357	(Figure 7A)
PMID:32282918	FYPO:0001357	(Figure 7A)
PMID:32282918	FYPO:0001357	(Figure 9B)
PMID:32282918	FYPO:0001357	(Figure 9B)
PMID:32282918	FYPO:0000082	(Figure 1)
PMID:32282918	FYPO:0001355	(Figure S3)
PMID:32282918	FYPO:0001355	(Figure S3)
PMID:32282918	FYPO:0002059	(Figure S3)
PMID:32282918	FYPO:0002059	(Figure S3)
PMID:32282918	FYPO:0001355	(Figure S3)
PMID:32282918	FYPO:0001355	(Figure S3)
PMID:32282918	FYPO:0002059	(Figure S3)
PMID:32282918	FYPO:0002059	(Figure S3)
PMID:32282918	PBO:0094778	(Figure S7)
PMID:32282918	PBO:0094772	(Figure S7)
PMID:32282918	PBO:0094781	(Figure S7)
PMID:32282918	PBO:0094773	(Figure S7)
PMID:32282918	PBO:0094785	(Figure S7)
PMID:32282918	PBO:0094788	(Figure S7)
PMID:32282918	PBO:0094789	(Figure S7)
PMID:32282918	PBO:0094791	(Figure S7)
PMID:32282918	PBO:0094792	(Figure S7)
PMID:32282918	PBO:0094794	(Figure S7)
PMID:32282918	PBO:0094795	(Figure S7)
PMID:32282918	PBO:0094796	(Figure S7)
PMID:32282918	PBO:0094800	(Figure S7)
PMID:32282918	PBO:0094803	(Figure S7)
PMID:32282918	PBO:0094805	(Figure S7)
PMID:32282918	PBO:0094810	(Figure S7)
PMID:32282918	PBO:0094812	(Figure S7)
PMID:32282918	PBO:0094815	(Figure S7)
PMID:32282918	PBO:0094817	(Figure S7)
PMID:32282918	PBO:0094822	(Figure S7)
PMID:32282918	PBO:0094828	(Figure S7)
PMID:32282918	PBO:0094832	(Figure S7)
PMID:32282918	PBO:0094833	(Figure S7)
PMID:32282918	PBO:0094834	(Figure S7)
PMID:32282918	PBO:0094837	(Figure S7)
PMID:32282918	PBO:0094838	(Figure S7)
PMID:32282918	PBO:0094839	(Figure S7)
PMID:32282918	PBO:0094840	(Figure S7)
PMID:32282918	PBO:0094841	(Figure S7)
PMID:32282918	PBO:0094842	(Figure S7)
PMID:32282918	PBO:0094843	(Figure S7)
PMID:32282918	PBO:0094844	(Figure S7)
PMID:32282918	PBO:0094847	(Figure S7)
PMID:32282918	PBO:0094848	(Figure S7)
PMID:32282918	PBO:0094849	(Figure S7)
PMID:32282918	PBO:0094852	(Figure S7)
PMID:32282918	FYPO:0002085	(Figure 1)
PMID:32282918	PBO:0094773	(Figure 3B, Figure 10)
PMID:32282918	PBO:0094772	(Figure 3B, Figure 10)
PMID:32282918	PBO:0094738	(Figure 3A)
PMID:32282918	PBO:0094771	(Figure 3A, 9C)
PMID:32282918	PBO:0094771	(Figure 3A)
PMID:32282918	FYPO:0001355	(Figure 2)
PMID:32282918	FYPO:0000080	(Figure 2)
PMID:32282918	FYPO:0000080	(Figure 2)
PMID:32282918	FYPO:0000080	(Figure 2)
PMID:32282918	FYPO:0000080	(Figure 2)
PMID:32282918	FYPO:0000080	(Figure 2)
PMID:32282918	FYPO:0002059	(Figure 1)
PMID:32282918	FYPO:0002059	(Figure 1)
PMID:32282918	FYPO:0002059	(Figure 1)
PMID:32282918	FYPO:0002059	(Figure 1)
PMID:32282918	FYPO:0002085	(Figure 1)
PMID:32282918	FYPO:0000080	(Figure 1)
PMID:32282918	FYPO:0000080	(Figure 1)
PMID:32282918	FYPO:0000082	(Figure 1)
PMID:32282918	FYPO:0000082	(Figure 1)
PMID:32282918	FYPO:0000080	(Figure 1)
PMID:32282918	FYPO:0000082	(Figure 1)
PMID:32282918	FYPO:0000082	(Figure 1)
PMID:32282918	PBO:0094774	(Figure 3B)
PMID:32282918	FYPO:0001355	(Figure 2)
PMID:32282918	PBO:0094772	(Figure 3B)
PMID:32282918	PBO:0094773	(Figure 3B)
PMID:32282918	PBO:0094774	(Figure 3B)
PMID:32282918	PBO:0094775	(Figure 3B)
PMID:32282918	PBO:0094776	(Figure 3B)
PMID:32282918	FYPO:0000082	(Figure 5A)
PMID:32282918	FYPO:0000082	(Figure 5A)
PMID:32282918	FYPO:0000082	(Figure 5A)
PMID:32282918	FYPO:0002059	(Figure 5A)
PMID:32282918	FYPO:0002059	(Figure 5A)
PMID:32282918	FYPO:0000082	(Figure 5A)
PMID:32282918	FYPO:0000082	(Figure 5A)
PMID:32282918	FYPO:0000082	(Figure 5A)
PMID:32282918	FYPO:0002059	(Figure 5A)
PMID:32282918	FYPO:0002059	(Figure 5A)
PMID:32282918	FYPO:0000080	(Figure 5A)
PMID:32282918	FYPO:0001357	(Figure 5B)
PMID:32282918	FYPO:0001357	(Figure 5B)
PMID:32282918	FYPO:0001357	(Figure 5B)
PMID:32282918	FYPO:0001357	(Figure 5B)
PMID:32282918	FYPO:0001355	(Figure 5B)
PMID:32282918	PBO:0094771	(Figure 6B)
PMID:32282918	PBO:0094771	(Figure 6B)
PMID:32282918	PBO:0094771	(Figure 6B)
PMID:32282918	PBO:0094771	(Figure 6B)
PMID:32282918	PBO:0094771	(Figure 6B)
PMID:32282918	FYPO:0001357	(Figure 6A)
PMID:32282918	FYPO:0001357	(Figure 6A)
PMID:32282918	FYPO:0001357	(Figure 6A)
PMID:32282918	FYPO:0001357	(Figure 6A)
PMID:32282918	FYPO:0001357	(Figure 6A)
PMID:32282918	PBO:0094771	(Figure 6B)
PMID:32282918	PBO:0094771	(Figure 6B)
PMID:32282918	PBO:0094771	(Figure 6B)
PMID:32282918	PBO:0094771	(Figure 6B)
PMID:32282918	PBO:0094771	(Figure 6B)
PMID:32282918	FYPO:0001357	(Figure 7A)
PMID:32282918	FYPO:0000080	(Figure 7A) pin∆ rescues the lethality of aps1∆ asp1-H397A
PMID:32282918	PBO:0094738	(Figure 7B)
PMID:32282918	FYPO:0002059	(Figure 7A)
PMID:32282918	FYPO:0002059	(Figure 7A)
PMID:32282918	FYPO:0002059	(Figure 7A)
PMID:32282918	FYPO:0002059	(Figure 7A)
PMID:32282918	FYPO:0001357	(Figure 8A)
PMID:32282918	FYPO:0001357	(Figure 8A)
PMID:32282918	FYPO:0001357	(Figure 8A)
PMID:32282918	FYPO:0001357	(Figure 8A)
PMID:32282918	FYPO:0001357	(Figure 8A)
PMID:32282918	PBO:0094771	(Figure 8B)
PMID:32282918	PBO:0094771	(Figure 8B)
PMID:32282918	PBO:0094771	(Figure 8B)
PMID:32282918	PBO:0094771	(Figure 8B)
PMID:32282918	PBO:0094771	(Figure 8B)
PMID:32282918	PBO:0094771	(Figure 8B)
PMID:32282918	PBO:0094738	(Figure 7B, 8B)
PMID:32282918	PBO:0094738	(Figure 7B)
PMID:32282918	PBO:0094738	(Figure 9C)
PMID:32282918	PBO:0094738	(Figure 9C)
PMID:32282918	PBO:0094771	(Figure 9C)
PMID:32282918	PBO:0094777	(Figure 9C)
PMID:32282918	FYPO:0000082	(Figure 9B)
PMID:32282918	FYPO:0000080	(Figure 9B)
PMID:32282918	FYPO:0000080	(Figure 9B)
PMID:32282918	FYPO:0001355	(Figure 9B)
PMID:32282918	FYPO:0001355	(Figure 9B)
PMID:32282918	FYPO:0001355	(Figure 9B)
PMID:32282918	FYPO:0001355	(Figure 9B)
PMID:32282918	FYPO:0001355	(Figure 9B)
PMID:32282918	FYPO:0001355	(Figure 9B)
PMID:32282918	PBO:0094778	(Figure 10)
PMID:32282918	PBO:0094780	(Figure 10)
PMID:32282918	PBO:0094781	(Figure 10)
PMID:32282918	PBO:0094782	(Figure 10)
PMID:32282918	PBO:0094783	(Figure 10)
PMID:32282918	PBO:0094784	(Figure 10)
PMID:32282918	PBO:0094785	(Figure 10)
PMID:32282918	PBO:0094786	(Figure 10)
PMID:32282918	PBO:0094787	(Figure 10)
PMID:32282918	PBO:0094788	(Figure 10)
PMID:32282918	PBO:0094789	(Figure 10)
PMID:32282918	PBO:0094790	(Figure 10)
PMID:32282918	PBO:0094791	(Figure 10)
PMID:32282918	PBO:0094792	(Figure 10)
PMID:32282918	PBO:0094793	(Figure 10)
PMID:32282918	PBO:0094794	(Figure 10)
PMID:32282918	PBO:0094795	(Figure 10)
PMID:32282918	PBO:0094796	(Figure 10)
PMID:32282918	PBO:0094797	(Figure 10)
PMID:32282918	PBO:0094798	(Figure 10)
PMID:32282918	PBO:0094799	(Figure 10)
PMID:32282918	PBO:0094800	(Figure 10)
PMID:32282918	PBO:0094801	(Figure 10)
PMID:32282918	PBO:0094802	(Figure 10)
PMID:32282918	PBO:0094803	(Figure 10)
PMID:32282918	PBO:0094779	(Figure 10)
PMID:32282918	PBO:0094804	(Figure 10)
PMID:32282918	PBO:0094805	(Figure 10)
PMID:32282918	PBO:0094806	(Figure 10)
PMID:32282918	PBO:0094807	(Figure 10)
PMID:32282918	PBO:0094808	(Figure 10)
PMID:32282918	PBO:0094809	(Figure 10)
PMID:32282918	PBO:0094810	(Figure 10)
PMID:32282918	PBO:0094811	(Figure 10)
PMID:32282918	PBO:0094812	(Figure 10)
PMID:32282918	PBO:0094813	(Figure 10)
PMID:32282918	PBO:0094814	(Figure 10)
PMID:32282918	PBO:0094815	(Figure 10)
PMID:32282918	PBO:0094816	(Figure 10)
PMID:32282918	PBO:0094817	(Figure 10)
PMID:32282918	PBO:0094818	(Figure 10)
PMID:32282918	PBO:0094819	(Figure 10)
PMID:32282918	PBO:0094820	(Figure 10)
PMID:32282918	PBO:0094821	(Figure 10)
PMID:32282918	PBO:0094822	(Figure 10)
PMID:32282918	PBO:0094823	(Figure 10)
PMID:32282918	PBO:0094824	(Figure 10)
PMID:32282918	PBO:0094825	(Figure 10)
PMID:32282918	PBO:0094826	(Figure 10)
PMID:32282918	PBO:0094827	(Figure 10)
PMID:32282918	PBO:0094828	(Figure 10)
PMID:32282918	PBO:0094829	(Figure 10)
PMID:32282918	PBO:0094830	(Figure 10)
PMID:32282918	PBO:0094778	(Figure 10)
PMID:32282918	PBO:0094772	(Figure 10)
PMID:32282918	PBO:0094780	(Figure 10)
PMID:32282918	PBO:0094781	(Figure 10)
PMID:32282918	PBO:0094782	(Figure 10)
PMID:32282918	PBO:0094783	(Figure 10)
PMID:32282918	PBO:0094773	(Figure 10)
PMID:32282918	PBO:0094784	(Figure 10)
PMID:32282918	PBO:0094785	(Figure 10)
PMID:32282918	PBO:0094786	(Figure 10)
PMID:32282918	PBO:0094788	(Figure 10)
PMID:32282918	PBO:0094789	(Figure 10)
PMID:32282918	PBO:0094790	(Figure 10)
PMID:32282918	PBO:0094792	(Figure 10)
PMID:32282918	PBO:0094794	(Figure 10)
PMID:32282918	PBO:0094796	(Figure 10)
PMID:32282918	PBO:0094797	(Figure 10)
PMID:32282918	PBO:0094798	(Figure 10)
PMID:32282918	PBO:0094800	(Figure 10)
PMID:32282918	PBO:0094803	(Figure 10)
PMID:32282918	PBO:0094779	(Figure 10)
PMID:32282918	PBO:0094804	(Figure 10)
PMID:32282918	PBO:0094806	(Figure 10)
PMID:32282918	PBO:0094807	(Figure 10)
PMID:32282918	PBO:0094808	(Figure 10)
PMID:32282918	PBO:0094809	(Figure 10)
PMID:32282918	PBO:0094810	(Figure 10)
PMID:32282918	PBO:0094811	(Figure 10)
PMID:32282918	PBO:0094812	(Figure 10)
PMID:32282918	PBO:0094813	(Figure 10)
PMID:32282918	PBO:0094814	(Figure 10)
PMID:32282918	PBO:0094815	(Figure 10)
PMID:32282918	PBO:0094817	(Figure 10)
PMID:32282918	PBO:0094819	(Figure 10)
PMID:32282918	PBO:0094820	(Figure 10)
PMID:32282918	PBO:0094821	(Figure 10)
PMID:32282918	PBO:0094822	(Figure 10)
PMID:32282918	PBO:0094825	(Figure 10)
PMID:32282918	PBO:0094826	(Figure 10)
PMID:32282918	PBO:0094828	(Figure 10)
PMID:32282918	PBO:0094829	(Figure 10)
PMID:32282918	PBO:0094830	(Figure 10)
PMID:32282918	PBO:0094831	(Figure 11)
PMID:32282918	PBO:0094832	(Figure 11)
PMID:32282918	PBO:0094833	(Figure 11)
PMID:32282918	PBO:0094834	(Figure 11)
PMID:32282918	PBO:0094835	(Figure 11)
PMID:32282918	PBO:0094836	(Figure 11)
PMID:32282918	PBO:0094837	(Figure 11)
PMID:32282918	PBO:0094838	(Figure 11)
PMID:32282918	PBO:0094839	(Figure 11)
PMID:32282918	PBO:0094840	(Figure 11)
PMID:32282918	PBO:0094841	(Figure 11)
PMID:32282918	PBO:0094842	(Figure 11)
PMID:32282918	PBO:0094843	(Figure 11)
PMID:32282918	PBO:0094844	(Figure 11)
PMID:32282918	PBO:0094845	(Figure 11)
PMID:32282918	PBO:0094846	(Figure 11)
PMID:32282918	PBO:0094847	(Figure 11)
PMID:32282918	PBO:0094848	(Figure 11)
PMID:32282918	PBO:0094849	(Figure 11)
PMID:32282918	PBO:0094850	(Figure 11)
PMID:32282918	PBO:0094851	(Figure 11)
PMID:32295063	PBO:0102522	KΔ::ade6+ monitored by qRT-PCR
PMID:32295063	PBO:0102536	Loss of the HMG domain of Lsd2 (but not Lsd1) produces inviable cells (lethal).
PMID:32295063	PBO:0102539	KΔ::ade6+ monitored by qRT-PCR
PMID:32295063	FYPO:0007339	(comment: CHECK compared to lsd1-ao single mutant)
PMID:32295063	FYPO:0003412	(comment: CHECK compared to Lsd1-ao single mutant)
PMID:32295063	PBO:0102552	KΔ::ade6+ monitored by qRT-PCR
PMID:32295063	GO:0031509	(Fig. 4C)
PMID:32295063	GO:0031509	(Fig. 4C)
PMID:32295063	GO:0031508	At all constitutive heterochromatic domains, lsd C-terminal mutants showed strong cumulative genetic interactions with clr3∆ and sir2∆, indicating that they play overlapping functions in epigenetic silencing. In particular, lsd2-∆C sir2∆ double mutants show the strongest silencing defects at centromeric regions and sub-telomeric regions, while lsd1-∆HMG clr3∆ double mutants have the most robust effect at the mating-type locus (Figure 7D).
PMID:32295063	GO:0031509	At all constitutive heterochromatic domains, lsd C-terminal mutants showed strong cumulative genetic interactions with clr3∆ and sir2∆, indicating that they play overlapping functions in epigenetic silencing. In particular, lsd2-∆C sir2∆ double mutants show the strongest silencing defects at centromeric regions and sub-telomeric regions, while lsd1-∆HMG clr3∆ double mutants have the most robust effect at the mating-type locus (Figure 7D).
PMID:32295063	GO:0030466	At all constitutive heterochromatic domains, lsd C-terminal mutants showed strong cumulative genetic interactions with clr3∆ and sir2∆, indicating that they play overlapping functions in epigenetic silencing. In particular, lsd2-∆C sir2∆ double mutants show the strongest silencing defects at centromeric regions and sub-telomeric regions, while lsd1-∆HMG clr3∆ double mutants have the most robust effect at the mating-type locus (Figure 7D).
PMID:32319721	PBO:0100665	(comment: CFU counts)
PMID:32320462	FYPO:0007676	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007676	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0004963	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007677	(comment: Evaluated with D4H sterol sensor; internal structures)
PMID:32320462	FYPO:0007676	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007676	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007677	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007677	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007677	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007440	Sterols accumulate in endosomes
PMID:32320462	FYPO:0007440	Sterols do not accumulate in endosomes after treatement with CK-666
PMID:32320462	FYPO:0007440	Sterols do not accumulate in endosomes after treatement with CK-666
PMID:32320462	FYPO:0007440	Sterols do not accumulate in endosomes
PMID:32320462	FYPO:0007439	Eisosomes protruding towards cell interior
PMID:32327557	PBO:0112499	(Fig. 2)
PMID:32327557	PBO:0097690	(Fig. 2)
PMID:32327557	PBO:0097689	(comment: CONDITION 5ug/mL)
PMID:32327557	PBO:0097688	(comment: Small rescue of cut7D pkl1D)
PMID:32327557	PBO:0097687	(Fig. 4)
PMID:32327557	PBO:0097686	(Fig. 4)
PMID:32327557	PBO:0097685	(Fig. 4)
PMID:32327557	PBO:0097684	(Fig. 3)
PMID:32327557	PBO:0097683	(Fig. 3)
PMID:32327557	PBO:0097682	(Fig. 3)
PMID:32327557	PBO:0097681	(Fig. 3)
PMID:32327557	PBO:0097681	(Fig. 3)
PMID:32327557	PBO:0097682	(Fig. 3)
PMID:32327557	PBO:0097681	(Fig. 3)
PMID:32327557	PBO:0097680	(Fig. 3)
PMID:32327557	PBO:0097679	(Fig. 3)
PMID:32327557	PBO:0097678	(Fig. 3)
PMID:32327557	PBO:0097677	(Fig. 3)
PMID:32327557	FYPO:0007987	(Fig. 2)
PMID:32327557	PBO:0097676	(Fig. 2)
PMID:32327557	PBO:0097675	(Fig. 2)
PMID:32327557	PBO:0097673	(Fig. 2)
PMID:32341083	PBO:0033067	(comment: HU absent)
PMID:32341083	FYPO:0001513	(comment: HU absent)
PMID:32341083	PBO:0033071	(comment: HU absent)
PMID:32341083	PBO:0104393	(comment: HU absent)
PMID:32355220	FYPO:0001859	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0007423	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0007423	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0001742	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0001742	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0005788	(comment: ade6B/ade6X at cen1)
PMID:32355220	PBO:0095493	(comment: ade6B/ade6X at cen1)
PMID:32355220	PBO:0095493	(comment: ade6B/ade6X at cen1)
PMID:32355220	PBO:0095493	(comment: ade6B/ade6X at cen1)
PMID:32355220	PBO:0095494	(comment: ade6B/ade6X at cen1)
PMID:32355220	PBO:0095494	(comment: ade6B/ade6X at cen1)
PMID:32355220	PBO:0095495	(comment: ade6B/ade6X at cen1)
PMID:32355220	PBO:0095494	(comment: ade6B/ade6X at cen1)
PMID:32355220	PBO:0095494	a(comment: de6B/ade6X at cen1)
PMID:32355220	PBO:0095494	(comment: ade6B/ade6X at cen1)
PMID:32355220	PBO:0095493	(comment: ade6B/ade6X at cen1)
PMID:32355220	PBO:0095493	(comment: ade6B/ade6X at cen1)
PMID:32355220	PBO:0095491	(comment: ade6B/ade6X at the ura4 locus)
PMID:32355220	PBO:0095492	ade6B/ade6X at the ura4 locus
PMID:32355220	PBO:0095491	(comment: ade6B/ade6X at the ura4 locus)
PMID:32355220	PBO:0095490	(comment: ade6B/ade6X at cen1)
PMID:32355220	PBO:0095490	(comment: ade6B/ade6X at cen1)
PMID:32355220	PBO:0095490	(comment: ade6B/ade6X at cen1)
PMID:32355220	FYPO:0006811	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0006810	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0007425	(comment: ade6B/ade6X at the ura4 locus)
PMID:32355220	FYPO:0006811	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0006811	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0006810	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0006810	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0007425	(comment: ade6B/ade6X at the ura4 locus)
PMID:32355220	FYPO:0006811	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0000185	(comment: ade6B/ade6X at the ura4 locus)
PMID:32355220	FYPO:0007423	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0007424	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0007424	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0007423	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0001742	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0006810	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0007423	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0000185	(comment: ade6B/ade6X at the ura4 locus)
PMID:32355220	FYPO:0006810	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0007425	(comment: ade6B/ade6X at the ura4 locus)
PMID:32355220	FYPO:0006811	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0006811	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0007423	(comment: An extrachromosome ChLC)
PMID:32361273	PBO:0104793	(Fig. 2) This conserved inhibitory phosphorylation occurs as the Cdc2-Cdc13 complex is being formed to prevent its premature activation during G2 phase
PMID:32361273	PBO:0104794	(Fig. 2D) length is 7.5 micron cf WT 6.2 in same conditions
PMID:32361273	PBO:0094966	(Fig. 2D) length is 10.299 micron cf WT 12.7 in same conditions
PMID:32361273	PBO:0104795	(Fig. 2E, S2A)
PMID:32361273	PBO:0104792	(Fig. 2)
PMID:32361273	PBO:0104791	(Fig. 2)
PMID:32361273	PBO:0104790	(Fig. 1C) (comment: i.e normal TOR signalloing)
PMID:32361273	PBO:0104795	(Fig. S2B)
PMID:32361273	PBO:0104795	(Fig. 2F)
PMID:32361273	FYPO:0001043	(Fig. 3)
PMID:32361273	PBO:0104797	(Fig. 3)
PMID:32361273	PBO:0104798	(Fig. 2F)
PMID:32361273	FYPO:0001043	(Fig. 3b)
PMID:32361273	FYPO:0001000	(Fig. 3)
PMID:32361273	PBO:0104791	deletion mutants of either ste9 or rum1 fail to degrade Cdc13 (Figures S4A and S4B).
PMID:32361273	PBO:0104791	deletion mutants of either ste9 or rum1 fail to degrade Cdc13 (Figures S4A and S4B).
PMID:32361273	PBO:0023774	(Figure S4D)
PMID:32361273	PBO:0099448	(Figure S4D)
PMID:32361273	PBO:0104789	(Fig. S1A)
PMID:32361273	PBO:0096075	(Fig. S1A)
PMID:32361273	FYPO:0000708	(Fig. 1)
PMID:32361273	FYPO:0001043	(Fig. 1)
PMID:32361273	PBO:0097920	(Fig. 1)
PMID:32361273	PBO:0101618	(Figure S4D)
PMID:32361273	PBO:0020550	(Figure S4D)
PMID:32361273	FYPO:0004233	Delay in the dephosphoryaltion of Ste9 and defect in the degradation of the cyclin Cdc13 in nitrogen starvation
PMID:32361273	FYPO:0000708	(Fig. 7A)
PMID:32361273	FYPO:0007476	(Fig. 2G) the use of cdc10 mutant backgrounds is common for checking the ability of cells to arrest in G1
PMID:32361273	PBO:0104799	(Fig. 2)
PMID:32361273	PBO:0104800	(Fig. 4) Notably, loss of cig1 and cig2 utterly overrode these defects
PMID:32361273	FYPO:0001387	Deletion of par1 also affected the survival of the wee1-50 mutant (Figure 4C), and this worsening of the phenotype correlated with the inability of the double wee1-50 par1D mutant to accumulate Rum1 (Figure 4D).
PMID:32361273	PBO:0103204	Deletion of par1 also affected the survival of the wee1-50 mutant (Figure 4C), and this worsening of the phenotype correlated with the inability of the double wee1-50 par1D mutant to accumulate Rum1 (Figure 4D).
PMID:32361273	PBO:0104801	(TAP-Par1F314Q), this interaction was reduced (Figure 6C)
PMID:32361273	PBO:0104802	(comment: protein phophatase substrate adaptor)
PMID:32361273	PBO:0096829	(Fig. 7)
PMID:32361273	PBO:0093823	(Fig. 1)
PMID:32361273	FYPO:0003345	(Fig. 1D) The cells also presented a defect in the degradation of the cyclin Cdc13 and a delay in the dephosphorylation of Ste9
PMID:32414915	PBO:0100930	The Meu13-Mcp7 complex activates the initiation step of DNA strand exchange by Dmc1. The Meu13-Mcp7 complex also stimulates Rad51-driven strand exchange to a much less extent in the presence of the Swi5-Sfr1 complex.
PMID:32414915	PBO:0100930	The Meu13-Mcp7 complex activates the initiation step of DNA strand exchange by Dmc1. The Meu13-Mcp7 complex also stimulates Rad51-driven strand exchange to a much less extent in the presence of the Swi5-Sfr1 complex.
PMID:32415063	PBO:0111092	Remarkably, strains carrying splice site mutations showed significant upregulation of the pho1 transcript (Fig. 3c), similar to the effect observed in pir2-1, cwf10- 1 and prtΔ (Figs. 1b, 2c and Supplementary Fig. 1b)
PMID:32415063	GO:0031047	These results confirm the biological significance of Pir2 association with splicing machinery and show that these factors collaborate to promote gene repression by lncRNAs.
PMID:32415063	FYPO:0002052	Importantly, cwf10-1 rescued the sporulation defect observed in rrp6Δ caused by the silencing of the byr2 gene by nam1 lncRNA (Fig. 2e), similar to pir2-1 (Fig. 1f).
PMID:32415063	PBO:0111092	A significant increase in the level of both pho1 and byr2 mRNAs in cwf10-1 as compared to WT confirmed that the splicing machinery indeed affects the expression of genes repressed by lncRNAs (Fig. 2c)
PMID:32415063	PBO:0111091	A significant increase in the level of both pho1 and byr2 mRNAs in cwf10-1 as compared to WT confirmed that the splicing machinery indeed affects the expression of genes repressed by lncRNAs (Fig. 2c)
PMID:32415063	PBO:0111097	However, the ago1Δ clr3Δ double mutant showed cumulative de-repression of pho1 (Fig. 5d).
PMID:32415063	PBO:0111092	The loss of Clr3 or Pob3 caused an increase in pho1 transcript levels, consistent with their involvement in repression by lncRNA8,38, but the extent of upregulation was less than in pir2-1 (Fig. 5c).
PMID:32415063	PBO:0111099	Moreover, quantitative ChIP analyses showed enrichment of Clr3 and Pob3 at prt-pho1 in WT cells and a reduced localization in pir2-1 cells (Fig. 5e).
PMID:32415063	PBO:0111098	Moreover, quantitative ChIP analyses showed enrichment of Clr3 and Pob3 at prt-pho1 in WT cells and a reduced localization in pir2-1 cells (Fig. 5e).
PMID:32415063	PBO:0111097	However, the ago1Δ clr3Δ double mutant showed cumulative de-repression of pho1 (Fig. 5d).
PMID:32415063	GO:0031047	Supporting the function of Pir2 and lncRNA in the same pathway, we found no additive effect on pho1 expression in the pir2-1 prtΔ double mutant when compared to the effect in the single mutants (Fig. 1e).
PMID:32415063	GO:0106222	Moreover, RNA immunoprecipitation sequencing analysis (RIP-seq) showed that Pir2 binds to the lncRNAs (Fig. 1d and Supplementary Fig. 1d)
PMID:32415063	PBO:0111093	Chromatin immunoprecipitation followed by sequencing (ChIP-seq) confirmed Pir2 enrichment at lncRNAs, including prt and nam1 (Fig. 1c and Supplementary Fig. 1c)
PMID:32415063	PBO:0111092	(Fig. 1b), similar to the effect observed upon deletion of the lncRNA (Supplementary Fig. 1b)6,7,11.
PMID:32415063	PBO:0111092	The loss of Clr3 or Pob3 caused an increase in pho1 transcript levels, consistent with their involvement in repression by lncRNA8,38, but the extent of upregulation was less than in pir2-1 (Fig. 5c).
PMID:32415063	PBO:0111092	Cells lacking Ago1 showed a considerable increase in pho1 transcript levels as determined by northern blot analysis (Fig. 4e), but the observed effect was weaker than in pir2-1 or cwf10-1, suggesting that additional factors likely cooperate with Pir2- splicing machinery.
PMID:32415063	PBO:0111096	We next wondered whether cryptic introns are required for Pir2- dependent generation of siRNAs. Mutations of the pho1 cryptic intron splice sites in rrp6Δ cells abolished the production of siRNAs mapping to the entire prt lncRNA, including the region upstream of pho1 (Fig. 4d). This result suggests that the cryptic intron acts as part of the prt lncRNA to engage RNAi machinery. Importantly, siRNAs mapping to other loci were not affected (Fig. 4d and Supplementary Fig. 5)
PMID:32415063	FYPO:0006076	We then analyzed the role of Pir2 in siRNA production in cells lacking Rrp6, which show accumulation of lncRNAs and robust repression of their target loci. We found that siRNAs, which ranged in size from 20-24 nt and mapped to lncRNAs targeting pho1 and byr2, were abolished in both pir2-1 and cwf10-1 mutant backgrounds (Fig. 4c and Supplementary Fig. 4a, b). Pir2 was also required for siRNA production at Tf2 elements, pericentromeric repeats, and other loci (Fig. 4c, Supplementary Fig. 5 and Supplementary Data 2).
PMID:32415063	FYPO:0006076	We then analyzed the role of Pir2 in siRNA production in cells lacking Rrp6, which show accumulation of lncRNAs and robust repression of their target loci. We found that siRNAs, which ranged in size from 20-24 nt and mapped to lncRNAs targeting pho1 and byr2, were abolished in both pir2-1 and cwf10-1 mutant backgrounds (Fig. 4c and Supplementary Fig. 4a, b).
PMID:32415063	PBO:0111089	The lncRNA-mediated repression of pho1 was impaired in cbc1-1 cells (Supplementary Fig. 1e), sug-
PMID:32415063	PBO:0111092	The lncRNA-mediated repression of pho1 was impaired in cbc1-1 cells (Supplementary Fig. 1e)
PMID:32415063	FYPO:0002052	Remarkably, entry into meiosis and sporulation efficiency were restored in pir2-1 rrp6Δ cells (Fig. 1f).
PMID:32415063	PBO:0093929	We asked if Pir2 is also required for the repression of byr2 that is observed upon the accumulation of nam1 lncRNA in cells lacking Rrp6. Since byr2 is required for meiotic induction, cells lacking Rrp6 are defective in sporulation (Fig. 1f)11.
PMID:32415063	GO:0031047	The requirement for Pir2 in mediating the repressive effects of lncRNAs is a highly significant finding.
PMID:32415063	PBO:0111089	Loss of the MTREC subunit Red1 resulted in the accumulation of longer readthrough transcripts (referred to as prt-L and nam1-L) (Fig. 1a), as was also observed in mmi1Δ and rrp6Δ cells (Fig. 1a and Supplementary Fig. 1a)6,7,11.
PMID:32415063	PBO:0111090	Loss of the MTREC subunit Red1 resulted in the accumulation of longer readthrough transcripts (referred to as prt-L and nam1-L) (Fig. 1a), as was also observed in mmi1Δ and rrp6Δ cells (Fig. 1a and Supplementary Fig. 1a)6,7,11.
PMID:32415063	PBO:0111089	as was also observed in mmi1Δ and rrp6Δ cells (Fig. 1a and Supplementary Fig. 1a)
PMID:32415063	PBO:0111089	as was also observed in mmi1Δ and rrp6Δ cells (Fig. 1a and Supplementary Fig. 1a)
PMID:32415063	PBO:0111090	as was also observed in mmi1Δ and rrp6Δ cells (Fig. 1a and Supplementary Fig. 1a)
PMID:32415063	PBO:0111090	as was also observed in mmi1Δ and rrp6Δ cells (Fig. 1a and Supplementary Fig. 1a)
PMID:32415063	PBO:0111091	Surprisingly, pir2-1 showed a drastic upregulation of pho1 and byr2 genes as compared to wild-type (WT) (Fig. 1b)
PMID:32415063	PBO:0111092	Surprisingly, pir2-1 showed a drastic upregulation of pho1 and byr2 genes as compared to wild-type (WT) (Fig. 1b)
PMID:32415063	PBO:0111097	However, the ago1Δ clr3Δ double mutant showed cumulative de-repression of pho1 (Fig. 5d).
PMID:32415063	PBO:0111091	(Fig. 1b), similar to the effect observed upon deletion of the lncRNA (Supplementary Fig. 1b)6,7,11.
PMID:32415063	PBO:0111092	(Fig. 1b), similar to the effect observed upon deletion of the lncRNA (Supplementary Fig. 1b)6,7,11.
PMID:32415063	PBO:0111091	(Fig. 1b), similar to the effect observed upon deletion of the lncRNA (Supplementary Fig. 1b)6,7,11.
PMID:32415063	PBO:0111095	Interestingly, this interaction was impaired in the cwf10- 1 mutant, indicating that splicing factors are required for association of Pir2 with Hrr1 (Fig. 4b)
PMID:32415063	PBO:0111092	Remarkably, strains carrying splice site mutations showed significant upregulation of the pho1 transcript (Fig. 3c), similar to the effect observed in pir2-1, cwf10- 1 and prtΔ (Figs. 1b, 2c and Supplementary Fig. 1b)
PMID:32496538	FYPO:0005518	(Supplementary Fig S8)
PMID:32496538	FYPO:0002913	(Figure 2)
PMID:32496538	FYPO:0006996	(Figure 2)
PMID:32496538	FYPO:0006996	(Figure 4 and Supplementary Fig S5)
PMID:32496538	FYPO:0006996	(Figure 4 and Supplementary Fig S5)
PMID:32496538	FYPO:0007347	(Supplementary Fig S7)
PMID:32496538	FYPO:0005516	(Figure 6 and Supplementary Fig S8)
PMID:32496538	FYPO:0004347	(Figure 6 and Supplementary Fig S8)
PMID:32496538	PBO:0101605	(Supplementary Fig S7)
PMID:32496538	FYPO:0002913	(Figure 4 and Supplementary Fig S5)
PMID:32496538	FYPO:0002913	(Figure 4 and Supplementary Fig S5)
PMID:32496538	FYPO:0002913	(Figure 4 and Supplementary Fig S5)
PMID:32496538	FYPO:0002913	(Figure 1, 2 and 4) Supplementary Fig S1, S3 and S5
PMID:32496538	FYPO:0002913	(Figure 2)
PMID:32496538	FYPO:0007347	(Supplementary Fig S7)
PMID:32496538	FYPO:0005518	(Figure 6 and Supplementary Fig S8)
PMID:32496538	FYPO:0007347	(Supplementary Fig S7)
PMID:32496538	FYPO:0002913	(Figure 1, 2 and 4) Supplementary Fig S1, S3 and S5
PMID:32496538	FYPO:0002913	(Figure 1, 2 and 4) Supplementary Fig S1, S3 and S5
PMID:32496538	PBO:0101606	(Supplementary Fig S7)
PMID:32496538	FYPO:0002913	(Figure 2)
PMID:32496538	FYPO:0006996	(Figure 4 and Supplementary Fig S5)
PMID:32496538	FYPO:0002913	(Figure 4 and Supplementary Fig S5)
PMID:32496538	FYPO:0002913	(Figure 2)
PMID:32496538	FYPO:0002913	(Figure 2)
PMID:32496538	FYPO:0002913	(Figure 4 and Supplementary Fig S5)
PMID:32496538	FYPO:0002913	(Figure 4 and Supplementary Fig S5)
PMID:32496538	PBO:0101604	(Figure 5)
PMID:32496538	PBO:0095888	(Figure 5)
PMID:32496538	PBO:0101604	(Figure 5) rbp1 also Figure 7
PMID:32496538	PBO:0095888	(Figure 5) rbp1 also Figure 7
PMID:32496538	PBO:0101604	(Figure 5) rbp1 also Figure 7
PMID:32496538	PBO:0095888	(Figure 5) rbp1 also Figure 7
PMID:32496538	PBO:0101605	(Supplementary Fig S7)
PMID:32496538	FYPO:0005518	(Supplementary Fig S8)
PMID:32496538	FYPO:0005518	(Supplementary Fig S8)
PMID:32499400	PBO:0101148	(comment: CONDITION EMM -U agar plates, supplemented with 6AU concentration ranging from 3.6 to 150 ug/mL)
PMID:32499400	PBO:0101155	(comment: at lncRNAs upstream of PHO regulon genes (nc-tgp1, nc-pho1, prt1))
PMID:32499400	PBO:0101151	(comment: CHECK at tgp1 promoter)
PMID:32499400	PBO:0101156	(comment: at lncRNAs upstream of PHO regulon genes (nc-tgp1, nc-pho1, prt1))
PMID:32499400	PBO:0101157	(comment: also assayed genome-wide)
PMID:32499400	PBO:0101157	(comment: also assayed genome-wide)
PMID:32499400	PBO:0101147	(comment: CONDITION 100 ug/mL MPA)
PMID:32499400	FYPO:0007411	(comment: at different lncRNA polyadenylation sites)
PMID:32499408	PBO:0098591	(Fig. 5e)
PMID:32499408	PBO:0098375	even at 25 °C, Arb1-associated Ago1 in the immunoprecipitates from hsp90-G84C cells was much reduced compared to wild-type samples (Figure 4E)
PMID:32499408	PBO:0098588	It is noteworthy that the amount of Arb1 was also drastically decreased in hsp90-G84C cells at high temperatures (Figure 4E)
PMID:32499408	PBO:0094679	(Figure 1B-E, S1B)
PMID:32499408	PBO:0094688	(Figure 1B-E, S1B
PMID:32499408	PBO:0095651	(Figure 1B-E, S1B)
PMID:32499408	PBO:0098590	(Figure 3)
PMID:32499408	PBO:0098592	(Figure 7A)
PMID:32499408	PBO:0094283	(Figure 1B-E, S1B)
PMID:32499408	PBO:0098583	(Figure 1B-E, S1B)
PMID:32499408	PBO:0094283	(Figure 1B-E, S1B)
PMID:32499408	PBO:0093562	(Figure 2E)
PMID:32499408	PBO:0098584	(Figure 3)
PMID:32499408	PBO:0098585	that the amount of Tas3 but not Ago1 was significantly reduced once the hsp90-G84C cells were shifted to restrictive temperature of 37 °C for 4 hours (Figure 4B)
PMID:32499408	PBO:0098586	(Figure 4B)
PMID:32499408	PBO:0098587	We then examined how the altered protein level of Tas3 affects the RITS complex formation in vivo. Notably, the low level of Tas3 in hsp90-G84C cells could only recruit minimal amount of Ago1 detected by co-immunoprecipitation assay at elevated temperatures (Figure 4C). (Figure 4B)
PMID:32499408	PBO:0098582	(Figure 1B-E, S1B)
PMID:32502403	PBO:0106708	Apq12 localized in tubules connected to or in close proximity to the MMD and at spindle pole regions, mirroring ER tubules marked with Yop1-GFP, Rtn1- GFP, or the artificial ER luminal marker mCherry-ADEL
PMID:32502403	PBO:0106712	Apq12 localized in tubules connected to or in close proximity to the MMD and at spindle pole regions, mirroring ER tubules marked with Yop1-GFP, Rtn1- GFP, or the artificial ER luminal marker mCherry-ADEL
PMID:32502403	PBO:0106713	The coalescence of daughter nuclei was also observed in apq12D cells that failed to undergo nuclear division (Figure 4F).
PMID:32502403	PBO:0106713	When these cells were left in this condition, daughter nuclei began to move closer to each other until they finally merged into one single nucleus (Figure 4E). This phenotype can be promoted if spindles are forced to disassemble by treating the cells with 30 mg/mL MBC, resulting in 35% (n = 34) of nuclear coalescence events.
PMID:32502403	PBO:0106711	Consistently, these cells showed a higher frequency of asymmetric NE divisions (Figure S2C)
PMID:32502403	PBO:0106710	ase1D cells that elongated the spindle, the MMD was not properly formed, and the number of NPCs was variable (Figure S2B
PMID:32502403	PBO:0106709	ase1D cells that elongated the spindle, the MMD was not properly formed, and the number of NPCs was variable (Figure S2B
PMID:32502403	PBO:0022963	(Figure 1A)
PMID:32502403	PBO:0106707	A failed mitotic nuclear envelope division is a cell phenotype observed at the end of mitosis during the vegetative life cycle in which the nuclear division does not occur and the two DNA masses remain linked by the internuclear membrane bridge. This can result in the coalescence of both DNA masses into one nucleus. We found that wild-type cells showed timed NE division in the absence of actomyosin ring (Figures 4A and 4B), demonstrating that NE division is independent of cell division. However, 100% of imp1D cells (n = 126) completely failed to undergo NE division, resulting in cells with two nuclei linked by a long NE bridge (Figures 4A and 4B; Video S4). This result demonstrates that Imp1 is required for NE division.
PMID:32502403	PBO:0106705	A failed mitotic nuclear division is a cell phenotype observed at the end of mitosis during the vegetative life cycle in which the nuclear division does not occur and the two DNA masses remain linked by the internuclear membrane bridge. This can result in the coalescence of both DNA masses into one nucleus.
PMID:32502403	PBO:0106704	A failed mitotic nuclear division is a cell phenotype observed at the end of mitosis during the vegetative life cycle in which the nuclear division does not occur and the two DNA masses remain linked by the internuclear membrane bridge. This can result in the coalescence of both DNA masses into one nucleus.
PMID:32502403	PBO:0106701	We found that, in imp1D cells, NPCs were detected at the MMD and the peripheral NPC component Nup60 was removed from this domain (Figure 4C); however, the removal of structural components such as Nup107 and the membrane nucleoporin Cut11 was not observed (Figures 4C, S3A, and S3B).
PMID:32502403	GO:0140515	(comment: CHECK causally upstreasm of?)
PMID:32518066	GO:0035613	Lsm1Δ56C-7 can only bind tightly to the RNA with a 5′ stem-loop and single stranded 3′ end (Kd = 70 and 32 nM, respectively) (Fig. 5C).
PMID:32518066	GO:0008266	These data indicate that high affinity binding sites for the Lsm1-7 complex must be at the 3′ termini of RNA.
PMID:32518066	GO:0035925	We conclude that the carboxy-terminal 12 amino acids of Lsm1 are important for the binding specificity of Lsm1-7.
PMID:32546512	FYPO:0002061	(Figure S1)
PMID:32546512	FYPO:0001357	(Figure 8)
PMID:32546512	FYPO:0001357	(Figure 8)
PMID:32546512	FYPO:0001357	(Figure 8)
PMID:32546512	FYPO:0001357	(Figure 8)
PMID:32546512	FYPO:0006821	(Figure 8)
PMID:32546512	FYPO:0002085	(Figure S1)
PMID:32546512	FYPO:0000080	(Figure S1)
PMID:32546512	FYPO:0000080	(Figure S1)
PMID:32546512	FYPO:0000080	(Figure S1)
PMID:32546512	FYPO:0000080	(Figure S1)
PMID:32546512	FYPO:0000080	(Figure S1)
PMID:32546512	FYPO:0000080	(Figure S1)
PMID:32546512	FYPO:0000080	(Figure S1)
PMID:32546512	FYPO:0000080	(Figure S1)
PMID:32546512	FYPO:0000082	(Figure S1)
PMID:32546512	FYPO:0004481	(Figure S1)
PMID:32546512	FYPO:0000082	(Figure S1)
PMID:32546512	GO:0043628	a scenario in which Erh1 acts as a brake on Mmi1’s ability to promote CPF-dependent termination during prt lncRNA synthesis.
PMID:32546512	GO:0043628	suggest ... Erh1 acts as a brake on Mmi1’s ability to promote CPF-dependent termination during prt lncRNA synthesis.
PMID:32546512	PBO:0094771	In addition, using the prt-pho1 reporter plasmid to gauge Pho1 acid phosphatase expression, we found that Pho1 activity was lower in mmi1Δ cells than in wild-type cells (Fig. 6C)
PMID:32546512	PBO:0106695	(Figure 4B)
PMID:32546512	PBO:0106695	(Figure 4B)
PMID:32546512	FYPO:0001045	(Figure 4B)
PMID:32546512	FYPO:0001045	(Figure 4B)
PMID:32546512	FYPO:0001045	(Figure 4B)
PMID:32546512	FYPO:0001234	(Figure S1)
PMID:32546512	FYPO:0001234	(Figure S1)
PMID:32546512	FYPO:0002061	(Figure S1)
PMID:32546512	PBO:0106693	(Figure 2C)
PMID:32546512	PBO:0094738	(Figure 2B)
PMID:32546512	PBO:0094738	(Figure 2C)
PMID:32546512	PBO:0094738	(Figure 5)
PMID:32546512	PBO:0094771	(Figure 2B)
PMID:32546512	PBO:0094771	(Figure 4)
PMID:32546512	PBO:0094771	(Figure 4)
PMID:32546512	FYPO:0001045	(Figure 4B)
PMID:32546512	PBO:0094777	(comment: (Normal compared to WT)) The instructive findings were that the de-repression of Pho1 by erh1Δ was effaced in rhn1Δ, ssu72-C13S, ctf1Δ, ppn1Δ, and swd22Δ cells and was attenuated in dis2Δ cells (Fig. 4B
PMID:32546512	PBO:0094777	(comment: (Normal compared to WT)) The instructive findings were that the de-repression of Pho1 by erh1Δ was effaced in rhn1Δ, ssu72-C13S, ctf1Δ, ppn1Δ, and swd22Δ cells and was attenuated in dis2Δ cells (Fig. 4B
PMID:32546512	FYPO:0003267	(Figure 4)
PMID:32546512	FYPO:0003267	(Figure 4)
PMID:32546512	FYPO:0001234	(Figure 2) We obtained viable erh1Figure 2A Δ asp1-D333A haploids after mating and sporulation; the doublemutant was slow-growing on YES agar and cold-sensitive: he de-repression of Pho1 activity by erh1Δ was erased in the asp1-D333A background
PMID:32546512	FYPO:0001234	(Figure 2) We obtained viable erh1Figure 2A Δ asp1-D333A haploids after mating and sporulation; the doublemutant was slow-growing on YES agar and cold-sensitive: he de-repression of Pho1 activity by erh1Δ was erased in the asp1-D333A background
PMID:32546512	FYPO:0000082	(Figure 4)
PMID:32546512	FYPO:0000080	(Figure 4)
PMID:32546512	FYPO:0000080	(Figure 4)
PMID:32546512	FYPO:0000080	(Figure 4)
PMID:32546512	FYPO:0000080	(Figure 4)
PMID:32546512	PBO:0094771	(Figure 4)
PMID:32546512	PBO:0094771	(Figure 4)
PMID:32546512	PBO:0094771	(Figure 4)
PMID:32546512	FYPO:0005369	(Figure 2A)
PMID:32546512	PBO:0094775	Northern blotting, Figure 6
PMID:32546512	PBO:0106694	Northern blotting and primer extension, Figure 6
PMID:32546512	FYPO:0000080	(Figure 5)
PMID:32546512	FYPO:0000080	(Figure 5)
PMID:32546512	PBO:0094771	(Figure 5)
PMID:32546512	PBO:0094771	(Figure 5)
PMID:32546512	PBO:0094771	(Figure 5)
PMID:32546512	FYPO:0000080	(Figure 5)
PMID:32546512	FYPO:0000080	(Figure 5)
PMID:32546512	PBO:0099750	(Figure 5)
PMID:32546512	PBO:0099750	(Figure 5)
PMID:32546512	PBO:0099750	(Figure 5)
PMID:32546512	PBO:0099750	(Figure 2C) the fivefold de-repression of Pho1 in the aps1Δ strain was enhanced additively to 12- fold in the erh1Δ aps1Δ background
PMID:32546512	PBO:0099750	(Figure 2C) the fivefold de-repression of Pho1 in the aps1Δ strain was enhanced additively to 12- fold in the erh1Δ aps1Δ background
PMID:32546512	FYPO:0000080	(Figure 2)
PMID:32546512	FYPO:0000080	(Figure 2)
PMID:32546512	FYPO:0000080	(Figure 2A)
PMID:32546512	FYPO:0000080	(Figure 2A)
PMID:32546512	PBO:0094771	(Figure 4)
PMID:32546512	PBO:0094777	(Figure 2) (comment: vw changed from decreased to normal (compared to WT))
PMID:32546512	PBO:0094777	(Figure 2) (comment: vw changed from decreased to normal (compared to WT))
PMID:32546830	FYPO:0002150	(Figure 2E) (comment: tetrad analysis)
PMID:32546830	GO:0005515	(comment: linker)
PMID:32546830	PBO:0099069	(Figure 2)
PMID:32571823	PBO:0093653	(Figure 1)
PMID:32571823	PBO:0093642	(Figure 2d)
PMID:32571823	PBO:0096345	(Figure 3A) (comment: increased cacineurin signalling)
PMID:32571823	FYPO:0001198	(Figure 3B)
PMID:32571823	FYPO:0000098	(Figure 3C)
PMID:32571823	PBO:0096346	(Figure 3D)
PMID:32571823	FYPO:0005253	(Fig 4) (comment: Ccr1 is a molecular target of TAM.)
PMID:32571823	FYPO:0002060	(Figure 1)
PMID:32571823	PBO:0096347	(Figure 2b)
PMID:32571823	PBO:0096347	(Figure 2b)
PMID:32571823	FYPO:0002716	(Fig. 5)
PMID:32571823	PBO:0093653	(Figure 1)
PMID:32571823	PBO:0096339	(Figure 2)
PMID:32571823	PBO:0096340	(Figure 2)
PMID:32571823	PBO:0093660	(Figure 2)
PMID:32571823	PBO:0093646	(Figure 2)
PMID:32571823	PBO:0096341	(Figure 2)
PMID:32571823	PBO:0093644	(Figure 2)
PMID:32571823	PBO:0094271	(Figure 2)
PMID:32571823	PBO:0093785	(Figure 2)
PMID:32571823	PBO:0096342	(Figure 2)
PMID:32571823	PBO:0096343	(Figure 2)
PMID:32571823	PBO:0093642	(Figure 2)
PMID:32571823	PBO:0096344	(Figure 2)
PMID:32571823	PBO:0093645	(Figure 2)
PMID:32571823	PBO:0094270	(Figure 2)
PMID:32571823	PBO:0093785	(Figure 2)
PMID:32571823	FYPO:0002792	(Figure 2c)
PMID:32571823	FYPO:0002643	(Figure 2d)
PMID:32571823	PBO:0093653	(Figure 2d)
PMID:32571823	FYPO:0005254	(Figure 2d)
PMID:32571823	PBO:0094271	(Figure 2d)
PMID:32571823	FYPO:0002343	(Figure 2d)
PMID:32571823	FYPO:0002328	(Figure 2d)
PMID:32571823	FYPO:0001470	(Figure 2d)
PMID:32571823	FYPO:0000086	(Figure 2d)
PMID:32571823	PBO:0093646	(Figure 2d)
PMID:32594847	FYPO:0001125	DNS
PMID:32594847	FYPO:0000047	DNS
PMID:32594847	FYPO:0001124	DNS
PMID:32650974	GO:0005515	(comment: split YFP and affinity capture)
PMID:32650974	GO:0018279	(Figure 1,2,4) These results suggested that the elongation of mannan takes place sequentially by the actions of the a-mannosyltransferases in the order of SpOch1p, SpMnn9p and SpAnp1p.
PMID:32650974	GO:0140497	(comment: CHECK M-Pol I complex)
PMID:32650974	FYPO:0007436	comment: CHECK swolle)
PMID:32650974	GO:0018279	(Figure 1,2,4) These results suggested that the elongation of mannan takes place sequentially by the actions of the a-mannosyltransferases in the order of SpOch1p, SpMnn9p and SpAnp1p.
PMID:32650974	GO:0140497	comment: CHECK M-Pol I complex)
PMID:32650974	GO:0018279	(Figure 4) These results suggested that the elongation of mannan takes place sequentially by the actions of the a-mannosyltransferases in the order of SpOch1p, SpMnn9p and SpAnp1p.
PMID:32692737	GO:2000779	(comment: regulates pathway choice)
PMID:32723864	PBO:0107261	(Fig. 3F) The results show that the absence of Klp2 affects the localization of Ase1-GFP to the meiotic spindles and leads to a decrease of the Ase1-GFP intensity on the meiotic spindles.
PMID:32723864	FYPO:0001513	(Figure 7)
PMID:32723864	PBO:0107269	(Figure 7)
PMID:32723864	FYPO:0007756	(Figure 7)
PMID:32723864	FYPO:0007756	(Figure 7)
PMID:32723864	FYPO:0007756	(Figure 7)
PMID:32723864	GO:0061804	Ase1 is required for promoting spindle elongation during mitotic prophase but synergizes with Klp2 to maintain spindle stability during metaphase I.
PMID:32723864	GO:0140642	Ase1 is required for promoting spindle elongation during mitotic prophase but synergizes with Klp2 to maintain spindle stability during metaphase I.
PMID:32723864	PBO:0107268	(Figure 6)
PMID:32723864	PBO:0107267	(Figure 6)
PMID:32723864	PBO:0107266	(Figure 6)
PMID:32723864	GO:0140642	Ase1 is required for promoting spindle elongation during mitotic prophase but synergizes with Klp2 to maintain spindle stability during metaphase I.
PMID:32723864	PBO:0107265	(Figure 5)
PMID:32723864	FYPO:0007752	(Figure 5) Three typical types of plots are shown: (I) WTlike metaphase spindle length (maintenance), (II) spindle regression (regression), and (III) continuous spindle elongation (lacking metaphase).
PMID:32723864	PBO:0107264	(Figure 5)
PMID:32723864	PBO:0107263	(Figure 5)
PMID:32723864	FYPO:0007744	(Figure S1) In contrast, 50% of the spindles in klp2D cells underwent abrupt collapse during metaphase I (Fig. 2, A, C, and E, 3A)
PMID:32723864	FYPO:0007748	In both mitotic and meiotic cells, the absence of Klp2 slightly but significantly prolonged the duration of preanaphase (Fig. 2, F and G).
PMID:32723864	FYPO:0007747	absence of Klp2 did not significantly affect spindle elongation during prophase I and only slightly lengthened the maximal spindle length during metaphase I (Fig. 2G).
PMID:32723864	FYPO:0007746	(Figure S1)
PMID:32723864	FYPO:0007746	(Figure S1)
PMID:32723864	PBO:0099173	(Figure S1)
PMID:32723864	FYPO:0007751	(Figure S1) In contrast, 50% of the spindles in klp2D cells underwent abrupt collapse during metaphase I (Fig. 2, A, C, and E, 3A)
PMID:32735772	PBO:0093561	(Fig. S1B)
PMID:32735772	FYPO:0006294	(Figure S1E) nitrogen starvation-induced ER-phagy appeared to be normal in epr1D
PMID:32735772	FYPO:0005264	(Fig. 6b)
PMID:32735772	FYPO:0000843	(Figure 6A)
PMID:32735772	FYPO:0005264	(Fig. 6b)
PMID:32735772	FYPO:0007446	(Figure 2B, 2G, 2H)
PMID:32735772	FYPO:0007446	(Fig. 3)
PMID:32735772	FYPO:0007447	(Figure S6B), indicating that Ire1 is dispensable for DTT-induced bulk autophagy but is essential for DTT-induced ER-phagy.
PMID:32735772	FYPO:0007446	(Figure 5A) reduced in scs2D and abolished in scs2D scs22D
PMID:32735772	GO:0005515	(Figure 3C) Epr1 interacted with both Scs2 and Scs22 in the Y2H assay
PMID:32735772	FYPO:0007447	(Figure 5A) reduced in scs2D and abolished in scs2D scs22D
PMID:32735772	PBO:0104093	(Figure 1C) AIM-mutated Epr1- C was pulled down as efficiently as wild-type Epr1-C by Scs2 but did not support the pull-down of Atg8 PLUS more experiments We hypothesized that the main role of Epr1 in ER-phagy is to mediate a connection between Atg8 and VAPs. requirement of Epr1 in ER-phagy can be by-passed by an artificial soluble tether that bridges an Atg8-VAP connection.Figure 4D).
PMID:32735772	FYPO:0007444	Mutating the FFAT motif or the AIM abolished the ability of Epr1-C to rescue epr1D (Figures 4A, 4B, and S3D).
PMID:32735772	GO:0005515	(Figures 1B and S1C)
PMID:32735772	PBO:0104087	(Figures 2G and 2H)
PMID:32735772	GO:0005783	(Figure 2a)
PMID:32735772	GO:0005515	(Figures 1B and S1C)
PMID:32735772	PBO:0104088	(Figure 3C) The 42-amino-acid Epr1-C region (residues 339-380), which is capable of Atg8 binding and contains the predicted FFAT motif, is sufficient for interacting with VAPs
PMID:32735772	PBO:0104089	(Figure 3C) The 42-amino-acid Epr1-C region (residues 339-380), which is capable of Atg8 binding and contains the predicted FFAT motif, is sufficient for interacting with VAPs
PMID:32735772	FYPO:0007444	Mutating the FFAT motif or the AIM abolished the ability of Epr1-C to rescue epr1D (Figures 4A, 4B, and S3D).
PMID:32735772	PBO:0104098	(Figure 7E) the ER-phagy defect of ire1D was largely rescued (Figure 7E).
PMID:32735772	PBO:0104091	(Figure 3D) (comment: CHECK ******check with DAN, is this an overexpression allele?)
PMID:32735772	FYPO:0000843	(Figure 6A)
PMID:32735772	FYPO:0007444	Remarkably, Epr1-C, but not Epr1-N, could completely rescue the defects of epr1D in DTT-induced ER- phagy
PMID:32735772	FYPO:0006378	(Figures S3B and S3D) Epr1-C showed ER localization in vegetatively growing cells, whereas Epr1-N was diffusely distributed in the cytoplasm and the nucleus
PMID:32735772	FYPO:0007449	(Figures S3B and S3D) Epr1-C showed ER localization in vegetatively growing cells, whereas Epr1-N was diffusely distributed in the cytoplasm and the nucleus
PMID:32735772	FYPO:0007449	(Figure 3D)
PMID:32735772	PBO:0104091	(Figure 3D) As expected, in cells lacking both Scs2 and Scs22, Epr1 became diffusely distributed in the cytoplasm
PMID:32735772	PBO:0104094	(Figure 3C) The 42-amino-acid Epr1-C region (residues 339-380), which is capable of Atg8 binding and contains the predicted FFAT motif, is sufficient for interacting with VAPs
PMID:32735772	PBO:0104093	(Figure 3C) The 42-amino-acid Epr1-C region (residues 339-380), which is capable of Atg8 binding and contains the predicted FFAT motif, is sufficient for interacting with VAPs
PMID:32735772	FYPO:0000843	(Figure 6A)
PMID:32735772	FYPO:0000843	(Figure 6A)
PMID:32735772	GO:0044804	(comment: CHECK check with Dan ****) Thus, Epr1 is an ER-phagy receptor required for ER stress-induced selective autophagy of both the nuclear envelope and the peripheral ER.
PMID:32735772	FYPO:0000843	(Figure 6A)
PMID:32735772	GO:0000407	(Figure 2a)
PMID:32735772	PBO:0104090	(Figure 1C)
PMID:32735772	PBO:0104090	(Figure 1C)
PMID:32735772	FYPO:0000843	(Figure 6A)
PMID:32735772	FYPO:0000843	(Figure 6A)
PMID:32735772	PBO:0104092	(Figure 1C)
PMID:32735772	PBO:0093561	(Fig. S1B)
PMID:32735772	FYPO:0001357	(Fig. S1B)
PMID:32735772	PBO:0104086	(Figure 7B) We found that DTT-induced increase of Epr1 was severely diminished in ire1D (Figure 7B), indicating that Epr1 upregulation requires Ire1.
PMID:32735772	FYPO:0006294	(Figure S1E)
PMID:32790622	PBO:0099295	viable spore yield assay; 16% of the surviving spores had inherited two copies of chromosome 3 and were thus aneuploid/diploid.
PMID:32790622	PBO:0099296	viable spore yield assay; 30% of the surviving spores had inherited the two centromere 3-linked markers suggesting they are aneuploid/diploid.
PMID:32790622	PBO:0099297	viable spore yield assay; 20% of the surviving spores had inherited the two centromere 3-linked markers suggesting they are aneuploid/diploid.
PMID:32790622	PBO:0099298	viable spore yield assay
PMID:32790622	FYPO:0002052	viable spore yield assay
PMID:32790622	PBO:0099293	viable spore yield assay
PMID:32790622	PBO:0099294	viable spore yield assay
PMID:32817556	PBO:0097418	(comment: Phenotype is greatly enhanced by mutation of the IR-R boundary element)
PMID:32841241	PBO:0102887	(comment: CHECK CCU codon/AGG anticodon tRNA)
PMID:32841241	PBO:0102886	(comment: CHECK ACU codon/AGU anticodon tRNA)
PMID:32841241	PBO:0102885	(comment: CHECK UAC codon/GUA anticodon tRNA)
PMID:32841241	PBO:0102884	(comment: CHECK CCU codon/AGG anticodon tRNA)
PMID:32841241	PBO:0102889	(comment: CHECK CCU codon/AGG anticodon tRNA)
PMID:32841241	PBO:0102890	(comment: CHECK UAC codon/GUA anticodon tRNA)
PMID:32841241	PBO:0102890	(comment: CHECK UAC codon/GUA anticodon tRNA)
PMID:32841241	PBO:0102889	(comment: CHECK CCU codon/AGG anticodon tRNA)
PMID:32841241	PBO:0102890	(comment: CHECK UAC codon/GUA anticodon tRNA)
PMID:32841241	PBO:0102889	(comment: CHECK CCU codon/AGG anticodon tRNA)
PMID:32841241	PBO:0102888	(comment: CHECK UAC codon/GUA anticodon tRNA)
PMID:32841241	PBO:0102887	(comment: CHECK CCU codon/AGG anticodon tRNA)
PMID:32841241	PBO:0102888	(comment: CHECK UAC codon/GUA anticodon tRNA)
PMID:32848252	PBO:0099373	(Fig. 4,6)
PMID:32848252	GO:0140510	(Fig. 3a) Extended Data Fig. 4a-c Removed from nuclear basket in bridge midzone during nuclear division
PMID:32848252	GO:0140510	(Fig. 3a) Extended Data Fig. 4a-c Removed from nuclear basket in bridge midzone during nuclear division
PMID:32848252	PBO:0099372	(Fig. 3a) Extended Data Fig. 4a-c Removed from nuclear basket in bridge midzone during nuclear division
PMID:32848252	GO:0140512	(Fig. 3b)
PMID:32848252	PBO:0099376	(comment: causally upstream?)
PMID:32848252	GO:0007084	Instead, the repair process was associated with recruitment of the ESCRTIII protein Cmp7 (Fig. 4d) to sites of local NEB20 (Fig. 4d, Extended Data Fig. 8b, c).
PMID:32848252	GO:0007084	lem2 (which encodes Lem2, the binding partner of Cmp7) is also SL with les1
PMID:32848252	PBO:0099372	(Fig. 3a) Extended Data Fig. 4a-c Removed from nuclear basket in bridge midzone during nuclear division
PMID:32848252	PBO:0099371	extended data 6 c,d
PMID:32848252	PBO:0099370	(Fig. 4a, b) Daughter nuclei in the les1Δ strain also suffered transient leakages at the time of maximum spindle elongation, as measured by loss of nuclear NLS-GFP
PMID:32848252	PBO:0099364	Extended Data fig4
PMID:32848252	GO:0005637	Extended Data Figure 2 (comment: nucleoplasmic side)
PMID:32848252	PBO:0099362	(Fig. 4) Extended Data Fig. 7
PMID:32848252	PBO:0099369	Les1 stalks functionally isolate daughter nuclei from the process of Imp1-dependent local NEB at the centre of the bridge probably acts to create a seal by gathering the inner nuclear envelope tightly around the spindle
PMID:32848252	PBO:0099368	(Fig. 3g)
PMID:32848252	PBO:0099366	Extended Data Figure 8
PMID:32848252	PBO:0099365	(Fig. 4, 6)
PMID:32878942	PBO:0099944	(Fig. S3F,G)
PMID:32878942	FYPO:0000674	(Fig. S3E)
PMID:32878942	FYPO:0000674	(Fig. S3E)
PMID:32878942	PBO:0099937	(Figure 2D,E)
PMID:32878942	FYPO:0000674	(Fig. S3E)
PMID:32878942	PBO:0099943	(Fig. 4H,I and S3F,G)
PMID:32878942	PBO:0099943	(Fig. 4H,I and S3F,G)
PMID:32878942	PBO:0099945	(Fig. 4)
PMID:32878942	PBO:0099946	(Fig. S3A)
PMID:32878942	PBO:0099946	(Fig. S3A)
PMID:32878942	PBO:0099947	(Fig. S3A)
PMID:32878942	PBO:0099947	(Fig. S3A)
PMID:32878942	GO:2000099	(Fig. 3D)
PMID:32878942	GO:2000099	(Fig. 3D)
PMID:32878942	GO:0061245	(Fig. 3D)
PMID:32878942	FYPO:0001396	(Figure 2F-H)
PMID:32878942	PBO:0099938	(Figure 2I)
PMID:32878942	FYPO:0003532	(Fig. S3B,C)
PMID:32878942	FYPO:0003532	(Fig. S3B,C)
PMID:32878942	PBO:0099943	(Fig. S3F)
PMID:32878942	FYPO:0003532	(Fig. S3B,C,D)
PMID:32878942	PBO:0099942	(Fig. 4D,E,F)
PMID:32878942	FYPO:0000674	(Fig. S3E)
PMID:32896087	PBO:0100496	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0100496	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0100493	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100493	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100492	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100496	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0100496	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0100496	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0100496	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0100492	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100492	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100492	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100493	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100492	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100492	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100492	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100493	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100494	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100494	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100496	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0100496	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0092433	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0100496	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0100496	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0100493	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100492	(comment: solid media screen using prototroph deletion library.)
PMID:32896087	PBO:0100494	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	GO:0005739	(comment: arg3-GFP fusion localisation in minimal media (EMM))
PMID:32896087	PBO:0100492	(comment: Liquid media growth assay. Mutant isolated from deletion collection.)
PMID:32896087	PBO:0100493	(comment: Liquid media growth assay. Mutant isolated from deletion collection.)
PMID:32896087	PBO:0100493	(comment: Liquid media growth assay. Mutant isolated from deletion collection.)
PMID:32896087	PBO:0100493	(comment: Liquid media growth assay. Mutant isolated from deletion collection.)
PMID:32896087	PBO:0100496	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0100496	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0100496	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0092433	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0100492	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100494	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100493	(comment: Liquid media growth assay. Mutant isolated from deletion collection.)
PMID:32896087	PBO:0100495	(comment: Data from screening of prototroph deletion library)
PMID:32896087	PBO:0100494	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	GO:0042450	genes detected in screen Figure EV2
PMID:32896087	GO:0042450	genes detected in screen Figure EV2
PMID:32896087	GO:0042450	genes detected in screen Figure EV2
PMID:32896087	GO:0042450	genes detected in screen Figure EV2
PMID:32896087	GO:0042450	genes detected in screen Figure EV2
PMID:32896087	GO:0042450	genes detected in screen Figure EV2
PMID:32896087	PBO:0100493	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100493	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100492	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100496	(comment: CHECK EMM media with arginine)
PMID:32896087	GO:0042450	genes detected in screen Figure EV2
PMID:32896087	GO:0042450	genes detected in screen Figure EV2
PMID:32896087	GO:0042450	genes detected in screen Figure EV2
PMID:32896087	PBO:0092433	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0100496	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0100496	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0100496	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0100496	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0092433	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0100494	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100494	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100494	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100494	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100493	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100492	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100493	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100492	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0092433	(comment: CHECK EMM media with arginine)
PMID:32896087	PBO:0100492	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	PBO:0100496	(comment: CHECK EMM media with arginine)
PMID:32908306	GO:0005739	(comment: Cup1-GFP immunofluorescence)
PMID:32909946	FYPO:0006295	(Fig. 1a)
PMID:32909946	FYPO:0006295	(Fig. 1a)
PMID:32909946	PBO:0096897	in vitro autophosphorylation activity of Atg1 from atg11D mutant was almost undetectable (Figure 1D
PMID:32909946	PBO:0096897	(Figure 1C) Such a band was not observed for D193A and T208A mutants, confirming that they are indeed kinase dead
PMID:32909946	PBO:0096898	we found that in S. pombe, Atg1 from atg13D, atg17D, or atg101D mutant exhibited autophosphorylation activities similar to that of Atg1 from wild type
PMID:32915139	PBO:0102266	(Figure 5B)
PMID:32915139	FYPO:0001368	(Figure 2—Figure supplement 5). ngs formed and constricted correctly in >85% of sty1D cells (Figure 2D).
PMID:32915139	FYPO:0004513	(comment: CHECK Overexpression under the control of B-estradiol promoter (vw: I added an allele synonym, later these will be searchable and visible))
PMID:32915139	PBO:0102263	(Fig. 3b)
PMID:32915139	PBO:0093569	(Fig. 3a)
PMID:32915139	FYPO:0001365	explicit delay in ring constriction and disassembly (21 ± 0.6 min in wild-type cells vs 36 ± 1.6 min in for3D cells; Figure 2—Figure supplement 5
PMID:32915139	PBO:0102262	(comment: CHECK 25%)
PMID:32915139	PBO:0102260	(Fig. 5b)
PMID:32915139	PBO:0102260	(Fig. 5b)
PMID:32915139	PBO:0102270	(Figure 1C)
PMID:32915139	PBO:0093570	(Fig. 1 SF)
PMID:32915139	PBO:0093570	(Fig. 1 SF)
PMID:32915139	PBO:0102259	(Fig. 2)
PMID:32915139	FYPO:0004513	upstream elements of this signaling cascade shared this phenotype... Mcs4, the redundant MAPKKK´s Wak1 and Win1, and MAPKK Wis1 (Figure 1A, Figure 1—Figure supplement 1
PMID:32915139	PBO:0093569	(Fig. 1)
PMID:32915139	PBO:0093569	(Fig. 1 S5)
PMID:32915139	PBO:0102254	cells lacking Sty1 grew in these low LatA concentrations (Figure 1B).
PMID:32915139	FYPO:0004513	(Fig. 1F)
PMID:32915139	PBO:0093569	(Fig. 3a)
PMID:32915139	PBO:0102271	(Fig. 4d)
PMID:32915139	PBO:0102263	(Fig. 3c)
PMID:32915139	PBO:0102277	(comment: CHECK replaces wt annotation)
PMID:32915139	PBO:0102277	(comment: CHECK replaces wt annotation)
PMID:32915139	PBO:0102270	(Figure 1C)
PMID:32915139	PBO:0102270	(Figure 1C)
PMID:32915139	PBO:0102275	(Figure 5; Figure supplement 4)
PMID:32915139	PBO:0102274	(Figure 5; Figure supplement 4)
PMID:32915139	PBO:0102273	We found that total For3 levels also decline in S. pombe wild-type cells in response to stimuli that activate Sty1, like heat shock (40 ̊C), osmotic saline (0.6 M KCl), and oxidative stress (1 mM H2O2) (Pe ́rez and Cansado, 2010) in a MAPK-dependent manner (Figure 5—Figure supplement 3).
PMID:32915139	PBO:0092160	We found that total For3 levels also decline in S. pombe wild-type cells in response to stimuli that activate Sty1, like heat shock (40 ̊C), osmotic saline (0.6 M KCl), and oxidative stress (1 mM H2O2) (Pe ́rez and Cansado, 2010) in a MAPK-dependent manner (Figure 5—Figure supplement 3).
PMID:32915139	PBO:0102272	We found that total For3 levels also decline in S. pombe wild-type cells in response to stimuli that activate Sty1, like heat shock (40 ̊C), osmotic saline (0.6 M KCl), and oxidative stress (1 mM H2O2) (Pe ́rez and Cansado, 2010) in a MAPK-dependent manner (Figure 5—Figure supplement 3).
PMID:32915139	PBO:0102269	upstream elements of this signaling cascade shared this phenotype... Mcs4, the redundant MAPKKK´s Wak1 and Win1, and MAPKK Wis1 (Figure 1A, Figure 1—Figure supplement 1
PMID:32915139	PBO:0102268	Cells expressing a mutant allele Mcs4(D512N) that does not activate the SAPK pathway upon stimulation with hydro- gen peroxide (Shieh et al., 1997), displayed Sty1 activation during LatA treatment
PMID:32915139	PBO:0102266	(Fig. 5c)
PMID:32915139	PBO:0102262	(comment: CHECK 50%)
PMID:32915139	FYPO:0007151	(Figure 2A, C) (comment: CHECK check, has synonym increased stability (better than increased length?))
PMID:33010152	PBO:0094738	(Fig. 8)
PMID:33010152	PBO:0094738	(Fig. 6)
PMID:33010152	PBO:0094738	(Fig. 6)
PMID:33010152	PBO:0094738	(Fig. 6)
PMID:33010152	PBO:0094738	(Fig. 6)
PMID:33010152	PBO:0094738	(Fig. 6)
PMID:33010152	PBO:0094738	(Fig. 6)
PMID:33010152	PBO:0094738	(Fig. 6)
PMID:33010152	PBO:0094738	(Fig. 6)
PMID:33010152	PBO:0094738	(Fig. 6)
PMID:33010152	PBO:0094738	(Fig. 6)
PMID:33010152	PBO:0094738	(Fig. 6)
PMID:33010152	PBO:0094738	(Fig. 6)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0000080	(Fig. 5)
PMID:33010152	FYPO:0000080	(Fig. 5)
PMID:33010152	FYPO:0000080	(Fig. 5)
PMID:33010152	FYPO:0000080	(Fig. 5)
PMID:33010152	FYPO:0000080	(Fig. 5)
PMID:33010152	FYPO:0000080	(Fig. 5)
PMID:33010152	FYPO:0000082	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0001357	(Fig. 5)
PMID:33010152	FYPO:0000080	(Fig. 5)
PMID:33010152	FYPO:0000080	(Fig. 5)
PMID:33010152	FYPO:0000080	(Fig. 8)
PMID:33010152	FYPO:0000080	(Fig. 8)
PMID:33010152	FYPO:0001355	(Fig. 4)
PMID:33010152	FYPO:0001355	(Fig. 4)
PMID:33010152	FYPO:0001355	(Fig. 4)
PMID:33010152	FYPO:0000080	(Fig. 4)
PMID:33010152	FYPO:0000082	(Fig. 4)
PMID:33010152	FYPO:0000080	(Fig. 4)
PMID:33010152	FYPO:0000080	(Fig. 4)
PMID:33010152	FYPO:0000082	(Fig. 4)
PMID:33010152	FYPO:0000080	(Fig. 4)
PMID:33010152	FYPO:0000082	(Fig. 4)
PMID:33010152	FYPO:0002061	(Fig. 3)
PMID:33010152	PBO:0094738	(Fig. 8)
PMID:33010152	PBO:0094738	(Fig. 8)
PMID:33010152	PBO:0094738	(Fig. 8)
PMID:33010152	PBO:0094738	(Fig. 8)
PMID:33010152	PBO:0094738	(Fig. 4)
PMID:33010152	PBO:0094738	(Fig. 4)
PMID:33010152	PBO:0094738	(Fig. 4)
PMID:33010152	PBO:0094738	(Fig. 4)
PMID:33010152	PBO:0094738	(Fig. 4)
PMID:33010152	PBO:0094738	(Fig. 4)
PMID:33010152	PBO:0094738	(Fig. 8)
PMID:33010152	PBO:0094738	(Fig. 8)
PMID:33010152	PBO:0094738	(Fig. 8)
PMID:33010152	PBO:0094738	(Fig. 1, Fig. 8)
PMID:33010152	PBO:0094738	(Fig. 1)
PMID:33010152	PBO:0094738	(Fig. 1)
PMID:33010152	PBO:0094738	(Fig. 1)
PMID:33010152	PBO:0094738	(Fig. 1)
PMID:33010152	PBO:0094738	(Fig. 1)
PMID:33010152	PBO:0094738	(Fig. 1)
PMID:33010152	PBO:0094738	(Fig. 1)
PMID:33010152	PBO:0094738	(Fig. 4)
PMID:33010152	PBO:0094738	(Fig. 1)
PMID:33049028	PBO:0119719	Further analysis revealed that the levels of intron-retaining cox1 and cob1 transcripts were increased in Δppr10 cells in the intron-containing background (Fig. 1A-C)
PMID:33049028	PBO:0100740	The results showed that in the intronless background, the cox1 and cob1 mRNAs were detected at similar levels in WT[Δi] and Δppr10[Δi] cells (Fig. 1E-G
PMID:33049028	PBO:0100738	The results showed that in the intronless background, the cox1 and cob1 mRNAs were detected at similar levels in WT[Δi] and Δppr10[Δi] cells (Fig. 1E-G
PMID:33049028	PBO:0119720	Further analysis revealed that the levels of intron-retaining cox1 and cob1 transcripts were increased in Δppr10 cells in the intron-containing background (Fig. 1A-C)
PMID:33049028	FYPO:0001934	(Fig. 4)
PMID:33108274	PBO:0107741	The wtf4poison proteins is distributed throughout asci and spores in the absence of the wtf4antidote. The antidote assembles with the poison and then both proteins are localized to the vacuole in spores.
PMID:33108274	PBO:0107741	The wtf4poison proteins is distributed throughout asci and spores in the absence of the wtf4antidote. The antidote assembles with the poison and then both proteins are localized to the vacuole in spores.
PMID:33109728	FYPO:0001357	(Fig. 4B)
PMID:33109728	FYPO:0001357	(Fig. 4B)
PMID:33109728	FYPO:0002061	(Fig. 4B)
PMID:33109728	FYPO:0001355	(Fig. 4B)
PMID:33109728	FYPO:0001357	(Fig. 4B)
PMID:33109728	FYPO:0002061	(Fig. 4B)
PMID:33109728	FYPO:0002061	(Fig. 4B)
PMID:33109728	FYPO:0001357	(Fig. 4B)
PMID:33109728	FYPO:0001355	(Fig. 4B)
PMID:33109728	FYPO:0001355	(Fig. 4B)
PMID:33125111	FYPO:0007208	(Fig. 1C).
PMID:33125111	FYPO:0000141	(Fig. 3).
PMID:33125111	FYPO:0001234	(Fig. 1B). (comment: decreasing slows after 6 hours)
PMID:33125111	FYPO:0002401	(Fig. 1C).
PMID:33125111	FYPO:0000177	(Fig. 3).
PMID:33125111	FYPO:0000056	(Fig. 1A).
PMID:33131769	FYPO:0001904	An fragile actomyosin contractile ring is an abnormal actomyosin contractile ring that disassemble by treatment with a low dose of Latrunculin A, an actin depolymerizing agent.
PMID:33131769	FYPO:0001904	An fragile actomyosin contractile ring is an abnormal actomyosin contractile ring that disassemble by treatment with a low dose of Latrunculin A, an actin depolymerizing agent.
PMID:33131769	PBO:0099617	(comment: CHECK *****(abnormal distribution in...)) inhomogeneous contractile Rng2 ring An inhomogeneous contractile Rng2 ring is an abnormal actomyosin contractile ring that show an uneven distribution of 2mYFP-Rng2-12A over the ring.
PMID:33137119	FYPO:0000674	(comment: CHECK pREP81-gad8-T260C) fig 1a
PMID:33137119	PBO:0105948	(comment: affecting substrate Fkh2 in vitro)
PMID:33137119	PBO:0105956	(Fig. 3A) Gad8-K263C was also phosphorylated at S546 under conditions that compromise Tor1 activity, such as osmotic or low glucose stress (S3A Fig), further supporting Tor1-independent phosphorylation of Gad8-K263C by an as yet unknown kinase.
PMID:33137119	PBO:0105954	(Fig. 3A) To our surprise, Gad8-K263C was phosphorylated at S546 in wild type cells, as well as in Δtor1 cells (S546-P, Fig 3A).This finding suggests that the Gad8-K263C mutant is phosphorylated by a kinase that normally does not recognize Gad8 as a substrate.
PMID:33137119	PBO:0105949	(Fig. 3A) affecting substrate Fkh2 in vitro
PMID:33137119	PBO:0105954	(Fig. 3C) we found that Gad8-K263C is phosphorylated at T387 in Δtor1 cells under normal or low-glucose growth conditions.
PMID:33137119	PBO:0105955	(Fig. 7B)
PMID:33137119	PBO:0093581	(Fig. 6c) (comment: dominent negative effect)
PMID:33137119	FYPO:0000088	Additionally, the phosphorylation sites of Gad8 are required for genotoxic stress, since gad8-S527A/S546A mutant alleles are also sensitive to DNA damage and DNA replication stress (S5B Fig).
PMID:33137119	FYPO:0000082	As previously described [33], mutating both Tor1-dependent phosphorylation sites, S546 and S527, to alanine, abolished the ability of cells to grow at high temperature or in the presence of osmotic stress (Fig 3B)
PMID:33137119	PBO:0093612	(Figure 3d)
PMID:33137119	PBO:0093558	(Fig. 3b)
PMID:33137119	PBO:0105954	(Fig. 3C) we found that Gad8-K263C is phosphorylated at T387 in Δtor1 cells under normal or low-glucose growth conditions.
PMID:33137119	FYPO:0005947	(Fig. 3b)
PMID:33137119	FYPO:0000674	(Fig. 3B)
PMID:33137119	PBO:0105952	(comment: Following release from campthotecin)
PMID:33137119	PBO:0105950	(comment: affecting Gad8-S546 phosphorylation)
PMID:33137119	PBO:0105950	(comment: affecting Gad8-S546 phosphorylation)
PMID:33137119	PBO:0105950	(comment: affecting Gad8-S546 phosphorylation)
PMID:33137119	PBO:0094345	(Fig. 3C) The wild type Gad8 is not phosphorylated at T387 in the absence of Tor1 and is only weakly phosphorylated under low-glucose conditions (Fig 3C).
PMID:33137119	FYPO:0000088	(S5A Fig)
PMID:33137119	PBO:0105948	(comment: affecting substrate Fkh2 in vitro)
PMID:33137119	PBO:0093581	(Fig. 6C,D)
PMID:33137119	PBO:0093823	(comment: pREP81-gad8-T260C) fig 2B
PMID:33137119	PBO:0105949	(Fig. 3A) (comment: affecting substrate Fkh2 in vitro)
PMID:33137119	FYPO:0001032	(comment: pREP81-gad8-Q298L)
PMID:33137119	FYPO:0002578	(comment: pREP81-gad8-Q298L) fig6D
PMID:33137119	PBO:0093824	(comment: pREP81-gad8-Q298L) fig 5a
PMID:33137119	FYPO:0004765	(Fig. 2)
PMID:33137119	PBO:0093580	(Fig. 6b)
PMID:33137119	PBO:0093613	(Fig. 6b)
PMID:33137119	PBO:0093824	(comment: pREP81-gad8-T260C) fig 2B
PMID:33137119	PBO:0093824	(comment: pREP81-gad8-K263C)
PMID:33137119	PBO:0105953	(Fig. 3A) (comment: affecting substrate Fkh2 in vitro)
PMID:33137119	FYPO:0000674	(Fig. 1c)
PMID:33137119	FYPO:0001021	(Fig. 1c)
PMID:33137119	FYPO:0000088	The only conditions under which we did not detect phosphorylation of Gad8-K263C were in Δtor1 cells in the presence of hydroxyurea or camptothecin (S3B Fig), a finding that may suggest that the activity of the kinase responsible for Gad8-K263C phosphorylation is inhibited under genotoxic stress conditions.
PMID:33137119	PBO:0105947	(comment: affecting substrate Fkh2 in vitro)
PMID:33137119	FYPO:0004765	(comment: pREP81-gad8-K263C)
PMID:33137119	PBO:0105948	(comment: affecting substrate Fkh2 in vitro)
PMID:33137119	FYPO:0004765	(comment: CHECK pREP81-gad8-T260C) Figure 2
PMID:33137119	FYPO:0001021	(comment: CHECK pREP81-gad8-K263C)
PMID:33137119	FYPO:0000674	(comment: CHECK pREP81-gad8-K263C) Figure 2
PMID:33137119	FYPO:0001021	(comment: CHECK pREP81-gad8-T260C) fig 1a
PMID:33138913	FYPO:0007594	(Figure 3B,4B)
PMID:33138913	PBO:0100132	This raises the possibility that the MIM complex assists Atg43 through facilitating its mitochondrial localization.
PMID:33138913	PBO:0100123	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—Figure supplement 1I)
PMID:33138913	PBO:0100116	Therefore, we propose that a major role of Atg43 in the mitophagy process is to tether Atg8 to mitochondria through direct interaction with Atg8 via the AIM region.
PMID:33138913	GO:0005741	(Figure 2F, 2G, 2H)
PMID:33138913	PBO:0100123	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—Figure supplement 1I)
PMID:33138913	PBO:0100132	This raises the possibility that the MIM complex assists Atg43 through facilitating its mitochondrial localization.
PMID:33138913	PBO:0100133	(Figure 6B,D)
PMID:33138913	PBO:0100134	(Figure 6B)
PMID:33138913	PBO:0100133	(Figure 6B)
PMID:33138913	FYPO:0007602	By contrast, the atg7D and atg43DAIM mutants did not exhibit such an increased in superoxide (Figure 7D)
PMID:33138913	FYPO:0007602	By contrast, the atg7D and atg43DAIM mutants did not exhibit such an increased in superoxide (Figure 7D)
PMID:33138913	PBO:0100131	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—Figure supplement 1I)
PMID:33138913	PBO:0100131	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—Figure supplement 1I)
PMID:33138913	PBO:0100130	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—Figure supplement 1I)
PMID:33138913	PBO:0100130	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—Figure supplement 1I)
PMID:33138913	PBO:0100123	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—Figure supplement 1I)
PMID:33138913	PBO:0100129	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—Figure supplement 1I)
PMID:33138913	PBO:0100128	We confirmed that Mim1 and Mim2 are required for stable localization of Tom70 on mitochondria in fission yeast (Figure 5—Figure supplement 1H
PMID:33138913	PBO:0100128	We confirmed that Mim1 and Mim2 are required for stable localization of Tom70 on mitochondria in fission yeast (Figure 5—Figure supplement 1H
PMID:33138913	PBO:0100127	This raises the possibility that the MIM complex assists Atg43 through facilitating its mitochondrial localization.
PMID:33138913	PBO:0100127	This raises the possibility that the MIM complex assists Atg43 through facilitating its mitochondrial localization.
PMID:33138913	PBO:0100122	The interaction between full-length Atg43 and Mim2 was confirmed using reciprocal immunoprecipitation experiments (Figure 5A and Figure 5—Figure supplement 1B).
PMID:33138913	PBO:0100123	(Figure 4G)
PMID:33138913	PBO:0093560	(Figure 4C)
PMID:33138913	PBO:0100125	(Figure 4B) Atg43 lacking the 20 C-terminal aa exhibited only a partial defect in mitophagy
PMID:33138913	FYPO:0007594	whereas Atg43 with a truncation of the 60 C-terminal aa was defective in mitophagy (Figure 4B)
PMID:33138913	FYPO:0003768	(Figure 3 Supp 1B&C)
PMID:33138913	FYPO:0007592	(Figure 4B)
PMID:33138913	PBO:0100124	(Figure 4D)
PMID:33138913	PBO:0100123	(Figure 4D)
PMID:33138913	PBO:0100123	(Figure 3K)
PMID:33138913	PBO:0093560	(Figure 3I)
PMID:33138913	FYPO:0001357	(Figure 3I)
PMID:33138913	FYPO:0007594	(Figure 1)
PMID:33138913	FYPO:0007594	(Figure 1D)
PMID:33138913	FYPO:0007592	(Figure 3H)
PMID:33138913	FYPO:0007592	(Figure 3H)
PMID:33138913	PBO:0092097	(Figure 2A)
PMID:33138913	FYPO:0001355	(Figure 5, Figure supplement 1F)
PMID:33138913	PBO:0100117	In the absence of Mim1 or Mim2, the GFP-Atg43 signal at the mitochondria was severely decreased (Figure 5C)
PMID:33138913	FYPO:0007596	Consistent with this, mitophagy was impaired in the mim1D and mim2D mutants (Figure 5D)
PMID:33138913	PBO:0100117	In the absence of Mim1 or Mim2, the GFP-Atg43 signal at the mitochondria was severely decreased (Figure 5C)
PMID:33138913	FYPO:0001355	(Figure 5, Figure supplement 1F)
PMID:33138913	FYPO:0007596	Consistent with this, mitophagy was impaired in the mim1D and mim2D mutants (Figure 5D)
PMID:33138913	FYPO:0007596	(Figure 1A)
PMID:33138913	FYPO:0007448	(Figure 1)
PMID:33138913	FYPO:0007448	(Figure 1)
PMID:33138913	PBO:0100119	(Figure 2)
PMID:33138913	FYPO:0007592	(Figure 3B)
PMID:33138913	FYPO:0007594	(comment: CHECK check genotype******)Figure 3C
PMID:33138913	PBO:0100120	(Figure 3D)
PMID:33138913	PBO:0100121	(Figure 3D)
PMID:33138913	PBO:0100120	(Figure 3D)
PMID:33138913	FYPO:0007592	(Figure 3H)
PMID:33153481	FYPO:0007519	(Fig. 2e) 3D quantification of DAPI stained DNA, G2 arrested cells by cdc2-asM17, + Thiolutin
PMID:33153481	FYPO:0007517	(Fig. 2, S5) (comment: CHECK G2 arrested cells by cdc2-asM17)
PMID:33153481	FYPO:0001352	(Fig. 2,3, S4)(comment CHECK Hi-C, G2 arrested cells by cdc2-asM17)
PMID:33153481	FYPO:0001221	(Fig. S2) (comment: CHECK -background? G2 arrested cells by cdc2-asM17)
PMID:33153481	FYPO:0007516	(Fig. 2a,d,e,f, S3, 3D) quantification of DAPI stained DNA, G2 arrested cells by cdc2-asM17, Shortened the distance between genomic loci
PMID:33153481	FYPO:0007518	(Fig. 6b-d) Rad52 foci quantification, G2 arrested cells by cdc2-asM17, + Thiolutin
PMID:33153481	FYPO:0007328	(Fig. 6b-d) (comment: CHECK Rad52 foci quantification, G2 arrested cells by cdc2-asM17, + Thiolutin
PMID:33153481	FYPO:0000972	(Fig. 6b-d); (comment CHECK Rad52 foci quantification, G2 arrested cells by cdc2-asM17)
PMID:33159083	FYPO:0007533	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	FYPO:0007532	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	FYPO:0007532	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	FYPO:0007532	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	FYPO:0007533	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	FYPO:0007533	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	FYPO:0007532	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	GO:1990426	(comment: CHECK pmt3-D81R pmt3-KallR)
PMID:33159083	PBO:0100676	(comment: same as nup132delta alone)
PMID:33159083	FYPO:0007532	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	FYPO:0007532	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	FYPO:0007532	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	FYPO:0007532	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	FYPO:0007532	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	FYPO:0007532	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	FYPO:0007533	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33172987	FYPO:0001357	(Figure S2)
PMID:33172987	PBO:0101373	(Figure S2)
PMID:33172987	PBO:0101372	(Figure 3A)
PMID:33172987	FYPO:0001357	(Figure S2)
PMID:33172987	FYPO:0001355	(Figure S3)
PMID:33172987	FYPO:0001357	(Figure S2)
PMID:33172987	PBO:0095685	(comment: CHECK THIS IS A GUESS I COULD NOT ACCESS THE SUPP SO ANNOTATED TO THE Snider ITS3-1 growth phenotype)
PMID:33172987	FYPO:0001357	(Figure S2)
PMID:33172987	FYPO:0001357	(Figure S2)
PMID:33172987	FYPO:0001357	(Figure S2)
PMID:33172987	FYPO:0001357	(Figure S2)
PMID:33172987	PBO:0101371	(Figure S1)
PMID:33172987	GO:0005515	(comment: PH1 domain) Fig. 2A, Table S2
PMID:33172987	PBO:0101375	(Figure 1C) (comment: CHECK requested normal membrane lipid binding)
PMID:33172987	PBO:0101376	(Figure 1C)
PMID:33172987	PBO:0101371	(Figure S1)
PMID:33172987	GO:1902635	(comment: I changed the function annotation to this process annotation because it precisely negates the SGD annotation)
PMID:33172987	PBO:0101371	(Figure S1)
PMID:33172987	GO:0005543	(comment: Opy1 PH1 (aa1-128) can directly bind phospholipids in vitro) (Figure 1)
PMID:33172987	GO:0005543	(Figure 3)
PMID:33172987	FYPO:0001357	(Figure S2)
PMID:33172987	FYPO:0001355	(Figure S3)
PMID:33172987	PBO:0101374	(Figure S3)
PMID:33172987	FYPO:0001357	(Figure S2)
PMID:33172987	FYPO:0001357	(Figure S2)
PMID:33172987	FYPO:0000339	(Figure 4E-F)
PMID:33172987	PBO:0101371	(Figure S1)
PMID:33172987	PBO:0101372	(Fig. S2B)
PMID:33172987	GO:0005546	(Fig. 1D-E)
PMID:33172987	PBO:0101371	(Fig. 1F-G
PMID:33176147	FYPO:0005555	(Figure 2c,3B and S3B Figures 4C and 4D)
PMID:33176147	FYPO:0007544	(Fig. 1E)
PMID:33176147	FYPO:0005018	(Fig. 1F)
PMID:33176147	FYPO:0007542	(Fig. S2A)
PMID:33176147	FYPO:0007544	(Fig. 1E)
PMID:33176147	FYPO:0007544	(Fig. 1E)
PMID:33176147	FYPO:0005018	(Fig. 1F)
PMID:33176147	PBO:0100478	(Figures 4E and 4F)
PMID:33176147	PBO:0100478	(Figures 4E and 4F)
PMID:33176147	PBO:0100477	(Figures 4E and 4F)
PMID:33176147	FYPO:0005555	(Figure 2c,3B and S3B Figures 4C and 4D)
PMID:33176147	FYPO:0007543	(Fig. 1F)
PMID:33176147	FYPO:0007542	(Fig. 1F,S2A)
PMID:33176147	PBO:0096647	(Fig. 2A)
PMID:33176147	PBO:0094949	(Fig. 2A)
PMID:33202882	PBO:0099385	(comment: intron 2)
PMID:33225241	PBO:0093559	(comment: same as mas5delta alone)
PMID:33225241	PBO:0093559	(comment: same as mas5delta alone)
PMID:33357436	FYPO:0001365	(Figures 3C, 3D)
PMID:33357436	PBO:0106495	(comment: In vitro binding assay with Cdc15 F-BAR domain and full length Pxl1)
PMID:33357436	PBO:0099724	(Figure S2E)
PMID:33357436	PBO:0119851	(Figure 4F)
PMID:33357436	FYPO:0005221	(Figure S2B) of purified Cdc15 F-BAR domain
PMID:33357436	PBO:0106497	(Figure S2C)
PMID:33357436	PBO:0106498	(comment: moved down from abnormal localization)
PMID:33357436	PBO:0108785	These results indicate that the Cdc15 F-BAR domain can position Cdc12 directly at the PM by binding membrane and Cdc12 simultaneously.
PMID:33357436	PBO:0106491	(Fig. 2B) (comment: in vitro binding assay with Cdc15 F-BAR domain and Cdc12 peptide aa20-40)
PMID:33357436	PBO:0106492	(Figure 3A)
PMID:33357436	FYPO:0004594	(comment: additional cewlll. poles)
PMID:33378674	GO:0006335	(comment: at pericentromeric regions)
PMID:33378677	PBO:0107727	inferred from abolished interaction between Pof8 and Lsm subunits
PMID:33378677	PBO:0107728	inferred from decreased interaction between Pof8 and Lsm subunits
PMID:33378677	PBO:0107726	inferred from abolished interaction between Pof8 and Lsm subunits
PMID:33400299	PBO:0103212	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	PBO:0103215	To further examine whether ROS and NO mediated increased Rst2 transcriptional activity caused by mitochondrial complex III/IV inhibitors, we examined the effect of antioxidant N-acetyl-L-cysteine (NAC) which aids in ROS detoxification and 2-(4-Carboxyphenyl)-4,4,5,5-tetramethy-limidazo-line-1-oxyl-3- oxide (Carboxy-PTIO), a NO-specific scavenger on the Rst2 transcriptional activity stimulated by mitochondrial complex III/IV inhibitors. The results showed that NAC and Carboxy-PTIO significantly inhibited mitochondrial complex III/IV inhibitors-induced activation of Rst2 in a dose-dependent manner (Figure 2e-j) suggesting that ROS and NO were involved in mitochondrial respiratory chain complex III/IV inhibitors-induced activation of Rst2. To further prove this result, we also examined the effect of a mammalian NO synthesis (NOS) inhibitor, N G-nitro-l-arginine methyl ester (NAME) on the Rst2 transcriptional activity stimulated by mitochondrial complex III/IV inhibitors, since it was reported that NAME treatment can reduce NO formation by more than 60% in yeast cells (Astuti et al., 2016a). As expected, NAME dose-dependently decreased mitochondrial complex III/IV inhibitors- induced Rst2 activation (Figure 2k-m).
PMID:33400299	PBO:0103212	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	PBO:0103216	(Figure 2k-m).
PMID:33400299	PBO:0103217	(Figure 2n)
PMID:33400299	FYPO:0007617	Table1
PMID:33400299	FYPO:0000440	Table1
PMID:33400299	PBO:0103212	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	PBO:0103212	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	PBO:0103212	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	PBO:0103217	(Figure 2n)
PMID:33400299	PBO:0103218	(Figure 2n)
PMID:33400299	PBO:0103212	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	PBO:0103212	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	PBO:0103212	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	PBO:0103212	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	FYPO:0000440	Table1
PMID:33400299	FYPO:0006141	(Figure 4b)
PMID:33400299	FYPO:0006141	(Figure 4b)
PMID:33400299	FYPO:0006141	(Figure 4b)
PMID:33400299	PBO:0103219	(Fig. 3a) glucose r excess
PMID:33400299	PBO:0020037	(Fig. 3a) glucose starve
PMID:33400299	PBO:0103220	(Fig. 3a) glucose starve
PMID:33400299	FYPO:0006141	(Figure 4b)
PMID:33400299	FYPO:0006141	(Figure 4b)
PMID:33400299	FYPO:0006141	(Figure 4b)
PMID:33400299	FYPO:0006141	(Figure 4b)
PMID:33400299	FYPO:0006141	(Figure 4b)
PMID:33400299	PBO:0103212	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	PBO:0103212	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	FYPO:0006141	(Figure 4b)
PMID:33400299	FYPO:0006141	(Figure 4b)
PMID:33400299	FYPO:0006141	(Figure 4b)
PMID:33400299	FYPO:0006141	(Figure 4b)
PMID:33400299	PBO:0103214	(Figure 1m)
PMID:33400299	PBO:0103212	(Figure 1m)
PMID:33410907	PBO:0103165	As shown in Figure 3C and D, upon H2O2 stress, Rpb1 was recruited to the promoter and extensively phosphorylated at Ser5.
PMID:33410907	PBO:0103181	(Figure 2c) (comment: CHECK this replaces the sty1 WT annotation Should this be normal? i.e. normal for the conditions? )
PMID:33410907	PBO:0103180	(Figure 2c) (comment: CHECK this replaces the sty1 WT annotation Should this be normal? i.e. normal for the conditions? )
PMID:33410907	PBO:0111318	(Figure 5D)
PMID:33410907	FYPO:0003004	(comment: CHECK is this +h2o2) the intracellular level of ROS was elevated in pin1 and ssu72 mutants (Figure 6H)
PMID:33410907	FYPO:0003004	(comment: CHECK is this +H2o2) the intracellular level of ROS was elevated in pin1 and ssu72 mutants (Figure 6H)
PMID:33410907	PBO:0111317	Ssu72, but not with the GST control in the pull down experiment. These results suggested that Pin1 directly interacted with and recruited Ssu72 for pSer5 dephosphorylation to facilitate progression of transcription important for cellular response to oxidative stress
PMID:33410907	PBO:0103178	(Figure 4) (comment: Sty1 interacted and phosphorylated Rpb1-CTD at Ser5)
PMID:33410907	PBO:0114650	(Figure 6c) (comment: The anti-myc, anti-Rpb1 CTD (8WG16) and anti-pS5-Rpb1 CTD (H14) antibodies were used for immunoprecipitation.)
PMID:33410907	PBO:0103177	These results suggested that, in addition to the binding to theRpb1-CTD, the isomerization activity was also required for the fu
PMID:33410907	PBO:0103175	Intriguingly, upon oxidative stress, the association between Rpb1 and Sty1 was decreased in wild type cells and up regulated in the pin1 mutant with reduced phosphorylation of Ser2 (Figure 4B).
PMID:33410907	PBO:0103172	In line with these results, Ser2 phosphorylation of Rpb1-CTD, which facilitated transcription elongation, was reduced in pin1 mutant as a secondary effect derived from defect in transcription initiation to elongation (Figure 3A and B).
PMID:33410907	PBO:0103170	In line with these results, Ser2 phosphorylation of Rpb1-CTD, which facilitated transcription elongation, was reduced in pin1 mutant as a secondary effect derived from defect in transcription initiation to elongation (Figure 3A and B).
PMID:33410907	PBO:0103169	In the absence of Pin1, Ser5 phosphorylated Rpb1 was associated and accumulated at the promoter region following H2O2 stress but was defective in entering elongation to generate transcripts of the corresponding genes (Figure 1C)
PMID:33410907	PBO:0103168	As shown in Figure 3C and D, upon H2O2 stress, Rpb1 was recruited to the promoter and extensively phosphorylated at Ser5.
PMID:33410907	PBO:0103167	2B
PMID:33410907	PBO:0103166	2B
PMID:33410907	PBO:0103165	2B
PMID:33410907	PBO:0094384	(Figure 1C)
PMID:33410907	PBO:0097079	(Figure 1C)
PMID:33410907	PBO:0097080	(Figure 1C)
PMID:33410907	PBO:0103164	fig? (comment: under calf alkaline phosphatase treated)
PMID:33410907	PBO:0101320	(Fig. 2a)
PMID:33410907	PBO:0092468	(Figure 1)
PMID:33410907	PBO:0092468	(Figure 1)
PMID:33410907	PBO:0092468	(Figure 1)
PMID:33410907	PBO:0096825	(Figure 4) (comment: Sty1 interacted and phosphorylated Rpb1-CTD at Ser5)
PMID:33410907	PBO:0103163	(Figure 4) (comment: Sty1 interacted and phosphorylated Rpb1-CTD at Ser5)
PMID:33410907	FYPO:0001103	(Figure 5)
PMID:33410907	FYPO:0000087	(Figure 5)
PMID:33410907	FYPO:0005889	(Figure 5e)
PMID:33410907	FYPO:0000087	(Figure 1)
PMID:33410907	FYPO:0006819	(Figure 1)
PMID:33419777	PBO:0107433	(Fig. 4A)
PMID:33419777	PBO:0102590	(Fig. 5A)
PMID:33419777	PBO:0102679	(Fig. 5A)
PMID:33419777	PBO:0107434	(Fig. 4B,C,D) A cellular phenotype found in multinucleated cells where nuclear division is no longer synchronous and cells with an odd number of nuclei are observed
PMID:33419777	FYPO:0007474	(Fig S1) delayed septation, Cellular phenotype where cells initiate growth before septation has taken place, resulting in variable cell size at division.
PMID:33419777	FYPO:0007474	(Fig. 3I) (comment: same in wild type background)
PMID:33419777	PBO:0107432	(Fig. 1A)
PMID:33419777	FYPO:0007474	(Fig. 1B, C Table 1)
PMID:33419777	FYPO:0007474	(Fig. 1B, C Table 1)
PMID:33419777	FYPO:0007474	(Fig. 1B, C Table 1)
PMID:33419777	FYPO:0007474	(Fig. 1B, C Table 1)
PMID:33419777	FYPO:0007474	(Fig. 1B, C Table 1)
PMID:33419777	FYPO:0007660	(Fig. 2, Table 2)
PMID:33419777	FYPO:0007660	(Fig. 2, Table 2)
PMID:33419777	FYPO:0007660	(Fig. 3A-F) (comment: same result in wild type background)
PMID:33419777	FYPO:0007660	(Fig. 3A-F) (comment: same result in Wild type background)
PMID:33419777	FYPO:0007474	(Fig. 3H) (comment: same in wild type background)
PMID:33419777	PBO:0107437	(Fig. 4A)
PMID:33419777	PBO:0104580	(Fig. 5A)
PMID:33419777	PBO:0107436	(Fig. 5E,F) abnormal protein localisation in multinucleated cells
PMID:33419777	FYPO:0007474	(Fig. 5C Table 3)
PMID:33419777	PBO:0107435	(Fig. 5C) compare16 and 17 Table 3 I don't quite know how to annotate this or whether I leave it as 'variable size at division and do a genetic interaction and Im not sure that the term I have suggested is right
PMID:33419777	PBO:0107435	cellular phenotype of variable cell size at division may be further increased in the absence of another cellular protein Fig5 compare 14 and 15 Table 3 I don't quite know how to annotate this or whether I leave it as 'variable size at division and do a genetic interaction and Im not sure that the term I have suggested is right
PMID:33419777	PBO:0107435	(Fig. 5C) compare 7 and 9 When cdc2 is not tyrosine phosphorylation mga2 delta does not increase the cell size variability any further.
PMID:33419777	PBO:0107435	(Fig. 5C) compare 4 and 6 the variability of cdc2cdc13 fusion protein is increased in mga2 delta. I don't quite know how to annotate this or whether I leave it as 'variable size at division and do a genetic interaction and Im not sure that the term I have suggested is right
PMID:33434270	PBO:0106087	(Figure 6A)
PMID:33434270	PBO:0106086	(Figure 5A)
PMID:33437930	FYPO:0000726	The spotting assay revealed the enhanced pyrogallol sensitivity of wat1/pop3 delete cells as compared to wild type cells (Fig. 1A)
PMID:33468217	FYPO:0003044	inferred from silencing and H3-K9 methylation phenotypes
PMID:33468217	GO:0031445	inferred from silencing and H3-K9 methylation phenotypes
PMID:33483504	PBO:0097071	As shown in Fig. 6b, c, Emr1-FL and Emr1-ΔN, but not Emr1-ΔC, restored the normal number of Mdm12 foci, confirming that the C-terminus of Emr1 is required for regulating the number of ERMES foci.
PMID:33483504	PBO:0097069	(Figure 3a)
PMID:33483504	PBO:0097070	(Figure 3b)
PMID:33483504	FYPO:0007611	(Fig. 3b)
PMID:33483504	FYPO:0001234	(Fig. 3d)
PMID:33483504	PBO:0097071	(Fig. 4) significantly decreased the number of Mdm12 (a constitutive component of the ERMES complex) foci
PMID:33483504	PBO:0097072	(Fig. 4d) (comment: though the expression levels of Mdm12 were comparable in WT and emr1Δ Cells)
PMID:33483504	PBO:0097073	(Fig. 5)
PMID:33483504	GO:0120010	(comment: er to mitochondria)
PMID:33483504	FYPO:0000895	(Fig. 1) (comment: cox4-GFP to label Mt)
PMID:33483504	FYPO:0007611	(Fig. 1a)
PMID:33483504	PBO:0097067	(Fig. 1b) (comment: n=344)
PMID:33483504	FYPO:0001234	(Fig. 1b) (comment: n=344)
PMID:33483504	PBO:0095634	(Fig. 1c)
PMID:33483504	PBO:0097068	(Fig. 1d) Despite the multiple types of abnormalities observed in emr1Δ cells, mitochondria of emr1Δ cells were still able to undergo fission and fusion (Fig. 1d), but improperly segregated into daughter cells after mitosis (Fig. 1e). This phenotype of defective mitochondrial segregation is consistent with the previous finding that spherical/giant mitochondria in mutant cells compromise mitochondrial movements, inheritance, and segregation7,8,2
PMID:33483504	GO:0032473	(comment: integral) Fig. 2a, 2b, 2c, 2d
PMID:33483504	PBO:0097069	(Figure 3a)
PMID:33496728	PBO:0104822	(Figures 1,5) +5 min, a 15-min delay compared with wild-type cells
PMID:33496728	FYPO:0003946	(Figure 5)
PMID:33496728	PBO:0104823	(Figure 5)
PMID:33496728	FYPO:0003946	(Figure S3)
PMID:33496728	FYPO:0003946	(Figure S3)
PMID:33496728	PBO:0104825	(Fig. 4 C). Cdc12p distributed in a smaller zone in the R-nodes of Δmid1 cells...node dimensions in the R-nodes of constricting contractile rings.....
PMID:33496728	FYPO:0003946	(Figure S3)
PMID:33496728	FYPO:0000161	(Figure S1)
PMID:33496728	FYPO:0001368	(Figure S1)
PMID:33496728	FYPO:0000161	(Figure S1)
PMID:33496728	FYPO:0001364	(Figure S1)
PMID:33496728	PBO:0104820	(Figure 1)
PMID:33496728	FYPO:0000161	(Figure 6)
PMID:33496728	PBO:0104819	(Figure 1)
PMID:33496728	FYPO:0007830	(Figure 3) (Figure 4) (Figure S2)
PMID:33496728	PBO:0104818	(Figure 2) (Figure 3) (Figure 4) (Figure S2)
PMID:33496728	FYPO:0000161	(Figure 1A, B)
PMID:33496728	PBO:0104817	(Figure 1E,F) The average constriction rate of Δmid1 contractile rings is 0.27 μm/min (Saha and Pollard, 2012a), but the distribution of constriction rates appears bimodal with fast and slow subpopulations. The type of strand that builds the contractile ring strongly correlates with its constriction rate, with contractile rings made from nascent strands constricting faster (0.32 μm/min) and contractile rings made from enduring strands constricting more slowly (0.20 μm/min; Fig. 1 E).
PMID:33496728	PBO:0104820	(Figure 1E, F) We generated Δmid1 Δmyp2 double-mutant cells and found that the distribution of constriction rates of their contractile rings is still bimodal, albeit with both populations constricting 25-50% more slowly than the Δmid1 populations, consistent with Myp2p being responsible for ∼50% of the constriction rate
PMID:33496728	PBO:0104821	(Figure 1E, F)
PMID:33496728	FYPO:0000161	(Figure 5) (comment: vw: changed severity from high to low as this seems to partially rescue mid1-delta?)
PMID:33496728	FYPO:0007832	(Figure 5)
PMID:33496728	PBO:0104824	(Figure 1E,F) (comment: VW instead of abnormal, I did increased and decreased rate with low penetrance i.e the rate is variable within the population someincreased and some decrreased, although there see to be 2 distinct sub-populations we can't capture this effectively)
PMID:33506191	PBO:0102838	(Fig. 1)
PMID:33506191	PBO:0102837	(Fig. 1)
PMID:33506191	PBO:0102837	(Fig. 1)
PMID:33506191	PBO:0102837	(Fig. 1)
PMID:33506191	PBO:0102837	(Fig. 1)
PMID:33506191	PBO:0102837	(Fig. 1)
PMID:33506191	PBO:0102837	(Fig. 1)
PMID:33506191	PBO:0102837	(Fig. 1)
PMID:33506191	PBO:0102838	(Fig. 1)
PMID:33506191	PBO:0102838	(Fig. 1)
PMID:33506191	PBO:0102838	(Fig. 1)
PMID:33506191	PBO:0102838	(Fig. 1)
PMID:33506191	PBO:0102838	(Fig. 1)
PMID:33506191	PBO:0102839	(Fig. 2) (comment: live cell imaging)
PMID:33506191	PBO:0102840	(Fig. 2) (comment: live cell imaging)
PMID:33506191	PBO:0102841	(Fig. 7) These results indicate that first, the main reason for lethality of cut7 is derived from the cut phenotype; second, some cells could escape from cut by displacing the nucleus from the middle of the cell axis; and finally, these cut7 survivors could resume cell division as diploid progenies at the permissive temperature.
PMID:33506191	PBO:0102842	"(Fig. 4) (comment: If possible, please add the following comment - “The nucleus is retained in the center of the cell during mitosis."")"
PMID:33506191	PBO:0102842	(Fig. 4)
PMID:33506191	PBO:0102842	(Fig. 4)
PMID:33506191	PBO:0102842	(Fig. 6)
PMID:33506191	PBO:0102843	(Fig. 7)
PMID:33511417	FYPO:0007656	(comment: genome-wide average; slightly increased amplitudes of the -2, -1, +1 nucleosome peaks (relative to NDR)
PMID:33511417	FYPO:0004491	(comment: genome-wide average)
PMID:33526714	PBO:0099413	(Figure 2)
PMID:33526714	PBO:0099413	(Figure 2)
PMID:33526714	PBO:0099413	(Figure 2)
PMID:33526714	PBO:0099413	(Figure 2)
PMID:33526714	PBO:0099413	(Figure 2)
PMID:33526714	PBO:0099410	(Figure 2)
PMID:33526714	PBO:0099410	(Figure 2)
PMID:33526714	PBO:0099410	(Figure 2)
PMID:33526714	PBO:0099412	(Figure 2)
PMID:33526714	PBO:0099411	(Figure 2)
PMID:33526714	PBO:0099410	(Figure 2)
PMID:33526714	PBO:0099410	(Figure 2)
PMID:33526714	PBO:0099410	(Figure 2)
PMID:33526714	PBO:0099413	(Figure 2)
PMID:33529549	FYPO:0005634	***** increased bi-oriented attachment of sister chromatids in meiosis I*****The frequencies of sister centromere splitting varied (electronic supplementary material, Figure S2A), but the mean splitting frequencies per centromere obtained by the bootstrap method were significantly higher in rec12Δ cells than in rec12+ cells (the difference was also significant in the usual t-test, p < 0.01; Figure 2d, +). The elevated frequency of sister centromere splitting in chiasma-lacking cells confirms that chiasmata prevent bi-oriented attachment of sister chromatids.
PMID:33529549	PBO:0109801	(Figure 1) These results indicate that the error correction mechanism decreases bi-oriented attachment of sister chromatids in the presence of chiasmata, but conversely increases bi-oriented attachment (thereby decreasing mono-oriented attachment) in the absence of chiasmata. In our previous study, the equational segregation frequencies of cen1 were somewhat higher in the rec12Δ background [28], although the reason for this is unknown. However, the mad2Δ mutation similarly decreased equational segregation, being consistent with our current results.
PMID:33529549	PBO:0109802	(Figure 1) Decreased equational segregation in the sgo1∆ rec12∆ background or the haploid sgo1∆ background.
PMID:33529549	PBO:0109803	(Figure 1) Increased equational segregation in the sgo1∆ background.
PMID:33529549	PBO:0109245	Importantly, the dam1Δ mutation impaired disjunction of homologous chromosomes (Figure 5a), as seen in mad2Δ and ark1-so mutants [25,52].
PMID:33529549	PBO:0109805	Furthermore, the dam1Δ mutation increased equational segregation of sister chromatids in rec12+ cells (Figure 5b, left) but it decreased equational segregation in sgo1Δ rec12Δ or haploid meiotic sgo1Δ cells (Figure 5b,c)
PMID:33529549	PBO:0109806	Decreased equational segregation in the diploid sgo1∆ rec12∆ background or the haploid sgo1∆ background.
PMID:33529549	FYPO:0008099	Anaphase A chromosome movement is completely abolished and only anaphase B chromosome movement occurs.
PMID:33529549	PBO:0109807	(Figure 1) Increased equational segregation in sgo1∆ background.
PMID:33529549	PBO:0109808	(Figure 1) Increased equational segregation in sgo1∆ background.
PMID:33529549	GO:0031619	The elevated frequency of sister centromere splitting in chiasma-lacking cells confirms that chiasmata prevent bi-oriented attachment of sister chromatids.
PMID:33533152	PBO:0093616	(Fig. 8B)
PMID:33533152	FYPO:0000969	(Fig. 10B)
PMID:33533152	FYPO:0000969	(Fig. 10B)
PMID:33533152	FYPO:0001689	(Fig. 10B)
PMID:33533152	FYPO:0001689	(Fig. 10B)
PMID:33533152	FYPO:0000957	(Fig. 10B)
PMID:33533152	FYPO:0000957	(Fig. 10B)
PMID:33533152	PBO:0116513	(Fig. 10C)
PMID:33533152	PBO:0116513	(Fig. 10C)
PMID:33533152	PBO:0116512	(Fig. 10C)
PMID:33533152	PBO:0116512	(Fig. 10C)
PMID:33533152	PBO:0116511	(Fig. 10C)
PMID:33533152	PBO:0116510	(Fig. 10C)
PMID:33533152	PBO:0116513	(Fig. 10A)
PMID:33533152	PBO:0116513	(Fig. 10A)
PMID:33533152	PBO:0116512	(Fig. 10A)
PMID:33533152	PBO:0116512	(Fig. 10A)
PMID:33533152	PBO:0116511	(Fig. 10A)
PMID:33533152	PBO:0116510	(Fig. 10A)
PMID:33533152	PBO:0116509	(Fig. 9B)
PMID:33533152	PBO:0116509	(Fig. 9B)
PMID:33533152	PBO:0116508	(Fig. 9B)
PMID:33533152	PBO:0116508	(Fig. 9B)
PMID:33533152	FYPO:0007074	(Fig. 9A)
PMID:33533152	FYPO:0007074	(Fig. 9A)
PMID:33533152	PBO:0116507	(Fig. 9B)
PMID:33533152	PBO:0116506	(Fig. 9B)
PMID:33533152	PBO:0099621	(Fig. 9A)
PMID:33533152	FYPO:0000969	(Fig. 8B)
PMID:33533152	FYPO:0000969	(Fig. 8B)
PMID:33533152	FYPO:0000957	(Fig. 8B)
PMID:33533152	FYPO:0000957	(Fig. 8B)
PMID:33533152	FYPO:0001689	(Fig. 8B)
PMID:33533152	FYPO:0001689	(Fig. 8B)
PMID:33533152	PBO:0106872	(Fig. 8B)
PMID:33533152	PBO:0093603	(Fig. 8B)
PMID:33533152	PBO:0116509	(Fig. 6B)
PMID:33533152	PBO:0116509	(Fig. 6B)
PMID:33533152	PBO:0116508	(Fig. 6B)
PMID:33533152	PBO:0116508	(Fig. 6B)
PMID:33533152	PBO:0116507	(Fig. 6B)
PMID:33533152	PBO:0116506	(Fig. 6B)
PMID:33533152	FYPO:0007074	(Fig. 6A)
PMID:33533152	FYPO:0007074	(Fig. 6A)
PMID:33533152	PBO:0099621	(Fig. 6A)
PMID:33533152	PBO:0112537	(Fig. 5)
PMID:33533152	FYPO:0003503	(Fig. 4C)
PMID:33533152	FYPO:0003503	(Fig. 4C)
PMID:33533152	PBO:0116505	(Fig. 4C)
PMID:33533152	FYPO:0000957	(Fig. 3D)
PMID:33533152	FYPO:0000957	(Fig. 3D)
PMID:33533152	FYPO:0001689	(Fig. 3D)
PMID:33533152	FYPO:0001689	(Fig. 3D)
PMID:33533152	FYPO:0000969	(Fig. 2C, 3A)
PMID:33533152	FYPO:0000969	(Fig. 2C, 3A)
PMID:33533152	FYPO:0000957	(Fig. 2C, 3A)
PMID:33533152	FYPO:0000957	(Fig. 2C, 3A)
PMID:33533152	FYPO:0001689	(Fig. 2A, 3A)
PMID:33533152	FYPO:0001689	(Fig. 2A, 3A)
PMID:33533152	PBO:0093616	(Fig. 2C)
PMID:33533152	PBO:0106872	(Fig. 2C)
PMID:33533152	PBO:0093603	(Fig. 2A)
PMID:33533152	FYPO:0000969	(Fig. 3D)
PMID:33533152	FYPO:0000969	(Fig. 3D)
PMID:33533152	PBO:0093616	(Fig. 3D)
PMID:33533152	PBO:0109839	(Fig. 3D)
PMID:33533152	PBO:0093603	(Fig. 3D)
PMID:33534698	PBO:0099993	Consistently, in the absence of intact GATOR1, the vacuolar localization of Sea3 (Figure 1E) was lost and the protein diffused throughout the cytosol (Figure 3I, Figure 3—Figure supplement 1A)
PMID:33534698	PBO:0099992	The binding of Sea3 to GATOR1 is dependent on the integrity of the GATOR1 complex, and the absence of any one of the GATOR1 subunits disrupted the Sea3-GATOR1 association (Figure 3F,G and H).
PMID:33534698	PBO:0099992	The binding of Sea3 to GATOR1 is dependent on the integrity of the GATOR1 complex, and the absence of any one of the GATOR1 subunits disrupted the Sea3-GATOR1 association (Figure 3F,G and H).
PMID:33534698	PBO:0099991	On the other hand, Iml1 and Sea3 were co-immunoprecipitated even in the absence of Seh1, Sea2, and Sea4 (Figure 3E), implying that Sea3 directly binds to GATOR1 and anchors the other GATOR2 components to GATOR1.
PMID:33534698	PBO:0099990	(Figure 2g)
PMID:33534698	FYPO:0001357	(Figure 2e) (comment:sea3 rescued by gtr1 GDP-locked)
PMID:33534698	GO:1990130	(Figure 1)
PMID:33534698	GO:0035859	(Figure 1)
PMID:33534698	GO:0061700	(Figure 1)
PMID:33534698	GO:0061700	(Figure 1)
PMID:33534698	GO:0061700	(Figure 1)
PMID:33534698	GO:0061700	(Figure 1)
PMID:33534698	GO:0061700	(Figure 1)
PMID:33534698	PBO:0099983	Indeed, we observed that, after leucine starvation, the Fil1 protein increased, which was dependent on Gcn2 and the phosphorylation of eIF2a (Figure 4—Figure supplement 1H).
PMID:33534698	FYPO:0007803	Moreover, S. pombe cells lacking Gcn3 (Figure 4D) or Fil1 (Figure 4F) displayed autophagy defects during leucine starvation.
PMID:33534698	PBO:0100003	However, no GFP accumulation was detected in gcn2D cells under leucine starvation (Figure 4C), demonstrating that the autophagy induced by leucine starvation is dependent on the Gcn2 kinase.
PMID:33534698	PBO:0100002	Recently, another conserved arginine residue in mammalian GATOR1, Arg78 of the Nprl2 subunit,was proposed to serve as an arginine finger that promotes GTP hydrolysis by RagA/B (Shen et al.,2019, Figure 3—Figure supplement 3B). To assess the role of the equivalent residue in the S.pombe GATOR1, Arg98 in Npr2 was substituted with alanine to construct an npr2R98A mutantstrain. The mutant cells exhibited a compromised growth phenotype that was rescued by rapamycinor the gtr1SN mutation, an indicative of compromised GAP activity of GATOR1 (Figure 3—Figure supplement 3C). Though the npr2R98A phenotype was not as severe as that of the npr2 nullmutant, these observations are in line with the model that the conserved Arg residue in Npr2, butnot the one in Iml1, acts as an arginine finger of GATOR1 also in fission yeast.
PMID:33534698	PBO:0100001	Recently, another conserved arginine residue in mammalian GATOR1, Arg78 of the Nprl2 subunit,was proposed to serve as an arginine finger that promotes GTP hydrolysis by RagA/B (Shen et al.,2019, Figure 3—Figure supplement 3B). To assess the role of the equivalent residue in the S.pombe GATOR1, Arg98 in Npr2 was substituted with alanine to construct an npr2R98A mutantstrain. The mutant cells exhibited a compromised growth phenotype that was rescued by rapamycinor the gtr1SN mutation, an indicative of compromised GAP activity of GATOR1 (Figure 3—Figuresupplement 3C). Though the npr2R98A phenotype was not as severe as that of the npr2 nullmutant, these observations are in line with the model that the conserved Arg residue in Npr2, butnot the one in Iml1, acts as an arginine finger of GATOR1 also in fission yeast.
PMID:33534698	FYPO:0001357	(Figure 2e) (comment: sea3 rescued by gtr1 GDP-locked)
PMID:33534698	FYPO:0001357	(Figure 2b) (comment: any1 rescues)
PMID:33534698	FYPO:0001357	(Figure 2b) (comment: any1 rescues)
PMID:33534698	PBO:0093560	(Figure 2b)
PMID:33534698	PBO:0099989	(Figure 2f)
PMID:33534698	PBO:0099997	In the case of the sea3D mutant, Iml1, Npr2, and Npr3 were all detectable on vacuoles (Figure 3—Figure supplement 2E,F and G)
PMID:33534698	PBO:0099996	(Figure 3 Figure supplement 1C-E).
PMID:33534698	PBO:0099995	(Figure 3 Figure supplement 1C-E).
PMID:33534698	PBO:0099994	Furthermore, consi tent with the essential role of Sea3 in the interaction between GATOR1 and the other GATOR2 subunits, the vacuolar localization of Sea2, Sea4, and Seh1 ( was abrogated in the sea3D background (Figure 3—Figure supplement 1C-E).
PMID:33534698	PBO:0099992	The binding of Sea3 to GATOR1 is dependent on the integrity of the GATOR1 complex, and the absence of any one of the GATOR1 subunits disrupted the Sea3-GATOR1 association (Figure 3F,G and H).
PMID:33534698	FYPO:0007803	(Fig. 4e) In order to test whether the Gcn2 kinase induces autophagy through phosphorylation of eIF2a, we constructed a strain that expresses eIF2a with its phosphorylation site Ser52 substituted by alanine (eIF2a-S52A).
PMID:33534698	GO:0005774	(Figure 1, Supp 1)
PMID:33534698	GO:0005774	(Figure 1, Supp 1)
PMID:33534698	GO:0005774	(Figure 1, Supp 1)
PMID:33534698	PBO:0099984	(comment: vw I edited to make the response the extension to GCN2 mediated signalling, but I hope to improve these GO terms.)
PMID:33534698	PBO:0099986	Gcn2-dependent induction of autophagy was also observed in cells treated by 3-amino-1,2,4-triazole (3-AT) or methionine sulfoximine (MSX), inhibitors of histidine and glutamine biosynthesis, respectively (Figure 4—Figure supplement 1D,E).
PMID:33534698	GO:0010508	Autophagy in response to leucine starvation was abrogated by the gcn1D, but not gcn20D, mutation (Figure 4D)
PMID:33534698	PBO:0099987	We found that autophagy after leucine starvation was severely impaired in cells lacking Cpc2 and in those overexpressing a fission yeast ortholog of Yih1/IMPACT (Figure 4—Figure supplement 1G), confirming the essential role of the Gcn2 activity in autophagy induction upon amino acid starvation.
PMID:33534698	PBO:0099988	(Fig. 4a) Though much less than that in wild-type cells, autophagy was still detectable in the tsc2D iml1D double mutant, indicating that, in addition to the GATOR1 and TSC complexes, there must be an additional mechanism to attenuate TORC1 upon nitrogen starvation for autophagy induction.
PMID:33534698	PBO:0099988	(Fig. 4a)
PMID:33534698	FYPO:0001357	(Figure 2a)
PMID:33534698	FYPO:0001357	(Figure 2a)
PMID:33534698	FYPO:0001357	(Figure 2a)
PMID:33534698	FYPO:0001357	(Figure 2a)
PMID:33534698	FYPO:0001357	(Figure 2a)
PMID:33534698	FYPO:0001357	(Figure 2a)
PMID:33534698	GO:0005774	(Figure 1, Supp 1)
PMID:33534698	GO:0005774	(Figure 1, Supp 1)
PMID:33534698	GO:0005774	(Figure 1, Supp 1)
PMID:33534698	GO:0005774	(Figure 1, Supp 1)
PMID:33534698	FYPO:0001355	(Figure 2a)
PMID:33534698	FYPO:0001357	(Figure 2a)
PMID:33534698	FYPO:0001355	(Figure 2a)
PMID:33534698	FYPO:0001357	(Figure 3—Figure supplement 3A), indicating that Arg854 of S. pombe Iml1 is not essential for the GATOR1 function.
PMID:33534698	PBO:0100000	On the other hand, immunoprecipitation of the GATOR1 subunit Iml1 found that the physical interaction between GATOR1 and the Gtr1 GTPase was reduced in the sea3D mutant (Figure 3M).
PMID:33534698	PBO:0099999	(Figure 3 Figure supplement 2E,F and G)
PMID:33534698	PBO:0099998	(Figure 3 Figure supplement 2E,F and G)
PMID:33534698	FYPO:0006295	In the gnc2D iml1D tsc2D triple mutant, a trace of released GFP was detected only after 14 hr of nitrogen starvation (Figure 6C) while autophagy takes place within 2 hr in wild-type cells after the starvation (Figure 4B).
PMID:33534698	FYPO:0007803	Moreover, the autophagy defect of the gcn2D mutant was complemented by TORC1 inactivation by the TORC1 inhibitors, rapamycin and caffeine (Figure 5B).
PMID:33534698	PBO:0100006	In contrast, Psk1 remained phosphorylated even after the starvation in the gcn2D, eIF2a-S52A, and fil1D mutant strains (Figure 5A), suggesting that TORC1 inactivation in leucine-starved cells is mediated by the Gcn2-eIF2a-Fil1 pathway.
PMID:33534698	PBO:0100004	(comment: CONDITION Arginine starvation) Similarly, in cells of arginine auxotrophy, Gcn2-dependent autophagy was detectable after incubation in the growth medium without arginine (Figure 4—Figure supplement 1C).
PMID:33536395	PBO:0094648	The gmn2∆ cells were found to be viable despite growing slightly slower than the wild type (Fig. 3A MM (leu-)) and exhibited the same phenotypes as those of the original gmn2 mutant.
PMID:33536395	FYPO:0007800	In contrast, gmn2∆ cells missorted and secreted a significant amount of BiP to the cell surface. These results indicate that Gmn2p is required for normal retention of a luminal ER protein in S. pombe cells.
PMID:33536395	GO:0006890	(comment: changed from protein retention in ER lumen)
PMID:33536395	FYPO:0007800	In contrast, gmn2∆ cells missorted and secreted a significant amount of BiP to the cell surface. These results indicate that Gmn2p is required for normal retention of a luminal ER protein in S. pombe cells.
PMID:33536395	PBO:0106842	As expected, Och1-EGFP expressed in the wild type strain showed strong fluorescence as a typical Golgi-like dots, but faint fluorescent dots were confirmed in gmn2∆ cells (Fig. 4A).
PMID:33536395	GO:0005794	As expected, Och1-EGFP expressed in the wild type strain showed strong fluorescence as a typical Golgi-like dots, but faint fluorescent dots were confirmed in gmn2∆ cells (Fig. 4A).
PMID:33536395	FYPO:0007288	(Fig. 3C)
PMID:33536395	PBO:0106841	(Fig. 3B)
PMID:33536395	PBO:0095408	The gmn2∆ cells were highly sensitive to hygromycin B, being unable to grow on YES plates containing 25 μg/ml of the drug (Fig. 3A)
PMID:33536395	GO:0000139	The Gmn2-EGFP protein was recycled back into the ER just as Gms1-EGFP, indicating that Gmn2-EGFP localized mostly to the Golgi membranes (Fig. 6B).
PMID:33536434	PBO:0108653	(comment: GI Redundancy)
PMID:33568651	FYPO:0007681	Rnh201-RED mutant, based on the S. cerevsiae equivalent, is unable to remove single rNMPs from DNA but, buy genetic analysis, is able to remove runs of rNMPs.
PMID:33568651	FYPO:0007254	replication dynamic analysis demonstrates that the priming strand is stable in the absence of Ku (previous work has shown resection is increased behind the arrested fork). Replication restart is slightly delayed, confirming previous work. Assayed by polymerase usage sequencing
PMID:33574613	PBO:0105045	restores the MTREC and Rrp6 association with Mmi1 and Erh1 during meiosis (Fig. 5d).
PMID:33574613	FYPO:0003066	abnormal asci containing fewer than four, or no, spores were frequently generated (Fig. 7c).
PMID:33574613	FYPO:0000581	Defective chromosome segregation and reduced spore viability were also noted (Fig. 7a and Supplementary Videos 1-3)
PMID:33574613	FYPO:0004159	Defective chromosome segregation and reduced spore viability were also noted (Fig. 7a and Supplementary Videos 1-3)
PMID:33574613	FYPO:0004966	cells showed impaired oscillation of chromosomes and a prolonged horsetail stage (approximately 160min compared with approximately 120min; Fig. 7a,b).
PMID:33574613	PBO:0105051	Compared with the WT, cells expressing Pir1-SD showed a marked decrease in recombination frequency (Fig. 6f).
PMID:33574613	PBO:0105050	Compared with the WT, cells expressing Pir1-SD showed a marked decrease in recombination frequency (Fig. 6f).
PMID:33574613	PBO:0105049	Compared with the WT, cells expressing Pir1-SD showed a marked decrease in recombination frequency (Fig. 6f).
PMID:33574613	PBO:0105048	(Figure 6B) DSBs; for example, rec25, rec27 and mug20), which are critical for recombination and proper chromosome segregation during meiosis-I4
PMID:33574613	PBO:0105047	(Figure 6B) DSBs; for example, rec25, rec27 and mug20), which are critical for recombination and proper chromosome segregation during meiosis-I4
PMID:33574613	PBO:0105046	(Figure 6B) DSBs; for example, rec25, rec27 and mug20), which are critical for recombination and proper chromosome segregation during meiosis-I4
PMID:33574613	PBO:0105032	Moreover, loss of the ubiquitin ligase-associated Cullin-RING finger family protein Cul4, a component of ClrC35,36 that interacts with MTREC15, also stabilized Pir1 in both tor2-ts6 and nitrogen-starved cells (Fig. 3c
PMID:33574613	PBO:0105038	The addition of ubi4∆, cul4∆ or ddb1∆ dramatically reduced Pir1 ubiquitination in tor2-ts6 mts2-1 cells (Fig. 3f).
PMID:33574613	PBO:0105038	The addition of ubi4∆, cul4∆ or ddb1∆ dramatically reduced Pir1 ubiquitination in tor2-ts6 mts2-1 cells (Fig. 3f).
PMID:33574613	PBO:0105038	The addition of ubi4∆, cul4∆ or ddb1∆ dramatically reduced Pir1 ubiquitination in tor2-ts6 mts2-1 cells (Fig. 3f).
PMID:33574613	GO:0080008	(comment: which?)
PMID:33574613	GO:0080008	(comment: which?)
PMID:33574613	FYPO:0007226	the deletion of ubi4, ddb1 or cul4 restored ade6-DSR silencing (Fig. 3g and Extended Data Fig. 3d).
PMID:33574613	FYPO:0007226	the deletion of ubi4, ddb1 or cul4 restored ade6-DSR silencing (Fig. 3g and Extended Data Fig. 3d).
PMID:33574613	FYPO:0007226	the deletion of ubi4, ddb1 or cul4 restored ade6-DSR silencing (Fig. 3g and Extended Data Fig. 3d).
PMID:33574613	FYPO:0007212	The restoration of silencing required Pir1, as a loss of Ubi4 failed to silence ade6-DSR in pir1∆ cells (Fig. 3g).
PMID:33574613	FYPO:0007212	The restoration of silencing required Pir1, as a loss of Ubi4 failed to silence ade6-DSR in pir1∆ cells (Fig. 3g).
PMID:33574613	PBO:0105040	Remarkably, the loss of Ubi4, Cul4 or Ddb1 in tor2-ts6 cells restored the silencing of gametogenic genes genome-wide (Fig. 3h and Extended Data Fig. 3g).
PMID:33574613	PBO:0105032	Moreover, loss of the ubiquitin ligase-associated Cullin-RING finger family protein Cul4, a component of ClrC35,36 that interacts with MTREC15, also stabilized Pir1 in both tor2-ts6 and nitrogen-starved cells (Fig. 3c
PMID:33574613	PBO:0105039	ubi4 gene, which encodes polyubiquitin implicated in sexual development34, was upregulate in tor2-ts6 cells (Fig. 3a).
PMID:33574613	PBO:0095162	Interestingly, the expression of Pir1-SD in tor2-ts6 cells restored the levels of Red1 (Extended Data Fig. 2e), suggesting that the reduction in Red1 in the tor2 mutant cells (Fig. 1c) is linked to the degradation of its interaction partner Pir1
PMID:33574613	PBO:0105025	(Fig. 1b) (comment: CHECK me2)
PMID:33574613	PBO:0105026	(Fig. 1b) (comment: CHECK me2)
PMID:33574613	PBO:0105027	(Fig. 1b) (comment: CHECK (1.5x) (me2))
PMID:33574613	FYPO:0003235	Extended data Fig 1b, c (comment: also at MTREC independent islands)
PMID:33574613	PBO:0105028	(Figure 1c)
PMID:33574613	PBO:0105029	(Figure 1e)
PMID:33574613	PBO:0105030	(Fig. 1a)
PMID:33574613	PBO:0105031	(Fig. 1a)
PMID:33574613	PBO:0105038	Consistently, ubiquitination of Pir1-SD in the tor2-ts6 mts2-1 mutant was reduced (Fig. 2e).
PMID:33574613	PBO:0105032	Replacement of the 12 phospho-serine residues with the phospho-mimic aspartic acid residue (Pir1-12SD) indeed conferred stability in tor2-ts6 cells (Extended Data Fig. 2d); Deletion of ubi4 in tor2-ts6 cells cells indeed stabilized Pir1 (Fig. 3b)
PMID:33574613	PBO:0105032	Replacement of the 12 phospho-serine residues with the phospho-mimic aspartic acid residue (Pir1-12SD) indeed conferred stability in tor2-ts6 cells (Extended Data Fig. 2d)
PMID:33574613	FYPO:0002033	Extended Data Fig. 2a, c
PMID:33574613	PBO:0116820	he Tor2-containing TORC1 complex phosphorylated Pir1 in vitro and mutation of the 12 serine residues to alanine attenuated Pir1 phosphorylation (Extended Data Fig. 2a,c).
PMID:33574613	PBO:0105031	(Fig. 1a)
PMID:33574613	PBO:0105030	(Fig. 1a)
PMID:33574613	PBO:0105041	Remarkably, the loss of Ubi4, Cul4 or Ddb1 in tor2-ts6 cells restored the silencing of gametogenic genes genome-wide (Fig. 3h and Extended Data Fig. 3g).
PMID:33574613	PBO:0105042	Remarkably, the loss of Ubi4, Cul4 or Ddb1 in tor2-ts6 cells restored the silencing of gametogenic genes genome-wide (Fig. 3h and Extended Data Fig. 3g). and Fig. 4g).
PMID:33574613	PBO:0105043	Remarkably, the loss of Ubi4, Cul4 or Ddb1 in tor2-ts6 cells restored the silencing of gametogenic genes genome-wide (Fig. 3h and Extended Data Fig. 3g). and Fig. 4g).
PMID:33574613	PBO:0105040	Remarkably, the loss of Ubi4, Cul4 or Ddb1 in tor2-ts6 cells restored the silencing of gametogenic genes genome-wide (Fig. 3h and Extended Data Fig. 3g).
PMID:33574613	PBO:0105041	Remarkably, the loss of Ubi4, Cul4 or Ddb1 in tor2-ts6 cells restored the silencing of gametogenic genes genome-wide (Fig. 3h and Extended Data Fig. 3g).
PMID:33574613	FYPO:0007685	Intriguingly, cells expressing Pir1-SD, but not Pir1-WT or Pir1-SA, continued to divide on nutrient-limiting medium at a low temperature (Fig. 4a), suggesting that stabilized Pir1 supports cell proliferation under suboptimal growth conditions.
PMID:33574613	FYPO:0001355	We indeed observed that pir1∆ cells exhibited a growth defect on minimal medium
PMID:33574613	PBO:0105033	Moreover, ubiquitination of Pir1 was detected in tor2-ts6 cells and increased in the tor2-ts6 mts2-1 mutant (Fig. 1h)
PMID:33574613	MOD:01148	(Figure 1h)
PMID:33574613	PBO:0105032	(Fig. 1f, g)
PMID:33574613	FYPO:0001357	We indeed observed that pir1∆ cells exhibited a growth defect on minimal medium
PMID:33574613	PBO:0093560	Similar to pir1∆, tor2-ts6 cells showed a severe growth defect at a semi-permissive temperature (29°C) on minimal medium but not on rich medium (Fig. 4d).
PMID:33574613	FYPO:0001357	Similar to pir1∆, tor2-ts6 cells showed a severe growth defect at a semi-permissive temperature (29°C) on minimal medium but not on rich medium (Fig. 4d).
PMID:33574613	PBO:0092302	Notably, Pir1 was depleted during early meiosis (Fig. 5a) but gradually recovered by middle meiosis.
PMID:33574613	FYPO:0007686	Whereas Pir1-WT disappeared, Pir1-SD persisted during meiosis as multiple nuclear foci coinciding with Mmi1 and Erh1 foci (Fig. 5b,c).
PMID:33574613	PBO:0105044	restores the MTREC and Rrp6 association with Mmi1 and Erh1 during meiosis (Fig. 5d).
PMID:33579781	PBO:0096579	(Fig. 4A)
PMID:33579781	PBO:0096580	(Fig. 4A)
PMID:33579781	PBO:0096580	(Fig. 4A)
PMID:33579781	PBO:0096581	(Fig. 4A)
PMID:33579781	PBO:0096582	(Fig. 4A)
PMID:33579781	PBO:0094738	(Fig. 5B)
PMID:33579781	PBO:0094738	(Fig. 5B)
PMID:33579781	FYPO:0001355	(Fig. 5A)
PMID:33579781	PBO:0096583	(Fig. 4A)
PMID:33579781	PBO:0094773	(Fig. 4A)
PMID:33579781	PBO:0096584	(Fig. 4A)
PMID:33579781	FYPO:0000080	(Fig. 2)
PMID:33579781	PBO:0094771	(Fig. 5B)
PMID:33579781	PBO:0094771	(Fig. 5B)
PMID:33579781	PBO:0094771	(Fig. 5B)
PMID:33579781	PBO:0094771	(Fig. 5B)
PMID:33579781	PBO:0096575	(Fig. 4A)
PMID:33579781	FYPO:0000080	(Fig. 2) However, S. pombe is viable when Pro3 or Pro6 is changed to alanine in every other heptad, including the rump, in the context of the full-length CTD (Fig. 2), signifying that reduced proline content is tolerated and that Pro3 and Pro6 need not be present in consecutive heptads
PMID:33579781	PBO:0094771	(Fig. 5B)
PMID:33579781	PBO:0094771	(Fig. 5B)
PMID:33579781	PBO:0094771	(Fig. 5B)
PMID:33579781	PBO:0096585	(Fig. 4A)
PMID:33579781	PBO:0094771	(Fig. 5B)
PMID:33579781	PBO:0094771	(Fig. 5B)
PMID:33579781	PBO:0094771	(Fig. 5B)
PMID:33579781	PBO:0096576	(Fig. 4A)
PMID:33579781	FYPO:0002141	(Fig. 2) However, S. pombe is viable when Pro3 or Pro6 is changed to alanine in every other heptad, including the rump, in the context of the full-length CTD (Fig. 2), signifying that reduced proline content is tolerated and that Pro3 and Pro6 need not be present in consecutive heptads
PMID:33579781	GO:0006369	(comment: CHECK Need to add modified version)
PMID:33579781	PBO:0096577	(Fig. 4A)
PMID:33579781	PBO:0096578	(Fig. 4A)
PMID:33579781	PBO:0096576	(Fig. 4A)
PMID:33658433	PBO:0103648	(comment: vw:added nucleosome assembly)
PMID:33683349	FYPO:0000082	(comment: High temp - 30 degrees. (VW I changed this from a cell phenotype term to a population phenotype term) ) fig1 We interpret this suppression to indicate that the lethal mitoses, which occur in the smallest cells, require Cig2/CDK activity instead of, or in addition to, Cdc13/CDK activity.
PMID:33683349	PBO:0094645	(Fig. 3)
PMID:33683349	FYPO:0002516	(Fig. 5)
PMID:33683349	FYPO:0000400	(Fig. 5b) (comment: (I only curated the red line temp inc at tome zero, becase it would be difficult to specify at 60 mins, I could not think of a way to do this). I'm assuming these cells do not enter mitosis, is that correct)
PMID:33683349	PBO:0019154	(Fig. 6a)
PMID:33683349	PBO:0098712	(Figure 4)
PMID:33683349	PBO:0094949	(Figure 4)
PMID:33683349	PBO:0107206	"(Fig. 1, 2) (comment: Nick suggested ""mitotic catastrophe""We would make this a related synonym?)"
PMID:33683349	PBO:0094949	(Fig. 5a)
PMID:33683349	FYPO:0002060	(Figure 6b)
PMID:33683349	PBO:0095165	(Fig. 2) (comment: CONDITION 30 degrees) wee1-50ts mik1D cells divide at a smaller size than wee1-50ts mik1D cig2D cells
PMID:33683349	PBO:0019208	(Fig. 3) (comment: i.e wee?)
PMID:33683349	PBO:0037130	(Fig. 3)
PMID:33683349	PBO:0037130	(Fig. 3)
PMID:33711009	PBO:0102976	Neither the N-terminal segment from aa 1-496 nor the C-terminal fragment from 578-710 was able to bind to Dis2 or Swd22 in the 2-hybrid format (Fig 11A)
PMID:33711009	FYPO:0005369	(comment: CONDITION 20°)
PMID:33711009	FYPO:0005369	(comment: CONDITION 20°)
PMID:33711009	FYPO:0005369	(comment: CONDITION 20°)
PMID:33711009	FYPO:0005369	(comment: CONDITION 20°)
PMID:33711009	FYPO:0005369	(comment: CONDITION 20°)
PMID:33711009	PBO:0102977	Neither the N-terminal segment from aa 1-496 nor the C-terminal fragment from 578-710 was able to bind to Dis2 or Swd22 in the 2-hybrid format (Fig 11A)
PMID:33723569	FYPO:0002573	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0000085	(comment: CONDITION 32ºC)
PMID:33723569	FYPO:0000089	(comment: CONDITION 32ºC)
PMID:33723569	FYPO:0000088	(comment: CONDITION 32ºC)
PMID:33723569	FYPO:0000268	(comment: CONDITION 32ºC)
PMID:33723569	FYPO:0001355	(comment: CONDITION 32ºC)
PMID:33723569	PBO:0093616	(comment: CONDITION 32ºC)
PMID:33723569	PBO:0093629	(comment: CONDITION 32ºC)
PMID:33723569	FYPO:0000268	(comment: CONDITION 32ºC)
PMID:33723569	FYPO:0000089	(comment: CONDITION 32ºC)
PMID:33723569	FYPO:0004709	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0004516	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0004516	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0004516	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0004516	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007328	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007328	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007328	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0002573	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0002573	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007710	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0006687	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0002553	(comment: CONDITION 25ºC)
PMID:33723569	PBO:0093585	(comment: CONDITION 25ºC)
PMID:33723569	PBO:0093773	(comment: CONDITION 25ºC)
PMID:33723569	FYPO:0007711	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007711	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007710	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007710	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007710	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007710	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007711	(comment: live-cell imaging, 25ºC)
PMID:33723569	PBO:0093585	(comment: CONDITION 25ºC)
PMID:33723569	PBO:0093585	(comment: CONDITION 25ºC)
PMID:33723569	PBO:0093585	(comment: CONDITION 25ºC)
PMID:33723569	FYPO:0006686	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0006686	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0002573	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0000972	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007328	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0004516	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0006686	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0003503	(comment: 25ºC, live-cell imaging, cell length at septation)
PMID:33723569	FYPO:0004466	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0003503	(comment: 25ºC, live-cell imaging, cell length at septation)
PMID:33723569	FYPO:0003906	(comment: CONDITION 25ºC)
PMID:33723569	FYPO:0000972	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0002573	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0002601	(comment: CONDITION 25ºC)
PMID:33723569	PBO:0093585	(comment: CONDITION 25ºC)
PMID:33723569	FYPO:0006686	(comment: live-cell imaging, 25ºC)
PMID:33754639	FYPO:0002061	(comment: temperature sensitive 37°)
PMID:33771877	PBO:0099498	(Fig. 3)
PMID:33771877	PBO:0099497	(Fig. 3)
PMID:33771877	PBO:0099489	(Fig. 3) At exg1, ecm33, eng1 et gas1, condensin is redistributed throughout the gene body instead of accumulating around transcription termination sites.
PMID:33771877	PBO:0099488	(Fig. 3) At exg1, ecm33, eng1 et gas1, condensin is redistributed throughout the gene body instead of accumulating around transcription termination sites.
PMID:33771877	PBO:0099496	(Fig. 3)
PMID:33771877	PBO:0099486	(Fig. 3) At exg1, ecm33, eng1 et gas1, condensin is redistributed throughout the gene body instead of accumulating around transcription termination sites.
PMID:33771877	PBO:0099487	(Fig. 3) At exg1, ecm33, eng1 et gas1, condensin is redistributed throughout the gene body instead of accumulating around transcription termination sites.
PMID:33771877	PBO:0099490	(Fig. 2b) Importantly, the accumulation of condensin in sen1Δ cells could not be caused by an accumulation of either TFIIIC or Tbp1 because their levels on chromatin remained largely unaffected in the absence of Sen1, as shown by ChIP with a GFP-tagged version of Tbp1 and a myc-tagged version of the TFIIIC component Sfc6 (Figs 2B and S1).
PMID:33771877	PBO:0099495	(Fig. 3)
PMID:33771877	PBO:0099494	(Fig. 1)
PMID:33771877	FYPO:0007738	(Fig. 1)
PMID:33771877	PBO:0099493	(Fig. 2)
PMID:33771877	PBO:0099492	(Fig. 2)
PMID:33771877	PBO:0099491	(Fig. 2b)
PMID:33775921	FYPO:0001355	(comment: highest overexpression level)
PMID:33788833	PBO:0095512	The mutant protein is observed at the vacuolar surface
PMID:33788833	PBO:0095530	(comment: Affecting Cps1 carboxypeptidase)
PMID:33788833	PBO:0095526	(comment: Affecting Cps1 carboxypeptidase)
PMID:33788833	PBO:0095520	(comment: CHECK same as fsv1delta alone)
PMID:33788833	PBO:0095501	(comment: CONDITION 80 mM MgCl2)
PMID:33788833	PBO:0095502	(comment: Affecting Cps1 carboxypeptidase)
PMID:33788833	PBO:0095503	(comment: Affecting Cps1 carboxypeptidase)
PMID:33788833	PBO:0095504	(comment: CHECK Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE)
PMID:33788833	PBO:0095505	(comment: CHECK Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE)
PMID:33788833	PBO:0095513	The mutant protein is observed faintly at the vacuolar surface of a low percentage of cells
PMID:33788833	PBO:0095506	(comment: CHECK Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE)
PMID:33788833	PBO:0095512	The mutant protein is observed at the vacuolar surface
PMID:33788833	PBO:0095512	The mutant protein is observed at the vacuolar surface
PMID:33788833	PBO:0095512	The mutant protein is observed at the vacuolar surface
PMID:33788833	PBO:0095509	The mutant protein is observed at the vacuolar surface
PMID:33788833	PBO:0095510	The mutant protein is observed faintly at the vacuolar surface of a low percentage of cells
PMID:33788833	PBO:0095511	(comment: same as vps35delta alone)
PMID:33788833	PBO:0095511	(comment: same as vps35delta alone)
PMID:33788833	PBO:0095512	The mutant protein is observed at the vacuolar surface
PMID:33788833	PBO:0095513	The mutant protein is observed faintly at the vacuolar surface of a low percentage of cells
PMID:33788833	PBO:0095509	The mutant protein is observed at the vacuolar surface
PMID:33788833	PBO:0095509	The mutant protein is observed at the vacuolar surface
PMID:33788833	PBO:0095509	The mutant protein is observed at the vacuolar surface
PMID:33788833	PBO:0095509	The mutant protein is observed at the vacuolar surface
PMID:33788833	PBO:0095509	The mutant protein is observed at the vacuolar surface
PMID:33788833	PBO:0095509	The mutant protein is observed at the vacuolar surface
PMID:33788833	PBO:0095509	The mutant protein is observed at the vacuolar surface
PMID:33788833	PBO:0095510	The mutant protein is observed faintly at the vacuolar surface of a low percentage of cells
PMID:33788833	PBO:0095507	(comment: CHECK Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE)
PMID:33788833	PBO:0095512	The mutant protein is observed at the vacuolar surface
PMID:33788833	PBO:0095512	The mutant protein is observed at the vacuolar surface
PMID:33788833	PBO:0095512	The mutant protein is observed at the vacuolar surface
PMID:33788833	PBO:0095504	(comment: CHECK Affecting Vps10 and the PI(3) probe Cherry-FYVE)
PMID:33788833	PBO:0095503	(comment: Affecting Cps1 carboxypeptidase)
PMID:33788833	GO:0034058	In the null mutant and the mutant without SNARE domain the fluorescence of prevacuolar endosome markers is reduced, and Cps1 processing is abnormal
PMID:33788833	PBO:0095512	The mutant protein is observed at the vacuolar surface
PMID:33788833	GO:0031902	co-localization with Vps35 and with Vps27
PMID:33788833	GO:0005802	co-localization with Cfr1
PMID:33788833	PBO:0095529	(comment: Affecting Cps1 carboxypeptidase)
PMID:33788833	PBO:0093594	(comment: CONDITION 1.0 M KCl)
PMID:33823663	PBO:0104294	(Figure 9)
PMID:33823663	FYPO:0007963	DNS
PMID:33823663	PBO:0104295	(Figure 9) (comment: modified form is activated for sexual differentiation)
PMID:33823663	FYPO:0007963	DNS
PMID:33825974	FYPO:0004602	(Figure S2C)
PMID:33825974	PBO:0104155	(Figure 4d, 4e; Figure s3b)
PMID:33829153	FYPO:0001667	(Fig. 1A and B)
PMID:33836577	PBO:0019133	(Figure 3D)
PMID:33836577	GO:0005515	(Figure 2) (comment: requires phosphorylated T89, T154, T155 to bind Nbs1 FHA domain)
PMID:33836577	PBO:0100201	(Figure 2)
PMID:33836577	PBO:0093613	(Figure 3B)
PMID:33836577	PBO:0019133	(Figure 3D)
PMID:33836577	PBO:0100206	(Figure 2E)
PMID:33836577	PBO:0093613	(Figure 3B)
PMID:33836577	PBO:0093613	(Figure 3B)
PMID:33836577	PBO:0019133	(Figure 3D)
PMID:33836577	PBO:0093613	(Figure 3B)
PMID:33836577	PBO:0093613	(Figure 3C)
PMID:33836577	PBO:0093613	(Figure 3C)
PMID:33836577	PBO:0019133	(Figure 3D)
PMID:33836577	PBO:0100206	(Figure 2E)
PMID:33836577	PBO:0100202	We therefore introduced a synthetic CT15 peptide into an endonuclease assay containing the MR complex, but lacking Nbs1 (Fig. 4A). Strikingly, the CT15 peptide stimulated the endonuclease activity of MR similarly to the unphosphorylated, full-length Ctp1 (Fig. 4B). Moreover, stimulation of MR at higher concentrations of the CT15 peptide (100 μM) was comparable to the maximal levels achieved with the MRN complex and phosphorylated full-length Ctp1 (Ctp1p in Fig. 4C).
PMID:33836577	PBO:0100203	(Figure 1)
PMID:33836577	PBO:0100204	(Figure 1)
PMID:33836577	PBO:0100205	(Figure 1)
PMID:33836577	PBO:0100202	(Figure 2D)
PMID:33836577	GO:1990238	(Figure 2)
PMID:33836577	PBO:0093613	(Figure 3C)
PMID:33836577	PBO:0093613	(Figure 3B)
PMID:33836577	PBO:0093613	(Figure 3C)
PMID:33836577	PBO:0019133	(Figure 3D)
PMID:33836577	PBO:0100206	(Figure 2D)
PMID:33836577	PBO:0093613	(Figure 3C)
PMID:33836577	PBO:0019133	(Figure 3D)
PMID:33888556	PBO:0109331	refer to model in Figure 4. Therefore, consistent with the genetic analyses, this biochemical analysis supports the notion that phosphorylation at Rec8-S450 and the adjacent site plays a role in promoting the PP2A-dependent removal of CK1-dependent phosphorylation of Rec8 (Fig. 4B).
PMID:33888556	PBO:0107039	(Figure 4)
PMID:33888556	PBO:0107033	(Figure 4) (comment: no rescue by sgo3)
PMID:33888556	PBO:0109333	To further examine this possibility, we reconstituted Rec8 dephosphorylation in vitro using immunoprecipitated Par1-containing PP2A complexes.
PMID:33888556	PBO:0109332	To further examine this possibility, we reconstituted Rec8 dephosphorylation in vitro using immunoprecipitated Par1-containing PP2A complexes.
PMID:33888556	FYPO:0002061	(Figure 3D) (comment: phosphomimetic rec8)
PMID:33888556	FYPO:0002060	(Figure 3D)
PMID:33888556	FYPO:0002060	(Figure 3D)
PMID:33888556	FYPO:0002061	(Figure 3D) (comment: phosphomimetic rec8)
PMID:33888556	FYPO:0002219	(Figure 2F)
PMID:33888556	FYPO:0006426	(Figure 2A)
PMID:33888556	PBO:0109716	(Figure 1C)
PMID:33888556	PBO:0109715	(Figure 1C)
PMID:33888556	FYPO:0006425	(Figure 1C)
PMID:33888556	FYPO:0006425	(Figure 1C)
PMID:33888556	FYPO:0005633	(Figure 1C)
PMID:33888556	FYPO:0002219	(Figure 3BC) Strikingly, the phenotype of rec8-2E was completely suppressed by sgo1Δ indicating that Rec8-2E was protected by Sgo1 not only at centromeres but also along the chromosome arm.
PMID:33888556	PBO:0107033	(Figure 4)
PMID:33888556	FYPO:0007759	(Figure 3)
PMID:33888556	FYPO:0007760	(Figure 3AB) vw repurposed this as it was essentially the same as the other annotation to this genotype (suggesting that Rec8-2A was properly expressed but not protected at centromeres during anaphase I.)
PMID:33888556	PBO:0107031	(Figure 2D)
PMID:33888556	PBO:0107030	(Figure 2A) (comment: cohesion protection defect)
PMID:33888556	PBO:0107029	(comment: we modelled this increased duration of cohesion in mitotic anaphase, and the ectopic rec8 expression is now part of the genotype,does that sound OK?)
PMID:33888556	PBO:0109714	(Figure 1B,C)
PMID:33888556	FYPO:0006424	(Figure 1C)
PMID:33909078	PBO:0105746	(comment: alpha-1,3-galactosylation of O-linked glycan)
PMID:33909078	PBO:0097092	(comment: alpha-1,2-galactosylation of O-linked glycan)
PMID:33909078	PBO:0097089	(comment: alpha-1,2-galactosylation of N-linked glycan)
PMID:33909078	PBO:0097089	(comment: alpha-1,2-galactosylation of N-linked glycan)
PMID:33909078	PBO:0097089	(comment: alpha-1,2-galactosylation of N-linked glycan)
PMID:33909078	PBO:0097092	(comment: alpha-1,2-galactosylation of O-linked glycan)
PMID:33909078	PBO:0105746	(comment: alpha-1,3-galactosylation of O-linked glycan)
PMID:33909078	PBO:0105746	(comment: alpha-1,3-galactosylation of O-linked glycan)
PMID:33925026	FYPO:0005703	(comment: CHECK same as alp14delta alone)
PMID:33925026	FYPO:0005681	(comment: CHECK same as alp14delta alone)
PMID:33925026	FYPO:0005682	(comment: CHECK same as alp14delta alone)
PMID:33925026	PBO:0097255	(comment: CHECK Assays were done in the MDR-sup (multi-drug resistance-suppressed) genetic background together with nda3-TB101)
PMID:33925026	PBO:0097256	(comment: CHECK reduced frequency of microtubule catastrophe)
PMID:33925026	PBO:0097257	(comment: CHECK reduced frequency of microtubule rescue)
PMID:33925026	FYPO:0001355	(comment: CHECK same as alp14delta alone)
PMID:33925026	FYPO:0000903	(comment: CHECK same as alp14delta alone)
PMID:33925026	FYPO:0005681	(comment: CHECK same as klp6delta alone)
PMID:33925026	FYPO:0005682	(comment: CHECK same as klp6delta alone)
PMID:33946513	PBO:0107007	(comment: CHECK to pac)
PMID:33946513	PBO:0107004	(Figure 2D)
PMID:33946513	PBO:0107001	(Figure 2A,B)
PMID:33946513	FYPO:0002060	(Fig. 1a)
PMID:33946513	FYPO:0002060	(Fig. 1c) (comment: CHECK dri1 supresses cut7)
PMID:33946513	FYPO:0002626	(Figure 6) We found that the dri1∆ cells acquired tolerance to high temperature, as they could form colonies at 39 ◦C, whereas wild-type cells could not (Figure 6C).
PMID:33946513	PBO:0107005	(comment: CHECK SHOULD THIS BE NORMAL?) However, the Mal3 protein levels did not change in the presence or absence of Dri1 (Supplementary Figure S3A). Similarly, the levels of Mal3-GFP on the spindle MTs were almost the same both in wild-type and dri1∆ cells (Supplementary Figure S3B).
PMID:33946513	PBO:0107006	(Fig. S4a)
PMID:33946513	PBO:0107007	(comment: CHECK to pac)
PMID:33946513	PBO:0107004	(Figure 2D)
PMID:33946513	PBO:0107002	Klp2 levels on spindle microtubules were significantly lower than those in cut7-22 (which are increased compared to WT)
PMID:33946513	PBO:0107001	(Figure 2A,B)
PMID:33946513	FYPO:0002060	(Fig. 1)
PMID:33946513	PBO:0107008	(comment: CHECK to pac)
PMID:33946513	PBO:0018470	(Figure 3A)
PMID:33946513	PBO:0023225	(Figure 3A)
PMID:33946513	GO:0005634	(Figure 3A)
PMID:33946513	PBO:0097109	(Figure 4a)
PMID:33946513	PBO:0107002	Klp2 levels on spindle microtubules were significantly lower than those in cut7-22 (which are increased compared to WT)
PMID:33946513	PBO:0107008	(comment: CHECK to pac)
PMID:33970532	FYPO:0007792	(comment: only amino acid auxotrophic cell)
PMID:33970532	PBO:0094358	(comment: only amino acid auxotrophic cell)
PMID:33970532	FYPO:0007792	(comment: only amino acid auxotrophic cell)
PMID:33970532	FYPO:0007791	The control strain ED668 expressed ecl1+ when Mg2+ was depleted but not in a strain lacking fil1+ (Figure 2a)
PMID:33970532	PBO:0094360	(comment: to capture target of ecl1)
PMID:34010645	FYPO:0007597	(Figure 2)
PMID:34010645	FYPO:0007597	(Figure 2)
PMID:34010645	FYPO:0007597	(Figure 2)
PMID:34010645	PBO:0095076	H3K9me3 levels at pericentric dh repeats and dh RNA levels in hht3-K9MK14R cells are similar to those in wild-type cells, comparing with hht3-K9M.
PMID:34019809	FYPO:0007841	(comment: CHECK fix catalytic activity)
PMID:34019809	GO:0000822	(Fig. 2)
PMID:34019809	FYPO:0007841	(comment: CHECK fix catalytic activity)
PMID:34028542	PBO:0092254	(Fig. 5)
PMID:34028542	PBO:0099303	Cytoplasmic Ght5-GFP was observed within the vacuolar membrane stained with FM4-64.
PMID:34028542	PBO:0099304	(Fig. 1) (comment: aly3 rescues)
PMID:34028542	PBO:0099302	top panel, Fig. 6A; Fig. S3B,C).
PMID:34028542	PBO:0114539	(comment: although not shown directly , genetic interactions are consistent with this activity)
PMID:34028542	PBO:0099308	(Fig. 6) (comment: phenocopies WT)
PMID:34028542	PBO:0099307	(Fig. 6)
PMID:34028542	PBO:0099307	(Fig. 6)
PMID:34028542	FYPO:0000047	Proliferation defect of gad8ts mutant in low glucose was restored by SPCC584.15c deletion.
PMID:34028542	FYPO:0003743	Proliferation defect of gad8ts rod1 mutant in low glucose was similar to that of gad8ts mutant.
PMID:34028542	FYPO:0003743	Proliferation defect of gad8ts aly2 mutant in low glucose was similar to that of gad8ts mutant.
PMID:34028542	FYPO:0003743	Proliferation defect of gad8ts aly1 mutant in low glucose was similar to that of gad8ts mutant.
PMID:34028542	PBO:0092077	After cultivation in low glucose MM for 10 h, medium was replaced with low-glucose nitrogen-starved MM, and cells were further cultivated for 4 h.
PMID:34067465	PBO:0092385	(Fig. 1C)
PMID:34067465	PBO:0092176	(Fig. 1C)
PMID:34067465	PBO:0092319	(Fig. 1C)
PMID:34067465	FYPO:0008313	(Fig. 8)
PMID:34067465	PBO:0114710	(Fig. 4 and Fig. S2)
PMID:34067465	PBO:0114711	In some nuclei, a diffuse pan-nuclear signal was also detected. (Fig. 5)
PMID:34067465	GO:0035974	These data indicate that the localization of the Crs1-GFP cyclin during meiosis is similar to that of a SPB component. (Fig. 5)
PMID:34067465	FYPO:0002043	(Fig. 4 and Fig. S2)
PMID:34067465	PBO:0114709	(Fig. 4 and Fig. S2)
PMID:34067465	PBO:0114710	(Fig. 4 and Fig. S2)
PMID:34067465	PBO:0114712	(Fig. 7, Fig. S4 and Fig. S5)
PMID:34067465	PBO:0102134	(Fig. 7, Fig. S4 and Fig. S5)
PMID:34067465	FYPO:0008314	(Fig. 8)
PMID:34067465	PBO:0114713	(Fig. S6)
PMID:34080538	FYPO:0005706	(Fig. 4)
PMID:34080538	PBO:0109507	(Fig. 5)
PMID:34080538	PBO:0109507	(Fig. 5)
PMID:34080538	PBO:0109507	(Fig. 5)
PMID:34080538	PBO:0109507	(Fig. 5)
PMID:34080538	PBO:0109508	(Fig. 5 Supp 3)
PMID:34080538	PBO:0109507	(Fig. 5 Supp 3)
PMID:34080538	FYPO:0007304	(Fig. 4)
PMID:34080538	FYPO:0005343	(Fig. 4)
PMID:34080538	PBO:0109504	(Fig. 4)
PMID:34080538	PBO:0097991	(Fig. 5) (comment: Phosph form) ((comment: From other publications, we know bona-fide that the localisation observed here is the kinetochore but here they study how it changes)
PMID:34080538	PBO:0109503	(Fig. 5) (comment: Dephosph form)
PMID:34080538	PBO:0109502	(Fig. 5) (comment: Dephosph form)
PMID:34080538	PBO:0109501	(Fig. 4)
PMID:34080538	PBO:0109500	(Fig. 4)
PMID:34080538	PBO:0022963	(Fig. 4)
PMID:34080538	FYPO:0007304	(Fig. 4)
PMID:34080538	FYPO:0007304	(Fig. 4)
PMID:34080538	FYPO:0005706	(Fig. 4)
PMID:34080538	FYPO:0005343	(Fig. 4)
PMID:34080538	PBO:0109499	(Fig. 4)
PMID:34080538	FYPO:0005706	(Fig. 4)
PMID:34080538	FYPO:0005343	(Fig. 4)
PMID:34086083	GO:0005737	(comment: CHECK YES, YES (low-glucose))
PMID:34086083	PBO:0108842	(comment: ALERTED FROM A LATER PAPER) Rst2 regulates the expression of ste11, which encodes a transcription factor to regulate sexual development (Sugimoto et al. 1991); fbp1, which encodes fructose-1,6-bisphosphatase (Hoffman and Winston 1990); and mug14, which encodes an adducin homolog (Inamura et al. 2021).
PMID:34086083	GO:0005634	(comment: CHECK YES, YES (low-glucose))
PMID:34119521	PBO:0114828	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	PBO:0114825	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	PBO:0114826	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	FYPO:0008316	We consistently found that disruption of ppr10, mpa1, or the PPR motifs of Ppr10 resulted in dissociation of Mti2 and Mti3 from the mt-SSU (Fig. 2, B-D).
PMID:34119521	PBO:0114769	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	PBO:0114827	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	PBO:0114828	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	PBO:0114770	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	PBO:0114830	The association of cob1 and cox1 mRNAs with assembled mitoribosomes was reduced by ppr10 deletion, whereas their association with the mt-SSU was increased (Fig. 3).
PMID:34119521	PBO:0114831	The PPR motifs of Ppr10 are not involved in the association of Ppr10 with a subset of mitoribosomal proteins
PMID:34119521	GO:0070124	Taken together, these data reveal that the PPR motifs in Ppr10 are critical for the Ppr10-Mpa1 interaction and that disruption of the PPR motifs in Ppr10 impairs mitochondrial protein synthesis and, consequently, respiratory growth of S. pombe cells.
PMID:34119521	FYPO:0008315	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) a
PMID:34119521	FYPO:0008316	We consistently found that disruption of ppr10, mpa1, or the PPR motifs of Ppr10 resulted in dissociation of Mti2 and Mti3 from the mt-SSU (Fig. 2, B-D).
PMID:34119521	FYPO:0008316	We consistently found that disruption of ppr10, mpa1, or the PPR motifs of Ppr10 resulted in dissociation of Mti2 and Mti3 from the mt-SSU (Fig. 2, B-D).
PMID:34119521	FYPO:0000562	Deletion of the PPR motifs in Ppr10 moderately affected the growth of S. pombe cells on glucose-containing media but severely impaired the growth on glycerol-containing media (Fig. 1E)
PMID:34119521	FYPO:0000705	The level of Ppr10ΔPPR-Myc is reduced compared with that of WT protein (Fig. 1B). We found that only the full-length Ppr10-Myc coimmunoprecipitated with Mpa1 from whole-cell extract, whereas the mutant Ppr10 did not (Fig. 1C).
PMID:34119521	PBO:0114789	deletion of PPR motifs in Ppr10 severely reduced the steady-state levels of Cob1 (subunit of the cytochrome bc 1 complex), the core subunits of cytochrome c oxidase (Cox1, Cox2, Cox3), and Atp6 (subunit of ATP synthase) (Fig. 1D).
PMID:34119521	PBO:0114794	deletion of PPR motifs in Ppr10 severely reduced the steady-state levels of Cob1 (subunit of the cytochrome bc 1 complex), the core subunits of cytochrome c oxidase (Cox1, Cox2, Cox3), and Atp6 (subunit of ATP synthase) (Fig. 1D).
PMID:34119521	PBO:0114791	deletion of PPR motifs in Ppr10 severely reduced the steady-state levels of Cob1 (subunit of the cytochrome bc 1 complex), the core subunits of cytochrome c oxidase (Cox1, Cox2, Cox3), and Atp6 (subunit of ATP synthase) (Fig. 1D).
PMID:34119521	PBO:0114792	deletion of PPR motifs in Ppr10 severely reduced the steady-state levels of Cob1 (subunit of the cytochrome bc 1 complex), the core subunits of cytochrome c oxidase (Cox1, Cox2, Cox3), and Atp6 (subunit of ATP synthase) (Fig. 1D).
PMID:34119521	PBO:0114793	deletion of PPR motifs in Ppr10 severely reduced the steady-state levels of Cob1 (subunit of the cytochrome bc 1 complex), the core subunits of cytochrome c oxidase (Cox1, Cox2, Cox3), and Atp6 (subunit of ATP synthase) (Fig. 1D).
PMID:34119521	PBO:0114823	We consistently found that disruption of ppr10, mpa1, or the PPR motifs of Ppr10 resulted in dissociation of Mti2 and Mti3 from the mt-SSU and reduced the association of Mti2 and Mti3 with mitoribosomes (Fig. 2, B-D).
PMID:34119521	PBO:0114824	We consistently found that disruption of ppr10, mpa1, or the PPR motifs of Ppr10 resulted in dissociation of Mti2 and Mti3 from the mt-SSU and reduced the association of Mti2 and Mti3 with mitoribosomes (Fig. 2, B-D).
PMID:34119521	PBO:0114823	We consistently found that disruption of ppr10, mpa1, or the PPR motifs of Ppr10 resulted in dissociation of Mti2 and Mti3 from the mt-SSU and reduced the association of Mti2 and Mti3 with mitoribosomes (Fig. 2, B-D).
PMID:34119521	PBO:0114824	We consistently found that disruption of ppr10, mpa1, or the PPR motifs of Ppr10 resulted in dissociation of Mti2 and Mti3 from the mt-SSU and reduced the association of Mti2 and Mti3 with mitoribosomes (Fig. 2, B-D).
PMID:34119521	PBO:0114823	We consistently found that disruption of ppr10, mpa1, or the PPR motifs of Ppr10 resulted in dissociation of Mti2 and Mti3 from the mt-SSU and reduced the association of Mti2 and Mti3 with mitoribosomes (Fig. 2, B-D).
PMID:34119521	PBO:0114824	We consistently found that disruption of ppr10, mpa1, or the PPR motifs of Ppr10 resulted in dissociation of Mti2 and Mti3 from the mt-SSU and reduced the association of Mti2 and Mti3 with mitoribosomes (Fig. 2, B-D).
PMID:34119521	PBO:0114825	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	PBO:0114826	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	PBO:0114829	The association of cob1 and cox1 mRNAs with assembled mitoribosomes was reduced by ppr10 deletion, whereas their association with the mt-SSU was increased (Fig. 3).
PMID:34119521	PBO:0114769	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	PBO:0114827	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34133210	PBO:0106246	(comment: although not IDA, there is experimental data to support this inference)
PMID:34133210	PBO:0106244	Cdk1 phosphorylation of Pxl1 reduced binding to the F-BAR domain of Cdc15 (Figure 5A), but not to Cdc15C (Figure 5B).
PMID:34133210	FYPO:0005543	Constriction took longer in pxl1(9A)
PMID:34133210	FYPO:0007828	Although there was a small difference in CR formation between pxl1(9A) (13.6 +/- 2.5; 33 cells) and pxl1(9D) (12.2 +/- 2.3 min; 41 cells), formation was similar in pxl1(9D) and pxl1+ (12.4 +/- 3.0; 32 cells), and there were no significant differences in the durations of CR maturation.
PMID:34133210	FYPO:0001368	Although there was a small difference in CR formation between pxl1(9A) (13.6 +/- 2.5; 33 cells) and pxl1(9D) (12.2 +/- 2.3 min; 41 cells), formation was similar in pxl1(9D) and pxl1+ (12.4 +/- 3.0; 32 cells), and there were no significant differences in the durations of CR maturation.
PMID:34133210	PBO:0092467	(Fig. 1)
PMID:34133210	FYPO:0007829	(Figure 4, A and B)
PMID:34147496	GO:0006799	inferred from polyphosphate absent from cell
PMID:34147496	PBO:0112697	These results imply that: (1) Pho84 is multiply ubiquitinated; (2) ubiquitination of Pho84 depends mainly on Pqr1.
PMID:34169534	PBO:0107987	(comment: also assayed using Pil1 co-tethering with microscopy)
PMID:34169534	PBO:0107986	(comment: also assayed using Pil1 co-tethering with microscopy)
PMID:34198697	PBO:0113578	(Figure 1a)
PMID:34198697	FYPO:0007521	(Figure 1B) (comment: This phenotype is known as “VIC” viable in the presence of immunosuppressant and chloride ion)
PMID:34198697	PBO:0113580	(comment: Cell wall damage induced with caspofungin)
PMID:34198697	FYPO:0000079	(Figure 1B)
PMID:34198697	FYPO:0005969	(Figure 1B)
PMID:34209806	PBO:0100508	The interactions of the Nrl1(NRDE-2) and the Nrl1(C-term) domain constructs with Mtl1 were significantly lower
PMID:34209806	GO:0005681	(comment: Need to curate ref42 for earlier part of this story, but this can be. inferred here from the interactions)
PMID:34209806	PBO:0100507	We observed similar intensities of interaction of the Nrl1(N-term) and the Nrl1(N-term + NRDE-2) constructs with Mtl1 (1511.2 ± 89.4 or 1558.2 ± 159.3 Miller units for the N-terminal region and the N-terminus with NRDE2 domain and Mtl1, respectively)
PMID:34209806	PBO:0100507	We observed similar intensities of interaction of the Nrl1(N-term) and the Nrl1(N-term + NRDE-2) constructs with Mtl1 (1511.2 ± 89.4 or 1558.2 ± 159.3 Miller units for the N-terminal region and the N-terminus with NRDE2 domain and Mtl1, respectively)
PMID:34228709	PBO:0095859	(comment: hypermutator)
PMID:34228709	FYPO:0000173	(comment: CHECK Cds1 is partially phosphorylated)
PMID:34228709	FYPO:0001707	(comment: CHECK Chk1 is partially phosphorylated)
PMID:34228709	FYPO:0003923	DNA combing
PMID:34228709	FYPO:0005032	(comment: equivalent substitution to cdc20-P287R)
PMID:34250083	FYPO:0000245	(comment: Phenotype determined with robotics-based CFU assay.)
PMID:34250083	FYPO:0000245	(comment: Phenotype determined with robotics-based CFU assay.)
PMID:34250083	FYPO:0001309	(comment: Phenotype determined with robotics-based CFU assay.)
PMID:34250083	FYPO:0001309	(comment: Phenotype determined with robotics-based CFU assay.)
PMID:34250083	FYPO:0001309	(comment: Phenotype determined with robotics-based CFU assay.)
PMID:34250083	FYPO:0000245	(comment: Phenotype determined with robotics-based CFU assay.)
PMID:34250083	FYPO:0000245	(comment: Phenotype determined with robotics-based CFU assay.)
PMID:3428262	FYPO:0003095	(comment: CHECK mitotic G2/M transition delay)
PMID:34292936	PBO:0096842	(comment: worse than rad51delta alone)
PMID:34292936	PBO:0096842	(comment: worse than rad51delta alone)
PMID:34296454	PBO:0104158	(Fig. 5E, 5F) from paper for partial inhibition protein synthesis phenotype
PMID:34296454	GO:2000767	hese observations are consistent with the idea that the essential TORC1 is the major complex responsible for the rapid inhibition of protein synthesis and that changes in phosphorylation levels relevant to regulating protein synthesis should be detectable within 20 min and significant by 40 min of TOR inhibition.
PMID:34296454	PBO:0104159	For the Torin1-resistant mutant, the phosphorylation levels remained constant throughout the time course
PMID:34296454	FYPO:0007877	This result indicates that the immediate decrease in protein synthesis rates upon TOR inhibition is not dependent upon the S6Ks or their downstream targets.
PMID:34296454	PBO:0104159	For the Torin1-resistant mutant, the phosphorylation levels remained constant throughout the time course
PMID:34309513	GO:0140588	(comment: CHECK in vitro) (Figure 4A, Video 1).
PMID:34309513	GO:0140588	(comment: CHECK in vitro) (Figure 4A, Video 1).
PMID:34309513	GO:0140588	(comment: CHECK in vitro) (Figure 4A, Video 1).
PMID:34309513	GO:0140588	(comment: CHECK in vitro) (Figure 4A, Video 1).
PMID:34309513	GO:0140588	(comment: CHECK in vitro) (Figure 4A, Video 1).
PMID:34309513	GO:0140588	(comment: CHECK in vitro) (Figure 4A, Video 1).
PMID:34346498	PBO:0099607	(Figure 1)
PMID:34346498	FYPO:0007864	(Figure 5) To confirm this, we evaluatedthe behaviour of bqt1Δ sad1.2 alp4-GFP cells harbouring the SPBmarkers Sid4-mCherry and Sad1.2-mCherry, effectively showingthat Alp4-GFP molecules located far from the nucleus wereassociated with the SPBs (Fig. 5C,D)
PMID:34346498	FYPO:0007849	(Figure 2F)
PMID:34346498	PBO:0099602	(Figure 3A)
PMID:34346498	PBO:0022389	(Figure 2)
PMID:34346498	PBO:0099601	(comment: CHECK decreased abnormal SPB-independent meiosis II)
PMID:34346498	PBO:0099600	(Figure 7C)
PMID:34346498	PBO:0099592	(comment: late spindle elongation (move down /when GO reflect stages of meiotic spindle elongation))
PMID:34346498	PBO:0099595	(Figure 7)
PMID:34346498	FYPO:0003614	(Figure 6B)
PMID:34346498	FYPO:0007755	(Figure 2F)
PMID:34346498	PBO:0099598	(Figure 6) Remarkably, we found that, in the case of bqt1Δ sad1.2 alp14-26 meiocytes, despite clear dysfunction of alp14-26, self-assembled spindles were still able to form and behaved normally (Fig. 6C,D). However, they formed in a smaller percentage of meiocytes (from ∼80% to ∼30%, Fig. 6F), indicating that the contribution of Alp14 to self-assembled spindle formation and behaviour is substantial.
PMID:34346498	FYPO:0007849	analysis of bqt1Δ sad1.2 dis1Δ meiocytes showed that the percentage of selfassembled spindles with normal formation and function was similar to that in the bqt1Δ sad1.2 setting (Fig. 6F,H).
PMID:34346498	PBO:0099599	(Figure 7) maximum length of self-assembled spindles increased upon deletion of klp6 (from 7.9±3.8 μm to 12.9±4.7 μm; Fig. 7E).
PMID:34346498	PBO:0099596	(Figure 7)
PMID:34346498	PBO:0099614	(Figure 7C)
PMID:34346498	PBO:0099616	(Figure 7C)
PMID:34346498	FYPO:0007846	(Figure 2F)
PMID:34346498	PBO:0099613	(Figure 5) To confirm this, we evaluatedthe behaviour of bqt1Δ sad1.2 alp4-GFP cells harbouring the SPBmarkers Sid4-mCherry and Sad1.2-mCherry, effectively showingthat Alp4-GFP molecules located far from the nucleus wereassociated with the SPBs (Fig. 5C,D)
PMID:34346498	PBO:0099612	(Figure 7) maximum length of self-assembled spindles increased upon deletion of klp6 (from 7.9±3.8 μm to 12.9±4.7 μm; Fig. 7E).
PMID:34346498	FYPO:0007852	(Figure 3)
PMID:34346498	PBO:0099611	(Figure 2E)
PMID:34346498	PBO:0099610	(Figure 2E)
PMID:34346498	PBO:0099609	(Figure 1) (comment: see above)
PMID:34346498	PBO:0099608	(Figure 1) (comment: see above)
PMID:34349749	FYPO:0005947	Nonetheless, we compared the growth of trk1delta and trk2delta with that of cfr1delta in the presence of high K+ concentrations. Additionally, we constructed double and triple mutants to determine whether cfr1+ acts in the same functional pathways as trk1+ and/or trk2+. The results showed that while cfr11 was sensitive to potassium salts, neither trk11, trk21 nor trk11 trk21 (denoted by trk11 in the figure) exhibited sensitivity (Figure 2A).
PMID:34349749	FYPO:0005947	Nonetheless, we compared the growth of trk1delta and trk2delta with that of cfr1delta in the presence of high K+ concentrations. Additionally, we constructed double and triple mutants to determine whether cfr1+ acts in the same functional pathways as trk1+ and/or trk2+. The results showed that while cfr1delta was sensitive to potassium salts, neither trk1delta, trk2delta nor trk1delta trk2delta exhibited sensitivity (Figure 2A).
PMID:34349749	PBO:0093595	We also analyzed the relationship between exomer and the calcium channels Cch1 and Yam8 (Ma et al., 2011). cch1delta was sensitive to low KCl concentrations, and both cch1delta cfr1delta and yam8delta cfr1delta were more sensitive than any of the single mutants.
PMID:34349749	PBO:0093595	We also analyzed the relationship between exomer and the calcium channels Cch1 and Yam8 (Ma et al., 2011). cch1delta was sensitive to low KCl concentrations, and both cch1delta cfr1delta and yam8delta cfr1delta were more sensitive than any of the single mutants.
PMID:34349749	PBO:0093595	We also analyzed the relationship between exomer and the calcium channels Cch1 and Yam8 (Ma et al., 2011). cch1delta was sensitive to low KCl concentrations, and both cch1delta cfr1delta and yam8delta cfr1delta were more sensitive than any of the single mutants.
PMID:34349749	PBO:0096586	Interestingly, deleting cch1+ suppressed cfr1delta sensitivity to CaCl2 (Supplementary Figure 4).
PMID:34349749	PBO:0096587	ent3delta and apm3delta were slightly sensitive to high concentrations of KCl and KNO3 and were very sensitive to CaCl2. (Figure 8)
PMID:34349749	PBO:0096587	ent3delta and apm3delta were slightly sensitive to high concentrations of KCl and KNO3 and were very sensitive to CaCl2. (Figure 8)
PMID:34349749	FYPO:0001020	(Figure 8) gga22delta, which was the only mutant that grew on CaCl2 plates as efficiently as the WT.
PMID:34349749	PBO:0096586	Interestingly, deleting cch1+ suppressed cfr1delta sensitivity to CaCl2 (Supplementary Figure 4).
PMID:34349749	GO:0006874	Taken together, these experiments showed that calcium homeostasis was altered in exomer mutants, that small defects in the transport of Pkd2 might contribute to this alteration, and that Cch1 facilitates a calcium import that is deleterious for exomer mutants.
PMID:34349749	GO:0006874	Taken together, these experiments showed that calcium homeostasis was altered in exomer mutants, that small defects in the transport of Pkd2 might contribute to this alteration, and that Cch1 facilitates a calcium import that is deleterious for exomer mutants.
PMID:34349749	GO:0032178	We found that Pkd2-GFP was at the cell surface, with strong accumulation at the septal area in both strains (Figure 5D). Quantitative analyses did not detect significant differences between the strains regarding the distribution and intensity of Pkd2-GFP fluorescence at the cell surface, neither under basal conditions nor in KCl (Supplementary Figure 3).
PMID:34349749	PBO:0116449	(Figure 5.)
PMID:34349749	PBO:0093595	pmr1delta was more sensitive to KCl than cfr1delta, and the double mutants were the most sensitive (Supplementary Figure 4).
PMID:34349749	PBO:0116447	(Figure 8) All mutants exhibited a degree of sensitivity to hygromycin B that was alleviated by KCl, an indication of membrane hyperpolarization.
PMID:34349749	PBO:0107560	Interestingly, deleting cch1+ suppressed cfr1delta sensitivity to CaCl2 (Supplementary Figure 4).
PMID:34349749	PBO:0093595	pmr1delta was more sensitive to KCl than cfr1delta, and the double mutants were the most sensitive (Supplementary Figure 4).
PMID:34349749	PBO:0093595	pmr1delta was more sensitive to KCl than cfr1delta, and the double mutants were the most sensitive (Supplementary Figure 4).
PMID:34349749	PBO:0093595	(Supplementary Figure 4).
PMID:34349749	PBO:0107560	Interestingly, deleting cch1+ suppressed cfr1delta sensitivity to CaCl2 (Supplementary Figure 4).
PMID:34349749	FYPO:0001020	pmr1delta was sensitive to 100 mM CaCl2 while pmr1delta cfr1delta was not (Supplementary Figure 4)
PMID:34349749	FYPO:0001020	pmr1delta was sensitive to 100 mM CaCl2 while pmr1delta cfr1delta was not (Supplementary Figure 4)
PMID:34349749	FYPO:0000098	pmr11 was sensitive to 100 mM CaCl2 while pmr11 cfr11 was not (Supplementary Figure 4)
PMID:34349749	PBO:0095508	erg51 exhibited a sensitivity to K+ salts and hygromycin B, that was milder than that of exomer mutants, was slightly more sensitive to CaCl2, and grew well on sorbitol (Figure 7A)
PMID:34349749	PBO:0116447	erg51 exhibited a sensitivity to K+ salts and hygromycin B, that was milder than that of exomer mutants, was slightly more sensitive to CaCl2, and grew well on sorbitol (Figure 7A)
PMID:34349749	GO:0030007	The results showed that this content was significantly higher in the exomer mutant than in the WT (Figure 1D), data that confirmed that exomer plays a role in the regulation of K+ homeostasis.
PMID:34349749	FYPO:0008346	The results showed that this content was significantly higher in the exomer mutant than in the WT (Figure 1D), data that confirmed that exomer plays a role in the regulation of K+ homeostasis.
PMID:34349749	PBO:0093594	we analyzed the growth of prototrophic WT and bch1delta strains on YES plates with 0.6 M KCl. We found that the mutant was sensitive under these conditions (Figure 1C). | Figure 5C
PMID:34349749	FYPO:0000961	In contrast, the mutant grew well in the presence of 1.2 M sorbitol, a medium with similar osmolarity to 0.6 M KCl.
PMID:34349749	PBO:0093594	First, we determined whether cfr1delta sensitivity to high KCl concentrations was due to an inability to grow under ionic or osmotic stress. To do so, we analyzed cfr11 sensitivity to several potassium salts at different concentrations, which depended on the concentration that inhibited the growth of the WT, and to sorbitol (Figure 1A). cfr11 exhibited growth defects in the presence of 0.6 M potassium chloride (KCl), 0.6 M potassium nitrate (KNO3), and 0.02 M potassium acetate (CH3 CO2 K). cfr11 exhibited growth defects in the presence of 0.6 M potassium chloride (KCl), 0.6 M potassium nitrate (KNO3), and 0.02 M potassium acetate (CH3 CO2 K). |Interestingly, deleting cch1+ suppressed cfr1delta sensitivity to CaCl2 (Supplementary Figure 4).
PMID:34349749	PBO:0116447	erg51 exhibited a sensitivity to K+ salts and hygromycin B, that was milder than that of exomer mutants, was slightly more sensitive to CaCl2, and grew well on sorbitol (Figure 7A)
PMID:34349749	PBO:0093593	erg51 exhibited a sensitivity to K+ salts and hygromycin B, that was milder than that of exomer mutants, was slightly more sensitive to CaCl2, and grew well on sorbitol (Figure 7A)
PMID:34349749	PBO:0093595	(Figure 7A). erg51 bch11 was more sensitive than the single mutants
PMID:34349749	PBO:0093595	(Figure 7A). erg51 bch11 was more sensitive than the single mutants
PMID:34349749	PBO:0116449	(Figure 5C)
PMID:34349749	PBO:0116449	(Figure 5C)
PMID:34349749	PBO:0093558	We found that cfr1delta enhanced its3-1 thermosensitivity, and that its3-1 enhanced cfr11 sensitivity to 0.6 M KCl, which showed genetic interaction (Figure 7D).
PMID:34349749	PBO:0093558	We found that cfr1delta enhanced its3-1 thermosensitivity, and that its3-1 enhanced cfr11 sensitivity to 0.6 M KCl, which showed genetic interaction (Figure 7D).
PMID:34349749	PBO:0093557	We found that cfr11 enhanced its3-1 thermosensitivity, and that its3-1 enhanced cfr11 sensitivity to 0.6 M KCl, which showed genetic interaction (Figure 7D).
PMID:34349749	PBO:0116455	In summary, in the absence of exomer and in the presence of KCl, the distribution of sterols and PI(4,5)P2 was different from that of the WT, which might contribute to altered membrane polarization and ion homeostasis in the mutant.
PMID:34349749	PBO:0093593	(Figure 8) We found that apm1delta, gga22delta, and gga21delta gga22delta (denoted by ggadeltadelta in the Figure 8) were sensitive to both high concentrations of K+ salts and sorbitol (Figure 8), which showed that they were defective in growth under osmotic stress.
PMID:34349749	PBO:0096178	(Figure 8) All mutants exhibited a degree of sensitivity to hygromycin B that was alleviated by KCl, an indication of membrane hyperpolarization.
PMID:34349749	PBO:0116447	(Figure 8) All mutants exhibited a degree of sensitivity to hygromycin B that was alleviated by KCl, an indication of membrane hyperpolarization.
PMID:34349749	PBO:0095408	All mutants exhibited a degree of sensitivity to hygromycin B that was alleviated by KCl, an indication of membrane hyperpolarization.
PMID:34349749	PBO:0095408	All mutants exhibited a degree of sensitivity to hygromycin B that was alleviated by KCl, an indication of membrane hyperpolarization.
PMID:34349749	PBO:0095408	(Figure 8) All mutants exhibited a degree of sensitivity to hygromycin B that was alleviated by KCl, an indication of membrane hyperpolarization.
PMID:34349749	PBO:0093595	We found that apm1delta, gga22delta, and gga21delta gga22delta (denoted by gga11 in the Figure 8) were sensitive to both high concentrations of K+ salts and sorbitol (Figure 8), which showed that they were defective in growth under osmotic stress.
PMID:34349749	PBO:0093593	(Figure 8) We found that apm1delta, gga22delta, and gga21delta gga22delta (denoted by ggadeltadelta in the Figure 8) were sensitive to both high concentrations of K+ salts and sorbitol (Figure 8), which showed that they were defective in growth under osmotic stress.
PMID:34349749	PBO:0093593	(Figure 8) We found that apm1delta, gga22delta, and gga21delta gga22delta (denoted by ggadeltadelta in the Figure 8) were sensitive to both high concentrations of K+ salts and sorbitol (Figure 8), which showed that they were defective in growth under osmotic stress.
PMID:34349749	PBO:0093595	We found that apm1delta, gga22delta, and gga21delta gga22delta (denoted by gga11 in the Figure 8) were sensitive to both high concentrations of K+ salts and sorbitol (Figure 8), which showed that they were defective in growth under osmotic stress.
PMID:34349749	PBO:0093593	(Figure 8) We found that apm1delta, gga22delta, and gga21delta gga22delta (denoted by ggadeltadelta in the Figure 8) were sensitive to both high concentrations of K+ salts and sorbitol (Figure 8), which showed that they were defective in growth under osmotic stress.
PMID:34349749	PBO:0093593	(Figure 8) We found that apm1delta, gga22delta, and gga21delta gga22delta (denoted by ggadeltadelta in the Figure 8) were sensitive to both high concentrations of K+ salts and sorbitol (Figure 8), which showed that they were defective in growth under osmotic stress.
PMID:34349749	PBO:0116449	(Figure 5.)
PMID:34349749	PBO:0096587	(Figure 5.)
PMID:34349749	PBO:0096587	(Figure 5.)
PMID:34349749	PBO:0107560	(Figure 5.)
PMID:34349749	PBO:0095508	(Figure 5C)
PMID:34349749	PBO:0093595	(Figure 5C)
PMID:34349749	PBO:0093595	(Figure 5C)
PMID:34349749	FYPO:0005947	(Figure 5C))
PMID:34349749	FYPO:0004203	A close observation of the results indicated that under basal conditions (0′), the WT amount of GFP was significantly greater in cfr11 than in the WT, which suggested increased intracellular Ca2 + . | However, in cfr11 cells the amount of Ca2+ continued increasing for another 15 min, and reached a peak that was more than three-fold the value of the baseline (Figure 5B). The maximum Ca2+ level in cfr11 was 67% higher than in the WT | To understand whether the cytoplasmic calcium increase was produced by influx from the exterior or by movements from internal reservoirs, we analyzed the Ca2+ level in the presence of EGTA. We found that the presence of the chelator in the medium completely blocked the increase in Ca2+ levels in both the WT and the mutant cells (Figure 5B). In summary, we concluded that Cfr1 modulated the cellular Ca2+ response to KCl stress by regulating some aspect of Ca2 + influx.
PMID:34349749	PBO:0116452	in the WT about 10% of the cells exhibited asymmetrical and subapical Cta3 distribution, while this percentage was over 50% in the mutant (lower right panel in Figure 4F).
PMID:34349749	GO:0032178	Regarding protein localization, microscopy observation showed that 1 h after the addition of KCl most Cta3-GFP accumulated at the cell periphery of the sites of polarized growth (cell poles and equator), and that the intensity of the fluorescence in this location was similar in WT and mutant cells (Figure 4E and Supplementary Figure 2).
PMID:34349749	GO:0031520	Regarding protein localization, microscopy observation showed that 1 h after the addition of KCl most Cta3-GFP accumulated at the cell periphery of the sites of polarized growth (cell poles and equator), and that the intensity of the fluorescence in this location was similar in WT and mutant cells (Figure 4E and Supplementary Figure 2).
PMID:34349749	PBO:0116449	The result was that overexpression of the extrusion pump alleviated the growth of cfr11 in the presence of high K+ concentrations (Figure 4C).
PMID:34349749	PBO:0116451	The result was that overexpression of the extrusion pump alleviated the growth of cfr11 in the presence of high K+ concentrations (Figure 4C).
PMID:34349749	PBO:0116451	The result was that overexpression of the extrusion pump alleviated the growth of cfr11 in the presence of high K+ concentrations (Figure 4C).
PMID:34349749	PBO:0093595	We also analyzed the relationship between exomer and the calcium channels Cch1 and Yam8 (Ma et al., 2011). cch1delta was sensitive to low KCl concentrations, and both cch1delta cfr1delta and yam8delta cfr1delta were more sensitive than any of the single mutants.
PMID:34349749	PBO:0116453	In addition, there was intracellular Pkd2-GFP fluorescence. All cells exhibited a faint signal that corresponded to the vacuoles, which in S. pombe are small and numerous, and some cells exhibited at least one bright intracellular dot (denoted by an arrow in Figure 5D). In the WT, less than 20% of the cells exhibited bright intracellular dots, while this number was over 40% in cfr11 (Figure 5F). This difference was evident in the absence of KCl, showing that it was produced by a lack of exomer. Moreover, the dots were brighter in the mutant than in the control (Figure 5G). Western blotting showed that stronger fluorescence was not due to higher levels of the protein (Figure 5H). Quantitative colocalization analyses showed that most of these dots corresponded to the TGN and that fewer dots corresponded to the PVE (Figure 5I and Supplementary Figure 3).
PMID:34349749	PBO:0116454	Exposure to KCl resulted in a small but significant change in Pkd2 distribution, with a reduction in the number of dots that corresponded to the TGN and an increase in the number of dots that corresponded to the PVE. Pkd2 accumulation in the PVE in the presence of KCl was stronger in cfr11 than in the WT. Thus, the effect of potassium in Pkd2 intracellular distribution was enhanced by exomer deletion.
PMID:34349749	FYPO:0005947	As shown in Supplementary Figure 4, their deletion neither produced sensitivity to KCl nor enhanced the sensitivity of bch1delta
PMID:34349749	FYPO:0005947	As shown in Supplementary Figure 4, their deletion neither produced sensitivity to KCl nor enhanced the sensitivity of bch1delta
PMID:34349749	PBO:0096587	Conversely, double mutants were more sensitive to CaCl2 than single mutants. (Figure S4)
PMID:34349749	PBO:0096587	Conversely, double mutants were more sensitive to CaCl2 than single mutants. (Figure S4)
PMID:34349749	PBO:0096587	Conversely, double mutants were more sensitive to CaCl2 than single mutants. (Figure S4)
PMID:34349749	PBO:0096587	Conversely, double mutants were more sensitive to CaCl2 than single mutants. (Figure S4)
PMID:34349749	FYPO:0001020	(Figure S4)
PMID:34349749	PBO:0093594	We also analyzed the relationship between exomer and the calcium channels Cch1 and Yam8 (Ma et al., 2011). cch11 was sensitive to low KCl concentrations, and both cch11 cfr11 and yam81 cfr11 were more sensitive than any of the single mutants.
PMID:34349749	PBO:0107560	Under these conditions, cta31 bch11 was sensitive to lower calcium concentrations.
PMID:34349749	PBO:0096586	Since Cta3 was originally described as an ATP-dependent Ca2+ pump (Ghislain et al., 1990; Halachmi et al., 1992), we also analyzed growth on CaCl2 plates and found that cta3delta was only sensitive to high calcium concentrations, and only in the absence of the Tup regulators.
PMID:34349749	FYPO:0001020	Since Cta3 was originally described as an ATP-dependent Ca2+ pump (Ghislain et al., 1990; Halachmi et al., 1992), we also analyzed growth on CaCl2 plates and found that cta3delta was only sensitive to high calcium concentrations, and only in the absence of the Tup regulators.
PMID:34349749	PBO:0116450	while cta31 was only sensitive to 0.6 M KCl in the tup11delta tup12delta background (Figure 4a)
PMID:34349749	PBO:0116449	We found that the simultaneous deletion of exomer components and cta3+ led to sensitivity to low concentrations of KCl and KNO3 (Figure 4a)
PMID:34349749	PBO:0116449	We found that the simultaneous deletion of exomer components and cta3+ led to sensitivity to low concentrations of KCl and KNO3 (Figure 4a)
PMID:34349749	PBO:0093595	We found that the simultaneous deletion of exomer components and cta3+ led to sensitivity to low concentrations of KCl and KNO3 (Figure 4a)
PMID:34349749	PBO:0093595	We found that the simultaneous deletion of exomer components and cta3+ led to sensitivity to low concentrations of KCl and KNO3 (Figure 4a)
PMID:34349749	PBO:0096586	cfr1delta was only sensitive to very high Na+ and Ca2+ concentrations (lower panels in Figure 3D)
PMID:34349749	PBO:0094278	cfr1delta was only sensitive to very high Na+ and Ca2+ concentrations (lower panels in Figure 3D)
PMID:34349749	PBO:0107560	The results showed that trk1delta was partially sensitive to 40 mM NaCl and sensitive to 100 mM CaCl2 (Figure 3D)
PMID:34349749	PBO:0094276	trk1delta trkdelta was the most sensitive of all the strains. ( (Figure 3D)
PMID:34349749	PBO:0094276	trk1delta trkdelta was the most sensitive of all the strains. ( (Figure 3D)
PMID:34349749	PBO:0094279	The results showed that trk1delta was partially sensitive to 40 mM NaCl and sensitive to 100 mM CaCl2 (Figure 3D)
PMID:34349749	PBO:0116448	(Figure 3C)
PMID:34349749	PBO:0096178	cfr1delta was partially sensitive to hygromycin B and deleting cfr1+ enhanced the sensitivity of trk1delta, trk2delta, and trk1delta trk2delta strains (Figure 3C).
PMID:34349749	PBO:0096178	cfr1delta was partially sensitive to hygromycin B and deleting cfr1+ enhanced the sensitivity of trk1delta, trk2delta, and trk1delta trk2delta strains (Figure 3C).
PMID:34349749	PBO:0095408	cfr1delta was partially sensitive to hygromycin B and deleting cfr1+ enhanced the sensitivity of trk1delta, trk2delta, and trk1delta trk2delta strains (Figure 3C).
PMID:34349749	PBO:0095408	cfr1delta was partially sensitive to hygromycin B and deleting cfr1+ enhanced the sensitivity of trk1delta, trk2delta, and trk1delta trk2delta strains (Figure 3C).
PMID:34349749	PBO:0116447	cfr1delta was partially sensitive to hygromycin B and deleting cfr1+ enhanced the sensitivity of trk1delta, trk2delta, and trk1delta trk2delta strains (Figure 3C).
PMID:34349749	PBO:0096178	cfr1delta was partially sensitive to hygromycin B and deleting cfr1+ enhanced the sensitivity of trk1delta, trk2delta, and trk1delta trk2delta strains (Figure 3C).
PMID:34349749	FYPO:0005947	We found that neither osr2delta nor kha1delta was sensitive to K+ salts and that the phenotype of the corresponding double mutant was similar to that of the single cfr1delta mutant (Figure 2D)
PMID:34349749	FYPO:0005947	We found that neither osr2delta nor kha1delta was sensitive to K+ salts and that the phenotype of the corresponding double mutant was similar to that of the single cfr1delta mutant (Figure 2D).
PMID:34349749	FYPO:0005947	We found that neither osr2delta nor kha1delta was sensitive to K+ salts and that the phenotype of the corresponding double mutant was similar to that of the single cfr11 mutant (Figure 2D).
PMID:34349749	PBO:0116446	GFP-Trk1 localized at the cell surface of the cell growing sites (cell poles and equator) in both, WT and cfr11 cells (Figure 2B), confirming proper Trk1 sorting in the absence of exomer.
PMID:34349749	GO:0032178	GFP-Trk1 localized at the cell surface of the cell growing sites (cell poles and equator) in both, WT and cfr11 cells (Figure 2B), confirming proper Trk1 sorting in the absence of exomer. (combined with existing knowledge)
PMID:34349749	GO:0031520	GFP-Trk1 localized at the cell surface of the cell growing sites (cell poles and equator) in both, WT and cfr11 cells (Figure 2B), confirming proper Trk1 sorting in the absence of exomer. (combined with existing knowledge)
PMID:34349749	PBO:0093593	The phenotype of trk1delta trk2delta cfr1delta was similar to that of trk2delta cfr1delta.
PMID:34349749	PBO:0093593	Regarding double mutants, trk1delta cfr1delta was more sensitive than cfr1delta, indicating that both genes cooperated and acted in parallel rather than in linear pathways related to K+ sensitivity.
PMID:34349749	PBO:0093593	Regarding double mutants, trk1delta cfr1delta was more sensitive than cfr1delta, indicating that both genes cooperated and acted in parallel rather than in linear pathways related to K+ sensitivity.
PMID:34349749	PBO:0093595	Regarding double mutants, trk1delta cfr1delta was more sensitive than cfr1delta, indicating that both genes cooperated and acted in parallel rather than in linear pathways related to K+ sensitivity.
PMID:34349749	PBO:0093595	Regarding double mutants, trk1delta cfr1delta was more sensitive than cfr1delta, indicating that both genes cooperated and acted in parallel rather than in linear pathways related to K+ sensitivity.
PMID:34349749	FYPO:0005947	Nonetheless, we compared the growth of trk1delta and trk2delta with that of cfr1delta in the presence of high K+ concentrations. Additionally, we constructed double and triple mutants to determine whether cfr1+ acts in the same functional pathways as trk1+ and/or trk2+. The results showed that while cfr11 was sensitive to potassium salts, neither trk1delta, trk2delta nor trk1delta trk2delta exhibited sensitivity (Figure 2A).
PMID:34352089	GO:0000956	(comment: CHECK waiting for GO:NEW.) We show this for only two mRNA: mfs2 and SPBC530.02. (comment: Can this be added in the annotation extension ?)
PMID:34352089	PBO:0104079	Pac1 strain (Pac1-AA) that allowed rapid rapamycin-dependent nuclear exclusion of Pac1 (Figure 1B).
PMID:34352089	PBO:0104078	(comment: MOVE DOWN)
PMID:34352089	PBO:0104077	(comment: MOVE DOWN)
PMID:34352089	PBO:0104076	we observed a sharp decline in RNAPII occupancy inside the gene body, directly downstream of the Pac1- bound region located in the first half of the genes (Figure 2B, blue profile). In contrast, Pac1 nuclear exclusion resulted in extended RNAPII occupancy throughout the entire ORFs (Figure 2B, red profile). Such differences in RNAPII profiles are suggestive of Pac1-dependent premature termination.
PMID:34352089	GO:0000956	(comment: CHECK waiting for GO:NEW.)inferred from association with prremature termination sites
PMID:34352089	FYPO:0007883	we observed a sharp decline in RNAPII occupancy inside the gene body, directly downstream of the Pac1- bound region located in the first half of the genes (Figure 2B, blue profile). In contrast, Pac1 nuclear exclusion resulted in extended RNAPII occupancy throughout the entire ORFs (Figure 2B, red profile). Such differences in RNAPII profiles are suggestive of Pac1-dependent premature termination.
PMID:34352089	PBO:0104074	(comment: 5' extended precursors, C/C box (but not H/ACA box))
PMID:34352089	PBO:0104073	(comment: 5' extended precursors, C/C box (but not H/ACA box))
PMID:34352089	PBO:0104072	(comment: 5' extended precursors, C/C box (but not H/ACA box).) Pac1 nuclear exclusion specifically led to the accumulation of 5′-extended precursors of Pac1-bound C/D box snoRNAs (Supplementary Figure S3A). This accumulation was confirmed by Northern blot assays on three C/D box snoRNAs (sno16, snoU14 and snr79), whereas a control H/ACA box snoRNA (sno12) was unaffected
PMID:34352089	PBO:0104071	(Figure 1c)
PMID:34352089	PBO:0104069	(Figure 3A and Supplementary Figure S5A)
PMID:34352089	PBO:0104069	(Figure 3A and Supplementary Figure S5A)
PMID:34352089	GO:0030847	(comment: CHECK NEW TERM REQUESTED CHILD OF BOTH termination of RNA polymerase II transcription, poly(A)-independent) We showed pac1-dependent poly(A)-independent RNA polymerase II termination for 2 mRNA genes (mfs2 and SPBC530.02), 4 snRNA genes (snU1, snU2, snU4 and snU5), and 2 snoRNA genes (snU3 and snU32) . (comment: Can this be added in the annotation extension ?)
PMID:34352089	PBO:0093558	Supplementary Figure S5B
PMID:34382912	MOD:00046	(Fig. 5)
PMID:34382912	MOD:00046	(Fig. 5)
PMID:34382912	PBO:0103460	(Fig. 4)
PMID:34382912	MOD:00046	(Fig. 5)
PMID:34382912	MOD:00046	(Fig. 5)
PMID:34382912	MOD:00046	(Fig. 5)
PMID:34382912	PBO:0103459	(Fig. 4)
PMID:34382912	PBO:0103458	(Fig. 4)
PMID:34382912	PBO:0103457	(Figure 2)
PMID:34382912	MOD:00046	(Fig. 5)
PMID:34382996	FYPO:0000413	(comment: CHECK Stronger phenotype in h+ than h- cell)
PMID:34382996	GO:1990819	(Figure 5)
PMID:34382996	GO:1990819	(Figure 5)
PMID:34382996	PBO:0108248	(Fig. 6, A-C) The density of vesicles was strongly reduced in the fus1Δ cells, whether this was h+ or h−, while WT h+ cells showed slightly higher vesicle density than h− cells, as in previous analysis ()
PMID:34382996	FYPO:0007876	Interestingly, the reduction in local secretion correlates with a strong loss of the wPM phenotype (Fig. 6, A and B; Fig. S4, E and F; and Fig. S5): only 4% of h+ fus1Δ cells (1/27) showed wPM, whereas 73% (16/22) and 20% (4/20) of h+ WT showed wPM in WT × WT and WT × fus1Δ crosses, respectively
PMID:34382996	PBO:0108245	(Fig. 6 E and Fig. S4 D) By LM, Myo52 and Exo84 also showed strong signal reduction in fus1Δ .
PMID:34382996	FYPO:0004804	no assembly of vesicles by (Because cell fusion completely fails when both partner cells lack fus1)
PMID:34382996	FYPO:0000413	(comment: CHECK Only when gpd1∆ is in h- cell)
PMID:34382996	FYPO:0007874	(Fig. 6,A-C) The density of vesicles was strongly reduced in the fus1Δ cells, whether this was h+ or h−, while WT h+ cells showed slightly higher vesicle density than h− cells, as in previous analysis ()
PMID:34389684	PBO:0099757	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	PBO:0099756	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	PBO:0099755	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	PBO:0099754	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	PBO:0099753	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	PBO:0099752	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	PBO:0099751	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	PBO:0093554	(Fig. 7A)
PMID:34389684	PBO:0093554	(Fig. 7A)
PMID:34389684	FYPO:0000080	(Fig. 7a)
PMID:34389684	PBO:0094771	(Fig. 7) (comment: compared to WT)
PMID:34389684	FYPO:0002061	The seb1-G476S and aps1Δ alleles were synthetically lethal
PMID:34389684	PBO:0099764	Here, we found that tgp1 promoter-driven acid phosphatase expression was increased 30-fold in seb1-G476S cells versus seb1-WT cells and that this derepression was effaced by mutating the promoter-proximal nc- tgp1 PAS (Fig. 4D).
PMID:34389684	PBO:0099749	(comment: compared to WT)
PMID:34389684	PBO:0099749	(Fig. 7) (comment: compared to WT)
PMID:34389684	PBO:0099763	(Fig. 4B), Pho1 expression from the wild-type plasmid was increased sevenfold in seb1-G476S cells versus seb1-WT cells thereby echoing the derepressive effect of seb1-G476S on pho1 expression from the chromosomal prt-pho1 locus.
PMID:34389684	FYPO:0001357	..... while rhn1Δ rescued the cs growth defect of seb1-G476S at 20 °C
PMID:34389684	FYPO:0002060	(Figure 3A) Notable findings were that seb1-G476S rescued the ts growth defect of rhn1Δ at 37 °C......
PMID:34389684	FYPO:0001355	(Figure 1c)
PMID:34389684	PBO:0099761	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	PBO:0099760	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	PBO:0099750	(comment: compared to WT)
PMID:34389684	PBO:0094738	(comment: compared to WT)
PMID:34389684	PBO:0099750	Although seb1- G476S asp1-H397A cells grew slowly in liquid medium at 30 °C, an assay of acid phosphatase showed that the double mutant expressed threefold higher levels of Pho1 than the seb1-G476S single mutant (Fig. 6B). (NOTE ABOUT 20 FOLD HIGHE TTHAN WT)
PMID:34389684	PBO:0094777	(comment: similar to wt)
PMID:34389684	PBO:0099749	(Figure 1A) (comment: vw changed to increased with low serverity as we compare to WT)
PMID:34389684	FYPO:0001489	(DNS)
PMID:34389684	FYPO:0001489	(DNS)
PMID:34389684	FYPO:0001489	(DNS)
PMID:34389684	PBO:0099748	(Figure 1A)
PMID:34389684	FYPO:0000080	(Figure 1C)
PMID:34389684	PBO:0099759	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	PBO:0099758	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34402513	PBO:0109289	This phenotype suggests that phosphorylation of the 17 CK1 consensus sites in Imp2 promotes the medial anchoring of the CR on the membrane, possibly by stabilizing an unknown interaction involving the Imp2 IDR.
PMID:34402513	PBO:0099838	(comment: vw added extensions to link MF to BP & phase)
PMID:34402513	PBO:0099837	(Figure 1A-C)
PMID:34402513	PBO:0099836	(Figure 1A-C)
PMID:34402513	FYPO:0001903	(Figure S2A and C)
PMID:34402513	PBO:0099835	(Figure 1A-C)
PMID:34402513	PBO:0099834	(Figure 1A-C)
PMID:34402513	PBO:0099833	(Figure 1A-C)
PMID:34402513	PBO:0099832	(Figure 1A-C)
PMID:34402513	PBO:0099831	(Figure 1A-C)
PMID:34402513	PBO:0099830	(Figure 1A-C)
PMID:34402513	PBO:0099829	(Figure 1A-C)
PMID:34402513	PBO:0099812	(Figure 1A-C)
PMID:34402513	PBO:0099812	(Figure 2G)
PMID:34402513	PBO:0099816	(Figure 2G,H)
PMID:34402513	PBO:0099816	(Figure 2G) However, mutation of 3 additional Cdk1 consensus sites abolished Imp2 phosphorylation by Cdk1 (Imp2-11A, Fig. 2C).
PMID:34402513	PBO:0099815	(Figure 3) Imp2-11E-mNG was not recruited to the CR later than Imp2-mNG but its peak accumulation was delayed compared to wild-type (Fig. 3A, B, and C)
PMID:34402513	FYPO:0001365	(Figure 4) However, imp2-17E cells exhibited slower CR constriction. In fact, CR remnants remained in 62% of imp2-17E cells for the duration of our observation.
PMID:34402513	FYPO:0007828	(Figure 4)
PMID:34402513	FYPO:0001368	(Figure 4)
PMID:34402513	FYPO:0002253	(Figure S3B-C)
PMID:34402513	FYPO:0001903	(Figure S2C)
PMID:34402513	PBO:0099814	(Figure S2F)
PMID:34402513	PBO:0099813	(Figure S2D-E)
PMID:34402513	PBO:0099828	(Figure 1A-C)
PMID:34402513	PBO:0099827	(Figure 1A-C)
PMID:34402513	PBO:0099826	(Figure 1A-C)
PMID:34402513	PBO:0099825	(Figure 1A-C)
PMID:34402513	PBO:0099824	(Figure 1A-C)
PMID:34402513	PBO:0099823	(Figure 1A-C)
PMID:34402513	PBO:0099822	(Figure 1A-C)
PMID:34402513	PBO:0099816	(Figure 2F)
PMID:34402513	FYPO:0001252	(Figure S2A-C)
PMID:34402513	FYPO:0001760	(Figure S2A-B)
PMID:34402513	PBO:0099816	(Figure 2D)
PMID:34402513	FYPO:0001368	(Figure 4)
PMID:34402513	FYPO:0007828	(Figure 4)
PMID:34402513	FYPO:0004097	(Figure 4)
PMID:34402513	FYPO:0004097	(Figure 4A-B)
PMID:34402513	FYPO:0007828	(Figure 4A-B)
PMID:34402513	FYPO:0001368	(Figure 4A-B)
PMID:34402513	PBO:0099811	(Figure S2D-E)
PMID:34402513	PBO:0099817	(Figure 3) Imp2-11A-mNG was recruited to the CR earlier (ca. 4 minutes) than Imp2-mNG (Fig. 3A, B, and C).
PMID:34402513	FYPO:0001903	(Figure SA and C)
PMID:34402513	PBO:0099818	(Figure S2D and F)
PMID:34402513	PBO:0099819	(Figure S2D-E)
PMID:34402513	FYPO:0002253	(Figure S3B-C)
PMID:34402513	PBO:0099813	(Figure S2D-E)
PMID:34402513	PBO:0099818	(Figure S2D and F)
PMID:34402513	FYPO:0001903	(Figure S2A and C)
PMID:34402513	FYPO:0001903	(Figure S2A and C)
PMID:34402513	FYPO:0000339	(Figure S3B-C)
PMID:34402513	FYPO:0005289	(Figure S3A) Interestingly, we noticed during imaging that imp2-17A rlc1-mNG sid4-mNG cells displayed CR sliding events where the CR formed in the middle of the cell but then slid towards one cell tip (6/18 cells) (Fig. S3A).
PMID:34402513	FYPO:0001903	(Figure S2A and C)
PMID:34402513	FYPO:0002253	(Figure S3B-C)
PMID:34402513	FYPO:0001368	(Figure 4)
PMID:34402513	FYPO:0007828	(Figure 4)
PMID:34402513	FYPO:0004097	(Figure 4)
PMID:34402513	PBO:0099820	(Figure 3)
PMID:34402513	PBO:0099821	(Figure 2E)
PMID:34402513	FYPO:0000316	(Figure S4B)
PMID:34402513	FYPO:0002062	(Figure S4A)
PMID:34402513	FYPO:0002062	(Figure S4A)
PMID:34402513	FYPO:0002062	(Figure S4A)
PMID:34402513	FYPO:0004085	(Figure S4A)
PMID:34402513	FYPO:0004085	(Figure S4B)
PMID:34402513	FYPO:0000316	(Figure S4B)
PMID:34402513	FYPO:0001971	(Figure S2A-B) there was no detectable defect in morphology or cell division in imp2-11A, imp2-11E, imp2-17E, imp2-28A or imp2-28E cells although some imp2-17A cells failed to separate, forming chains (Fig. S2A and B).
PMID:34402513	FYPO:0001760	(Figure S2A-B)
PMID:34402513	FYPO:0001760	(Figure S2A-B)
PMID:34402513	FYPO:0001760	(Figure S2A-B)
PMID:34402513	FYPO:0001760	(Figure S2A-B)
PMID:34402513	PBO:0099841	Imp2 was phosphorylated by Hhp1 in vitro, and mutation of the 15 identified and two more CK1 consensus sites eliminated this phosphorylation (Fig. 2B)
PMID:34402513	PBO:0099840	Together these findings implicate Cdk1 in modulating the timing of Imp2 localization to the CR, and are consistent with the general theme of Cdk1 inhibiting cytokinesis until chromosome segregation is complete
PMID:34402513	FYPO:0001971	(Figure S2A-B)
PMID:34460892	PBO:0103878	(comment: Evidence form RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence was from RNA-seq not from microarray)
PMID:34460892	PBO:0103879	(comment: Evidence code was RNA-seq)
PMID:34460892	PBO:0103880	(comment: Evidence from RNA-seq data)
PMID:34460892	PBO:0092337	(comment: Evidence from RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0092337	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0092140	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0092337	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence was from RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence form RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence form RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence form RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence form RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence form RNA-seq data)
PMID:34460892	PBO:0092337	(comment: Evidence form RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence form RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence form RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence form RNA-seq data)
PMID:34460892	PBO:0092337	(comment: Evidence form RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence form RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence from RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence from RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence from RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence from RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence from RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence from RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence from RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence from RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence from RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence from RNA-seq data)
PMID:34460892	PBO:0092337	(comment: Evidence from RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence from RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence from RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence from RNA-seq data)
PMID:34460892	PBO:0103878	(comment: Evidence from RNA-seq data)
PMID:34460892	PBO:0103880	(comment: Evidence from RNA-seq data)
PMID:34464389	PBO:0106084	(comment: CHECK during stationary phase). Figure 6C In fact, the protein levels of Scw1 markedly decreased in ageing cells.
PMID:34464389	PBO:0103668	(Figure 5A) Cells lacking Sir2 showed a subtle extension of chronological lifespan compared to wild-type, especially at later timepoints
PMID:34464389	FYPO:0007937	Based on DNA breakpoint junctions in genome sequence data (Fig 5B While wild-type cells showed a substantial increase of indels in aged cells, sir2Δ cells showed only a subtle increase
PMID:34464389	FYPO:0000245	(Figure S7C) Moreover, the tlh2 overexpression strain was substantially shorter-lived than wild-type cells
PMID:34464389	FYPO:0007936	(Fig. 5B) Notably, in aged cells the double mutant showed an ~3-fold increase in chromosomal junctions on average, albeit with large variation, but no increase in indels
PMID:34464389	FYPO:0001309	(Fig. 5A) Given the increased lifespan of rnh1Δ rnh201Δ cells
PMID:34464389	PBO:0105656	(Fig. S7A) A re-analysis of RNA-seq data from non-dividing cells [68] revealed a subtle increase in tlh2 expression during chronological ageing
PMID:34464389	PBO:0110916	(Figure 4B) Accordingly, our smFISH experiment showed that tlh2 was de-repressed in sir2 deletion cells
PMID:34464389	FYPO:0007936	(Figure S7B) The proportion of junctions downstream of tlh2 was higher in the tlh2 overexpression strain compared to wild-type
PMID:3448096	FYPO:0000998	cells are longer that wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N
PMID:3448096	FYPO:0000998	cells are longer that wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N
PMID:3448096	FYPO:0000998	cells are longer that wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N
PMID:3448096	FYPO:0000998	cells are longer that wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N
PMID:3448096	FYPO:0000998	cells are longer that wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N
PMID:3448096	FYPO:0000998	cells are longer that wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N
PMID:3448096	FYPO:0000998	cells are longer that wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N
PMID:3448096	FYPO:0000998	cells are longer that wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N
PMID:34499159	FYPO:0000111	(Figure 3c)
PMID:34499159	PBO:0105145	Thus, in addition to Psk1, Atg13 also appears to be phosphorylated by TORC1 in a manner dependent on Mip1 Tyr-533, a residue critical for the TOS motif-mediated recruitment of TORC1 substrates.
PMID:34499159	PBO:0105143	(Figure 1)
PMID:34499159	FYPO:0002672	(Figure 5A)
PMID:34499159	FYPO:0002672	(Figure 5A)
PMID:34499159	PBO:0105141	(Figure 2)
PMID:34499159	PBO:0105140	(Figure 2)
PMID:34499159	PBO:0105131	(Figure 2)
PMID:34499159	PBO:0105139	(Figure 5E)
PMID:34499159	PBO:0105136	(Figure 5D) These observations indicate that the mip1 mutation does not affect the TORC1-dependent phosphorylation of Sck1, Sck2 and Maf1.
PMID:34499159	PBO:0105135	(Figure 4B)
PMID:34499159	PBO:0105132	(Figure 4c)
PMID:34499159	PBO:0105131	(Figure 3d)
PMID:34499159	PBO:0105133	(Figure 4B)
PMID:34499159	FYPO:0001147	(Figure S2B)
PMID:34499159	PBO:0105133	(Figure 4b)
PMID:34499159	FYPO:0001357	(Figure 3C)
PMID:34499159	FYPO:0000111	(Figure 3c)
PMID:34523683	PBO:0119335	(Fig. 7D)
PMID:34523683	PBO:0119330	(Fig. 6)
PMID:34523683	PBO:0119331	(Fig. 7)
PMID:34523683	PBO:0119331	(Fig. 7)
PMID:34523683	PBO:0119332	(Fig. 5)
PMID:34523683	PBO:0119333	(Fig. 5)
PMID:34523683	PBO:0119334	(Fig. 7)
PMID:34523683	PBO:0119336	(Fig. 7E and F)
PMID:34523683	FYPO:0008389	(Fig. S4)
PMID:34523683	FYPO:0008389	(Fig. S4)
PMID:34523683	PBO:0119335	(Fig. 7D)
PMID:34523683	FYPO:0008389	(Fig. S4)
PMID:34524082	PBO:0111588	hht-ub14 substrate which both manifest a similar degree of strong stimulation by H3K14ub (Figure 1C, Figure 1—Figure supplement 1E-H).
PMID:34524082	PBO:0111591	(Figure 1, 3F) These experiments confirm the observation by Oya et al., 2019 that the H3K14ub substrate triggers a dramatic and specific increase in the methyltransferase activity of Clr4. However, in contrast to the previous study, we observe that the KMT domain is sufficient to mediate this regulatory mechanism.
PMID:34524082	PBO:0111592	(Figure 1, 3F)
PMID:34524082	PBO:0095978	(Fig. 4D)
PMID:34524082	PBO:0119846	(comment: consistent with Clr4’s KMT domain mediating the crosstalk between H3K14ub and H3K9me2/3 as an essential step in heterochromatin formation and maintenance.)
PMID:34524082	PBO:0111593	(Figure1 3F)
PMID:34524082	FYPO:0007334	(Fig. 4A)
PMID:34524082	PBO:0095979	(Fig. 4D)
PMID:34524082	PBO:0095976	(Fig. 4E) (comment: CHECK REQUESTED ABOLISHED)
PMID:34524082	PBO:0095980	(Fig. 4D)
PMID:34524082	PBO:0095981	(Fig. 4D)
PMID:34524082	PBO:0095983	(Fig. 4E)
PMID:34524082	PBO:0095983	(Fig. 4E)
PMID:34524082	PBO:0095984	(Fig. 4E)
PMID:34524082	FYPO:0007334	(Fig. 4A)
PMID:34524082	PBO:0095984	(Fig. 4E)
PMID:34524082	PBO:0095977	(Fig. 4D) (comment: Currently, we cannot explain why the dg transcripts in the 3FA mutant are only slightly elevated while completely losing H3K9me2/3.)
PMID:34524082	PBO:0095982	(Fig. 4D)
PMID:34524082	PBO:0095976	(comment: CHECK VW REQUESTED ABOLISHED) Fig. 4E Both H3K9me2 and H3K9me3 were completely abolished in clr4-GS253 and clr4-3FA strains at centromeric dg/dh repeats, being indistinguishable from clr4Δ
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093560	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34580178	PBO:0093559	(Figure 1B)
PMID:34608864	PBO:0105486	(comment: CHECK presence or absence of HU)
PMID:34608864	PBO:0105485	(comment: CHECK presence or absence of HU)
PMID:34608864	PBO:0105479	(comment: CHECK presence or absence of MMS)
PMID:34608864	MOD:01148	(comment: CHECK in presence or absence of MMS)
PMID:34608864	PBO:0105486	(comment: CHECK presence or absence of HU)
PMID:34608864	PBO:0105485	(comment: CHECK presence or absence of HU)
PMID:34608864	FYPO:0004240	(comment: CHECK presence or absence of MMS)
PMID:34608864	FYPO:0004240	(comment: CHECK presence or absence of MMS)
PMID:34613787	GO:1903475	We conclude that type II myosins contribute to both the assembly and disassembly of actin filaments in contractile rings.
PMID:34613787	FYPO:0004854	(Fig. 3C) The number of Cdc12-3GFP molecules in the contractile rings of adf1-M3 mutant cells was on average about twice that of wild-type cells and much more variable
PMID:34613787	FYPO:0004854	(Fig. 3A-B and Table 2). Contractile rings of adf1-M3 mutant cells that were able to constrict had twice as many myosin molecules as the wild-type cells, translating to one myosin motor domain for every 70 nm of filament
PMID:34613787	FYPO:0004854	(Fig. 3A-B and Table 2). Contractile rings of adf1-M3 mutant cells that were able to constrict had twice as many myosin molecules as the wild-type cells, translating to one myosin motor domain for every 70 nm of filament
PMID:34613787	PBO:0098928	(Figure 2B)
PMID:34613787	FYPO:0003014	Second, the normalized disassembly rate, which took the number of actin molecules in the ring into consideration, was 40% lower in the mutant than wild-type cells.
PMID:34613787	PBO:0098929	In contrast, these myosins persisted at nearly their highest levels for an hour and the time course of the process was much more variable in the adf1-M3 mutant cells (Fig. 4C and D). In a few cofilin mutant cells, the myosins dwelled at the cell division site for more than 10 minutes after the completion of the ring constriction (Fig. 5A).
PMID:34613787	FYPO:0002699	Mutations of either type II myosin gene in the myo2-E1 or myp2Δ strains reduced the numbers of actin molecules in contractile rings by more than half compared with wild-type cells at the end of 10 the maturation period and the onset of constriction (Fig. 6A-B and Table 1).
PMID:34613787	PBO:0098926	(Figure 2B)
PMID:34613787	PBO:0098927	Contractile rings of adf1-M3 mutant cells accumulated actin twice as fast over a similar period of time as wild-type cells (Table 2).
PMID:34613787	FYPO:0007898	In prior work the mutant cells appeared to assemble normal contractile rings, but our quantitative measurements revealed that the cdc12-4A mutation reduced by about half both the rate of accumulation and the peak numbers of polymerized actin in the ring (Fig. 2E and Table 1).
PMID:34613787	FYPO:0004854	Therefore, mature rings of the mutant had on average about 1.9 times as much actin as wild-type cells
PMID:34613787	PBO:0098931	Mutations of either type II myosin gene in the myo2-E1 or myp2Δ strains reduced the numbers of actin molecules in contractile rings by more than half compared with wild-type cells at the end of 10 the maturation period and the onset of constriction (Fig. 6A-B and Table 1).
PMID:34613787	FYPO:0001365	(comment: CHECK WHY ISNNT THIS PART. OF ????FYPO:0000230 abnormal actomyosin contractile ring actin filament organization)
PMID:34613787	FYPO:0001365	(comment: CHECK WHY ISNNT THIS PART. OF ????FYPO:0000230 abnormal actomyosin contractile ring actin filament organization)
PMID:34613787	GO:1902404	We conclude that type II myosins contribute to both the assembly and disassembly of actin filaments in contractile rings.
PMID:34613787	GO:1902404	We conclude that type II myosins contribute to both the assembly and disassembly of actin filaments in contractile rings.
PMID:34613787	GO:1903475	We conclude that type II myosins contribute to both the assembly and disassembly of actin filaments in contractile rings.
PMID:34634819	PBO:0114789	(comment: ABOLISHED PROTEIN SPECIFIC TRANSLATION) Radioactive labeling of newly translated mitochondrial proteins showed that the combination of Δmug178 with either Δcbp7 or Δcbp8 abolished cytb translation while Δcbp7 Δcbp8 was similar to Δcbp8 (Figure 8B)
PMID:34634819	FYPO:0000251	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	FYPO:0000251	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	FYPO:0000251	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	FYPO:0000251	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	FYPO:0000251	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	FYPO:0000251	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	FYPO:0000251	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	FYPO:0000251	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	PBO:0119612	However, as with Δcbp7 cells, the newly synthesized Cytb protein showed an aberrant degradation pattern compared to the wild-type since it remained stable for up to 20 h in a chase experiment (Supplementary Figure S5).
PMID:34634819	PBO:0119967	Thus, our mass spectrometry and phenotypic analyses show that Mrh5, Ppr4, Mtf2 and Sls1 are part of a cox1 translational complex interacting with the mitoribosome, at least through Mrh5.
PMID:34634819	PBO:0119967	Thus, our mass spectrometry and phenotypic analyses show that Mrh5, Ppr4, Mtf2 and Sls1 are part of a cox1 translational complex interacting with the mitoribosome, at least through Mrh5.
PMID:34634819	PBO:0119967	Thus, our mass spectrometry and phenotypic analyses show that Mrh5, Ppr4, Mtf2 and Sls1 are part of a cox1 translational complex interacting with the mitoribosome, at least through Mrh5.
PMID:34634819	PBO:0119967	In Δi cells, the mature cox1 mRNA was absent in Δmrh5 and the precursor RNA containing both cox1 introns accumulated; in the point mutant, partial splicing deficiency was observed.
PMID:34634819	PBO:0114622	In brief, Δcbp8 looked similar to Δcbp7 since complex III was barely detectable in BN-PAGE, cytochrome b and c1 were not spectrally detected and a low level of cytb RNA was observed
PMID:34634819	PBO:0105069	The deletion of the cbp8 gene in both ∑i and Δi backgrounds yielded respiratory deficient but antimycin resistant cells showing that ATP synthase was not affected (Figure 3D and not shown).
PMID:34634819	FYPO:0001437	The deletion of the cbp8 gene in both ∑i and Δi backgrounds yielded respiratory deficient but antimycin resistant cells showing that ATP synthase was not affected (Figure 3D and not shown).
PMID:34634819	PBO:0119614	The deletion of the cbp8 gene in both ∑i and Δi backgrounds yielded respiratory deficient but antimycin resistant cells showing that ATP synthase was not affected (Figure 3D and not shown).
PMID:34634819	FYPO:0003731	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	PBO:0119613	This absence of degradation was surprising since Cytb steady state seemed dramatically decreased in the mutant compared to the wt, as revealed in purified mitochondria (Figure 2E) as well as in the total protein chase samples (Supplementary Figure S3) using our in-house antibody. We have no definitive solution to this paradox; the answer might lie with a particularity of our Cytb antibody. This only recognizes Cytb in non-boiled samples, suggesting that the epitope recognised by the antibody is a small structural motif, rather than a linear sequence. Thus, if the neo-synthesized Cytb cannot be correctly folded and inserted into the membrane, the epitope recognised by our antibody may no longer be present.
PMID:34634819	PBO:0119612	Cytb showed a clear pattern of degradation over a 20 h chase in the wt, but appeared repeatedly resistant to degradation in the Δcbp7 mutant in several independent experiments (Figure 2H). This unexpected degradation pattern could indicate that in Δcbp7 cells, the newlysynthetized Cytb might escape recognition and/or accessibility by mitochondrial proteases (65), possibly because of misfolding, aggregation and/or defective membrane insertion.
PMID:34634819	PBO:0114622	First, the cytb mRNA was significantly, although never fully, destabilized (Figure 2F) whereas other mRNAs were not affected.
PMID:34634819	PBO:0105069	Cytochrome spectra showed strongly decreased peaks for cytochromes b and c1 of complex III but normal to increased absorbance for cytochrome a + a3 of complex IV (Figure 2D).
PMID:34634819	FYPO:0001437	but grew normally on fermentable medium containing antimycin, showing that the ATP synthase (complex V) is not strongly affected by the mutation (Figure 2C)
PMID:34634819	FYPO:0003730	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	PBO:0119611	(Figure 2C)
PMID:34634819	GO:0005739	A tagged version of Cbp7 was generated and found to be highly enriched in purified mitochondria (Figure 2B)
PMID:34634819	PBO:0116458	Δsls1 cells lacked spectral a+a3 peak, were devoid of Cox1 and very depleted in Cox2 (Figure 11B, C).
PMID:34634819	PBO:0119615	Δsls1 cells lacked spectral a+a3 peak, were devoid of Cox1 and very depleted in Cox2 (Figure 11B, C).
PMID:34634819	GO:0097177	SMALL SUBUNIT In Δi cells, the mature cox1 mRNA was absent in Δmrh5 and the precursor RNA containing both cox1 introns accumulated; in the point mutant, partial splicing deficiency was observed.
PMID:34634819	PBO:0119618	In Δi cells, the mature cox1 mRNA was absent in Δmrh5 and the precursor RNA containing both cox1 introns accumulated
PMID:34634819	PBO:0119618	In Δi cells, the mature cox1 mRNA was absent in Δmrh5 and the precursor RNA containing both cox1 introns accumulated
PMID:34634819	PBO:0102226	(comment: ABOLISHED PROTEIN SPECIFIC TRANSLATION) Whereas newly-synthesized Cox2 and Cox3 were radioactively labeled, Cox1 synthesis was abolished although the mature cox1 mRNA was only slightly decreased in Δi cells, showing that Mrh5 is required for cox1 translation.
PMID:34634819	PBO:0119613	Cytb level was partly decreased in Δmrh5 and only slightly in the point mutant.
PMID:34634819	PBO:0119617	Cytb level was partly decreased in Δmrh5 and only slightly in the point mutant.
PMID:34634819	PBO:0119616	Western blot analysis was performed on the Δmrh5 and mrh5-G230E mutants, as well as the tagged Mrh5-cMyc strain (Figure 9C). The results showed that Mrh5 is a mitochondrial protein and that Cox1 and Cox2 were undetectable in both mutants.
PMID:34634819	PBO:0119615	Western blot analysis was performed on the Δmrh5 and mrh5-G230E mutants, as well as the tagged Mrh5-cMyc strain (Figure 9C). The results showed that Mrh5 is a mitochondrial protein and that Cox1 and Cox2 were undetectable in both mutants.
PMID:34634819	PBO:0119616	Western blot analysis was performed on the Δmrh5 and mrh5-G230E mutants, as well as the tagged Mrh5-cMyc strain (Figure 9C). The results showed that Mrh5 is a mitochondrial protein and that Cox1 and Cox2 were undetectable in both mutants.
PMID:34634819	PBO:0119615	Western blot analysis was performed on the Δmrh5 and mrh5-G230E mutants, as well as the tagged Mrh5-cMyc strain (Figure 9C). The results showed that Mrh5 is a mitochondrial protein and that Cox1 and Cox2 were undetectable in both mutants.
PMID:34634819	FYPO:0001437	The Δmrh5 mutation did not impair growth on antimycin containing medium, showing that ATPase activity is not affected (Figure 9A).
PMID:34634819	FYPO:0003730	We found that Δmrh5 was essential for respiratory growth, even in Δi background, suggesting that if Mrh5 is involved in intron excision, it also has another role.
PMID:34634819	FYPO:0000251	Second, we found that growth of Δmug178 cells on non-fermentable medium was restored by the ppr4, mrh5 or mrp51 suppressor alleles of Δcbp7 (Supplementary Figure S10A).
PMID:34634819	FYPO:0000251	Second, we found that growth of Δmug178 cells on non-fermentable medium was restored by the ppr4, mrh5 or mrp51 suppressor alleles of Δcbp7 (Supplementary Figure S10A).
PMID:34634819	FYPO:0000251	Second, we found that growth of Δmug178 cells on non-fermentable medium was restored by the ppr4, mrh5 or mrp51 suppressor alleles of Δcbp7 (Supplementary Figure S10A).
PMID:34634819	FYPO:0000251	Second, we found that growth of Δmug178 cells on non-fermentable medium was restored by the ppr4, mrh5 or mrp51 suppressor alleles of Δcbp7 (Supplementary Figure S10A).
PMID:34634819	FYPO:0000251	Second, we found that growth of Δmug178 cells on non-fermentable medium was restored by the ppr4, mrh5 or mrp51 suppressor alleles of Δcbp7 (Supplementary Figure S10A).
PMID:34634819	FYPO:0000251	Second, we found that growth of Δmug178 cells on non-fermentable medium was restored by the ppr4, mrh5 or mrp51 suppressor alleles of Δcbp7 (Supplementary Figure S10A).
PMID:34634819	PBO:0114789	(comment: ABOLISHED PROTEIN SPECIFIC TRANSLATION) Radioactive labeling of newly translated mitochondrial proteins showed that the combination of Δmug178 with either Δcbp7 or Δcbp8 abolished cytb translation while Δcbp7 Δcbp8 was similar to Δcbp8 (Figure 8B)
PMID:34634819	FYPO:0001437	but was not sensitive to antimycin A, showing that ATP synthase is not defective (Figure 7A-B)
PMID:34634819	FYPO:0003730	The Δmug178 mutant was unable to grow on non-fermentable medium and lacked spectrally detectable cytochromes b and c1 but was not sensitive to antimycin A, showing that ATP synthase is not defective (Figure 7A-B).
PMID:34634819	FYPO:0002060	On the contrary, the deletion of mug178 yielded viable cells.
PMID:34634819	FYPO:0002060	The mrp51 deletion could be obtained in the ptp1-1 strain, which allows S. pombe to remain alive without mtDNA (47)
PMID:34634819	FYPO:0002060	The mrp51 deletion could be obtained in the ptp1-1 strain, which allows S. pombe to remain alive without mtDNA (47)
PMID:34634819	FYPO:0002061	The complete absence of Mrp51 was unviable in a wild-type background. This is expected for an essential mitoribosomal protein because S. pombe is a petite- negative yeast, i.e. that cannot tolerate the complete loss of the mtDNA, or similarly a complete block in mitochondrial translation
PMID:34634819	FYPO:0005261	The strength of suppression by the mug178 or ppr7 plasmids was similar in terms of respiratory growth and cytochrome spectra (Figure 5A, B).
PMID:34634819	FYPO:0005261	The strength of suppression by the mug178 or ppr7 plasmids was similar in terms of respiratory growth and cytochrome spectra (Figure 5A, B).
PMID:34634819	FYPO:0005261	High copy suppressors were also searched for starting from the Δcbp8 deletion and identified the same genes (Table 2): mug178, ppr7 and zfs1, reinforcing the idea that Cbp7 and Cbp8 are acting at the same step of Cytb biogenesis.
PMID:34634819	FYPO:0005261	High copy suppressors were also searched for starting from the Δcbp8 deletion and identified the same genes (Table 2): mug178, ppr7 and zfs1, reinforcing the idea that Cbp7 and Cbp8 are acting at the same step of Cytb biogenesis.
PMID:34634819	GO:0005763	First, fractionations of mitochondria and post-mitochondrial supernatant in a double tagged strain showed that both are indeed mitochondrial proteins (Figure 6C). Second, western blot analysis of mitochondrial extracts from the double tagged strain fractionated on EDTA-sucrose gradients to separate both ribosomal subunits, showed that both tagged proteins co-sediment with the small ribosomal protein mS45 (Figure 6D). Third, immunoprecipitations performed under EDTA conditions showed that both Mrp51 and Mug178 did co-immunoprecipitate mS45 but not mL58 (Figure 6E).
PMID:34634819	GO:0005763	First, fractionations of mitochondria and post-mitochondrial supernatant in a double tagged strain showed that both are indeed mitochondrial proteins (Figure 6C). Second, western blot analysis of mitochondrial extracts from the double tagged strain fractionated on EDTA-sucrose gradients to separate both ribosomal subunits, showed that both tagged proteins co-sediment with the small ribosomal protein mS45 (Figure 6D). Third, immunoprecipitations performed under EDTA conditions showed that both Mrp51 and Mug178 did co-immunoprecipitate mS45 but not mL58 (Figure 6E).
PMID:34634819	FYPO:0005261	High copy suppressors were also searched for starting from the Δcbp8 deletion and identified the same genes (Table 2): mug178, ppr7 and zfs1, reinforcing the idea that Cbp7 and Cbp8 are acting at the same step of Cytb biogenesis.
PMID:34634819	FYPO:0005261	High copy suppressors were also searched for starting from the Δcbp8 deletion and identified the same genes (Table 2): mug178, ppr7 and zfs1, reinforcing the idea that Cbp7 and Cbp8 are acting at the same step of Cytb biogenesis.
PMID:34634819	FYPO:0005261	High copy suppressors were also searched for starting from the Δcbp8 deletion and identified the same genes (Table 2): mug178, ppr7 and zfs1, reinforcing the idea that Cbp7 and Cbp8 are acting at the same step of Cytb biogenesis.
PMID:34634819	FYPO:0005261	High copy suppressors were also searched for starting from the Δcbp8 deletion and identified the same genes (Table 2): mug178, ppr7 and zfs1, reinforcing the idea that Cbp7 and Cbp8 are acting at the same step of Cytb biogenesis.
PMID:34634819	FYPO:0005261	The strength of suppression by the mug178 or ppr7 plasmids was similar in terms of respiratory growth and cytochrome spectra (Figure 5A, B).
PMID:34634819	FYPO:0005261	The strength of suppression by the mug178 or ppr7 plasmids was similar in terms of respiratory growth and cytochrome spectra (Figure 5A, B).
PMID:34634819	FYPO:0005261	The strength of suppression by the mug178 or ppr7 plasmids was similar in terms of respiratory growth and cytochrome spectra (Figure 5A, B).
PMID:34634819	FYPO:0005261	The strength of suppression by the mug178 or ppr7 plasmids was similar in terms of respiratory growth and cytochrome spectra (Figure 5A, B).
PMID:34634819	FYPO:0003731	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34666001	PBO:0101579	(Figure 5)
PMID:34666001	PBO:0101580	In sharp contrast, Wsc1DSTR-GFP, Wsc1DWSC-GFP and Wsc1DSTRDWSC-GFP cells were completely devoid of any clustering phenotype, with an enrichment at contacts close to $2 (Figures 5D, 5E, and S2F-S2H).
PMID:34666001	PBO:0101581	increased lateral diffusion in membrane. Finally, Wsc1DWSC-GFP and Wsc1DSTR-GFP, which are incapable of clustering, exhibited much smaller half-times—closer to that of mCherry-Psy1 (Figures 6A, 6B, and S6A).
PMID:34666001	PBO:0101582	n these videos, we did not detect any lysis in WT red cells, but a high incidence of dying wsc1DCC-GFP of $26%
PMID:34666001	FYPO:0008012	In microchannels, where clusters form at high frequency, due to larger and more frequent compressive mechanical stresses onto the CWs, the survival behavior was markedly different. First, wsc1D cells exhibited a much higher yield of death of $28%. Second, all alleles exhibited a high yield of death around $25% including wsc1DWSC
PMID:34666001	FYPO:0008012	(comment: CHECK (vw: 25% cell death))
PMID:34666001	PBO:0101579	(Figure 5)
PMID:34666001	FYPO:0008003	(Figure 5)
PMID:34666001	PBO:0101579	(Figure 5)
PMID:34666001	PBO:0101579	(Figure 5)
PMID:34666001	PBO:0101579	(Figure 5)
PMID:34666001	PBO:0101579	(Figure 5)
PMID:34666001	PBO:0101579	(Figure 5)
PMID:34666001	PBO:0101579	(Figure 5)
PMID:34666001	PBO:0101579	(Figure 5)
PMID:34666001	PBO:0101579	(Figure 5)
PMID:34666001	PBO:0101579	(Figure 5)
PMID:34666001	PBO:0101579	(Figure 5)
PMID:34666001	PBO:0101579	(Figure 5)
PMID:34666001	PBO:0101579	(Figure 5)
PMID:34666001	FYPO:0008003	(Figure 5)
PMID:34666001	PBO:0101581	increased lateral diffusion in membrane. Finally, Wsc1DWSC-GFP and Wsc1DSTR-GFP, which are incapable of clustering, exhibited much smaller half-times—closer to that of mCherry-Psy1 (Figures 6A, 6B, and S6A).
PMID:34666001	FYPO:0008003	(Figure 5)
PMID:34666001	PBO:0101579	(Figure 5)
PMID:34666001	PBO:0101579	(Figure 5)
PMID:34666001	PBO:0101579	(Figure 5)
PMID:34666001	PBO:0101579	Remarkably, the Wsc1DCC-GFP lacking a large fraction of the cytoplasmic C-terminal tail, and thus presumably defective in downstream signal transduction was dispensable for clustering. This finding reinforces the notion that Wsc1 clustering occurs independently of downstream CWI signaling.
PMID:34666001	PBO:0101580	In sharp contrast, Wsc1DSTR-GFP, Wsc1DWSC-GFP and Wsc1DSTRDWSC-GFP cells were completely devoid of any clustering phenotype, with an enrichment at contacts close to $2 (Figures 5D, 5E, and S2F-S2H).
PMID:34666001	PBO:0101580	In sharp contrast, Wsc1DSTR-GFP, Wsc1DWSC-GFP and Wsc1DSTRDWSC-GFP cells were completely devoid of any clustering phenotype, with an enrichment at contacts close to $2 (Figures 5D, 5E, and S2F-S2H).
PMID:34666001	PBO:0101578	Together, these results indicate that Wsc1 clustering may be triggered by local surface compression, independently of putative ‘‘trans’’ homotypic interactions between extracellular sensors from neighbor cells or general cell-to-cell signaling.
PMID:34666001	PBO:0101579	(Figure 5)
PMID:34666001	PBO:0101579	(Figure 5)
PMID:34674264	PBO:0094514	(Fig. 2B). Dma1-6D/E auto-ubiquitination was modestly but reproducibly reduced relative to wild-type. Specifically, while 82% of wild-type Dma1 became ubiquitinated on at least one site, 71% of Dma1-6D/E did.
PMID:34674264	PBO:0094516	(Fig. 2A-C). Reduced contractile ring localization during mitosis. However, we observed that Dma1-6A was significantly more difficult to detect at the first instance of CR localization early in mitosis than either Dma1 or Dma1-6D/E
PMID:34674264	PBO:0094517	Normal localization to medial cortical nodes, SPB, and division septum as wild-type
PMID:34674264	PBO:0094517	Normal localization to medial cortical nodes, mitotic contractile ring, SPB, and septum as wild-type
PMID:34674264	FYPO:0003762	(Fig. 4a) We observed that nda3-km311, dma1- 6A nda3-km311, and dma1-6D/E nda3-km311 cells delayed septation relative to wild-type cells and that dma1Δ cells did not
PMID:34674264	FYPO:0003762	(Fig. 4a)
PMID:34674264	PBO:0094518	Localization to SPBs at the same level as wild-type during spindle stress
PMID:34674264	FYPO:0000776	(comment: CHECK ALLELELS) we combined analog-sensitive (cdc2-as, orb5-as) and temperature-sensitive (plo1-1) alleles. Despite these kinases targeting Dma1 in vitro, we found no evidence that inhibiting any of them singly (not shown) or together (Fig. 1G) changed Dma1 phosphostatus as monitored by SDS/PAGE mobility suggesting that these kinases are not responsible for regulating Dma1 phosphostatus in cells.
PMID:34674264	PBO:0094520	Normal localization to medial cortical nodes, SPB, and division septum as wild-type
PMID:34674264	PBO:0094511	(comment: CHECK in vitro assay)
PMID:34674264	PBO:0093475	(comment: CHECK in vitro kinase assay showed S166 is phosphorylated by Cdk1)
PMID:34674264	PBO:0094506	(comment: CHECK in vitro kinase assay showed S251 is phosphorylated by Plo1)
PMID:34674264	PBO:0094507	(comment: CHECK in vitro kinase assay showed T18, S20, and S266 are phosphorylated by CK2)
PMID:34674264	PBO:0094512	(comment: CHECK Decreased Dma1 auto-ubiquitination by in vitro assay)
PMID:34674264	PBO:0094513	(Fig. 2B). (comment: CHECK Almost abolished Dma1 auto-ubiquitination by in vitro assay)
PMID:34674264	MOD:00046	(comment: in vivo phosphorylation sites identified by mass spectrometry)
PMID:34674264	MOD:00047	(comment: in vivo phosphorylation site identified by mass spectrometry)
PMID:34674264	PBO:0098166	(comment: CHECK in vitro kinase assay showed T18, S20, and S266 are phosphorylated by CK2)
PMID:34674264	PBO:0094507	(comment: CHECK in vitro kinase assay showed T18, S20, and S266 are phosphorylated by CK2)
PMID:34674264	PBO:0094509	Although this assay is not quantitative, we found that Sid4 was ubiquitinated to similar levels as in wild-type in both dma1-6A and dma1-6D/E but was not ubiquitinated in dma1D (Fig. 2A).
PMID:34674264	PBO:0094517	Localization to SPBs at the same level as wild-type during spindle stress
PMID:34686329	GO:0110078	(Figure 1A)
PMID:34686329	GO:0110078	(Figure 1A)
PMID:34686329	GO:0110078	Altogether, our quantitative proteomic analyses indicate that Tti2, Tel2, and Tti1, together with Asa1, form a stable multi-meric complex that interacts with most PIKKs in S. pombe (Figure 1A)
PMID:34686329	FYPO:0000705	(comment: Abolished incorporation of Tra1 into SAGA complex)
PMID:34686329	FYPO:0000705	(comment: Abolished incorporation of Tra1 into SAGA complex)
PMID:34686329	FYPO:0000705	(comment: Abolished incorporation of Tra1 into SAGA complex)
PMID:34686329	FYPO:0000705	(comment: Abolished incorporation of Tra1 into SAGA complex)
PMID:34686329	FYPO:0000705	(comment: Abolished incorporation of Tra1 into SAGA complex)
PMID:34686329	PBO:0109900	(Figure 7A)
PMID:34686329	PBO:0109869	(Figure 7A)
PMID:34686329	GO:0051083	(Figures 2A and 2B). To determine whether this interaction occurs cotranslationally, we then repeated Tti1 RIPs in cells treated either with puromycin, an inhibitor of translation elongation, or with EDTA, which dissociates ribosomes. Both treatments abolished Tti1 binding to tra1+ (Figure 2C).
PMID:34686329	GO:0051083	(Figures 2A and 2B). To determine whether this interaction occurs cotranslationally, we then repeated Tti1 RIPs in cells treated either with puromycin, an inhibitor of translation elongation, or with EDTA, which dissociates ribosomes. Both treatments abolished Tti1 binding to tra1+ (Figure 2C).
PMID:34686329	PBO:0109908	Tti1 caused a strong decrease of Tti2 and Tel2 binding (Figure 2J).
PMID:34686329	PBO:0109963	We conclude that Tti1, and to a lesser extent Tti2, recruits TTT to nascent Tra1 polypeptides
PMID:34686329	PBO:0109963	We conclude that Tti1, and to a lesser extent Tti2, recruits TTT to nascent Tra1 polypeptides
PMID:34686329	FYPO:0002430	(Figure 6I)
PMID:34686329	FYPO:0002430	(Figure 6I)
PMID:34686329	PBO:0109899	(Figure 6F)
PMID:34686329	PBO:0109898	(Figure 6H)
PMID:34686329	PBO:0109898	(Figure 6H)
PMID:34686329	FYPO:0000847	(Figure 6J)
PMID:34686329	PBO:0109866	RNA-seq
PMID:34686329	PBO:0093580	(Figure 6B)
PMID:34686329	PBO:0093581	(Figure 6B)
PMID:34686329	PBO:0109896	(Figure 3E)
PMID:34686329	PBO:0109896	(Figure 3E)
PMID:34686329	PBO:0109893	(Figure 3E)
PMID:34686329	PBO:0109897	(Figure 3E)
PMID:34686329	PBO:0109897	(Figure 3E)
PMID:34686329	PBO:0109890	(Figure 2C) Abolished interaction between Tti2 protein and tra1 mRNA
PMID:34686329	PBO:0093612	(Figure 6B)
PMID:34686329	PBO:0093576	(Figure 6B)
PMID:34686329	PBO:0100916	(Figure 6B)
PMID:34686329	PBO:0093580	(Figure 6B)
PMID:34686329	PBO:0109866	RNA-seq
PMID:34686329	PBO:0093580	(Figure 6B)
PMID:34686329	PBO:0109888	Surprisingly, despite a strong decrease of Tor2 steady-state levels, its stability appears unaffected, even increasing 6 h after CHX treatment. It is possible that Tor2 is subjected to rapid turnover and compensatory mechanisms boosting its synthesis.
PMID:34686329	PBO:0109882	(Figure 2H)
PMID:34686329	PBO:0109881	In contrast, Tti2 and Tti1 interaction with tra1+ does not change in the absence of Tel2 (Figure 2I)
PMID:34686329	PBO:0109880	(Figure 3C)
PMID:34686329	PBO:0109871	Western blotting followed by quantification of signal intensities showed that both the steady-state levels and the stability of Tra1, Tra2, and Tor1 decrease following Tti2 depletion (Figures 1C-1F).
PMID:34686329	PBO:0109872	Western blotting followed by quantification of signal intensities showed that both the steady-state levels and the stability of Tra1, Tra2, and Tor1 decrease following Tti2 depletion (Figures 1C-1F).
PMID:34686329	PBO:0109873	Western blotting followed by quantification of signal intensities showed that both the steady-state levels and the stability of Tra1, Tra2, and Tor1 decrease following Tti2 depletion (Figures 1C-1F).
PMID:34686329	FYPO:0001355	Depletion of each protein reduces S. pombe viability and proliferation compared with control strains and culture conditions (Figures S1C and S1D).
PMID:34686329	FYPO:0001355	(Figures S1C and S1D).
PMID:34686329	PBO:0109880	(Figure 3C)
PMID:34686329	FYPO:0001355	(Figures S1C and S1D).
PMID:34686329	PBO:0109874	We used qRT-PCR to determine the effect of TTT depletion on the expression of two sexual differentiation genes, ste11+ and mei2+. We observed that the mRNA levels of both genes increase upon depletion of Tel2, Tti1, and Tti2 compared with control strains and conditions (Figures S1E and S1F)
PMID:34686329	PBO:0102818	We used qRT-PCR to determine the effect of TTT depletion on the expression of two sexual differentiation genes, ste11+ and mei2+. We observed that the mRNA levels of both genes increase upon depletion of Tel2, Tti1, and Tti2 compared with control strains and conditions (Figures S1E and S1F)
PMID:34686329	PBO:0109874	(Figures S1E and S1F)
PMID:34686329	PBO:0102818	(Figures S1E and S1F)
PMID:34686329	PBO:0109874	(Figures S1E and S1F)
PMID:34686329	PBO:0102818	(Figures S1E and S1F)
PMID:34686329	PBO:0109875	Western blotting showed decreased phosphorylation of the ribosomal protein S6, a canonical TORC1 substrate, following Tel2, Tti1, and Tti2 depletion (Figure S1G)
PMID:34686329	PBO:0109878	(Figure 3D)
PMID:34686329	PBO:0109878	(Figure 3D)
PMID:34686329	PBO:0109876	Western blotting showed decreased phosphorylation of the ribosomal protein S6, a canonical TORC1 substrate, following Tel2, Tti1, and Tti2 depletion (Figure S1G)
PMID:34686329	PBO:0109875	(Figure S1G)
PMID:34686329	PBO:0109876	(Figure S1G)
PMID:34686329	PBO:0109875	(Figure S1G)
PMID:34686329	PBO:0109876	(Figure S1G)
PMID:34686329	PBO:0109877	(Figure S4C)
PMID:34686329	PBO:0109878	(Figure 3C)
PMID:34686329	PBO:0109879	(Figure S5)
PMID:34686329	PBO:0109878	(Figure S4C)
PMID:34686329	PBO:0109877	(Figure S4C)
PMID:34686329	PBO:0109878	(Figure 3D)
PMID:34686329	PBO:0109905	Finally, our published transcriptomic analysis of tti2-CKO mutants showed that PIKK mRNA levels remain unaffected following Tti2 depletion (FigureS1H)
PMID:34686329	PBO:0109906	Finally, our published transcriptomic analysis of tti2-CKO mutants showed that PIKK mRNA levels remain unaffected following Tti2 depletion (FigureS1H)
PMID:34686329	PBO:0109907	Finally, our published transcriptomic analysis of tti2-CKO mutants showed that PIKK mRNA levels remain unaffected following Tti2 depletion (FigureS1H)
PMID:34686329	GO:0005737	(Figure S2B).
PMID:34686329	GO:0005634	Tel2 does not localize to the nucleus in standard growth conditions (Figure S2B).
PMID:34686329	PBO:0109904	Finally, our published transcriptomic analysis of tti2-CKO mutants showed that PIKK mRNA levels remain unaffected following Tti2 depletion (FigureS1H)
PMID:34686329	GO:0051083	Conventional and qRT-PCR analyses revealed a specific enrichment of the tra1+ mRNA in RIPs of all three TTT subunits, Tel2, Tti1, and Tti2, compared with several negative controls (Figures 2A and 2B). To determine whether this interaction occurs cotranslationally, we then repeated Tti1 RIPs in cells treated either with puromycin, an inhibitor of translation elongation, or with EDTA, which dissociates ribosomes. Both treatments abolished Tti1 binding to tra1+ (Figure 2C).
PMID:34706246	PBO:0119343	(Fig. 5D)
PMID:34706246	PBO:0119343	(Fig. 5D)
PMID:34706246	PBO:0119342	(Fig. 5D)
PMID:34706246	PBO:0119340	(Fig. 5D)
PMID:34706246	PBO:0119342	(Fig. 5D)
PMID:34706246	PBO:0119341	(Fig. 5D)
PMID:34706246	PBO:0119340	(Fig. 5D)
PMID:34706246	PBO:0119339	(Fig. 4)
PMID:34706246	PBO:0119339	(Fig. 4)
PMID:34706246	PBO:0119337	(Fig. 2C)
PMID:34706246	PBO:0119338	(Fig. 2D)
PMID:34706246	PBO:0119337	(Fig. 2C)
PMID:34731638	FYPO:0002360	(Figure 1 G)
PMID:34731638	FYPO:0004742	(Figure S2F)
PMID:34731638	FYPO:0005917	we observed derepression of several subtelomeric genes (Figures 2E and S2G).
PMID:34731638	FYPO:0007480	(Figure 2D) reduced heterochromatin spreading at mating-type and subtelomeric heterochromatin
PMID:34731638	PBO:0094681	(Figure 1B) In contrast, there was a substantial reduction of H3K9me2 at the mating-type locus, in agreement with a previous study (Holla et al., 2020) (Figure S1A), and at the subtelomeres
PMID:34731638	PBO:0101104	(Figures 1B, 1C, S1D) only a subtle change of H3K9me2 at pericentromere
PMID:34731638	PBO:0101105	(Figure 2C) Conversely, in the pob3Δ strain, the orange reporter was also fully derepressed in the majority of cells, yet the green reporter remained silenced or mildly derepressed. This result implies that pob3Δ cells have a heterochromatin spreading defect
PMID:34731638	FYPO:0007892	Nonetheless, the pob3Δ mutant exhibited increased incorporation of H3-T7 at the TEL1L region (Figure 4G), implying that the H3 turnover rate is increased at subtelomeric heterochromatin.
PMID:34731638	FYPO:0004604	(Figure 4E)
PMID:34731638	FYPO:0003412	(Figure 4E)
PMID:34731638	FYPO:0004577	Intriguingly, while H3K9me2 levels were unaltered in spt16-1, H3K9me3 levels were reduced at several loci at the TEL1L subtelomeric region (i.e., SPAC212.09c, SPAC212.08c, and SPAC212.06c; compare Figure 4B with 4A)
PMID:34731638	FYPO:0003412	synthetic defect in the silencing of dg and tlh1/2 transcripts (Figure 4C)
PMID:34731638	FYPO:0003412	(Figure 4E)
PMID:34731638	FYPO:0004604	(Figure 4E)
PMID:34731638	FYPO:0006299	(Figure 1F)
PMID:34731638	FYPO:0004542	(Figure 1F)
PMID:34731638	FYPO:0002360	(comment: vw: changed from decreased to normal because look WT?)
PMID:34731638	FYPO:0003555	(Figure 1 G)
PMID:34731638	FYPO:0006299	(fig 1G ) (comment: vw: changed to increased -compared to WT)
PMID:34731638	PBO:0101106	(fig 1G ) (comment: vw: changed to increased -compared to WT)
PMID:34731638	FYPO:0002360	Moreover, epe1Δ reduced the expression of several subtelomeric genes in pob3Δ, suggesting that it also counteracts heterochromatin spreading (Figure 3G)
PMID:34731638	FYPO:0004604	Partial suppression of pob3∆ silencing phenotype.
PMID:34731638	FYPO:0002336	To test this more directly, we performed the HSS assay in the double spt16-1epe1Δ mutant. Indeed, heterochromatin spreading was completely restored (Figure 3H, compare with Figure 2D)
PMID:34731638	FYPO:0007894	(Figures 1E and S1D) we found increased signals of elongating RNAPII (RNAPII Ser2P) and H2B ubiquitination (H2Bub), a histone mark associated with active transcription
PMID:34731638	GO:0000791	(Figure S1E)
PMID:34731638	PBO:0101107	(Figures S2C-S2E) in chromatin/euchromatin
PMID:34731638	PBO:0101108	(Figures S2C-S2E) in chromatin/euchromatin
PMID:34731638	FYPO:0002387	Although degradation of Epe1 still occurs in pob3Δ in S phase, we found increased steady-state levels of Epe1 in cycling cells (Figure S3A).
PMID:34731638	PBO:0101110	found reduced Swi6 binding in spt16-1 at subtelomeric genes close to the heterochromatin boundary (SPAC212.12, SPAC212.06c; Figure 4D).
PMID:34731638	PBO:0101111	(Figures S4A-S4C) Histone H3 ChIP-seq revealed a small but reproducible reduction of H3 at subtelomeres in pob3Δ
PMID:34731638	PBO:0101112	(Figures S4A-S4C) Histone H3 ChIP-seq revealed a small but reproducible reduction of H3 at subtelomeres in pob3Δ
PMID:34731638	PBO:0101113	(Figures S4A-S4C) Histone H3 ChIP-seq revealed a small but reproducible reduction of H3 at subtelomeres in pob3Δ
PMID:34731638	FYPO:0007891	(Figure 2D) reduced heterochromatin spreading at mating-type and subtelomeric heterochromatin
PMID:34731638	FYPO:0007895	(Figures 1E and S1D) we found increased signals of elongating RNAPII (RNAPII Ser2P) and H2B ubiquitination (H2Bub), a histone mark associated with active transcription
PMID:34731638	FYPO:0005917	we observed derepression of several subtelomeric genes (Figures 2E and S2G).
PMID:34738170	FYPO:0001357	A serial dilution spotting assay (Fig. 2B) showed that the growth of och1Δ with either pAL-pwp1+ or pAU-pwp1+ was as fast as that of wild-type cells, indicating that the growth defect of och1Δ cells was alleviated by expression of pwp1+.
PMID:34738170	FYPO:0001357	A serial dilution spotting assay (Fig. 2B) showed that the growth of och1Δ with either pAL-pwp1+ or pAU-pwp1+ was as fast as that of wild-type cells, indicating that the growth defect of och1Δ cells was alleviated by expression of pwp1+.
PMID:34738170	FYPO:0001357	A serial dilution spotting assay (Fig. 2B) showed that the growth of och1Δ with either pAL-pwp1+ or pAU-pwp1+ was as fast as that of wild-type cells, indicating that the growth defect of och1Δ cells was alleviated by expression of pwp1+.
PMID:34798057	FYPO:0000708	Both mutants displayed meiosis defects with a reduction in gamete numbers and viability more marked in the nda2noD mutant (Figures 6A, 6B, and 6C).
PMID:34798057	PBO:0093564	(comment: weird!) Intriguingly, the double nda2noD nda3noD mutant was less sensitive than the single ones. Therefore, a possible explanation for the lower sensitivity of the double mutant is that defects resulting from the elevated level of one monomer are compensated for by a similar overexpression of the second monomer.
PMID:34798057	PBO:0093564	(Figure S7A)
PMID:34798057	PBO:0093562	(Figure S7A)
PMID:34798057	FYPO:0000708	(Figure S1D)
PMID:34798057	PBO:0100613	(comment: CHECK V348A)
PMID:34798057	FYPO:0005599	(Figure 6E) When dus3D diploids were induced to enter meiosis, the time needed in prophase for spindle assembly in MI was increased, while a marked increase in the duration of metaphase was noted in both MI and MII (Figures 6D-6H).
PMID:34798057	FYPO:0002091	(Figures 6I, 6J)
PMID:34805795	PBO:0108106	(comment: CONDITION during amino acid starvation)
PMID:34805795	PBO:0108097	(Figure 5)
PMID:34805795	PBO:0108097	(Figure 5)
PMID:34805795	PBO:0108097	(Figure S1A)
PMID:34805795	PBO:0108097	(Figure S1A)
PMID:34805795	PBO:0099985	results in a significant growth advantage of BFC mutant over wild-type strains when equal number of log phase cells are grown on rapamycin-containing EMM plates supplemented with amino acids (Figures S1A and S1B). Moreover, treating cells with 125 or 150 ng/mL of rapamycin for 90 min revealed that the growth advantage of BFC mutants correlates with an increase in P-Rps6 levels compared to wild-type cells (Figure S5C). Together, these data support a model in which BFC participates in TORC1 repression.
PMID:34805795	PBO:0117221	Bhd1 and Fnp1 appear diffusely distributed throughout the cytoplasm in amino acid replete conditions, but localize to vacuoles in response to amino acid starvation evidenced by the strong overlap between Bhd1-/Fnp1-GFP and the FM4-64 dye under amino acid starvation conditions (Figures 2A-2F)
PMID:34805795	FYPO:0007909	(Figure 4d) (comment: vw: assayed vacuolar pH as a surrogate for V-ATPase activity)
PMID:34805795	FYPO:0001159	(Figure 4d) (comment: vw: assayed vacuolar pH as a surrogate for V-ATPase activity)
PMID:34805795	PBO:0108099	(Figure 4F) (comment: CONDITION ph9)
PMID:34805795	PBO:0108099	(Figure 4F) (comment: CONDITION ph9)
PMID:34805795	FYPO:0006266	(Figure S1A)
PMID:34805795	FYPO:0006266	(Figure S1A)
PMID:34805795	PBO:0108101	(Figure S3) Bhd1 and Fnp1 localize to vacuoles in response to amino acid starvation and that this localization is largely independent of the presence of the other protein.
PMID:34805795	PBO:0108102	(Figure S3) Bhd1 and Fnp1 localize to vacuoles in response to amino acid starvation and that this localization is largely independent of the presence of the other protein.
PMID:34805795	PBO:0108103	(comment: CONDITION during amino acid supplementation) (Figures 2G and S4), demonstrating that the BFC, is required for efficient activation of TORC1 following amino acid supplementation.
PMID:34805795	PBO:0108103	(comment: CONDITION during amino acid supplementation) (Figures 2G and S4), demonstrating that the BFC, is required for efficient activation of TORC1 following amino acid supplementation.
PMID:34805795	PBO:0108104	BFC augments TORC1 activation in response to amino acid stimulation
PMID:34805795	PBO:0108106	(comment: CONDITION during amino acid starvation)
PMID:34810257	PBO:0101615	Cnp20-14A showed a strong interaction with Ccp1 (Fig. 5F)
PMID:34810257	PBO:0101613	Yeast two hybrid To investigate how phosphorylation of the CIM domain affects the interaction between Ccp1 and CENP-TCnp20, we conducted yeast two-hybrid assays with Cnp20-14D and Ccp1. We found that the interaction between Cnp20-14D and Ccp1 was dramatically reduced (Fig. 5F).
PMID:34810257	PBO:0101620	Consistent with the key role of CENP-TCnp20 in the assembly of the Ndc80 complex, we found that the association of Ndc80-GFP with centromeres is lost in cnp20-9 at the restrictive temperature (Fig. 2 C and D).
PMID:34810257	PBO:0101612	We found that GFP-Ccp1 was delocalized from centromeres at the restrictive temperature in cnp20-9 at all stages of the cell cycle (Fig. 2 E and F and SI Appendix, Fig. S3)
PMID:34810257	PBO:0101621	whereas the localization of GFP-Ccp1 at centromeres only has a mild reduction in the CENP-A ts mutant, cnp1-1 (SI Appendix, Fig. S4).
PMID:34810257	PBO:0101622	We next checked the distribution of CENP-TCnp20-GFP in ccp1Δ and found that its centromere localization was unaffected in the mutant (Fig. 2 G-I).
PMID:34810257	PBO:0101623	whereas the localization of GFP-Ccp1 at centromeres only has a mild reduction in the CENP-A ts mutant, cnp1-1 (SI Appendix, Fig. S4).
PMID:34810257	PBO:0101624	In addition, we found that CENP-ACnp1-GFP partially reduced its centromere localization in cnp20-9 at the restrictive temperature (SI Appendix, Fig. S6).
PMID:34810257	PBO:0101625	(These data suggest that phosphorylation of the CIM domain leads to disassociation of Ccp1 from centromeres. CIM domain) Together,our data indicate that CENP-TCnp20 is required for Ccp1 centromere localization
PMID:34810257	PBO:0101612	But GFP-Ccp1 is completely disassociated from centromeric regions in cnp20-ΔCIM at all stages of the cell cycle (Fig. 4 C and D and SI Appendix, Fig. S13).
PMID:34810257	PBO:0101627	(comment: CHECK during mitotc M-phase) In contrast, we found that GFP-Ccp1 in all cnp20-14A mutant cells remains associated with centromeres during all the stages of the cell cycle (Fig. 6 B and C).
PMID:34810257	FYPO:0000141	But most cnp20-14A cells display mitotic delay, and more than 12% of mutant cells failed to complete chromosome segregation within 30 min (Fig. 6 E and F)
PMID:34810257	PBO:0112401	(Fig. 3) Our results indicate that the first 55 amino acids of CENP-TCnp20 are the minimal interaction domain with Ccp1, which we named the Ccp1- interacting motif (CIM). Yeast two hybrid
PMID:34810257	PBO:0101628	((comment: CHECK ndc80) These co-IP experiments showed that the interaction between Ndc80 and CENP-TCnp20 is drastically increased during mitosis (Fig. 7C), supporting the idea that the presence of Ccp1 interferes with the interaction between Ndc80 and CENP-TCnp2
PMID:34810257	PBO:0101629	These data demonstrate that CDK1 is capable of phosphorylating the CIM domain of CENP-TCnp20. Various slow migrating bands were observed in the assay with Cnp201-55 (Fig. 7D), indicating that the domain contains multiple phosphorylation sites, consistent with our point mutation analysis. (ASSAYED USING HUMAN CDK1)
PMID:34810257	PBO:0112400	Yeast two hybrid The yeast two-hybrid assays showed that the Ccp1 homodimer mutant, Ccp1-4A, was unable to interact with CENP-TCnp20 (Fig. 3A and SI Appendix, Fig. S8)
PMID:34810257	FYPO:0000091	We found that cnp20-14A is highly sensitive to TBZ, even more strongly than the cnp20-ΔCIM mutant (Fig. 6D and SI Appendix, Fig. S16)
PMID:34810257	PBO:0112398	(Fig. 3) Our results indicate that the first 55 amino acids of CENP-TCnp20 are the minimal interaction domain with Ccp1, which we named the Ccp1- interacting motif (CIM).
PMID:34810257	FYPO:0000091	(Fig. 4 E and F).
PMID:34810257	PBO:0112397	However, we found that Spc25-GFP appeared not to attach to microtubules in ∼20% of cnp20-14A mitotic cells, indicating that dephosphorylation of the CIM domain leads to mislocalization of Ndc80C during mitosis (Fig. 7A). Importantly, our co-IP results indicated that the interaction between Cnp20-14A and Ndc80 is significantly reduced during mitosis (Fig. 7B).
PMID:34849791	FYPO:0000674	Supplemental Figure S3B
PMID:34849791	FYPO:0000082	Supplemental Figure S5B
PMID:34849791	PBO:0094560	(Figure 4)
PMID:34849791	FYPO:0000964	Supplemental Figure S3B
PMID:34849791	FYPO:0000674	Supplemental Figure S3B
PMID:34849791	FYPO:0000674	Supplemental Figure S2B
PMID:34849791	FYPO:0000964	Supplemental Figure S2B
PMID:34849791	PBO:0094562	(Figure 4)
PMID:34849791	FYPO:0000674	Supplemental Figure S2B
PMID:34849791	FYPO:0000964	Supplemental Figure S2B
PMID:34849791	PBO:0094559	(Figure 4)
PMID:34849791	FYPO:0000674	Supplemental Figure S2B
PMID:34849791	FYPO:0000964	Supplemental Figure S2B
PMID:34849791	FYPO:0000674	Supplemental Figure S2B
PMID:34849791	FYPO:0000964	Supplemental Figure S2B
PMID:34849791	FYPO:0000674	Supplemental Figure S3B
PMID:34849791	FYPO:0000964	Supplemental Figure S3B
PMID:34849791	PBO:0094559	(Figure 4)
PMID:34849791	FYPO:0000674	Supplemental Figure S3B
PMID:34849791	FYPO:0000964	Supplemental Figure S3B
PMID:34849791	PBO:0094561	(Figure 4)
PMID:34849791	FYPO:0000674	Supplemental Figure S3B
PMID:34849791	FYPO:0000964	Supplemental Figure S3B
PMID:34849791	FYPO:0000964	Supplemental Figure S3B
PMID:34849791	FYPO:0000964	Supplemental Figure S5B
PMID:34849791	PBO:0094561	(Figure 4)
PMID:34849791	PBO:0094562	(Figure 4)
PMID:34849791	FYPO:0000082	Supplemental Figure S5B
PMID:34849791	FYPO:0000964	Supplemental Figure S5B
PMID:34849791	PBO:0094563	(Figure 4)
PMID:34849791	FYPO:0000082	Supplemental Figure S5B
PMID:34849791	FYPO:0000964	Supplemental Figure S5B
PMID:34849791	PBO:0094566	(Figure 4)
PMID:34849791	FYPO:0000082	Supplemental Figure S5B
PMID:34849791	FYPO:0000964	Supplemental Figure S5B
PMID:34849791	PBO:0094559	(Figure 4)
PMID:34849791	FYPO:0000674	Supplemental Figure S5B
PMID:34849791	FYPO:0000964	Supplemental Figure S5B
PMID:34849791	PBO:0094559	(Figure 4)
PMID:34849791	FYPO:0000674	Supplemental Figure S5B
PMID:34849791	FYPO:0000964	Supplemental Figure S5B
PMID:34849791	FYPO:0000082	(Figure 3A)
PMID:34849791	FYPO:0000964	(Figure 3B)
PMID:34849791	FYPO:0001513	(Figure 4)
PMID:34849791	PBO:0094562	(Figure 4)
PMID:34849791	FYPO:0000082	(Figure 3A)
PMID:34849791	FYPO:0000964	(Figure 3B)
PMID:34849791	PBO:0094563	(Figure 4)
PMID:34849791	FYPO:0000082	(Figure 3A)
PMID:34849791	FYPO:0000964	(Figure 3B)
PMID:34849791	PBO:0094560	(Figure 4)
PMID:34849791	FYPO:0000674	(Figure 3A)
PMID:34849791	FYPO:0000964	(Figure 3B)
PMID:34849791	PBO:0094567	(Figure 4)
PMID:34849791	FYPO:0000082	(Figure 3A)
PMID:34849791	FYPO:0000964	(Figure 3B)
PMID:34849791	PBO:0094567	(Figure 4)
PMID:34849791	FYPO:0000082	(Figure 3A)
PMID:34849791	FYPO:0000964	(Figure 3B)
PMID:34849791	FYPO:0000674	Supplemental Figure S4B
PMID:34849791	FYPO:0000964	Supplemental Figure S4B
PMID:34849791	FYPO:0001513	(Figure 4)
PMID:34849791	PBO:0094562	(Figure 4)
PMID:34849791	FYPO:0000964	Supplemental Figure S4B
PMID:34849791	FYPO:0000674	Supplemental Figure S4B
PMID:34849791	PBO:0094560	(Figure 4)
PMID:34849791	FYPO:0000964	Supplemental Figure S4B
PMID:34849791	FYPO:0000674	Supplemental Figure S4B
PMID:34849791	PBO:0094566	(Figure 4)
PMID:34849791	FYPO:0000964	Supplemental Figure S4B
PMID:34849791	FYPO:0000082	Supplemental Figure S4B
PMID:34849791	PBO:0094559	(Figure 4)
PMID:34849791	FYPO:0000964	Supplemental Figure S4B
PMID:34849791	FYPO:0000082	Supplemental Figure S4B
PMID:34849791	PBO:0094560	(Figure 4)
PMID:34849791	FYPO:0000964	Supplemental Figure S4B
PMID:34849791	FYPO:0000082	Supplemental Figure S4B
PMID:34849791	FYPO:0000674	Supplemental Figure S6B
PMID:34849791	FYPO:0000964	Supplemental Figure S6B
PMID:34849791	FYPO:0001513	(Figure 4)
PMID:34849791	PBO:0094565	(Figure 4)
PMID:34849791	FYPO:0000674	Supplemental Figure S6B
PMID:34849791	FYPO:0000964	Supplemental Figure S6B
PMID:34849791	PBO:0094560	(Figure 4)
PMID:34849791	FYPO:0000674	Supplemental Figure S6B
PMID:34849791	FYPO:0000964	Supplemental Figure S6B
PMID:34849791	PBO:0094564	(Figure 4)
PMID:34849791	FYPO:0000674	Supplemental Figure S6B
PMID:34849791	FYPO:0000964	Supplemental Figure S6B
PMID:34849791	PBO:0094559	(Figure 4)
PMID:34849791	FYPO:0000674	Supplemental Figure S6B
PMID:34849791	FYPO:0000964	Supplemental Figure S6B
PMID:34849791	PBO:0094559	(Figure 4)
PMID:34849791	FYPO:0000674	Supplemental Figure S6B
PMID:34849791	FYPO:0000964	Supplemental Figure S6B
PMID:34849791	FYPO:0000674	Supplemental Figure S1B
PMID:34849791	FYPO:0000964	Supplemental Figure S1B
PMID:34849791	FYPO:0001513	(Figure 4)
PMID:34849791	PBO:0094561	(Figure 4)
PMID:34849791	FYPO:0000674	Supplemental Figure S1B
PMID:34849791	FYPO:0000964	Supplemental Figure S1B
PMID:34849791	PBO:0094565	(Figure 4)
PMID:34849791	FYPO:0000674	Supplemental Figure S1B
PMID:34849791	FYPO:0000964	Supplemental Figure S1B
PMID:34849791	PBO:0094564	(Figure 4)
PMID:34849791	FYPO:0000674	Supplemental Figure S1B
PMID:34849791	FYPO:0000964	Supplemental Figure S1B
PMID:34849791	PBO:0094563	(Figure 4)
PMID:34849791	FYPO:0000674	Supplemental Figure S1B
PMID:34849791	FYPO:0000964	Supplemental Figure S1B
PMID:34849791	PBO:0094562	(Figure 4)
PMID:34849791	FYPO:0000674	Supplemental Figure S1B
PMID:34849791	FYPO:0000964	Supplemental Figure S1B
PMID:34849791	FYPO:0000674	Supplemental Figure S2B
PMID:34849791	FYPO:0000964	Supplemental Figure S2B
PMID:34849791	FYPO:0001513	(Figure 4)
PMID:34849791	PBO:0094561	(Figure 4)
PMID:34849791	FYPO:0000674	Supplemental Figure S2B
PMID:34849791	FYPO:0000964	Supplemental Figure S2B
PMID:34849791	PBO:0094559	(Figure 4)
PMID:34849791	FYPO:0001513	(Figure 4)
PMID:34849791	FYPO:0000964	(Figure 3B)
PMID:34849791	FYPO:0000674	(Figure 3A)
PMID:34849791	FYPO:0000091	(Figure 3B)
PMID:34849791	FYPO:0000082	(Figure 3A)
PMID:34849791	PBO:0094554	(Figure 4)
PMID:34849791	FYPO:0000091	(Figure 3B)
PMID:34849791	FYPO:0000082	(Figure 3A)
PMID:34849791	PBO:0094555	(Figure 4)
PMID:34849791	FYPO:0000091	(Figure 3B)
PMID:34849791	FYPO:0000082	(Figure 3A)
PMID:34849791	PBO:0094556	(Figure 4)
PMID:34849791	FYPO:0000091	(Figure 3B)
PMID:34849791	FYPO:0000082	(Figure 3A)
PMID:34849791	PBO:0094557	(Figure 4)
PMID:34849791	FYPO:0000091	(Figure 3B)
PMID:34849791	FYPO:0000082	(Figure 3A)
PMID:34849791	PBO:0094558	(Figure 4)
PMID:34849791	PBO:0094559	(Figure 4)
PMID:34849791	FYPO:0001513	(Figure 4)
PMID:34849791	FYPO:0000964	Supplemental Figure S3B
PMID:34849791	FYPO:0000674	Supplemental Figure S3B
PMID:34849791	PBO:0094559	(Figure 4)
PMID:34849791	PBO:0094560	(Figure 4)
PMID:34851357	FYPO:0008420	(comment: LLOs synthesized: G2M9 52%, G1M9 48%)
PMID:34851357	FYPO:0008420	(comment: LLOs synthesized: M5 100%)
PMID:34851357	FYPO:0008420	(comment: LLOs synthesized: M9 100%)
PMID:34851357	FYPO:0008420	(comment: LLOs synthesized: M6 100%)
PMID:34851357	FYPO:0008420	(comment: LLOs synthesized: M7 100%)
PMID:34851357	FYPO:0008420	(comment: LLOs synthesized: G1M5 63%, M5 37%)
PMID:34851357	FYPO:0008420	(comment: LLOs synthesized: G3M5 85%, G1M5 2%, M5 13%)
PMID:34851357	FYPO:0008420	(comment: LLOs synthesized: G3M7 85%, G1M7 7%, M7 8%)
PMID:34851357	FYPO:0008420	(comment: LLOs synthesized: G1M6 72%, M6 28%)
PMID:34851357	FYPO:0008420	(comment: LLOs synthesized: G1M7 80%, M7 20%)
PMID:34851357	FYPO:0008420	(comment: LLOs synthesized: G2M5 73%, G1M5 21%)
PMID:34851357	FYPO:0008420	(comment: LLOs synthesized: G2M6 19%, G1M6 46%, M6 35%)
PMID:34851357	FYPO:0008420	(comment: LLOs synthesized: G2M7 68%, M7 32%)
PMID:34851357	FYPO:0008420	(comment: LLOs synthesized: G3M6 24%, G2M6 48%, G1M6 10%, M6 18%)
PMID:34851357	FYPO:0008420	(comment: LLOs synthesized: G1M9 100%)
PMID:34851403	PBO:0109232	In cells lacking Sgo1 (sgo1Δ), which protects centromeric cohesin during anaphase, no separated kinetochore signals were observed (Fig. 3A,C), although sister chromatids frequently underwent equational segregation in the absence of chiasmata (Fig. S2B).
PMID:34851403	PBO:0109237	Additionally, the DNA replication checkpoint function of Mrc1 is not required for sister kinetochore association, because deletion of cds1, which encodes an effector kinase functioning downstream of Mrc1 in the DNA replication checkpoint pathway (Alcasabas et al., 2001; Murakami and Okayama, 1995; Tanaka and Russell, 2001), did not affect the kinetochore association state or sister chromatid segregation (Fig. 3C,E; Fig. S2C).
PMID:34851403	FYPO:0005648	Non-separated signals were found to be significantly or nearly significantly wider than in wild-type cells (Fig. 3E,F;)
PMID:34851403	FYPO:0005648	In mrc1Δ cells, sister kinetochores and centromere cores separated at a low, but significant, level (Fig. 3A-D; Figs S2C and S3A,B), and non-separated signals were significantly wider in shape (Fig. 3E,F; Fig. S3C,D).
PMID:34864879	FYPO:0000276	We notified that a small percentage of either Eg5-NLS or Cut7 overproducing cells showed the monopolar spindle phenotype (Figure 2c; after 18 h, 10% for Cut7 vs 11% for Eg5-NLS).
PMID:34864879	FYPO:0003787	Observation of spindle morphology showed that cells in which either Cut7 or Eg5-NLS is overproduced displayed the emergence of protruding spindles, which was never observed in the vector control strain. In these cells, the spindle MTs extended away from one side or both sides of the spindle poles, in which the spindle pole bodies (SPBs, fungi equivalents of animal centrosomes) localized to the MT tips (Figure 2b).
PMID:34864879	FYPO:0002061	As shown in Figure 2a, cells overproducing Cut7 under the induced condition is lethal
PMID:34910579	FYPO:0005840	We confirmed the defects in septa ....... In cells with closed septa, the primary septum was uneven (Figure 3, red arrows) and thinner in smi1-1 cells than in WT (Figure 3A).
PMID:34910579	PBO:0035615	(Figure 1C,D)
PMID:34910579	PBO:0102297	(comment: recruits glucanases and glucan synthases to division site)
PMID:34910579	FYPO:0001188	(Figure 2A)
PMID:34910579	FYPO:0003890	We confirmed the defects in septa ....... In cells with closed septa, the primary septum was uneven (Figure 3, red arrows) and thinner in smi1-1 cells than in WT (Figure 3A).
PMID:34910579	PBO:0102298	(comment: CONDITION 36 degrees)
PMID:34910579	PBO:0102299	(comment: CONDITION 36 degrees)
PMID:34910579	PBO:0102300	(comment: CONDITION 36 degrees)
PMID:34910579	PBO:0102301	(comment: CONDITION 36 degrees)
PMID:34910579	PBO:0102302	(comment: CONDITION 36 degrees)
PMID:34910579	PBO:0102304	(comment: CONDITION 36 degrees)
PMID:34910579	PBO:0035615	Supplemental Figure S2, A-D
PMID:34910579	FYPO:0004292	Supplemental Figure S2, A-D
PMID:34910579	PBO:0102299	(comment: CONDITION 36 degrees)
PMID:34910579	PBO:0102308	(comment: CONDITION 36 degrees)
PMID:34910579	PBO:0102308	(comment: CONDITION 36 degrees)
PMID:34910579	PBO:0102306	(comment: CONDITION 36 degrees)
PMID:34910579	FYPO:0000650	(comment: 38.5% cf WT 11.5%, cannot put % on population phenotype) Figure 1F
PMID:34910579	PBO:0102309	recruits glucanases and glucan synthases to division site
PMID:34910579	PBO:0102309	Together, these results confirmed that Sbg1 is specific to Bgs1, while Smi1 regulates the levels of both Bgs4 and Bgs1 at the division site, with a more important role for Bgs4 (Figure 7, A-C).
PMID:34951983	GO:0007052	required for spindle repair following laser ablation
PMID:34951983	GO:0007052	Not required for spindle repair following laser ablation
PMID:34951983	GO:0007052	Microtubule dynamics required for spindle repair following laser ablation
PMID:34951983	GO:0007052	required for spindle repair following laser ablation
PMID:34958661	PBO:0101336	The slower-migrating, hyperphosphorylated form of Wee1 was lost in arf6Δ and syt22Δ, similar to cdr2Δ (Fig. 1 H). We conclude that activated Arf6 functions in the Cdr2 pathway to control cell size at division through inhibition of Wee1.
PMID:34958661	FYPO:0006616	The cell length at division phenotype for arf6Δ was minor, but these cells were wider than wild type (Fig. S1 E).
PMID:34958661	PBO:0101335	This is from GIs, phenocopy, PLUS If the Arf6 localization defect in syt22Δ is due to loss of the GTP-bound state, then it should be suppressed by arf6(Q75L). Indeed, arf6(Q75L)-mNG localized to nodes even in syt22Δ cells (Fig. 2 G)
PMID:34958661	PBO:0096312	(Fig. S1A) (comment: 24.6 micron)
PMID:34958661	PBO:0096312	(Fig. S1A) (comment: 26.6 micron)
PMID:34958661	PBO:0096312	(Fig. S1A) (comment: 27 micron)
PMID:34958661	GO:0010971	(Figure 1)
PMID:34958661	GO:0010971	(Figure 1)
PMID:34958661	FYPO:0002455	All three double mutants exhibited synthetic defects in cell growth and cytokinesis as judged by tilted and disorganized septa (Fig. 5, C-E; and Fig. S3 M).
PMID:34958661	FYPO:0002455	All three double mutants exhibited synthetic defects in cell growth and cytokinesis as judged by tilted and disorganized septa (Fig. 5, C-E; and Fig. S3 M).
PMID:34958661	PBO:0101346	(comment: CHECK actually mid1-Nter)
PMID:34958661	PBO:0101345	The resulting arf6 alleles reduced node localization and instead enriched at the cytoplasm (Fig. S2, H and I)
PMID:34958661	PBO:0101343	o explain this connection, we examined the localization of Wee1 and Cdr1 at cortical nodes in arf6Δ mutants. Wee1 localized to nodes in arf6Δ, but Cdr1 did not (Fig. 3, D and E; and Fig. S3 D)
PMID:34958661	PBO:0112444	Thus, Arf6 and Mid1 are partially overlapping anchors for Cdr2 nodes.
PMID:34958661	PBO:0101337	Arf6 localizes stably to Cdr2 nodes during interphase in a manner that depends on nucleotide binding, membrane binding, and Cdr2 itself.; strongly enriched at cortical nodes in the cell middle (Fig. 2 A). Arf6 and Cdr2 colocalized at nodes (Figs. 2 B and S2 A)
PMID:34958661	PBO:0101336	The slower-migrating, hyperphosphorylated form of Wee1 was lost in arf6Δ and syt22Δ, similar to cdr2Δ (Fig. 1 H). We conclude that activated Arf6 functions in the Cdr2 pathway to control cell size at division through inhibition of Wee1.
PMID:34958661	PBO:0101336	The slower-migrating, hyperphosphorylated form of Wee1 was lost in arf6Δ and syt22Δ, similar to cdr2Δ (Fig. 1 H). We conclude that activated Arf6 functions in the Cdr2 pathway to control cell size at division through inhibition of Wee1.
PMID:34958661	PBO:0021076	trongly enriched at cortical nodes in the cell middle (Fig. 2 A). Arf6 and Cdr2 colocalized at nodes (Figs. 2 B and S2 A)
PMID:34958661	PBO:0101338	Arf6 node localization required Cdr2 but not other node proteins (Figs. 2 E and S2 B).
PMID:34958661	PBO:0101338	A GDP-locked mutant arf6(T52N)-mNG lost node localization, (Fig. 2 F)
PMID:34958661	PBO:0101339	but the GTP-locked allele arf6(Q75L)-mNG remained at nodes (Fig. 2 F)
PMID:34958661	PBO:0101343	We combined arf6Δ with the mid1(400-450Δ) mutant that cannot bind Cdr2. In the resulting cells, Cdr2 was absent from the cell cortex and formed large cytoplasmic puncta (Figs. 4 A and S2 J).
PMID:34958661	PBO:0101338	Further, Arf6 localization to nodes was lost upon deletion of its GEF Syt22 (Fig. 2 G
PMID:34958661	PBO:0101339	Indeed, arf6(Q75L)-mNG localized to nodes even in syt22Δ cells (Fig. 2 G)
PMID:34958661	GO:0051285	Ucp3-mNG localized to spots at the cell tips, which likely represent endocytic actin patches due to colocalization with actin patch component Pan1 (Fig. S2, E and F)
PMID:34958661	PBO:0101340	The resulting arf6 alleles reduced node localization and instead enriched at the cytoplasm (Fig. S2, H and I)
PMID:34958661	PBO:0101340	The resulting arf6 alleles reduced node localization and instead enriched at the cytoplasm (Fig. S2, H and I)
PMID:34958661	PBO:0101340	The resulting arf6 alleles reduced node localization and instead enriched at the cytoplasm (Fig. S2, H and I)
PMID:34958661	PBO:0101341	rf6Δ cells had cytoplasmic Cdr2 clusters that were absent in wild-type cells (Figs. 3 A and S2 J), indicating defects in cortical anchoring.
PMID:34958661	PBO:0101342	"Modified form is indirect because GDP bound does not localize to nodes) ""These defects indicate that Arf6 anchors Cdr2 stably at nodes, meaning that Arf6 and Cdr2 reciprocally promote each other’s node localization."""
PMID:34958661	FYPO:0002455	All three double mutants exhibited synthetic defects in cell growth and cytokinesis as judged by tilted and disorganized septa (Fig. 5, C-E; and Fig. S3 M).
PMID:34959732	FYPO:0001367	(Figure 3A and Figure S1A. Table 3) (comment: CHECK Suppression of the lytic phenotype at cytokinesis)
PMID:34959732	FYPO:0000164	(Figure 4B and Figure S2B) Also in the Table 3. The pbr1-8 mutation partially suppresses the slowing cytokinesis caused by lethal concentrations of caspofungin, suggesting that besides Bgs4, this drug affects other Bgs subunits (Bgs1 and/or Bgs3)
PMID:34959732	FYPO:0002060	(Table 5 and Figure S3, and Figure S4C) Vegetative cell lysis caused by lethal and sublethal concentrations of micafungin is suppressed in the pbr1-8
PMID:34959732	FYPO:0001367	(comment: (Sub lethal and lethat doese)) Figure 5 and Figure S3. Also in the Table 3.
PMID:34959732	FYPO:0001367	(comment: (Sub lethal and lethat doese)) Figure 5 and Figure S3. Also in the Table 3.
PMID:34959732	FYPO:0000417	(Figure 3B,S1B) Also in the Table 3. Cytokinesis is blocked in both wild-type and pbr1-8 strains treated with lethal concentrations of the echinocandin drug anidulafungin, suggesting that this drug affects the function of Bgs4 and Bgs1 and/or Bgs3
PMID:34959732	FYPO:0000005	(Figure 4A,S2A) (comment: Sublethal concentrations of caspofungin)
PMID:34959732	FYPO:0002060	(Table 5 and Figure S3, and Figure S4C) Vegetative cell lysis caused by lethal and sublethal concentrations of micafungin is suppressed in the pbr1-8
PMID:34959732	FYPO:0001367	(Figure 4B, S2B, Table 3) The pbr1-8 mutation partially suppresses the slowing cytokinesis caused by lethal concentrations of caspofungin, suggesting that besides Bgs4, this drug affects other Bgs subunits (Bgs1 and/or Bgs3)
PMID:34959732	FYPO:0000005	(Figure 4A,S2A) (comment: Sublethal concentrations of caspofungin)
PMID:34967420	PBO:0102819	(comment: RNA-Seq)
PMID:34967420	PBO:0102818	(comment: RNA-Seq)
PMID:34967420	PBO:0102815	(comment: RNA-Seq)
PMID:34967420	PBO:0102810	(comment: Northern Blotting, RNA-Seq)
PMID:34967420	PBO:0102817	(comment: RNA-Seq)
PMID:34967420	PBO:0102812	(comment: RNA-Seq)
PMID:34967420	PBO:0102813	(comment: RNA-Seq)
PMID:34967420	PBO:0102823	(comment: RNA-Seq)
PMID:34967420	PBO:0102827	(comment: RNA-Seq)
PMID:34967420	PBO:0102828	(comment: RNA-Seq)
PMID:34967420	PBO:0102816	(comment: RNA-Seq)
PMID:34967420	PBO:0102822	(comment: RNA-Seq)
PMID:34967420	PBO:0102821	(comment: RNA-Seq)
PMID:34967420	PBO:0102820	(comment: RNA-Seq)
PMID:34967420	PBO:0102814	(comment: RNA-Seq)
PMID:34967420	PBO:0102824	(comment: RNA-Seq)
PMID:34967420	PBO:0102825	(comment: RNA-Seq)
PMID:34967420	PBO:0102826	(comment: RNA-Seq)
PMID:34967420	PBO:0102811	(comment: RNA-Seq)
PMID:35008733	PBO:0094647	(Fig. 3) Live cell imaging revealed that GFP-Lac1 and Lag1-GFP remain localized at the ER in the absence of Lag1 or Lac1 respectively, indicating that their ER localizations are not interdependent.
PMID:35008733	PBO:0094645	Live cell imaging revealed that GFP-Lac1 and Lag1-GFP remain localized at the ER in the absence of Lag1 or Lac1 respectively, indicating that their ER localizations are not interdependent.
PMID:35008733	FYPO:0006133	(Fig. 5b) We detected an accumulation of PHS and sphingoid bases-1-phosphate levels (PHS-1P or DHS-1P)
PMID:35008733	PBO:0094646	(Fig. 3) Live cell imaging revealed that GFP-Lac1 and Lag1-GFP remain localized at the ER in the absence of Lag1 or Lac1 respectively, indicating that their ER localizations are not interdependent.
PMID:35008733	FYPO:0005593	Additionally, the pattern of complex sphingolipids in Lac1-depleted cells shows a strong accumulation of IPC and the appearance of new bands that might correspond to different IPC species
PMID:35011726	GO:0061631	(Figure 1A)
PMID:35011726	GO:0061631	(Figure 1A)
PMID:35011726	FYPO:0001913	(Figure 2D
PMID:35011726	PBO:0105578	Among the Nse1-bound factors, we repeatedly observed the Ubc13, Mms2, and Uba1 (Data File S1A,B, Data File S2A-C—ProteomeXchange: PXD029573, and Table S3).
PMID:35011726	FYPO:0002061	Nse1- R188E mutant shows synthetic lethality with smc6-74
PMID:35011726	FYPO:0002061	Nse1- R188E mutant shows synthetic lethality with smc6-74
PMID:35011726	FYPO:0001355	severe growth defects with smc6-X and nse6∆
PMID:35011726	FYPO:0001355	severe growth defects with smc6-X and nse6∆
PMID:35011726	FYPO:0001355	severe growth defects with smc6-X and nse6∆
PMID:35011726	FYPO:0001355	severe growth defects with smc6-X and nse6∆
PMID:35011726	PBO:0093616	The Nse1 ubiquitin ligase mutant showed a synthetic relationship with the Nse2 SUMO ligase mutant (C195S, H197A), indicating their separate roles in SMC5/6 function
PMID:35011726	FYPO:0000957	Interestingly, the addition of nse1- C216S mutation suppressed the R188E phenotypes (Figure 3A), suggesting that it leads to a ubiquitin-ligase-independent outcome.
PMID:35011726	FYPO:0000963	Interestingly, the addition of nse1- C216S mutation suppressed the R188E phenotypes (Figure 3A), suggesting that it leads to a ubiquitin-ligase-independent outcome.
PMID:35011726	FYPO:0001357	These synthetic phenotypes were again suppressed by the nse1-C216S mutation (Figure S5).
PMID:35011726	PBO:0105580	(Figure 1A) The MS analysis of the Nse1/3/4- and Ubc13/Mms2-containing in vitro ubiquitination assay led to the identification of Nse4 ubiquitination at K181 and Nse3 at K195 (Data Files S3 and S4).
PMID:35011726	PBO:0105579	(Figure 1A) The MS analysis of the Nse1/3/4- and Ubc13/Mms2-containing in vitro ubiquitination assay led to the identification of Nse4 ubiquitination at K181 and Nse3 at K195 (Data Files S3 and S4).
PMID:35011726	PBO:0105577	Nse4 ubiquitination at K181 and Nse3 at K195 (Data Files S3 and S4).
PMID:35011726	PBO:0105577	Nse4 ubiquitination at K181 and Nse3 at K195 (Data Files S3 and S4).
PMID:35011726	PBO:0093581	(Figure 3A) ubiquitin ligase mutant
PMID:35011726	PBO:0093618	(Figure 3A) ubiquitin ligase mutant
PMID:35012333	PBO:0094738	(Fig. 10B)
PMID:35012333	PBO:0094738	(Fig. 10B)
PMID:35012333	PBO:0094738	(Fig. 10B)
PMID:35012333	PBO:0094738	(Fig. 10B)
PMID:35012333	PBO:0094738	(Fig. 10B)
PMID:35012333	PBO:0093557	(Fig. 5A)
PMID:35012333	FYPO:0000080	(Fig. S4)
PMID:35012333	FYPO:0001357	(Fig. S4)
PMID:35012333	FYPO:0001357	(Fig. S4)
PMID:35012333	PBO:0094777	(Fig. S5B)
PMID:35012333	PBO:0094777	(Fig. S5B)
PMID:35012333	FYPO:0001357	(Fig. S5A)
PMID:35012333	FYPO:0001357	(Fig. S5A)
PMID:35012333	FYPO:0008027	(Fig. 12B)
PMID:35012333	FYPO:0008027	(Fig. 12B)
PMID:35012333	FYPO:0008027	(Fig. 12B)
PMID:35012333	PBO:0096728	(Fig. S6) new term suggested
PMID:35012333	FYPO:0007820	(Fig. S6)
PMID:35012333	FYPO:0001357	(Fig. S7)
PMID:35012333	FYPO:0001357	(Fig. S7)
PMID:35012333	FYPO:0001357	(Fig. S7)
PMID:35012333	FYPO:0001357	(Fig. S7)
PMID:35012333	FYPO:0001357	(Fig. S7)
PMID:35012333	FYPO:0001357	(Fig. S7)
PMID:35012333	PBO:0093557	(Fig. 5A)
PMID:35012333	PBO:0093557	(Fig. 5A)
PMID:35012333	PBO:0093557	(Fig. 5A)
PMID:35012333	PBO:0093557	(Fig. 5A)
PMID:35012333	PBO:0093557	(Fig. 5A)
PMID:35012333	PBO:0093558	(Fig. 5A)
PMID:35012333	PBO:0093558	(Fig. 5A)
PMID:35012333	PBO:0093558	(Fig. 5A)
PMID:35012333	PBO:0093558	(Fig. 5A)
PMID:35012333	PBO:0093558	(Fig. 5A)
PMID:35012333	PBO:0093558	(Fig. 5A)
PMID:35012333	PBO:0093558	(Fig. 5A)
PMID:35012333	PBO:0093558	(Fig. 5A)
PMID:35012333	PBO:0094771	(Fig. 6B)
PMID:35012333	PBO:0094771	(Fig. 6B)
PMID:35012333	FYPO:0001357	(Fig. 6A)
PMID:35012333	FYPO:0001357	(Fig. 6A)
PMID:35012333	FYPO:0001357	(Fig. 7A)
PMID:35012333	FYPO:0001357	(Fig. 7A)
PMID:35012333	PBO:0093553	(Fig. 7A)
PMID:35012333	PBO:0094738	(Fig. 7B)
PMID:35012333	PBO:0094738	(Fig. 7B)
PMID:35012333	PBO:0094738	(Fig. 7B)
PMID:35012333	PBO:0094777	(Fig. 7B)
PMID:35012333	PBO:0094777	(Fig. 7B)
PMID:35012333	PBO:0094777	(Fig. 7B)
PMID:35012333	PBO:0093555	(Fig. 7A)
PMID:35012333	PBO:0093555	(Fig. 7A)
PMID:35012333	PBO:0093557	(Fig. 7A)
PMID:35012333	PBO:0093557	(Fig. 7A)
PMID:35012333	PBO:0094771	(Fig. 8B)
PMID:35012333	PBO:0094738	(Fig. 8B)
PMID:35012333	PBO:0093557	(Fig. 5A)
PMID:35012333	PBO:0093557	(Fig. 5A)
PMID:35012333	PBO:0093554	(Fig. 5A)
PMID:35012333	PBO:0093554	(Fig. 5A)
PMID:35012333	PBO:0094738	(Fig. 5B)
PMID:35012333	PBO:0094738	(Fig. 5B)
PMID:35012333	PBO:0094738	(Fig. 5B)
PMID:35012333	PBO:0094738	(Fig. 5B)
PMID:35012333	PBO:0094738	(Fig. 5B)
PMID:35012333	PBO:0094738	(Fig. 5B)
PMID:35012333	PBO:0094738	(Fig. 5B)
PMID:35012333	PBO:0094738	(Fig. 10B)
PMID:35012333	PBO:0094771	(Fig. 4B)
PMID:35012333	FYPO:0001357	(Fig. 4)
PMID:35012333	PBO:0093555	(Fig. 8A)
PMID:35012333	PBO:0093553	(Fig. 8A)
PMID:35012333	FYPO:0001357	(Fig. S2)
PMID:35012333	FYPO:0002085	(Fig. S3)
PMID:35012333	FYPO:0001357	(Fig. S3)
PMID:35012333	FYPO:0001357	(Fig. S3)
PMID:35012333	FYPO:0001357	(Fig. S3)
PMID:35012333	FYPO:0000080	(Fig. S4)
PMID:35012333	FYPO:0007820	(Fig. 13)
PMID:35012333	PBO:0094738	(Fig. 5B)
PMID:35012333	FYPO:0000080	(Fig. S4)
PMID:35012333	FYPO:0000080	(Fig. S4)
PMID:35012333	FYPO:0008028	(Fig. 12A)
PMID:35012333	FYPO:0007820	(Fig. 13)
PMID:35012333	PBO:0096729	(Fig. 13)
PMID:35012333	PBO:0096730	(Fig. 13)
PMID:35012333	PBO:0096731	(Fig. 13) new term suggested
PMID:35012333	PBO:0096731	(Fig. 13) new term suggested
PMID:35012333	PBO:0096728	(Fig. 13) new term suggested
PMID:35012333	PBO:0096731	(Fig. 13) new term suggested
PMID:35012333	PBO:0096731	(Fig. 13) new term suggested
PMID:35012333	PBO:0096732	(Fig. 13)
PMID:35012333	PBO:0096729	(Fig. 13)
PMID:35012333	PBO:0096732	(Fig. 13)
PMID:35012333	FYPO:0001357	(Fig. 11A)
PMID:35012333	FYPO:0001357	(Fig. 11A)
PMID:35012333	FYPO:0001357	(Fig. 11A)
PMID:35012333	FYPO:0001357	(Fig. 11A)
PMID:35012333	FYPO:0001357	(Fig. 11A)
PMID:35012333	FYPO:0000080	(Fig. 11A)
PMID:35012333	FYPO:0000080	(Fig. 11A)
PMID:35012333	FYPO:0000080	(Fig. 11A)
PMID:35012333	FYPO:0000080	(Fig. 11A)
PMID:35012333	FYPO:0000080	(Fig. 11A)
PMID:35012333	FYPO:0000080	(Fig. 11A)
PMID:35012333	GO:0006799	(comment: from polyphosphate absent from cell)
PMID:35012333	FYPO:0001357	(Fig. 1A)
PMID:35012333	FYPO:0001357	(Fig. 1A)
PMID:35012333	FYPO:0001357	(Fig. 1A)
PMID:35012333	PBO:0093561	(Fig. 1A)
PMID:35012333	PBO:0093561	(Fig. 1A)
PMID:35012333	PBO:0093561	(Fig. 1A)
PMID:35012333	PBO:0093553	(Fig. 1A)
PMID:35012333	PBO:0093553	(Fig. 1A)
PMID:35012333	PBO:0094738	(Fig. 2B)
PMID:35012333	PBO:0094738	(Fig. 2B)
PMID:35012333	PBO:0094738	(Fig. 2B)
PMID:35012333	PBO:0093553	(Fig. 2A)
PMID:35012333	PBO:0093553	(Fig. 2A)
PMID:35012333	PBO:0093553	(Fig. 2A)
PMID:35012333	PBO:0094771	(Fig. 2B)
PMID:35012333	FYPO:0001357	(Fig. 2A)
PMID:35012333	PBO:0093558	(Fig. 4A)
PMID:35012333	PBO:0093558	(Fig. 4A)
PMID:35012333	PBO:0093558	(Fig. 4A)
PMID:35012333	FYPO:0001357	(Fig. 4A)
PMID:35012333	FYPO:0001357	(Fig. 4A)
PMID:35012333	FYPO:0001357	(Fig. 4A)
PMID:35012333	FYPO:0001357	(Fig. 4A)
PMID:35012333	FYPO:0001357	(Fig. 4A)
PMID:35012333	FYPO:0001357	(Fig. 4A)
PMID:35012333	PBO:0094738	(Fig. 5B)
PMID:35012333	PBO:0094738	(Fig. 5B)
PMID:35012333	PBO:0094738	(Fig. 5B)
PMID:35012333	PBO:0094777	(Fig. 4B)
PMID:35012333	PBO:0094777	(Fig. 4B)
PMID:35012333	PBO:0094777	(Fig. 4B)
PMID:35012333	FYPO:0000080	(Fig. 11A)
PMID:35012333	FYPO:0000080	(Fig. 11A)
PMID:35012333	PBO:0094777	(Fig. 11B)
PMID:35012333	PBO:0094777	(Fig. 11B)
PMID:35012333	PBO:0094738	(Fig. 11B)
PMID:35012333	PBO:0094738	(Fig. 11B)
PMID:35012333	PBO:0094738	(Fig. 11B)
PMID:35012333	PBO:0094738	(Fig. 11B)
PMID:35012333	PBO:0094738	(Fig. 11B)
PMID:35012333	PBO:0094738	(Fig. 11B)
PMID:35012333	FYPO:0002061	(comment: Described in Garg et al. PMID:33010152)
PMID:35012333	FYPO:0002061	(comment: Described in Garg et al. PMID:33010152)
PMID:35012333	FYPO:0001357	(Fig. 10A)
PMID:35012333	FYPO:0001357	(Fig. 10A)
PMID:35012333	FYPO:0001357	(Fig. 10A)
PMID:35012333	FYPO:0001357	(Fig. 10A)
PMID:35012333	FYPO:0001357	(Fig. 10A)
PMID:35012333	FYPO:0001357	(Fig. 10A)
PMID:35012333	FYPO:0001357	(Fig. 10A)
PMID:35012333	FYPO:0001357	(Fig. 10A)
PMID:35012333	FYPO:0001357	(Fig. 10A)
PMID:35012333	FYPO:0001357	(Fig. 10A)
PMID:35012333	FYPO:0001357	(Fig. 10A)
PMID:35012333	FYPO:0001357	(Fig. 10A)
PMID:35012333	PBO:0094771	(Fig. 4)
PMID:35012333	PBO:0094771	(Fig. 10B)
PMID:35012333	PBO:0094771	(Fig. 10B)
PMID:35012333	PBO:0094771	(Fig. 10B)
PMID:35012333	PBO:0094771	(Fig. 10B)
PMID:35012333	PBO:0094738	(Fig. 10B)
PMID:35012333	PBO:0094738	(Fig. 10B)
PMID:35024575	PBO:0098550	Conclusion is dawn by comparing Fig. 1H and Fig. 1I in https://www.micropublication.org/journals/biology/micropub-biology-000508.
PMID:35024575	PBO:0098549	Conclusion is dawn by comparing Fig. 1H and Fig. 1I in https://www.micropublication.org/journals/biology/micropub-biology-000508.
PMID:35058438	PBO:0112402	(comment: CHECK abolished) Figure 1E
PMID:35058438	PBO:0112402	(comment: CHECK abolished) Figure 1E
PMID:35058438	PBO:0112402	(Figure 1j)
PMID:35075549	PBO:0095252	(comment: CHECK ****STATIONARY PhASE****) the protein level of Fzo1 is unstable during the stationary phase.
PMID:35075549	PBO:0095254	(Fig. 3). We found that Fzo1 protein was not degraded at late time points in the ∆rsv2 mutant
PMID:35075549	PBO:0095254	(Fig. S1) The results showed that Fzo1 protein was not degraded at late time points only in the Δubc8 mutant (Fig. 4). Fzo1 protein was not degraded in ∆rsv2 and Δubc8 mutants after longer incubation times (60 and 72 h)
PMID:35075549	PBO:0095254	(Fig. 5) We found that when Fzo1 protein was overexpressed, it was no longer degraded at late time points
PMID:35075549	PBO:0095255	(comment: -ve regulation stationary phase)
PMID:35079912	PBO:0105960	We found that only Δfio1 cells were sensitive to Cu2+
PMID:35079912	PBO:0095304	(Figure 3A) 25 µM of iron chelator bathophenanthroline disulfonate (BPS) was added to YES media to create iron-depleted condition.
PMID:35079912	PBO:0095303	(Figure 3A) 25 µM of iron chelator bathophenanthroline disulfonate (BPS) was added to YES media to create iron-depleted condition.
PMID:35079912	PBO:0105959	(Figure 3A) Fe2(SO4)3 was added to YES media for a final concentration of 2.75 mM.
PMID:35079912	PBO:0105959	(Figure 3A) Fe2(SO4)3 was added to YES media for a final concentration of 2.75 mM.
PMID:35082773	PBO:0096833	(Figure 5A). we found that the protein level of Cdr2 in ksg1-208 cells was significantly lower than that in wild-type cells (Figures 4A, 4B)
PMID:35082773	FYPO:0000648	It should be noted that cdr2+ overexpressed wild-type cells showed a shorter cell length at 27◦C, but a longer cell length at 35◦C than cdr2+ non-overexpressed wild-type cells (Figure 3B).
PMID:35082773	PBO:0095096	(Figure 3C). In addition, the cdr2+ overexpressed wild-type cells showed a higher septation index than cdr2+ non-overexpressed wild-type cells at 35◦C
PMID:35082773	FYPO:0003503	(Figures 3A, 3B) overexpression of cdr2+ also reversed the defects in the cell length and the septation index of ksg1-208 cells
PMID:35082773	FYPO:0000339	(Figure 2D and Supplementary Figure 1) The results showed that the septation ring of the ksg1-208 delta-ppk21 double mutant was off-centered at 33◦C, which was more severe than that of ksg1-208 cells
PMID:35082773	PBO:0093560	(Figure 1A)
PMID:35082773	PBO:0096311	(Figure 2A) significantly longer than that of wild-type cells at 27◦C
PMID:35082773	PBO:0096830	(Figure 2B) ...which was recovered by the overexpression of ppk21+
PMID:35082773	PBO:0096831	(Figure 2B) ...which was recovered by the overexpression of ppk21+
PMID:35082773	FYPO:0002061	(Figure 2C) (comment: CONDITION 33 degrees)
PMID:35082773	PBO:0096314	(Figures 2D, 2E) results showed that ksg1-208 Δppk21 cells exhibited a longer cell length than either ksg1-208 or Δppk21 cells at both 27 and 33◦C
PMID:35082773	PBO:0096835	(Figure 5A) Western blot analysis showed that the level of Cdc25 protein was dramatically lower in ksg1-208 cells than that in wild-type cells, indicating that Ksg1 played a crucial role in the accumulation of Cdc25 protein
PMID:35082773	PBO:0096834	(Figure 4c) In contrast, a fraction of ksg1-208 cells showed septum or division site localized Cdr2-mEGFP in the dividing cells at 27◦C, indicating the cortex dissociation of Cdr2 was hindered.
PMID:35082773	PBO:0096832	(Figures 4A, 4B) we found that the protein level of Cdr2 in ksg1-208 cells was significantly lower than that in wild-type cells
PMID:35082773	PBO:0093561	(Figure 1A)
PMID:35082773	PBO:0096835	(Figure 5A). In addition, the Cdc25 protein level decreased in Δppk21 and Δcdr2 cells as well, indicating the role of Ppk21 and Cdr2 on regulating Cdc25 protein level
PMID:35082773	PBO:0096835	(Figure 5A) In addition, the Cdc25 protein level decreased in Δppk21 and Δcdr2 cells as well, indicating the role of Ppk21 and Cdr2 on regulating Cdc25 protein level .
PMID:35099006	PBO:0096598	Increased percentage of septated cells at both permissive and restrictive temperature.
PMID:35099006	PBO:0093558	The growth rate of pkd2-B42 at the restrictive temperature of 36C or higher is 80% lower than wild-type cells.
PMID:35099006	GO:0009992	pkd2 mutants show temporary deflation followed by reinflation. pkd2-B42 has 50% lower spring constant as measured by Atomic Force Microscopy implicating reduced cellular stiffness. This indicates a reduced ability of this mutant at maintaining cellular turgor.
PMID:35108037	FYPO:0002060	(Figure S2E)
PMID:35108037	FYPO:0002060	(Figure S2E)
PMID:35108037	FYPO:0002060	(Figure S2E)
PMID:35108037	PBO:0104529	(Figure 4A,C)
PMID:35108037	PBO:0104530	(Figure 4A,C)
PMID:35108037	PBO:0104531	(Figure 4B,D)
PMID:35108037	PBO:0104532	(Figure 4B,D)
PMID:35108037	PBO:0104532	(Figure 4B,D)
PMID:35108037	PBO:0104533	(Figure S1D-E)
PMID:35108037	FYPO:0002141	(Figure S2D)
PMID:35108037	FYPO:0002141	(Figure S2D)
PMID:35108037	FYPO:0002060	(Figure S2E)
PMID:35108037	FYPO:0002141	(Figure S2D) (comment: CONDITION 19 degrees C)
PMID:35108037	FYPO:0000674	(Figure S2D)
PMID:35108037	FYPO:0002060	(Figure S2E)
PMID:35108037	FYPO:0001357	(Figure S2D)
PMID:35108037	FYPO:0003809	(Figure S2D)
PMID:35108037	FYPO:0004675	(Fig. S2D)
PMID:35108037	FYPO:0002060	(Figure S2E)
PMID:35108037	FYPO:0000674	(Figure S2D)
PMID:35108037	FYPO:0000674	(Figure S2D)
PMID:35108037	FYPO:0001357	(Figure S2D) (25,29,32)
PMID:35108037	FYPO:0001357	(Figure S2D) (25,29,32)
PMID:35108037	FYPO:0003809	(Figure S2D)
PMID:35108037	FYPO:0003809	(Figure S2D)
PMID:35108037	FYPO:0004675	(Fig. S2D)
PMID:35108037	FYPO:0004675	(Fig. S2D)
PMID:35108037	FYPO:0002060	(Figure S2E)
PMID:35108037	FYPO:0002060	(Figure S2E)
PMID:35108037	FYPO:0002060	(Figure S2E)
PMID:35108037	FYPO:0002060	(Figure S2E)
PMID:35108037	FYPO:0002177	(Figure S2A-C)
PMID:35108037	FYPO:0002177	(Figure S2A-C)
PMID:35108037	FYPO:0002177	(Figure S2A-C)
PMID:35108037	FYPO:0001903	(Figure S2A-C)
PMID:35108037	FYPO:0001903	(Figure S2A-C)
PMID:35108037	FYPO:0001903	(Figure S2A-C)
PMID:35108037	FYPO:0002060	(Figure S2E)
PMID:35108037	FYPO:0002060	(Figure S2E)
PMID:35108037	GO:0005515	(Figure 1B, 1D-F, 2B-E, 3A-B, S1A-B)
PMID:35108037	FYPO:0002060	(Figure S2E)
PMID:35108037	FYPO:0002060	(Figure S2E)
PMID:35108037	PBO:0104534	(Figure 2B) Pxl1(AxxA1-6) reduced binding to Cdc15C(aa441-end) compared to wild-type Pxl1
PMID:35108037	PBO:0104528	Pxl1 (aa177-188 P181A, P184A) abolished binding to Cdc15 SH3 and Cdc15C1(aa600-end), Figure 2D
PMID:35108037	FYPO:0002060	(Figure S2E)
PMID:35108037	PBO:0104527	(comment: CHECK in vitro binding assay) Figure 3B
PMID:35108037	PBO:0104528	(comment: in vitro binding assay with purified Cdc15 F-BAR domain and purified Pxl1) (Fig 1E)
PMID:35108037	PBO:0104535	Pxl1-P18A+AxxA6 reduced binding to full-length Cdc15 compared to wild type Pxl1 (Figure 3A)
PMID:35108037	PBO:0104534	Pxl1-AxxA6 reduced binding to full-length Cdc15 (Figure 3A) and Cdc15 C1 (Figure S1A)
PMID:35108037	PBO:0104535	Pxl1-P18A reduced binding to full-length Cdc15 compared to wild-type Pxl1 (Figure 3A)
PMID:35108037	PBO:0104536	Pxl1-AxxA1-3 bound Cdc15C1(aa600-end) just as well as wild type Pxl1 (Figure S1A)
PMID:35108037	PBO:0104534	Mutant reduced binding to Cdc15C1(aa600-end) compared to wild type Pxl1 (Figure S1A)
PMID:35108037	PBO:0104534	Mutant reduced binding to Cdc15C1(aa600-end) compared to wild type Pxl1 (Figure S1A)
PMID:35108037	PBO:0104534	Mutant reduced binding to Cdc15C1(aa600-end) compared to wild type Pxl1 (Figure S1A)
PMID:35108037	PBO:0104536	Mutant bound Cdc15C1(aa600-end) as well as wild-type Pxl1 (Figure S1A)
PMID:35108037	FYPO:0006187	(Figure S3A) (comment: CONDITION 25C)
PMID:35108037	FYPO:0006187	(Figure S3A) (comment: CONDITION 25C)
PMID:35108037	FYPO:0006187	(Figure S3A) (comment: CONDITION 25C)
PMID:35108037	FYPO:0007828	(Figure S3A) (comment: CONDITION 25C)
PMID:35108037	FYPO:0007828	(Figure S3A)
PMID:35108037	FYPO:0007828	(Figure S3A) (comment: CONDITION 25C)
PMID:35108037	FYPO:0004895	(Figure S3A) (comment: CONDITION 25C)
PMID:35108037	FYPO:0001365	(Figure S3A) (comment: CONDITION 25C)
PMID:35108037	FYPO:0001365	(Figure S3A) (comment: CONDITION 25C)
PMID:35108037	PBO:0104537	(Figure S3B) (comment: CONDITION 25C)
PMID:35108037	FYPO:0002060	(Figure S2E)
PMID:35108037	FYPO:0002060	(Figure S2E)
PMID:35108037	FYPO:0002060	(Figure S2E)
PMID:35157728	FYPO:0003555	(Figure 2A)
PMID:35157728	PBO:0100683	The Δbdf2 mutation also suppresses the elevated levels of Gcn5 at the subtelomeric chromatin in Δtor1 cells (Fig 4E).
PMID:35157728	GO:0000122	Tor1 inhibits the binding of Gcn5 at sub-telomeric genes and MBF promoters
PMID:35157728	PBO:0110918	30 fold. Fig 2
PMID:35157728	PBO:0110919	280 fold. Fig 2
PMID:35157728	PBO:0110920	120 fold. Fig 2
PMID:35157728	FYPO:0003555	(Figure 2A)
PMID:35157728	FYPO:0003555	(Figure 2A)
PMID:35157728	FYPO:0003555	(Figure 2A)
PMID:35157728	FYPO:0006395	Consistently, we detected higher levels of H3K9Ac at subtelomeric genes in Δtor1 cells compared to wild type cells, and this defect was suppressed by either Δgcn5 or Δbdf2 (Fig 4C)
PMID:35157728	PBO:0100682	Consistently, we detected higher levels of H3K9Ac at subtelomeric genes in Δtor1 cells compared to wild type cells, and this defect was suppressed by either Δgcn5 or Δbdf2 (Fig 4C)
PMID:35157728	FYPO:0006395	Consistently, we detected higher levels of H3K9Ac at subtelomeric genes in Δtor1 cells compared to wild type cells, and this defect was suppressed by either Δgcn5 or Δbdf2 (Fig 4C)
PMID:35157728	PBO:0100681	We detected a markedly higher level of Gcn5 binding at subtelomeric genes in Δtor1 cells, compared with wild type cells (Fig 4A).
PMID:35157728	FYPO:0006742	(Figure 2A)
PMID:35157728	FYPO:0006742	(Figure 2A)
PMID:35157728	FYPO:0006742	(Figure 2A)
PMID:35157728	FYPO:0003555	(Figure 2A)
PMID:35157728	FYPO:0003555	(Figure 2A)
PMID:35157728	FYPO:0003555	(Figure 2A)
PMID:35157728	FYPO:0003555	(Figure 2A)
PMID:35157728	FYPO:0003555	(Figure 2A)
PMID:35157728	FYPO:0003555	(Figure 2A)
PMID:35157728	FYPO:0003555	(Figure 2A)
PMID:35157728	FYPO:0003555	(Figure 2A)
PMID:35157728	PBO:0100685	Unexpectedly, although there is no increase in MBF-dependent transcription, we detected an increase in Gcn5 binding at the promoters of cdc22+ or cdc18+ in Δtor1 or Δgad8 cells under normal or replication stress conditions (Fig 5A)
PMID:35157728	PBO:0100685	Unexpectedly, although there is no increase in MBF-dependent transcription, we detected an increase in Gcn5 binding at the promoters of cdc22+ or cdc18+ in Δtor1 or Δgad8 cells under normal or replication stress conditions (Fig 5A)
PMID:35157728	FYPO:0006740	Unexpectedly, although there is no increase in MBF-dependent transcription, we detected an increase in Gcn5 binding at the promoters of cdc22+ or cdc18+ in Δtor1 or Δgad8 cells under normal or replication stress conditions (Fig 5A)
PMID:35157728	PBO:0093580	(comment: no supression)
PMID:35157728	PBO:0100686	Significantly, Δbdf2 restores low levels of Gcn5 binding at MBF promoters in Δtor1 cells under normal growth conditions and also restores the normal pattern of an increased level of Gcn5 in response to HU (Fig 6C).
PMID:35157728	PBO:0100686	Significantly, Δbdf2 restores low levels of Gcn5 binding at MBF promoters in Δtor1 cells under normal growth conditions and also restores the normal pattern of an increased level of Gcn5 in response to HU (Fig 6C).
PMID:35157728	PBO:0093824	(comment: 24%)
PMID:35157728	PBO:0093824	(comment: 25%)
PMID:3516412	GO:0004672	(comment: CHECK activated_by(CHEBI:18420))
PMID:35171902	PBO:0104712	(comment: polysome profiling)
PMID:35171902	PBO:0104712	(comment: polysome profiling)
PMID:35171902	PBO:0101109	nterestingly, we found that Epe1 protein levels are significantly reduced in git3Δ nmt41-epe1+ and pka1Δ nmt41-epe1+ cells (Fig 2F)
PMID:35171902	PBO:0104709	Consistent with the results of the genetic screen, serial dilution analyses show that git1Δ, git3Δ, git5Δ, gpa2Δ, pka1Δ, and cyr1Δ all rescue silencing defects of otr::ura4+ caused by Epe1 overexpression, as indicated by better growth on EMM medium containing 5-FOA (Fig 1D)
PMID:35171902	PBO:0104711	. Interestingly, although git3Δ nmt41-epe1+ cells form heterochromatin at pericentric repeats
PMID:35171902	FYPO:0003574	H3K9me2 levels at dh repeats are restored close to wild-type levels in git3Δ nmt41-epe1+ cells (Fig 1E).
PMID:35172472	PBO:0094271	Table 1. List of the 13 TAM-sensitive heterozygous strains/Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	PBO:0094273	Table 1. List of the 13 TAM-sensitive heterozygous strains/Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	PBO:0094271	Table 1. List of the 13 TAM-sensitive heterozygous strains/Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	PBO:0094271	Table 1. List of the 13 TAM-sensitive heterozygous strains/Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	PBO:0094270	Table 1. List of the 13 TAM-sensitive heterozygous strainsFig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	PBO:0094270	Table 1. List of the 13 TAM-sensitive heterozygous strains/ Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	PBO:0094270	Table 1. List of the 13 TAM-sensitive heterozygous strains/Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	PBO:0094273	Table 1. List of the 13 TAM-sensitive heterozygous strains/ Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	PBO:0113566	When treated with TAM, the vps54 heterozygous mutants showed more enlarged vesicles (yellow arrows in Fig. 3) ....., compared with the SP286 control.
PMID:35172472	FYPO:0002654	Even without TAM treatment, the vps54 heterozygous mutant showed a high penetrance of enlarged vesicles (red arrows in Fig. 3) without any detectable change in cell shape (Fig. 3) and growth fitness (Fig. 2), compared with the SP286 control strain (comment: vw: cells are in fact quite misshapen)
PMID:35172472	PBO:0094273	Table 1. List of the 13 TAM-sensitive heterozygous strains/Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	PBO:0094273	Table 1. List of the 13 TAM-sensitive heterozygous strains/Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	PBO:0094273	Table 1. List of the 13 TAM-sensitive heterozygous strains/Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	PBO:0094273	Table 1. List of the 13 TAM-sensitive heterozygous strains/Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35194019	PBO:0032778	(Figure 5D)
PMID:35194019	FYPO:0003412	(Figure 5C) (comment: forward strand RT-qPCR (dh repeat))
PMID:35194019	FYPO:0000964	(comment: CHECK TBZ 15ug/ml)
PMID:35194019	PBO:0093562	(comment: CHECK TBZ 15ug/ml)
PMID:35194019	PBO:0093562	(comment: CHECK TBZ 15ug/ml)
PMID:35194019	PBO:0093564	(comment: CHECK TBZ 15ug/ml)
PMID:35194019	PBO:0093562	(comment: CHECK TBZ 15ug/ml)
PMID:35194019	FYPO:0001357	(Fig. S10) (comment: tetrad analysis)
PMID:35194019	FYPO:0001357	(Fig. S10) (comment: tetrad analysis)
PMID:35194019	FYPO:0001357	(Fig. S10) (comment: tetrad analysis)
PMID:35194019	FYPO:0001357	(Fig. S10) (comment: tetrad analysis)
PMID:35194019	FYPO:0001357	(Fig. S10) (comment: tetrad analysis)
PMID:35194019	FYPO:0002061	(Fig. S10) (comment: tetrad analysis)
PMID:35194019	FYPO:0002061	(Fig. S10) (comment: tetrad analysis)
PMID:35194019	FYPO:0004742	(Figure 5C) (comment: forward strand RT-qPCR (dh repeat))
PMID:35194019	FYPO:0004742	(Figure 5C) (comment: forward strand RT-qPCR (dh repeat))
PMID:35194019	PBO:0096785	(Figure 5D)
PMID:35194019	FYPO:0004742	(Figure 5C) (comment: forward strand RT-qPCR (dh repeat))
PMID:35194019	FYPO:0003412	(Figure 5C) (comment: forward strand RT-qPCR (dh repeat))
PMID:35194019	FYPO:0004742	(Figure 5C) (comment: forward strand RT-qPCR (dh repeat))
PMID:35277511	FYPO:0002060	(comment: CONDITION growth >48 hrs, growth to exponential phase)
PMID:35277511	FYPO:0002239	(comment: telomere southern (experiment))
PMID:35277511	FYPO:0002239	(comment: telomere southern (experiment))
PMID:35286199	FYPO:0002061	(Fig. 1)
PMID:35286199	PBO:0107138	(Fig. 5)
PMID:35286199	PBO:0107137	(Fig. 5)
PMID:35286199	PBO:0107135	(Fig. 4)
PMID:35286199	PBO:0107134	(Fig. 4)
PMID:35286199	FYPO:0000339	(Fig. 4)
PMID:35286199	PBO:0107133	(Fig. 4)
PMID:35286199	FYPO:0000069	(Fig. 4)
PMID:35286199	FYPO:0003227	(Fig. 4)
PMID:35286199	PBO:0101442	(Fig. 3)
PMID:35286199	FYPO:0001357	(Fig. 1)
PMID:35286199	FYPO:0001357	(Fig. 1)
PMID:35286199	PBO:0093559	(Fig. 1)
PMID:35286199	PBO:0107132	(Fig. 2)
PMID:35286199	FYPO:0001357	(Fig. 1)
PMID:35286199	PBO:0093559	(Fig. 1)
PMID:35286199	PBO:0093559	(Fig. 1)
PMID:35286199	PBO:0093561	(Fig. 1)
PMID:35286199	PBO:0093560	(Fig. 1)
PMID:35286199	PBO:0093561	(Fig. 1)
PMID:35286199	PBO:0093561	(Fig. 1)
PMID:35286199	PBO:0093561	(Fig. 1)
PMID:35286199	FYPO:0002058	(Fig. 1)
PMID:35286199	FYPO:0002058	(Fig. 1)
PMID:35286199	FYPO:0002058	(Fig. 1)
PMID:35286199	FYPO:0002058	(Fig. 1)
PMID:35286199	FYPO:0002058	(Fig. 1)
PMID:35286199	PBO:0093561	(Fig. 1)
PMID:35286199	FYPO:0002060	(Fig. 1)
PMID:35286199	FYPO:0002058	(Fig. 1)
PMID:35286199	FYPO:0000276	(Fig. 2)
PMID:35293864	FYPO:0007974	(Fig. 4) Figure supplement 2 We found that in both les1Δ and nem1Δ cells microtubule growth speed inside the nuclear bridge was faster than in wild-type cells
PMID:35293864	PBO:0106717	(Fig. 2) Figure supplement 2F
PMID:35293864	PBO:0106716	(Fig. 2) Figure supplement 1 klp5Δklp6Δ cells exhibited slightly longer microtubule growth events
PMID:35293864	PBO:0106719	(Fig. 5E) Ase1 is required for normal rescue distribution
PMID:35293864	FYPO:0007974	(Fig. 5F, G) The decrease in growth speed associated with internalisation of microtubules in the nuclear membrane bridge is reduced upon Ase1 deletion
PMID:35293864	PBO:0106718	(Fig. 5 supp 3E)
PMID:35293864	PBO:0096311	(comment: Note: not sure about the term name and the child.) Fig. 3 supp 1A, C
PMID:35293864	FYPO:0007971	(Fig. 5F,G) The decrease in growth speed associated with internalisation of microtubules in the nuclear membrane bridge is reduced upon Ase1 deletion
PMID:35293864	FYPO:0007972	mal3Δ cells exhibited lower microtubule growth speed throughout anaphase B (Fig. 2G)
PMID:35293864	PBO:0106718	(Fig. 2) Figure supplement 2E
PMID:35293864	FYPO:0007974	(Fig. 4) Figure supplement 2 We found that in both les1Δ and nem1Δ cells microtubule growth speed inside the nuclear bridge was faster than in wild-type cells
PMID:35300005	FYPO:0001029	(comment: CONDITION 100 ug/ml canavanine)
PMID:35314193	FYPO:0002085	(Figure 12)
PMID:35314193	PBO:0094738	(Figure 12)
PMID:35314193	PBO:0110566	(comment: Cobalt/nickel-dependent inorganic pyrophosphatase activity) Figure 4
PMID:35314193	PBO:0110566	(comment: Cobalt/nickel-dependent inorganic pyrophosphatase activity) Figure 3
PMID:35314193	PBO:0098306	(Figures 1 and 3)
PMID:35314193	GO:0016791	(comment: Cobalt/nickel-dependent inorganic pyrophosphatase activity) Figure 4
PMID:35314193	GO:0016791	(comment: Cobalt/nickel-dependent inorganic pyrophosphatase activity) Figure 1
PMID:35314193	PBO:0098307	(Figure 8)
PMID:35314193	FYPO:0002085	(Figure 12)
PMID:35314193	PBO:0098307	(Figure 8)
PMID:35314193	PBO:0098307	(Figure 8)
PMID:35314193	PBO:0098307	(Figure 10)
PMID:35314193	PBO:0098306	(Figure 10)
PMID:35314193	PBO:0098306	(Figures 1 and 3)
PMID:35314193	PBO:0098307	(Figure 8)
PMID:35314193	PBO:0094738	(Figure 12)
PMID:35314193	PBO:0094777	(Figure 12)
PMID:35314193	PBO:0098307	(Figure 8)
PMID:35320724	FYPO:0002061	(Figure 4)
PMID:35320724	FYPO:0002060	(Figure 5)
PMID:35320724	FYPO:0002061	(Figure 5)
PMID:35320724	PBO:0107693	(Figure 4)
PMID:35320724	PBO:0107690	(Figure 4)
PMID:35320724	FYPO:0002060	(Figure 4)
PMID:35320724	PBO:0107689	(Figure S6G)
PMID:35320724	PBO:0107690	(Figure 1B, 2D, 5B, 6C, 7B, 7C)
PMID:35320724	PBO:0107691	(Figure 1B, 5B)
PMID:35320724	PBO:0107692	(Figure 1B, 5B)
PMID:35320724	PBO:0096891	(Figure 4)
PMID:35320724	FYPO:0002061	(Figure S6D)
PMID:35320724	FYPO:0002060	(Figure 4)
PMID:35320724	FYPO:0001234	(Figure 4)
PMID:35320724	FYPO:0002060	(Figure 6)
PMID:35320724	FYPO:0001489	(Figure 6)
PMID:35320724	FYPO:0002061	(Figure 6)
PMID:35320724	FYPO:0002060	(Figure 6)
PMID:35320724	FYPO:0002061	(Figure 6)
PMID:35320724	FYPO:0002060	(Figure 6)
PMID:35320724	PBO:0107698	(Figure 5)
PMID:35320724	PBO:0107697	(Figure 5)
PMID:35320724	PBO:0107696	(Figure 5)
PMID:35320724	PBO:0107695	(Figure 4)
PMID:35320724	FYPO:0002060	(Figure 4)
PMID:35320724	PBO:0107694	(Figure 4)
PMID:35320724	FYPO:0001489	(Figure 2C)
PMID:35320724	FYPO:0001489	(Figure 2A) even if securin levels were elevated to only about eight times the wild-type level (Kamenz et al., 2015) (Figure 2A
PMID:35320724	PBO:0107692	(Figure S1)
PMID:35320724	FYPO:0001491	(Figure 2C)
PMID:35320724	FYPO:0001491	(Figure 2C)
PMID:35320724	PBO:0107691	(Figure 3, S1)
PMID:35320724	PBO:0107690	(Figure 3, S1)
PMID:35320724	PBO:0107690	(Figure S6B)
PMID:35320724	PBO:0107690	(Figure 6)
PMID:35320724	PBO:0107707	(Figure 3a) Similar results were obtained for Cdc13-GFP (Figure S1). Hence securin and Cdc13 are still efficiently targeted for proteasomal degradation in the cdc48-353 mutant.
PMID:35320724	PBO:0107706	(Figure 3a) However, the cellular degradation kinetics of securin-GFP were indistinguishable in cdc48+ and cdc48-353 mutant cells after normalizing for the reduced level (Figure 3A), suggesting that securin degradation was unaffected in the cdc48-353 mutant.
PMID:35320724	FYPO:0004705	Consistent with the low levels of separase, we found that sister chromatid separation was delayed in cdc48- 353 mutant cells relative to the decline in CDK1 activity at mitotic exit (Figure 1C).
PMID:35320724	PBO:0107702	(Figure 5)
PMID:35320724	FYPO:0001489	(Figure 6)
PMID:35320724	PBO:0107690	(Figure S7)
PMID:35320724	PBO:0107705	(Figure S5)
PMID:35320724	PBO:0107704	(Figure S5)
PMID:35320724	PBO:0107702	(Figure S4)
PMID:35320724	PBO:0107703	(Figure 4)
PMID:35320724	PBO:0107702	(Figure 4)
PMID:35320724	PBO:0107700	(Figure 7)
PMID:35320724	PBO:0107700	(Figure 7)
PMID:35320724	PBO:0107701	(Figure 7)
PMID:35320724	PBO:0107700	(Figure 7)
PMID:35320724	PBO:0107699	(Figure 7)
PMID:35320724	PBO:0107699	(Figure 7)
PMID:35325114	FYPO:0007990	(comment: CHECK TERM REQUESTED growth auxotrophic for isoleucine)
PMID:35325114	FYPO:0007991	(comment: CHECK TERM REQUESTED growth auxotrophic for valine)
PMID:35333350	FYPO:0007945	(Figure 6B). The alignment index of chromosome 1 at meiotic prophase (2.5 h) decreased in rec8-F204S (1.6) compared with the wild-type (rec8-wt, 2.6)
PMID:35333350	FYPO:0003613	(Figure 5C) The rec8-F204S mutant maintained sister chromatid cohesion as assessed at the cut3 gene locus
PMID:35333350	FYPO:0002485	(Figure 7) rec8-F204S mutant is defective in LinE formation and recombination
PMID:35333350	FYPO:0000900	(Figure 7) rec8-F204S mutant is defective in LinE formation and recombination (Rec10-mCherry forms aberrant dotty or filamentous aggregates within the nucleus, similar to rec8∆.)
PMID:35333350	PBO:0102339	These results sugest that in the rec8-F204S mutant, as in rec8Δ, the Rec8- dependent meiosis-specific short chromatin loop structures are lost, resulting in a concomitant loss of the structural property of the chromosome required for proper alignment.
PMID:35333350	FYPO:0000197	Supplementary Figure S4B) wpl1Δ rarely showed torsional turning (Supplementary Figure S4C, Supplemental Movies 1, and 2) during horsetail movements that is important for the alignment of homologs
PMID:35333350	FYPO:0007939	(Figures 2A and B) Hi-C analysis for rec10Δ and rec12Δ cells showed X-shaped contacts similar to wild-type cells AND (Figure 3A).... punctate Hi-C interactions observed in the wild-type were mostly lost in rec8Δ
PMID:35333350	FYPO:0002890	(Figure 5D, Supplemental Movies 1, and 3) In the rec8-F204S mutant, only the leading edge of the nucleus followed the horsetail movement, while the bulk of chromosomes were left behind, similar to rec8Δ
PMID:35333350	FYPO:0007944	(comment: DECREASED NUMBER) (Figure 6 and Figure 5e, S6BC) defective loop formation also supported by increased distance between the telomere-ade8 distance was longer in the rec8-F204S mutant than in the wild-type, suggesting that the chromatin of the rec8-F204S mutant was flexible and was abnormally stretched by the traction of the horsetail movement
PMID:35333350	FYPO:0003054	(comment: CHECK during horsetail/ prophase)
PMID:35333350	GO:0007129	These results suggest that Wpl1 plays a role in alignment of homologs through Rec8-dependent formation of axis-loop chromatin structure.
PMID:35333350	FYPO:0007939	(Figures 2A and B) Hi-C analysis for rec10Δ and rec12Δ cells showed X-shaped contacts similar to wild-type cells AND (Figure 3A).... punctate Hi-C interactions observed in the wild-type were mostly lost in rec8Δ
PMID:35333350	GO:0007129	These results suggest that Wpl1 plays a role in alignment of homologs through Rec8-dependent formation of axis-loop chromatin structure.
PMID:35333350	FYPO:0001357	(Figure S5B)
PMID:35333350	FYPO:0001357	(Figure S5B)
PMID:35333350	FYPO:0007942	(Figure 4c,e) Fluorescence images of Rec8- GFP showed that axial structures in meiotic chromosomes were more prominent in wpl1Δ than in the wild-type
PMID:35333350	FYPO:0003179	(Figure 7)
PMID:35333350	FYPO:0007945	(Figure S4B)
PMID:35333350	FYPO:0002092	rec8-S552P and rec8Δ, which showed the cohesion defect, were used as a control strain (see Supplementary Figure S5C, S5D, and S5E for details of the rec8-S552P mutant)
PMID:35354597	FYPO:0003750	(Fig. 2D)
PMID:35354597	FYPO:0003750	(Fig. 2C)
PMID:35354597	FYPO:0003750	(Fig. 2C)
PMID:35354597	FYPO:0003750	(Fig. 2C)
PMID:35354597	FYPO:0003750	(Fig. 2B)
PMID:35354597	FYPO:0003750	(Fig. 2D)
PMID:35354597	PBO:0112110	(Fig. 3A, B and C)
PMID:35354597	FYPO:0008171	(Fig. 3D)
PMID:35354597	PBO:0112111	(Fig. 3E)
PMID:35354597	FYPO:0003750	(Fig. 2B)
PMID:35354597	GO:0051292	Continued NPC assembly in cdc25.22 arrested cells that have low Cdk1 activity suggests that unlike in metazoans, Cdk1 (SpCdc2) is not required for NPC assembly in S. pombe.
PMID:35354597	PBO:0112115	(Fig. 6E)
PMID:35354597	PBO:0112114	(Fig. 6D)
PMID:35354597	PBO:0112113	(Fig. 6D)
PMID:35354597	PBO:0112113	(Fig. 6D)
PMID:35354597	PBO:0112113	(Fig. 6D)
PMID:35354597	PBO:0112114	(Fig. 6B)
PMID:35354597	PBO:0112114	(Fig. 6B)
PMID:35354597	PBO:0112113	(Fig. 6B)
PMID:35354597	GO:0044732	(Fig. 6A)
PMID:35354597	PBO:0112112	NPC clusters in nup132Δ nuclei coalesced into larger clusters that preferentially localized to the SPBs in mitosis. Fig. 3F
PMID:35354597	GO:0044732	(Fig. 5)
PMID:35354597	GO:0044732	(Fig. 5F)
PMID:35354597	GO:0044732	(Fig. 5F)
PMID:35354597	GO:0044732	(Fig. 5F)
PMID:35354597	GO:0044732	(Fig. 5F)
PMID:35354597	GO:0044732	(Fig. 5F)
PMID:35416247	PBO:0092325	(comment: CHECK in presence of tschimganine)
PMID:35416247	PBO:0095654	(comment: CHECK in presence of tschimganine)
PMID:35416247	PBO:0095654	(comment: CHECK in presence of tschimganine)
PMID:35416247	PBO:0095654	(comment: CHECK in presence of tschimganine)
PMID:35416247	PBO:0095654	(comment: CHECK in presence of tschimganine)
PMID:35416247	PBO:0092325	(comment: CHECK in presence of tschimganine)
PMID:35416247	PBO:0092325	(comment: CHECK in presence of tschimganine)
PMID:35416247	PBO:0092325	(comment: CHECK in presence of tschimganine)
PMID:35512546	GO:0008266	(comment: At RRM3 motif)
PMID:35536002	PBO:0100390	(Fig. 7)
PMID:35536002	PBO:0100391	(Fig. 7)
PMID:35536002	PBO:0100391	(Fig. 7)
PMID:35536002	PBO:0100392	(Fig. 7)
PMID:35536002	PBO:0100392	(Fig. 7)
PMID:35536002	PBO:0100392	(Fig. 7)
PMID:35536002	PBO:0100393	(Fig. 7)
PMID:35536002	PBO:0100393	(Fig. 7)
PMID:35536002	PBO:0100391	(Fig. 12) (Note how the levels are the same as when the pyrophosphatase is inactivated in the full-length protein)
PMID:35536002	PBO:0100394	(Fig. 8, 12)
PMID:35536002	PBO:0100395	(Fig. 12)
PMID:35536002	PBO:0100389	(Fig. 8) and text
PMID:35536002	PBO:0100390	(Fig. 7)
PMID:35536002	PBO:0100390	(Fig. 7)
PMID:35536002	PBO:0100396	(Fig. 8)
PMID:35536002	PBO:0100395	(Fig. 8)
PMID:35536002	PBO:0100394	(Fig. 12)
PMID:35536002	PBO:0100394	(Fig. 12)
PMID:35536002	PBO:0100396	(Fig. 8)
PMID:35536002	PBO:0100396	(Fig. 8)
PMID:35536002	PBO:0114323	(Fig. 1)
PMID:35536002	PBO:0114324	(Fig. 1)
PMID:35536002	PBO:0100390	(Fig. 7)
PMID:35536002	PBO:0100390	(Fig. 7)
PMID:35609605	PBO:0099981	(Figure 4D)
PMID:35609605	PBO:0099982	(Figure 4D)
PMID:35609605	PBO:0099979	(comment: COMPACTION )Figures 3A, 3B, and S3A (inhibiting exocytosis rescues defect of compaction)
PMID:35609605	PBO:0099978	Incomplete ring compaction was still observed in myo2- E1pil1D, although such fraction was reduced as compared with myo2-E1 (Figure 3B) (comment: I don't see the images - this is from the bar chart))
PMID:35609605	PBO:0099978	Incomplete ring compaction was still observed in myo2- E1pil1D, although such fraction was reduced as compared with myo2-E1 (Figure 3B) (comment: I don't see the images - this is from the bar chart))
PMID:35609605	PBO:0099980	(comment: COMPACTION) Figures 3A, 3B, and S3A
PMID:35609605	PBO:0099977	(Figure 3) (comment: COMPACTION)
PMID:35609605	FYPO:0001009	"(Figures 3A, 3B, and S3A)(comment: no rescue dan says ""FigS3A (bottom panel) shows that ring compaction completely failed in scs2Δscs22Δmyo2-E1(aaG345R) at 36 degree. In fact, we did not directly show that these cells failed ring contraction similarly as myo2-E1(aaG345R) at high temperature (which is well known) in the paper, as we mainly focused on ring compaction process. But we have implied that in the context."""
PMID:35609605	PBO:0099976	(Fig. S3C bottom panel) (comment: COMPACTION I asked is this the correct genotype? Dan answered: Our quantification in FigS3C bottom panel shows that ring compaction is slightly faster in scs2Δscs22Δmyo2-E1 than wt at 24 degree, although such a difference is not significant quantitatively. Qualitatively, compaction -in terms of mobility of individual nodes was indeed faster. So, I felt reluctant to use either “normal” or “abnormal” to describe that.)
PMID:35609605	FYPO:0003339	and is already defective in actomyosin  17 compaction at the permissive temperature of 24 C (Figure S1C, video S2) and (Figures 3A, 3B, and S3A))
PMID:35622906	PBO:0113860	(comment: CHECK OLD SPB)
PMID:35639710	PBO:0104695	Second, Any1R175C does not show an increase but rather a strong decrease in its ubiquitination level.
PMID:35639710	PBO:0104696	(Fig. 1)
PMID:35639710	PBO:0097854	(Figure 3) (comment: confirms dominance of can1-1)
PMID:35639710	PBO:0104698	(comment: CHECK Increased protein ubiquitination.)
PMID:35639710	PBO:0097854	(Figure 1)
PMID:35639710	PBO:0104699	(Figure 2A)
PMID:35639710	FYPO:0001545	(Figure 1) (comment: same as WT)
PMID:35639710	PBO:0104696	(Fig. 1)
PMID:35657410	FYPO:0008395	Deletion of ppr2 also increased the sensitivity of cells to ferrous iron (Fe2+) and ferric iron (Fe3+) (Fig. 1b).
PMID:35657410	FYPO:0001934	However, DFO could not enables growth of Δppr2 cells on glycerol medium, which requires mitochondrial respiration, suggesting that DFO could not rescue of the respiratory growth defect of Δppr2 cells (Fig. 1d)
PMID:35657410	PBO:0119724	(Table 2)
PMID:35657410	FYPO:0008395	+ Fe2(SO4)3 Deletion of ppr2 also increased the sensitivity of cells to ferrous iron (Fe2+) and ferric iron (Fe3+) (Fig. 1b).
PMID:35657410	PBO:0119725	(Table 2)
PMID:35657410	FYPO:0008397	Increased lipid peroxidation was detected in Δppr2 cells
PMID:35657410	FYPO:0001310	We found that DFO significantly increases the viability of Δppr2 cells (Fig. 1c). (normal compared to WT)
PMID:35657410	FYPO:0008396	+ Fe2(SO4)3 Deletion of ppr2 also increased the sensitivity of cells to ferrous iron (Fe2+) and ferric iron (Fe3+) (Fig. 1b).
PMID:35657410	PBO:0093606	As shown in Fig. 1a, Δppr2 cells progressively lost viability during growth in YES medium (Fig. 1a)
PMID:35657410	PBO:0119727	(Table 2)
PMID:35657410	PBO:0119723	(Table 2)
PMID:35657410	PBO:0110745	(Table 2)
PMID:35657410	PBO:0119722	(Table 2)
PMID:35657410	PBO:0113677	(Table 2)
PMID:35657410	PBO:0119721	(Table 2)
PMID:35657410	PBO:0110747	(Table 2)
PMID:35657410	PBO:0110737	(Table 2)
PMID:35657410	PBO:0110732	(Table 2)
PMID:35657410	FYPO:0008399	Increased lipid peroxidation was detected in Δppr2 cells
PMID:35657410	FYPO:0001934	However, DFO could not enables growth of Δppr2 cells on glycerol medium, which requires mitochondrial respiration, suggesting that DFO could not rescue of the respiratory growth defect of Δppr2 cells (Fig. 1d)
PMID:35657410	FYPO:0001934	However, deletion of frp1 could not rescue respiratory growth defect in Δppr2 cells as Δppr2Δfrp1 could not grow on glycerol medium (Fig. 4b).
PMID:35657410	PBO:0119726	(Table 2)
PMID:35658118	FYPO:0002009	Three independent experiments consistently showed that the oxygen consumption rate of acb1Δ cells was significantly decreased when the cells were cultured in nutrient-rich medium (i.e. YE) (Fig. 3B).
PMID:35658118	PBO:0110554	(Figure 2c)
PMID:35658118	PBO:0110554	(Figure 2c)
PMID:35658118	PBO:0110553	(Figure 2c)
PMID:35658118	FYPO:0009007	Therefore, increased cell death rather than abnormal cell division was the consequence of the impaired cell proliferation caused by the absence of Acb1 (Fig. 3D).
PMID:35658118	FYPO:0008137	Intriguingly, the size of lipid droplets became larger and the number of lipid droplets became less as acb1+ and acb1Δ+acb1 cells grew older in nutrient-rich medium (Fig. 4C,D). By contrast, the size and number of lipid droplets did not change as acb1Δ cells grew older in nutrient-rich medium (Fig. 4C,D).
PMID:35658118	PBO:0107530	Therefore, increased cell death rather than abnormal cell division was the consequence of the impaired cell proliferation caused by the absence of Acb1 (Fig. 3D).
PMID:35658118	PBO:0109726	he expression of Dnm1 was comparable in wild-type and acb1Δ cells (Fig. 2E).
PMID:35658118	PBO:0093797	(comment: phenotypoe seems to be additive on glycerol) Consistently, the growth of acb1Δ and acb1Δdnm1Δ cells on nonfermentable medium plates (YE plates plus 0.1% glucose and 3% glycerol) was comparable but was slower than the growth of WT and dnm1Δ cells (Fig. 2D,F).
PMID:35658118	PBO:0110551	(Figure 2a, 2b)
PMID:35658118	PBO:0110551	(Figure 2a, 2b)
PMID:35658118	PBO:0112557	By contrast, mitochondria became fragmented/aggregated (74.4%) PLUS This result indicates that mitochondrial mass/biogenesis was reduced by the absence of Acb1 or Dnm1. Note that dnm1-deletion in acb1Δ cells did not restore mitochondrial mass (Fig. 2C)
PMID:35658118	PBO:0112556	Consistent with the finding reported previously by our group [8], mitochondria formed a highly branch network (47.8%) in dnm1Δ cells (Fig. 2A,B)
PMID:35658118	PBO:0093798	As shown in Fig. 1B, acb1Δ grew slightly slower on fermentable medium than acb1+ cells and much slower on nonfermentable medium.
PMID:35658118	PBO:0093559	(Figure 1b, 3c)
PMID:35658118	FYPO:0001357	(Figure 1b, 3C)
PMID:35658118	PBO:0110548	We noticed that mitochondrial fragmentation caused by the absence of Acb1 was more apparent when cells were cultured in nutrient-rich medium than in minimal medium.
PMID:35658118	PBO:0110547	Microscopic observation showed that mitochondria were tubular in acb1+ cells but became fragmented in acb1Δ cells (Fig. 1A).
PMID:35673994	PBO:0108173	(Fig. 2B)
PMID:35673994	FYPO:0006108	(Fig. 6)
PMID:35673994	PBO:0108178	(Fig. 6)
PMID:35673994	PBO:0102716	(Fig. 4E)
PMID:35673994	PBO:0102716	(Fig. 4E)
PMID:35673994	PBO:0108173	(Fig. 2B)
PMID:35673994	PBO:0108172	(Fig. 2B)
PMID:35673994	FYPO:0005989	(Fig. 2A)
PMID:35673994	PBO:0108178	(Fig. 2B)
PMID:35673994	PBO:0102728	(Fig. 6)
PMID:35673994	PBO:0108175	(Fig. 5)
PMID:35673994	PBO:0108171	(Fig. 2B)
PMID:35673994	PBO:0102728	(comment: chimera expressed from the ura4 locus [@ura4] - kept because not assayed from fus1 locus)
PMID:35673994	PBO:0102727	(Fig. 2H)
PMID:35673994	PBO:0102726	(Fig. 2C)
PMID:35673994	FYPO:0006108	(Fig. 5)
PMID:35673994	PBO:0102728	(Fig. 5)
PMID:35673994	PBO:0102726	(Fig. 5)
PMID:35673994	FYPO:0006108	(Fig. 5)
PMID:35673994	PBO:0102727	(Fig. 5)
PMID:35673994	FYPO:0006108	(Fig. 5)
PMID:35673994	FYPO:0006108	(Fig. 6)
PMID:35673994	PBO:0108170	(Fig. 3)
PMID:35673994	PBO:0108178	(Fig. 5)
PMID:35673994	PBO:0108178	(Fig. 6)
PMID:35673994	FYPO:0007683	(Fig. 3)
PMID:35673994	PBO:0102720	(Fig. 2D)
PMID:35673994	PBO:0108177	(Fig. 5F)
PMID:35673994	PBO:0102728	(Fig. 5C)
PMID:35673994	PBO:0108175	(Fig. 5)
PMID:35673994	PBO:0108176	(Fig. 5)
PMID:35673994	PBO:0102728	(Fig. 5)
PMID:35673994	PBO:0108175	(Fig. 4E)
PMID:35673994	PBO:0108174	(Fig. 4E)
PMID:35673994	FYPO:0006108	(Fig. 6)
PMID:35673994	PBO:0102726	(Fig. 6)
PMID:35781263	PBO:0103077	"The Δght5 strain is always in 27 a ""low glucose state"" even when cultured in high glucose medium, and this may be the reason why the 28 lifespan extension phenotype appears."
PMID:35781263	PBO:0108273	(comment: CHECK decreased)
PMID:35820914	FYPO:0001309	we have found that deletion of the fission genes dnm1 or fis1 caused a significant increase of longevity whereas the loss of the fusion GTPase Msp1 had no effect on lifespan (Fig. 5C).
PMID:35820914	FYPO:0003811	Interestingly, the short-lived mutant yta12Δ displayed aggregated mitochondria at the cell poles similar to msp1Δ cells, suggesting that this matrix protease may participate in the regulation of mitochondrial fusion (Fig. 5D, E).
PMID:35820914	FYPO:0000565	In contrast, long-lived mutants mgr3Δ and yme1Δ displayed a normal growth in low glucose conditions (Fig. 4A).
PMID:35820914	PBO:0116458	(Fig. 4E) show that the levels of Cox1, Cox2, Cox3, and Atp6 proteins are similar in wild-type and the long-lived mutants mgr3Δ and yme1Δ. However, the blots demonstrate highly reduced levels of these proteins in lon1Δ and yta12Δ mutants which might explain the respi
PMID:35820914	FYPO:0003004	(vw: increased hydrogen peroxide formation) In contrast, the yta12Δ strain displayed enhanced levels of basal probe oxidation (OxD0 of 0.46) at the mitochondrial matrix compared to the wild-type strain (OxD0 of 0.4), indicative of higher steady-state levels of H2O2 (Additional file 5: Fig. S2). Cells lacking Lon1 displayed a slight increase in basal oxidation of MTS-Hyper7, suggesting that both short-lived mutants show enhanced production of mitochondrial ROS (Additional file 5: Fig. S2).
PMID:35820914	PBO:0116459	(Fig. 4E) show that the levels of Cox1, Cox2, Cox3, and Atp6 proteins are similar in wild-type and the long-lived mutants mgr3Δ and yme1Δ. However, the blots demonstrate highly reduced levels of these proteins in lon1Δ and yta12Δ mutants which might explain the respi
PMID:35820914	PBO:0116460	(Fig. 4E) show that the levels of Cox1, Cox2, Cox3, and Atp6 proteins are similar in wild-type and the long-lived mutants mgr3Δ and yme1Δ. However, the blots demonstrate highly reduced levels of these proteins in lon1Δ and yta12Δ mutants which might explain the respi
PMID:35820914	FYPO:0000245	Moreover, cells lacking the protease Yme1 displayed increased lifespan in a similar manner to mgr3Δ mutant, whereas the loss of the protease Yta12 resulted in a significant reduction of longevity (Fig. 3B).
PMID:35820914	PBO:0116461	(Fig. 4E) show that the levels of Cox1, Cox2, Cox3, and Atp6 proteins are similar in wild-type and the long-lived mutants mgr3Δ and yme1Δ. However, the blots demonstrate highly reduced levels of these proteins in lon1Δ and yta12Δ mutants which might explain the respi
PMID:35820914	PBO:0112960	(0.08% Glu) that promote respiratory metabolism (Fig. 4A). We observed that the short-lived mutants lon1Δ and yta12Δ showed a severe growth defect in respiratory-prone media, comparable to that detected in cox6Δ lacking a subunit of the ETC complex IV
PMID:35820914	FYPO:0000245	Lack of the mitochondrial protease Lon1 reduced longevity whereas the absence of Mgr3, adaptor protein of the protease Yme1 [13], led to increased lifespan.
PMID:35820914	PBO:0116461	(Fig. 4E) show that the levels of Cox1, Cox2, Cox3, and Atp6 proteins are similar in wild-type and the long-lived mutants mgr3Δ and yme1Δ. However, the blots demonstrate highly reduced levels of these proteins in lon1Δ and yta12Δ mutants which might explain the respi
PMID:35820914	FYPO:0000342	(0.08% Glu) that promote respiratory metabolism (Fig. 4A). We observed that the short-lived mutants lon1Δ and yta12Δ showed a severe growth defect in respiratory-prone media, comparable to that detected in cox6Δ lacking a subunit of the ETC complex IV
PMID:35820914	FYPO:0003004	In contrast, the yta12Δ strain displayed enhanced levels of basal probe oxidation (OxD0 of 0.46) at the mitochondrial matrix compared to the wild-type strain (OxD0 of 0.4), indicative of higher steady-state levels of H2O2 (Additional file 5: Fig. S2). Cells lacking Lon1 displayed a slight increase in basal oxidation of MTS-Hyper7, suggesting that both short-lived mutants show enhanced production of mitochondrial ROS (Additional file 5: Fig. S2).
PMID:35820914	PBO:0116459	(Fig. 4E) show that the levels of Cox1, Cox2, Cox3, and Atp6 proteins are similar in wild-type and the long-lived mutants mgr3Δ and yme1Δ. However, the blots demonstrate highly reduced levels of these proteins in lon1Δ and yta12Δ mutants which might explain the respi
PMID:35820914	PBO:0116458	(Fig. 4E) show that the levels of Cox1, Cox2, Cox3, and Atp6 proteins are similar in wild-type and the long-lived mutants mgr3Δ and yme1Δ. However, the blots demonstrate highly reduced levels of these proteins in lon1Δ and yta12Δ mutants which might explain the respi
PMID:35820914	FYPO:0007737	we detected a significant loss of ΔΨ in yta12Δ mutant and increased ΔΨ in yme1Δ cells, both results in consonance with our previous findings (Fig. 4C, Additional file 4: Fig. S1).
PMID:35820914	FYPO:0004944	we detected a significant loss of ΔΨ in yta12Δ mutant and increased ΔΨ in yme1Δ cells, both results in consonance with our previous findings (Fig. 4C, Additional file 4: Fig. S1).
PMID:35820914	FYPO:0000342	cells lacking Lon1 or Yta12 displayed decreased respiratory capacity in high and low glucose (Fig. 4B)
PMID:35820914	FYPO:0000342	cells lacking Lon1 or Yta12 displayed decreased respiratory capacity in high and low glucose (Fig. 4B)
PMID:35820914	FYPO:0003811	Interestingly, the short-lived mutant yta12Δ displayed aggregated mitochondria at the cell poles similar to msp1Δ cells, suggesting that this matrix protease may participate in the regulation of mitochondrial fusion (Fig. 5D, E).
PMID:35820914	FYPO:0001309	we have found that deletion of the fission genes dnm1 or fis1 caused a significant increase of longevity whereas the loss of the fusion GTPase Msp1 had no effect on lifespan (Fig. 5C).
PMID:35820914	PBO:0103077	Moreover, cells lacking the protease Yme1 displayed increased lifespan in a similar manner to mgr3Δ mutant, whereas the loss of the protease Yta12 resulted in a significant reduction of longevity (Fig. 3B). This increase in the respiratory activity was more evident for yme1Δ mutant in high glucose medium (Fig. 4B, left panel).
PMID:35820914	PBO:0116460	(Fig. 4E) show that the levels of Cox1, Cox2, Cox3, and Atp6 proteins are similar in wild-type and the long-lived mutants mgr3Δ and yme1Δ. However, the blots demonstrate highly reduced levels of these proteins in lon1Δ and yta12Δ mutants which might explain the respi
PMID:35820914	FYPO:0001309	Lack of the mitochondrial protease Lon1 reduced longevity whereas the absence of Mgr3, adaptor protein of the protease Yme1 [13], led to increased lifespan.
PMID:35820914	FYPO:0000565	In contrast, long-lived mutants mgr3Δ and yme1Δ displayed a normal growth in low glucose conditions (Fig. 4A).
PMID:35901126	FYPO:0001357	Similarly, the temperature sensitivity of the S. pombe trm61Δ strain was completely suppressed by expression of the stand-alone imt06+ gene (S5 Fig).
PMID:35901126	PBO:0093558	(Fig. S1)
PMID:35901126	PBO:0093558	(Fig. S1)
PMID:35901126	PBO:0111628	Examination by HPLC of the nucleoside composition of purified tRNATyr(GUA) from trm6Δ and trm61Δ mutants revealed that m1A levels were less than 0.03 moles/mole, compared to 0.60 moles/mole in WT cells, whereas levels of C, m5C, and m7G were very similar in the tRNATyr(GUA) from both mutant and WT cells (Fig 1B and 1C)
PMID:35901126	PBO:0111628	Examination by HPLC of the nucleoside composition of purified tRNATyr(GUA) from trm6Δ and trm61Δ mutants revealed that m1A levels were less than 0.03 moles/mole, compared to 0.60 moles/mole in WT cells, whereas levels of C, m5C, and m7G were very similar in the tRNATyr(GUA) from both mutant and WT cells (Fig 1B and 1C)
PMID:35901126	PBO:0111629	Similarly, poison primer extension showed that tRNAiMet(CAU) was nearly completely modified with m1A58 in WT cells (97%), but not visibly modified in trm6Δ and trm61Δ mutants (although quantification with the high background gave 2.0% for trm6Δ and 2.8% in trm61Δ).
PMID:35901126	PBO:0111630	Similarly, poison primer extension showed that tRNAiMet(CAU) was nearly completely modified with m1A58 in WT cells (97%), but not visibly modified in trm6Δ and trm61Δ mutants (although quantification with the high background gave 2.0% for trm6Δ and 2.8% in trm61Δ).
PMID:35901126	PBO:0111631	These results show that S. pombe trm6+ and trm61+ are required for all detectable m1A58 modification of cytoplasmic tRNAs.
PMID:35901126	PBO:0111631	These results show that S. pombe trm6+ and trm61+ are required for all detectable m1A58 modification of cytoplasmic tRNAs.
PMID:35901126	PBO:0111632	The northern analysis revealed that tRNAiMet(CAU) levels were substantially reduced in the S. pombe trm6Δ mutants, both at 30 ̊C and 38.5 ̊C. At 30 ̊C, tRNAiMet(CAU) levels were 49% of those in WT cells, whereas each of the other eight tRNAs had levels between 82% and 121% of those in WT cells (Figs 2A, 2B and S3).
PMID:35901126	FYPO:0000674	Similarly, the temperature sensitivity of the S. pombe trm61Δ strain was completely suppressed by expression of the stand-alone imt06+ gene (S5 Fig).
PMID:35901126	FYPO:0000674	Similarly, the temperature sensitivity of the S. pombe trm61Δ strain was completely suppressed by expression of the stand-alone imt06+ gene (S5 Fig).
PMID:35901126	FYPO:0000674	We found that the temperature sensitive growth defect of S. pombe trm6Δ mutants on EMMC-leu media was completely suppressed by expression of the stand-alone imt06+ gene, growing identically to that of an S. pombe trm6Δ [Ptrm6 trm6+] strain at high temperature (Fig 2C)
PMID:35901126	FYPO:0000674	We found that the temperature sensitive growth defect of S. pombe trm6Δ mutants on EMMC-leu media was completely suppressed by expression of the stand-alone imt06+ gene, growing identically to that of an S. pombe trm6Δ [Ptrm6 trm6+] strain at high temperature (Fig 2C)
PMID:35901126	PBO:0093556	Growth analysis on plates showed that the trm6Δ dhp1-5 and trm6Δ dhp1-6 mutants were nearly as healthy at high temperatures as the WT strain on both YES and EMMC-his media, whereas the trm6Δ tol1-1 mutant was slightly less healthy at higher temperatures (Fig 3A).
PMID:35901126	PBO:0093556	Growth analysis on plates showed that the trm6Δ dhp1-5 and trm6Δ dhp1-6 mutants were nearly as healthy at high temperatures as the WT strain on both YES and EMMC-his media, whereas the trm6Δ tol1-1 mutant was slightly less healthy at higher temperatures (Fig 3A).
PMID:35901126	PBO:0093556	Growth analysis on plates showed that the trm6Δ dhp1-5 and trm6Δ dhp1-6 mutants were nearly as healthy at high temperatures as the WT strain on both YES and EMMC-his media, whereas the trm6Δ tol1-1 mutant was slightly less healthy at higher temperatures (Fig 3A).
PMID:35901126	PBO:0093556	Growth analysis on plates showed that the trm6Δ dhp1-5 and trm6Δ dhp1-6 mutants were nearly as healthy at high temperatures as the WT strain on both YES and EMMC-his media, whereas the trm6Δ tol1-1 mutant was slightly less healthy at higher temperatures (Fig 3A).
PMID:35901126	PBO:0111633	Northern analysis of tRNA from strains grown at 30 ̊C and after temperature shift to 38.5 ̊C showed that the dhp1 and tol1 suppressors substantially restored tRNAiMet(CAU) levels at both high and low temperatures, without affecting any of a number of other tRNAs (Fig 3B and 3C).
PMID:35901126	PBO:0111633	Northern analysis of tRNA from strains grown at 30 ̊C and after temperature shift to 38.5 ̊C showed that the dhp1 and tol1 suppressors substantially restored tRNAiMet(CAU) levels at both high and low temperatures, without affecting any of a number of other tRNAs (Fig 3B and 3C).
PMID:35901126	GO:0180037	The discovery of dhp1 and tol1 mutations as suppressors of the S. pombe trm6Δ temperature sensitivity demonstrates the involvement of the RTD pathway in decay of tRNAiMet(CAU) lacking m1A58 in S. pombe.
PMID:35901126	GO:0180037	The discovery of dhp1 and tol1 mutations as suppressors of the S. pombe trm6Δ temperature sensitivity demonstrates the involvement of the RTD pathway in decay of tRNAiMet(CAU) lacking m1A58 in S. pombe.
PMID:35901126	FYPO:0001357	Similarly, the temperature sensitivity of the S. pombe trm61Δ strain was completely suppressed by expression of the stand-alone imt06+ gene (S5 Fig).
PMID:35901126	PBO:0093558	As anticipated, the resulting trm6Δ imt06Δ strain grew very poorly at 30 ̊C, and was temperature sensitive at higher temperatures, not growing at all at 37 ̊C
PMID:35901126	PBO:0093558	As anticipated, the resulting trm6Δ imt06Δ strain grew very poorly at 30 ̊C, and was temperature sensitive at higher temperatures, not growing at all at 37 ̊C
PMID:35901126	PBO:0093560	As anticipated, the resulting trm6Δ imt06Δ strain grew very poorly at 30 ̊C, and was temperature sensitive at higher temperatures, not growing at all at 37 ̊C, These results show a prominent synthetic growth defect in the S. pombe trm6Δ imt06Δ strain, due only to reduced levels of tRNAiMet(CAU).
PMID:35901126	PBO:0093560	As anticipated, the resulting trm6Δ imt06Δ strain grew very poorly at 30 ̊C, and was temperature sensitive at higher temperatures, not growing at all at 37 ̊C, These results show a prominent synthetic growth defect in the S. pombe trm6Δ imt06Δ strain, due only to reduced levels of tRNAiMet(CAU).
PMID:35901126	PBO:0093558	We observed little, if any, suppression of the trm6Δ growth defect in the trm6Δ cid14Δ strains (S13A Fig), and only very minor restoration of tRNAiMet(CAU) levels at high temperature, relative to levels in trm6Δ mutants (21% vs 18%, compared to 39% in the trm6Δ dhp1-5 strain) (S13B and S13C Fig). Thus, we infer that tRNAiMet(CAU) is degraded in S. pombe trm6Δ and trm6Δ imt06Δ mutants primarily by the RTD pathway, and not appreciably by the TRAMP complex of the nuclear surveillance pathway.
PMID:35901126	PBO:0111633	Northern analysis of tRNA from strains grown at 30 ̊C and after temperature shift to 38.5 ̊C showed that the dhp1 and tol1 suppressors substantially restored tRNAiMet(CAU) levels at both high and low temperatures, without affecting any of a number of other tRNAs (Fig 3B and 3C).
PMID:35901126	PBO:0111633	Northern analysis of tRNA from strains grown at 30 ̊C and after temperature shift to 38.5 ̊C showed that the dhp1 and tol1 suppressors substantially restored tRNAiMet(CAU) levels at both high and low temperatures, without affecting any of a number of other tRNAs (Fig 3B and 3C).
PMID:35908934	PBO:0119626	(Fig. 6C)
PMID:35908934	PBO:0119626	(Fig. 6C)
PMID:35908934	PBO:0119624	(Fig. 6C)
PMID:35908934	FYPO:0008364	(Fig. 5D)
PMID:35908934	GO:0007535	We propose that the resultant chromatin organization is at least in part responsible for the altered donor choices in HULC and Set1C mutants (Fig. 7).
PMID:35908934	FYPO:0002336	(Fig. 6B)
PMID:35908934	FYPO:0002336	(Fig. 6B)
PMID:35908934	GO:0007535	We propose that the resultant chromatin organization is at least in part responsible for the altered donor choices in HULC and Set1C mutants (Fig. 7).
PMID:35908934	GO:0007535	We propose that the resultant chromatin organization is at least in part responsible for the altered donor choices in HULC and Set1C mutants (Fig. 7).
PMID:35908934	GO:0007535	We propose that the resultant chromatin organization is at least in part responsible for the altered donor choices in HULC and Set1C mutants (Fig. 7).
PMID:35908934	GO:0007535	We propose that the resultant chromatin organization is at least in part responsible for the altered donor choices in HULC and Set1C mutants (Fig. 7).
PMID:35908934	PBO:0119624	(Fig. 6C)
PMID:35908934	PBO:0119624	(Fig. 6C)
PMID:35908934	PBO:0119624	(Fig. 6C)
PMID:35908934	PBO:0119624	(Fig. 6C)
PMID:35908934	FYPO:0002336	(Fig. 6B)
PMID:35908934	FYPO:0002336	(Fig. 6B)
PMID:35908934	FYPO:0000468	(Fig. 2A)
PMID:35908934	FYPO:0002336	(Fig. 6B)
PMID:35908934	FYPO:0000468	(Fig. 2A)
PMID:35908934	FYPO:0000468	(Fig. 2A)
PMID:35908934	FYPO:0000708	(Fig. 2B)
PMID:35908934	FYPO:0000708	(Fig. 2B)
PMID:35908934	PBO:0119625	(Fig. 2A, Fig. 4A)
PMID:35908934	PBO:0119624	(Fig. 4C, Fig. 6C)
PMID:35908934	FYPO:0000708	(Fig. 2B)
PMID:35908934	FYPO:0000708	(Fig. 2B)
PMID:35908934	FYPO:0000969	(Fig. 2D)
PMID:35908934	FYPO:0000969	(Fig. 2D)
PMID:35908934	FYPO:0000969	(Fig. 2D)
PMID:35908934	FYPO:0000472	(Fig. 5C)
PMID:35908934	FYPO:0000472	(Fig. 5C)
PMID:35908934	PBO:0095651	(Fig. 6B)
PMID:35908934	PBO:0095651	(Fig. 6B)
PMID:35908934	PBO:0119624	(Fig. 4A)
PMID:35908934	PBO:0119624	(Fig. 4A)
PMID:35908934	FYPO:0000468	(Fig. 4D)
PMID:35908934	FYPO:0000472	(Fig. 4E)
PMID:35908934	FYPO:0000472	(Fig. 4E)
PMID:35908934	PBO:0112683	(Fig. 5B)
PMID:35908934	PBO:0112540	(Fig. 5B)
PMID:35908934	FYPO:0002355	(Fig. 5C)
PMID:35908934	FYPO:0006987	(Fig. 5C)
PMID:35908934	FYPO:0007509	(Fig. 5D)
PMID:35908934	PBO:0119625	(Fig. 6C)
PMID:35924983	PBO:0093561	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093561	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	PBO:0093559	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093559	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093560	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0109486	(Fig. 6)
PMID:35924983	PBO:0020040	(Fig. 6)
PMID:35924983	PBO:0093770	(Figure 3)
PMID:35924983	PBO:0109485	(comment: through nuclear exclusion)
PMID:35924983	PBO:0109485	(comment: through nuclear exclusion)
PMID:35924983	PBO:0109485	(comment: through degradation by ubiquitination)
PMID:35924983	PBO:0109485	(comment: through degradation by ubiquitination)
PMID:35924983	PBO:0093767	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093767	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001492	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001492	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093767	(Figure 3)
PMID:35924983	PBO:0093767	(Figure 3)
PMID:35924983	PBO:0109483	(Figure 6)
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	PBO:0093561	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093561	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093561	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093561	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093561	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093561	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	PBO:0109483	(Figure 6)
PMID:35924983	PBO:0109482	(Figure 6)
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	PBO:0109482	(Figure 6)
PMID:35924983	PBO:0093561	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093561	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	PBO:0109482	(Figure 6)
PMID:35924983	PBO:0109482	(Figure 6)
PMID:35924983	PBO:0109480	(Figure 7)
PMID:35924983	PBO:0109480	(Figure 7)
PMID:35924983	PBO:0109480	(Figure 7)
PMID:35924983	PBO:0109481	(Figure 7)
PMID:35924983	PBO:0109481	(Figure 7)
PMID:35924983	PBO:0109480	(Figure 7)
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	PBO:0093561	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093561	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093559	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0109480	(Figure 7)
PMID:35924983	FYPO:0009111	(Figure 7)
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093559	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	PBO:0093561	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093561	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	PBO:0093560	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093560	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35924983	PBO:0093560	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	FYPO:0001355	Supplemental Figure 4
PMID:35924983	PBO:0093561	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093561	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093560	Supplemental Figure 6
PMID:35940128	FYPO:0003480	(comment: Queuosine absent from tRNA when cells are supplied with queuosine nucleoside, but not when supplied with queuine nucleobase)
PMID:35970865	PBO:0105696	Note that an increase of transcript levels from centromeres has not been demonstrated in the paper. What has been exactly demonstrated is an increased association of RNA polII to the cnt region of centromeres.
PMID:35970865	PBO:0095634	(Fig. 2a) The resultant mis6-302 cut9-665 double mutant exhibited severe growth defects, even at the semi-restrictive temperature (Fig. 2a). This suggests that the mitotic function of Mis6 is crucial for prolonged metaphase.
PMID:35970865	PBO:0105695	(comment: CHECK normal CENP-A maintenance)
PMID:35970865	PBO:0095634	(Fig. 2a) The resultant mis6-302 cut9-665 double mutant exhibited severe growth defects, even at the semi-restrictive temperature (Fig. 2a). This suggests that the mitotic function of Mis6 is crucial for prolonged metaphase.
PMID:35970865	PBO:0105697	(Figure 2a) (comment: CHECK during M-phase)
PMID:35970865	FYPO:0008025	(comment: CHECK during M-phase) Mis15 localises to the inner regions of centromeres as does Mis6, while Mis12 and Nuf2 localise to the outer regions relative to Mis6, and Mis6 localised to centromeres in the mis12 and nuf2 mutants but not in the mis15 mutant (Supplementary Fig. 6)
PMID:35970865	FYPO:0008025	during M-phase Mis15 localises to the inner regions of centromeres as does Mis6, while Mis12 and Nuf2 localise to the outer regions relative to Mis6, and Mis6 localised to centromeres in the mis12 and nuf2 mutants but not in the mis15 mutant (Supplementary Fig. 6)
PMID:35970865	FYPO:0002360	(comment: CHECK during M-phase) Supplementary Fig. 9b). These results demonstrate that kinetochore mutants with the intact inner kinetochore architecture retained the ability to silence transcription at the central core region.
PMID:35970865	FYPO:0002360	(comment: CHECK during M-phase) Supplementary Fig. 9b). These results demonstrate that kinetochore mutants with the intact inner kinetochore architecture retained the ability to silence transcription at the central core region.
PMID:35970865	PBO:0093558	(Fig. 2a)
PMID:35970865	PBO:0105695	(comment: CHECK normal CENP-A maintenance)
PMID:35970865	PBO:0105695	(comment: CHECK normal CENP-A maintenance)
PMID:35970865	PBO:0103733	(comment: CHECK decreased CENP-A maintenance)
PMID:35970865	PBO:0105695	(comment: CHECK normal CENP-A maintenance)
PMID:35970865	PBO:0105694	(Figure 4)
PMID:35970865	PBO:0105693	(Figure 4)
PMID:35970865	PBO:0105692	Defective in CENP-A maintenance. Mis15 localises to the inner regions of centromeres as does Mis6, while Mis12 and Nuf2 localise to the outer regions relative to Mis6, and Mis6 localised to centromeres in the mis12 and nuf2 mutants but not in the mis15 mutant (Supplementary Fig. 6)In the mis15-68 mutants, signal intensities of Cnp1 at centromeres during mitotic arrest were decreased like in the mis6-302 mutant, whereas not in the mis12-537 and nuf2-2 mutants (Fig. 2h-j and Supplementary Figs. 5b-d and 7)
PMID:35970865	PBO:0093556	(Fig. 2a)
PMID:35970865	PBO:0105691	"(Fig. 2c, d) (comment: CHECK ""decreased CENP-A maintenance during M-phase"".) defective in CENP-A maintenance during M phase, as well as defective in CENP-A loading during interphase The GFP-Cnp1 intensity at centromeres decayed more rapidly in mis6-302 cells than in WT cells (Fig. 2f, g and Supplementary Figs. 4 and 5a). Taken together, these results suggest that Mis6, but not Scm3, is responsible for the maintenance of Cnp1 at centromeres during metaphase."
PMID:35970865	PBO:0095634	(Fig. 2a)
PMID:35970865	PBO:0095634	(Fig. 2a)
PMID:35970865	PBO:0105696	Note that an increase of transcript levels from centromeres has not been demonstrated in the paper. What has been exactly demonstrated is an increased association of RNA polII to the cnt region of centromeres.
PMID:35970865	PBO:0092503	When we followed the temporal kinetics of GFP- Cnp1 intensity during metaphase, the reduction of GFP-Cnp1 intensity seen in mis6-302 and mis15-68 cells was rescued by the additional knockout of Fft3 (mis6-302 fft3Δ, Supplementary Fig. 11a-c; mis15-68 fft3Δ, Supplementary Fig. 11d-f), confirming that Fft3 removes Cnp1 upon transcription at centromeres.
PMID:36002457	PBO:0108631	However, no significant changes were observed for several meiotic mRNAs and PROMPTs/CUTs MTREC targets (Supplementary Fig. 8b, c)
PMID:36002457	PBO:0110941	While A198E retained the WT level of binding (Fig. 2i, lanes 3 and 7), the L205R and F215R mutants no longer bound Iss10 (Fig. 2i, lanes 4, 5, 8 and 9).
PMID:36002457	PBO:0110942	While A198E retained the WT level of binding (Fig. 2i, lanes 3 and 7), the L205R and F215R mutants no longer bound Iss10 (Fig. 2i, lanes 4, 5, 8 and 9).
PMID:36002457	PBO:0110959	Interestingly, quantification of the intensity of the signal within each nucleus showed a reduction of Ars2-GFP nuclear signal in red1-E32R mutant cells compared to wild-type cells, suggesting that some of Ars2-GFP proteins diffuse to the cytoplasm (Supplementary Fig. 8e).
PMID:36002457	PBO:0116212	These findings indicate that the interaction of Iss10 with Red1 is required for Iss10 recruitment to Red1 nuclear foci and suggest that it may promote the clustering of Red1 nuclear foci.
PMID:36002457	PBO:0110946	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	PBO:0110947	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	PBO:0110948	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	PBO:0110949	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	PBO:0110948	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	PBO:0110947	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	PBO:0110950	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	PBO:0110951	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	PBO:0110952	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	PBO:0110953	In Strep-tag pull down assays, both mutations (K483D, F490D) essentially disrupted the Red1 binding (Supplementary Fig. 7d, lanes 3, 4).
PMID:36002457	PBO:0110944	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	PBO:0110943	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	PBO:0093555	Importantly, red1-L205R cells showed a similar growth defect, when grown on minimal medium, suggesting that Red1-Iss10 interaction can be important for Red1-dependent cell growth function depending on the environmental conditions (Fig. 3b).
PMID:36002457	PBO:0093555	While red1Δ cells showed only a moderate growth defect on solid rich medium at 30°C, this defect was more pronounced at lower temperature of 25 or 18°C (Supplementary Fig. 3b), as published previously14,34 or when the cells were grown on minimal medium (Supplementary Fig. 3c).
PMID:36002457	PBO:0110953	Using Y2H assays, we could show that the Red1 E32R mutation is sufficient to prevent the interaction with Ars2 in the context of full-length proteins (Fig. 5f). mportantly, while Red1-TAP and Ars2-GFP interact, as expected, this interaction was lost in cells expressing Red1-E32R-TAP (Fig. 5g).
PMID:36002457	PBO:0093555	A similar growth defect was visible for the red1-E32R-TAP mutant cells grown on minimal medium, suggesting that Red1-Ars2 interaction, depending on the growth conditions, can be important for the normal growth of the cell population (Fig. 5h).
PMID:36002457	PBO:0110954	However, no significant changes were observed for several meiotic mRNAs and PROMPTs/CUTs MTREC targets (Supplementary Fig. 8b, c)
PMID:36002457	PBO:0110958	We examined the possible effect of red1-E32R mutation on pho1 and byr2 mRNAs. However, no significant changes in pho1 and byr2 mRNA levels were observed between wild-type and red1-E32R mutant cells (Supplementary Fig. 8d).
PMID:36002457	PBO:0110957	We examined the possible effect of red1-E32R mutation on pho1 and byr2 mRNAs. However, no significant changes in pho1 and byr2 mRNA levels were observed between wild-type and red1-E32R mutant cells (Supplementary Fig. 8d).
PMID:36002457	PBO:0112760	However, no significant changes were observed for several meiotic mRNAs and PROMPTs/CUTs MTREC targets (Supplementary Fig. 8b, c)
PMID:36002457	PBO:0110955	However, no significant changes were observed for several meiotic mRNAs and PROMPTs/CUTs MTREC targets (Supplementary Fig. 8b, c)
PMID:36002457	PBO:0110942	Using these cells, reciprocal co-immunoprecipitation experiments showed that the Red1-L205R mutation also compromised Red1 association with Iss10 in S. pombe (Fig. 3a and Supplementary Fig. 3a).
PMID:36002457	PBO:0093555	While red1Δ cells showed only a moderate growth defect on solid rich medium at 30°C, this defect was more pronounced at lower temperature of 25 or 18°C (Supplementary Fig. 3b), as published previously1
PMID:36002457	PBO:0093559	While red1Δ cells showed only a moderate growth defect on solid rich medium at 30°C, this defect was more pronounced at lower temperature of 25 or 18°C (Supplementary Fig. 3b), as published previously1
PMID:36006032	FYPO:0005728	(Figure 1D)
PMID:36006032	FYPO:0005727	(Figure 1D)
PMID:36006032	PBO:0105587	(Figure 1D)
PMID:36006032	FYPO:0005728	(Figure 1D)
PMID:36006032	PBO:0105585	Overexpression of Par1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	PBO:0105585	Overexpression of Par1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	PBO:0105585	Overexpression of Ppa2 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	PBO:0105585	Overexpression of Ppa2 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	PBO:0105585	Overexpression of Ppa2 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	PBO:0105585	Overexpression of Ppa2 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	PBO:0105585	Overexpression of all Ppa1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	PBO:0105585	Overexpression of all Ppa1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	PBO:0105585	Pab1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrestand-release in the nda3-KM311 mutant background (Figure 2 and Figure S2).
PMID:36006032	PBO:0105585	Pab1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrestand-release in the nda3-KM311 mutant background (Figure 2 and Figure S2).
PMID:36006032	PBO:0105581	Our in vitro dephosphorylation assay results demonstrated that individually overexpressing PP2A subunits indeed boosted the overall phosphatase activity compared to expressing endogenous subunits alone (Figure 3B).
PMID:36006032	PBO:0105585	Overexpression of Par2 suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	PBO:0105585	Overexpression of Par2 suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	PBO:0105586	(Figure 1D)
PMID:36006032	FYPO:0005728	(Figure 1D)
PMID:36006032	FYPO:0005728	(Figure 1D)
PMID:36006032	FYPO:0005728	(Figure 1D)
PMID:36006032	FYPO:0005727	(Figure 1D)
PMID:36088506	PBO:0110211	(comment: proteasome inhibitor MG132)
PMID:36088506	PBO:0110212	Assessment of Mrz1 levels in these strains (Fig. 3) showed that the levels of Mrz1 markedly increased in ubc13 deletion background and no others, apart from the expected increase in the addition of MG132 controls.
PMID:36088506	GO:0005741	As observed, most of Mrz1 was localized in the mitochondrial fraction (Fig. 1B).
PMID:36088506	FYPO:0001164	The growth of the mrz1 mutant was almost like WT strain in both glucose- and glycerol-containing media at 30 °C (Fig. 4A).
PMID:36088506	PBO:0110210	As shown in Fig. 2A, Mrz1 expression was decreased during the stationary phase grown on YES.
PMID:36090151	PBO:0093664	(comment: CONDITION 1.6 mM)
PMID:36090151	PBO:0093664	(comment: CONDITION 1.6 mM)
PMID:36095128	PBO:0109791	(Figure S13C) (comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	FYPO:0008118	Among the mutants studied, Δcay1 and Δtls1 strains also showed splicing defects specific for rap1 intron 2 (Supplementary Figure S10A).
PMID:36095128	FYPO:0008118	Among the mutants studied, Δcay1 and Δtls1 strains also showed splicing defects specific for rap1 intron 2 (Supplementary Figure S10A).
PMID:36095128	PBO:0109788	(Figure 1) (comment: rap1 intron2, ftp105 intron 3 and pyp3 intron 1)
PMID:36095128	PBO:0109791	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	PBO:0109791	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	PBO:0109791	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	PBO:0109791	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	PBO:0109791	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	PBO:0109791	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	PBO:0109791	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	PBO:0109791	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	PBO:0109791	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	PBO:0109791	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	PBO:0109791	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	PBO:0109791	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	PBO:0109791	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	PBO:0109792	(comment: Semi quantitative RT-PCR followed by gel electrophoresis); Intron retention observed in absence of sde2, cay1 and tls1
PMID:36095128	PBO:0109793	(comment: Semi quantitative RT-PCR followed by gel electrophoresis); Intron retention observed in absence of sde2, cay1 and tls1
PMID:36095128	PBO:0109792	(comment: Semi quantitative RT-PCR followed by gel electrophoresis); Intron retention observed in absence of sde2, cay1 and tls1
PMID:36095128	PBO:0109793	(comment: Semi quantitative RT-PCR followed by gel electrophoresis); Intron retention observed in absence of sde2, cay1 and tls1
PMID:36095128	PBO:0109794	(Supplementary Figures S6 and S7A). ...the disruption of secondary structures by exposure to elevated temperatures could open the fold and increase the distance between the BP and 3′ss.... Indeed, excision of introns with secondary structures such as rap1 intron 2, whi5 intron 1, atg20 intron 2 and mug65 intron 2 was sensitive to 15 min treatment at 42◦C. After lowering the temperature to 25◦C, splicing defects of these introns recovered in wt cells, but the recovery with whi5 and atg20 introns was slower in Δsde2.
PMID:36095128	PBO:0109795	(Supplementary Figures S6 and S7A). (comment: rap1 intron 2)
PMID:36095128	PBO:0109797	(Figure S12B)
PMID:36095128	PBO:0109798	(Figure S12B)
PMID:36095128	PBO:0109799	(Figure S12B)
PMID:36095128	PBO:0109800	(Figure S12B)
PMID:36095128	PBO:0109797	(Figure S12B)
PMID:36095128	PBO:0109798	(Figure S12B)
PMID:36095128	PBO:0109799	(Figure S12B)
PMID:36095128	PBO:0109800	(Figure S12B)
PMID:36095128	PBO:0109797	(Figure S12B)
PMID:36095128	PBO:0109798	(Figure S12B)
PMID:36095128	PBO:0109799	(Figure S12B)
PMID:36095128	PBO:0109800	(Figure S12B)
PMID:36095128	FYPO:0008118	(Figure 1)
PMID:36095128	FYPO:0008118	(Figure 1)
PMID:36095128	FYPO:0008118	(Figure 1)
PMID:36095128	FYPO:0003619	(Figure 1) (rap1 intron2 branch site distance decreased)
PMID:36095128	FYPO:0003619	(Figure 1) (rap1 intron2 branch site distance decreased)
PMID:36095128	GO:0045292	(Figure S13C)
PMID:36095128	GO:0045292	(Figure S13C)
PMID:36095128	GO:0045292	(Figure S13C)
PMID:36095128	GO:0045292	(Figure S13C)
PMID:36095128	GO:0045292	(Figure S13C)
PMID:36095128	GO:0045292	(Figure S13C)
PMID:36095128	GO:0045292	(Figure S13C)
PMID:36095128	GO:0045292	(Figure S13C)
PMID:36095128	GO:0045292	(Figure S13C)
PMID:36095128	GO:0045292	(Figure S13C)
PMID:36095128	GO:0045292	(Figure S13C)
PMID:36095128	PBO:0109790	(Figure 1) (comment: rap1 intron2, ftp105 intron 3 and pyp3 intron 1)
PMID:36095128	PBO:0109789	(Figure 1) (comment: rap1 intron2, ftp105 intron 3 and pyp3 intron 1)
PMID:36095128	PBO:0109791	(Figure S13C) (comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36108046	FYPO:0005727	inefficient anaphase initiation upon SAC inactivation/ persistent MCC-APC/C binding upon SAC activation The SAC was first robustly activated by the nda3-KM311 mutant then inactivated by shifting mitotically arrested cells back to permissive temperature(30˚C)/ We found that dnt1Δ cells retained high amounts of SPB-localized Cdc13-GFP and nuclear Cut2-GFP for much prolonged period compared to wild-type cells, almost to the same degree as previously identified SAC-inactivation defective mutant dis2Δ
PMID:36108046	PBO:0102944	Consistent with this assumption, we found that dnt1Δ cells lost minichromosomes (Ch16, ade6-M216) at an elevated rate that is almost 100 times higher than that of the wild-type (Fig 1B), and displayed increased frequency of lagging chromosomes and chromosome mis-segregation at mitotic anaphase (Fig 1C).
PMID:36108046	PBO:0093563	Consequently, sensitivity of dnt1Δ cells to TBZ was largely but not completely suppressed by excessive Slp1Cdc20 expression achieved by three copies of slp1+ (Fig 3E).
PMID:36108046	FYPO:0008032	but dnt1Δ cells stayed for extended length of time at anaphase B (Fig 1D-1F)
PMID:36108046	FYPO:0005706	but dnt1Δ cells stayed for extended length of time at anaphase B (Fig 1D-1F)
PMID:36108046	PBO:0102945	Surprisingly, Slp1Cdc20 was slightly, but appreciably and reproducibly, less abundant (ranging from roughly 20% to 50% at different time points) in dnt1Δ cells than in wild-type cells (Fig 3B), suggesting Dnt1 may indeed positively regulate the levels of intact Slp1Cdc20. In addition, this regulation of Slp1Cdc20 stability by Dnt1 is Dma1-independent, as the dnt1Δ dma1Δ double mutant has a similar level and degradation profile of Slp1Cdc20 as dnt1Δ single mutant (S5 Fig).
PMID:36108046	PBO:0093556	(comment: I changed to decreased. becasue the phenotype is compared to WT,)
PMID:36108046	PBO:0093556	(comment: I changed to decreased. becasue the phenotype is compared to WT,)
PMID:36112198	FYPO:0006717	(Figure S2)
PMID:36112198	PBO:0107566	(comment: CHECK low glucose MM)
PMID:36112198	PBO:0107562	(comment: CHECK glucose MM)
PMID:36112198	PBO:0107561	(comment: CHECK glucose MM)
PMID:36112198	FYPO:0000961	rst2∆ rescues pka1∆ plb1∆ on KCl
PMID:36112198	PBO:0093594	rst2∆ partially rescues pka1∆ plb1∆ on KCl
PMID:36112198	PBO:0093595	(Fig. 1b)
PMID:36112198	PBO:0093593	(Fig. 2) Overexpression of Pka1 restores the KCl-sensitive phenotype of the plb1∆ strain.
PMID:36112198	FYPO:0005947	(Fig. 4)
PMID:36112198	FYPO:0000112	(Figure 2)
PMID:36112198	PBO:0093595	(Figure 2)
PMID:36112198	PBO:0093595	(Figure 2)
PMID:36112198	PBO:0093595	(Figure 2b)
PMID:36112198	PBO:0093595	(Figure 2b)
PMID:36112198	FYPO:0001214	cgs1∆ partially rescues plb1∆ on KCl
PMID:36112198	PBO:0107570	(comment: observed Pka1-GFP)
PMID:36112198	PBO:0107569	(Fig. 5)
PMID:36112198	PBO:0107568	(comment: observed Pka1-GFP)
PMID:36112198	PBO:0107568	(comment: observed Pka1-GFP)
PMID:36112198	PBO:0107567	(comment: observed Pka1-GFP)
PMID:36112198	PBO:0093595	(Figure 2)
PMID:36112198	PBO:0093595	(Figure 2)
PMID:36112198	FYPO:0000098	(Fig. S2)
PMID:36112198	PBO:0093593	(Fig. 4) rst2∆ partially rescues plb1∆ on KCl
PMID:36112198	PBO:0093593	(Fig. 4) rst2∆ partially rescues plb1∆ on KCl
PMID:36112198	FYPO:0005947	rst2∆ rescues pka1∆ on KCl
PMID:36112198	PBO:0093594	(Figure 2)
PMID:36112198	FYPO:0005947	rst2∆ rescues pka1∆ on KCl
PMID:36112198	PBO:0093593	cgs1∆ partially rescues cyr1∆ plb1∆ on KCl
PMID:36112198	FYPO:0000961	cgs1∆ rescues cyr1∆ plb1∆ on sorbitol
PMID:36112198	PBO:0093594	(Fig. 1) (double mutant with cyr1 is more sensitive)
PMID:36112198	PBO:0093593	(Fig. 2) Overexpression of Pka1 restores the KCl-sensitive phenotype of the plb1∆ strain.
PMID:36112198	FYPO:0005947	(Figure 3)
PMID:36112198	FYPO:0000961	(Fig. S2)
PMID:36112198	FYPO:0006717	(Fig. S2)
PMID:36112198	FYPO:0006717	(Fig. S2)
PMID:36112198	PBO:0107560	(Fig. S2)
PMID:36112198	PBO:0107560	(Fig. S2)
PMID:36112198	FYPO:0006717	(Fig. S2)
PMID:36112198	FYPO:0001020	(Fig. S2)
PMID:36112198	FYPO:0001214	cgs1∆ partially rescues plb1∆ on KCl
PMID:36112198	PBO:0093594	(Figure 2)
PMID:36138017	PBO:0020227	(Figure 1D)
PMID:36138017	PBO:0096644	Dma1 ubiquitinates Tip1
PMID:36138017	PBO:0096651	Strikingly, Tip1 ubiquitination was abolished in both dma1 mutants (Fig. 2d), demonstrating that both functional FHA and RF domains in Dma1 are required for Tip1 ubiquitination in vivo.
PMID:36138017	PBO:0096651	(Fig. 2d)
PMID:36138017	FYPO:0002657	(Fig. 4)
PMID:36138017	PBO:0096652	We found that Tip1 was efficiently ubiquitinated in the absence of the calcineurin catalytic subunit Ppb1, with a similar degree of modification to that of wild-type cells (Fig. 6a).
PMID:36138017	FYPO:0001017	(Fig. 4)
PMID:36138017	FYPO:0004601	though HU treatment caused equally efficient arrest at S phase in both wild-type and dma1Δ cells (Supplementary Fig. 4)
PMID:36138017	PBO:0096648	More interestingly, in the presence of HU, the binding between Tea4 and Tip1 was elevated in dma1Δ cells and in wild-type cells treated with deubiquitinating enzyme USP2 to remove Tip1 ubiquitination (Fig. 4f), this is consistent with increased polar growth in dma1Δ cells (Fig. 4b).
PMID:36174923	FYPO:0003095	Microscopic examination revealed that Δsty1Δppr10 cells were highly elongated compared to WT, Δppr10, and Δsty1 cells (Fig. 5B), suggesting that progression from G2 into mitosis was impaired in Δsty1Δppr10 cells.
PMID:36174923	FYPO:0000245	(Fig. 6)
PMID:36174923	PBO:0095001	(Figure 1)
PMID:36174923	PBO:0095013	(Fig. S2)
PMID:36174923	PBO:0095014	(Fig. S2)
PMID:36174923	PBO:0095015	(Fig. S2)
PMID:36174923	PBO:0095016	(Fig. S2)
PMID:36174923	PBO:0095017	(Fig. S2)
PMID:36174923	PBO:0095018	(Fig. 4)
PMID:36174923	PBO:0093605	(Fig. 5)
PMID:36174923	PBO:0093605	(Fig. 5)
PMID:36174923	FYPO:0000245	(Fig. 5)
PMID:36174923	FYPO:0000245	(Fig. 7b) (comment: partial rescue - still loses viabiltiy at 48 hours)
PMID:36174923	FYPO:0000245	(Fig. 7b) (comment: partial rescue - still loses viabiltiy at 48 hours)
PMID:36174923	PBO:0093605	(Fig. 5)
PMID:36174923	PBO:0093605	(Fig. 5)
PMID:36174923	FYPO:0001357	(Fig. S5)
PMID:36174923	FYPO:0001357	(Fig. S5)
PMID:36174923	FYPO:0000245	(Fig. 5)
PMID:36174923	FYPO:0002060	(Fig. S5)
PMID:36200823	PBO:0093564	sfh1-13 clr3Δ cells were faster growing on TBZ-containing plates than sfh1-13 cells, indicating that deletion of clr3 partially rescues the TBZ sensitivity of sfh1-13.
PMID:36200823	PBO:0093564	sfh1-13 clr3Δ cells were faster growing on TBZ-containing plates than sfh1-13 cells, indicating that deletion of clr3 partially rescues the TBZ sensitivity of sfh1-13.
PMID:36200823	PBO:0094594	Importantly, no significant difference in the level of Cnp1 protein or mRNA was seen in sfh1-13 cells (Figure 1E).
PMID:36200823	PBO:0094598	(Figure 3E). As reported previously, deletion of clr3 increased the loading of Snf21 at pericentromeric repeats; however, we did not observe greater Snf21 occupancy in our sfh1-13 clr3Δ double mutant relative to a sfh1-13 single mutant, suggesting that sfh1-13 prevents the acetylation- dependent recruitment of Snf21 at pericentromeres, and that the elimination of misloaded CENP-ACnp1 in sfh1-13Δ clr3Δ cells is not due to the increase in Snf21 level.
PMID:36200823	PBO:0094597	In sfh1-13 mutant cells, a small but significant increase in the localization of CENP-CCnp3 and CENP- IMis6 was observed at surrounding pericentromeric repeats (Figure 2B and C)
PMID:36200823	PBO:0093564	sfh1-13 clr3Δ cells were faster growing on TBZ-containing plates than sfh1-13 cells, indicating that deletion of clr3 partially rescues the TBZ sensitivity of sfh1-13.
PMID:36200823	FYPO:0006842	while loss of Clr3 eliminated CENP-ACnp1 accumulation at the pericentromere in a sfh1- 13 mutant background, indicating that Clr3 is required for ectopic deposition of CENP-ACnp1 (Figure 3D).
PMID:36200823	PBO:0093562	In addition, a low concentration of TBZ enhanced the chromosome segregation defects of the temperature-sensitive sfh1-13 mutant (Supplementary Figure S1A).
PMID:36200823	PBO:0094593	at pericentromeric heterochromatin When CENP-ACnp1 was expressed at wild-type levels, specific accumulation at pericentromeric heterochromatin domains of all centromeres (Figure 1A), but not at non-centromeric locations
PMID:36200823	FYPO:0006842	Furthermore, we observed ectopic CENP-ACnp1 deposition at pericentromeric heterochromatin domains in snf21-36 but not in rsc1 and rsc4 deletion mutants (Figure 1F)
PMID:36200823	PBO:0094595	However, the sfh1-13 mutation had only a mild influence on H3K9me levels (Figure 1C), as we reported previously (12).
PMID:36200823	PBO:0094596	In sfh1-13 mutant cells, a small but significant increase in the localization of CENP-CCnp3 and CENP- IMis6 was observed at surrounding pericentromeric repeats (Figure 2B and C)
PMID:36200823	FYPO:0000141	In addition, a low concentration of TBZ enhanced the chromosome segregation defects of the temperature-sensitive sfh1-13 mutant (Supplementary Figure S1A).
PMID:36200823	FYPO:0001234	sfh1-13 mutant strain exhibited a slow growth phenotype at 32◦C upon nmt41-cnp1 expression (sfh1-13 at 32◦C in the lower panel of Supplementary Figure S1B
PMID:36200823	FYPO:0001234	sfh1-13 mutant strain exhibited a slow growth phenotype at 32◦C upon nmt41-cnp1 expression (sfh1-13 at 32◦C in the lower panel of Supplementary Figure S1B
PMID:36200823	FYPO:0000047	However, deletion strains of two genes encoding SWI/SNF core components, snf5 and snf22, did not exhibit sensitivity to CENP-ACnp1 overexpression (Supplementary Figure S2A).
PMID:36200823	FYPO:0000047	However, deletion strains of two genes encoding SWI/SNF core components, snf5 and snf22, did not exhibit sensitivity to CENP-ACnp1 overexpression (Supplementary Figure S2A).
PMID:36200823	FYPO:0008036	Importantly, MNase protection at sites i, iii, and v, which are located between CENP-ACnp1 and heterochromatin domains, was elevated in sfh1-13 cells (site i: 1.5-fold, P-value = 0.027; site iii: 2.2-fold, P-value = 0.0001; site v: 1.2-fold, P-value = 0.02; left panel of Figure 5B), indicating that Sfh1/RSC contributes to chromatin decompaction at the boundary.
PMID:36200823	PBO:0094593	at pericentromeric heterochromatin When CENP-ACnp1 was expressed at wild-type levels, specific accumulation at pericentromeric heterochromatin domains of all centromeres (Figure 1A), but not at non-centromeric locations
PMID:36200871	PBO:0109062	(Figure 2E,F) We concluded that Pkd2 is calcium-permeable under the mechanical stimulus of membrane stretching.
PMID:36200871	GO:0005886	Supplemental Figure S5A). We concluded that the calcium-permeable Pkd2 primarily localizes to the plasma membrane.
PMID:36200871	FYPO:0008063	The peak amplitude of the calcium spikes in pkd2-B42 cells was similarly reduced by 62% (Figure 4D).
PMID:36200871	FYPO:0001197	At 36°C, the average calcium level of pkd2-B42 cells was 34% lower than that of wild type cells (Figure 3, C and D).
PMID:36202103	PBO:0119757	(Fig. 1F and G)
PMID:36202103	PBO:0119753	(Fig. 1F and G)
PMID:36202103	PBO:0119756	(Fig. 1F and G)
PMID:36202103	PBO:0119751	(Fig. 1F and G)
PMID:36202103	PBO:0119755	(Fig. 1F and G)
PMID:36202103	PBO:0119754	(Fig. 1F and G)
PMID:36202103	PBO:0119751	(Fig. 1F and G)
PMID:36202103	PBO:0119753	(Fig. 1F and G)
PMID:36202103	PBO:0119753	(Fig. 1F and G)
PMID:36202103	PBO:0119768	(Fig. 4H)
PMID:36202103	PBO:0099941	(Fig. S1E)
PMID:36202103	PBO:0119770	(Fig. 4D)
PMID:36202103	PBO:0119752	(Fig. S1D)
PMID:36202103	PBO:0119750	(Fig. S1A)
PMID:36202103	PBO:0119749	(Fig. 1E)
PMID:36202103	PBO:0119770	(Fig. 4D)
PMID:36202103	PBO:0119751	(Fig. 1E, F and G)
PMID:36202103	PBO:0119750	(Figure S1)
PMID:36202103	PBO:0119749	(Fig. 1D)
PMID:36202103	PBO:0119748	(Fig. 1D)
PMID:36202103	PBO:0102728	(Fig. 1C)
PMID:36202103	FYPO:0008393	(Fig. 4E and F)
PMID:36202103	FYPO:0008393	(Fig. 4E and F)
PMID:36202103	PBO:0119771	(Fig. 4D)
PMID:36202103	PBO:0119769	(Fig. 4I)
PMID:36202103	PBO:0119765	(Fig. S2)
PMID:36202103	PBO:0119772	(Fig. S2)
PMID:36202103	PBO:0119747	(Fig. 3D)
PMID:36202103	PBO:0119762	(Fig. 3D)
PMID:36202103	PBO:0119763	(Fig. 3F and G)
PMID:36202103	PBO:0102728	(Fig. 3I)
PMID:36202103	PBO:0119764	(Fig. 3F and G)
PMID:36202103	PBO:0119764	(Fig. 3F and G)
PMID:36202103	PBO:0119765	(Fig. 3F and G)
PMID:36202103	PBO:0119764	(Fig. 3F and G)
PMID:36202103	PBO:0119766	(Fig. 3I)
PMID:36202103	PBO:0102726	(Fig. 3I)
PMID:36202103	PBO:0102726	(Fig. 3I)
PMID:36202103	PBO:0119767	(Fig. 3I)
PMID:36202103	PBO:0108178	(Fig. 3I)
PMID:36202103	FYPO:0008400	(Fig. 2)
PMID:36202103	PBO:0119758	(Fig. S1D)
PMID:36202103	PBO:0102726	(Fig. 4C)
PMID:36202103	PBO:0102728	(Fig. 4C)
PMID:36202103	PBO:0102726	(Fig. 4C)
PMID:36202103	PBO:0119768	(Fig. 4H)
PMID:36202103	PBO:0119769	(Fig. 4I)
PMID:36202103	PBO:0099942	(Fig. S1E)
PMID:36202103	PBO:0102728	(Fig. 4C)
PMID:36202103	PBO:0119757	(Fig. 1F ang G)
PMID:36202103	PBO:0119747	(Fig. 1B)
PMID:36202103	PBO:0102728	(Fig. 1C)
PMID:36202103	PBO:0102716	(Fig. 4F)
PMID:36202103	PBO:0119759	(Fig. 3A, B, C and D)
PMID:36202103	PBO:0119760	(Fig. 1G)
PMID:36202103	PBO:0119761	(Fig. 3A)
PMID:36202103	PBO:0119762	(Fig. 3D)
PMID:36259651	FYPO:0003031	When cells were grown in media containing nitrogen sources, some of the nc1669Δ cells underwent mating (followed by meiosis), whereas WT cells never initiated mating (Figure 3B, C)
PMID:36259651	PBO:0094617	When cells were grown in media containing nitrogen sources, some of the nc1669Δ cells underwent mating (followed by meiosis), whereas WT cells never initiated mating (Figure 3B, C)
PMID:36287824	PBO:0107510	(comment: Its localization to the ring is dependent on actin (LatA treatment).)
PMID:36287824	FYPO:0005289	This result suggests that rings either slid off the center of the cell after assembly or assembled off center in ∆imp2 cells (Figure 1B).
PMID:36302945	FYPO:0002988	(Figure 4) In 3.0% NH4Cl medium, the growth speed of both strains became slower after exposure to the high NH4Cl condition for 14 h.
PMID:36302945	FYPO:0001723	data not shown, related data in Figure 2A
PMID:36302945	FYPO:0002988	(Figure 1) Cells with leucine auxotrophy (leu1-32 strain) show weak growth on the synthetic medium EMM supplemented with 0.2 mM leucine (Fig. 1B). EMM contains 0.5% NH4Cl
PMID:36302945	FYPO:0002988	(Figure 3) this phenotype was observed for cat1_delta leu1-32 double mutant.
PMID:36361590	PBO:0102893	(Figure 2)
PMID:36361590	GO:0005681	(comment: Gpl1-Gih35-Wdr83 complex)
PMID:36361590	GO:0005681	(comment: Gpl1-Gih35-Wdr83 complex)
PMID:36361590	PBO:0102896	We detected wdr83 (Figure S1) and performed the Western blot and RT-qPCR analyses. We detected no significant changes in the mRNA levels of gpl1, gih35 or wdr83 in the analyzed mu- no significant changes in the mRNA levels of gpl1, gih35 or wdr83 in the analyzed mutants tants (Figure 5a).
PMID:36361590	PBO:0102895	(Figure 3)
PMID:36361590	PBO:0102894	(Figure 3)
PMID:36361590	PBO:0102895	(Figure 3)
PMID:36361590	PBO:0102894	(Figure 3)
PMID:36361590	GO:0005681	(comment: Gpl1-Gih35-Wdr83 complex)
PMID:36361590	PBO:0102893	(Figure 2, 4) These results indicated that the Gih35 helicase is part of the Gih35 and Wdr83 on one side, and as an anchoring protein that allows the binding of the Gpl1-Gih35-Wdr83 complex to the spliceosome on the other side. Gpl1- Gih35-Wdr83 complex, but to associate with the spliceosome, it requires the interaction with Gpl1. Altogether, these findings confirmed the above results of the Y2H assay and provided further support for the hypothesis that Gpl1 functions as a bridging protein for
PMID:36408846	FYPO:0002150	(Figure 3F)
PMID:36408846	PBO:0112497	Consistent with earlier findings, we frequently observed spores with two GFP dots in a single nucleus of a tetrad derived from clr4D/clr4D cells (Fig 3E, green fraction). Such a pattern (i.e., normal segregation during MI but not MII) occurred in < 1% of clr4F449Y/clr4F449Y cells that we have analyzed (Fig 3E)
PMID:36408846	PBO:0109787	(Fig 3C and D). Indeed, the distribution of the GFP dots revealed aberrant segregation of sister chromatids in MI of clr4F449Y/clr4F449Y cells, with a high frequency of equational segregation that normally occurs during MII (Fig 3D
PMID:36408846	FYPO:0008050	(comment: CHECK Check tomorrow should this be tri methylation)
PMID:36408846	FYPO:0008052	clr4F449Y/clr4F449Y cells displayed strongly elevated H3K9me2 levels when in mitosis, while H3K9me3 was absent (Figs 2A and EV3A).
PMID:36408846	FYPO:0008038	clr4F449Y/clr4F449Y cells displayed strongly elevated H3K9me2 levels when in mitosis, while H3K9me3 was absent (Figs 2A and EV3A).
PMID:36408846	FYPO:0005641	(Fig 3C and D). Indeed, the distribution of the GFP dots revealed aberrant segregation of sister chromatids in MI of clr4F449Y/clr4F449Y cells, with a high frequency of equational segregation that normally occurs during MII (Fig 3D
PMID:36408846	FYPO:0008047	clr4F449Y/clr4F449Y cells displayed strongly elevated H3K9me2 levels when in mitosis, while H3K9me3 was absent (Figs 2A and EV3A).
PMID:36408846	FYPO:0008048	This revealed reduced H3K9me2, but increased H3K9me3 levels upon 1-NM-PP1 addition in cdk1-as cells specifically (Fig 6F)
PMID:36408846	PBO:0111081	Indeed, CDK1/Cyclin B phosphorylated recombinant Clr4 specifically at S458 (Fig 6E).
PMID:36408846	PBO:0100299	Upon inhibition of Cdk1-as, Clr4S458 phosphorylation rapidly decreased and was undetectable 3 h postinhibition, whereas Clr4 phosphorylation levels remained unaffected in cdk1+ cells (Figs 6D and EV5D).
PMID:36408846	FYPO:0000278	spores formed colonies again (Fig 4G).
PMID:36408846	PBO:0100297	Furthermore, fewer clr4F449Y/clr4F449Y cells displayed lagging DNA upon expression of Swi6Chp1-like-CD (Fig 4C and D).
PMID:36408846	PBO:0100296	(Figure 4A) (This observation indicates that highest binding affinity of Swi6 towards H3 is necessary for proper subnuclear localization in meiocytes, for which H3K9 needs to be tri-methylated.
PMID:36408846	PBO:0100295	(Figure 4a)
PMID:36408846	PBO:0100295	(Figure 4a)
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	We identified 4 major states of nascent 60S, and each state could be further classified into multiple substates (Figures 2A and S3; Table 1). The nascent 60S associated with Fkbp39 represents early ribosome biogenesis stages as described below.
PMID:36423630	GO:0140693	This supports the role of histones in promoting heterotypic LLPS of Fkbp39 with DNA (Figures 1D and S2E). These observations suggest that Fkbp39 could organize the rDNA-containing chromatin into a phase-separated compartment.
PMID:36423630	FYPO:0004227	We mutated the active site of the prolyl isomerase domain of Fkbp39 (F301C/W314C/Y337K)29 and found that it was impaired in the ability to bind nucleosomes but not DNA (Figure S2B).
PMID:36423630	GO:0031491	On the other hand, Fkbp39 could bind to DNA and nucleosomes with a 40-bp-long linker DNA (Figures 1C, S1I, and S1J) but not to nucleosomes lacking or with short 10 bp linker DNA (Figure S2A).
PMID:36423630	GO:0000182	On the other hand, Fkbp39 could bind to DNA and nucleosomes with a 40-bp-long linker DNA (Figures 1C, S1I, and S1J) but not to nucleosomes lacking or with short 10 bp linker DNA (Figure S2A).
PMID:36423630	PBO:0111363	We found that chromatin-associated Fkbp39 and Fkbp41 predominately localized to the rDNA locus, similar to previous observations on budding yeast and mammalian nucleophosmins,20-23 but our ChIP-seq data also revealed a strong enrichment at the 25S rDNA, which had not been described before (Figures 1A, 1B, and S1D).
PMID:36423630	PBO:0111363	We found that chromatin-associated Fkbp39 and Fkbp41 predominately localized to the rDNA locus, similar to previous observations on budding yeast and mammalian nucleophosmins,20-23 but our ChIP-seq data also revealed a strong enrichment at the 25S rDNA, which had not been described before (Figures 1A, 1B, and S1D).
PMID:36423630	GO:0000785	By contrast, Fkbp41 is found primarily in the insoluble chromatin fraction (Figure S1C).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	PBO:0111365	Although the overall Fkbp39 protein levels are slightly reduced in fkbp41D total lysates (Figure S7E), there was a marked reduction of Fkbp39 localization specifically at 25S rDNA in those cells compared with wild- type (Figures 6A, 6B, and S7F).
PMID:36423630	GO:0042790	To determine if Fkbp39 is required for transcription or RNA processing, we performed nascent RNA-seq using 4-thiouracil labeling. Immediately after labeling, the levels of nascent rRNA in wild-type or fkbp39D cells were comparable (Figures 4B, S5F, and S5G), indicating that Fkbp39 is not required for rRNA transcription.
PMID:36423630	FYPO:0003694	reduced levels of 18S and 25S rRNA and accumulation of 50 ETS RNA and unprocessed rRNA in the mutant compared with wild-type cells (Figures S5D and S5E).
PMID:36423630	FYPO:0001137	reduced levels of 18S and 25S rRNA and accumulation of 50 ETS RNA and unprocessed rRNA in the mutant compared with wild-type cells (Figures S5D and S5E).
PMID:36423630	GO:0042273	Fkbp39 separates nascent ribosomes from chromatin in cells
PMID:36423630	GO:0042274	Fkbp39 separates nascent ribosomes from chromatin in cells
PMID:36423630	PBO:0111364	By contrast, in fkbp39D cells, we detected Ytm1 on chromatin, primarily at the 30 end of the rDNA repeats, specifically enriched at the 30 ETS and the non-transcribed spacer (NTS) DNA sites (Figures 4A, S5A, and S5B).
PMID:36423630	GO:0000785	In wild-type cells, Ytm1 is not detectable on chromatin, in agreement with our in vitro data showing that Fkbp39 separates ribosome biogenesis intermediates from chromatin (Figures 4A, S5A, and S5B).
PMID:36423630	GO:0032040	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0003723	Similarly to human nucleosphosmin,12 Fkbp39 can bind RNA in vitro and phase separate with RNA (Figures S4A and S4B). Fkbp39 robustly forms liquid-like condensates with RNA in sharp contrast to condensates with DNA (Figures S4B and S2D).
PMID:36423630	GO:1902626	State 2 has 24 ribosomal proteins but only 9 biogenesis factors, and ITS2 is cleaved and its associated factors are released (Figures 2A and S3D; Table S2).
PMID:36423630	GO:1902626	State 2 has 24 ribosomal proteins but only 9 biogenesis factors, and ITS2 is cleaved and its associated factors are released (Figures 2A and S3D; Table S2).
PMID:36423630	GO:1902626	State 2 has 24 ribosomal proteins but only 9 biogenesis factors, and ITS2 is cleaved and its associated factors are released (Figures 2A and S3D; Table S2).
PMID:36423630	GO:1902626	State 2 has 24 ribosomal proteins but only 9 biogenesis factors, and ITS2 is cleaved and its associated factors are released (Figures 2A and S3D; Table S2).
PMID:36423630	GO:1902626	In state 3, RNA domain III is folded and the biogenesis complex Ytm1-Erb1-Ppp1 (Ytm1-Erb1-Nop7 in S. cerevisiae) is incorporated32 for a total of 30 ribosomal proteins and 15 biogenesis factors (Figure 2A).
PMID:36423630	GO:1902626	In state 3, RNA domain III is folded and the biogenesis complex Ytm1-Erb1-Ppp1 (Ytm1-Erb1-Nop7 in S. cerevisiae) is incorporated32 for a total of 30 ribosomal proteins and 15 biogenesis factors (Figure 2A).
PMID:36423630	GO:1902626	In state 3, RNA domain III is folded and the biogenesis complex Ytm1-Erb1-Ppp1 (Ytm1-Erb1-Nop7 in S. cerevisiae) is incorporated32 for a total of 30 ribosomal proteins and 15 biogenesis factors (Figure 2A).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36435910	PBO:0109110	(Figure 2a)
PMID:36435910	PBO:0109110	(Figure 2a)
PMID:36435910	PBO:0109109	(Figure 2a)
PMID:36435910	PBO:0116838	(comment: CHECK Evidence: in vitro biochemical assays using purified tubulin and recombinant Dis1 protein / New GO term requested: microtubule destabilization activity)
PMID:36435910	FYPO:0009057	(Figure 2a)
PMID:36435910	PBO:0109107	Dis1 uses its TOG domains to induce microtubule catastrophe, in which polymerisation turns into depolymerisation
PMID:36481249	FYPO:0000648	Interestingly, the average cell size of tor-287 mutant cells also decreases from 18.2 μm at 25 ◦C to 7.0 μm at 36 ◦C (Fig. 3A and 3B
PMID:36481249	FYPO:0005097	having 1C and 2C DNA peak (Fig. 3C, upper panel) with a majority of cells having 1C DNA peak indicating a G1 arrest while only 2C DNA peak was observed in wild type cells grown under similar conditions
PMID:36481249	FYPO:0001029	cells were unable to grow on the plates containing canavanine (Fig. 4C). Interestingly, wat1Δ, wat1-17, and tor2-287 mutant cells exhibited resistance to canavanine (Fig. 4C) suggesting that disruption of wat1 leads to inactivation of the TORC1 pathway resulting in the defect in amino acid uptake
PMID:36481249	FYPO:0005097	The tor2-287 mutant cells also showed a similar phenotype after shifting at 36 ◦C (Fig. 3C, upper panel), indicating the G1 arrest.
PMID:36481249	PBO:0108768	Real-time quantitative PCR analysis revealed the up-regulation of transcripts of per1 and isp5 genes and down regulation of cat1 gene in wat1Δ, wat1-17, and tor2-287 mutant background at the non-permissive temperature (Fig. 4B)
PMID:36481249	FYPO:0001492	wat1Δ and wat1-17 mutant cells were a little elongated with an average size of 18.5 μm (Fig. 3A and 3B).
PMID:36481249	PBO:0108775	The phosphorylation of Psk1 and Rps602 was completely abolished in wat1Δ, wat1-17, and tor2-287 mutants after shifting the cells at non-permissive temperature (Fig. 4A, upper and middle panel).
PMID:36481249	FYPO:0001492	wat1Δ and wat1-17 mutant cells were a little elongated with an average size of 18.5 μm (Fig. 3A and 3B).
PMID:36481249	FYPO:0000648	In contrast, under the same condition, the wat1Δ and wat1-17 mutant cells became shorter in size with a round morphology having an average cell length of 7.7 and 8.3 μm, respectively (Fig. 3A and 3B)
PMID:36481249	FYPO:0002151	(Figure 1a)
PMID:36481249	PBO:0108766	The phosphorylation of Psk1 and Rps602 was completely abolished in wat1Δ, wat1-17, and tor2-287 mutants after shifting the cells at non-permissive temperature (Fig. 4A, upper and middle panel).
PMID:36537249	FYPO:0004318	As shown in Fig. 1A,B, the percentage of mitotic WT cells displaying Plo1-GFP signals increased over time upon incubation at 16°C and, 8 h after cold treatment, ∼90% of WT cells were arrested at preanaphase presumably due to the activation of the SAC. As Bub1 is a core component of the SAC (Fischer et al., 2021), the absence of Bub1 was expected to abolish the SAC. Consistently, the percentage of mitotic bub1Δ cells remained low (<10%) throughout the period of cold treatment (Fig. 1A,B).
PMID:36537249	PBO:0108746	Intriguingly, similar to the percentage of mitotic WT cells, the percentage of mitotic mhf2Δ cells increased over time upon cold treatment, but to a lesser degree (Fig. 1A,B).
PMID:36537249	PBO:0108788	(comment: CHECK mitotic prophase)
PMID:36537249	GO:0005515	(comment: CHECK binds to Mhf2)
PMID:36537249	GO:0005515	(comment: CHECK binds to Mhf1)
PMID:36537249	PBO:0108732	(comment: CHECK abolished Mhf1 localization)
PMID:36574843	PBO:0110788	(Figure 3)
PMID:36574843	FYPO:0000017	neither Cdr2(1-330) nor Cdr2(1-590) truncations reduced cell size or formed cytoplasmic clusters (Fig. 7, B-D) despite expression of all constructs to similar levels (Fig. S3A).
PMID:36574843	FYPO:0000017	neither Cdr2(1-330) nor Cdr2(1-590) truncations reduced cell size or formed cytoplasmic clusters (Fig. 7, B-D) despite expression of all constructs to similar levels (Fig. S3A).
PMID:36574843	FYPO:0000648	However, induction of PTet-cdr2 in cdr1Δ cdr2Δ cells still reduced cell size, whereas PTet-cdr2(E177A) had no effect (Fig. 2, C and D).
PMID:36574843	FYPO:0003481	In contrast, Tet-based overexpression of cdr2(E177A) increased the size of dividing cells, consistent with dominant-negative effects for
PMID:36574843	PBO:0110786	(comment: (vw: did not reduce cell size further) EPISTATIC) Consistent with this prediction, PTet-cdr2 did not reduce cell J. Biol. Chem. (2023) 299(2) 102831 3 Regulation of cell size and Wee1 by elevated levels of Cdr2 size in the temperature-sensitive wee1-50 mutant grown at 36 C (Fig. 2E).
PMID:36574843	GO:0031569	(comment: dosage dependent) (We conclude that increased levels of Cdr2 cause hyperphosphorylation of Wee1 leading to reduced cell size at division.)
PMID:36574843	PBO:0110794	(comment: CHECK HYPERPHOSPHORYLATED WEE1 (get identifier))
PMID:36574843	PBO:0110786	Addition of Tet to PTet-cdr2 cells caused a marked and significant decrease in cell length at division (Fig. 2, A and B)
PMID:36574843	PBO:0110789	(Figure 3)
PMID:36617881	GO:0010964	These results suggest that Epe1 promotes assembly of the RNAi machinery at constitutive heterochromatin by expressing dg/dh ncRNAs.
PMID:36626373	PBO:0025083	Thus we found that wild-type Cat1-GFP cells growing in nitrogen-starvation conditions is localised to the plasma membrane, particularly at the growing cell ends, as previously reported [12,26].
PMID:36633091	PBO:0107937	(Fig. 2A and 2C)
PMID:36633091	PBO:0107936	(Fig. 1C, ID and 1E)
PMID:36633091	PBO:0107938	(Fig. 2A and 2B)
PMID:36633091	FYPO:0002071	(Fig. 3B)
PMID:36633091	PBO:0107936	(Fig. S1D and S1E)
PMID:36633091	FYPO:0002029	Supplementary Fig. S1D and S1E
PMID:36633091	PBO:0107939	(Fig. 1C, Fig. 1D and Fig. 1E)
PMID:36633091	FYPO:0003190	(Fig. 2C)
PMID:36633091	PBO:0107940	(Fig. 2D)
PMID:36633091	FYPO:0002071	(Fig. 3B)
PMID:36633091	PBO:0107939	(Fig. 1C, 1D and 1E)
PMID:36633091	FYPO:0003194	(Fig. 2C)
PMID:36633091	FYPO:0002071	(Fig. 3B)
PMID:36633091	PBO:0107941	(Fig. 5C)
PMID:36633091	PBO:0107942	(Fig. 5C)
PMID:36633091	FYPO:0009002	(Fig. 1A, 1B, S1A)
PMID:36633091	FYPO:0000056	(Fig. 1A, 1B, S1A)
PMID:36633091	FYPO:0000895	(Fig. 1A, 1B, S1A)
PMID:36633091	PBO:0107943	(Fig. 2A and 2C)
PMID:36633091	PBO:0107941	(Fig. 5C)
PMID:36633091	PBO:0107942	(Fig. 5C)
PMID:36650056	FYPO:0002890	(comment: change to: twin horsetail nucleus)
PMID:36650056	FYPO:0000510	(comment: Change to: Nuclear congression without nuclear fusion)
PMID:36650056	FYPO:0002890	(comment: change to: twin horsetail nucleus)
PMID:36650056	PBO:0102168	(comment: palmitoylation of tht1D is reduced by akr1D)
PMID:36650056	PBO:0102167	(comment: Lower levels in the akr1 mutant)
PMID:36650056	PBO:0102167	(comment: Lower levels in the akr1 mutant)
PMID:36650056	FYPO:0000510	(comment: Change to: Nuclear congression without nuclear fusion)
PMID:36650056	PBO:0102161	(comment: akr1Δ affecting tht1)
PMID:36650056	FYPO:0002890	(comment: change to: twin horsetail nucleus)
PMID:36650056	FYPO:0000510	(comment: Change to: Nuclear congression without nuclear fusion)
PMID:36695178	PBO:0103279	(comment: Very high levels of diploidization in minimal medium)
PMID:36695178	PBO:0103284	Severe buckling of the mitotic spindle was observed in 31% of cells, resulting in bowshaped nuclear intermediates during anaphase (Fig. 4D). It took longer for these nuclei to divide, and they often formed daughter nuclei of unequal sizes (Fig. S4E)
PMID:36695178	FYPO:0006716	Severe buckling of the mitotic spindle was observed in 31% of cells, resulting in bowshaped nuclear intermediates during anaphase (Fig. 4D). It took longer for these nuclei to divide, and they often formed daughter nuclei of unequal sizes (Fig. S4E)
PMID:36695178	PBO:0103281	(comment: Sub-lethal phenotype, with only 10% of expected double mutants recovered.)
PMID:36695178	FYPO:0000229	(comment: Very prominent in minimal medium due to the lack of the Kennedy pathway precursors)
PMID:36695178	PBO:0019210	(comment: Very prominent in minimal medium due to the lack of the Kennedy pathway precursors)
PMID:36695178	PBO:0103280	(comment: Very prominent in minimal medium due to the lack of the Kennedy pathway precursors)
PMID:36705602	PBO:0100540	(Figure 3) summarizes data
PMID:36705602	PBO:0100540	(Figure 3) summarizes data
PMID:36705602	PBO:0100540	(Figure 3) summarizes data
PMID:36705602	PBO:0100540	(Figure 3) summarizes data
PMID:36705602	PBO:0100540	(Figure 3) summarizes data
PMID:36705602	PBO:0109293	(Figure 3) summarizes data
PMID:36705602	PBO:0100540	(Figure 3) summarizes data
PMID:36705602	PBO:0109293	(Figure 3) summarizes data
PMID:36705602	PBO:0109293	(Figure 3) summarizes data
PMID:36749320	PBO:0108668	(Fig. 5 S2)
PMID:36749320	PBO:0108669	(Fig. 5 S2)
PMID:36749320	PBO:0108669	(Fig. 5 S2)
PMID:36749320	PBO:0108669	(Fig. 5 S2)
PMID:36749320	PBO:0108669	(Fig. 5 S2)
PMID:36749320	PBO:0108670	(Fig. 3E)
PMID:36749320	PBO:0109286	(Figure 5A)
PMID:36749320	PBO:0103081	(Figure 3)
PMID:36749320	PBO:0103081	(Figure 3)
PMID:36749320	PBO:0103081	(Figure 3)
PMID:36749320	PBO:0103081	(Figure 3)
PMID:36749320	PBO:0103081	(Figure 3)
PMID:36749320	PBO:0098304	(Figure 3)
PMID:36749320	PBO:0098304	(Figure 3)
PMID:36749320	PBO:0098304	(Figure 3)
PMID:36749320	PBO:0098304	(Figure 3)
PMID:36749320	PBO:0098304	(Figure 3)
PMID:36749320	PBO:0098304	(Figure 3)
PMID:36749320	PBO:0098304	(Figure 3)
PMID:36749320	PBO:0098304	(Figure 3)
PMID:36749320	PBO:0098304	(Figure 3)
PMID:36749320	PBO:0098304	(Figure 3)
PMID:36749320	PBO:0108658	(Figure 3)
PMID:36749320	PBO:0109275	(Figure 10)
PMID:36749320	PBO:0109276	(Figure 10)
PMID:36749320	PBO:0108661	(Figure 4)
PMID:36749320	PBO:0109287	(Figure 5)
PMID:36749320	PBO:0109286	(Figure 5C)
PMID:36749320	PBO:0109286	(Figure 5A)
PMID:36749320	PBO:0109287	(Figure 5A)
PMID:36749320	PBO:0109288	(Figure 5A)
PMID:36749320	PBO:0098304	(Figure 3)
PMID:36749320	PBO:0109288	(Figure 5A)
PMID:36749320	PBO:0109286	(Figure 5A)
PMID:36749320	PBO:0109287	(Figure 5A)
PMID:36749320	PBO:0109287	(Figure 5A)
PMID:36749320	PBO:0109287	(Figure 5A)
PMID:36749320	PBO:0109288	(Figure 5A)
PMID:36749320	PBO:0109286	(Figure 5A)
PMID:36749320	PBO:0109288	(Figure 5A)
PMID:36749320	PBO:0109288	(Figure 5A)
PMID:36749320	PBO:0109288	(Figure 5A)
PMID:36749320	PBO:0109286	(Figure 5A)
PMID:36749320	PBO:0109286	(Figure 5A)
PMID:36749320	PBO:0109286	(Figure 5A)
PMID:36749320	PBO:0109286	(Figure 5A)
PMID:36749320	PBO:0109287	(Figure 5A)
PMID:36749320	PBO:0109287	(Figure 5B)
PMID:36749320	PBO:0109286	(Figure 10) (comment: Manu: transfer to FYPO:0008075)
PMID:36749320	PBO:0109286	(Figure 10) (comment: Manu: transfer to FYPO:0008075)
PMID:36749320	PBO:0109288	(Figure 5C)
PMID:36749320	PBO:0109288	(Figure 5C)
PMID:36749320	PBO:0108664	(Figure 10)
PMID:36749320	PBO:0108665	(Figure 10)
PMID:36749320	PBO:0108666	(Fig. 5 S2)
PMID:36749320	PBO:0108667	(Fig. 5 S2)
PMID:36749320	PBO:0108668	(Fig. 5 S2)
PMID:36779416	PBO:0098000	non detectable Fig. 1. Phosphate starvation induces ecl3+ expression in a pho7+-dependent manner.
PMID:36779416	PBO:0092197	(Figure 1A, B)
PMID:36779416	PBO:0098001	non detectable Fig. 1. Phosphate starvation induces ecl3+ expression in a pho7+-dependent manner.
PMID:36779416	PBO:0098002	non detectable Fig. 1. Phosphate starvation induces ecl3+ expression in a pho7+-dependent manner.
PMID:36779416	PBO:0098004	phosphate replete. Zfs1 is involved in the repression of the ecl3+ transcript level in a nutrient-rich environment but is not required for the induction by phosphate starvation. Next
PMID:36779416	PBO:0098000	Phosphate starvation did not induce ecl3+ expression in Δckb1 cells, indicating that the induction was dependent on Ckb1 (Fig. 2B)
PMID:36793083	PBO:0093581	(Fig. 3)
PMID:36793083	PBO:0093581	(Fig. 3)
PMID:36793083	PBO:0093581	(Fig. 3)
PMID:36793083	PBO:0093580	(Fig. 3)
PMID:36793083	PBO:0093581	(Fig. 3)
PMID:36793083	PBO:0093616	(Fig. 3)
PMID:36793083	PBO:0093616	(Fig. 3)
PMID:36793083	PBO:0093616	(Fig. 3)
PMID:36793083	PBO:0093616	(Fig. 3)
PMID:36793083	PBO:0093616	(Fig. 3)
PMID:36793083	PBO:0093616	(Fig. 3)
PMID:36793083	PBO:0093616	(Fig. 3)
PMID:36793083	PBO:0100816	(Fig. 4D)
PMID:36793083	PBO:0100815	(Fig. 4D)
PMID:36793083	PBO:0100814	(Fig. 4D)
PMID:36793083	PBO:0100813	(Fig. 4D)
PMID:36793083	PBO:0100813	(Fig. 4D)
PMID:36793083	PBO:0100812	(Fig. 4D)
PMID:36793083	PBO:0100812	(Fig. 4D)
PMID:36793083	PBO:0100811	(Fig. 4D)
PMID:36793083	PBO:0100810	(Fig. 4D)
PMID:36793083	PBO:0093616	(Fig. 3)
PMID:36793083	PBO:0093616	(Fig. 3)
PMID:36794724	PBO:0109745	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109746	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0109747	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109748	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0109749	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109750	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109751	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109752	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109753	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109766	(Figure 6)
PMID:36794724	PBO:0109765	(Figure 6)
PMID:36794724	PBO:0109754	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109755	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109756	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109757	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109758	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109759	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109764	(Figure 6)
PMID:36794724	PBO:0109763	(Figure 6)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0109760	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0109762	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109736	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109735	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109734	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109733	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109732	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109731	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0008123	(Figure 5B)
PMID:36794724	FYPO:0008119	(Figure 5D,G)
PMID:36794724	PBO:0101499	(Figure 1B)
PMID:36794724	PBO:0109974	(Figure 3A)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0092197	(Figure 2)
PMID:36794724	PBO:0109739	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109974	(Figure 3B)
PMID:36794724	PBO:0109974	(Figure 3C)
PMID:36794724	PBO:0109740	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109741	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109742	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109743	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109744	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0109738	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109737	(Figure 6, 7, 9 and 10)
PMID:36794724	PBO:0109761	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0008102	(Figure 8)
PMID:36794724	PBO:0092357	(Figure S3)
PMID:36794724	PBO:0092357	(Figure S3)
PMID:36794724	PBO:0092357	(Figure S3)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36794724	PBO:0092197	(Figure S4)
PMID:36799444	PBO:0109158	Finally, we examined whether Lem2 affected their subcellular localization. GFP-Cho2, GFP-Ole1 and Erg11-GFP were localized in the cortical ER and NE (or perinuclear ER), and deletion of the lem2+ gene did not affect the localization (Fig. 2B), indicating that Lem2 is not necessary for their NE localization
PMID:36799444	PBO:0109159	Finally, we examined whether Lem2 affected their subcellular localization. GFP-Cho2, GFP-Ole1 and Erg11-GFP were localized in the cortical ER and NE (or perinuclear ER), and deletion of the lem2+ gene did not affect the localization (Fig. 2B), indicating that Lem2 is not necessary for their NE localization
PMID:36799444	PBO:0109160	Finally, we examined whether Lem2 affected their subcellular localization. GFP-Cho2, GFP-Ole1 and Erg11-GFP were localized in the cortical ER and NE (or perinuclear ER), and deletion of the lem2+ gene did not affect the localization (Fig. 2B), indicating that Lem2 is not necessary for their NE localization
PMID:36799444	PBO:0109162	We performed an IP-WB experiment on the bqt4Δ background (‘bqt4Δ’ in Fig. 2A). Deletion of bqt4+ did not affect these interactions, indicating that Cho2, Ole1 and Erg11 interact with Lem2 independent of Bqt4.
PMID:36799444	PBO:0109161	We performed an IP-WB experiment on the bqt4Δ background (‘bqt4Δ’ in Fig. 2A). Deletion of bqt4+ did not affect these interactions, indicating that Cho2, Ole1 and Erg11 interact with Lem2 independent of Bqt4.
PMID:36799444	PBO:0109168	(Fig. 2D)
PMID:36799444	PBO:0109163	We performed an IP-WB experiment on the bqt4Δ background (‘bqt4Δ’ in Fig. 2A). Deletion of bqt4+ did not affect these interactions, indicating that Cho2, Ole1 and Erg11 interact with Lem2 independent of Bqt4.
PMID:36820394	PBO:0108808	(Table 1)
PMID:36820394	PBO:0108832	(Table 1)
PMID:36820394	PBO:0108831	(Table 1)
PMID:36820394	PBO:0108830	(Table 1)
PMID:36820394	PBO:0108829	(Table 1)
PMID:36820394	PBO:0108828	(Table 1)
PMID:36820394	PBO:0108827	(Table 1)
PMID:36820394	PBO:0108826	(Table 1)
PMID:36820394	PBO:0108825	(Table 1)
PMID:36820394	PBO:0108824	(Table 1)
PMID:36820394	PBO:0108823	(Table 1)
PMID:36820394	PBO:0108822	(Table 1)
PMID:36820394	PBO:0108821	(Table 1)
PMID:36820394	PBO:0108820	(Table 1)
PMID:36820394	PBO:0108819	(Table 1)
PMID:36820394	PBO:0108818	(Table 1)
PMID:36820394	PBO:0108817	(Table 1)
PMID:36820394	PBO:0108816	(Table 1)
PMID:36820394	PBO:0108815	(Table 1)
PMID:36820394	PBO:0108814	(Table 1)
PMID:36820394	PBO:0108813	(Table 1)
PMID:36820394	PBO:0108812	(Table 1)
PMID:36820394	PBO:0108811	(Table 1)
PMID:36820394	PBO:0108810	(Table 1)
PMID:36820394	PBO:0108809	(Table 1)
PMID:36820394	PBO:0108807	(Table 1)
PMID:36820394	PBO:0108806	(Table 1)
PMID:36820394	PBO:0108805	(Table 1)
PMID:36820394	PBO:0108804	(Table 1)
PMID:36820394	PBO:0108803	(Table 1)
PMID:36820394	PBO:0108802	(Table 1)
PMID:36820394	PBO:0108801	(Table 1)
PMID:36820394	PBO:0108800	(Table 1)
PMID:36820394	PBO:0108799	(Table 1)
PMID:36820394	PBO:0108798	(Table 1)
PMID:36820394	PBO:0108797	(Table 1)
PMID:36820394	PBO:0108796	(Table 1)
PMID:36820394	PBO:0108795	(Table 1)
PMID:36820394	PBO:0108791	(Table 1)
PMID:36820394	PBO:0108794	(Table 1)
PMID:36820394	PBO:0108793	(Table 1)
PMID:36820394	PBO:0108792	(Table 1)
PMID:36820394	PBO:0108793	(Fig. 2)
PMID:36820394	PBO:0108793	(Fig. 2)
PMID:36820394	PBO:0108793	(Fig. 2)
PMID:36820394	PBO:0108792	(Fig. 2)
PMID:36820394	PBO:0108792	(Fig. 2)
PMID:36820394	PBO:0108792	(Fig. 2)
PMID:36820394	PBO:0108791	(Fig. 2)
PMID:36820394	PBO:0108791	(Fig. 2)
PMID:36820394	PBO:0108791	(Fig. 2)
PMID:36854376	FYPO:0001357	(comment: The mutant strain appears to grow normally) (Figure 2b).
PMID:36854376	FYPO:0008215	(comment: ...decreased the average population cell length from 12 µm to 10.3 µm in the wild-type strain after incubation for 6 h at 29°C whereas no such decrease by O1 was observed in the rho1-A62T strain, where average cell size is 12.3 µm in the DMSO control and 11.8 µm in the presence of O1 (Figure 2c).)
PMID:36882296	PBO:0108875	(Fig. S3)
PMID:36882296	FYPO:0000080	(Fig. 9A)
PMID:36882296	FYPO:0001355	(Fig. 9A)
PMID:36882296	FYPO:0000082	(Fig. 9A)
PMID:36882296	PBO:0094738	(Fig. 9B)
PMID:36882296	PBO:0094738	(Fig. 9B)
PMID:36882296	PBO:0094738	(Fig. 9B)
PMID:36882296	PBO:0094771	(Fig. 9B)
PMID:36882296	PBO:0094771	(Fig. 9B)
PMID:36882296	PBO:0094771	(Fig. 9B)
PMID:36882296	PBO:0094771	(Fig. 9B)
PMID:36882296	FYPO:0002085	(Fig. 10A)
PMID:36882296	FYPO:0002085	(Fig. 10A)
PMID:36882296	FYPO:0001355	(Fig. 10A)
PMID:36882296	FYPO:0001355	(Fig. 10A)
PMID:36882296	PBO:0094771	(Fig. 10B)
PMID:36882296	PBO:0094771	(Fig. 10B)
PMID:36882296	FYPO:0002085	(Fig. 11A)
PMID:36882296	PBO:0094738	(Fig. 11B)
PMID:36882296	PBO:0094738	(Fig. 11B)
PMID:36882296	PBO:0094738	(Fig. 11B)
PMID:36882296	PBO:0094738	(Fig. 11B)
PMID:36882296	FYPO:0002085	(Fig. 12A)
PMID:36882296	PBO:0094777	(Fig. 12B)
PMID:36882296	PBO:0094777	(Fig. 7B)
PMID:36882296	PBO:0094777	(Fig. 9B)
PMID:36882296	FYPO:0002085	(Fig. 12A)
PMID:36882296	PBO:0094738	(Fig. 12B)
PMID:36882296	FYPO:0002085	(Fig. 12A)
PMID:36882296	PBO:0108812	(Fig. S4)
PMID:36882296	PBO:0108850	(Fig. S4)
PMID:36882296	PBO:0108809	(Fig. S4)
PMID:36882296	PBO:0108808	(Fig. S4)
PMID:36882296	PBO:0108804	(Fig. S4)
PMID:36882296	PBO:0108851	(Fig. S4)
PMID:36882296	PBO:0108807	(Fig. S4)
PMID:36882296	PBO:0108810	(Fig. S4)
PMID:36882296	PBO:0108852	(Fig. S4)
PMID:36882296	PBO:0108813	(Fig. S4)
PMID:36882296	PBO:0108822	(Fig. S4)
PMID:36882296	PBO:0108853	(Fig. S4)
PMID:36882296	PBO:0108854	(Fig. S4)
PMID:36882296	PBO:0108801	(Fig. S4)
PMID:36882296	PBO:0108855	(Fig. S4)
PMID:36882296	PBO:0108856	(Fig. S4)
PMID:36882296	PBO:0108857	(Fig. S4)
PMID:36882296	PBO:0108858	(Fig. S4)
PMID:36882296	PBO:0108859	(Fig. S4)
PMID:36882296	PBO:0108860	(Fig. S4)
PMID:36882296	PBO:0108800	(Fig. S4)
PMID:36882296	PBO:0108861	(Fig. S4)
PMID:36882296	PBO:0108862	(Fig. S4)
PMID:36882296	PBO:0096777	(Fig. S3)
PMID:36882296	PBO:0108863	(Fig. S3)
PMID:36882296	PBO:0098004	(Fig. S3)
PMID:36882296	PBO:0108864	(Fig. S3)
PMID:36882296	PBO:0108865	(Fig. S3)
PMID:36882296	PBO:0108866	(Fig. S3)
PMID:36882296	PBO:0108867	(Fig. S3)
PMID:36882296	PBO:0108868	(Fig. S3)
PMID:36882296	PBO:0108869	(Fig. S3)
PMID:36882296	PBO:0108870	(Fig. S3)
PMID:36882296	PBO:0108871	(Fig. S3)
PMID:36882296	PBO:0108872	(Fig. S3)
PMID:36882296	PBO:0108873	(Fig. S3)
PMID:36882296	PBO:0108874	(Fig. S3)
PMID:36882296	FYPO:0002085	(Fig. S5A)
PMID:36882296	PBO:0106693	(Fig. S5B)
PMID:36882296	FYPO:0002085	(Fig. S6A)
PMID:36882296	FYPO:0002085	(Fig. S6A)
PMID:36882296	PBO:0094771	(Fig. S6B)
PMID:36882296	PBO:0094771	(Fig. S6B)
PMID:36882296	FYPO:0002085	(Fig. S7A)
PMID:36882296	FYPO:0002085	(Fig. S7A)
PMID:36882296	FYPO:0002085	(Fig. S7A)
PMID:36882296	PBO:0094738	(Fig. S7B)
PMID:36882296	PBO:0094738	(Fig. S7B)
PMID:36882296	PBO:0094738	(Fig. S7B)
PMID:36882296	FYPO:0002061	(Fig. S8)
PMID:36882296	FYPO:0002061	(Fig. S8)
PMID:36882296	FYPO:0002061	(Fig. S8)
PMID:36882296	FYPO:0002061	(Fig. S8)
PMID:36882296	FYPO:0001355	(Fig. S8)
PMID:36882296	FYPO:0001355	(Fig. S8)
PMID:36882296	FYPO:0001355	(Fig. S8)
PMID:36882296	FYPO:0001355	(Fig. S8)
PMID:36882296	FYPO:0001355	(Fig. S8)
PMID:36882296	FYPO:0001355	(Fig. S8)
PMID:36882296	FYPO:0001355	(Fig. S8)
PMID:36882296	FYPO:0001355	(Fig. S8)
PMID:36882296	FYPO:0000080	(Fig. 1A) Redundancy with rpb1-T4A
PMID:36882296	PBO:0108864	(Fig. 3)
PMID:36882296	PBO:0108876	(Fig. 3)
PMID:36882296	PBO:0094771	(Fig. 4)
PMID:36882296	PBO:0094771	(Fig. 4)
PMID:36882296	PBO:0099749	(Fig. 4)
PMID:36882296	PBO:0099749	(Fig. 4)
PMID:36882296	FYPO:0001357	(Fig. 9A)
PMID:36882296	PBO:0094771	(Fig. 13)
PMID:36882296	PBO:0106693	(Fig. 13)
PMID:36882296	PBO:0106693	(Fig. 13)
PMID:36882296	PBO:0106693	(Fig. 13)
PMID:36882296	PBO:0106693	(Fig. 13)
PMID:36882296	FYPO:0002085	(Fig. 6A)
PMID:36882296	FYPO:0002085	(Fig. 6A, 10A)
PMID:36882296	FYPO:0002085	(Fig. 6A)
PMID:36882296	FYPO:0002085	(Fig. 6A)
PMID:36882296	FYPO:0002085	(Fig. 6A)
PMID:36882296	FYPO:0002085	(Fig. 6A)
PMID:36882296	PBO:0094777	(Fig. 5B)
PMID:36882296	PBO:0094738	(Fig. 5B)
PMID:36882296	PBO:0094738	(Fig. 5B)
PMID:36882296	PBO:0094738	(Fig. 5B)
PMID:36882296	PBO:0094738	(Fig. 5B)
PMID:36882296	FYPO:0002085	(Fig. 5A)
PMID:36882296	FYPO:0002085	(Fig. 5A)
PMID:36882296	FYPO:0002061	(Fig. 5A)
PMID:36882296	FYPO:0002061	(Fig. 5A)
PMID:36882296	FYPO:0002061	(Fig. 5A)
PMID:36882296	FYPO:0002061	(Fig. 5A)
PMID:36882296	FYPO:0002085	(Fig. 5A)
PMID:36882296	FYPO:0002085	(Fig. 5A)
PMID:36882296	PBO:0094771	(Fig. 1B)
PMID:36882296	PBO:0094771	(Fig. 1B)
PMID:36882296	PBO:0094771	(Fig. 1B)
PMID:36882296	FYPO:0000080	(Fig. 1A)
PMID:36882296	PBO:0094771	(Fig. 1B)
PMID:36882296	FYPO:0002085	(Fig. 7A)
PMID:36882296	FYPO:0002085	(Fig. 7A)
PMID:36882296	PBO:0094738	(Fig. 7B, 10B, 12B)
PMID:36882296	PBO:0094771	(Fig. 6B)
PMID:36882296	PBO:0094771	(Fig. 6B)
PMID:36882296	PBO:0094771	(Fig. 6B)
PMID:36882296	PBO:0094771	(Fig. 6B)
PMID:36882296	PBO:0094771	(Fig. 6B)
PMID:36882296	PBO:0094771	(Fig. 6B)
PMID:36882296	FYPO:0002085	(Fig. 7A)
PMID:36882296	FYPO:0002085	(Fig. 7A)
PMID:36882296	PBO:0093554	(Fig. 7A)
PMID:36882296	FYPO:0002085	(Fig. 7A)
PMID:36882296	FYPO:0002085	(Fig. 7A)
PMID:36882296	PBO:0094738	(Fig. 7B)
PMID:36882296	PBO:0094738	(Fig. 7B)
PMID:36882296	PBO:0094738	(Fig. 7B)
PMID:36882296	PBO:0094738	(Fig. 7B)
PMID:36882296	PBO:0094738	(Fig. 7B)
PMID:36882296	PBO:0094738	(Fig. 7B)
PMID:36882296	FYPO:0002085	(Fig. 8A)
PMID:36882296	PBO:0094771	(Fig. 8B)
PMID:36882296	FYPO:0002085	(Fig. 8A)
PMID:36882296	PBO:0094771	(Fig. 8B)
PMID:36882296	FYPO:0000080	(Fig. 9A)
PMID:36882296	FYPO:0002085	(Fig. 6A)
PMID:36882296	FYPO:0000080	(Fig. 9A)
PMID:36882296	FYPO:0000080	(Fig. 9A)
PMID:36882296	FYPO:0000080	(Fig. 9A)
PMID:36882296	PBO:0094771	(Fig. 6B)
PMID:36882296	PBO:0094771	(Fig. 6B)
PMID:36882296	PBO:0094771	(Fig. 6B)
PMID:36882296	PBO:0094771	(Fig. 6B)
PMID:36882296	PBO:0094771	(Fig. 6B)
PMID:36882296	PBO:0094771	(Fig. 6B)
PMID:36882296	PBO:0094771	(Fig. 6B)
PMID:36882296	PBO:0094771	(Fig. 6B)
PMID:36882296	PBO:0094771	(Fig. 1B)
PMID:36882296	PBO:0094771	(Fig. 1B)
PMID:36882296	FYPO:0000080	(Fig. 1A)
PMID:36882296	FYPO:0000080	(Fig. 1A)
PMID:36882296	PBO:0094738	(Figs. 1B, 5B, 6B, 7B, 8B, 9B, 10B)
PMID:36882296	FYPO:0002085	(Fig. 1A)
PMID:36882296	FYPO:0002085	(Figs. 1A, 5A, 6A, 7A, 8A)
PMID:36882296	FYPO:0002061	(Fig. 1A)
PMID:36882296	FYPO:0002061	(Fig. 1A)
PMID:36951094	PBO:0112665	the AT-hook motifs were required for the mat3-M donor choice.
PMID:36951094	PBO:0112664	the Swi6-binding site was required for the mat2-P donor choice
PMID:36951094	GO:0007534	Rad54 further stimulates the activation of strand invasion of Rad51 by the Swi2-Swi5 complex.
PMID:36951094	GO:0007534	we demonstrated that the Swi2-Swi5 complex promotes Rad51-driven strand invasion in vitro
PMID:36951094	GO:0007534	we demonstrated that the Swi2-Swi5 complex promotes Rad51-driven strand invasion in vitro
PMID:36951094	PBO:0112307	(Fig. 6C)
PMID:36951094	PBO:0112657	(Fig. 6C)
PMID:36951094	PBO:0112663	(Fig. 6A)
PMID:36951094	PBO:0112663	(Fig. 6A)
PMID:36951094	PBO:0112308	(Fig. 5C)
PMID:36951094	PBO:0112661	(Fig. 3C)
PMID:36951094	PBO:0112659	(Fig. 2D)
PMID:36951094	PBO:0112659	(Fig. 2D)
PMID:36951094	PBO:0112658	(Fig. 2D)
PMID:36951094	PBO:0112658	(Fig. 2D)
PMID:36951094	PBO:0112658	(Fig. 2D)
PMID:36951094	PBO:0112660	(Fig. 2D)
PMID:36951094	PBO:0112660	(Fig. 2D)
PMID:36951094	PBO:0112660	(Fig. 2D)
PMID:36951094	PBO:0112660	(Fig. 2D)
PMID:36951094	PBO:0112660	(Fig. 2D)
PMID:36951094	PBO:0112659	(Fig. 2A)
PMID:36951094	PBO:0112658	(Fig. 2A)
PMID:36951094	PBO:0112307	(Fig. 5C)
PMID:36951094	PBO:0112307	(Fig. 5B and 5C)
PMID:36951094	FYPO:0000468	(Fig. 5B)
PMID:36951094	FYPO:0000468	(Fig. 5B)
PMID:36951094	PBO:0112657	(Fig. 5B and 5C)
PMID:36951094	PBO:0112308	(Fig. 6C)
PMID:36951094	PBO:0112661	(Fig. 3C)
PMID:36951094	PBO:0112662	(Fig. 3C)
PMID:36951094	PBO:0112657	(Fig. 5C)
PMID:36951094	PBO:0112308	(Fig. 5C)
PMID:36951094	PBO:0112308	(Fig. 5C)
PMID:36951094	GO:0007535	we demonstrated that the Swi2-Swi5 complex promotes Rad51-driven strand invasion in vitro
PMID:37039135	PBO:0114613	(Fig. S5)
PMID:37039135	PBO:0114611	(Fig. 6D)
PMID:37039135	PBO:0114612	(Fig. 6D,S7F)
PMID:37039135	PBO:0114611	(Fig. 6D,S7F)
PMID:37039135	PBO:0114612	(Fig. 7)
PMID:37039135	FYPO:0003250	(Fig. 7)
PMID:37039135	PBO:0114612	(Fig. 5D)
PMID:37039135	PBO:0114611	(Fig. 5D)
PMID:37039135	PBO:0114616	(Fig. 6)
PMID:37039135	PBO:0114612	(Fig. 6)
PMID:37039135	PBO:0114612	(Fig. 6D)
PMID:37039135	PBO:0114617	(Fig. S4A)
PMID:37039135	FYPO:0001357	(Fig. 5A)
PMID:37039135	FYPO:0001357	(Fig. 5A)
PMID:37039135	FYPO:0001357	(Fig. 5A)
PMID:37039135	PBO:0114611	(Fig. 4)
PMID:37039135	PBO:0114617	(Fig. S4A)
PMID:37039135	PBO:0114611	(Fig. 3)
PMID:37039135	PBO:0114618	(Fig. S4A)
PMID:37039135	PBO:0114613	(Fig. S5)
PMID:37039135	PBO:0114618	(Fig. S4A)
PMID:37039135	PBO:0114612	(Fig. 4)
PMID:37039135	PBO:0114612	However, early RBD-mNG localization at the division site observed in gef1Δ cells was rescued upon pak1OE, restoring it to late anaphase (Fig. S6A, B).
PMID:37039135	PBO:0114612	However, early RBD-mNG localization at the division site observed in gef1Δ cells was rescued upon pak1OE, restoring it to late anaphase (Fig. S6A, B).
PMID:37039135	FYPO:0001357	(Fig. 5A)
PMID:37039135	PBO:0114612	(Fig. S4)
PMID:37039135	PBO:0114614	(Fig. S7D)
PMID:37039135	PBO:0114615	(Fig. S7C)
PMID:37039135	PBO:0093560	(Fig. 5A)
PMID:37039135	PBO:0114612	(Fig. S4)
PMID:37039135	PBO:0018611	we found that in most cells, Rgf1- GFP and Rgf3-eGFP was localized to the division site at early stages in anaphase (Fig. S3D,E).
PMID:37039135	PBO:0018611	we found that in most cells, Rgf1- GFP and Rgf3-eGFP was localized to the division site at early stages in anaphase (Fig. S3D,E).
PMID:37039135	PBO:0018611	we found that the Rho probe RBD-tdTomato localized to the division site in late anaphase, immediately preceding the onset of ring constriction and septum ingression. Fig. 2
PMID:37039135	PBO:0018611	we observed Cdc42 activation in early anaphase, at the time of ring assembly. Fig. 2
PMID:37052630	PBO:0097264	(Fig. 2b)
PMID:37052630	PBO:0107560	(Fig. S1)
PMID:37052630	PBO:0093594	(Fig. S1)
PMID:37052630	PBO:0093564	Main text Table S1
PMID:37052630	PBO:0093564	Main text Table S1
PMID:37052630	PBO:0093564	(Fig. 2b) (comment: control)
PMID:37052630	PBO:0109067	(Fig. 2b)
PMID:37052630	PBO:0093564	Main text Table S1
PMID:37052630	PBO:0093564	Main text Table S1
PMID:37052630	PBO:0093564	Main text Table S1
PMID:37052630	PBO:0097264	(Fig. 2b)
PMID:37052630	PBO:0093570	(Fig. S1)
PMID:37052630	PBO:0097264	(Fig. 2b)
PMID:37052630	PBO:0097264	(Fig. 2b)
PMID:37052630	PBO:0109067	(Fig. 2b)
PMID:37076472	GO:0033698	(Figure 1)
PMID:37076472	GO:0033698	(Figure 1)
PMID:37076472	GO:0032221	(Figure 3)
PMID:37076472	GO:0033698	(Figure 1)
PMID:37076472	GO:0032221	(Figure 3)
PMID:37076472	GO:0032221	(Figure 3)
PMID:37076472	GO:0032221	(Figure 3)
PMID:37076472	GO:0032221	(Figure 3)
PMID:37076472	GO:0032221	(Figure 3)
PMID:37076472	GO:0033698	(Figure 1)
PMID:37076472	GO:0033698	(Figure 1)
PMID:37076472	GO:0033698	(Figure 1)
PMID:37076472	GO:0033698	(Figure 1)
PMID:37076472	GO:0033698	(Figure 1)
PMID:37076472	GO:0033698	(Figure 1)
PMID:37099380	FYPO:0009106	(comment: Closer to ring)
PMID:37099380	FYPO:0006338	(comment: Closer to ring)
PMID:37099380	FYPO:0006338	(comment: Closer to ring)
PMID:37120429	FYPO:0002060	Using this system, we observed that SpHsp90-EA supported viability of Sz. pombe cells (Fig. 1b).
PMID:37120429	FYPO:0001234	The suppressive effect of TA and EK on EA defects in non-essential functions were not specific to S. cerevisiae, as these mutations also rescued SpHsp90-EA mediated temperature sensitivity in Sz. pombe (Fig. 5d).
PMID:37120429	FYPO:0001234	The suppressive effect of TA and EK on EA defects in non-essential functions were not specific to S. cerevisiae, as these mutations also rescued SpHsp90-EA mediated temperature sensitivity in Sz. pombe (Fig. 5d).
PMID:37120429	FYPO:0001357	Sz. pombe cells expressing SpHsp90-EA had an osmolyte-remediated temperature sensitivity phenotype, which strongly suggested conservation of EA-specific phenotypes (Fig. 3b).
PMID:37120429	FYPO:0002061	Sz. pombe cells expressing SpHsp90-EA had an osmolyte-remediated temperature sensitivity phenotype, which strongly suggested conservation of EA-specific phenotypes (Fig. 3b).
PMID:37128864	PBO:0109305	(comment: The phenotype can be seen at 32˚C. The phenotype can be seen at 32˚C.) Furthermore, the log phase chromosomes more actively fluctuated in cdc2-L7 cells than in WT cells, and despite a repression in chromosome fluctuation, fluctuation was still elevated in the stationary phase, as demonstrated by an upward shift of the cdc2-L7 MSD plot of the ade6 locus and a complete lack of an overlap of their 95% confidence intervals with those of the WT plot (Fig. 5H).
PMID:37128864	PBO:0109304	The N/C ratio was also reduced but not significantly different from that of stationary phase cells (Fig. 1E; Fig. S1G), suggesting that the observed nuclear size differences from stationary phase originate from the cell size differences.
PMID:37128864	PBO:0093606	Loss of viability is evident only when cells are exposed to 32 degree before and upon entry into stationary phase.
PMID:37128864	PBO:0109302	Cell length increases during log and stationary phases at 32 degree.
PMID:37128864	GO:0140602	Localization depends on Cdc2 kinase activity but not on Clp1.
PMID:37128864	PBO:0102449	(comment: The phenotype can be seen at 32 degree.)
PMID:37156397	PBO:0105857	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	FYPO:0000087	(Figs. 3, S1C) Similar to the Δcoq2 (ppt1) strain, the Δcoq11 and Δcoq12 strains grew more slowly in the presence of 1 and 2 mM hydrogen peroxide or 0.5 mM CuSO4 than in its absence
PMID:37156397	PBO:0093578	(Figs. 3, S1C) Similar to the Δcoq2 (ppt1) strain, the Δcoq11 and Δcoq12 strains grew more slowly in the presence of 1 and 2 mM hydrogen peroxide or 0.5 mM CuSO4 than in its absence
PMID:37156397	FYPO:0002061	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	(Figs. 2B, S1B)
PMID:37156397	FYPO:0001355	We first noticed that ∆coq11 and ∆coq12 strains did not grow well on minimal medium, as was observed for CoQ-deficient S. pombe (Fig. 2A, S1A)
PMID:37156397	PBO:0105857	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	PBO:0105857	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	PBO:0105857	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	PBO:0105857	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	PBO:0105857	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	PBO:0105857	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	PBO:0105857	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	PBO:0109155	Interestingly, NAD+ reduction activity was clearly detected in purified Coq12-8xHis from S. pombe (Fig. 9A)
PMID:37156397	PBO:0109154	The amount of Coq4 was significantly reduced in ∆coq11 and ∆coq12 single mutants
PMID:37156397	PBO:0109153	(Fig. 4) The results revealed higher sulfide levels in both Δcoq11 and Δcoq12 strains
PMID:37156397	FYPO:0000103	(Figs. 3, S1C) Similar to the Δcoq2 (ppt1) strain, the Δcoq11 and Δcoq12 strains grew more slowly in the presence of 1 and 2 mM hydrogen peroxide or 0.5 mM CuSO4 than in its absence
PMID:37156397	PBO:0109151	(Fig. 2A) By contrast, the ∆coq12 strain showed almost no growth on PMLU medium containing cysteine.
PMID:37156397	GO:0005739	(comment: LC-MS)
PMID:37156397	GO:0005739	Coq12-GFP fusion (Fig. 8A). The GFP fluorescence pattern was similar to that of Mitotracker Red, a mitochondria stain. Mitochondrial localization of Coq12 was therefore confirmed
PMID:37156397	GO:0006744	(comment: low CoQ10 level)
PMID:37156397	PBO:0109152	The amount of Coq4 was significantly reduced in ∆coq11 and ∆coq12 single mutants
PMID:37156397	FYPO:0001413	(Fig. 4) The results revealed higher sulfide levels in both Δcoq11 and Δcoq12 strains
PMID:37156397	PBO:0105960	(Figs. 3, S1C) Similar to the Δcoq2 (ppt1) strain, the Δcoq11 and Δcoq12 strains grew more slowly in the presence of 1 and 2 mM hydrogen peroxide or 0.5 mM CuSO4 than in its absence
PMID:37156397	PBO:0109151	(Figs. 2A, S1A) Like other mutants lacking CoQ, the ∆coq11 strain showed better growth on cysteine-containing medium.
PMID:37156397	GO:0005739	(comment: LC-MS)
PMID:37156397	GO:0006744	(comment: low CoQ10 level)
PMID:37158439	FYPO:0000674	(Figure S2)
PMID:37158439	FYPO:0000674	(Figure S1)
PMID:37158439	FYPO:0000082	(Figure S1)
PMID:37158439	FYPO:0000082	(Figure S1)
PMID:37158439	FYPO:0004481	(Figure 1C)
PMID:37158439	FYPO:0000674	(Figure S3)
PMID:37158439	FYPO:0007774	(Figure 4C)
PMID:37158439	FYPO:0007774	(Figure 4C)
PMID:37158439	FYPO:0007774	(Figure 4C)
PMID:37158439	FYPO:0007774	(Figure 4C)
PMID:37158439	FYPO:0007774	(Figure 4C)
PMID:37158439	FYPO:0007774	(Figure 4C)
PMID:37158439	FYPO:0003532	(Figure 4A)
PMID:37158439	FYPO:0003532	(Figure 4A)
PMID:37158439	FYPO:0003532	(Figure 4A)
PMID:37158439	FYPO:0003532	(Figure 4A)
PMID:37158439	FYPO:0003532	(Figure 4A)
PMID:37158439	FYPO:0003532	(Figure 4A)
PMID:37158439	FYPO:0003532	(Figure 4A)
PMID:37158439	FYPO:0004481	(Figure 3C) We next asked if S. pombe Cyk3 was required for fic1-2A’s suppression of myo2-E1. Indeed, cyk3Δ prevented fic1-2A from suppressing myo2-E1
PMID:37158439	FYPO:0004481	(Figure 3C)
PMID:37158439	FYPO:0004481	(Figure 3C)
PMID:37158439	FYPO:0000674	(Figure 3C)
PMID:37158439	FYPO:0000674	(Figure 3C)
PMID:37158439	FYPO:0000674	(Figure 3B)
PMID:37158439	FYPO:0004481	(Figure 3B)
PMID:37158439	FYPO:0004481	(Figure 3C) We next asked if S. pombe Cyk3 was required for fic1-2A’s suppression of myo2-E1. Indeed, cyk3Δ prevented fic1-2A from suppressing myo2-E1
PMID:37158439	FYPO:0004481	(Figure 3C)
PMID:37158439	FYPO:0004481	(Figure 3B)
PMID:37158439	FYPO:0000639	(Figure 2) fic1-2A myo2-E1 cells can achieve membrane ingression and cell separation at myo2-E1’s restrictive temperature
PMID:37158439	FYPO:0000639	(Figure 2) fic1-2A myo2-E1 cells can achieve membrane ingression and cell separation at myo2-E1’s restrictive temperature
PMID:37158439	PBO:0109256	(Figure 2)
PMID:37158439	FYPO:0001760	(Figure 2)
PMID:37158439	FYPO:0006879	(Figure 2)
PMID:37158439	FYPO:0008090	(Figure 2)
PMID:37158439	FYPO:0008090	(Figure 1)
PMID:37158439	FYPO:0008090	(Figure 1)
PMID:37158439	FYPO:0008090	(Figure 1)
PMID:37158439	FYPO:0004481	(Figure S3)
PMID:37158439	FYPO:0004481	(Figure S2)
PMID:37158439	FYPO:0004481	(Figure S3)
PMID:37158439	FYPO:0000674	(Figure 3C)
PMID:37158439	FYPO:0000202	(Figure 1E and G)
PMID:37158439	FYPO:0008090	(Figure 1)
PMID:37158439	FYPO:0004557	From this screen we observed one significant interaction: fic1’s phospho-ablating mutant, fic1-2A, suppressed myo2-E1
PMID:37158439	FYPO:0004557	From this screen we observed one significant interaction: fic1’s phospho-ablating mutant, fic1-2A, suppressed myo2-E1
PMID:37158439	FYPO:0000674	(Figure S3)
PMID:37158439	FYPO:0004481	(Figure S3)
PMID:37158439	FYPO:0000674	(Figure S3)
PMID:37158439	FYPO:0000674	(Figure S3)
PMID:37158439	FYPO:0004481	(Figure S2)
PMID:37158439	FYPO:0000674	(Figure S2)
PMID:37158439	FYPO:0004481	(Figure 1B) From this screen we observed one significant interaction: fic1’s phospho-ablating mutant, fic1-2A, suppressed myo2-E1
PMID:37158439	PBO:0109255	(Figure 1B)
PMID:37158439	FYPO:0000674	(Figure 4D)
PMID:37158439	FYPO:0000082	(Figure 4D)
PMID:37158439	FYPO:0000082	(Figure 4D)
PMID:37158439	FYPO:0000080	(Figure S1)
PMID:37158439	FYPO:0000674	(Figure S1)
PMID:37158439	FYPO:0000674	(Figure S1)
PMID:37158439	FYPO:0000674	(Figure S1)
PMID:37158439	FYPO:0005905	(Figure 1E and G)
PMID:37158439	FYPO:0005905	(Figure 1E and G)
PMID:37158439	FYPO:0000202	(Figure 1E and G)
PMID:37158439	FYPO:0004481	(Figure 1C)
PMID:37160462	PBO:0109839	Phenotype complementation by human RAD23A
PMID:37162093	FYPO:0002058	(Figure 5A,B)
PMID:37162093	FYPO:0001420	(Figure 5AB; Figure S3)
PMID:37162093	FYPO:0002104	(Figure 7)
PMID:37162093	FYPO:0002104	(Figure 7)
PMID:37162093	FYPO:0002104	(Figure 7)
PMID:37162093	PBO:0093560	(Figure 3A,D, 6A,C,E)
PMID:37162093	FYPO:0001420	(Figure 6B,D,E, S2)
PMID:37162093	PBO:0093561	(Figure 3B,E; Figure 6A,C,E)
PMID:37162093	FYPO:0002058	(Figure 4A,C)
PMID:37162093	FYPO:0002058	(Figure 4A,C)
PMID:37162093	PBO:0093561	(Figure 4A,C; Figure 6B,D,E)
PMID:37162093	FYPO:0000017	(Figure 7)
PMID:37162093	PBO:0093559	(Figure 3C,F; Figure 6A,C,E)
PMID:37162093	FYPO:0002105	(Figure 7)
PMID:37162093	FYPO:0002058	(Figure S2)
PMID:37162093	FYPO:0002058	(Figure S2)
PMID:37162093	FYPO:0001420	(Figure 4B,D, 6B,D,E)
PMID:37162093	FYPO:0002058	(Figure 4B,D)
PMID:37162093	FYPO:0002058	(Figure 4B,D)
PMID:37162093	FYPO:0002058	(Figure 5A,B)
PMID:37162093	FYPO:0002273	(Figure 7)
PMID:37164017	PBO:0112859	Surprisingly, the growth defect of S. pombe cox6D mutants in EMM could be rescued by arginine but not glutamate or glutamine (Figure 2H).
PMID:37164017	PBO:0093559	(comment: CHECK Growth rate improved by addition of either glutamate, glutamine, or arginine)
PMID:37164017	PBO:0093559	(comment: CHECK Growth rate improved by addition of either glutamate, glutamine, or arginine)
PMID:37164017	PBO:0093559	(comment: CHECK Growth rate improved by addition of either glutamate, glutamine, or arginine)
PMID:37164017	GO:0019643	Interestingly, both wild-type and cox6D S. pombe, and wild-type S. japonicus, showed high M + 3 fumarate fractions (Figure 2D). This indicates that not only S. japonicus and nonrespiring S. pombe but also the wild-type S. pombe operate the reductive TCA branch.
PMID:37164017	GO:0006099	M + 2 fumarate is typically associated with the oxidative TCA cycle52,57-59 (Figure 2A). Indeed, only respiro-fermenting wild-type S. pombe showed M + 2 fumarate (Figure 2C). M + 3 fumarate likely originates from the reductive TCA branch52,57-59 (Figure 2B).
PMID:37164017	FYPO:0001563	The non-respiring S. pombe cox6D mutant did not upregulate G3P synthesis as compared with the wild-type. S. japonicus also maintained a larger pool of G3P than S. pombe (Figure S1G)
PMID:37164017	GO:0006099	inferred from isotope labelling Figure 1A and We assessed the TCA cycle architecture in S. pombe and S. japonicus using stable isotope tracing metabolomics, quantifying the ratios of different TCA-intermediate isotopologs after feeding cells with 13C6-glucose (Figures 2A and 2B).
PMID:37164017	GO:0006099	inferred from isotope labelling Figure 1A and We assessed the TCA cycle architecture in S. pombe and S. japonicus using stable isotope tracing metabolomics, quantifying the ratios of different TCA-intermediate isotopologs after feeding cells with 13C6-glucose (Figures 2A and 2B).
PMID:37164017	GO:0006099	inferred from isotope labelling Figure 1A and We assessed the TCA cycle architecture in S. pombe and S. japonicus using stable isotope tracing metabolomics, quantifying the ratios of different TCA-intermediate isotopologs after feeding cells with 13C6-glucose (Figures 2A and 2B).
PMID:37164017	GO:0006099	inferred from isotope labelling Figure 1A and We assessed the TCA cycle architecture in S. pombe and S. japonicus using stable isotope tracing metabolomics, quantifying the ratios of different TCA-intermediate isotopologs after feeding cells with 13C6-glucose (Figures 2A and 2B).
PMID:37164017	GO:0006099	inferred from isotope labelling Figure 1A and We assessed the TCA cycle architecture in S. pombe and S. japonicus using stable isotope tracing metabolomics, quantifying the ratios of different TCA-intermediate isotopologs after feeding cells with 13C6-glucose (Figures 2A and 2B).
PMID:37164017	GO:0006099	inferred from isotope labelling Figure 1A and We assessed the TCA cycle architecture in S. pombe and S. japonicus using stable isotope tracing metabolomics, quantifying the ratios of different TCA-intermediate isotopologs after feeding cells with 13C6-glucose (Figures 2A and 2B).
PMID:37164017	GO:0006099	inferred from isotope labelling Figure 1A and We assessed the TCA cycle architecture in S. pombe and S. japonicus using stable isotope tracing metabolomics, quantifying the ratios of different TCA-intermediate isotopologs after feeding cells with 13C6-glucose (Figures 2A and 2B).
PMID:37164017	GO:0006099	inferred from isotope labelling Figure 1A & We assessed the TCA cycle architecture in S. pombe and S. japonicus using stable isotope tracing metabolomics, quantifying the ratios of different TCA-intermediate isotopologs after feeding cells with 13C6-glucose (Figures 2A and 2B).
PMID:37164017	PBO:0093561	(comment: CHECK Growth rate improved by addition of either glutamate, glutamine, or arginine)
PMID:37164017	FYPO:0007368	Consistent with previous work,63 the higher Pyk1 activity in S. pombe increased the cellular ATP/ADP ratio, whereas the lower Pyk1 activity in S. japonicus reduced it (Figure 3B).
PMID:37164017	FYPO:0001420	Strikingly, while the deletion of gpd1 in S. pombe did not negatively affect its growth, regardless of respiratory activity (Figures 1E and S1J)
PMID:37164017	PBO:0093559	(comment: CHECK Growth rate improved by addition of arginine)
PMID:37164017	PBO:0109238	Whereas the deletion of cox6 critically decreased oxygen consumption in S. pombe, we observed no such effect in S. japonicus (Figure 1A).
PMID:37191320	GO:0044804	We further found that the inner nuclear membrane protein Lem2 [26] was also degraded in a manner dependent on Hva22 (Figure 1H,I), indicating that the nuclear envelope undergoes Hva22- dependent reticulophagy. (vw I think this should be nucleophagy becasue IMN is not comnnected to ER)
PMID:37191320	GO:0016236	Next, selective types of autophagy, such as mitophagy and pexophagy, were monitored by the processing of the mitochondrial protein Tuf1- RFP or Sdh2-GFP [21] and the peroxisomal protein Pex11- GFP, respectively. We observed that the hva22Δ mutant was partially defective in both mitophagy (Figure 2D and Fig. S2E) and pexophagy (Figure 2E).
PMID:37191320	PBO:0104254	In hva22Δ cells, reticulophagy was abolished, similar to cells lacking the core autophagy protein Atg1 (Figure 1B).
PMID:37191320	PBO:0109202	(Fig. S4E) revealed that the ER-shaping activities of the ΔC21-60 and ΔN29 mutants were partially and severely impaired, respectively (Fig. S4E)
PMID:37191320	PBO:0109201	(Fig. S4F), the ΔC21-60 and ΔN29 mutants exhibited partial and severe defects in reticulophagy, respectively, whereas the both mutant proteins were detectable on the ER (Fig. S4G)
PMID:37191320	PBO:0109200	(Fig. S4E) revealed that the ER-shaping activities of the ΔC21-60 and ΔN29 mutants were partially and severely impaired, respectively (Fig. S4E)
PMID:37191320	PBO:0109199	(Fig. S4F), the ΔC21-60 and ΔN29 mutants exhibited partial and severe defects in reticulophagy, respectively, whereas the both mutant proteins were detectable on the ER (Fig. S4G)
PMID:37191320	GO:0090158	The growth defect of the triple mutant strain defective in Spo7, Rtn1, and Yop1 is restored by the overexpression of the budding yeast reticulophagy receptor Atg40, a reticulon- and REEP-like protein that contains an ER-shaping activit
PMID:37191320	GO:0005783	Consistently, Hva22 was observed on the ER under both nitrogen-rich and starvation conditions (Figure 3C).
PMID:37192628	FYPO:0007448	Loss of Atg44 in either S. pombe or S. cerevisiae did not or only marginally affected non-selective macroautophagy, as measured by GFP/RFP processing (Figures S1C, S1D, and S1F) or the Pho8D60 assay (Figure 1E), or other types of selective autophagy including the Cvt pathway that delivers the precursor form of the hydrolase aminopeptidase I to the vacuole (Figure S1G), endoplasmic reticulum-phagy/reticulophagy (Figures S1E and S1H), and pexophagy (Figure S1I), suggesting that Atg44 is specifically required for mitophagy.
PMID:37192628	PBO:0109197	As expected, in S. pombe atg44D cellslacking Mgm1, some of the mitochondria became fragmented and mitophagy was partially rescued (Figures 4A and S3F).
PMID:37192628	FYPO:0003810	Overexpression of Atg44 in both species caused mitochondrial fragmentation not only in wild-type cells but also in Dnm1-deficient cells (Figures 3E and 3F).
PMID:37192628	GO:0008289	Atg44 binds to lipid membranes in vitro (Figures 5A and 5E), and the cryo-EM and HS-AFM analyses (Figures 5F-5I) suggest that Atg44 tends to bind to lipid membranes with high curvature.
PMID:37192628	PBO:0109196	Unexpectedly, we noticed that addition of Sp-Atg44 caused fragmentation of lipid bilayers on the mica (compare Figures 7B and 7C), and the fragmented lipid bilayers abundant with Sp-Atg44 underwent division and fusion (Figure 7D; Video S6). These observations suggest that Sp-Atg44 has the ability to cause membrane fragility through physical interaction.
PMID:37192628	GO:0005758	Based on these results, we conclude that Atg44 localizes in the IMS and is not a transmembrane protein.
PMID:37192628	FYPO:0007594	In atg44D cells, mitophagy was completely blocked similarly to cells lacking Atg1, a core autophagy protein (Figures 1A and S1B).
PMID:37192628	FYPO:0004340	Similarly, loss of Atg44 in S. pombe affected mitochondrial morphology; some of the Sp-atg44D cells showed spherically enlarged mitochondria like Sp-dnm1D cells (Figure 3D)
PMID:37192628	PBO:0109197	As expected, in S. pombe atg44D cellslacking Mgm1, some of the mitochondria became fragmented and mitophagy was partially rescued (Figures 4A and S3F).
PMID:37200372	PBO:0109418	(Fig. 6)
PMID:37200372	PBO:0093587	(Fig. 7)
PMID:37200372	PBO:0093587	(Fig. 7)
PMID:37200372	PBO:0093613	(Fig. 7)
PMID:37200372	FYPO:0000268	(Fig. 7)
PMID:37200372	FYPO:0000268	(Fig. 7)
PMID:37200372	PBO:0093587	(Fig. 7)
PMID:37200372	PBO:0093587	(Fig. 7)
PMID:37200372	PBO:0093587	(Fig. 7)
PMID:37200372	PBO:0093613	(Fig. 7)
PMID:37200372	FYPO:0000085	(Fig. 7)
PMID:37200372	FYPO:0000085	(Fig. 7)
PMID:37200372	FYPO:0000268	(Fig. 7)
PMID:37200372	PBO:0093629	(Fig. 7)
PMID:37200372	FYPO:0000268	(Fig. 7)
PMID:37200372	PBO:0109430	(Fig. S12)
PMID:37200372	PBO:0109430	(Fig. S12)
PMID:37200372	PBO:0109429	(Fig. S12)
PMID:37200372	PBO:0109428	(Fig. S12)
PMID:37200372	PBO:0100985	(Fig. S12)
PMID:37200372	PBO:0109421	(Fig. 6)
PMID:37200372	PBO:0109421	(Fig. 6)
PMID:37200372	PBO:0109427	(Fig. 6)
PMID:37200372	PBO:0109427	(Fig. 6)
PMID:37200372	PBO:0109426	(Fig. 6)
PMID:37200372	PBO:0109426	(Fig. 6)
PMID:37200372	PBO:0109419	(Fig. 6)
PMID:37200372	PBO:0109414	(Fig. 6)
PMID:37200372	PBO:0109414	(Fig. 6)
PMID:37200372	FYPO:0000088	(Fig. 6)
PMID:37200372	PBO:0109412	(Fig. 6B)
PMID:37200372	FYPO:0000089	(Fig. 6)
PMID:37200372	PBO:0109425	(Fig. 6B)
PMID:37200372	FYPO:0000089	(Fig. 6)
PMID:37200372	FYPO:0000088	(Fig. 6)
PMID:37200372	FYPO:0001355	(Fig. S2) and text
PMID:37200372	FYPO:0002060	(Fig. S2) and text
PMID:37200372	FYPO:0002061	(Fig. S2) and text
PMID:37200372	FYPO:0002061	(Fig. S2) and text
PMID:37200372	PBO:0109424	(Fig. 2)
PMID:37200372	PBO:0109424	(Fig. 2)
PMID:37200372	PBO:0109424	(Fig. 2)
PMID:37200372	PBO:0109423	(Fig. 2)
PMID:37200372	PBO:0109423	(Fig. 2)
PMID:37200372	PBO:0109422	(Fig. 2)
PMID:37200372	PBO:0109422	(Fig. 2)
PMID:37200372	PBO:0109422	(Fig. 2)
PMID:37200372	PBO:0109421	(Fig. 2)
PMID:37200372	PBO:0109420	(Fig. 2)
PMID:37200372	PBO:0109421	(Fig. 2)
PMID:37200372	PBO:0109420	(Fig. 2)
PMID:37200372	PBO:0109419	(Fig. 1)
PMID:37200372	PBO:0109419	(Fig. 1)
PMID:37200372	PBO:0109418	(Fig. 1)
PMID:37200372	PBO:0109418	(Fig. 1)
PMID:37200372	PBO:0109417	(Fig. 1)
PMID:37200372	PBO:0109416	(Fig. 1)
PMID:37200372	PBO:0109415	(Fig. 1)
PMID:37200372	PBO:0109415	(Fig. 1)
PMID:37200372	PBO:0109414	(Fig. 1)
PMID:37200372	PBO:0109413	(Fig. 1)
PMID:37200372	PBO:0109412	(Fig. 1)
PMID:37200372	PBO:0109411	(Fig. 1)
PMID:37200372	PBO:0109411	(Fig. 1)
PMID:37200372	PBO:0109411	(Fig. 1)
PMID:37200372	FYPO:0000089	(Fig. 1)
PMID:37200372	FYPO:0000089	(Fig. 1)
PMID:37200372	FYPO:0000089	(Fig. 1)
PMID:37200372	FYPO:0000089	(Fig. 1)
PMID:37200372	FYPO:0000089	(Fig. 1)
PMID:37200372	FYPO:0000089	(Fig. 1)
PMID:37200372	FYPO:0000088	(Fig. 1)
PMID:37200372	FYPO:0000088	(Fig. 1)
PMID:37200372	FYPO:0000088	(Fig. 1)
PMID:37200372	FYPO:0000088	(Fig. 1)
PMID:37200372	FYPO:0000088	(Fig. 1)
PMID:37200372	FYPO:0000088	(Fig. 1)
PMID:37200372	FYPO:0000088	(Fig. 1)
PMID:37237082	PBO:0096838	To our surprise, not only srr1Δ but also skb1Δ reduced GCR rates in the rad51Δ background, demonstrating that both Srr1 and Skb1 cause GCRs.
PMID:37237082	PBO:0109253	In the wild-type background, srr1Δ but not skb1Δ slightly reduced GCR rates, showing that Srr1 is required for GCRs even in the presence of Rad51
PMID:37237082	PBO:0093615	(Figure 5e)
PMID:37237082	PBO:0093579	(Figure 5e)
PMID:37237082	PBO:0093618	(Figure 5e)
PMID:37237082	PBO:0093615	(Figure 5e)
PMID:37237082	PBO:0093579	(Figure 5e)
PMID:37237082	PBO:0093618	(Figure 5e)
PMID:37237082	PBO:0096838	Both srr1-D111A,P112A and srr1- H148A mutations reduced GCR rates (Fig. 5d).
PMID:37237082	PBO:0096838	Both srr1-D111A,P112A and srr1- H148A mutations reduced GCR rates (Fig. 5d).
PMID:37237082	PBO:0096838	(Fig. 1e) Genome sequencing of one of them identified the srr1/ ber1-W157R and skb1-A377V mutations in their SRR1-like and arginine methyltransferase (RMTase) domains, respectively (Fig. 1b).
PMID:37237082	PBO:0093615	(Figure 3a)
PMID:37237082	PBO:0096839	(Fig. 6A)
PMID:37237082	PBO:0096839	(Fig. 6A)
PMID:37237082	FYPO:0005371	(Fig. 3e)
PMID:37237082	FYPO:0002150	We crossed srr1Δ and rad52Δ haploid strains and dissected the tetrads but failed to obtain srr1Δ rad52Δ progenies (Fig. 4b)
PMID:37237082	GO:0000076	Unlike chk1Δ, in the srr1Δ strain, the septation index declined to the wild-type level by 6 h after MMS addition, suggesting that Srr1 is dispensable for cell cycle arrest.
PMID:37237082	PBO:0108250	(Fig. 3e) We found that srr1Δ and srr1-W157R increased the rate of chromosome loss. (In WT and rad51 backgrounds)
PMID:37237082	PBO:0108250	(Fig. 3e) We found that srr1Δ and srr1-W157R increased the rate of chromosome loss. (In WT and rad51 backgrounds)
PMID:37237082	PBO:0096838	The rad52-R45K, rad52Δ, and srr1Δ mutations eliminate ~90% of isochromosomes in rad51Δ cells (Fig. 2c and ref. 32), indicating that both Rad52 and Srr1 are essential for the major pathway of isochromosome formation.
PMID:37237082	FYPO:0001355	Like srr1Δ cells, srr1-W157R, srr1-D111A,P112A, and srr1-H184A cells produced small colonies (Supplementary Fig. 2b), consistent with the role of the SRR1-like domain even in the absence of exogenous DNA damage.
PMID:37237082	FYPO:0001355	Like srr1Δ cells, srr1-W157R, srr1-D111A,P112A, and srr1-H184A cells produced small colonies (Supplementary Fig. 2b), consistent with the role of the SRR1-like domain even in the absence of exogenous DNA damage.
PMID:37237082	FYPO:0001355	Like srr1Δ cells, srr1-W157R, srr1-D111A,P112A, and srr1-H184A cells produced small colonies (Supplementary Fig. 2b), consistent with the role of the SRR1-like domain even in the absence of exogenous DNA damage.
PMID:37237082	FYPO:0001355	Like srr1Δ cells, srr1-W157R, srr1-D111A,P112A, and srr1-H184A cells produced small colonies (Supplementary Fig. 2b), consistent with the role of the SRR1-like domain even in the absence of exogenous DNA damage.
PMID:37237082	PBO:0096839	(Fig. 6A)
PMID:37237082	PBO:0096839	(Fig. 6A)
PMID:37237082	PBO:0093579	(Figure 3a)
PMID:37237082	PBO:0093618	(Figure 3a)
PMID:37237082	PBO:0096838	srr1-W157R and rad52-R45K or pcn1-K107R additively reduce gross chromosomal rearrangement. srr1-W157R and pcn1-K107R also additively reduced GCR rates in rad51Δ cells (Fig. 4a).
PMID:37237082	PBO:0096838	srr1-W157R and rad52-R45K or pcn1-K107R additively reduce gross chromosomal rearrangement. srr1-W157R and pcn1-K107R also additively reduced GCR rates in rad51Δ cells (Fig. 4a).
PMID:37237082	FYPO:0006437	Normal Chk1 phosphorylation and cell cycle arrest
PMID:37237082	PBO:0103454	To our surprise, not only srr1Δ but also skb1Δ reduced GCR rates in the rad51Δ background, demonstrating that both Srr1 and Skb1 cause GCRs.
PMID:37237082	PBO:0103454	To our surprise, not only srr1Δ but also skb1Δ reduced GCR rates in the rad51Δ background, demonstrating that both Srr1 and Skb1 cause GCRs.
PMID:37237082	FYPO:0001690	(Figure 3a)
PMID:37237082	FYPO:0000963	(Figure 3a)
PMID:37237082	FYPO:0000957	(Figure 3a)
PMID:37237082	PBO:0109251	skb1∆ and srr1∆ additively reduce the rate of gross chromosomal rearrangements in rad51 deletion background.
PMID:37237082	PBO:0109251	skb1∆ and srr1∆ additively reduce the rate of gross chromosomal rearrangements in rad51 deletion background.
PMID:37237082	PBO:0096838	To our surprise, not only srr1Δ but also skb1Δ reduced GCR rates in the rad51Δ background, demonstrating that both Srr1 and Skb1 cause GCRs.
PMID:37237082	PBO:0093618	(Figure 3a)
PMID:37237082	PBO:0093579	(Figure 3a)
PMID:37237082	PBO:0093615	(Figure 3a)
PMID:37237082	FYPO:0005371	(Fig. 3e)
PMID:37237082	FYPO:0006437	Normal Chk1 phosphorylation and cell cycle arrest
PMID:37237082	FYPO:0002150	We crossed srr1Δ and rad52Δ haploid strains and dissected the tetrads but failed to obtain srr1Δ rad52Δ progenies (Fig. 4b)
PMID:37279920	PBO:0095652	We also detected intermediate phenotypes for the 8 ccr4∆ mutant, pointing to a partial contribution of this RNA deadenylase (Fig. 1g-h; 9 Supplementary Fig. 1b-d).
PMID:37279920	PBO:0109206	Strikingly, however, silencing at the mating type locus was completely abolished in the 22 absence of Caf1 and Mot2, similar to clr4∆ cells, as revealed by the lack of cell growth on 23 5FOA-containing medium and the marked accumulation of ura4+ transcripts (Fig. 1g-h).
PMID:37279920	PBO:0109206	Strikingly, however, silencing at the mating type locus was completely abolished in the 22 absence of Caf1 and Mot2, similar to clr4∆ cells, as revealed by the lack of cell growth on 23 5FOA-containing medium and the marked accumulation of ura4+ transcripts (Fig. 1g-h).
PMID:37279920	PBO:0109208	(Figure 2)
PMID:37288768	FYPO:0007664	Notably, the nuclear displacement phenotypewas associated with mid-anaphase spindle bending and/or detachment of one of the daughter chromosome masses from the spindle, and subsequent spindle disassembly and merger of the two daughter chromosome masses into one diploid nucleus (Figs 1B and 2B).
PMID:37288768	PBO:0110055	(Fig. 1B)
PMID:37288768	PBO:0110056	(Fig. 4C)
PMID:37288768	PBO:0110298	(Fig. 1B)
PMID:37288768	PBO:0110057	(Fig. 2G)
PMID:37288768	PBO:0019031	(Fig. 3)
PMID:37288768	PBO:0019031	(Fig. 3)
PMID:37288768	PBO:0093562	(Fig. S2A) We first validated the previous report of cbf11Δ cells being sensitive to TBZ. When plated on YES medium containing TBZ, the cbf11Δ mutant indeed showed strong sensitivity to the drug (Fig. S2A)
PMID:37288768	FYPO:0000891	(Fig. 4A, S2)
PMID:37288768	PBO:0110059	(Fig. 4D)
PMID:37288768	FYPO:0000886	(Fig. 4A, S3)
PMID:37288768	PBO:0019232	(Fig. 3)
PMID:37288768	PBO:0019232	(Fig. 3)
PMID:37288768	PBO:0019031	(Fig. 3)
PMID:37288768	PBO:0110058	(Fig. 2E)
PMID:37288768	PBO:0019031	(Fig. 3)
PMID:37400983	PBO:0109932	The hinge and the N-terminal disordered regions of Chp2 (Chp2-H and Chp2-N) also bound DNA (Fig. 2H, J and M)
PMID:37400983	PBO:0109931	no detectable DNA-binding activity was observed for Chp2-CD (Fig. 2I and M).
PMID:37400983	PBO:0109932	Interestingly, we found that Chp2-CSD exhibited a robust DNA binding activity (Fig. 2K and M)
PMID:37400983	PBO:0109933	when these were replaced by alanine (Fig. 3A), the resulting Chp2-H mutant (Chp2-H5A) no longer bound to DNA (Fig. 3B and C, and Supplementary Fig. S2A and S2D)
PMID:37400983	FYPO:0002336	(comment: mat3M::ura4+ reporter silencing)
PMID:37400983	FYPO:0002336	(comment: mat3M::ura4+ reporter silencing)
PMID:37400983	FYPO:0002827	(comment: mat3M::ura4+ reporter silencing) |combined mutations of the hinge and one of the mutations in the N-terminus of CSD (mut3 and mut5) showed a silencing defect (Fig. 4C)
PMID:37400983	PBO:0109934	exhibited only a very weak DNA binding activity compared to wild-type Chp2-CD (Chp2-CSDWT ) (Fig. 3D and E, and Supplementary Fig. S2B and S2E)
PMID:37400983	PBO:0109933	Chp2-CSD (Chp2-CSD3A) no longer bound DNA (Fig. 3F and Supplementary Fig. S2B), Chp2 with H5A mutation in the hinge (Chp2-mut1) or with either CSD2A or CSD3A mutation in the CSD (Chp2-mut2 and Chp2- mut4) exhibited weaker DNA-binding activity compared to wild-type Chp2 (Chp2-WT) (Fig. 3H, I, J and L and Supplementary Fig. S2C and S2F)
PMID:37400983	PBO:0109933	Interestingly, when amino acid substitutions in the hinge and CSD were combined, the resulting Chp2 mutants (Chp2-mut3 and Chp3-mut5) no longer bound DNA (Fig. 3K and M, and Supplementary Fig. S2F)
PMID:37400983	FYPO:0004984	Chp2 mutants lacking DNA-binding activities associated with both the hinge and the N-terminus of CSD (mut 3 and mut 5) exhibited reduced heterochromatin association compared to wild-type Chp2 at representative heterochromatic regions (centromeric dg, the mating-type cenH, telomere and mat3M::ura4+), and the reduction was more severe for Chp2-mut3 compared to Chp2-mut5 (Fig. 6A).
PMID:37400983	FYPO:0002336	(comment: mat3M::ura4+ reporter silencing)
PMID:37400983	FYPO:0002827	(comment: mat3M::ura4+ reporter silencing )| combined mutations of the hinge and one of the mutations in the N-terminus of CSD (mut3 and mut5) showed a silencing defect (Fig. 4C)
PMID:37400983	FYPO:0005929	Chp2 mutants lacking DNA-binding activities associated with both the hinge and the N-terminus of CSD (mut 3 and mut 5) exhibited reduced heterochromatin association compared to wild-type Chp2 at representative heterochromatic regions (centromeric dg, the mating-type cenH, telomere and mat3M::ura4+), and the reduction was more severe for Chp2-mut3 compared to Chp2-mut5 (Fig. 6A).
PMID:37400983	FYPO:0007336	(comment: mat3M::ura4+ reporter silencing )| combined mutations of the hinge and one of the mutations in the N-terminus of CSD (mut3 and mut5) showed a silencing defect (Fig. 4C)
PMID:37400983	FYPO:0003231	Chp2 mutants lacking DNA-binding activities associated with both the hinge and the N-terminus of CSD (mut 3 and mut 5) exhibited reduced heterochromatin association compared to wild-type Chp2 at representative heterochromatic regions (centromeric dg, the mating-type cenH, telomere and mat3M::ura4+), and the reduction was more severe for Chp2-mut3 compared to Chp2-mut5 (Fig. 6A).
PMID:37400983	PBO:0109927	As previously reported, in wild-type cells, Swi6 was present in both the soluble (S) and chromatin-enriched pellet (P) fractions, with approximately 40% of the total Swi6 protein detected in the pellet fraction, and most of the Swi6 in the pellet fraction was redistributed to the soluble fraction in clr4∆ cells (Fig. 1A).
PMID:37400983	PBO:0109928	In contrast, Chp2 was preferentially present in the chromatin-enriched pellet fraction in wild-type cells, and the Chp2 in this fraction was not altered by the clr4+ depletion (Fig. 1B).
PMID:37400983	PBO:0109928	Interestingly, we found that Chp2 in the chromatin-enriched pellet fraction was not affected by the Mit1I11R mutation (Fig. 1B).
PMID:37400983	GO:0003677	Using purified full-length, dimerized Chp2 and Swi6, we performed EMSAs using pericentromeric DNA as a probe. Consistent with previous results, Swi6 bound DNA efficiently, and Chp2 also showed similar DNA binding activity (Fig. 2B and C).
PMID:37400983	GO:0003677	Using purified full-length, dimerized Chp2 and Swi6, we performed EMSAs using pericentromeric DNA as a probe. Consistent with previous results, Swi6 bound DNA efficiently, and Chp2 also showed similar DNA binding activity (Fig. 2B and C).
PMID:37400983	PBO:0109930	(comment: CHECK ****NEED TO FIX allele description*****.) The N-terminal disordered region of Swi6 (Swi6-N) bound weakly to DNA (Fig. 2D and L)
PMID:37400983	PBO:0109931	whereas no DNA binding activity was detected for Swi6-CD or Swi6-CSD (Fig. 2E, G and L).
PMID:37400983	PBO:0109931	whereas no DNA binding activity was detected for Swi6-CD or Swi6-CSD (Fig. 2E, G and L).
PMID:37400983	PBO:0109932	The hinge and the N-terminal disordered regions of Chp2 (Chp2-H and Chp2-N) also bound DNA (Fig. 2H, J and M)
PMID:37400983	PBO:0109933	Interestingly, when amino acid substitutions in the hinge and CSD were combined, the resulting Chp2 mutants (Chp2-mut3 and Chp3-mut5) no longer bound DNA (Fig. 3K and M, and Supplementary Fig. S2F)
PMID:37403782	FYPO:0008110	reproducible decrease in modification at several other sites, most notably A64 (Figure 1C, D, Supplementary Figure S3).
PMID:37403782	FYPO:0008110	reproducible decrease in modification at several other sites, most notably A64 (Figure 1C, D, Supplementary Figure S3).
PMID:37403782	FYPO:0008110	reproducible decrease in modification at several other sites, most notably A64 (Figure 1C, D, Supplementary Figure S3).
PMID:37403782	PBO:0109442	Deletion of snoZ30 and sno530 resulted in a loss of 2′-O-methylation at A41 and A64, respectively, suggesting that sno530 is indeed the A64 U6-modifying snoRNA (Figure 1C, D, Supplementary Figure S3).
PMID:37403782	PBO:0109443	Still, as mean intron retention values indeed showed an increase upon Bmc1 deletion (Figure 5A), we chose several representative intron retention events to validate with semiquantitative RT-PCR (one of which, intron 1 of pud1, displayed a statistically significant increase upon Bmc1 deletion at 32 ̊C in our RNA Seq dataset).
PMID:37403782	PBO:0109444	Deletion of snoZ30 and sno530 resulted in a loss of 2′-O-methylation at A41 and A64, respectively, suggesting that sno530 is indeed the A64 U6-modifying snoRNA (Figure 1C, D, Supplementary Figure S3).
PMID:37403782	PBO:0109444	Deletion of snoZ30 and sno530 resulted in a loss of 2′-O-methylation at A41 and A64, respectively, suggesting that sno530 is indeed the A64 U6-modifying snoRNA (Figure 1C, D, Supplementary Figure S3).
PMID:37403782	GO:0005732	we found that all three proteins are necessary for an interaction with U6 (Figure 1A, Supplementary Figure S1B).
PMID:37403782	GO:0005732	we found that all three proteins are necessary for an interaction with U6 (Figure 1A, Supplementary Figure S1B).
PMID:37403782	GO:0005732	we found that all three proteins are necessary for an interaction with U6 (Figure 1A, Supplementary Figure S1B).
PMID:37403782	FYPO:0008112	Importantly, co-migration of Pof8 with U6 was lost upon deletion of Bmc1 (Figure 1B), as well as co-migration of Bmc1 with U6 upon deletion of Pof8 (Supplementary Figure S1C).
PMID:37403782	FYPO:0008112	Importantly, co-migration of Pof8 with U6 was lost upon deletion of Bmc1 (Figure 1B), as well as co-migration of Bmc1 with U6 upon deletion of Pof8 (Supplementary Figure S1C).
PMID:37403782	GO:0030515	we examined our Bmc1 RIP-Seq dataset (20), which revealed an interaction between Bmc1 and snoZ30, which guides 2′-O-methylation of U6 at position 41 (41) (Supplementary Figures S1A, S2A, B).
PMID:37403782	PBO:0109446	Further supporting the idea that U6 complex formation is contingent on the presence of all three proteins, we observed a loss of snoZ30 binding to Bmc1 upon knockout of any member of the complex (Supplementary Figure S2A).
PMID:37403782	PBO:0109446	Further supporting the idea that U6 complex formation is contingent on the presence of all three proteins, we observed a loss of snoZ30 binding to Bmc1 upon knockout of any member of the complex (Supplementary Figure S2A).
PMID:37403782	PBO:0109446	Further supporting the idea that U6 complex formation is contingent on the presence of all three proteins, we observed a loss of snoZ30 binding to Bmc1 upon knockout of any member of the complex (Supplementary Figure S2A).
PMID:37403782	GO:0030515	We validated the interaction between Bmc1 and sno530 by RNP immunoprecipitation/qPCR and showed that much like snoZ30 and U6, this interaction is dependent on the presence of the assembled Bmc1-Pof8-Thc1 complex (Figure 1A).
PMID:37403782	PBO:0109449	Deletion of snoZ30 and sno530 resulted in a loss of 2′-O-methylation at A41 and A64, respectively, suggesting that sno530 is indeed the A64 U6-modifying snoRNA (Figure 1C, D, Supplementary Figure S3).
PMID:37403782	GO:0016180	(comment: U6)
PMID:37403782	GO:0016180	(comment: U6)
PMID:37403782	GO:0016180	(comment: U6)
PMID:37403782	PBO:0109669	Still, as mean intron retention values indeed showed an increase upon Bmc1 deletion (Figure 5A), we chose several representative intron retention events to validate with semi-quantitative RT-PCR (one of which, intron 1 of pud1, displayed a statistically significant increase upon Bmc1 deletion at 32 ̊C in our RNA Seq dataset).
PMID:37403782	FYPO:0008113	Still, as mean intron retention values indeed showed an increase upon Bmc1 deletion (Figure 5A), we chose several representative intron retention events to validate with semi-quantitative RT-PCR (one of which, intron 1 of pud1, displayed a statistically significant increase upon Bmc1 deletion at 32 ̊C in our RNA Seq dataset).
PMID:37403782	PBO:0112458	(comment: Bmc1 5 capping catalytic activity is not required for promoting 2 -O-methylation of U6)
PMID:37445861	PBO:0093786	(Fig. 2)
PMID:37445861	PBO:0093785	(Fig. 2)
PMID:37445861	PBO:0093786	(Fig. 2)
PMID:37445861	PBO:0112326	(Fig. 5)
PMID:37445861	PBO:0112317	(Fig. 5)
PMID:37445861	PBO:0112326	(Fig. 5)
PMID:37445861	PBO:0112317	(Fig. 5)
PMID:37445861	PBO:0093786	(Fig. S2)
PMID:37445861	PBO:0093785	(Fig. S2)
PMID:37445861	PBO:0093564	(Fig. S3)
PMID:37445861	PBO:0093564	(Fig. S3)
PMID:37445861	PBO:0093564	(Fig. S3)
PMID:37445861	PBO:0093564	(Fig. S3)
PMID:37445861	PBO:0093564	(Fig. S3)
PMID:37445861	PBO:0093564	(Fig. S4)
PMID:37445861	PBO:0093564	(Fig. S4)
PMID:37445861	PBO:0093564	(Fig. S4)
PMID:37445861	PBO:0093564	(Fig. S4)
PMID:37445861	PBO:0093564	(Fig. S4)
PMID:37445861	PBO:0093564	(Fig. S4)
PMID:37445861	PBO:0093564	(Fig. S4)
PMID:37445861	PBO:0093564	(Fig. S4)
PMID:37445861	PBO:0093564	(Fig. S4)
PMID:37445861	FYPO:0000964	(Fig. S4)
PMID:37445861	FYPO:0000964	(Fig. S4)
PMID:37445861	PBO:0093785	(Fig. S2)
PMID:37445861	PBO:0093563	(Fig. S3)
PMID:37445861	PBO:0093563	(Fig. S3)
PMID:37445861	PBO:0093563	(Fig. S3)
PMID:37445861	PBO:0093563	(Fig. S3)
PMID:37445861	PBO:0093563	(Fig. S3)
PMID:37445861	FYPO:0000069	(Fig. S3)
PMID:37445861	FYPO:0000069	(Fig. S3)
PMID:37445861	FYPO:0000069	(Fig. S3)
PMID:37445861	FYPO:0000069	(Fig. S3)
PMID:37445861	FYPO:0000069	(Fig. S3)
PMID:37445861	FYPO:0000069	(Fig. S3)
PMID:37445861	FYPO:0000069	(Fig. S3)
PMID:37445861	FYPO:0000069	(Fig. S3)
PMID:37445861	FYPO:0000069	(Fig. S3)
PMID:37445861	FYPO:0000964	(Fig. S3)
PMID:37445861	FYPO:0000964	(Fig. S3)
PMID:37445861	FYPO:0000964	(Fig. S3)
PMID:37445861	FYPO:0000964	(Fig. S3)
PMID:37445861	PBO:0093786	(Fig. 3)
PMID:37445861	PBO:0093564	(Fig. S3)
PMID:37445861	PBO:0093564	(Fig. S4)
PMID:37445861	PBO:0093786	(Fig. 2)
PMID:37445861	PBO:0093786	(Fig. 2)
PMID:37445861	PBO:0093786	(Fig. 2)
PMID:37445861	PBO:0093786	(Fig. 2)
PMID:37445861	PBO:0093786	(Fig. 2)
PMID:37445861	PBO:0093786	(Fig. 2)
PMID:37445861	PBO:0093786	(Fig. 2)
PMID:37445861	PBO:0093786	(Fig. 2)
PMID:37445861	PBO:0093786	(Fig. 2)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093784	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093784	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093785	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093784	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093784	(Fig. 1)
PMID:37445861	PBO:0093785	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	PBO:0093785	(Fig. 1)
PMID:37445861	PBO:0093785	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093784	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093785	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. 1)
PMID:37445861	PBO:0093785	(Fig. 1)
PMID:37445861	PBO:0093785	(Fig. 1)
PMID:37445861	FYPO:0001986	(Fig. 1)
PMID:37445861	FYPO:0001986	(Fig. 1)
PMID:37445861	FYPO:0001986	(Fig. 1)
PMID:37445861	FYPO:0001986	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	PBO:0093785	(Fig. 2)
PMID:37445861	PBO:0093784	(Fig. 2)
PMID:37445861	PBO:0093784	(Fig. 2)
PMID:37445861	PBO:0093786	(Fig. 3)
PMID:37445861	PBO:0093786	(Fig. 3)
PMID:37445861	PBO:0093786	(Fig. 3)
PMID:37445861	PBO:0112315	(Fig. 4)
PMID:37445861	PBO:0112319	(Fig. 4)
PMID:37445861	PBO:0112320	(Fig. 4)
PMID:37445861	PBO:0112315	(Fig. 4)
PMID:37445861	PBO:0112319	(Fig. 4)
PMID:37445861	PBO:0112320	(Fig. 4)
PMID:37445861	PBO:0112321	(Fig. 4)
PMID:37445861	PBO:0099465	(Fig. 4)
PMID:37445861	FYPO:0001986	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	FYPO:0007035	(Fig. 1)
PMID:37445861	PBO:0112318	(Fig. 5)
PMID:37445861	PBO:0112318	(Fig. 5)
PMID:37445861	PBO:0112318	(Fig. 5)
PMID:37445861	PBO:0112318	(Fig. 5)
PMID:37445861	PBO:0112317	(Fig. 5)
PMID:37445861	PBO:0112317	(Fig. 5)
PMID:37445861	PBO:0112316	(Fig. 4)
PMID:37445861	PBO:0112315	(Fig. 4)
PMID:37445861	PBO:0112315	(Fig. 4)
PMID:37445861	PBO:0112315	(Fig. 4)
PMID:37445861	PBO:0112315	(Fig. 4)
PMID:37445861	PBO:0093786	(Fig. 3)
PMID:37445861	PBO:0093785	(Fig. 3)
PMID:37445861	PBO:0093785	(Fig. 3)
PMID:37445861	PBO:0093785	(Fig. 3)
PMID:37445861	PBO:0093785	(Fig. 3)
PMID:37445861	PBO:0093785	(Fig. 3)
PMID:37445861	PBO:0093785	(Fig. 3)
PMID:37445861	PBO:0093785	(Fig. 3)
PMID:37445861	PBO:0093785	(Fig. 3)
PMID:37445861	PBO:0093786	(Fig. 3)
PMID:37445861	FYPO:0007035	(Fig. 3)
PMID:37445861	FYPO:0007035	(Fig. 3)
PMID:37445861	FYPO:0001986	(Fig. 1)
PMID:37445861	FYPO:0001986	(Fig. 1)
PMID:37445861	FYPO:0001986	(Fig. 1)
PMID:37445861	FYPO:0001986	(Fig. 1)
PMID:37445861	PBO:0099465	(Fig. 4)
PMID:37445861	PBO:0037349	(Fig. 4)
PMID:37445861	PBO:0099465	(Fig. 4)
PMID:37445861	PBO:0112319	(Fig. 4)
PMID:37445861	PBO:0112319	(Fig. 4)
PMID:37445861	PBO:0112322	(Fig. 4)
PMID:37445861	PBO:0112316	(Fig. 4)
PMID:37445861	PBO:0112316	(Fig. 4)
PMID:37445861	PBO:0112323	(Fig. 4)
PMID:37445861	FYPO:0001986	(Fig. 1)
PMID:37445861	FYPO:0001986	(Fig. 1)
PMID:37445861	FYPO:0001986	(Fig. 1)
PMID:37445861	PBO:0093786	(Fig. S2)
PMID:37445861	PBO:0093785	(Fig. S2)
PMID:37445861	PBO:0093786	(Fig. S2)
PMID:37445861	PBO:0093786	(Fig. S2)
PMID:37445861	PBO:0093785	(Fig. S2)
PMID:37445861	PBO:0093785	(Fig. 2)
PMID:37445861	PBO:0093786	(Fig. 2)
PMID:37445861	PBO:0093786	(Fig. 2)
PMID:37445861	PBO:0093786	(Fig. 2)
PMID:37445861	PBO:0093786	(Fig. 2)
PMID:37445861	PBO:0093786	(Fig. 2)
PMID:37445861	PBO:0112316	(Fig. 4)
PMID:37445861	PBO:0112324	(Fig. 4)
PMID:37445861	PBO:0112325	(Fig. 5)
PMID:37445861	PBO:0112325	(Fig. 5)
PMID:37445861	PBO:0095977	(Fig. 5)
PMID:37446379	FYPO:0008363	(Figure 7b) the absence of Mas5 also blocked the accumulation of Hsp104-GFP into NuRs (Figure 7b)
PMID:37459529	PBO:0111389	Deletion of the active center loop compromised the HDAC activity of Clr6S (Fig. 6G), consistent with a role of the loop in catalytic activity, although a secondary effect, due to perturbation of the protein structure could not be excluded.
PMID:37459529	GO:0060090	Thus, Cph2 interacts with all the other subunits except Prw1, whose association with the complex occurs only through the Pst2-CTD (Fig. 4C).
PMID:37459529	GO:0060090	Pst2 evidently serves as a structural platform, bringing together almost all the other subunits of the complex.
PMID:37459529	GO:0032221	Alp13b is connected to the complex by both Cph1 and Cph2 (Figs. 2C and 3A)
PMID:37459529	GO:0180033	(comment: assayed complex)
PMID:37459529	GO:0140937	(comment: assayed complex)
PMID:37459529	GO:0034739	(comment: assayed complex)
PMID:37459529	GO:0032221	All six subunits of the Clr6S complex are seen in the map (Fig. 2 B and C and SI Appendix, Table S1). Unexpectedly, the structure also reveals two copies of Alp13 (hereafter referred to as Alp13a and Alp13b) (Fig. 2C)
PMID:37459529	GO:0032221	The structure shows that Pst2, Clr6, and Prw1, a WD40-containing subunit, form a subcomplex, within which Pst2 associates with the catalytic subunit Clr6, as well as interacting with Prw1 (Fig. 2C)
PMID:37459529	GO:0032221	The structure shows that Pst2, Clr6, and Prw1, a WD40-containing subunit, form a subcomplex, within which Pst2 associates with the catalytic subunit Clr6, as well as interacting with Prw1 (Fig. 2C)
PMID:37459529	GO:0032221	Unexpectedly, the structure also reveals two copies of Alp13 (hereafter referred to as Alp13a and Alp13b) (Fig. 2C)
PMID:37459529	GO:0180032	(comment: assayed complex)
PMID:37459529	GO:0032221	Alp13b is connected to the complex by both Cph1 and Cph2 (Figs. 2C and 3A)
PMID:37531259	PBO:0109537	(Figure 3A)
PMID:37531259	PBO:0109539	(Figure 1C)
PMID:37531259	GO:0008289	(comment: vw: I think we can conclude this from the EXP, especially as we know that myo1 binds phopshilipids in other species) Addition of Ank1 resulted in a reduction in the amount of co-pelleting of the Myo1(1-964)-FLAG-Cam1-Cam2 complex with liposomes (Fig. 2F). We therefore conclude that Ank1 directly binds and inhibits Myo1 membrane binding, supporting our model.
PMID:37531259	PBO:0109541	Given the AF model and the above results, we hypothesized that Ank1 In contrast, in myo1-mNG fim1-mCherry cells overproducing Ank1, while Fim1-mCherry was at patches, almost all Myo1-mNG was cytoplasmic (Fig. 3A). These data support our model that Ank1 blocks Myo1 membrane association and normally sequesters the bulk of Myo1 in the cytoplasm.precludes Myo1 membrane binding and sequesters the myosin-1 complex in the cytoplasm (Fig. 2F).Addition of Ank1 resulted in a reduction in the amount of co-pelleting of the Myo1(1-964)-FLAG-Cam1-Cam2 complex with liposomes (Fig. 2F). We therefore conclude that Ank1 directly binds and inhibits Myo1 membrane binding, supporting our model.
PMID:37531259	PBO:0109540	(Figure 1C)
PMID:37531259	PBO:0109538	(Figure 1E)
PMID:37531259	PBO:0109538	(Figure 1E)
PMID:37531259	FYPO:0004085	(Figure S1D)
PMID:37531259	FYPO:0004085	(Figure S1D)
PMID:37531259	FYPO:0004085	(Figure S1D)
PMID:37531259	FYPO:0001357	(Figure S1D) (comment: vw: same pathway)
PMID:37531259	GO:0051285	(Figure 1C)
PMID:37531259	FYPO:0004085	(Figure S1D)
PMID:37531259	GO:0005737	(Figure 1F)
PMID:37531259	PBO:0109524	(Figure 3E)
PMID:37531259	PBO:0109524	(Figure 3E)
PMID:37531259	PBO:0109534	(Figure 3C)
PMID:37531259	PBO:0109535	(Figure 3B) Furthermore, in cells overproducing ank1+, ~10% of Fim1-mCherry patches internalized compared to ~95% of Fim1-mCherry patches internalized in the control cells (Fig. 3B)
PMID:37531259	PBO:0109536	(Figure 3A) in myo1-mNG fim1-mCherry cells overproducing Ank1, while Fim1-mCherry was at patches, almost all Myo1-mNG was cytoplasmic (Fig. 3A).
PMID:37531259	GO:0051285	(Figure 1C)
PMID:37531259	PBO:0109524	(Figure 1D)
PMID:37531259	PBO:0109525	(Figure 1C)
PMID:37531259	PBO:0109526	(Figure 1C)
PMID:37531259	PBO:0109527	(Figure 1C)
PMID:37531259	PBO:0109528	(Figure 1C)
PMID:37531259	FYPO:0001366	(Figure 1C)
PMID:37531259	PBO:0109529	(Figure S1C)
PMID:37531259	FYPO:0000744	(Figure S1C)
PMID:37531259	PBO:0109530	(Figure S1A)
PMID:37531259	PBO:0109531	(Figure S1B)
PMID:37531259	PBO:0109532	(Fig. 1, 1B, 2D)
PMID:37531259	GO:0061645	(Figure 1C,F)
PMID:37531259	PBO:0109533	(Figure 3C)
PMID:37540145	GO:0000266	Thus, our data indicate that Mdi1 plays a conserved role as a profission factor that is not required for Dnm1 recruitment but is required to facilitate the completion of mitochondrial division. Fig 4
PMID:37540145	PBO:0109593	(Figure 4G)
PMID:37540145	PBO:0109719	(Figure 4F) (comment: mitochondrial net-like morphology)
PMID:37540145	PBO:0109720	(Figure 4F) (comment: mitochondrial net-like morphology)
PMID:37540145	PBO:0109596	(Figure 4G)
PMID:37540145	PBO:0109587	loss of Mdi1 did not impact Dnm1 recruitment to mitochondria and Dnm1 foci appeared associated with the hyperfused net structures (Fig. 4 F, arrows).
PMID:37550452	PBO:0108475	(Figure 6)
PMID:37550452	PBO:0109824	Extended Data Figure 9e
PMID:37550452	PBO:0109823	(Figure 6)
PMID:37550452	PBO:0093561	(Figure 5)
PMID:37550452	PBO:0108473	(Figure 6)
PMID:37550452	PBO:0093561	(Figure 5)
PMID:37550452	PBO:0108474	(Figure 6)
PMID:37550452	FYPO:0002061	(Figure 5)
PMID:37553386	PBO:0112256	(Fig. 5A)
PMID:37553386	PBO:0102947	(Fig. 5A)
PMID:37553386	PBO:0102947	(Fig. 5A)
PMID:37553386	FYPO:0001030	(Fig. 5A)
PMID:37553386	FYPO:0001030	(Fig. 5A)
PMID:37553386	PBO:0112261	(Fig. 3G)
PMID:37553386	FYPO:0001030	(Fig. 5A)
PMID:37553386	PBO:0112258	(Fig. S2G and H)
PMID:37553386	PBO:0112260	(Fig. 2C)
PMID:37553386	PBO:0112259	(Fig. 2C)
PMID:37553386	PBO:0112258	(Fig. S2G and H)
PMID:37553386	PBO:0112257	(Fig. 1G)
PMID:37553386	PBO:0112257	(Fig. 1G)
PMID:37553386	FYPO:0000355	(Fig. S2D)
PMID:37553386	FYPO:0001030	(Fig. 1F)
PMID:37553386	FYPO:0001030	(Fig. 1F)
PMID:37553386	PBO:0112256	(Fig. 1F)
PMID:37553386	FYPO:0001357	(Fig. 1F)
PMID:37553386	FYPO:0007448	(Fig. 1B and C)
PMID:37553386	PBO:0112254	(Fig. 1B and C)
PMID:37553386	PBO:0112255	(Fig. 1B and C)
PMID:37553386	PBO:0112253	(Fig. 1B and C)
PMID:37553386	PBO:0112254	(Fig. 1B and C)
PMID:37553386	PBO:0112253	(Fig. 1B and C)
PMID:37553386	PBO:0112252	(Fig. 6)
PMID:37553386	PBO:0112251	(Fig. 1B)
PMID:37553386	PBO:0112250	Assayed using S. japonicus yop1 in vitro. Fig. 4
PMID:37553386	FYPO:0000381	(Fig. 1D and E)
PMID:37553386	PBO:0112248	Assayed using S. japonicus rop1 in vitro. Fig. 4
PMID:37553386	FYPO:0001357	(Fig. 1F)
PMID:37553386	PBO:0112256	(Fig. 1F)
PMID:37553386	PBO:0112256	(Fig. 1F)
PMID:37553386	FYPO:0001357	(Fig. 1F)
PMID:37553386	FYPO:0001357	(Fig. 1F)
PMID:37553386	FYPO:0001357	(Fig. 1F)
PMID:37553386	PBO:0112252	(Fig. 6)
PMID:37553386	PBO:0112265	(Fig. 5B)
PMID:37553386	PBO:0112264	(Fig. 5B)
PMID:37553386	PBO:0112263	(Fig. 5B)
PMID:37553386	PBO:0112263	(Fig. 5B)
PMID:37553386	PBO:0112256	(Fig. 5A)
PMID:37553386	PBO:0112262	(Fig. 5A)
PMID:37572670	PBO:0111043	We observed a small, but reproducible, stress-induced decrease in Wis1DD mobility in these cells, corroborating that Wis1 undergoes a stressinduced phosphorylation on different sites from those phosphorylated by the MAP3K (Figures 4A, S5A, S4A, S4B, and S4F).
PMID:37572670	FYPO:0003481	Next, we co-expressed the Sty1-Tpx1C48S fusion with a Wis1AA mutant, in which the MAP3K-phosphorylated residues are substituted with alanine. Wis1AA cells are significantly elongated, reflecting the mitotic delay associated with Sty1 hypophosphorylation (Figures 4B, 4C, and S6A).50
PMID:37572670	FYPO:0003481	Next, we co-expressed the Sty1-Tpx1C48S fusion with a Wis1AA mutant, in which the MAP3K-phosphorylated residues are substituted with alanine. Wis1AA cells are significantly elongated, reflecting the mitotic delay associated with Sty1 hypophosphorylation (Figures 4B, 4C, and S6A).50
PMID:37572670	PBO:0111045	Although expression of Sty-Tpx1C48S stimulated a bigger increase in Sty1 activity in cells expressing wild-type Wis1, expression of Sty1-Tpx1C48S also increased Sty1 phosphorylation and partially rescued the cell-cycle defect of Wis1AA cells (Figures 4B and 4C)
PMID:37572670	PBO:0111044	Although, both Wis1M395G and Wis1M395A were expressed at wild-type levels, Sty1 phosphorylation was very low and minimally increased even in response to 6 mM H2O2 in these cells (Figure 4D).
PMID:37572670	PBO:0111044	Although, both Wis1M395G and Wis1M395A were expressed at wild-type levels, Sty1 phosphorylation was very low and minimally increased even in response to 6 mM H2O2 in these cells (Figure 4D).
PMID:37572670	PBO:0111043	Strikingly, the stress-induced phosphorylation of Wis1M395G and Wis1M395A was also compromised, strongly suggesting that Wis1 kinase activity was required for the stress-induced phosphorylation and activation of Wis1 (Figure 4D).
PMID:37572670	PBO:0111043	Strikingly, the stress-induced phosphorylation of Wis1M395G and Wis1M395A was also compromised, strongly suggesting that Wis1 kinase activity was required for the stress-induced phosphorylation and activation of Wis1 (Figure 4D).
PMID:37572670	FYPO:0003481	Dmcs4 mutant cells are delayed in entry to mitosis, reaching a significantly longer size than wild-type cells before dividing (Figure 5A).45,47,48
PMID:37572670	PBO:0111035	Sty1-Tpx1 expression stimulated similar levels of constitutive Wis1 phosphorylation in Dmcs4 mutant as in wild-type (mcs4+) cells (Figure 5B). Accordingly, there were similar levels of Sty1 phosphorylati
PMID:37572670	GO:0005078	Sty1-Tpx1 complexes provide a scaffold for Wis1
PMID:37572670	FYPO:0002059	Moreover, when we crossed strains expressing Sty1-Tpx1 fusion and Dpyp1 mutant alleles, we observed a very strong synthetic lethal interaction, with 95% of spores with a sty1-tpx1 Dpyp1 genotype failing to give rise to a colony (Figure 2I and not shown). This strongly suggests that sty1- tpx1 and Dpyp1 alleles act independently to increase Sty1 phosphorylation, thus increasing it to lethal levels when co-expressed. Indeed, analysis of colonies bearing markers of both alleles revealed that surviving cells had completely eliminated Sty1-Tpx1 expression and activity (Figures 2J and 2K and not shown).
PMID:37572670	FYPO:0003481	Our analysis revealed that Sty15CS-mutant-expressing cells were longer at the point of division than wild-type cells, strongly suggesting that Sty15CS’s promitotic function was compromised (Figures S1D and S1E).
PMID:37572670	FYPO:0001122	Indeed, consistent with the requirement of Wis1-dependent phosphorylation of Sty1 for timely entry into mitosis, cells expressing Wis1M395G or Wis1M395A were elongated (Figure S6B).
PMID:37572670	FYPO:0006822	This revealed that Sty1- Tpx1- and Sty1-Tpx1C48S-expressing cells both divided at a significantly smaller size than wild-type cells (Figure 1F).
PMID:37572670	PBO:0111034	(Figure 1) Strikingly, Sty1 phosphorylation was increased in cells expressing either Sty1-Tpx1 or Sty1-Tpx1C48S (Figure 1D)
PMID:37572670	FYPO:0001122	Indeed, consistent with the requirement of Wis1-dependent phosphorylation of Sty1 for timely entry into mitosis, cells expressing Wis1M395G or Wis1M395A were elongated (Figure S6B).
PMID:37572670	FYPO:0002059	Moreover, when we crossed strains expressing Sty1-Tpx1 fusion and Dpyp1 mutant alleles, we observed a very strong synthetic lethal interaction, with 95% of spores with a sty1-tpx1 Dpyp1 genotype failing to give rise to a colony (Figure 2I and not shown). This strongly suggests that sty1- tpx1 and Dpyp1 alleles act independently to increase Sty1 phosphorylation, thus increasing it to lethal levels when co-expressed. Indeed, analysis of colonies bearing markers of both alleles revealed that surviving cells had completely eliminated Sty1-Tpx1 expression and activity (Figures 2J and 2K and not shown).
PMID:37572670	PBO:0111035	(Figure 3) Sty1-Tpx1 fusion proteins, Wis1 was hyperphosphorylated to less electrophoretically mobile forms even in the absence of stress (Figures 3A and 3D).
PMID:37572670	FYPO:0000544	Sty1-Tpx1 disulfide formation abrogated (Figure S1C).
PMID:37572670	PBO:0111036	Consistent with lower Sty1 activity, Sty15CS-expressing cells contained less Pyp1 than wild-type cells (Figure S1F). This likely explains the slightly elevated phosphorylation of Sty15CS (Figure S1G)
PMID:37572670	PBO:0093578	Sty15CS-expressing cells were able to adapt to osmotic stress but were less tolerant than wild-type cells to higher levels of H2O2 (Figure 1B).
PMID:37572670	FYPO:0005947	Sty15CS-expressing cells were able to adapt to osmotic stress but were less tolerant than wild-type cells to higher levels of H2O2 (Figure 1B).
PMID:37572670	PBO:0111037	Crucially, both Sty1-Tpx1 fusions were expressed at similar levels to wild-type Sty1 and supported growth under stress conditions, confirming retention of Sty1 function (Figures 1B and 1D). By contrast, the oxidative stress sensitivity and lower Pyp1 levels in cells expressing a Sty15CS-Tpx1 fusion protein, provided further evidence that cysteines in Sty1 are required for Sty1 function independently from forming disulfide-bonded complexes with Tpx1 (Figures 1B and S1F).39
PMID:37572670	PBO:0111034	(Figure 1) Strikingly, Sty1 phosphorylation was increased in cells expressing either Sty1-Tpx1 or Sty1-Tpx1C48S (Figure 1D)
PMID:37572670	FYPO:0006822	This revealed that Sty1- Tpx1- and Sty1-Tpx1C48S-expressing cells both divided at a significantly smaller size than wild-type cells (Figure 1F).
PMID:37572670	PBO:0111038	By contrast, cells expressing Sty1-Tpx1C48S contained substantially increased levels of lower mobility and phosphorylated Pyp2 (p-Pyp2), even prior to addition of H2O2. Together these data strongly support the conclusion that the Sty1-Tpx1 and Sty1-Tpx1C48S fusion proteins are constitutively hyperactive compared with wild-type Sty1 (Figures 1F and 1G).
PMID:37572670	FYPO:0009007	Hence, the lower viability of cells co-expressing sty1-tpx1 and wis1DD suggested a synthetic negative interaction, with both alleles acting independently to increase Sty1 phosphorylation to lethal levels.
PMID:37572670	FYPO:0001122	Indeed, our examination indicated that ‘‘sty1-tpx1 wis1DD’’ strains, which genotypically bore both alleles, had adapted to the deleterious effect of hyperactivated Sty1 by lowering Sty1 expression to such an extent that they exhibited the long cell phenotype associated with its loss (Figures S3A and S3B).
PMID:37572670	PBO:0111039	As expected, Sty1 phosphorylation was increased in Dpyp1 mutant cells, confirming the importance of this phosphatase in maintaining low levels of Sty1 activity (Figure 2A)
PMID:37572670	PBO:0111040	By contrast, overexpression of Tpx1 increased H2O2-induced Sty1 phosphorylation in wild-type cells and also restored some H2O2-inducibility to Sty1 phosphorylation in Dpyp2 cells (Figures 2A and S3E).
PMID:37572670	PBO:0111041	By contrast, overexpression of Tpx1 increased H2O2-induced Sty1 phosphorylation in wild-type cells and also restored some H2O2-inducibility to Sty1 phosphorylation in Dpyp2 cells (Figures 2A and S3E).
PMID:37572670	PBO:0111041	Consistent with Pyp1 oxidation providing a similar mechanism to reversibly inhibit Pyp1 and activate Sty1, there was a much smaller H2O2-induced increase in Sty1 phosphorylation in Dtrx1 mutant cells, where H2O2-induced Pyp1 disulfides were not detected (Figures 2D and 2F).
PMID:37572670	PBO:0095350	(comment: CHECK Tpx1 is required for H2O2-induced activation of Sty1, over a range of concentrations up to 10 mM H2O2.31)
PMID:37572670	PBO:0111042	Indeed, our analysis of Dtpx1 mutant cells indicated that Tpx1 was important for maximal Wis1 phosphorylation (pppWis1) in response to 6 mM H2O2 (Figures 3C, S4E, and S4F).
PMID:37572670	PBO:0111044	Significantly, this stress-induced increase in Wis1DD phosphorylation was mirrored by stress-induced increases in Sty1 phosphorylation, strongly suggesting that it increases Wis1 activity (Figure 4A).
PMID:37590302	FYPO:0007194	(Figure 1)
PMID:37590302	FYPO:0003810	(Figure 1)
PMID:37590302	FYPO:0007197	(Figure 1F and 1G) Analysis by live-cell microscopy further showed that both fission and fusion frequencies increased significantly in cells lacking Yta4
PMID:37590302	FYPO:0008122	(Figure 1F and 1G) Analysis by live-cell microscopy further showed that both fission and fusion frequencies increased significantly in cells lacking Yta4
PMID:37590302	PBO:0109729	Hence, these results show the characteristic property of Yta4 in reducing the affinity of Dnm1 for GTP and in inhibiting Dnm1 assembly.
PMID:37590302	FYPO:0001531	To reduce the complexity in analyzing Dnm1 GTPase activity, we performed colorimetric assays by using the assembly-defective version of Dnm1 (i.e., Dnm1(G380D), see S6A Fig). Interestingly, Dnm1(G380D) still exhibited a GTPase activity but has a very low rate of GTP hydrolysis (Km = 85.00 μM, Vmax = 1.02 μM/min, versus the control Dnm1(WT): Km = 126.59 μM, Vmax = 4.82 μM/min) (S8 Fig).
PMID:37590302	FYPO:0000897	the expression of Yta4(WT), Yta4(AA), or Yta4(EQ) from the yta4 promoter restored Dnm1-associated mitochondrial fission to the WT level in yta4∆ cells (S3D Fig)
PMID:37590302	FYPO:0000897	the expression of Yta4(WT), Yta4(AA), or Yta4(EQ) from the yta4 promoter restored Dnm1-associated mitochondrial fission to the WT level in yta4∆ cells (S3D Fig)
PMID:37590302	PBO:0109728	showed that the delocalized GFP-Fis1 appeared to be present in the cytoplasm of Yta4-overexpressing cells, while GFP-Fis1 in Yta4(AA)-overexpressing or Yta4 (EQ)-overexpressing cells was still present on mitochondria, which were clearly separated from the ER (S1D and S2 Figs).
PMID:37590302	PBO:0109728	showed that the delocalized GFP-Fis1 appeared to be present in the cytoplasm of Yta4-overexpressing cells, while GFP-Fis1 in Yta4(AA)-overexpressing or Yta4 (EQ)-overexpressing cells was still present on mitochondria, which were clearly separated from the ER (S1D and S2 Figs).
PMID:37590302	PBO:0109727	As shown in Figs 4D and S1C, overexpression of WT Yta4 impaired the formation of Dnm1 foci on mitochondria but did not change the tubular mitochondrial morphology.
PMID:37590302	FYPO:0000895	Yta4(EQ) impaired the formation of Dnm1 foci on mitochondria but unexpectedly caused mitochondria to aggregate (Figs 4D and S1C)
PMID:37590302	PBO:0109726	Quantification showed that the expression levels of endogenous Dnm1 were comparable in WT and yta4Δ cells (Fig 3B)
PMID:37590302	FYPO:0007197	(Figure 1F and 1G) Analysis by live-cell microscopy further showed that both fission and fusion frequencies increased significantly in cells lacking Yta4
PMID:37615341	PBO:0112328	(Fig. 3C and D)
PMID:37615341	FYPO:0005353	(Fig. 4)
PMID:37615341	FYPO:0005353	(Fig. 4)
PMID:37615341	FYPO:0005353	(Fig. 4)
PMID:37615341	FYPO:0006603	(Fig. 1)
PMID:37615341	FYPO:0006603	expression of an intron-less rtf1 gene that encodes the same additional 15 amino acids between residues 202-203 (Rtf1 intron2NE) does not provoke increased replication slippage downstream of RTS1 (Figure 4—Figure supplement 3), indicating that this protein is indeed dysfunctional.
PMID:37615341	FYPO:0001357	(Fig. 2-S1A)
PMID:37615341	FYPO:0000963	(Fig. 2-S1A)
PMID:37615341	FYPO:0001357	(Fig. 2-S1A)
PMID:37615341	FYPO:0001357	(Fig. 2-S1A)
PMID:37615341	FYPO:0000963	(Fig. 2-S1A)
PMID:37615341	FYPO:0000963	(Fig. 2-S1A)
PMID:37615341	PBO:0093617	(Fig. 2-S1A)
PMID:37615341	PBO:0093617	(Fig. 2-S1A)
PMID:37615341	FYPO:0000957	(Fig. 2-S1A)
PMID:37615341	PBO:0112327	This further suggests that Mud1 is not playing the same role in regulating Rtf2 in S. pombe as has been observed for DDI1/2 in human cells. Fig. 2-S1B
PMID:37637271	FYPO:0002061	(Figure 1D)
PMID:37637271	FYPO:0000964	(Figure 1H)
PMID:37637271	FYPO:0001355	(Figure 1E)
PMID:37637271	FYPO:0001355	(Figure 1E)
PMID:37637271	FYPO:0001355	(Figure 1E)
PMID:37637271	FYPO:0001355	(Figure 1E)
PMID:37637271	FYPO:0001355	(Figure 1E)
PMID:37637271	FYPO:0001355	(Figure 1E)
PMID:37637271	FYPO:0001355	(Figure 1G)
PMID:37637271	FYPO:0001355	(Figure 1G)
PMID:37637271	FYPO:0001235	(Figure 1E)
PMID:37637271	FYPO:0001235	(Figure 1E)
PMID:37637271	FYPO:0000964	(Figure 1H)
PMID:37637271	PBO:0093563	(Figure 1H)
PMID:37637271	PBO:0093563	(Figure 1H)
PMID:37637271	FYPO:0002061	(Figure 1D)
PMID:37694715	PBO:0110252	The Bqt4 fragment containing the helix domain and the adjacent intrinsically disordered sequence (Bqt4C369-432) reproduced the behavior of full-length Bqt4 (Fig. 1A), that is, localization to the NE and responses to BZ, both in the presence and absence of Bqt3 (Fig. 6A, Bqt4C369-432).
PMID:37694715	PBO:0110248	To confirm this result, we measured protein levels by western blotting, which consistently showed an increase in GFP-Bqt4 protein levels in these strains upon proteasomal inhibition by BZ Fig. 1B
PMID:37694715	MOD:01148	Ubiquitinated forms of Bqt4 were detected in bqt3Δ cells and were enriched in both bqt3+ and bqt3Δ cells when proteasomal activity was inhibited (Fig. 1E), suggesting that Bqt4 was targeted to the proteasome by polyubiquitin modification.
PMID:37694715	PBO:0110249	Ubiquitinated forms of Bqt4 were detected in bqt3Δ cells and were enriched in both bqt3+ and bqt3Δ cells when proteasomal activity was inhibited (Fig. 1E), suggesting that Bqt4 was targeted to the proteasome by polyubiquitin modification.
PMID:37694715	PBO:0110250	We constructed mutants of E3 ligases and their components that have been suggested to localize to or function in the ER and nucleus, namely ......... The mutants tested showed no detectable increase in fluorescence, except for the hul5Δ mutant (Fig. S2)
PMID:37694715	PBO:0110250	We constructed mutants of E3 ligases and their components that have been suggested to localize to or function in the ER and nucleus, namely ......... The mutants tested showed no detectable increase in fluorescence, except for the hul5Δ mutant (Fig. S2)
PMID:37694715	PBO:0110250	We constructed mutants of E3 ligases and their components that have been suggested to localize to or function in the ER and nucleus, namely ......... The mutants tested showed no detectable increase in fluorescence, except for the hul5Δ mutant (Fig. S2)
PMID:37694715	PBO:0110250	We constructed mutants of E3 ligases and their components that have been suggested to localize to or function in the ER and nucleus, namely ......... The mutants tested showed no detectable increase in fluorescence, except for the hul5Δ mutant (Fig. S2)
PMID:37694715	PBO:0110250	We constructed mutants of E3 ligases and their components that have been suggested to localize to or function in the ER and nucleus, namely ......... The mutants tested showed no detectable increase in fluorescence, except for the hul5Δ mutant (Fig. S2)
PMID:37694715	PBO:0110250	We constructed mutants of E3 ligases and their components that have been suggested to localize to or function in the ER and nucleus, namely ......... The mutants tested showed no detectable increase in fluorescence, except for the hul5Δ mutant (Fig. S2)
PMID:37694715	PBO:0110250	We constructed mutants of E3 ligases and their components that have been suggested to localize to or function in the ER and nucleus, namely ......... The mutants tested showed no detectable increase in fluorescence, except for the hul5Δ mutant (Fig. S2)
PMID:37694715	GO:0016020	(comment: Bqt4 is an integral membrane protein)
PMID:37694715	PBO:0110251	The Bqt4 fragment containing the helix domain and the adjacent intrinsically disordered sequence (Bqt4C369-432) reproduced the behavior of full-length Bqt4 (Fig. 1A), that is, localization to the NE and responses to BZ, both in the presence and absence of Bqt3 (Fig. 6A, Bqt4C369-432).
PMID:37694715	PBO:0110253	The helix domain alone (Bqt4C394-432) showed weaker localization to the NE and was somewhat diffused to the membrane compartments in the cytoplasm; (Fig. 6A, Bqt4C394-432)
PMID:37694715	PBO:0110252	nevertheless, this fragment was degraded in the absence of Bqt3 and its levels increased with BZ treatment (Fig. 6A, Bqt4C394-432) These results indicate that the C-terminal fragment containing residues 369-432 was necessary and sufficient for the NE localization of Bqt4, and its truncation successively reduced NE localization. These results also indicate that the C-terminal TMD of Bqt4 is sufficient for its proteasome-mediated degradation.
PMID:37694715	PBO:0110254	The TMD alone (Bqt4C414-432) showed even weaker localization at the NE with diffusion to the cytoplasm, but showed the same responses, that is, degradation in the absence of Bqt3 and increased levels upon BZ treatment (Fig. 6A, Bqt4C414-432).
PMID:37694715	PBO:0110252	The TMD alone (Bqt4C414-432) showed even weaker localization at the NE with diffusion to the cytoplasm, but showed the same responses, that is, degradation in the absence of Bqt3 and increased levels upon BZ treatment (Fig. 6A, Bqt4C414-432).
PMID:37694715	PBO:0110252	The fragment Bqt4C369-425 lost its dependency on Bqt3 for degradation and exhibited similar behaviors in the presence or absence of Bqt3 (Fig. 6A, Bqt4C369-425):
PMID:37694715	PBO:0110252	The fragment Bqt4C369-425 lost its dependency on Bqt3 for degradation and exhibited similar behaviors in the presence or absence of Bqt3 (Fig. 6A, Bqt4C369-425):
PMID:37694715	PBO:0110255	The results of the yeast-two-hybrid assay showed that the fragments lacking the last seven residues did not bind to Bqt3 (Fig. 6B).
PMID:37694715	FYPO:0000769	To ascertain whether this abnormal phenotype was caused by an accumulation of Bqt4, we overexpressed GFP-Bqt4 under the nmt1 promoter using the chemical compound YAM2 to control the expression level. YAM2 suppresses nmt1 promoter activity depending on its concentration (Nakamura et al., 2011). Overexpression of GFP-Bqt4 reproduced the nuclear-deformed morphology (Fig. 7B)
PMID:37694715	GO:0005637	These results are consistent with previous studies that showed that Doa10 partially localizes to the INM and is involved in the degradation of certain nuclear and INM substrates, whereas Hrd1 is found exclusively in the ER (Deng and Hochstrasser, 2006; Boban et al., 2014).
PMID:37694715	PBO:0093554	(Fig. 5B)
PMID:37694715	PBO:0110248	We confirmed it by microscopy as well. Fig 3A and B. Deletion of doa10+ partially restored GFP-Bqt4 levels in the absence of Bqt3, whereas deletion of hrd1+ did not (Fig. 3A,B, comparing hrd1Δ to doa10Δ)
PMID:37694715	PBO:0110248	We confirmed it by microscopy as well. Fig 3C and D. We also measured the amount of GFP-Bqt4 in mutants lacking Ubc6 and Ubc7, which are E2 ubiquitin-conjugating enzymes associated with Doa10 (Swanson et al., 2001). We found that GFP-Bqt4 levels increased to some extent in ubc6Δ and ubc7Δ single and ubc6Δ ubc7Δ double mutants (Fig. 3C,D).
PMID:37694715	PBO:0110248	We confirmed it by microscopy as well. Fig 3C and D. We also measured the amount of GFP-Bqt4 in mutants lacking Ubc6 and Ubc7, which are E2 ubiquitin-conjugating enzymes associated with Doa10 (Swanson et al., 2001). We found that GFP-Bqt4 levels increased to some extent in ubc6Δ and ubc7Δ single and ubc6Δ ubc7Δ double mutants (Fig. 3C,D).
PMID:37694715	PBO:0110248	(Fig. 5C and D)
PMID:37694715	PBO:0110248	We confirmed it by microscopy as well. Fig 2A and B. We found that GFP-Bqt4 degradation was suppressed in cut8-563 cells shifted to the nonpermissive temperature of 36°C (Fig. 2A,B).
PMID:37694715	PBO:0110248	We confirmed it by microscopy as well. Fig 1C and D.
PMID:37694715	PBO:0110248	(Fig. S1)
PMID:37694715	PBO:0110248	GFP-Bqt4 fluorescence in the nuclei of both bqt3+ and bqt3Δ cells was elevated (Fig. 1A)
PMID:37723847	FYPO:0002061	(Figure 3b) (comment: tetrad analysis)
PMID:37723847	PBO:0110118	Localizations of Pkd2ΔN170, Pkd2ΔC577, or Pkd2TM were identical to full length Pkd2 (Figures 2b and S2A).
PMID:37723847	PBO:0110120	whereas C-terminus of Pkd2 (Pkd2C) displayed a uniform cytoplasmic pattern (Figures 2b and S2A).
PMID:37723847	PBO:0110118	Localizations of Pkd2ΔN170, Pkd2ΔC577, or Pkd2TM were identical to full length Pkd2 (Figures 2b and S2A).
PMID:37723847	PBO:0110118	Localizations of Pkd2ΔN170, Pkd2ΔC577, or Pkd2TM were identical to full length Pkd2 (Figures 2b and S2A).
PMID:37723847	FYPO:0002061	Overexpression of either construct inhibited the growth like full length (Figure 1d), indicating that each of them is capable of inducing cytotoxicity upon overexpression.
PMID:37723847	FYPO:0002061	Overexpression of either construct inhibited the growth like full length (Figure 1d), indicating that each of them is capable of inducing cytotoxicity upon overexpression.
PMID:37723847	GO:0000935	localized to the septum and the plasma membrane, especially enriched at cell tips (Figure 2d).
PMID:37723847	GO:0031520	localized to the septum and the plasma membrane, especially enriched at cell tips (Figure 2d).
PMID:37723847	FYPO:0002061	Interestingly, the internal transmembrane region was sufficient to induce both CDRE activation and growth inhibition (Figure 1a,d).
PMID:37723847	FYPO:0002061	Although the CDRE signal is disappeared (Figure S1B), the cells did not grow in inducible condition in prz1 deletion background (Figure 1b), suggesting that the activation of calcium signaling and the cytotoxicity induced by overexpression of pkd2+ are independent.
PMID:37723847	FYPO:0002061	In accordance with previous observation, the colony did not form under the inducible condition of pkd2+ overexpression (Figure 1b).
PMID:37723847	PBO:0096587	Although C-terminal deleted cells (mCh-pkd2ΔC) did not affect to the growth under the normal condition, the strain was hypersensitive to CaCl2 (Figure 3c)
PMID:37723847	FYPO:0001252	Although C-terminal deleted cells (mCh-pkd2ΔC) did not affect to the growth under the normal condition, the strain was hypersensitive to CaCl2 (Figure 3c)
PMID:37723847	GO:0005783	full length of Pkd2 (GFP-Pkd2) colocalized with Pmr1, a marker for the ER (Nakazawa et al., 2019)
PMID:37723847	PBO:0110119	N-terminus of Pkd2 (Pkd2N) localized to the cytoplasm and slightly to the ER
PMID:37723847	FYPO:0002060	(Figure 3b) (comment: tetrad analysis)
PMID:37746062	PBO:0110025	(Figure 1G-H)
PMID:37746062	PBO:0110026	(Figure 1G-H)
PMID:37746062	PBO:0110026	(Figure 1G-H)
PMID:37746062	PBO:0110026	(Figure 1G-H)
PMID:37772819	PBO:0108800	Table S3
PMID:37772819	FYPO:0002061	(Fig. 7)
PMID:37772819	FYPO:0002061	(Fig. 7)
PMID:37772819	FYPO:0001357	(Fig. 7)
PMID:37772819	FYPO:0001357	(Fig. 7)
PMID:37772819	FYPO:0001357	(Fig. 7)
PMID:37772819	FYPO:0001357	(Fig. 7)
PMID:37772819	FYPO:0001357	(Fig. 7)
PMID:37772819	FYPO:0001357	(Fig. 8)
PMID:37772819	FYPO:0001357	(Fig. 8)
PMID:37772819	FYPO:0001357	(Fig. 8)
PMID:37772819	FYPO:0001357	(Fig. 8)
PMID:37772819	FYPO:0001357	(Fig. 8)
PMID:37772819	FYPO:0000080	(Fig. 8)
PMID:37772819	FYPO:0000080	(Fig. 9)
PMID:37772819	FYPO:0001357	(Fig. 9)
PMID:37772819	FYPO:0001357	(Fig. 9)
PMID:37772819	FYPO:0001357	(Fig. 9)
PMID:37772819	FYPO:0001357	(Fig. 8)
PMID:37772819	FYPO:0004469	(Figs. 1B and 2B)
PMID:37772819	FYPO:0004303	(Fig. 1B)
PMID:37772819	FYPO:0004303	(Fig. 1B)
PMID:37772819	GO:0052845	(Figs. 5 and 6)
PMID:37772819	GO:0052843	(Figs. 5 and 6)
PMID:37772819	GO:0004309	(Fig. 4)
PMID:37772819	GO:0052846	Siw14 acts on 1,5-IP8, but it has no preference for either the 5 or 1-beta phosphates (Figs.5 and 6)
PMID:37772819	FYPO:0005485	(Fig. 5)
PMID:37772819	FYPO:0008134	(Fig. S1)
PMID:37772819	PBO:0110077	Table S3
PMID:37772819	PBO:0110078	Table S3
PMID:37772819	PBO:0108806	Table S3
PMID:37772819	PBO:0108804	Table S3
PMID:37772819	PBO:0108808	Table S3
PMID:37772819	PBO:0108810	Table S3
PMID:37772819	PBO:0110079	Table S3
PMID:37772819	PBO:0108850	Table S3
PMID:37772819	PBO:0108811	Table S3
PMID:37772819	PBO:0108797	Table S3
PMID:37772819	PBO:0108822	Table S3
PMID:37772819	GO:0004427	(Fig. 3)
PMID:37772819	GO:0052847	Siw14 acts on 1,5-IP8, but it has no preference for either the 5 or 1-beta phosphates (Figs.5 and 6)
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	PBO:0092114	(comment: 25 ± 10 molecules at the spindle pole body) Fig. 2
PMID:37783794	PBO:0092114	(comment: 77 ± 51 molecules at the spindle pole body) Fig. 2
PMID:37783794	PBO:0092114	(comment: 30 ± 17 molecules at the spindle pole body) Fig. 2
PMID:37783794	PBO:0110098	(comment: 25 ± 13 molecules at the spindle pole body) Fig. 2
PMID:37783794	PBO:0092114	(comment: 69 ± 37 molecules at the spindle pole body) Fig. 2
PMID:37783794	PBO:0110098	(comment: 75 ± 45 molecules at the spindle pole body) Fig. 2
PMID:37783794	PBO:0092114	(comment: 15 ± 8 molecules at the spindle pole body) Fig. 2
PMID:37783794	PBO:0110098	(comment: 16 ± 8 molecules at the spindle pole body) Fig. 2
PMID:37783794	PBO:0110095	(Fig. 5)
PMID:37783794	FYPO:0008125	(Fig. 5A-C)
PMID:37783794	FYPO:0008125	(Fig. 4H)
PMID:37783794	PBO:0110096	(Fig. 4)
PMID:37783794	PBO:0110095	(Fig. 4)
PMID:37783794	GO:0005737	Extended Data Fig. 1A,B
PMID:37783794	PBO:0110439	(Fig. 1B-D)
PMID:37783794	PBO:0110439	(Fig. 1B-D)
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001357	Extended Data Fig. 4
PMID:37783794	FYPO:0001357	Extended Data Fig. 4
PMID:37783794	FYPO:0001357	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0002141	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	(Fig. 7B)
PMID:37783794	FYPO:0001355	(Fig. 7B)
PMID:37783794	FYPO:0001355	(Fig. 7B)
PMID:37783794	FYPO:0001355	(Fig. 7B)
PMID:37783794	PBO:0110080	(Fig. 3C)
PMID:37783794	PBO:0110081	(Fig. 3C)
PMID:37783794	PBO:0110082	(Fig. 3C)
PMID:37783794	PBO:0110083	(Fig. 3C)
PMID:37783794	PBO:0110084	(Fig. 3E)
PMID:37783794	PBO:0110085	(Fig. 3D)
PMID:37783794	PBO:0110086	(Fig. 3D)
PMID:37783794	PBO:0110087	(Fig. 3D)
PMID:37783794	PBO:0110088	(Fig. 3D)
PMID:37783794	PBO:0110089	(Fig. 3F,G) (comment: CHECK into G2)
PMID:37783794	PBO:0110090	(comment: CHECK *********** Fig. 3G decreased protein localization to spindle pole body during G1/S)
PMID:37783794	PBO:0110089	(Fig. 3H-J) (comment:CHECK into G2)
PMID:37783794	PBO:0112754	(Fig. 3I)
PMID:37783794	PBO:0110091	(comment: CEHCK ******** Fig. 3I decreased protein localization to spindle pole body during G1/S)
PMID:37783794	PBO:0110092	(Fig. 3A,B)
PMID:37783794	PBO:0110085	(Fig. 3A,B)
PMID:37783794	FYPO:0008124	(Fig. 4E-H)
PMID:37783794	FYPO:0008126	(Fig. 6B-I)
PMID:37783794	FYPO:0008126	(Fig. 7C,D)
PMID:37783794	FYPO:0008126	(Fig. 7C-E)
PMID:37783794	FYPO:0008126	(Fig. 7C-E)
PMID:37783794	FYPO:0008127	(Fig. 7G)
PMID:37783794	FYPO:0008127	(Fig. 7G)
PMID:37783794	PBO:0110080	Extended Data Fig. 3C
PMID:37783794	FYPO:0008126	Extended Data Fig. B,C
PMID:37783794	PBO:0110093	Extended Data Fig. 5B,C
PMID:37783794	PBO:0110093	Extended Data Fig. 5B,C
PMID:37783794	FYPO:0008126	Extended Data Fig. 5E,F
PMID:37783794	FYPO:0008126	Extended Data Fig. 5E,F
PMID:37783794	FYPO:0008126	Extended Data Fig. 5E,F
PMID:37783794	FYPO:0005695	Extended Data Fig. 5G
PMID:37783794	PBO:0024258	Extended Data Fig. 5I
PMID:37783794	FYPO:0005695	Extended Data Fig. 5H
PMID:37783794	FYPO:0004429	Extended Data Fig. 5G
PMID:37783794	FYPO:0004429	Extended Data Fig. 5G
PMID:37783794	FYPO:0004429	Extended Data Fig. 5H
PMID:37783794	FYPO:0004429	Extended Data Fig. 5H
PMID:37783794	PBO:0110438	(Fig. 1B-D)
PMID:37783794	PBO:0110438	(Fig. 1B-D)
PMID:37783794	PBO:0110438	(Fig. 1B-D)
PMID:37783794	PBO:0110439	(Fig. 1B-D)
PMID:37783794	PBO:0110439	(Fig. 1B-D)
PMID:37783794	PBO:0110439	(Fig. 1B-D)
PMID:37783794	FYPO:0001355	(Fig. 7B)
PMID:37783794	FYPO:0001355	(Fig. 7B)
PMID:37783794	FYPO:0001355	(Fig. 7B)
PMID:37783794	FYPO:0001355	(Fig. 7B)
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001357	Extended Data Fig. 4
PMID:37783794	FYPO:0001357	Extended Data Fig. 4
PMID:37783794	FYPO:0001357	Extended Data Fig. 4
PMID:37783794	FYPO:0001357	Extended Data Fig. 4
PMID:37783794	FYPO:0001357	Extended Data Fig. 4
PMID:37783794	FYPO:0001357	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37787465	PBO:0112708	(Fig. 4C and D)
PMID:37787465	PBO:0112709	(Fig. 4F and G)
PMID:37787465	FYPO:0004166	(Fig. 5A)
PMID:37787465	PBO:0112771	(Fig. 1I and J)
PMID:37787465	PBO:0112772	(Fig. 1C and D)
PMID:37787465	PBO:0112702	Table 1
PMID:37787465	FYPO:0002780	(Fig. 5C and D)
PMID:37787465	PBO:0112703	Table 1
PMID:37787465	PBO:0112704	Table 1
PMID:37787465	PBO:0112705	Table 1
PMID:37787465	PBO:0112704	Table 1
PMID:37787465	PBO:0112703	Table 1
PMID:37787465	PBO:0112703	Table 1
PMID:37787465	PBO:0112705	Table 1
PMID:37787465	FYPO:0002780	(Fig. 5C and D)
PMID:37787465	PBO:0112705	(Fig. 5E and F)
PMID:37787465	PBO:0112811	(Fig. 5B)
PMID:37787465	FYPO:0008213	(Fig. 2J)
PMID:37787465	FYPO:0008213	(Fig. 2I)
PMID:37787465	FYPO:0008213	(Fig. 2I)
PMID:37787465	PBO:0112706	(Fig. 3A and B)
PMID:37787465	FYPO:0008213	(Fig. 2J)
PMID:37787465	PBO:0112707	(Fig. 3C and D)
PMID:37787465	PBO:0112810	(Fig. 5B)
PMID:37788281	GO:0005654	exclusion from nucleoplasm is delayed in rad24 deletion background
PMID:37788281	FYPO:0001864	(comment: dominat negative)
PMID:37788281	PBO:0092097	(comment: CHECK in sam3 mutant)
PMID:37788281	GO:0005654	(comment: CHECK in sam3 mutant)
PMID:37788281	PBO:0099115	(comment: CHECK by expression of rad24-E185K)
PMID:37792890	FYPO:0000135	(comment: using GFP-D4H biosensor)
PMID:37792890	FYPO:0005803	(comment: assayed using FRAP)
PMID:37792890	FYPO:0001357	Indeed, we isolated a cold-sensitive mutant of cut6, cut6-1, as a strong suppressor of css1-3 (S3A Fig).
PMID:37792890	FYPO:0001235	(ags1-664, bgs1-191 and/or bgs4-1 of α1,3-glucan synthase, linear β1,3-glucan synthase and 1,6 branched β1,3-glucan synthase, respectively) [18,24,39], improved css1-3 cell growth at semi-permissive temperatures (S1B Fig) while growth in hypoosomotic conditions (sorbitol-containing media) did not (S1C Fig).
PMID:37792890	PBO:0110142	we predicted that the glucan synthases Ags1, Bgs1, Bgs3, and Bgs4 would localize normally and adjacent to the glucan deposits in css1-3 mutant cells. Indeed, all four proteins localized at tips and septa of css1-3, as in wild-type cells
PMID:37792890	FYPO:0001235	(ags1-664, bgs1-191 and/or bgs4-1 of α1,3-glucan synthase, linear β1,3-glucan synthase and 1,6 branched β1,3-glucan synthase, respectively) [18,24,39], improved css1-3 cell growth at semi-permissive temperatures (S1B Fig) while growth in hypoosomotic conditions (sorbitol-containing media) did not (S1C Fig).
PMID:37792890	FYPO:0000135	(comment: Using GFP-D4H biosensor)
PMID:37792890	FYPO:0002627	In the periplasmic space***** glucans were deposited between the PM and the cell wall at the restrictive temperature (Fig 1B).
PMID:37792890	FYPO:0001357	Indeed, we isolated a cold-sensitive mutant of cut6, cut6-1, as a strong suppressor of css1-3 (S3A Fig).
PMID:37805140	FYPO:0000257	(comment: normal stop codon readthrough)
PMID:37805140	FYPO:0008129	(Figure 4a)
PMID:37805140	FYPO:0007020	(Figure 4a)
PMID:37805140	FYPO:0004529	pulse labeling revealed no defects in mitochondrial translation upon Trm1 deletion (Figure S1)
PMID:37805140	PBO:0116941	Trm1 robustly modified nuclear- and mitochondrial-encoded tRNAs, consistent with its proposed localization to the nucleus and mitochondria, while M1 Trm1 only modified mitochondrially-encoded tRNAs Certain nuclear-encoded tRNAs, including tRNA SerUGA and tRNA LeuAAG were robustly modified by endogenous Trm1 (Figure 1D, “wild type”, lane 1) and overexpressed M24 Trm1 (Figure 1D, lane 3)
PMID:37805140	PBO:0116942	Trm1 robustly modified nuclear- and mitochondrial-encoded tRNAs, consistent with its proposed localization to the nucleus and mitochondria, while M1 Trm1 only modified mitochondrially-encoded tRNAs Certain nuclear-encoded tRNAs, including tRNA SerUGA and tRNA LeuAAG were robustly modified by endogenous Trm1 (Figure 1D, “wild type”, lane 1) and overexpressed M24 Trm1 (Figure 1D, lane 3)
PMID:37805140	PBO:0116943	Trm1 robustly modified nuclear- and mitochondrial-encoded tRNAs, consistent with its proposed localization to the nucleus and mitochondria, while M1 Trm1 only modified mitochondrially-encoded tRNAs Certain nuclear-encoded tRNAs, including tRNA SerUGA and tRNA LeuAAG were robustly modified by endogenous Trm1 (Figure 1D, “wild type”, lane 1) and overexpressed M24 Trm1 (Figure 1D, lane 3)
PMID:37805140	PBO:0116944	Trm1 robustly modified nuclear- and mitochondrial-encoded tRNAs, consistent with its proposed localization to the nucleus and mitochondria, while M1 Trm1 only modified mitochondrially-encoded tRNAs Certain nuclear-encoded tRNAs, including tRNA SerUGA and tRNA LeuAAG were robustly modified by endogenous Trm1 (Figure 1D, “wild type”, lane 1) and overexpressed M24 Trm1 (Figure 1D, lane 3)
PMID:37805140	PBO:0116945	Trm1 robustly modified nuclear- and mitochondrial-encoded tRNAs, consistent with its proposed localization to the nucleus and mitochondria, while M1 Trm1 only modified mitochondrially-encoded tRNAs Certain nuclear-encoded tRNAs, including tRNA SerUGA and tRNA LeuAAG were robustly modified by endogenous Trm1 (Figure 1D, “wild type”, lane 1) and overexpressed M24 Trm1 (Figure 1D, lane 3)
PMID:37805140	PBO:0116946	Trm1 robustly modified nuclear- and mitochondrial-encoded tRNAs, consistent with its proposed localization to the nucleus and mitochondria, while M1 Trm1 only modified mitochondrially-encoded tRNAs Certain nuclear-encoded tRNAs, including tRNA SerUGA and tRNA LeuAAG were robustly modified by endogenous Trm1 (Figure 1D, “wild type”, lane 1) and overexpressed M24 Trm1 (Figure 1D, lane 3)
PMID:37805140	PBO:0116947	Trm1 robustly modified nuclear- and mitochondrial-encoded tRNAs, consistent with its proposed localization to the nucleus and mitochondria, while M1 Trm1 only modified mitochondrially-encoded tRNAs Certain nuclear-encoded tRNAs, including tRNA SerUGA and tRNA LeuAAG were robustly modified by endogenous Trm1 (Figure 1D, “wild type”, lane 1) and overexpressed M24 Trm1 (Figure 1D, lane 3)
PMID:37805140	FYPO:0003957	the D201A mutant showed the same lack of modification of nuclear- and mitochondrial-encoded tRNAs as trm1∆ cells transformed with an empty vector, despite similar levels of protein accumulation as the wild type overexpressed isoform (Figure 1D).
PMID:37805140	FYPO:0003957	the D201A mutant showed the same lack of modification of nuclear- and mitochondrial-encoded tRNAs as trm1∆ cells transformed with an empty vector, despite similar levels of protein accumulation as the wild type overexpressed isoform (Figure 1D).
PMID:37805140	FYPO:0006253	Wild type and D201A exhibited comparable binding affinity, suggesting that disruption of the putative catalytic site does not impair tRNA binding affinity or binding cooperativity (Figure 2A, B, Figure S2, Table S5).
PMID:37805140	FYPO:0008130	We found that both wild type and catalytically inactive nuclear-targeted (M24) Trm1 promoted suppression of the tRNA SerUCA allele in a sla1∆ background, suggesting that modification is not strictly required for suppression activity and that Trm1 promotes pre-tRNA maturation even in the absence of catalysis (Figure 3A, B).
PMID:37815455	GO:0046854	We conclude that pik1-11 cells lack a Golgi PI4P pool, and have reduced PM PI4P that does not result in a corresponding decrease in PM PI(4,5)P2.
PMID:37815455	FYPO:0003736	(Figure 1F)
PMID:37815455	PBO:0110109	In contrast, PM Its3-mNG was mildly reduced at 25°C and increased 1.8-fold at 36°C in pik1-11 compared to wild-type cells (Fig. 2E-F and S1E)
PMID:37815455	FYPO:0002150	when we attempted to combine ncs1Δ with pik1-11 we found that they were synthetically lethal (Fig. 4A)
PMID:37815455	FYPO:0002150	when we attempted to combine ncs1Δ with pik1-11 we found that they were synthetically lethal (Fig. 4A)
PMID:37815455	GO:0180048	This is known from the MF but can be futher supported from the fact that PIP4 levels decrease when stt4 is not localized correctly
PMID:37815455	GO:0098744	To determine whether there was Golgi PI4P in ncs1∆, a proxy for a change in Pik1 activity, we imaged cells expressing GFP-P4CSidC in wild-type and ncs1Δ cells. We observed the persistence of Golgi PI4P puncta as well as increased cytoplasmic and PM PI4P levels in ncs1∆ cells (Fig. 4E-F). Combined with the fact that Pik1 is essential whereas Ncs1 is not (Hamasaki-Katagiri et al., 2004; Park et al., 2009), it seems unlikely that Ncs1 is required for S. pombe Pik1 activity and perhaps even acts as a negative regulator.
PMID:37815455	FYPO:0002061	pik1-11 cells grow similarly to wild-type at 25 ̊C and 29 ̊C but pik1-11 cells do not grow at 32 ̊C or 36 ̊C (Fig. 1C)
PMID:37815455	FYPO:0002060	pik1-11 cells grow similarly to wild-type at 25 ̊C and 29 ̊C but pik1-11 cells do not grow at 32 ̊C or 36 ̊C (Fig. 1C)
PMID:37815455	PBO:0110112	(Fig. S1D)
PMID:37815455	PBO:0110111	(Fig. S1D)
PMID:37815455	PBO:0110110	(Fig. S1D)
PMID:37815455	FYPO:0007489	We found that Pik1-D450- mNG still localized to the trans-Golgi marked by Sec72-mCherry in ncs1∆ cells (Fig. 4C), Interestingly, there was a high cytoplasmic Pik1 population in ncs1Δ cells that was not observed in wild-type cells; indeed, there was >2- fold more Pik1 overall (Fig. 4D). We currently do not have a mechanistic explanation for this observation.
PMID:37815455	FYPO:0001355	(Fig. S2A)
PMID:37815455	FYPO:0001355	(Fig. S2A)
PMID:37815455	FYPO:0001355	(Fig. S2A)
PMID:37815455	FYPO:0001355	(Fig. S2A)
PMID:37815455	PBO:0110108	We conclude that pik1-11 cells lack a Golgi PI4P pool, and have reduced PM PI4P that does not result in a corresponding decrease in PM PI(4,5)P2.
PMID:37815455	GO:0032588	found co-localization only with the trans-Golgi marker (Fig. 3B)
PMID:37815455	GO:0032588	we observed co-localization of Ncs1-mCherry with Pik1- D450-mNG at the trans-Golgi (Fig. 4B)
PMID:37815455	FYPO:0001903	(Fig. 1D-E).
PMID:37820734	GO:0061776	A reaction time course revealed that most dsDNA binding occurred within the first 15 min of incubation, whereas dsDNA binding by Walker A ATPase motif mutant condensin was not stimulated by ATP addition (Figures S1B and S1C). These results show that recombinant fission yeast condensin binds to DNA in an ATP-stimulated, high-salt-resistant manner, characteristic of topological DNA interactions by SMC complexes.
PMID:37820734	GO:0106260	sequential topological entrapment of two or more DNAs, A DNA tethering activity where a protein complex encircles two or more DNA molecules, one at a time, with its loose fitting ring.
PMID:37820734	GO:0106260	sequential topological entrapment of two or more DNAs, A DNA tethering activity where a protein complex encircles two or more DNA molecules, one at a time, with its loose fitting ring.
PMID:37820734	GO:0061776	A reaction time course revealed that most dsDNA binding occurred within the first 15 min of incubation, whereas dsDNA binding by Walker A ATPase motif mutant condensin was not stimulated by ATP addition (Figures S1B and S1C). These results show that recombinant fission yeast condensin binds to DNA in an ATP-stimulated, high-salt-resistant manner, characteristic of topological DNA interactions by SMC complexes.
PMID:37820734	GO:0061776	A reaction time course revealed that most dsDNA binding occurred within the first 15 min of incubation, whereas dsDNA binding by Walker A ATPase motif mutant condensin was not stimulated by ATP addition (Figures S1B and S1C). These results show that recombinant fission yeast condensin binds to DNA in an ATP-stimulated, high-salt-resistant manner, characteristic of topological DNA interactions by SMC complexes. Three topologically closed dsDNA substrates—supercoiled, relaxed circular, and nicked circular— were all recovered with similar efficiency (Figure 1B). Condensin also bound, albeit less efficiently, circular single-stranded DNA (ssDNA). By contrast, we observed no detectable recovery of linear dsDNA, consistent with a topological condensin-DNA interaction.
PMID:37820734	GO:0003690	(comment: author suggested) double-stranded DNA gripping or clamping A DNA binding activity, stimulated by the binding of a non-hydrolylsable ATP analogue, where a ATPase protein complex tightly grips a stretch of double-stranded DNA with some or all of its subunits. Such a conformation is usually interpretted as the intermediate state before the ATP hydrolysis by the protein complex.
PMID:37820734	GO:0106260	DNA-DNA tethering activity, sequential topological entrapment: sequential topological entrapment of two or more DNAs, A DNA tethering activity where a protein complex encircles two or more DNA molecules, one at a time, with its loose fitting ring.
PMID:37820734	GO:0061776	A reaction time course revealed that most dsDNA binding occurred within the first 15 min of incubation, whereas dsDNA binding by Walker A ATPase motif mutant condensin was not stimulated by ATP addition (Figures S1B and S1C). These results show that recombinant fission yeast condensin binds to DNA in an ATP-stimulated, high-salt-resistant manner, characteristic of topological DNA interactions by SMC complexes. Although an intact supercoiled plasmid remained stably bound to condensin in the bead fraction, linearized dsDNA was released into the supernatant. This experiment confirms that ATP-dependent condensin loading results in a topological DNA interaction.
PMID:37820734	GO:0106260	sequential topological entrapment of two or more DNAs, A DNA tethering activity where a protein complex encircles two or more DNA molecules, one at a time, with its loose fitting ring.
PMID:37820734	GO:0061776	A reaction time course revealed that most dsDNA binding occurred within the first 15 min of incubation, whereas dsDNA binding by Walker A ATPase motif mutant condensin was not stimulated by ATP addition (Figures S1B and S1C). These results show that recombinant fission yeast condensin binds to DNA in an ATP-stimulated, high-salt-resistant manner, characteristic of topological DNA interactions by SMC complexes.
PMID:37820734	GO:0106260	sequential topological entrapment of two or more DNAs, A DNA tethering activity where a protein complex encircles two or more DNA molecules, one at a time, with its loose fitting ring.
PMID:37831774	PBO:0113807	In ent1-Δ(572-702) cells, force on End4 is increased to above 20 piconewton at G857, but remains the same as in wild type at P337 and D155.
PMID:37831774	FYPO:0002177	In ent1-Δ(572-702) cells, force on End4 is increased to above 20 piconewton at G857, but remains the same as in wild type at P337 or D155.
PMID:37831774	PBO:0113806	A gradient of force is detected along End4 molecule in wild-type cells. ~19 piconewton force near the actin cytoskeleton (G857), ~11 piconewtons near the clathrin lattice (P337), and ~9 piconewtons near the plasma membrane (D155).
PMID:37831774	PBO:0019716	In wild-type cells, fluorescently tagged End4p is present at endocytic sites and appears as diffraction-limited puncta (hereafter referred to as End4p patches) that are enriched at cell tips during interphase and around the division plane during mitosis (Fig. 1F; figs. S2A and S5, B and C; and movie S1).
PMID:37831774	PBO:0097629	In wild-type cells, fluorescently tagged End4p is present at endocytic sites and appears as diffraction-limited puncta (hereafter referred to as End4p patches) that are enriched at cell tips during interphase and around the division plane during mitosis (Fig. 1F; figs. S2A and S5, B and C; and movie S1).
PMID:37831774	GO:0061645	In wild-type cells, fluorescently tagged End4p is present at endocytic sites and appears as diffraction-limited puncta (hereafter referred to as End4p patches) that are enriched at cell tips during interphase and around the division plane during mitosis (Fig. 1F; figs. S2A and S5, B and C; and movie S1).
PMID:37913773	FYPO:0001134	Moreover, we found that the diminution of 18S rRNA levels in the tor2-287 mutant could be mitigated by overexpression of Atf1 (atf1 o.p) or disruption of the ago1+ gene (ago1D), which encodes a crucial factor for RNAi-dependent heterochromatinization (Figure 3I).
PMID:37913773	PBO:0111445	Chromatin immunoprecipitation (ChIP) experiments targeting FLAG-tagged Tor2, Pop3/LST8, Tco89, and Mip1/Raptor, constituents of TORC1,31 exhibited significant TORC1 accumulation across the rDNA, predominantly in the 18S and 28S regions (Figures 1A and 1B).
PMID:37913773	PBO:0111446	Chromatin immunoprecipitation (ChIP) experiments targeting FLAG-tagged Tor2, Pop3/LST8, Tco89, and Mip1/Raptor, constituents of TORC1,31 exhibited significant TORC1 accumulation across the rDNA, predominantly in the 18S and 28S regions (Figures 1A and 1B).
PMID:37913773	GO:0060963	Taken together, the transcription of ribosome-associated genes is regulated by TORC1.
PMID:37913773	GO:0061188	We thus conclude that heterochromatinization of rDNA induced by glucose starvation is initiated by TORC1 inactivation (Figure 3F).
PMID:37913773	FYPO:0003694	Our result indicated that the total amount of 18S rRNA transcripts was reduced by half in the tor2-287 mutant, even under nutrient-rich conditions (Figure 3A).
PMID:37913773	PBO:0110877	Furthermore, we discovered that this reduction was caused by the dissociation of RNA polymerase I from the rDNA region (Figures 3B and S3B).
PMID:37913773	PBO:0110878	heterochromatin formation in rDNA is prompted by the dissociation of the stress- responsive transcription factor Atf1 and the accumulation of the histone chaperone FACT, which maintains H3K9 methylation,40 in addition to the RNAi-dependent pathway.14 We therefore performed ChIP-qPCR targeting Atf1 and FLAG-tagged Pob3 (a component of FACT), and found that Atf1 diminished from the entire rDNA region, while Pob3-FLAG selectively accumulated between rDNA repeats (Figures 3D and 3E).
PMID:37913773	FYPO:0006074	To investigate this, we performed ChIP-qPCR targeting H3K9 methylation, a marker of heterochromatin formation, in both wild-type and tor2-287 cells. We found that tor2-287 cells exhibited a marked increase in H3K9me2 levels, accompanied by a slight increase in histone H3 occupancy in the rDNA region (Figures 3C and S3C).
PMID:37913773	PBO:0110880	we conducted ChIP-qPCR targeting Gcn5-HA and found that it diminished from rDNA in the tor2-287 mutant compared with wild-type (Figure S3D).
PMID:37913773	PBO:0110881	we found that the intracellular Atf1 protein levels were significantly reduced in the tor2-287 mutants when detected with an anti-Atf1 antibody (Figures 3G and 3H).
PMID:37913773	PBO:0110882	We performed RT-qPCR and found that transcription of selected ribosome-related genes (rpl102+, rlp7+, and gar2+) was reduced in the tor2-287 mutant (Figure 4A).
PMID:37913773	PBO:0110883	We performed RT-qPCR and found that transcription of selected ribosome-related genes (rpl102+, rlp7+, and gar2+) was reduced in the tor2-287 mutant (Figure 4A).
PMID:37913773	PBO:0110884	We performed RT-qPCR and found that transcription of selected ribosome-related genes (rpl102+, rlp7+, and gar2+) was reduced in the tor2-287 mutant (Figure 4A).
PMID:37913773	PBO:0110885	nuc1-632 mutant strain, wherein RNA polymerase I function was impaired.33,34 As a result, we found a considerable reduction in Tor2 accumulation in the rDNA region compared with wild-type cells, concomitant with a decrease in rRNA abundance (Figures 2A and 2B).
PMID:37913773	FYPO:0001134	Moreover, we found that the diminution of 18S rRNA levels in the tor2-287 mutant could be mitigated by overexpression of Atf1 (atf1 o.p) or disruption of the ago1+ gene (ago1D), which encodes a crucial factor for RNAi-dependent heterochromatinization (Figure 3I).
PMID:37913773	FYPO:0001134	Although the downstream S6K kinase Psk1 in the TORC1 pathway has been implicated in RP phosphorylation,39 our finding demonstrated that rRNA abundance was unaffected in the psk1D strain (Figure S3A)
PMID:37913773	PBO:0111445	Chromatin immunoprecipitation (ChIP) experiments targeting FLAG-tagged Tor2, Pop3/LST8, Tco89, and Mip1/Raptor, constituents of TORC1,31 exhibited significant TORC1 accumulation across the rDNA, predominantly in the 18S and 28S regions (Figures 1A and 1B).
PMID:37913773	PBO:0111446	Chromatin immunoprecipitation (ChIP) experiments targeting FLAG-tagged Tor2, Pop3/LST8, Tco89, and Mip1/Raptor, constituents of TORC1,31 exhibited significant TORC1 accumulation across the rDNA, predominantly in the 18S and 28S regions (Figures 1A and 1B).
PMID:37913773	PBO:0110891	Nevertheless, our analysis revealed that deletion of atf1+ gene (atf1D) did not significantly affect Tor2 accumulation in rDNA (Figures S2A and S2B).
PMID:37913773	GO:0042134	In addition, the RNA immunoprecipitation analysis revealed a notable association between FLAG-Tor2 and rDNA transcripts, specifically at the 18S, 5.8S, and 28S regions (Figures 2E and S2D)
PMID:37913773	PBO:0110885	We then examined their accumulation at rDNA using ChIP assays and found a decrease in the rDNA accumulation of FLAG-Tor2 lacking the HTH domain (Figure 2G).
PMID:37923140	PBO:0113736	(Fig. 5)
PMID:37923140	PBO:0113736	(Fig. 5)
PMID:37923140	GO:0008270	Metal and acid-labile sulfide analysis of anaerobically purified Fep1-DBD from three independent samples indicated 0.76 ± 0.12 Zn, 0.69 ± 0.08 Fe, and 0.85 ± 0.10 S2- bound per monomer.
PMID:37923140	PBO:0113732	(Fig. 3)
PMID:37923140	PBO:0113733	(Fig. 3)
PMID:37923140	PBO:0113734	(Fig. 3)
PMID:37923140	FYPO:0007933	(Fig. 4)
PMID:37923140	FYPO:0007933	(Fig. 4)
PMID:37923140	FYPO:0007933	(Fig. 4)
PMID:37923140	FYPO:0007933	(Fig. 4)
PMID:37923140	PBO:0105380	(Fig. 5)
PMID:37923140	PBO:0113735	(Fig. 5)
PMID:37923140	PBO:0113736	(Fig. 5)
PMID:37939137	FYPO:0007447	(Fig. 3L)
PMID:37939137	PBO:0119328	In the absence of Rtn1, Yop1, and Tts1, the cortical ER becomes less reticulate and more sheet-like, with the frequent appearance of large holes in images of the top or bottom plane of the cells and extended gaps in images of the midplane of the cells [50]. We found that this alteration of ER morphology can be reversed to a large extent by either introducing back Rtn1 or increasing the expression level of Yep1 (Figs 3B and S4B)
PMID:37939137	PBO:0119328	Thus, Yep1, when overexpressed, can fulfill the function of maintaining tubular ER independently of Rtn1, Yop1, and Tts1.
PMID:37939137	PBO:0119327	(Figure 2) Taken together, the above findings demonstrate that Yep1 is required for the autophagosomal enclosure of ER-phagy/nucleophagy cargos.
PMID:37939137	PBO:0119326	In the absence of Rtn1, Yop1, and Tts1, the cortical ER becomes less reticulate and more sheet-like, with the frequent appearance of large holes in images of the top or bottom plane of the cells and extended gaps in images of the midplane of the cells [50]. We found that this alteration of ER morphology can be reversed to a large extent by either introducing back Rtn1 or increasing the expression level of Yep1 (Figs 3B and S4B).
PMID:37939137	PBO:0119325	(Figure 2) Taken together, the above findings demonstrate that Yep1 is required for the autophagosomal enclosure of ER-phagy/nucleophagy cargos.
PMID:37939137	FYPO:0008388	(Figure 2) Taken together, the above findings demonstrate that Yep1 is required for the autophagosomal enclosure of ER-phagy/nucleophagy cargos.
PMID:37939137	PBO:0119324	(comment: during nucleophagy abnd reticulophagy)
PMID:37939137	PBO:0119323	In both wild-type and yep1Δ cells, Epr1 and Atg8 colocalized at punctate structures shortly after ER-phagy induction by DTT or starvation treatment (S2A Fig), indicating that Yep1 is not essential for the initial stage of ER-phagy during which Epr1 mediates a connection between the ER and Atg8-decorated autophagic membranes.
PMID:37939137	PBO:0119322	In both wild-type and yep1Δ cells, Epr1 and Atg8 colocalized at punctate structures shortly after ER-phagy induction by DTT or starvation treatment (S2A Fig), indicating that Yep1 is not essential for the initial stage of ER-phagy during which Epr1 mediates a connection between the ER and Atg8-decorated autophagic membranes.
PMID:37939137	FYPO:0008386	The loss of the ER-phagy receptor Epr1 diminished the processing of Pus1-mECi- trine, suggesting that Epr1 also acts as a nucleophagy receptor
PMID:37939137	GO:0097038	As Ost4 and Erg11 localize to both the cortical ER and the nuclear envelope..... (Fig 1F and 1G)
PMID:37939137	GO:0097038	As Ost4 and Erg11 localize to both the cortical ER and the nuclear envelope..... (Fig 1F and 1G)
PMID:37939137	FYPO:0007447	(Fig. S6A)
PMID:37939137	PBO:0119329	(Fig. S5; Fig S6)
PMID:37939137	PBO:0119329	(Fig. S5, S6)
PMID:37939137	PBO:0119329	(Fig. S5, S6)
PMID:37939137	PBO:0119329	(Fig. S5, S6)
PMID:37939137	FYPO:0007446	(Fig. 3K)
PMID:37939137	FYPO:0007446	(Fig. 3K)
PMID:37939137	FYPO:0007446	(Fig. 3L)
PMID:37939137	FYPO:0007446	(Fig. 3L)
PMID:37939137	FYPO:0007447	(Fig. 3 J-K, S6 E)
PMID:37939137	FYPO:0007446	(Fig. S6A)
PMID:37939137	FYPO:0007447	(Fig. 3J-K, S6 E)
PMID:37939137	FYPO:0007447	(Fig. 3J-K, S6 E)
PMID:37939137	PBO:0098140	(Fig. 3C) We observed that yep1Δ caused a noticeable but even weaker septum positioning defect than rtn1Δ, yop1Δ, or tts1Δ. Combined yep1Δ with the double and triple deletion of rtn1, yop1, and tts1 invariably resulted in a more severe phenotype (Fig 3C).
PMID:37939137	PBO:0119321	(Fig. 3C)
PMID:37939137	FYPO:0008385	(Fig. 1H)
PMID:37939137	FYPO:0008086	(Fig. 1I) Deletion of yep1 abolished the processing of Pus1-mECitrine in both DTT- and starvation-treated cells, indicating that Yep1 is essential for nucleophagy.
PMID:37939137	FYPO:0007444	(Fig. 1J) In contrast to the severe ER-phagy and nucleophagy defects of yep1Δ cells, bulk autophagy in yep1Δ cells was largely normal as indicated by the processing of CFP-Atg8 (Fig 1J).
PMID:37939137	FYPO:0006294	(Fig. 1J) In contrast to the severe ER-phagy and nucleophagy defects of yep1Δ cells, bulk autophagy in yep1Δ cells was largely normal as indicated by the processing of CFP-Atg8 (Fig 1J). In addition, another readout of bulk autophagy, the processing of fluorescent protein-tagged cytosolic protein Tdh1 (glyceraldehyde-3-phosphate dehydrogenase (GAPDH)) [43], was also largely unaffected in yep1Δ cells (S1E Fig). Consistent with the lack of bulk autophagy defects, transmission (TEM) analysis showed that autophagosome accumulation in the fsc1Δ mutant, which is defective in autophagosome-vacuole fusion [44], was not notably affected by the deletion of yep1 (S1F Fig).
PMID:37939137	FYPO:0008084	(Fig. 1C) Consistent with this idea, deletion of yep1 severely diminished the relocalization of Ost4-CFP to the vacuole upon DTT treatment (+DTT) or nitrogen starvation treatment (−N) (Fig 1C). yep1Δ cells also exhibited a severe defect in the autophagic processing of GFP-tagged integral ER membrane protein Erg11 into free GFP (Fig 1D and 1E).
PMID:37939137	FYPO:0008084	(Fig. 1D)
PMID:37939137	FYPO:0007447	(Fig. 1C) Consistent with this idea, deletion of yep1 severely diminished the relocalization of Ost4-CFP to the vacuole upon DTT treatment (+DTT) or nitrogen starvation treatment (−N) (Fig 1C).
PMID:37939137	FYPO:0007447	(Fig. 1E)
PMID:37939137	GO:0032541	As Ost4 and Erg11 localize to both the cortical ER and the nuclear envelope..... (Fig 1F and 1G)
PMID:37939137	GO:0032541	As Ost4 and Erg11 localize to both the cortical ER and the nuclear envelope..... (Fig 1F and 1G)
PMID:37939137	GO:0005783	Human REEP1-4 are ER-localizing proteins [38,41,42], Similarly, we found that Yep1 exhibited an ER localization pattern during vegetative growth (S1B Fig).
PMID:37939137	PBO:0119318	These results demonstrate that Yep1 shares the membrane-shaping ability of Rtn1, Yop1, and Tts1 and contributes to the maintenance of normal ER structure.
PMID:37939137	PBO:0119317	These results demonstrate that Yep1 shares the membrane-shaping ability of Rtn1, Yop1, and Tts1 and contributes to the maintenance of normal ER structure.
PMID:37949217	FYPO:0002061	We found that spores assumed to be Δpqr1Δxpr1Δvtc4 did not form colonies, suggesting synthetic lethality of gene deletions of pqr1+, xpr1+, and vtc4+ on YES.
PMID:37949217	FYPO:0008267	(Figure 1A)
PMID:37949217	PBO:0113629	(Figure 1A)
PMID:37949217	PBO:0113629	(Figure 1A)
PMID:37949217	PBO:0113628	(Figure 1a)
PMID:37949217	PBO:0113627	(Figure 1a)
PMID:37949217	GO:0005886	It was localized mainly in the cell periphery, probably at the plasma membrane (Fig. 1C), consistent with its role in Pi export.
PMID:37949217	FYPO:0000364	(Figure 3)
PMID:37949217	FYPO:0008228	Xpr1-dependent Pi export is accelerated by either Δpqr1 or Δvtc4. Importantly, the elevation of Pi export activity in Δpqr1 and Δvtc4 is synergistic. In Δpqr1Δvtc4, exported Pi was far greater than that in the single mutant (Fig. 5D
PMID:37949217	FYPO:0008228	Xpr1-dependent Pi export is accelerated by either Δpqr1 or Δvtc4. Importantly, the elevation of Pi export activity in Δpqr1 and Δvtc4 is synergistic. In Δpqr1Δvtc4, exported Pi was far greater than that in the single mutant (Fig. 5D
PMID:37949217	PBO:0112796	Xpr1-dependent Pi export is accelerated by either Δpqr1 or Δvtc4. Importantly, the elevation of Pi export activity in Δpqr1 and Δvtc4 is synergistic. In Δpqr1Δvtc4, exported Pi was far greater than that in the single mutant (Fig. 5D
PMID:37949217	PBO:0112796	Xpr1-dependent Pi export is accelerated by either Δpqr1 or Δvtc4. Importantly, the elevation of Pi export activity in Δpqr1 and Δvtc4 is synergistic. In Δpqr1Δvtc4, exported Pi was far greater than that in the single mutant (Fig. 5D
PMID:37949217	PBO:0112796	Xpr1-dependent Pi export is accelerated by either Δpqr1 or Δvtc4. Importantly, the elevation of Pi export activity in Δpqr1 and Δvtc4 is synergistic. In Δpqr1Δvtc4, exported Pi was far greater than that in the single mutant (Fig. 5D
PMID:37949217	PBO:0112797	We found that Xpr1-GFP did not increase in Δpqr1, Δvtc4, or Δpqr1Δvtc4 (Fig. 5G). Accelerated Pi export in these mutants may not be caused by increased amounts of Xpr1 protein.
PMID:37949217	PBO:0112797	We found that Xpr1-GFP did not increase in Δpqr1, Δvtc4, or Δpqr1Δvtc4 (Fig. 5G). Accelerated Pi export in these mutants may not be caused by increased amounts of Xpr1 protein.
PMID:37949217	PBO:0112797	We found that Xpr1-GFP did not increase in Δpqr1, Δvtc4, or Δpqr1Δvtc4 (Fig. 5G). Accelerated Pi export in these mutants may not be caused by increased amounts of Xpr1 protein.
PMID:37949217	PBO:0112798	In the mutants, Xpr1- GFP was similarly localized to the cell periphery, suggesting that accelerated Pi export in these mutants may not be caused by dynamic alteration of the localization of the exporter, Xpr1
PMID:37949217	PBO:0112798	In the mutants, Xpr1- GFP was similarly localized to the cell periphery, suggesting that accelerated Pi export in these mutants may not be caused by dynamic alteration of the localization of the exporter, Xpr1
PMID:37949217	PBO:0112798	In the mutants, Xpr1- GFP was similarly localized to the cell periphery, suggesting that accelerated Pi export in these mutants may not be caused by dynamic alteration of the localization of the exporter, Xpr1
PMID:37949217	FYPO:0001357	The Pi hyper-sensitivity of Δpqr1Δxpr1 was suppressed by the double gene deletion of Pho84 and Pho842 (Figs. 6A and S6).
PMID:37949217	FYPO:0008227	(Figure 3)
PMID:37949217	FYPO:0002060	All double mutants, Δpqr1Δxpr1, Δpqr1Δvtc4, and Δxpr1Δvtc4, were able to form colonies at 100 mM Pi. Δpqr1Δxpr1 showed slow growth at 100 mM Pi and failed to grow at 300 mM Pi (Fig. 2C).
PMID:37949217	FYPO:0001355	All double mutants, Δpqr1Δxpr1, Δpqr1Δvtc4, and Δxpr1Δvtc4, were able to form colonies at 100 mM Pi. Δpqr1Δxpr1 showed slow growth at 100 mM Pi and failed to grow at 300 mM Pi (Fig. 2C).
PMID:37949217	FYPO:0002060	All double mutants, Δpqr1Δxpr1, Δpqr1Δvtc4, and Δxpr1Δvtc4, were able to form colonies at 100 mM Pi. Δpqr1Δxpr1 showed slow growth at 100 mM Pi and failed to grow at 300 mM Pi (Fig. 2C).
PMID:37949217	FYPO:0000646	Cells were severely deformed/swollen and many were collapsed and probably dying (Figs. 2D and S2).
PMID:37949217	FYPO:0002060	This time, we obtained Δpqr1Δxpr1Δvtc4 colonies on PMG with 0.15 mM Pi, which did not grow on either normal PMG (15 mM Pi) or YES.
PMID:37956308	GO:0045815	ells lacking Snf22 and Hrp3 were largely unable to open the chromatin structure at the ctt1 gene upon stress imposition.
PMID:37956308	FYPO:0001103	On the contrary, deletion of hrp1 yielded a strain resistant to H2 O2 , almost to the same extent as Δtop1 (Figure 6B).
PMID:37956308	PBO:0093578	Regarding tolerance to oxidative stress, cells lacking Hrp3 or Snf22 are severely sensitive to oxidative stress (Figure 6A)
PMID:37956308	PBO:0093578	Regarding tolerance to oxidative stress, cells lacking Hrp3 or Snf22 are severely sensitive to oxidative stress (Figure 6A)
PMID:37956308	FYPO:0001103	Cells expressing a catalytically-dead version of the enzyme, Top1.Y773F, also displayed resistance to peroxides (Supplementary Figure S1B), suggesting that lack of topoisomerase activity is involved in this phenotype.
PMID:37956308	FYPO:0001103	To our surprise, cells lacking Top1 were resistant to H2O2 on plates, when compared to a wild-type strain (Figure 1A).
PMID:37956308	GO:0006338	As shown in Supplementary Figure S7F, the stress-dependent recruitment of Ser2-phosphorylated Pol II to the ctt1 gene was significantly higher in cells lacking Hrp1 than in wild-type cells.
PMID:37956308	FYPO:0001032	In fact, the Top1 deficient strains displayed resistance to camptothecin, as expected (Supplementary Figure S1C):
PMID:37956308	PBO:0116515	We determined by northern blot that the ctt1, srx1 and hsp9 genes, coding for the anti-stress proteins catalase, sulfiredoxin and the chaperone Hsp9, respectively, were up-regulated in Δtop1 cells to a larger extent that in a wild-type strain upon H2O2 stress (Figure 1B and Supplementary Figure S1E)
PMID:37956308	PBO:0116516	We determined by northern blot that the ctt1, srx1 and hsp9 genes, coding for the anti-stress proteins catalase, sulfiredoxin and the chaperone Hsp9, respectively, were up-regulated in Δtop1 cells to a larger extent that in a wild-type strain upon H2O2 stress (Figure 1B and Supplementary Figure S1E)
PMID:37956308	PBO:0116517	We determined by northern blot that the ctt1, srx1 and hsp9 genes, coding for the anti-stress proteins catalase, sulfiredoxin and the chaperone Hsp9, respectively, were up-regulated in Δtop1 cells to a larger extent that in a wild-type strain upon H2O2 stress (Figure 1B and Supplementary Figure S1E)
PMID:37956308	FYPO:0001103	The resistance phenotypes of the single deletes did not add in the double deletion strain, suggesting that Top1 and Hrp1 contribute to H2O2 tolerance through a similar mechanism.
PMID:37956308	FYPO:0000962	and the combination of gene deletions of Δtop1 with either Δhrp3 or Δsnf22 yielded strains with intermediate phenotypes, suggesting that Top1 and these chromatin remodelers affect oxidative stress tolerance through independent mechanisms. (Figure 6A)
PMID:37956308	FYPO:0000962	and the combination of gene deletions of Δtop1 with either Δhrp3 or Δsnf22 yielded strains with intermediate phenotypes, suggesting that Top1 and these chromatin remodelers affect oxidative stress tolerance through independent mechanisms. (Figure 6A)
PMID:37956308	PBO:0116518	Nevertheless, we showed by western blot that Atf1 phosphorylation was not exacerbated in cells lacking Top1 (Figure 1C).
PMID:37956308	PBO:0116519	Similarly, we determined by ChIP that Atf1 recruitment to stress promoters was unaltered in Δtop1 cells (Figure 1D).
PMID:37956308	PBO:0112712	As shown in Figure 2A, Top1-HA accumulated at ORFs of the ctt1 and gpd1 genes after peroxide stress
PMID:37956308	PBO:0116520	In cells lacking Top1, Pol II recruitment was more sustained than in wild-type cells (compare 60 min in both backgrounds in Figure 2B).
PMID:37956308	GO:0045815	ells lacking Snf22 and Hrp3 were largely unable to open the chromatin structure at the ctt1 gene upon stress imposition.
PMID:37956308	FYPO:0005951	15 min after stress imposition, only few nucleosomes were still partially evicted in a wild-type background, whereas the number of nucleosomes which remained significantly less occupied relative to untreated conditions was much higher in cells lacking Top1 (Figure 4D and E; Supplementary Table S5). Of note, the differences observed for the averaged nucleosome maps of the 494 stress genes between wild-type and Δtop1 strains was more dramatic for the highly expressed genes of the quartil 1, than for the genes of the other quartils (unpublished data).
PMID:37956308	FYPO:0000962	and the combination of gene deletions of Δtop1 with either Δhrp3 or Δsnf22 yielded strains with intermediate phenotypes, suggesting that Top1 and these chromatin remodelers affect oxidative stress tolerance through independent mechanisms. (Figure 6A)
PMID:37956308	FYPO:0000962	and the combination of gene deletions of Δtop1 with either Δhrp3 or Δsnf22 yielded strains with intermediate phenotypes, suggesting that Top1 and these chromatin remodelers affect oxidative stress tolerance through independent mechanisms. (Figure 6A)
PMID:37970674	PBO:0112070	(comment: CHECK inhibits)
PMID:37970674	GO:0072766	(comment: CHECK inhibits)
PMID:37970674	FYPO:0006995	(Figure 3D)
PMID:37970674	PBO:0112061	However, in nup132Δ cells, whereas wild-type Pli1 was destabilised, Pli1K3R levels remained high (Fig. 1B).
PMID:37970674	PBO:0112060	However, in nup132Δ cells, whereas wild-type Pli1 was destabilised, Pli1K3R levels remained high (Fig. 1B).
PMID:37970674	PBO:0096188	, deletion of either nup132+ or pli1+ results in reduced growth in the presence of 5-FOA, indicating increased expression of ura4+ and hence loss of silencing (Fig. 1C).
PMID:37970674	PBO:0096188	, deletion of either nup132+ or pli1+ results in reduced growth in the presence of 5-FOA, indicating increased expression of ura4+ and hence loss of silencing (Fig. 1C).
PMID:37970674	PBO:0096188	If the silencing defect in nup132Δ cells were due to destabilisation of Pli1, we would expect it to be rescued by expression of the stabilised Pli1K3R mutant. However, this was not the case - nup132Δ cells expressing Pli1K3R-Flag displayed a defect in silencing equivalent to those expressing wild-type Pli1-Flag
PMID:37970674	FYPO:0000964	Similarly, both nup132Δ and pli1Δ cells showed sensitivity to the microtubule-stabilising drug thiabendazole (TBZ), consistent with defects in centromere function, and this TBZ sensitivity was also not rescued by the Pli1K3R mutation (Fig. 1C). T
PMID:37970674	PBO:0093564	Similarly, both nup132Δ and pli1Δ cells showed sensitivity to the microtubule-stabilising drug thiabendazole (TBZ), consistent with defects in centromere function, and this TBZ sensitivity was also not rescued by the Pli1K3R mutation (Fig. 1C). T
PMID:37970674	PBO:0093564	Similarly, both nup132Δ and pli1Δ cells showed sensitivity to the microtubule-stabilising drug thiabendazole (TBZ), consistent with defects in centromere function, and this TBZ sensitivity was also not rescued by the Pli1K3R mutation (Fig. 1C). T
PMID:37970674	PBO:0093564	Similarly, both nup132Δ and pli1Δ cells showed sensitivity to the microtubule-stabilising drug thiabendazole (TBZ), consistent with defects in centromere function, and this TBZ sensitivity was also not rescued by the Pli1K3R mutation (Fig. 1C). T
PMID:38041816	FYPO:0000729	The rng2-CykFΔ cells also assembled actin rings (Figures 6A and 6B), but the ring emergence and removal were significantly delayed (Figures 6B-6D)
PMID:38041816	FYPO:0004652	s. Surprisingly, the rng2- CHDΔ cells formed WT-like actin rings, as revealed by phalloidin staining (Figure 6A), despite the ability of CHD to bind F-actin.3
PMID:38041816	FYPO:0001365	The removal of GFP-Rng2-CykFΔ was also slowed down (Figures 5E and 5F), and its rate of constriction was reduced by ~30% compared with GFP-Rng2 (Figure 5H, p < 0.01)
PMID:38041816	FYPO:0005022	GFP-Rng2-CHDΔ behaved like the WT in all aspects (Figures 5E-5H), except for the loss of accumulation during the slow phase (Figure 5F, from −15 to 0 min).
PMID:38041816	PBO:0113570	However, when both domains were deleted together (rng2-CHDΔ-CykFΔ), most cells showed strong defects in cytokinesis, especially at 36°C, where >90% of the cells formed cell chains with various abnormal septa, including some “catastrophic” structures (Figures 5B-5D).
PMID:38041816	PBO:0113569	However, when both domains were deleted together (rng2-CHDΔ-CykFΔ), most cells showed strong defects in cytokinesis, especially at 36°C, where >90% of the cells formed cell chains with various abnormal septa, including some “catastrophic” structures (Figures 5B-5D).
PMID:38041816	PBO:0037118	The rng2-CykFΔ cells did not show any apparent defect in cell morphology, but ~10% of the cells formed a partial or complete septum doublet at both temperatures, suggesting a moderate defect in cytokinesis (Figures 5B-5D and S4C).
PMID:38041816	FYPO:0006213	We found that the rng2-CHDΔ cells displayed similar cell and septum morphologies compared with the WT (rng2 +) cells at both temperatures (Figures 5B-5D and S4C).
PMID:38041816	PBO:0113568	Indeed, the fragment (aa 185-300) containing the CykF domain localized weakly, but consistently, to the division site during cytokinesis (Figures 4E and S4A and Video S3), suggesting that the binding affinity between CykF and the cytokinesis factor(s) is low.
PMID:38041816	PBO:0113568	Strikingly, the Rng2 fragment (aa 1-300), previously called Rng2Ns,44 began to localize to the division site at the onset of anaphase and constricted during cytokinesis (Figure 4D and Video S3)
PMID:38041816	PBO:0113567	whereas the CHD (aa 1-190) localized to all F-actin structures including actin cables, actin patches, and the actin ring (Figure 4C and Video S3).44,45
PMID:38041816	PBO:0094433	As expected, Rng2 localized to the nodes and ring upon entry into mitosis (Figure 4B), w
PMID:38048463	GO:0031509	(Fig. 5D)
PMID:38048463	GO:0031509	(Fig. 1H)
PMID:38048463	PBO:0093618	We found that the rex1BDΔ cells were also sensitive to MMS, but relatively mild compared with apn2Δ (SI Appendix, Fig. S4).
PMID:38048463	GO:0005634	We observed that overexpressed Rex1BD-GFP was enriched within the nucleus, consistent with its role as a heterochromatin factor (SI Appendix, Fig. S3).
PMID:38048463	PBO:0111621	Phenotype of rad25 deletion amplified by rex1BD deletion at otr3R10 (Fig. 5B)
PMID:38048463	PBO:0111621	Phenotype of rad25 deletion amplified by rex1BD deletion at otr3R10 (Fig. 5B)
PMID:38048463	PBO:0112032	(Fig. 5D)
PMID:38048463	PBO:0112031	(Fig. 5B and C)
PMID:38048463	PBO:0112030	(Fig. 4E)
PMID:38048463	PBO:0112029	(Fig. 4E)
PMID:38048463	PBO:0111621	(Fig. 4B)
PMID:38048463	PBO:0111621	(Fig. 3C)
PMID:38048463	PBO:0112027	(Fig. 3B)
PMID:38048463	PBO:0112027	(Fig. 3B)
PMID:38048463	PBO:0111621	(Fig. 3B)
PMID:38048463	PBO:0112027	(Fig. 2F)
PMID:38048463	PBO:0111621	(Fig. 1C)
PMID:38048463	PBO:0112025	(Fig. 1E)
PMID:38048463	PBO:0112188	(Fig. 4D)
PMID:38048463	PBO:0096299	(Fig. 1E)
PMID:38048463	PBO:0098772	(Fig. 1F)
PMID:38048463	FYPO:0002336	(Fig. 1G)
PMID:38048463	PBO:0097417	(Fig. 1G)
PMID:38048463	PBO:0097417	(Fig. 1G)
PMID:38048463	FYPO:0003555	(Fig. 1H)
PMID:38048463	PBO:0112026	(Fig. 1H)
PMID:38048463	PBO:0120548	(Fig. 4C)
PMID:38048463	GO:0140727	Our genetic assays revealed that Rex1BD acts in an RNAi- independent manner.
PMID:38048463	PBO:0112027	(Fig. 5D)
PMID:38048463	PBO:0112027	(Fig. 5D)
PMID:38048463	PBO:0120549	(Fig. 5C)
PMID:38048463	PBO:0112026	(Fig. 1H)
PMID:38048463	PBO:0112027	(Fig. 2E)
PMID:38051102	PBO:0110677	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110676	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110675	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110674	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110673	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0093557	The screen isolated a plasmid, pALSK53, which suppressed the ts growth phenotype and rapamycin sensitivity of the tor2-13 mutant (Fig. 1A).
PMID:38051102	PBO:0093557	The screen isolated a plasmid, pALSK53, which suppressed the ts growth phenotype and rapamycin sensitivity of the tor2-13 mutant (Fig. 1A).
PMID:38051102	PBO:0093558	The screen isolated a plasmid, pALSK53, which suppressed the ts growth phenotype and rapamycin sensitivity of the tor2-13 mutant (Fig. 1A).
PMID:38051102	PBO:0093558	Truncation of amino acids 84 to 105 or amino acids 293 to 442 of Sfp1, which removes the N-terminal or C-terminal zinc finger domains, resulted in reduced growth defect suppression in the tor2-287 mutant compared to full-length Sfp1 (Fig. 1D).
PMID:38051102	PBO:0093558	Truncation of amino acids 84 to 105 or amino acids 293 to 442 of Sfp1, which removes the N-terminal or C-terminal zinc finger domains, resulted in reduced growth defect suppression in the tor2-287 mutant compared to full-length Sfp1 (Fig. 1D).
PMID:38051102	PBO:0110572	The level of Psk1 phosphorylation was comparable between wild-type and tor2-287 cells growing at 25  C (Fig. 1E). Upon temperature shift to the restrictive temperature, dephosphorylation of Psk1 was observed with similar kinetics both in the presence and absence of Sfp1 overexpression (Fig. 1E), suggesting that Sfp1 does not affect TORC1 activity.
PMID:38051102	PBO:0110572	TORC1 activity monitored by the Psk1 phosphorylation was comparable between wild-type and Dsfp1 cells before and after nitrogen starvation (Fig. 1F), further confirming that Sfp1 does not affect TORC1 activity.
PMID:38051102	PBO:0093779	In contrast, the Dsfp1 mutant exhibited a modest growth defect as well as limited rapamycin sensitivity (Fig. 1G), consistent with the notion that Sfp1 is involved in cell proliferation regulated by TORC1.
PMID:38051102	FYPO:0001409	Although the growth defect of the Dsfp1 mutant was observed on glucose medium, it grew normally on medium containing glycerol as the carbon source (Fig. 1H), similar to the situation in budding yeast.27
PMID:38051102	PBO:0094263	Although the growth defect of the Dsfp1 mutant was observed on glucose medium, it grew normally on medium containing glycerol as the carbon source (Fig. 1H), similar to the situation in budding yeast.27. ALSO Figure 4B for severity
PMID:38051102	PBO:0094264	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	PBO:0094263	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	PBO:0094264	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	PBO:0094264	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	PBO:0094263	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	PBO:0094263	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	PBO:0110573	In the tor2-287 and tor2-13 mutants, the Sfp1 protein dramatically decreased within 2h after shifting to the restrictive temperature (Fig. 2A)
PMID:38051102	PBO:0110573	In the tor2-287 and tor2-13 mutants, the Sfp1 protein dramatically decreased within 2h after shifting to the restrictive temperature (Fig. 2A)
PMID:38051102	PBO:0110574	(SHOULD I CHANGE THIS TO DELAYED?????) The reduction of the Sfp1 protein upon nitrogen starvation was significantly delayed in the mts3-1 mutant (Fig. 2K), suggesting that the stability of Sfp1 during starvation is regulated by the proteasome.
PMID:38051102	PBO:0110575	An in vitro kinase assay using Sfp1 as a substrate indicated that Sfp1 is a substrate of TORC1 (Fig. 2M).
PMID:38051102	PBO:0110576	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110577	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110578	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110579	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110580	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110581	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110582	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110583	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110584	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110585	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110586	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110587	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110588	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110589	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110590	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110591	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110592	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110593	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110594	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110595	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110596	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110597	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110598	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110699	The Ifh1-Fhl1 association was detected both in the presence and absence of Sfp1, suggesting that Sfp1 is not required for their interaction (Fig. 4F).
PMID:38051102	PBO:0110599	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110600	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110601	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110602	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110603	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110604	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110605	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110606	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0094263	Although the growth defect of the Dsfp1 mutant was observed on glucose medium, it grew normally on medium containing glycerol as the carbon source (Fig. 1H), similar to the situation in budding yeast.27. ALSO Figure 4B for severity
PMID:38051102	PBO:0110608	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110609	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110610	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110611	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110612	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110613	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110614	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110700	It was found, however, that the amount of the Ifh1-Fhl1 complex was reduced in the Dsfp1 mutant when compared to that in the wild-type strain.
PMID:38051102	PBO:0110615	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110616	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110617	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110618	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110619	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110620	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110621	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110622	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110623	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110624	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110625	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110626	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110627	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110628	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110629	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110630	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110631	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110632	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110633	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110634	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110635	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110636	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110637	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110638	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110639	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110640	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110641	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110642	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110643	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110644	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110645	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110646	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110647	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110648	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110649	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110650	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110651	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110652	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110653	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110654	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110607	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0094263	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	PBO:0094263	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	PBO:0094263	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	PBO:0094263	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	PBO:0110698	The interaction between Fhl1 and Ifh1 was impaired in the mutant expressing Fhl1 without the N-terminal 150 amino acid residues (Fig. 4E), indicating that the Ifh1-FHl1 interaction depends on the forkhead-associated (FHA) domain of Fhl1.
PMID:38051102	PBO:0110701	When TORC1 was inactivated in the tor2-13 or tor2-287 mutants at the restrictive temperature, the electrophoretic mobility of Ifh1 was notably decreased (Fig. 6A). The slow migrating form of Ifh1 was also observed when TORC1 was inactivated in wild-type cells starved of nitrogen (Fig. 6B). Phosphatase treatment experiments confirmed that slow-migrating Ifh1 was its phosphorylated form (Fig. 6B).
PMID:38051102	PBO:0110701	When TORC1 was inactivated in the tor2-13 or tor2-287 mutants at the restrictive temperature, the electrophoretic mobility of Ifh1 was notably decreased (Fig. 6A). The slow migrating form of Ifh1 was also observed when TORC1 was inactivated in wild-type cells starved of nitrogen (Fig. 6B). Phosphatase treatment experiments confirmed that slow-migrating Ifh1 was its phosphorylated form (Fig. 6B).
PMID:38051102	GO:0005634	Remarkably, we discovered that Ifh1 accumulates in the nucleus in a TORC1- dependent manner. In wild-type cells expressing Ifh1 with the fluorescent mEGFP tag, Ifh1 appeared to be concentrated in the nucleus, with some cytoplasmic signals (Fig. 6D).
PMID:38051102	PBO:0110702	or the tor2-287 mutation (Fig. 6E), the nuclear accumulation of Ifh1 was largely lost while no change in the Ifh1 protein levels was observed (Fig. 6B), implying that TORC1 promotes the nuclear localization of Ifh
PMID:38051102	PBO:0110573	Moreover, the nuclear signal of Ifh1 was also significantly reduced in the Dsfp1 mutant (Fig. 6F), though neither the protein level nor the mobility shift of Ifh1 was affected by the Dsfp1 mutation (Fig. 6G).
PMID:38051102	GO:0005634	Fhl1 was constitutively found in the nucleus, without being affected by TORC1 inactivation (Fig. 6D) or the loss of Sfp1 (Fig. 6F).
PMID:38051102	PBO:0094263	Importantly, no significant additive phenotype was observed when the mutations were combined (Fig. 4B), suggesting that Sfp1, Ifh1, and Fhl1 function in the same pathway that regulates cell proliferation. Consistently, like the Dsfp1 mutation (Fig. 1I), the Difh1 and Dfhl1 mutations were also able to ameliorate the growth defect caused by the absence of the functional GATOR1 complex (Fig. 4C).
PMID:38051102	PBO:0110697	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110696	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110695	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110694	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110693	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110692	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110691	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110690	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110689	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110688	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110687	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110686	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110685	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110684	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110683	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110682	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110681	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110680	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110679	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110678	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110655	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110656	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110657	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110658	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110659	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110660	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110661	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110662	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110663	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110664	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110665	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110666	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110667	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110668	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110669	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110670	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110671	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	PBO:0110672	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38097609	FYPO:0001489	(Fig. 6A)
PMID:38097609	FYPO:0001357	(Fig. S6A)
PMID:38097609	FYPO:0001489	(Fig. 6A)
PMID:38097609	FYPO:0001489	(Fig. 6A)
PMID:38097609	FYPO:0001489	(Fig. S6D)
PMID:38097609	FYPO:0001489	(Fig. S6D)
PMID:38097609	FYPO:0001357	(Fig. S6C)
PMID:38097609	FYPO:0001357	(Fig. S6C)
PMID:38097609	FYPO:0001489	(Fig. S6C)
PMID:38097609	FYPO:0001489	(Fig. S6C)
PMID:38097609	FYPO:0001357	(Fig. S6A)
PMID:38097609	FYPO:0001357	(Fig. S6A)
PMID:38097609	FYPO:0001357	(Fig. S6A)
PMID:38097609	FYPO:0001489	(Fig. 6A)
PMID:38097609	FYPO:0001489	(Fig. 6A)
PMID:38097609	FYPO:0001357	(Fig. S6A)
PMID:38097609	FYPO:0001357	(Fig. S6A)
PMID:38097609	PBO:0093560	(Fig. 6A)
PMID:38097609	FYPO:0001489	(Fig. 6A)
PMID:38097609	FYPO:0001489	(Fig. 6A)
PMID:38097609	FYPO:0001489	(Fig. 6A)
PMID:38097609	FYPO:0001489	(Fig. 6A)
PMID:38133430	PBO:0094771	(Fig. 5B)
PMID:38133430	PBO:0110727	(Fig. 8B)
PMID:38133430	PBO:0108846	(Fig. 8B)
PMID:38133430	PBO:0108843	(Fig. 8B)
PMID:38133430	FYPO:0001357	(Fig. S5)
PMID:38133430	FYPO:0001357	(Fig. S5)
PMID:38133430	FYPO:0001357	(Fig. S3A)
PMID:38133430	PBO:0094738	(Fig. S3B)
PMID:38133430	FYPO:0002085	(Fig. S3A)
PMID:38133430	FYPO:0002085	(Fig. S3A)
PMID:38133430	PBO:0094738	(Fig. S3B)
PMID:38133430	FYPO:0000082	(Fig. S3A)
PMID:38133430	FYPO:0005369	(Fig. S3A)
PMID:38133430	FYPO:0001355	(Fig. S3A)
PMID:38133430	PBO:0094738	(Fig. S3B)
PMID:38133430	FYPO:0001357	(Fig. 9)
PMID:38133430	FYPO:0001357	(Fig. 9)
PMID:38133430	FYPO:0001355	(Fig. 9)
PMID:38133430	FYPO:0001355	(Fig. 9)
PMID:38133430	PBO:0110729	(Fig. 8B)
PMID:38133430	PBO:0110729	(Fig. 8B)
PMID:38133430	PBO:0110729	(Fig. 8B)
PMID:38133430	PBO:0110728	(Fig. 8B)
PMID:38133430	PBO:0110728	(Fig. 8B)
PMID:38133430	PBO:0110728	(Fig. 8B)
PMID:38133430	PBO:0110727	(Fig. 8B)
PMID:38133430	PBO:0110727	(Fig. 8B)
PMID:38133430	PBO:0108846	(Fig. 8B)
PMID:38133430	PBO:0108846	(Fig. 8B)
PMID:38133430	PBO:0108843	(Fig. 8B)
PMID:38133430	PBO:0108843	(Fig. 8B)
PMID:38133430	PBO:0094771	(Fig. 7B)
PMID:38133430	PBO:0094771	(Fig. 7B)
PMID:38133430	PBO:0094771	(Fig. 7B)
PMID:38133430	FYPO:0001357	(Fig. 7A)
PMID:38133430	FYPO:0001357	(Fig. 7A)
PMID:38133430	FYPO:0001357	(Fig. 7A)
PMID:38133430	PBO:0094738	(Fig. 6B)
PMID:38133430	PBO:0094738	(Fig. 6B)
PMID:38133430	PBO:0094771	(Fig. 6B)
PMID:38133430	PBO:0094738	(Fig. 6B)
PMID:38133430	PBO:0094738	(Fig. 6B)
PMID:38133430	FYPO:0001357	(Fig. 6A)
PMID:38133430	FYPO:0000674	(Fig. 6A)
PMID:38133430	FYPO:0002141	(Fig. 6A)
PMID:38133430	FYPO:0001357	(Fig. 6A)
PMID:38133430	FYPO:0000674	(Fig. 6A)
PMID:38133430	FYPO:0002141	(Fig. 6A)
PMID:38133430	FYPO:0000080	(Fig. 6A)
PMID:38133430	FYPO:0004481	(Fig. 6A)
PMID:38133430	FYPO:0000082	(Fig. 6A, S3A)
PMID:38133430	FYPO:0000082	(Fig. 6A, S3A)
PMID:38133430	FYPO:0005369	(Fig. 6A, S3A)
PMID:38133430	FYPO:0005369	(Fig. 6A, S3A)
PMID:38133430	FYPO:0001355	(Fig. 6A, S3A)
PMID:38133430	FYPO:0001355	(Fig. 6A, S3A)
PMID:38133430	FYPO:0002141	(Fig. 5A)
PMID:38133430	FYPO:0002141	(Fig. 5A)
PMID:38133430	FYPO:0001357	(Fig. 5A)
PMID:38133430	FYPO:0001357	(Fig. 5A)
PMID:38133430	FYPO:0001357	(Fig. 5A)
PMID:38133430	FYPO:0001357	(Fig. 5A)
PMID:38133430	FYPO:0004481	(Fig. 5A)
PMID:38133430	FYPO:0004481	(Fig. 5A)
PMID:38133430	PBO:0094771	(Fig. 5B)
PMID:38133430	FYPO:0004481	(Fig. 5A)
PMID:38133430	FYPO:0004481	(Fig. 5A)
PMID:38133430	PBO:0094777	(Fig. 4C)
PMID:38133430	PBO:0094777	(Fig. 4C)
PMID:38133430	PBO:0094738	(Fig. 4C)
PMID:38133430	PBO:0094738	(Fig. 4C)
PMID:38133430	PBO:0094738	(Fig. 4C)
PMID:38133430	PBO:0094738	(Fig. 4C, Fig. S3B)
PMID:38133430	FYPO:0001357	(Fig. 4A)
PMID:38133430	FYPO:0000080	(Fig. 4A)
PMID:38133430	FYPO:0004481	(Fig. 4A)
PMID:38133430	FYPO:0001357	(Fig. 4A)
PMID:38133430	FYPO:0001357	(Fig. 4A)
PMID:38133430	FYPO:0001357	(Fig. 4A)
PMID:38133430	FYPO:0001357	(Fig. 4A)
PMID:38133430	FYPO:0000082	(Fig. 4A)
PMID:38133430	FYPO:0005369	(Fig. 4A)
PMID:38133430	FYPO:0001357	(Fig. 4A)
PMID:38133430	FYPO:0001357	(Fig. 4A)
PMID:38133430	FYPO:0001357	(Fig. 4A)
PMID:38133430	FYPO:0001357	(Fig. 4A)
PMID:38133430	FYPO:0001357	(Fig. 4A)
PMID:38133430	FYPO:0001357	(Fig. 4A)
PMID:38133430	FYPO:0001357	(Fig. 4A)
PMID:38133430	FYPO:0001357	(Fig. 4A)
PMID:38133430	FYPO:0001357	(Fig. 4A)
PMID:38133430	PBO:0094738	(Fig. 4C, S3B)
PMID:38133430	FYPO:0000082	(Fig. 4A, Fig. S3A)
PMID:38133430	FYPO:0000082	(Fig. 4A, Fig. S3A)
PMID:38133430	FYPO:0005369	(Fig. 4A, Fig. S3A)
PMID:38133430	FYPO:0005369	(Fig. 4A, Fig. S3A)
PMID:38133430	PBO:0110726	(Fig. 3B)
PMID:38133430	PBO:0110725	(Fig. 3B)
PMID:38133430	PBO:0108867	(Fig. 3B)
PMID:38133430	PBO:0108864	(Fig. 3B)
PMID:38133430	PBO:0096777	(Fig. 3B)
PMID:38133430	PBO:0108863	(Fig. 3B)
PMID:38133430	PBO:0110726	(Fig. 3B)
PMID:38133430	PBO:0110725	(Fig. 3B)
PMID:38133430	PBO:0108867	(Fig. 3B)
PMID:38133430	PBO:0108864	(Fig. 3B)
PMID:38133430	PBO:0096777	(Fig. 3B)
PMID:38133430	PBO:0108863	(Fig. 3B)
PMID:38133430	FYPO:0001357	(Fig. 2, Fig. 4A, Fig. S3A)
PMID:38133430	FYPO:0001357	(Fig. 2, Fig. 4A, Fig. S3A)
PMID:38133430	FYPO:0001355	(Fig. 2, Fig. 4A, Fig. S3A)
PMID:38133430	FYPO:0001355	(Fig. 2, Fig. 4A, Fig. S3A)
PMID:38166399	PBO:0093556	As shown in electronic supplementary material, Figure S1B, introduction of deletion for mad2+ did not cause the lethality in the cdc2-1w and cdc2-3w mutants.
PMID:38166399	PBO:0093556	As shown in electronic supplementary material, Figure S1B, introduction of deletion for mad2+ did not cause the lethality in the cdc2-1w and cdc2-3w mutants.
PMID:38166399	PBO:0110821	Time-lapse imaging analysis revealed abnormal positioning of kinetochores in the wee1 (wee1Δ) mutant. ThBecause the kinetochores, which are captured and bioriented, are clustered and found on the spindle, the satellite kinetochores remained unattached, or detached from the spindle during the progression to anaphase in the wee1 mutant (electronic supplementary material, Figure S2).e cluster of kinetochores frequently fell apart into a main cluster and a small ‘satellite kinetochore’ during mitosis (Figure 1b).
PMID:38166399	FYPO:0000324	Importantly, the onset of anaphase was postponed until all the satellite kinetochores merged with the main cluster in the mutant (Figure 2a,b).
PMID:38166399	FYPO:0000730	Importantly, the onset of anaphase was postponed until all the satellite kinetochores merged with the main cluster in the mutant (Figure 2a,b).
PMID:38166399	PBO:0110822	Importantly, the onset of anaphase was postponed until all the satellite kinetochores merged with the main cluster in the mutant (Figure 2a,b).
PMID:38166399	FYPO:0002638	As mitosis progressed, it was faintly found on the entire length of the spindle and SPB in the wild-type cells (Figure 3a). By contrast, Mad2 was found as one or two bright speckles in the vicinity of the spindle during mitosis in the wee1 mutant (Figure 3b,c). Judged by the length of the spindle, anaphase was initiated soon after Mad2 speckles disappeared (Figure 4a,b). In approximately 28% (28 cells out of 101 cells observed) of the wee1 mutants, the Mad2 speckle appeared at least once (Figure 4c). The observation thus suggested that the spindle checkpoint was activated in the wee1 mutants.
PMID:38166399	PBO:0037150	s shown in Figure 5, the wee1 mutants with no functional spindle checkpoint indeed failed in accurate chromosome segregation and generated two sister cells with unequal nuclear size.
PMID:38166399	PBO:0094567	s shown in Figure 5, the wee1 mutants with no functional spindle checkpoint indeed failed in accurate chromosome segregation and generated two sister cells with unequal nuclear size.
PMID:38166399	PBO:0110823	s shown in Figure 5, the wee1 mutants with no functional spindle checkpoint indeed failed in accurate chromosome segregation and generated two sister cells with unequal nuclear size.
PMID:38166399	PBO:0094567	s shown in Figure 5, the wee1 mutants with no functional spindle checkpoint indeed failed in accurate chromosome segregation and generated two sister cells with unequal nuclear size.
PMID:38166399	FYPO:0002061	As shown in electronic supplementary material, Figure S1A, we found that a wee1-50 mad2Δ double mutant is lethal at 36°C.
PMID:38166399	FYPO:0002061	As shown in electronic supplementary material, Figure S1A, we found that a wee1-50 mad2Δ double mutant is lethal at 36°C.
PMID:38181050	PBO:0112716	The western blot results suggest that the loss of any member of CLRC complex enhances the protein amount of Lsd1 (Fig 3C) or Lsd2 (Fig 3D).
PMID:38181050	PBO:0112716	The western blot results suggest that the loss of any member of CLRC complex enhances the protein amount of Lsd1 (Fig 3C) or Lsd2 (Fig 3D).
PMID:38181050	PBO:0112716	that without Clr4, both Lsd1-FTP and Lsd2-FTP show an increase in protein levels, compared to the wild-type cells (Fig 2I).
PMID:38181050	FYPO:0002061	lsd1-ΔHMG set1Δ and lsd2-ΔC clr4Δ double mutants resulted in inviable daughter cells, suggesting that Lsd1 has essential overlapping functions with Set1, while Lsd2 has critical overlapping roles with Clr4 (Fig 2A).
PMID:38181050	FYPO:0002061	lsd1-ΔHMG set1Δ and lsd2-ΔC clr4Δ double mutants resulted in inviable daughter cells, suggesting that Lsd1 has essential overlapping functions with Set1, while Lsd2 has critical overlapping roles with Clr4 (Fig 2A).
PMID:38181050	FYPO:0002061	lsd1-ΔHMG set1Δ and lsd2-ΔC clr4Δ double mutants resulted in inviable daughter cells, suggesting that Lsd1 has essential overlapping functions with Set1, while Lsd2 has critical overlapping roles with Clr4 (Fig 2A).
PMID:38181050	FYPO:0002061	lsd1-ΔHMG set1Δ and lsd2-ΔC clr4Δ double mutants resulted in inviable daughter cells, suggesting that Lsd1 has essential overlapping functions with Set1, while Lsd2 has critical overlapping roles with Clr4 (Fig 2A).
PMID:38181050	PBO:0112715	Notably, the localizations of Lsd1 and Lsd2 are diminished at the promoter regions in the absence of a functional C-terminus (Fig 1C). This result demonstrates that the C-terminal domains of Lsd1 and Lsd2 are involved in their chromatin binding at these regions.
PMID:38181050	PBO:0112715	Notably, the localizations of Lsd1 and Lsd2 are diminished at the promoter regions in the absence of a functional C-terminus (Fig 1C). This result demonstrates that the C-terminal domains of Lsd1 and Lsd2 are involved in their chromatin binding at these regions.
PMID:38181050	PBO:0112714	We also observed that the loss of the C-terminus of Lsd2 does not disrupt the interactions between Lsd2 and Phf1 (Fig 1F) or Phf2 (Fig 1G).
PMID:38181050	PBO:0112713	Additionally, we established that the loss of the HMG-domain of Lsd1 does not affect the interaction between Lsd1 and Phf1 (Fig 1D) or Phf2 (Fig 1E)
PMID:38181050	PBO:0112720	In contrast, the protein levels of Lsd1-FTP and Lsd2-FTP show a notable decrease in the absence of Set1 (Fig 2I).
PMID:38181050	PBO:0112719	loss of most members of the COMPASS complex, including Set1, Spp1, Swd1, Swd3, Swd2, and Ash2 leads to a significantly decreased amount of Lsd1 protein (Fig 3A)
PMID:38181050	PBO:0112719	loss of most members of the COMPASS complex, including Set1, Spp1, Swd1, Swd3, Swd2, and Ash2 leads to a significantly decreased amount of Lsd1 protein (Fig 3A)
PMID:38181050	PBO:0112719	loss of most members of the COMPASS complex, including Set1, Spp1, Swd1, Swd3, Swd2, and Ash2 leads to a significantly decreased amount of Lsd1 protein (Fig 3A)
PMID:38181050	PBO:0112719	loss of most members of the COMPASS complex, including Set1, Spp1, Swd1, Swd3, Swd2, and Ash2 leads to a significantly decreased amount of Lsd1 protein (Fig 3A)
PMID:38181050	PBO:0112719	loss of most members of the COMPASS complex, including Set1, Spp1, Swd1, Swd3, Swd2, and Ash2 leads to a significantly decreased amount of Lsd1 protein (Fig 3A)
PMID:38181050	PBO:0112719	In contrast, the protein levels of Lsd1-FTP and Lsd2-FTP show a notable decrease in the absence of Set1 (Fig 2I).
PMID:38181050	PBO:0112718	The western blot results suggest that the loss of any member of CLRC complex enhances the protein amount of Lsd1 (Fig 3C) or Lsd2 (Fig 3D).
PMID:38181050	PBO:0112726	Additionally, we established that the loss of the HMG-domain of Lsd1 does not affect the interaction between Lsd1 and Phf1 (Fig 1D) or Phf2 (Fig 1E)
PMID:38181050	GO:1990841	Previous studies have shown that Lsd1/2 proteins bind to the promoters of a few hundred genes [70,73,74], suggesting that Lsd1/2 proteins are selectively recruited to those genes. Our ChIP-Seq analysis yields a highly similar set of genomic loci where Lsd1 and Lsd2 are enriched just upstream of the transcriptional start site (TSS) (Fig 1C). This result indicates that Lsd1 and Lsd2 mostly bind to the promoter region of genes and are likely to cooperate with other transcription factors that are involved in regulating gene expression.
PMID:38181050	GO:1990841	Previous studies have shown that Lsd1/2 proteins bind to the promoters of a few hundred genes [70,73,74], suggesting that Lsd1/2 proteins are selectively recruited to those genes. Our ChIP-Seq analysis yields a highly similar set of genomic loci where Lsd1 and Lsd2 are enriched just upstream of the transcriptional start site (TSS) (Fig 1C). This result indicates that Lsd1 and Lsd2 mostly bind to the promoter region of genes and are likely to cooperate with other transcription factors that are involved in regulating gene expression.
PMID:38181050	FYPO:0002061	Notably, deletion of the Lsd2 HMG-domain results in lethality akin to that in the complete loss of Lsd2, which further implies the unknown and important functions of the C-terminus of these two proteins
PMID:38181050	PBO:0112725	At 37 ̊C, only marginal changes in Lsd1 protein levels were observed in H3K4R and H2B-K119R mutants (Fig 6D). However, a significant reduction of Lsd2 was seen in both H3K4R and H2B K119R mutants (Fig 6E)
PMID:38181050	PBO:0112725	(Figure 6)
PMID:38181050	PBO:0112728	To our surprise, clr4Δ increases the enrichments of Lsd1/2 while set1Δ decreases the enrichments of Lsd1 at its enriched genomic loci (Figs 2G, 2H, S6 and S7).
PMID:38181050	PBO:0112729	To our surprise, clr4Δ increases the enrichments of Lsd1/2 while set1Δ decreases the enrichments of Lsd1 at its enriched genomic loci (Figs 2G, 2H, S6 and S7).
PMID:38181050	PBO:0112722	Lsd1 (Fig 4A) or Lsd2 (Fig 4B) was detected in the presence of a temperature-sensitive 26S proteasome subunit mutant, mts2-1, which inactivates the proteasome at 33 ̊C [111] and thereby stabilizes Lsd1 and Lsd2 (Fig 4A and 4B).
PMID:38181050	PBO:0112721	Lsd1 (Fig 4A) or Lsd2 (Fig 4B) was detected in the presence of a temperature-sensitive 26S proteasome subunit mutant, mts2-1, which inactivates the proteasome at 33 ̊C [111] and thereby stabilizes Lsd1 and Lsd2 (Fig 4A and 4B).
PMID:38181050	PBO:0112720	A similar pattern was observed in the Lsd2 samples, although the Lsd2 protein levels also decreased with shg1Δ (Fig 3B).
PMID:38181050	PBO:0112720	A similar pattern was observed in the Lsd2 samples, although the Lsd2 protein levels also decreased with shg1Δ (Fig 3B).
PMID:38181050	PBO:0112717	The western blot results suggest that the loss of any member of CLRC complex enhances the protein amount of Lsd1 (Fig 3C) or Lsd2 (Fig 3D).
PMID:38181050	PBO:0112717	that without Clr4, both Lsd1-FTP and Lsd2-FTP show an increase in protein levels, compared to the wild-type cells (Fig 2I).
PMID:38181050	PBO:0112720	A similar pattern was observed in the Lsd2 samples, although the Lsd2 protein levels also decreased with shg1Δ (Fig 3B).
PMID:38181050	PBO:0112720	A similar pattern was observed in the Lsd2 samples, although the Lsd2 protein levels also decreased with shg1Δ (Fig 3B).
PMID:38181050	PBO:0112720	A similar pattern was observed in the Lsd2 samples, although the Lsd2 protein levels also decreased with shg1Δ (Fig 3B).
PMID:38181050	PBO:0112720	A similar pattern was observed in the Lsd2 samples, although the Lsd2 protein levels also decreased with shg1Δ (Fig 3B).
PMID:38181050	PBO:0112716	Loss of Ddb1 slightly enhances the Lsd1-FTP level, while having no significant effect on the Lsd2-FTP level (Fig 3E).
PMID:38181050	PBO:0112716	The western blot results suggest that the loss of any member of CLRC complex enhances the protein amount of Lsd1 (Fig 3C) or Lsd2 (Fig 3D).
PMID:38181050	PBO:0112724	(Figure 6)
PMID:38181050	PBO:0112724	(Figure 6)
PMID:38181050	PBO:0112723	(Figure 6)
PMID:38181050	PBO:0112723	(Figure 6)
PMID:38181050	PBO:0112724	However, without Set1, Lsd1/2 protein levels are no longer upregulated during heat stress (Fig 4C and 4D), which implies that Set1 is required to elevate the protein levels of Lsd1 and Lsd2 under heat stress.
PMID:38181050	PBO:0112723	Although no significant alterations were detected for Flag-Set1 protein levels between wild-type and clr4W31G cells at 30 ̊C, the elevated Flag-Set1 is less pronounced in clr4W31G compared to clr4Δ at 37 ̊C (Fig 5B)
PMID:38181050	PBO:0112718	Both cul4-1 or ddb1Δ enhanced the amount of Set1 protein, indicating that both CLRC and CRL4 complexes modulate Set1 levels (Fig 5C)
PMID:38181050	PBO:0112718	We found that the loss of any members in CLRC promotes the protein levels of Set1, both at 30 ̊C or 37 ̊C (Fig 5A), indicating that the intact CLRC restricts the amount of Set1.
PMID:38181050	PBO:0112718	We found that the loss of any members in CLRC promotes the protein levels of Set1, both at 30 ̊C or 37 ̊C (Fig 5A), indicating that the intact CLRC restricts the amount of Set1.
PMID:38181050	PBO:0112718	We found that the loss of any members in CLRC promotes the protein levels of Set1, both at 30 ̊C or 37 ̊C (Fig 5A), indicating that the intact CLRC restricts the amount of Set1.
PMID:38181050	PBO:0095652	(Fig. S1E)
PMID:38181050	PBO:0112725	At 37 ̊C, only marginal changes in Lsd1 protein levels were observed in H3K4R and H2B-K119R mutants (Fig 6D). However, a significant reduction of Lsd2 was seen in both H3K4R and H2B K119R mutants (Fig 6E)
PMID:38181050	PBO:0112740	Set1 significantly at 37 ̊C compared to that at 30 ̊C, which is due to the temperature sensitive nature of cul4-1.
PMID:38181050	PBO:0112740	Protein levels of Lsd1 and Lsd2 are similar between wild-type and clr4Δ cells at 37 ̊C, indicating that Clr4 is not responsible for Lsd1/2 upregulation in this condition (Fig 4C and 4D)
PMID:38181050	PBO:0112738	Intriguingly, about 72% of downregulated genes in lsd1-ΔHMG, lsd2-ΔC, and set1Δ are antisense non-coding RNAs (S1 Table)
PMID:38181050	PBO:0112739	Intriguingly, about 72% of downregulated genes in lsd1-ΔHMG, lsd2-ΔC, and set1Δ are antisense non-coding RNAs (S1 Table)
PMID:38181050	PBO:0112738	Intriguingly, about 72% of downregulated genes in lsd1-ΔHMG, lsd2-ΔC, and set1Δ are antisense non-coding RNAs (S1 Table)
PMID:38181050	PBO:0112738	Intriguingly, about 72% of downregulated genes in lsd1-ΔHMG, lsd2-ΔC, and set1Δ are antisense non-coding RNAs (S1 Table)
PMID:38181050	PBO:0112737	Under heat stress (37 ̊C), it was consistently found that ubiquitination of Lsd1 and Lsd2 is drastically enhanced in set1Δ cells, even without mts2-1 as a background (Fig 4F)
PMID:38181050	PBO:0112736	Under heat stress (37 ̊C), it was consistently found that ubiquitination of Lsd1 and Lsd2 is drastically enhanced in set1Δ cells, even without mts2-1 as a background (Fig 4F)
PMID:38181050	PBO:0112735	In wild-type cells, we observed a significantly increased amount of Set1 at 37 ̊C (Fig 6A), indicating that Set1 is also stabilized during heat stress.
PMID:38181050	PBO:0112725	However, without Set1, Lsd1/2 protein levels are no longer upregulated during heat stress (Fig 4C and 4D), which implies that Set1 is required to elevate the protein levels of Lsd1 and Lsd2 under heat stress.
PMID:38181050	PBO:0112734	Protein levels of Lsd1 and Lsd2 are similar between wild-type and clr4Δ cells at 37 ̊C, indicating that Clr4 is not responsible for Lsd1/2 upregulation in this condition (Fig 4C and 4D)
PMID:38181050	PBO:0112733	Protein levels of Lsd1 and Lsd2 are similar between wild-type and clr4Δ cells at 37 ̊C, indicating that Clr4 is not responsible for Lsd1/2 upregulation in this condition (Fig 4C and 4D)
PMID:38181050	PBO:0098997	The triple mutants lsd1- ΔHMG set1Δ clr4Δ and lsd2-ΔC set1Δ clr4Δ are lethal (S1D Fig).
PMID:38181050	PBO:0098997	The triple mutants lsd1- ΔHMG set1Δ clr4Δ and lsd2-ΔC set1Δ clr4Δ are lethal (S1D Fig).
PMID:38181050	PBO:0093560	lsd1-ΔHMG clr4Δ cells are viable but sick, which implies a negative genetic interaction between Lsd1 and Clr4 (Figs 2A and S1B).
PMID:38181050	PBO:0093560	lsd1-ΔHMG clr4Δ cells are viable but sick, which implies a negative genetic interaction between Lsd1 and Clr4 (Figs 2A and S1B).
PMID:38181050	PomGeneEx:0000018	Both Lsd1 (Fig 4C) and Lsd2 (Fig 4D) protein levels drastically increase after heat treatment, although the mRNA levels of Lsd1 and Lsd2 were not significantly altered between wild-type and set1Δ cells (S10 Fig), suggesting that enhanced Lsd1/2 proteins are required for cell survival under heat stress [61].
PMID:38181050	PomGeneEx:0000018	Both Lsd1 (Fig 4C) and Lsd2 (Fig 4D) protein levels drastically increase after heat treatment, although the mRNA levels of Lsd1 and Lsd2 were not significantly altered between wild-type and set1Δ cells (S10 Fig), suggesting that enhanced Lsd1/2 proteins are required for cell survival under heat stress [61].
PMID:38181050	PBO:0112717	The western blot results suggest that the loss of any member of CLRC complex enhances the protein amount of Lsd1 (Fig 3C) or Lsd2 (Fig 3D).
PMID:38181050	GO:0003713	The Lsd2-BD and Phf1-BD strains could self-activate the reporter genes without Gal4 activating domain, suggesting that Lsd2 and Phf1 alone could recruit basal transcriptional factors to initiate reporter gene transcription (S4 Fig).
PMID:38181050	PBO:0112732	However, the loss of Shg1 and Sdc1 seems to have little or no effect on Lsd1 protein levels.
PMID:38181050	PBO:0112731	However, the loss of Shg1 and Sdc1 seems to have little or no effect on Lsd1 protein levels.
PMID:38181050	PBO:0112730	To our surprise, clr4Δ increases the enrichments of Lsd1/2 while set1Δ decreases the enrichments of Lsd1 at its enriched genomic loci (Figs 2G, 2H, S6 and S7).
PMID:38181050	PBO:0112718	(Fig 5A)
PMID:38181050	PBO:0095652	(Fig. S1E)
PMID:38181050	PBO:0095652	(Fig. S1E)
PMID:38181050	GO:0003713	The Lsd2-BD and Phf1-BD strains could self-activate the reporter genes without Gal4 activating domain, suggesting that Lsd2 and Phf1 alone could recruit basal transcriptional factors to initiate reporter gene transcription (S4 Fig).
PMID:38181050	PBO:0112727	We also observed that the loss of the C-terminus of Lsd2 does not disrupt the interactions between Lsd2 and Phf1 (Fig 1F) or Phf2 (Fig 1G).
PMID:38181050	PBO:0112725	(Figure 6)
PMID:38188419	PBO:0093579	(Fig. 1G)
PMID:38188419	PBO:0114646	(Fig. 1F)
PMID:38188419	PBO:0093580	(Fig. 1G)
PMID:38188419	PBO:0093581	(Fig. 1G)
PMID:38188419	PBO:0093580	(Fig. 1G)
PMID:38188419	PBO:0093579	(Fig. 1G)
PMID:38188419	PBO:0093580	(Fig. 1A)
PMID:38188419	FYPO:0000963	(Fig. 1A)
PMID:38188419	PBO:0114645	(Fig. 1D)
PMID:38188419	FYPO:0000957	(Fig. 1D)
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112487	Table S3
PMID:38269097	PBO:0112487	Table S3
PMID:38269097	PBO:0112487	Table S3
PMID:38269097	FYPO:0000674	(Figure 2)
PMID:38269097	PBO:0093556	(Figure 2)
PMID:38269097	PBO:0093556	(Figure 2)
PMID:38269097	FYPO:0000674	(Figure 2)
PMID:38269097	FYPO:0002672	(Figure 1)
PMID:38269097	PBO:0093558	We serendipitously discovered that fission yeast cells exhibit significant proliferation even at 38°C and 39°C, but not at 40°C, on agar medium supplemented with rapamycin, a TORC1-specific inhibitor [...] the fkh1 null mutant failed to grow at 39°C even in the presence of rapamycin. Figure 1
PMID:38269097	PBO:0112336	(Figure 1)
PMID:38269097	PBO:0112338	(Figure 1)
PMID:38269097	PBO:0112337	(Figure 1)
PMID:38269097	PBO:0112336	(Figure 2 and 3)
PMID:38269097	PBO:0112337	(Figure 3)
PMID:38269097	PBO:0112336	(Figure 3)
PMID:38269097	PBO:0112337	(Figure 3)
PMID:38269097	FYPO:0000674	(Figure 2 and 3)
PMID:38269097	PBO:0112336	(Figure 2)
PMID:38269097	PBO:0092185	(Figure 2)
PMID:38269097	PBO:0112338	(Figure 3)
PMID:38269097	PBO:0112487	Table S3
PMID:38269097	PBO:0112487	Table S3
PMID:38269097	PBO:0112487	Table S3
PMID:38269097	PBO:0112487	Table S3
PMID:38269097	PBO:0112487	Table S3
PMID:38269097	PBO:0112487	Table S3
PMID:38269097	PBO:0112487	Table S3
PMID:38269097	PBO:0112487	Table S3
PMID:38269097	PBO:0093561	(Figure 3)
PMID:38269097	PBO:0112336	(Figure 4)
PMID:38269097	PBO:0112337	(Figure 4)
PMID:38269097	PBO:0112487	Table S3
PMID:38269097	PBO:0112487	Table S3
PMID:38269097	PBO:0112394	(Fig. 4C)
PMID:38269097	PBO:0093561	(Figure 3)
PMID:38269097	FYPO:0001357	(Figure 1)
PMID:38269097	FYPO:0001357	(Figure 1)
PMID:38269097	FYPO:0001357	(Figure 1)
PMID:38269097	PBO:0112393	(Fig. 2C)
PMID:38269097	FYPO:0001357	(Figure 1)
PMID:38269097	PBO:0093556	(Figure 2)
PMID:38269097	PBO:0112393	(Fig. 2C)
PMID:38269097	PBO:0112392	Table S2
PMID:38269097	PBO:0112391	Table S2
PMID:38269097	PBO:0112390	Table S2
PMID:38269097	PBO:0112389	Table S2
PMID:38269097	PBO:0112388	Table S2
PMID:38269097	PBO:0112387	Table S2
PMID:38269097	PBO:0112386	Table S2
PMID:38269097	PBO:0112385	Table S2
PMID:38269097	PBO:0112384	Table S2
PMID:38269097	PBO:0112383	Table S2
PMID:38269097	PBO:0112382	Table S2
PMID:38269097	PBO:0112381	Table S2
PMID:38269097	PBO:0112380	Table S2
PMID:38269097	PBO:0112486	(Figure 5)
PMID:38269097	PBO:0092105	(Figure 5)
PMID:38269097	PBO:0112339	(Figure 5)
PMID:38269097	PBO:0112336	(Figure 6)
PMID:38269097	PBO:0112379	Table S2
PMID:38269097	PBO:0112378	Table S2
PMID:38269097	PBO:0112377	Table S2
PMID:38269097	PBO:0112376	Table S2
PMID:38269097	PBO:0112375	Table S2
PMID:38269097	PBO:0112374	Table S2
PMID:38269097	PBO:0112373	Table S2
PMID:38269097	PBO:0112372	Table S2
PMID:38269097	PBO:0112371	Table S2
PMID:38269097	PBO:0112370	Table S2
PMID:38269097	PBO:0112369	Table S2
PMID:38269097	PBO:0112368	Table S2
PMID:38269097	PBO:0112367	Table S2
PMID:38269097	PBO:0112366	Table S2
PMID:38269097	PBO:0112365	Table S2
PMID:38269097	PBO:0112364	Table S2
PMID:38269097	PBO:0112336	(Figure 6)
PMID:38269097	PBO:0112336	(Figure 6)
PMID:38269097	PBO:0112338	(Figure 6)
PMID:38269097	PBO:0112336	(Figure 6)
PMID:38269097	PBO:0112336	(Figure 6)
PMID:38269097	FYPO:0001357	(Figure 2 and 3)
PMID:38269097	FYPO:0002141	(Figure S3)
PMID:38269097	FYPO:0001357	(Figure 3)
PMID:38269097	FYPO:0001357	(Figure 2)
PMID:38269097	FYPO:0001357	(Figure 2)
PMID:38269097	FYPO:0001357	(Figure 2)
PMID:38269097	FYPO:0001357	(Figure 2)
PMID:38269097	PBO:0093559	(Figure 4)
PMID:38269097	PBO:0093557	(Figure 4)
PMID:38269097	PBO:0093556	(Figure 4)
PMID:38269097	FYPO:0001357	(Figure 4)
PMID:38269097	FYPO:0001357	(Figure 4)
PMID:38269097	FYPO:0000674	(Figure 4)
PMID:38269097	FYPO:0000674	(Figure 4)
PMID:38269097	MOD:00696	(Figure S3)
PMID:38269097	FYPO:0002141	(Figure S3)
PMID:38269097	FYPO:0002141	(Figure S3)
PMID:38269097	FYPO:0002141	(Figure S3)
PMID:38269097	PBO:0112336	(Figure 6)
PMID:38269097	PBO:0112337	(Figure 6)
PMID:38269097	PBO:0112336	(Figure 6)
PMID:38269097	PBO:0112337	(Figure 6)
PMID:38269097	PBO:0112336	(Figure 6)
PMID:38269097	PBO:0112336	(Figure 6)
PMID:38269097	PBO:0112336	(Figure 6)
PMID:38269097	PBO:0112336	(Figure 6)
PMID:38269097	PBO:0092185	(Figure S2)
PMID:38269097	PBO:0112340	(Fig. S7)
PMID:38269097	PBO:0112340	(Fig. 6A)
PMID:38269097	PBO:0112341	(Fig. 6A)
PMID:38269097	PBO:0112340	(Fig. 6A)
PMID:38269097	PBO:0112340	(Fig. 6A)
PMID:38269097	PBO:0112340	(Fig. S7)
PMID:38269097	PBO:0112340	(Fig. S7)
PMID:38269097	PBO:0112340	(Fig. S7)
PMID:38269097	PBO:0112340	(Fig. S7)
PMID:38269097	PBO:0112340	(Fig. S7)
PMID:38269097	PBO:0112340	(Fig. S7)
PMID:38269097	PBO:0112340	(Fig. S7)
PMID:38269097	PBO:0112340	(Fig. S7)
PMID:38269097	PBO:0112340	(Fig. S7)
PMID:38269097	PBO:0112340	(Fig. S7)
PMID:38269097	PBO:0112342	(Fig. 6A)
PMID:38269097	PBO:0112343	(Figure 5)
PMID:38269097	PBO:0112344	(Figure 5)
PMID:38269097	PBO:0112345	(Figure S3)
PMID:38269097	PBO:0112345	(Figure S3)
PMID:38269097	PBO:0112346	(Figure S6)
PMID:38269097	PBO:0112346	(Figure S6)
PMID:38269097	PBO:0112337	(Figure 3)
PMID:38269097	PBO:0112336	(Figure S4)
PMID:38269097	PBO:0112336	(Figure S4)
PMID:38269097	PBO:0112336	(Figure S4)
PMID:38269097	PBO:0112336	(Figure S4)
PMID:38269097	PBO:0112336	(Figure 3)
PMID:38269097	PBO:0112347	Table S4
PMID:38269097	PBO:0112348	Table S4
PMID:38269097	PBO:0112349	Table S4
PMID:38269097	PBO:0112350	Table S4
PMID:38269097	PBO:0112351	Table S2
PMID:38269097	PBO:0112352	Table S2
PMID:38269097	PBO:0112353	Tabls S2
PMID:38269097	PBO:0112354	Table S2
PMID:38269097	PBO:0112355	Table S2
PMID:38269097	PBO:0112356	Table S2
PMID:38269097	PBO:0112357	Table S2
PMID:38269097	PBO:0112358	Table S2
PMID:38269097	PBO:0112359	Table S2
PMID:38269097	PBO:0112360	Table S2
PMID:38269097	PBO:0112361	Table S2
PMID:38269097	PBO:0112362	Table S2
PMID:38269097	PBO:0112363	Table S2
PMID:38269097	PBO:0112340	(Fig. 6A)
PMID:38269097	FYPO:0001357	(Figure 6)
PMID:38269097	FYPO:0001357	(Figure 6)
PMID:38269097	FYPO:0001357	(Figure 6)
PMID:38269097	FYPO:0001357	(Figure 6)
PMID:38269097	FYPO:0001357	(Figure 6)
PMID:38269097	FYPO:0001357	(Figure 6)
PMID:38269097	FYPO:0001357	(Figure 6)
PMID:38269097	PBO:0112338	(Figure 6)
PMID:38269097	PBO:0112337	(Figure 6)
PMID:38269097	FYPO:0002141	(Figure S3)
PMID:38269097	FYPO:0002141	(Figure S3)
PMID:38269097	FYPO:0002141	(Figure S3)
PMID:38269097	FYPO:0002141	(Figure S3)
PMID:38269097	FYPO:0001357	(Figure S4)
PMID:38269097	FYPO:0001357	(Figure S4)
PMID:38269097	FYPO:0001357	(Figure S4)
PMID:38269097	FYPO:0001357	(Figure S4)
PMID:38269097	FYPO:0001357	(Figure 6)
PMID:38269097	FYPO:0001357	(Figure 6)
PMID:38269097	FYPO:0001357	(Figure 6)
PMID:38269097	FYPO:0001357	(Figure 6)
PMID:38269097	FYPO:0000674	(Fig. 6D)
PMID:38269097	FYPO:0001357	(Fig. 6D)
PMID:38269097	FYPO:0001357	(Figure 6)
PMID:38269097	FYPO:0001357	(Figure 6)
PMID:38269097	FYPO:0001357	(Figure 6)
PMID:38269097	FYPO:0001357	(Figure 6)
PMID:38269097	FYPO:0001357	(Fig. 6B)
PMID:38269097	FYPO:0000674	(Fig. 6B)
PMID:38269097	FYPO:0001357	(Fig. 6B)
PMID:38269097	FYPO:0000674	(Fig. 6B)
PMID:38269097	FYPO:0001357	(Fig. 6B)
PMID:38269097	FYPO:0000674	(Figure 4)
PMID:38269097	FYPO:0001357	(Figure 4)
PMID:38269097	FYPO:0000674	(Figure 4)
PMID:38269097	FYPO:0001357	(Figure 4)
PMID:38269097	FYPO:0001357	(Figure 4)
PMID:38269097	FYPO:0001357	(Figure 4)
PMID:38269097	FYPO:0001357	(Figure 4)
PMID:38269097	FYPO:0001357	(Figure 3)
PMID:38269097	FYPO:0001357	(Figure 3)
PMID:38269097	FYPO:0000674	(Figure 3)
PMID:38269097	FYPO:0001357	(Figure 3)
PMID:38269097	FYPO:0000674	(Figure 3)
PMID:38269097	FYPO:0001357	(Figure 3)
PMID:38269097	FYPO:0001357	(Figure 3)
PMID:38269097	FYPO:0000674	(Figure 3)
PMID:38269097	FYPO:0001357	(Figure 3)
PMID:38269097	FYPO:0001357	(Figure 3)
PMID:38269097	FYPO:0000674	(Figure 3)
PMID:38269097	FYPO:0001357	(Figure 2)
PMID:38269097	FYPO:0001357	(Figure 2)
PMID:38269097	FYPO:0001357	(Figure 2)
PMID:38269097	FYPO:0000674	(Figure 2)
PMID:38269097	FYPO:0001357	(Figure 2)
PMID:38269097	FYPO:0000674	(Figure 2)
PMID:38269097	FYPO:0001357	(Figure 2)
PMID:38269097	FYPO:0000674	(Figure 2)
PMID:38269097	FYPO:0001357	(Figure 2)
PMID:38269097	FYPO:0000674	(Figure 2)
PMID:38269097	FYPO:0001357	(Figure 2 and 3)
PMID:38269097	FYPO:0000674	(Figure 1)
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38272226	PBO:0116373	(Fig. 3C)
PMID:38272226	PBO:0095252	Php4 degraded in stationary phase (Fig. 1A)
PMID:38272226	PBO:0116343	(Fig. 1B)
PMID:38272226	PBO:0116344	(Fig. 2B)
PMID:38272226	PBO:0116344	(Fig. 2B)
PMID:38272226	PBO:0116345	(Fig. 2B)
PMID:38272226	PBO:0116345	(Fig. 2C)
PMID:38272226	PBO:0116345	(Fig. 2C)
PMID:38272226	PBO:0116346	(Fig. 2D)
PMID:38272226	PBO:0116345	(Fig. 3A and 3E)
PMID:38272226	PBO:0116347	(Fig. 3C)
PMID:38272226	PBO:0116346	(Fig. 3D)
PMID:38272226	PBO:0116348	(Fig. 3F)
PMID:38272226	PBO:0116349	(Fig. 4B)
PMID:38272226	PBO:0116350	(Fig. 4B)
PMID:38272226	PBO:0116351	(Fig. 4B)
PMID:38272226	PBO:0116352	(Fig. 4B)
PMID:38272226	PBO:0116353	(Fig. 4B)
PMID:38272226	PBO:0116354	(Fig. 4C)
PMID:38272226	PBO:0116355	(Fig. 4C)
PMID:38272226	PBO:0116356	(Fig. 4C)
PMID:38272226	PBO:0116357	(Fig. 4C)
PMID:38272226	PBO:0116358	(Fig. 4C)
PMID:38272226	PBO:0116359	(Fig. 4B)
PMID:38272226	PBO:0116360	(Fig. 4B)
PMID:38272226	PBO:0116361	(Fig. 4B)
PMID:38272226	PBO:0116362	(Fig. 4B)
PMID:38272226	PBO:0116363	(Fig. 4B)
PMID:38272226	PBO:0116364	(Fig. 4C)
PMID:38272226	PBO:0116365	(Fig. 4C)
PMID:38272226	PBO:0116366	(Fig. 4C)
PMID:38272226	PBO:0116367	(Fig. 4C)
PMID:38272226	PBO:0116368	(Fig. 4C)
PMID:38272226	PBO:0105959	(Fig. 4A)
PMID:38272226	PBO:0093797	(Fig. 4A)
PMID:38272226	GO:0005741	These results suggest that Hul6 loosely associates with the outer mitochondrial membrane. (Fig. 6)
PMID:38272226	PBO:0116369	(Fig. 7A)
PMID:38272226	PBO:0116345	(Fig. 7C)
PMID:38272226	PBO:0116370	(Fig. 7B)
PMID:38272226	PBO:0114265	(Fig. 1C)
PMID:38272226	PBO:0116371	(Fig. 1D)
PMID:38272226	PBO:0116371	(Fig. 1D)
PMID:38272226	PBO:0116345	(Fig. S5B)
PMID:38272226	PBO:0116372	(Fig. 2D)
PMID:38272226	PBO:0116372	(Fig. 2D)
PMID:38272226	PBO:0116373	(Fig. 3C)
PMID:38272226	PBO:0116373	(Fig. 3C)
PMID:38272226	PBO:0116375	(Fig. 4B)
PMID:38272226	PBO:0116375	(Fig. 4B)
PMID:38272226	PBO:0116375	(Fig. 4B)
PMID:38272226	PBO:0116376	(Fig. 4B)
PMID:38272226	PBO:0116377	(Fig. 4B)
PMID:38272226	PBO:0116377	(Fig. 4B)
PMID:38272226	PBO:0116378	(Fig. 4B)
PMID:38272226	PBO:0116378	(Fig. 4B)
PMID:38272226	PBO:0116378	(Fig. 4B)
PMID:38272226	PBO:0116379	(Fig. 4B)
PMID:38272226	PBO:0116380	(Fig. 4B)
PMID:38272226	PBO:0116380	(Fig. 4B)
PMID:38272226	PBO:0114584	(Fig. 4B)
PMID:38272226	PBO:0116381	(Fig. 4B)
PMID:38272226	PBO:0116381	(Fig. 4B)
PMID:38272226	PBO:0116382	(Fig. 4C)
PMID:38272226	PBO:0116383	(Fig. 4C)
PMID:38272226	PBO:0116384	(Fig. 4C)
PMID:38272226	PBO:0116385	(Fig. 4C)
PMID:38272226	PBO:0116386	(Fig. 4C)
PMID:38272226	PBO:0116385	(Fig. 4C)
PMID:38272226	PBO:0116385	(Fig. 4C)
PMID:38272226	PBO:0116382	(Fig. 4C)
PMID:38272226	PBO:0116382	(Fig. 4C)
PMID:38272226	PBO:0116386	(Fig. 4C)
PMID:38272226	PBO:0116386	(Fig. 4C)
PMID:38272226	PBO:0116384	(Fig. 4C)
PMID:38272226	PBO:0116384	(Fig. 4C)
PMID:38272226	PBO:0116383	(Fig. 4C)
PMID:38272226	PBO:0116383	(Fig. 4C)
PMID:38272226	PBO:0093798	(Fig. 4A and Fig. S6B)
PMID:38272226	PBO:0116387	(Fig. 4A and Fig. S6B)
PMID:38272226	FYPO:0001409	(Fig. 4A)
PMID:38272226	FYPO:0001814	(Fig. 4A)
PMID:38272226	FYPO:0001814	(Fig. 4A)
PMID:38272226	FYPO:0007121	(Fig. 4A)
PMID:38272226	PBO:0095303	(Fig. 4A)
PMID:38272226	PBO:0116387	(Fig. 4A)
PMID:38272226	FYPO:0001814	(Fig. 4A)
PMID:38272226	PBO:0093798	(Fig. 4A)
PMID:38272226	FYPO:0007121	(Fig. 4A)
PMID:38272226	FYPO:0007121	(Fig. 4A)
PMID:38272226	FYPO:0001409	(Fig. 4A)
PMID:38272226	FYPO:0001409	(Fig. 4A)
PMID:38272226	PBO:0095303	(Fig. 4A)
PMID:38272226	FYPO:0000245	Δhul6 cells show a progressive loss of viability, starting at 72 h (Fig. S6B).
PMID:38272226	PBO:0116388	(Fig. 5B and 5C)
PMID:38272226	PBO:0116388	(Fig. 5B and 5C)
PMID:38272226	PBO:0116389	(Fig. 5B and 5C)
PMID:38285941	PBO:0095651	(Fig. S1) (comment: Genetic screen for mutants defective in heterochromatin propagation.)
PMID:38285941	FYPO:0007159	(Fig. 4E and F).
PMID:38285941	PBO:0111391	(Fig. 4E and F).
PMID:38285941	PBO:0112230	FACT associates with subunits of MCM (Mcm2) and GINS (Psf3) when Mcl1 is present, but these interactions are lost in cells lacking Mcl1 (Fig. 6A)
PMID:38285941	PBO:0112229	FACT associates with subunits of MCM (Mcm2) and GINS (Psf3) when Mcl1 is present, but these interactions are lost in cells lacking Mcl1 (Fig. 6A)
PMID:38285941	FYPO:0000217	Compared to WT, swi6Δ cells showed a considerable decrease in BrdU incorporation across mat, which persisted through the time course (Fig. 2D and SI Appendix, Fig. S3). Mcm2 was still detected, although with more defined peaks, likely reflecting licensed, but not activated, replication ori­ gins across the domain (Fig. 2D)
PMID:38285941	FYPO:0003246	(Fig. 2D and E and SI Appendix, Figs. S2A-D and S3). Mcm2 mapping was performed 60 min after release from the cdc25-22 block. A similar septation index for WT and swi6Δ cells indicated normal progression of swi6Δ cells through S phase (SI Appendix, Fig. S2B).
PMID:38285941	PBO:0095653	(Fig. S1) (comment: Genetic screen for mutants defective in heterochromatin propagation.)
PMID:38285941	PBO:0095651	(Fig. S1) (comment: Genetic screen for mutants defective in heterochromatin propagation.)
PMID:38285941	FYPO:0008187	(Fig. 4E and F).
PMID:38285941	PBO:0095653	(Fig. S1) (comment: Genetic screen for mutants defective in heterochromatin propagation.)
PMID:38285941	FYPO:0002827	The other two mutants showed defective silencing of the mat2P::ura4+ reporter and haploid meiosis (Fig. 4C), as well as detectable levels of the mat2P transcript (Fig. 4D).
PMID:38285941	PBO:0112226	Thus, although both mutants affect the retention of parental histones, Mcl1 plays a more critical role in the process.
PMID:38285941	PBO:0112228	Notably, the addition of the WT Mcm2 HBD during the purification of the H3 and H4 histones promoted their solubili­ zation, highlighting its role as a histone chaperone (SI Appendix, Fig. S5D).
PMID:38285941	FYPO:0000088	The mcm2-6 mutant showed sensitivity to hydroxyurea (HU) (SI Appendix, Fig. S5C), indicating defective replication, and was not further analyzed.
PMID:38285941	PBO:0095651	(Fig. S1) (comment: Genetic screen for mutants defective in heterochromatin propagation.)
PMID:38285941	FYPO:0002827	The other two mutants showed defective silencing of the mat2P::ura4+ reporter and haploid meiosis (Fig. 4C), as well as detectable levels of the mat2P transcript (Fig. 4D).
PMID:38285941	PBO:0112223	, mcm2-1 and mcl1-4 cells failed to maintain heterochromatin, as indicated by white colony color and loss of the H3K9me3 mark (SI Appendix, Fig. S7). Thus, both Mcl1 and Mcm2 are required for propagation of heterochromatin at an ectopic site.
PMID:38285941	PBO:0112223	, mcm2-1 and mcl1-4 cells failed to maintain heterochromatin, as indicated by white colony color and loss of the H3K9me3 mark (SI Appendix, Fig. S7). Thus, both Mcl1 and Mcm2 are required for propagation of heterochromatin at an ectopic site.
PMID:38285941	PBO:0095653	(Fig. S1) (comment: Genetic screen for mutants defective in heterochromatin propagation.)
PMID:38285941	FYPO:0003247	(Fig. 4E and F).
PMID:38285941	PBO:0095652	(Fig. S1) (comment: Genetic screen for mutants defective in heterochromatin propagation.)
PMID:38285941	PBO:0112227	Mcl1 localized to heterochromatic loci in S phase, like Mcm2 (Fig. 2B).
PMID:38285941	PBO:0112227	Mcl1 localized to heterochromatic loci in S phase, like Mcm2 (Fig. 2B).
PMID:38289024	FYPO:0002336	(Figure 6B) (comment: CHECK endogenous atf1+ was deleted)
PMID:38289024	FYPO:0002336	(Figure 8A)
PMID:38289024	PBO:0112216	Intriguingly, removal of Sty1 kinase activity by introducing either sty1 deletion mutant (sty1Δ) or ATP analogue-sensitive mutant of sty1 (sty1-T97A, i.e. sty1-as2) (Zuin et al., 2010) into wis1-DD mutant background could relieve the negative effect of constitutive activation of MAPK Sty1 on kΔ::ade6+ reporter gene silencing, binding affinity between Atf1 and Swi6HP1 and heterochromatin stability at the mat locus (Figure 5 and Figure 5—Figure supplement 2).
PMID:38289024	PBO:0112214	Furthermore, in vitro pull-down assays demonstrated that the interaction between Atf1 and Swi6HP1 was also largely disrupted in wis1-DD mutants (Figure 5E and Figure 5—Figure supplement 1E).
PMID:38289024	FYPO:0002827	(Figure 5B) Notably, cells expressing two copies, but not one copy, of wis1-DD showed severe gene silencing defects (Figure 5B and Figure 5—Figure supplement 1B), and consistently the mRNA levels of the kΔ::ade6+ increased dramatically in these cells (Figure 5C and Figure 5—Figure supplement 1C).
PMID:38289024	FYPO:0002336	(Figure 3 S2A,B)
PMID:38289024	FYPO:0002336	(Figure 3D) (comment: CHECK endogenous atf1+ was deleted)
PMID:38289024	FYPO:0002336	Intriguingly, removal of Sty1 kinase activity by introducing either sty1 deletion mutant (sty1Δ) or ATP analogue-sensitive mutant of sty1 (sty1-T97A, i.e. sty1-as2) (Zuin et al., 2010) into wis1-DD mutant background could relieve the negative effect of constitutive activation of MAPK Sty1 on kΔ::ade6+ reporter gene silencing, binding affinity between Atf1 and Swi6HP1 and heterochromatin stability at the mat locus (Figure 5 and Figure 5—Figure supplement 2).
PMID:38289024	PBO:0093558	(Figure 6B; Figure 3-S1) (comment: CHECK endogenous atf1+ was deleted)
PMID:38289024	PBO:0112216	Intriguingly, removal of Sty1 kinase activity by introducing either sty1 deletion mutant (sty1Δ) or ATP analogue-sensitive mutant of sty1 (sty1-T97A, i.e. sty1-as2) (Zuin et al., 2010) into wis1-DD mutant background could relieve the negative effect of constitutive activation of MAPK Sty1 on kΔ::ade6+ reporter gene silencing, binding affinity between Atf1 and Swi6HP1 and heterochromatin stability at the mat locus (Figure 5 and Figure 5—Figure supplement 2).
PMID:38289024	FYPO:0002336	Intriguingly, removal of Sty1 kinase activity by introducing either sty1 deletion mutant (sty1Δ) or ATP analogue-sensitive mutant of sty1 (sty1-T97A, i.e. sty1-as2) (Zuin et al., 2010) into wis1-DD mutant background could relieve the negative effect of constitutive activation of MAPK Sty1 on kΔ::ade6+ reporter gene silencing, binding affinity between Atf1 and Swi6HP1 and heterochromatin stability at the mat locus (Figure 5 and Figure 5—Figure supplement 2).
PMID:38289024	FYPO:0002336	Intriguingly, removal of Sty1 kinase activity by introducing either sty1 deletion mutant (sty1Δ) or ATP analogue-sensitive mutant of sty1 (sty1-T97A, i.e. sty1-as2) (Zuin et al., 2010) into wis1-DD mutant background could relieve the negative effect of constitutive activation of MAPK Sty1 on kΔ::ade6+ reporter gene silencing, binding affinity between Atf1 and Swi6HP1 and heterochromatin stability at the mat locus (Figure 5 and Figure 5—Figure supplement 2).
PMID:38289024	PBO:0112216	Intriguingly, removal of Sty1 kinase activity by introducing either sty1 deletion mutant (sty1Δ) or ATP analogue-sensitive mutant of sty1 (sty1-T97A, i.e. sty1-as2) (Zuin et al., 2010) into wis1-DD mutant background could relieve the negative effect of constitutive activation of MAPK Sty1 on kΔ::ade6+ reporter gene silencing, binding affinity between Atf1 and Swi6HP1 and heterochromatin stability at the mat locus (Figure 5 and Figure 5—Figure supplement 2).
PMID:38289024	PBO:0095652	(Figure 3 S2A,B) More strikingly, Patf1-atf1(10D/E) also visibly compromised epigenetic silencing even at 30°C (Figure 3—Figure supplement 2A, B).
PMID:38289024	FYPO:0002827	cells at 37°C restored gene silencing rapidly at normal temperature 30°C after being re-plated on medium containing limited adenine (Figure 2A and B). However, when this re-plating assay was applied to dcr1Δ, one of the RNAi mutants, a considerable proportion of cells still emerged as variegated colonies (designated as dcr1ΔV), which was in sharp contrast to wild type cells (Figure 2B).
PMID:38289024	PBO:0112213	Binding affinity between Atf1 and Swi6HP1 is maintained for non-phosphorylatable Atf1(10A/I) at 37°C, but disrupted for phosphomimetic Atf1(10D/E) even at 30°C.
PMID:38289024	PBO:0112214	Binding affinity between Atf1 and Swi6HP1 is maintained for non-phosphorylatable Atf1(10A/I) at 37°C, but disrupted for phosphomimetic Atf1(10D/E) even at 30°C.
PMID:38289024	PBO:0112215	Consistently, ChIP- qPCR analyses showed that the abundance of both H3K9me3 and Swi6HP1 bound at the mat locus but not at pericentromere decreased dramatically in cells with two copies of wis1-DD (Figure 5F and Figure 5—Figure supplement 1F).
PMID:38289024	PBO:0111016	Consistently, ChIP- qPCR analyses showed that the abundance of both H3K9me3 and Swi6HP1 bound at the mat locus but not at pericentromere decreased dramatically in cells with two copies of wis1-DD (Figure 5F and Figure 5—Figure supplement 1F).
PMID:38289024	FYPO:0004376	(Figure 6B) (comment: CHECK endogenous atf1+ was deleted)
PMID:38289024	PBO:0112216	Intriguingly, removal of Sty1 kinase activity by introducing either sty1 deletion mutant (sty1Δ) or ATP analogue-sensitive mutant of sty1 (sty1-T97A, i.e. sty1-as2) (Zuin et al., 2010) into wis1-DD mutant background could relieve the negative effect of constitutive activation of MAPK Sty1 on kΔ::ade6+ reporter gene silencing, binding affinity between Atf1 and Swi6HP1 and heterochromatin stability at the mat locus (Figure 5 and Figure 5—Figure supplement 2).
PMID:38289024	FYPO:0002336	indicating full rescue of silencing defects at the mat locus under heat stress.
PMID:38289024	FYPO:0002336	demonstrating that tethering Swi6HP1 to the mat locus was sufficient to rescue heat stress-induced defective epigenetic maintenance of heterochromatin.
PMID:38289024	FYPO:0002336	(Figure 6B) (comment: CHECK endogenous atf1 was deleted)
PMID:38289024	FYPO:0002336	(Figure 6B) (comment: CHECK endogenous atf1+ was deleted)
PMID:38289024	FYPO:0002336	(Figure 6B) (comment: CHECK endogenous atf1+ was deleted)
PMID:38295128	FYPO:0001234	Consistent with a defect in translation due to loss of ribosomal protein paralogs, we find that each of four rplΔ mutants and three rpsΔ mutants has a substantially reduced growth rate (increased generation time) relative to that of the WT strain in YES media at 30 ̊C (Fig 7A and 7B and S1 Table).
PMID:38295128	PBO:0116484	rpl2802Δ mutation efficiently suppresses the growth phenotypes of an S. pombe tan1Δ mutant, resulting in temperature resistance on EMMC-His media and YES media at 38 ̊C, 3-AT resistance at 35 ̊C .....Fig 5A).
PMID:38295128	PBO:0093557	Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	FYPO:0000674	Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	FYPO:0000674	Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	PBO:0093784	Similarly, all five of the trm8Δ rplΔ and trm8Δ rpsΔ mutants that were robust trm8Δ suppressors were also sensitive on YES +5-FU media at 33 ̊C, whereas the weak trm8Δ rpl1601Δ suppressor was slightly sensitive on YES+5-FU.
PMID:38295128	PBO:0093784	Similarly, all five of the trm8Δ rplΔ and trm8Δ rpsΔ mutants that were robust trm8Δ suppressors were also sensitive on YES +5-FU media at 33 ̊C, whereas the weak trm8Δ rpl1601Δ suppressor was slightly sensitive on YES+5-FU.
PMID:38295128	PBO:0093784	Similarly, all five of the trm8Δ rplΔ and trm8Δ rpsΔ mutants that were robust trm8Δ suppressors were also sensitive on YES +5-FU media at 33 ̊C, whereas the weak trm8Δ rpl1601Δ suppressor was slightly sensitive on YES+5-FU.
PMID:38295128	PBO:0093785	Similarly, all five of the trm8Δ rplΔ and trm8Δ rpsΔ mutants that were robust trm8Δ suppressors were also sensitive on YES +5-FU media at 33 ̊C, whereas the weak trm8Δ rpl1601Δ suppressor was slightly sensitive on YES+5-FU.
PMID:38295128	PBO:0093784	Similarly, all five of the trm8Δ rplΔ and trm8Δ rpsΔ mutants that were robust trm8Δ suppressors were also sensitive on YES +5-FU media at 33 ̊C, whereas the weak trm8Δ rpl1601Δ suppressor was slightly sensitive on YES+5-FU.
PMID:38295128	PBO:0116492	(fig 3) By contrast, we found that 3-AT resistance was not correlated with the efficiency of suppression in trm8Δ rplΔ strain, as one of the robust trm8Δ suppressors was almost completely 3-AT sensitive (trm8Δ rpl1202Δ) and two other robust suppressors were only moderately 3-AT resistant (trm8Δ rps2801Δ and trm8Δ rps802Δ), whereas the robust trm8Δ rplΔ2802Δ and trm8Δ rpl1701Δ suppressor strains were strongly 3-AT resistant. This result is consistent with our finding above that 3-AT resistance is a property of the mutation in the ribosomal protein gene, and not the trm8Δ mutation, However, it is not immediately clear why some mutations in ribosomal protein genes result in 3-AT resistance and others result in sensitivity
PMID:38295128	PBO:0116492	(fig 3) By contrast, we found that 3-AT resistance was not correlated with the efficiency of suppression in trm8Δ rplΔ strain, as one of the robust trm8Δ suppressors was almost completely 3-AT sensitive (trm8Δ rpl1202Δ) and two other robust suppressors were only moderately 3-AT resistant (trm8Δ rps2801Δ and trm8Δ rps802Δ), whereas the robust trm8Δ rplΔ2802Δ and trm8Δ rpl1701Δ suppressor strains were strongly 3-AT resistant. This result is consistent with our finding above that 3-AT resistance is a property of the mutation in the ribosomal protein gene, and not the trm8Δ mutation, However, it is not immediately clear why some mutations in ribosomal protein genes result in 3-AT resistance and others result in sensitivity
PMID:38295128	PBO:0116489	By contrast, trm8Δ rpl1701-Q72X and trm8Δ rpl502-Y44X mutants had near baseline relative lys4+ expression at both temperatures (0.97 and 0.88 vs 0.88 for WT, at 38.5 ̊C) (Fig 1D).
PMID:38295128	PBO:0116489	By contrast, trm8Δ rpl1701-Q72X and trm8Δ rpl502-Y44X mutants had near baseline relative lys4+ expression at both temperatures (0.97 and 0.88 vs 0.88 for WT, at 38.5 ̊C) (Fig 1D).
PMID:38295128	PBO:0116487	and a follow-up analysis shows that the trm8Δ rpl1102-K93X suppressor also did not restore the reduced levels of tRNATyr(GUA) and tRNAPro(AGG), whereas levels of a known unaffected Trm8 substrate (tRNAVal(AAC)) remained constant (S3 Fig).
PMID:38295128	PBO:0116486	Similar analysis shows that the trm8Δ rpl502-Y44X suppressor had slightly increased levels of tRNATyr(GUA) (36% vs 30%) and of tRNAPro(AGG) (13% vs 9%) relative to WT (Fig 1B and 1C)
PMID:38295128	PBO:0116486	Surprisingly, we found that in the trm8Δ rpl1701-Q72X suppressor the tRNATyr(GUA) levels were not restored, but were if anything slightly reduced, relative to the trm8Δ mutant (23% vs 30%).....Thus, for the trm8Δ rpl1701-Q72X suppressor, suppression is occurring without a detectable increase in levels of tRNATyr(GUA) or of tRNAPro(AGG).
PMID:38295128	PBO:0116493	(fig 3) By contrast, we found that 3-AT resistance was not correlated with the efficiency of suppression in trm8Δ rplΔ strain, as one of the robust trm8Δ suppressors was almost completely 3-AT sensitive (trm8Δ rpl1202Δ) and two other robust suppressors were only moderately 3-AT resistant (trm8Δ rps2801Δ and trm8Δ rps802Δ), whereas the robust trm8Δ rplΔ2802Δ and trm8Δ rpl1701Δ suppressor strains were strongly 3-AT resistant. This result is consistent with our finding above that 3-AT resistance is a property of the mutation in the ribosomal protein gene, and not the trm8Δ mutation, However, it is not immediately clear why some mutations in ribosomal protein genes result in 3-AT resistance and others result in sensitivity
PMID:38295128	PBO:0116493	(fig 3) By contrast, we found that 3-AT resistance was not correlated with the efficiency of suppression in trm8Δ rplΔ strain, as one of the robust trm8Δ suppressors was almost completely 3-AT sensitive (trm8Δ rpl1202Δ) and two other robust suppressors were only moderately 3-AT resistant (trm8Δ rps2801Δ and trm8Δ rps802Δ), whereas the robust trm8Δ rplΔ2802Δ and trm8Δ rpl1701Δ suppressor strains were strongly 3-AT resistant. This result is consistent with our finding above that 3-AT resistance is a property of the mutation in the ribosomal protein gene, and not the trm8Δ mutation, However, it is not immediately clear why some mutations in ribosomal protein genes result in 3-AT resistance and others result in sensitivity
PMID:38295128	PBO:0093784	Similarly, all five of the trm8Δ rplΔ and trm8Δ rpsΔ mutants that were robust trm8Δ suppressors were also sensitive on YES +5-FU media at 33 ̊C, whereas the weak trm8Δ rpl1601Δ suppressor was slightly sensitive on YES+5-FU.
PMID:38295128	FYPO:0000674	Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	PBO:0093558	(Figure 4 B) S. pombe tan1Δ mutants are temperature sensitive due to decay of two tRNA species by the RTD pathway.
PMID:38295128	PBO:0116494	(Figure 4 C) Consistent with the biology of Tan1 in S. cerevisiae, we find that S. pombe tan1Δ mutants are temperature sensitive due to decay of two tRNA species by the RTD pathway.
PMID:38295128	PBO:0116495	(Figure 4 C) Consistent with the biology of Tan1 in S. cerevisiae, we find that S. pombe tan1Δ mutants are temperature sensitive due to decay of two tRNA species by the RTD pathway.
PMID:38295128	PBO:0116496	(Figure 4 C) As anticipated based on the conservation of Tan1 sequence and the Tan1 requirement for ac4C12 modification of tRNALeu and tRNASer within a CCG motif [35-38], purified tRNALeu(CAA) from S. pombe tan1Δ mutants lacks any detectable ac4C, compared to that in WT cells, but has similar levels of four control modifications (Fig 4A).
PMID:38295128	PBO:0116497	"phenotypes support conservation of role in S. cerevisiae which is binding tRNA and ""The interaction of NAT10 and THUMPD1 suggests that they work together in tRNA acetylation and that THUMPD1 acts as a specific tRNA adaptor. In agreement with this view, we found Kre33 and Tan1 to interact in a 2-hybrid assay in budding yeast cells (Figure 5J)."
PMID:38295128	PBO:0116498	"(comment: phenotypes support conservation of role in S. cerevisiae which is binding tRNA and) ""The interaction of NAT10 and THUMPD1 suggests that they work together in tRNA acetylation and that THUMPD1 acts as a specific tRNA adaptor. In agreement with this view, we found Kre33 and Tan1 to interact in a 2-hybrid assay in budding yeast cells (Figure 5J)."
PMID:38295128	FYPO:0000674	rpl2802Δ mutation efficiently suppresses the growth phenotypes of an S. pombe tan1Δ mutant, resulting in temperature resistance on EMMC-His media and YES media at 38 ̊C, 3-AT resistance at 35 ̊C ..... (Fig 5A).
PMID:38295128	FYPO:0000674	rpl2802Δ mutation efficiently suppresses the growth phenotypes of an S. pombe tan1Δ mutant, resulting in temperature resistance on EMMC-His media and YES media at 38 ̊C, 3-AT resistance at 35 ̊C ..... (Fig 5A).
PMID:38295128	FYPO:0000674	rpl2802Δ mutation efficiently suppresses the growth phenotypes of an S. pombe tan1Δ mutant, resulting in temperature resistance on EMMC-His media and YES media at 38 ̊C, 3-AT resistance at 35 ̊C ..... (Fig 5A).
PMID:38295128	FYPO:0000674	rpl2802Δ mutation efficiently suppresses the growth phenotypes of an S. pombe tan1Δ mutant, resulting in temperature resistance on EMMC-His media and YES media at 38 ̊C, 3-AT resistance at 35 ̊C ..... (Fig 5A).
PMID:38295128	PBO:0093558	(Figure 4 B) S. pombe tan1Δ mutants are temperature sensitive due to decay of two tRNA species by the RTD pathway.
PMID:38295128	PBO:0116495	As we saw for the trm8Δ rpl502Δ strain, we find that the tan1Δ rpl502Δ strain does not have restored tRNA levels after growth at 39 ̊C (Fig 6A and 6B).... Relative tRNALeu(AAG) levels are reduced substantially in tan1Δ strains after growth at 39 ̊C (to 24% of WT)
PMID:38295128	PBO:0116495	(Fig 6A and 6B) Relative tRNALeu(AAG) levels are reduced substantially in tan1Δ strains after growth at 39 ̊C (to 24% of WT)
PMID:38295128	PBO:0116499	However, we find that although an S. pombe tan1Δ mutant activates the GAAC pathway, based on analysis of relative lys4+ mRNA levels, the activation is weak, and is only modestly reduced in a tan1Δ rpl502Δ strain (Fig 6C).
PMID:38295128	FYPO:0000674	These weak effects of the tan1Δ mutant and the tan1Δ rpl502Δ mutant on GAAC activation are consistent with the observation that an rpl502Δ mutation is a more efficient suppressor of the temperature sensitivity of an S. pombe tan1Δ mutant than is a gcn2Δ mutation, on either YES media or EMMC-His media at 38 ̊C (Fig 6D).
PMID:38295128	FYPO:0000674	These weak effects of the tan1Δ mutant and the tan1Δ rpl502Δ mutant on GAAC activation are consistent with the observation that an rpl502Δ mutation is a more efficient suppressor of the temperature sensitivity of an S. pombe tan1Δ mutant than is a gcn2Δ mutation, on either YES media or EMMC-His media at 38 ̊C (Fig 6D).
PMID:38295128	PBO:0093557	These weak effects of the tan1Δ mutant and the tan1Δ rpl502Δ mutant on GAAC activation are consistent with the observation that an rpl502Δ mutation is a more efficient suppressor of the temperature sensitivity of an S. pombe tan1Δ mutant than is a gcn2Δ mutation, on either YES media or EMMC-His media at 38 ̊C (Fig 6D).
PMID:38295128	PBO:0093557	These weak effects of the tan1Δ mutant and the tan1Δ rpl502Δ mutant on GAAC activation are consistent with the observation that an rpl502Δ mutation is a more efficient suppressor of the temperature sensitivity of an S. pombe tan1Δ mutant than is a gcn2Δ mutation, on either YES media or EMMC-His media at 38 ̊C (Fig 6D).
PMID:38295128	FYPO:0000674	We found that a reconstructed trm8Δ rpl502Δ strain suppressed the growth defect of a trm8Δ mutant almost identically to the trm8Δ rpl502-Y44X mutant, with similar growth in YES and EMMC media at high temperature, and similar 5-FU sensitivity and 3-AT resistance (Fig 2A)(Figs 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	PBO:0093784	We found that a reconstructed trm8Δ rpl502Δ strain suppressed the growth defect of a trm8Δ mutant almost identically to the trm8Δ rpl502-Y44X mutant, with similar growth in YES and EMMC media at high temperature, and similar 5-FU sensitivity and 3-AT resistance (Fig 2A)
PMID:38295128	PBO:0116484	We found that a reconstructed trm8Δ rpl502Δ strain suppressed the growth defect of a trm8Δ mutant almost identically to the trm8Δ rpl502-Y44X mutant, with similar growth in YES and EMMC media at high temperature, and similar 5-FU sensitivity and 3-AT resistance (Fig 2A)
PMID:38295128	PBO:0116485	As expected, in trm8Δ mutants at 38.5 ̊C, relative tRNATyr(GUA) levels were reduced, to 30% of WT levels (Fig 1B and 1C).
PMID:38295128	PBO:0116484	(Figs 1A and S1) and unlike the GAAC or dhp1 suppressors, these suppressors were resistant to 3-AT at 37 ̊C
PMID:38295128	PBO:0116490	whereas levels of tRNATyr(GUA) were modestly restored in trm8Δ gcn2Δ mutants (58% vs 41%), as we observed previously [23] (Fig 2B and 2C).
PMID:38295128	PBO:0116491	(Fig 1B and 1C).
PMID:38295128	PBO:0116491	(Fig 1B and 1C)
PMID:38295128	PBO:0116491	(Fig 1B and 1C)
PMID:38295128	PBO:0093784	(Figs 1A and S1) However, unlike the dhp1 suppressors, these suppressors grew poorly on media containing 5-FU at 33 ̊C (Figs 1A)
PMID:38295128	FYPO:0001234	Consistent with a defect in translation due to loss of ribosomal protein paralogs, we find that each of four rplΔ mutants and three rpsΔ mutants has a substantially reduced growth rate (increased generation time) relative to that of the WT strain in YES media at 30 ̊C (Fig 7A and 7B and S1 Table).
PMID:38295128	FYPO:0001234	Consistent with a defect in translation due to loss of ribosomal protein paralogs, we find that each of four rplΔ mutants and three rpsΔ mutants has a substantially reduced growth rate (increased generation time) relative to that of the WT strain in YES media at 30 ̊C (Fig 7A and 7B and S1 Table).
PMID:38295128	PBO:0116491	(Fig 1B and 1C). Similarly, tRNAPro(AGG) levels were not efficiently restored in trm8Δ rpl502Δ mutants (38%) relative to 25% in trm8Δ mutants and 49% in trm8Δ gcn2Δ strains.
PMID:38295128	PBO:0116489	Furthermore, like trm8Δ rpl502-Y44X mutants, trm8Δ rpl502Δ mutants efficiently suppressed the GAAC activation observed in trm8Δ mutants, measured by relative lys4+ levels (from a 14.5-fold increase in trm8Δ mutants, to a 1.9-fold increase in trm8Δ rpl502Δ mutants), compared to a near baseline 1.2-fold increase in a trm8Δ gcn2Δ strain (Figs 2D and S5).
PMID:38295128	FYPO:0000674	Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	FYPO:0000674	Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	PBO:0093556	(vw: growth seems slightly reduced compared to WT) Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	PBO:0093556	(vw: growth seems slightly reduced compared to WT) Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	FYPO:0000674	Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	FYPO:0000674	Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	FYPO:0000674	We found that a reconstructed trm8Δ rpl502Δ strain suppressed the growth defect of a trm8Δ mutant almost identically to the trm8Δ rpl502-Y44X mutant, with similar growth in YES and EMMC media at high temperature, and similar 5-FU sensitivity and 3-AT resistance (Fig 2A)
PMID:38295128	PBO:0116489	By contrast, trm8Δ rpl1701-Q72X and trm8Δ rpl502-Y44X mutants had near baseline relative lys4+ expression at both temperatures (0.97 and 0.88 vs 0.88 for WT, at 38.5 ̊C) (Fig 1D).
PMID:38295128	PBO:0116489	By contrast, trm8Δ rpl1701-Q72X and trm8Δ rpl502-Y44X mutants had near baseline relative lys4+ expression at both temperatures (0.97 and 0.88 vs 0.88 for WT, at 38.5 ̊C) (Fig 1D).
PMID:38295128	PBO:0093557	Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	FYPO:0001234	Consistent with a defect in translation due to loss of ribosomal protein paralogs, we find that each of four rplΔ mutants and three rpsΔ mutants has a substantially reduced growth rate (increased generation time) relative to that of the WT strain in YES media at 30 ̊C (Fig 7A and 7B and S1 Table).
PMID:38295128	FYPO:0001234	Consistent with a defect in translation due to loss of ribosomal protein paralogs, we find that each of four rplΔ mutants and three rpsΔ mutants has a substantially reduced growth rate (increased generation time) relative to that of the WT strain in YES media at 30 ̊C (Fig 7A and 7B and S1 Table).
PMID:38295128	FYPO:0001234	Consistent with a defect in translation due to loss of ribosomal protein paralogs, we find that each of four rplΔ mutants and three rpsΔ mutants has a substantially reduced growth rate (increased generation time) relative to that of the WT strain in YES media at 30 ̊C (Fig 7A and 7B and S1 Table).
PMID:38295128	FYPO:0001234	Consistent with a defect in translation due to loss of ribosomal protein paralogs, we find that each of four rplΔ mutants and three rpsΔ mutants has a substantially reduced growth rate (increased generation time) relative to that of the WT strain in YES media at 30 ̊C (Fig 7A and 7B and S1 Table).
PMID:38295128	FYPO:0001234	Consistent with a defect in translation due to loss of ribosomal protein paralogs, we find that each of four rplΔ mutants and three rpsΔ mutants has a substantially reduced growth rate (increased generation time) relative to that of the WT strain in YES media at 30 ̊C (Fig 7A and 7B and S1 Table).
PMID:38295128	FYPO:0007317	Polysome profiling of three of these mutants provides additional evidence for a defect in translation in the mutants (Fig 7C).
PMID:38295128	FYPO:0007317	Polysome profiling of three of these mutants provides additional evidence for a defect in translation in the mutants (Fig 7C).
PMID:38295128	FYPO:0006037	Moreover, both rplΔ mutant profiles, but not the WT, exhibit substantial populations of halfmers, monosomes and polysomes with an additional 40S subunit
PMID:38295128	FYPO:0006037	Moreover, both rplΔ mutant profiles, but not the WT, exhibit substantial populations of halfmers, monosomes and polysomes with an additional 40S subunit
PMID:38295128	FYPO:0007317	The rps23Δ mutant also has reduced polysome density, indicative of reduced translation, accompanied by an undetectable 40S peak and a greatly pronounced 60S peak that substantially overshadows the 80 monosome peak
PMID:38295128	GO:0002181	The rps23Δ mutant also has reduced polysome density, indicative of reduced translation, accompanied by an undetectable 40S peak and a greatly pronounced 60S peak that substantially overshadows the 80 monosome peak
PMID:38295128	GO:0002181	Polysome profiling of three of these mutants provides additional evidence for a defect in translation in the mutants (Fig 7C).
PMID:38295128	FYPO:0000674	(Figs 1A and S1) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0000674	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I) [23
PMID:38295128	PBO:0116484	and unlike the GAAC or dhp1 suppressors, these suppressors were resistant to 3-AT at 37 ̊C (Fig 1A)
PMID:38295128	PBO:0116484	and unlike the GAAC or dhp1 suppressors, these suppressors were resistant to 3-AT at 37 ̊C (Fig 1A)
PMID:38295128	PBO:0116484	and unlike the GAAC or dhp1 suppressors, these suppressors were resistant to 3-AT at 37 ̊C (Fig 1A)
PMID:38295128	PBO:0093784	However, unlike the dhp1 suppressors, these suppressors grew poorly on media containing 5-FU at 33 ̊C (Fig 1A)
PMID:38295128	PBO:0093784	However, unlike the dhp1 suppressors, these suppressors grew poorly on media containing 5-FU at 33 ̊C (Fig 1A)
PMID:38295128	PBO:0093784	However, unlike the dhp1 suppressors, these suppressors grew poorly on media containing 5-FU at 33 ̊C (Fig 1A)
PMID:38295128	FYPO:0000674	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0000674	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	PBO:0093558	(Figure 4 B) S. pombe tan1Δ mutants are temperature sensitive due to decay of two tRNA species by the RTD pathway.
PMID:38295128	FYPO:0000674	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0000674	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0000674	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0000674	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0000674	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I) [23
PMID:38295128	FYPO:0000674	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I) [23
PMID:38295128	FYPO:0000674	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I) [23
PMID:38295128	FYPO:0000674	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I) [23
PMID:38295128	FYPO:0000674	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I) [23
PMID:38295128	PBO:0093558	(Fig. 1A)
PMID:38295128	PBO:0116482	(Fig. 1A)
PMID:38295128	PBO:0093785	(Fig. 1A)
PMID:38295128	PBO:0093789	(comment: vw: grows slightly better than WT) However, unlike the dhp1 suppressors, these suppressors grew poorly on media containing 5-FU at 33 ̊C, and unlike the GAAC or dhp1 suppressors, these suppressors were resistant to 3-AT at 37 ̊C (Figs 1A and S1)
PMID:38295128	PBO:0093789	(comment: vw: grows slightly better than WT) However, unlike the dhp1 suppressors, these suppressors grew poorly on media containing 5-FU at 33 ̊C, and unlike the GAAC or dhp1 suppressors, these suppressors were resistant to 3-AT at 37 ̊C (Figs 1A and S1)
PMID:38295128	FYPO:0000674	(Fig. 1A)
PMID:38295128	FYPO:0000674	(Fig. 1A)
PMID:38295128	FYPO:0000674	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0000674	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	PBO:0093789	(comment: vw: grows slightly better than WT) However, unlike the dhp1 suppressors, these suppressors grew poorly on media containing 5-FU at 33 ̊C, and unlike the GAAC or dhp1 suppressors, these suppressors were resistant to 3-AT at 37 ̊C (Figs 1A and S1)
PMID:38295128	PBO:0093789	(comment: vw: grows slightly better than WT) However, unlike the dhp1 suppressors, these suppressors grew poorly on media containing 5-FU at 33 ̊C, and unlike the GAAC or dhp1 suppressors, these suppressors were resistant to 3-AT at 37 ̊C (Figs 1A and S1)
PMID:38295128	PBO:0116483	(Fig. 1A)
PMID:38295128	FYPO:0000674	(Fig. 1A)
PMID:38295128	FYPO:0000674	(Fig. 1A)
PMID:38295128	FYPO:0000674	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0000674	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0000674	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I) [23
PMID:38295128	GO:0002181	Polysome profiling of three of these mutants provides additional evidence for a defect in translation in the mutants (Fig 7C).
PMID:38359013	FYPO:0002061	(comment: erratum corrected previous annotation)
PMID:38360270	PBO:0112128	(Fig. 4)
PMID:38360270	PBO:0112129	(Fig. 4)
PMID:38360270	PBO:0112134	(Fig. 5)
PMID:38360270	PBO:0112208	(Fig. 5)
PMID:38360270	FYPO:0001457	(Fig. 5) Cells defective in UPR are sensitive to tunicamycin (32). Consistently, ire1Δ cells failed to grow on EMM plates containing tunicamycin (Fig. 2B)
PMID:38360270	FYPO:0001457	Paradoxically, erd2Δ cells, in which UPR was activated (Fig. 2A), also grew poorly on EMM plates containing tunicamycin.
PMID:38360270	PBO:0112127	(Fig. 4)
PMID:38360270	PBO:0112122	(Fig. 2B)
PMID:38360270	FYPO:0003896	(Fig. 3) mitochondria were fragmented in erd2Δ cells but not in WT, ire1Δ, or erd2Δire1Δ cells
PMID:38360270	FYPO:0003896	(Fig. 3) mitochondria were fragmented in erd2Δ cells but not in WT, ire1Δ, or erd2Δire1Δ cells
PMID:38360270	PBO:0112123	(comment: CHECK DID WE NEED TO CHANGE THIS TO LOW) Fig. 3 The results showed that the oxygen consumption rate of erd2Δ cells, but not ire1Δ or erd2Δire1Δ cells, was increased.
PMID:38360270	PBO:0112123	(comment: CHECK DID WE NEED TO CHANGE THIS TO LOW) Fig. 3 The results showed that the oxygen consumption rate of erd2Δ cells, but not ire1Δ or erd2Δire1Δ cells, was increased.
PMID:38360270	FYPO:0003118	(Fig. 3)
PMID:38360270	FYPO:0003118	(Fig. 3)
PMID:38360270	PBO:0112124	(Fig. 4)
PMID:38360270	PBO:0112198	(Fig. 4)
PMID:38360270	PBO:0112199	(Fig. 4)
PMID:38360270	PBO:0112125	(Fig. 4)
PMID:38360270	PBO:0112200	(Fig. 4)
PMID:38360270	PBO:0112201	(Fig. 4)
PMID:38360270	PBO:0112202	(Fig. 4)
PMID:38360270	PBO:0112203	(Fig. 4)
PMID:38360270	PBO:0112126	(Fig. 4)
PMID:38360270	PBO:0112126	(Fig. 4)
PMID:38360270	PBO:0112127	(Fig. 4)
PMID:38360270	PBO:0112127	(Fig. 4)
PMID:38360270	PBO:0112128	(Fig. 4)
PMID:38360270	PBO:0112128	(Fig. 4)
PMID:38360270	PBO:0112129	(Fig. 4)
PMID:38360270	PBO:0112129	(Fig. 4)
PMID:38360270	PBO:0112130	(Fig. 4)
PMID:38360270	PBO:0112130	(Fig. 4)
PMID:38360270	PBO:0112131	(Fig. 4)
PMID:38360270	PBO:0112131	(Fig. 4)
PMID:38360270	PBO:0112132	(Fig. 4)
PMID:38360270	PBO:0112132	(Fig. 4)
PMID:38360270	PBO:0112133	(Fig. 4)
PMID:38360270	PBO:0112133	(Fig. 4)
PMID:38360270	PBO:0112204	(Fig. 4)
PMID:38360270	PBO:0112205	(Fig. 4)
PMID:38360270	PBO:0112206	(Fig. 4)
PMID:38360270	PBO:0112207	(Fig. 4)
PMID:38360270	PBO:0112126	(Fig. 4)
PMID:38360270	PBO:0112117	(Fig. 1) Intriguingly, we observed that the absence of erd2 caused mitochondrial fragmentation (Fig. 1, A and B)
PMID:38360270	FYPO:0004166	(Fig. 1C) Moreover, the oxygen consumption rate of erd2Δ cells was higher than that of WT cells (Figs. 1C and S1A), suggesting that mitochondrial respiration was increased in erd2Δ cells.
PMID:38360270	FYPO:0003004	((Fig. 1) As shown in Figure 1, D and E, mitochondrial ROS was higher in erd2Δ cells than in WT cells.)
PMID:38360270	PBO:0112118	(Fig. 2A)
PMID:38360270	PBO:0112119	(Fig. 2A)
PMID:38360270	PBO:0112119	(Fig. 2A)
PMID:38360270	PBO:0112120	(Fig. 2A)
PMID:38360270	PBO:0112121	(Fig. 2A)
PMID:38360270	PBO:0112121	(Fig. 2A)
PMID:38360270	PBO:0093559	(Fig. 2B) Under unstressed conditions, that is, when cells were grown on EMM plates, ire1Δ and erd2Δ had no noticeable effect on cell growth, but ire1Δerd2Δ impaired cell growth (Fig. 2B).
PMID:38360270	PBO:0093561	(Fig. 2B)
PMID:38360270	PBO:0093560	(Fig. 2B)
PMID:38376141	PBO:0114145	(Fig. 6C and D)
PMID:38376141	PBO:0094679	(Fig. 7A)
PMID:38376141	PBO:0114143	(Fig. 6A)
PMID:38376141	PBO:0114142	(Fig. 6C and D)
PMID:38376141	PBO:0114141	(Fig. 7B and C)
PMID:38376141	PBO:0094679	(Fig. 7A)
PMID:38376141	PBO:0112225	In contrast, when we complemented the depleted extract with SpCAF-1 mutant complexes SpCAF-1-ED*, SpCAF-1-KER*, SpCAF- 1-ΔWHD we did not detect the supercoiled form I. This indicates that these mutants cannot promote nucleosome assembly (Figure 5).
PMID:38376141	PBO:0114147	The KER* mutation was then introduced in the full complex SpCAF-1-KER* (Figure 1—Figure supplement 1B, Figure 2— Figure supplement 2B) and we confirmed by MST and EMSA its lower affinity for dsDNA (Figure 3B, Figure 3—Figure supplement 2G, Table 1).
PMID:38376141	PBO:0094679	(Fig. 7A)
PMID:38376141	PBO:0114145	(Fig. 6C and D)
PMID:38376141	FYPO:0007158	(Fig. 2 supplement 1A)
PMID:38376141	PBO:0114140	(Fig. 6)
PMID:38376141	PBO:0112225	In contrast, when we complemented the depleted extract with SpCAF-1 mutant complexes SpCAF-1-ED*, SpCAF-1-KER*, SpCAF- 1-ΔWHD we did not detect the supercoiled form I. This indicates that these mutants cannot promote nucleosome assembly (Figure 5).
PMID:38376141	PBO:0114143	(Fig. 6A)
PMID:38376141	FYPO:0002150	(Fig. 7D)
PMID:38376141	FYPO:0002150	(Fig. 7D)
PMID:38376141	FYPO:0002150	(Fig. 7D)
PMID:38376141	FYPO:0002150	(Fig. 7D)
PMID:38376141	FYPO:0000278	(Fig. 7D)
PMID:38376141	PBO:0114146	(Fig. 7B and C)
PMID:38376141	PBO:0114144	When we used the SpCAF-1-PIP* mutant, we did not detect supercoiling on labeled DNA at 45 min, yet at 2 hr supercoiling ultimately reached levels achieved using the WT SpCAF-1 (Figure 5, bottom, synthesized DNA).
PMID:38376141	FYPO:0000278	(Fig. 7D)
PMID:38376141	PBO:0114149	In addition, the NMR signals of all IDR for this mutant with or without histones were close to that of the WT (Figure 3—Figure supplement 3A-B) indicating that the KER* mutation did not impair histone binding.
PMID:38376141	PBO:0114148	In addition, the NMR signals of all IDR for this mutant with or without histones were close to that of the WT (Figure 3—Figure supplement 3A-B) indicating that the KER* mutation did not impair histone binding.
PMID:38376141	FYPO:0007159	(Fig. 2 supplement 1A)
PMID:38376141	FYPO:0002150	(Fig. 7D)
PMID:38376141	FYPO:0002150	(Fig. 7D)
PMID:38376141	PBO:0114150	We observed the similar DNA binding property and IDR properties for SpCAF-1-ΔWHD and the WT complex (Table 1, Figure 3B, Figure 3—Figure supplement 2G, Figure 3—Figure supplement 3A-B).
PMID:38376141	PBO:0114151	(Fig. 6)
PMID:38376141	PBO:0114152	(Fig. 6C and D)
PMID:38376141	FYPO:0004742	(Fig. 7A)
PMID:38376141	FYPO:0007328	(Fig. 7B and C)
PMID:38376141	PBO:0114141	(Fig. 7B and C)
PMID:38376141	PBO:0112225	In contrast, when we complemented the depleted extract with SpCAF-1 mutant complexes SpCAF-1-ED*, SpCAF-1-KER*, SpCAF- 1-ΔWHD we did not detect the supercoiled form I. This indicates that these mutants cannot promote nucleosome assembly (Figure 5).
PMID:38376141	PBO:0114146	(Fig. 7B and C)
PMID:38399762	FYPO:0000387	The extent of biofilm formed in SPBPJ4664.02∆ decreased by 40% as compared to WT (p < 0.05), indicating that SPBPJ4664.02 is required for biofilm formation.
PMID:38424265	PBO:0111039	(Fig. 6B)
PMID:38424265	FYPO:0008237	(Fig. 5)
PMID:38424265	FYPO:0001190	(Fig. 7B)
PMID:38424265	PBO:0093588	(Fig. 7A)
PMID:38424265	PBO:0093589	(Fig. 7A)
PMID:38424265	PBO:0111039	(Fig. 6B)
PMID:38424265	FYPO:0000245	(Fig. 6A)
PMID:38424265	FYPO:0000245	(Fig. 6A)
PMID:38424265	FYPO:0008237	(Fig. 5)
PMID:38424265	PBO:0112935	(Fig. 4B)
PMID:38424265	PBO:0112934	(Fig. 4A)
PMID:38424265	PBO:0093578	(Fig. 3C)
PMID:38424265	PBO:0093577	(Fig. 3C)
PMID:38424265	PBO:0093595	(Fig. 3B)
PMID:38424265	FYPO:0005947	(Fig. 3B)
PMID:38424265	FYPO:0001043	(Fig. 3A)
PMID:38424265	PBO:0103077	(Fig. 2C)
PMID:38424265	FYPO:0001357	(Fig. 2C)
PMID:38424265	FYPO:0001357	(Fig. 1A)
PMID:38424265	FYPO:0001043	(Fig. 3A)
PMID:38424265	PBO:0100665	(Fig. 1A)
PMID:38442865	FYPO:0008233	(Fig. S4)
PMID:38442865	FYPO:0008233	(Fig. S4)
PMID:38442865	FYPO:0008233	(Fig. S4)
PMID:38442865	FYPO:0008233	(Fig. S4)
PMID:38442865	PBO:0112942	(Fig. 2A, B and C)
PMID:38442865	FYPO:0007114	(Fig. 2A, B and C)
PMID:38442865	FYPO:0007114	(Fig. 2A, B and C)
PMID:38442865	PBO:0112941	(Fig. 1A and B)
PMID:38442865	PBO:0112945	(Fig. 2D, E and F)
PMID:38442865	PBO:0112943	(Fig. 2D, E and F)
PMID:38442865	PBO:0112946	(Fig. 2D, E and F)
PMID:38442865	FYPO:0008233	(Fig. 2D, E and F)
PMID:38442865	PBO:0112947	((Fig. 3A and C))
PMID:38442865	PBO:0112948	((Fig. 3A and C))
PMID:38442865	PBO:0112949	((Fig. 3A and C))
PMID:38442865	PBO:0112950	((Fig. 3B and C))
PMID:38442865	PBO:0112951	((Fig. 3B and C))
PMID:38442865	PBO:0112952	((Fig. 3B and C))
PMID:38442865	FYPO:0000177	(Fig. 1C)
PMID:38442865	PBO:0111723	(Fig. 1E)
PMID:38442865	PBO:0093562	(Fig. S1)
PMID:38442865	PBO:0112953	(Fig. 3D, E and F)
PMID:38442865	PBO:0112946	(Fig. 3D, E and F)
PMID:38442865	PBO:0093562	(Fig. S1)
PMID:38442865	PBO:0093562	(Fig. S1)
PMID:38442865	PBO:0093564	(Fig. 1D)
PMID:38442865	PBO:0113834	Our studies have shed light on novel functions of the MOR in non-centrosomal MTOCs and cytoplasmic microtubule organization.
PMID:38442865	PBO:0113834	Our studies have shed light on novel functions of the MOR in non-centrosomal MTOCs and cytoplasmic microtubule organization.
PMID:38442865	PBO:0113834	Our studies have shed light on novel functions of the MOR in non-centrosomal MTOCs and cytoplasmic microtubule organization.
PMID:38442865	PBO:0112943	(Fig. S1E and F)
PMID:38442865	PBO:0113834	Our studies have shed light on novel functions of the MOR in non-centrosomal MTOCs and cytoplasmic microtubule organization.
PMID:38442865	FYPO:0008233	(Fig. 3D, E and F)
PMID:38442865	FYPO:0008233	(Fig. 3D, E and F)
PMID:38442865	PBO:0112942	(Fig. S1E and F)
PMID:38442865	PBO:0112954	(Fig. 4B)
PMID:38442865	PBO:0093562	(Fig. 1D)
PMID:38442865	PBO:0093559	(Fig. 1D)
PMID:38442865	PBO:0093560	(Fig. 1D)
PMID:38442865	PBO:0112944	(Fig. 1E)
PMID:38442865	PBO:0112942	(Fig. S1E and F)
PMID:38442865	PBO:0112945	(Fig. S1E and F)
PMID:38442865	FYPO:0008233	(Fig. S4)
PMID:38442865	FYPO:0008233	(Fig. S4)
PMID:38448160	GO:0031619	Indeed, cells expressing Psm3-2A (alanine substitution at T182 and S1001) showed mono-orientation defects (20%) albeit mildly, compared with WT (12%) (Fig 3C), suggesting that phosphorylation of these sites might contribute to establishing cohesion at the core centromeres.....We speculate that the Psm3 phosphorylation at the gate may play a role in transiently loosening Rec8-Psm3 gate to facilitate establishment of cohesion at the core centromere.
PMID:38448160	PBO:0112245	(Figure 2D)
PMID:38448160	PBO:0112136	(Fig. 3C)
PMID:38448160	PBO:0112137	(Figure 3D)
PMID:38448160	PBO:0112138	(Figure 4B)
PMID:38448160	PBO:0112155	(Figs 3A and S3A-E) We examined if Psm3 is phosphorylated by Plo1 in vitro and found phosphorylation of T182 in the N terminus and S1001 in the C terminus, both locate in the coiled-coil region of the DNA exit gate (Figs 3A and S3A-E), These results suggest that the phosphorylation at Psm3-S110 specifically regulates Rec8 cohesin at centromeres most likely depending on Moa1-Plo1.
PMID:38448160	PBO:0095113	We examined if Psm3 is phosphorylated by Plo1 in vitro and found phosphorylation of T182 in the N terminus and S1001 in the C terminus (Fig. S3)
PMID:38448160	FYPO:0003176	(Fig. 2B)
PMID:38448160	PBO:0095113	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	PBO:0112146	(Fig. 3D)
PMID:38448160	GO:0031619	Accordingly, rec8-15A psm3-3A double mutant showed more defects in mono-orientation than either rec8-15A or psm3-3A mutant (Fig 4E), suggesting that the phosphorylation on Rec8 and Psm3 cooperatively act to establish cohesion at the core centromeres.
PMID:38448160	PBO:0095113	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	PBO:0095113	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	PBO:0095113	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	PBO:0095113	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	PBO:0095113	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	PBO:0095113	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	GO:0031619	Indeed, cells expressing Psm3-2A (alanine substitution at T182 and S1001) showed mono-orientation defects (20%) albeit mildly, compared with WT (12%) (Fig 3C), suggesting that phosphorylation of these sites might contribute to establishing cohesion at the core centromeres.
PMID:38448160	PBO:0095113	We examined if Psm3 is phosphorylated by Plo1 in vitro and found phosphorylation of T182 in the N terminus and S1001 in the C terminus (Fig. S3)
PMID:38448160	GO:0031619	In moa1Δ cells, a minority population (11%) of cells underwent equational segregation at meiosis I (because of defects in mono-orientation), whereas the majority underwent reductional segregation due to the presence of chiasmata and tension exerted across homologs, as reported previously (Miyazaki et al, 2017) (Fig 2B)
PMID:38448160	GO:1990813	suggesting that 40% of the reductional population underwent random segregation at meiosis II which is originated from loss of cohesion (a defect in cohesion protection) in anaphase I.
PMID:38448160	PBO:0112138	(Figure 4B)
PMID:38448160	PBO:0112138	(Figure 4E)
PMID:38448160	PBO:0112141	(Fig. 1B)
PMID:38448160	PBO:0112142	(Fig. 1B)
PMID:38448160	PBO:0112143	(Fig. 2B) In moa1Δ cells, a minority population (11%) of cells underwent equational segregation at meiosis I (because of defects in mono-orientation), whereas the majority underwent reductional segregation due to the presence of chiasmata and tension exerted across homologs, as reported previously (Miyazaki et al, 2017) (Fig 2B).
PMID:38448160	PBO:0112497	(comment: CHECK Unequal sister chromatid segregation in meiosis II after reductional segregation in meiosis I.) Fig. 2B
PMID:38448160	PBO:0112502	(Fig. 2B)
PMID:38448160	PBO:0112246	(Figure 2D)
PMID:38448160	PBO:0112146	(Figure 2D)
PMID:38448160	PBO:0112147	(Figure 2D) Remarkably, introducing the rec8-15A mutation into rec12Δ rec8-2A cells increased equational segregation to 36% (Fig 2D), suggesting that phosphorylation at some or all 15S/T sites in Rec8 is contributing at least partly to establishing mono-orientation, most likely by promoting cohesion at the core centromeres.
PMID:38448160	PBO:0095113	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	PBO:0095113	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	PBO:0095113	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	PBO:0095113	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	PBO:0095113	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	PBO:0095113	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	PBO:0095113	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	PBO:0095113	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	PBO:0095113	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	PBO:0095113	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	MOD:00696	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	PBO:0112148	(comment: Measured in two-hybrid assay using only the N-terminal 245aa part of Rec8) (Fig. 2F)
PMID:38448160	PBO:0095113	We examined if Psm3 is phosphorylated by Plo1 in vitro and found phosphorylation of T182 in the N terminus and S1001 in the C terminus (Fig. S3)
PMID:38448160	PBO:0112510	(comment: Unequal sister chromatid segregation in meiosis II after reductional segregation in meiosis I.) Fig. 3D
PMID:38448160	PBO:0109783	(Figure 3D)
PMID:38448160	PBO:0112510	(comment: Unequal sister chromatid segregation in meiosis II after reductional segregation in meiosis I.) Fig. 3D
PMID:38448160	PBO:0112149	(Fig. 3E)
PMID:38448160	PBO:0112150	(Fig. 3E)
PMID:38448160	PBO:0112151	(Fig. 3F)
PMID:38448160	FYPO:0003176	(Fig. 3D)
PMID:38448160	FYPO:0003176	(Fig. 4D)
PMID:38448160	FYPO:0003176	(Fig. 4D)
PMID:38448160	PBO:0112137	(Figure 4E)
PMID:38448160	PBO:0112247	(Figure 4E)
PMID:38448160	PBO:0109676	(Figure 4E)
PMID:38448160	PBO:0109676	(Figure 4E)
PMID:38448160	PBO:0112153	(Figure 4E)
PMID:38448160	PBO:0112153	segregation defects in psm3-3A in achiasmatic meiosis I suppressed by wpl1 deletion. Figure 4E
PMID:38448160	PBO:0112153	segregation defects in psm3-3A in achiasmatic meiosis I suppressed by wpl1 deletion. Figure 4E
PMID:38448160	PBO:0112154	(Fig. 1B) In moa1Δ cells, Rec8 cohesin localization increases at the core centromere although sister chromatid cohesion is abolished at this sit
PMID:38448160	PBO:0095113	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	PBO:0095113	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	PBO:0095113	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	PBO:0095113	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	PBO:0095113	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	PBO:0095113	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	PBO:0095113	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448439	PBO:0112877	All subunits in the Arp2/3 complex, except for Arp2 and ARPC5, contact the mother filament directly.
PMID:38448439	PBO:0112877	All subunits in the Arp2/3 complex, except for Arp2 and ARPC5, contact the mother filament directly.
PMID:38448439	PBO:0112877	All subunits in the Arp2/3 complex, except for Arp2 and ARPC5, contact the mother filament directly.
PMID:38448439	PBO:0112877	All subunits in the Arp2/3 complex, except for Arp2 and ARPC5, contact the mother filament directly.
PMID:38448439	PBO:0112877	All subunits in the Arp2/3 complex, except for Arp2 and ARPC5, contact the mother filament directly.
PMID:38448439	PBO:0112877	All subunits in the Arp2/3 complex, except for Arp2 and ARPC5, contact the mother filament directly.
PMID:38448439	GO:0090135	Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 comple
PMID:38448439	GO:0090135	Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 comple
PMID:38448439	GO:0090135	Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 comple
PMID:38448439	GO:0090135	Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 comple
PMID:38448439	GO:0090135	Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 comple
PMID:38448439	GO:0090135	Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 comple
PMID:38448439	GO:0090135	Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 comple
PMID:38479839	PBO:0112329	(comment: Transfers parental histone H3-H4 on the lagging strand.)
PMID:38479839	PBO:0112329	(comment: Work with Dpb4 for parental histone H3-H4 transfer on the leading strand)
PMID:38479839	PBO:0112332	(Fig. 3)
PMID:38479839	PBO:0103245	(Fig. 3D)
PMID:38479839	PBO:0103245	(Fig. 3D)
PMID:38479839	FYPO:0008199	(Fig. 3D)
PMID:38479839	PBO:0112318	(Fig. 3E)
PMID:38479839	PBO:0095977	(Fig. 3E)
PMID:38479839	PBO:0095977	(Fig. 3E)
PMID:38479839	PBO:0095977	(Fig. 3E)
PMID:38479839	PBO:0095977	(Fig. 3E)
PMID:38479839	PBO:0103246	(Fig. 3F)
PMID:38479839	PBO:0103247	(Fig. 3F)
PMID:38479839	PBO:0103247	(Fig. 3F)
PMID:38479839	PBO:0103247	(Fig. 3F)
PMID:38479839	PBO:0103247	(Fig. 3F)
PMID:38479839	PBO:0112333	(Fig. 5D)
PMID:38479839	PBO:0112334	(Fig. 6A)
PMID:38479839	PBO:0112330	(Fig. 6A)
PMID:38479839	PBO:0096192	(Fig. 6A)
PMID:38479839	PBO:0096192	(Fig. 6A)
PMID:38479839	PBO:0112767	(Fig. 6B, C and D)
PMID:38479839	PBO:0112331	(Fig. 6B, C and D)
PMID:38479839	PBO:0112335	(Fig. 5D)
PMID:38479839	PBO:0096191	(Fig. S2)
PMID:38479839	PBO:0096191	(Fig. S2)
PMID:38479839	PBO:0112766	(Fig. S2)
PMID:38479839	PBO:0112766	(Fig. S2)
PMID:38479839	FYPO:0004742	(Fig. S2)
PMID:38479839	FYPO:0004742	(Fig. S2)
PMID:38479839	PBO:0112331	(Fig. S5)
PMID:38479839	GO:0006335	(comment: Deposits parental histone H3-H4 on both daughter strands during DNA replication)
PMID:38479839	GO:0006335	(comment: Works with Dpb3 for parental histone H3-H4 transfer on the leading strand)
PMID:38479839	GO:0006335	(comment: Transfers parental histone H3-H4 on the lagging strand.)
PMID:38479839	PBO:0112766	(Fig. 2)
PMID:38479839	PBO:0112766	(Fig. 2)
PMID:38479839	PBO:0096192	(Fig. 1)
PMID:38479839	FYPO:0004742	(Fig. 3)
PMID:38479839	PBO:0112331	(Fig. 2)
PMID:38479839	FYPO:0008186	(Fig. 1E)
PMID:38479839	FYPO:0008186	(Fig. 1E)
PMID:38479839	FYPO:0008186	(Fig. 1E)
PMID:38479839	PBO:0112330	(Fig. 1E)
PMID:38479839	PBO:0096191	(Fig. 1)
PMID:38479839	PBO:0096191	(Fig. 1)
PMID:38479839	PBO:0096191	(Fig. 1)
PMID:38479839	PBO:0094679	(Fig. 3)
PMID:38479839	PBO:0112329	(comment: Deposits parental histone H3-H4 on both daughter strands during DNA replication.)
PMID:38479839	PBO:0112329	(comment: Work with Dpb3 for parental histone H3-H4 transfer on the leading strand)
PMID:38482739	PBO:0093564	(Fig. S3)
PMID:38482739	PBO:0114170	in the present study we show that the DNA-binding activity of Cbf11 is implicated in all its known functions, with the regulation of lipid metabolism genes remaining the best characterized role of Cbf11.
PMID:38482739	FYPO:0001403	(Fig. 1A)
PMID:38482739	FYPO:0000010	(Fig. 1B)
PMID:38482739	PBO:0114171	(Fig. 1D and E)
PMID:38482739	PBO:0114172	(Fig. 1D and E)
PMID:38482739	PBO:0114173	(Fig. S2C)
PMID:38482739	PBO:0114174	(Fig. S2C)
PMID:38482739	PBO:0114175	(Fig. S2C)
PMID:38482739	PBO:0114176	(Fig. S2C)
PMID:38482739	PBO:0114177	(Fig. S2C)
PMID:38482739	PBO:0114154	(Fig. S2C)
PMID:38482739	PBO:0114178	(Fig. S2C)
PMID:38482739	PBO:0114178	(Fig. S2C)
PMID:38482739	PBO:0033073	(Fig. 2A and B)
PMID:38482739	PBO:0093564	(Fig. S3)
PMID:38482739	PBO:0114158	(Fig. 3A and B)
PMID:38482739	PBO:0114159	(Fig. 3C and D)
PMID:38482739	PBO:0114160	(Fig. 3C and D)
PMID:38482739	PBO:0114161	(Fig. 3C and D)
PMID:38482739	PBO:0114162	(Fig. 3C and D)
PMID:38482739	PBO:0114163	(Fig. 3C and D)
PMID:38482739	PBO:0114164	(Fig. 3C and D)
PMID:38482739	PBO:0114165	(Fig. 3C and D)
PMID:38482739	PBO:0114166	(Fig. 3C and D)
PMID:38482739	PBO:0114179	(Fig. 3F and G)
PMID:38482739	PBO:0114180	(Fig. 3F and G)
PMID:38482739	PBO:0114181	(Fig. S2E)
PMID:38482739	PBO:0114182	(Fig. S2E)
PMID:38482739	PBO:0114183	(Fig. S2E)
PMID:38482739	PBO:0093579	(Fig. 4D)
PMID:38482739	FYPO:0001355	(Fig. 4D)
PMID:38482739	FYPO:0001403	(Fig. 1A)
PMID:38482739	FYPO:0000010	(Fig. 1B)
PMID:38482739	PBO:0114153	(Fig. 2A and B)
PMID:38482739	FYPO:0002737	(Fig. 2A)
PMID:38482739	FYPO:0001118	(Fig. 2A)
PMID:38482739	PBO:0114154	(Fig. 1C)
PMID:38482739	PBO:0114155	(Fig. 1C)
PMID:38482739	PBO:0114154	(Fig. 1C)
PMID:38482739	PBO:0114155	(Fig. 1C)
PMID:38482739	PBO:0114156	(Fig. 1C)
PMID:38482739	PBO:0114157	(Fig. 1D and E)
PMID:38482739	PBO:0114158	(Fig. 3A and B)
PMID:38482739	PBO:0114159	(Fig. 3C and D)
PMID:38482739	PBO:0114160	(Fig. 3C and D)
PMID:38482739	PBO:0114161	(Fig. 3C and D)
PMID:38482739	PBO:0114162	(Fig. 3C and D)
PMID:38482739	PBO:0114163	(Fig. 3C and D)
PMID:38482739	PBO:0114164	(Fig. 3C and D)
PMID:38482739	PBO:0114165	(Fig. 3C and D)
PMID:38482739	PBO:0114166	(Fig. 3C and D)
PMID:38482739	PBO:0114167	(Fig. 3F and G)
PMID:38482739	PBO:0093614	(Fig. 4)
PMID:38482739	PBO:0093615	(Fig. 4)
PMID:38482739	PBO:0093613	(Fig. 4B)
PMID:38482739	PBO:0093614	(Fig. 4)
PMID:38482739	FYPO:0001690	(Fig. 4B)
PMID:38482739	PBO:0093613	(Fig. 4C)
PMID:38482739	PBO:0093615	(Fig. 4C)
PMID:38482739	FYPO:0000957	(Fig. 4D)
PMID:38482739	FYPO:0000957	(Fig. 4D)
PMID:38482739	FYPO:0000957	(Fig. 4D)
PMID:38482739	PBO:0114168	(Fig. 4D)
PMID:38482739	PBO:0097220	(Fig. 4D)
PMID:38482739	FYPO:0000006	(Fig. 4G and H)
PMID:38482739	FYPO:0000006	(Fig. 6)
PMID:38482739	FYPO:0005995	(Fig. 5)
PMID:38482739	FYPO:0005995	(Fig. 5)
PMID:38482739	FYPO:0000972	(Fig. 7A and B)
PMID:38482739	FYPO:0006494	(Fig. 7C)
PMID:38482739	FYPO:0006470	(Fig. 7D)
PMID:38482739	PBO:0114169	(Fig. 7F)
PMID:38482739	PBO:0093563	(Fig. 7G)
PMID:38482739	PBO:0093563	(Fig. 7G)
PMID:38482739	PBO:0093615	(Fig. 7G)
PMID:38482739	PBO:0093615	(Fig. 7G)
PMID:38482739	FYPO:0001355	(Fig. S1)
PMID:38482739	FYPO:0001357	(Fig. S1)
PMID:38499131	PBO:0116341	We found that Rsv2, Zym1 and Gst2 were upregulated both at the mRNA and protein levels in Δppr2 cells in exponential phase (6 h after incubation) (Fig. 5). The protein levels of Sod2 was increased in Δppr2 cells but their mRNA levels were unchanged (Fig. 5).
PMID:38499131	PBO:0116340	We found that Rsv2, Zym1 and Gst2 were upregulated both at the mRNA and protein levels in Δppr2 cells in exponential phase (6 h after incubation) (Fig. 5). The protein levels of Sod2 was increased in Δppr2 cells but their mRNA levels were unchanged (Fig. 5).
PMID:38499131	PBO:0116333	. Interestingly, deletion of ppr2 increased Gpx1 in cytosolic, whereas decreased Gpx1 in the mitochondria (Fig. 2A).
PMID:38499131	PBO:0116334	In Δppr2 cells, Php4-GFP was localized in the nucleus at time points from 6 h to 36 h, in iron-replete conditions. In wild-type strains, Php4-GFP was exported from the nucleus, exhibiting fluorescence in the cytoplasm of cells from 6hto36h(Fig. 2).
PMID:38499131	FYPO:0004164	The levels of ROS in Ppr2-deficient cells were significantly higher compared to WT cells (Fig. 4A). The ppr2 deletion mutant was sensitive to H2O2 during the stationary phase, whereas WT retained tolerance to H2O2 (Fig. 4B).
PMID:38499131	FYPO:0000087	(Figure 4) (comment: vw: not mentioned in text)
PMID:38499131	PBO:0095014	We found that Rsv2, Zym1 and Gst2 were upregulated both at the mRNA and protein levels in Δppr2 cells in exponential phase (6 h after incubation) (Fig. 5). The protein levels of Sod2 was increased in Δppr2 cells but their mRNA levels were unchanged (Fig. 5).
PMID:38499131	PBO:0095012	We found that Rsv2, Zym1 and Gst2 were upregulated both at the mRNA and protein levels in Δppr2 cells in exponential phase (6 h after incubation) (Fig. 5). The protein levels of Sod2 was increased in Δppr2 cells but their mRNA levels were unchanged (Fig. 5).
PMID:38499131	PBO:0093798	We observed reduced growth of the ppr2 deletion mutant on glycerol- and galactose-containing media compared to on the glucose-containing media (Fig. 1A).
PMID:38499131	FYPO:0001357	(Figure 2C) control We found that the overexpression of Gpx1 could rescue the viability of Δppr2 cells as Gpx1-HA showed significantly increased viability compared with Δppr2 cells and similar to WT strain on YE plates (Fig. 2C). Additionally, overexpression of Gpx1 could also partially rescue respiratory growth defect in Δppr2 cells as Gpx1-HA could grow on Gly plates better than Δppr2 cells (Fig. 2D).
PMID:38499131	FYPO:0001357	(Figure 2C) control We found that the overexpression of Gpx1 could rescue the viability of Δppr2 cells as Gpx1-HA showed significantly increased viability compared with Δppr2 cells and similar to WT strain on YE plates (Fig. 2C). Additionally, overexpression of Gpx1 could also partially rescue respiratory growth defect in Δppr2 cells as Gpx1-HA could grow on Gly plates better than Δppr2 cells (Fig. 2D).
PMID:38499131	FYPO:0001357	(Figure 2C) control We found that the overexpression of Gpx1 could rescue the viability of Δppr2 cells as Gpx1-HA showed significantly increased viability compared with Δppr2 cells and similar to WT strain on YE plates (Fig. 2C). Additionally, overexpression of Gpx1 could also partially rescue respiratory growth defect in Δppr2 cells as Gpx1-HA could grow on Gly plates better than Δppr2 cells (Fig. 2D).
PMID:38499131	PBO:0116338	3.7. Sty1 and Pap1 accumulate in the nucleus during the stationary phase in Δppr2 cells
PMID:38499131	PBO:0116337	3.7. Sty1 and Pap1 accumulate in the nucleus during the stationary phase in Δppr2 cells
PMID:38499131	PBO:0116336	We found that Rsv2, Zym1 and Gst2 were upregulated both at the mRNA and protein levels in Δppr2 cells in exponential phase (6 h after incubation) (Fig. 5). The protein levels of Sod2 was increased in Δppr2 cells but their mRNA levels were unchanged (Fig. 5).
PMID:38499131	PBO:0112960	respiration deficient: Glycerol is a carbon source that can be metabolized only through oxidative phosphorylation, producing ATP through the electron transport chain in the mitochondria. . Like other respiration-deficient mutants, the reduced growth rate of the ppr2 mutant on this medium indicates that it is not able to effectively carry out this process.
PMID:38499131	PBO:0112960	respiration deficient: Glycerol is a carbon source that can be metabolized only through oxidative phosphorylation, producing ATP through the electron transport chain in the mitochondria. . Like other respiration-deficient mutants, the reduced growth rate of the ppr2 mutant on this medium indicates that it is not able to effectively carry out this process.
PMID:38499131	PBO:0116328	We found that Sdh2 and Hem15 were downregulated at the protein levels in Δppr2 cells (Fig. 1B)
PMID:38499131	PBO:0116329	We found that Sdh2 and Hem15 were downregulated at the protein levels in Δppr2 cells (Fig. 1B)
PMID:38499131	PBO:0095013	We found that Rsv2, Zym1 and Gst2 were upregulated both at the mRNA and protein levels in Δppr2 cells in exponential phase (6 h after incubation) (Fig. 5). The protein levels of Sod2 was increased in Δppr2 cells but their mRNA levels were unchanged (Fig. 5).
PMID:38499131	PBO:0116330	We found that Sdh2 and Hem15 were downregulated at the protein levels in Δppr2 cells (Fig. 1B)
PMID:38499131	PBO:0116331	The results in our qRT-PCR analysis on the genes of hem15 showed to be slightly down-regulated and the expression of sdh2 was not significantly altered by deletion of ppr2 (Fig. S1).
PMID:38499131	PBO:0116332	. Interestingly, deletion of ppr2 increased Gpx1 in cytosolic, whereas decreased Gpx1 in the mitochondria (Fig. 2A).
PMID:38499131	PBO:0116335	We found that Rsv2, Zym1 and Gst2 were upregulated both at the mRNA and protein levels in Δppr2 cells in exponential phase (6 h after incubation) (Fig. 5). The protein levels of Sod2 was increased in Δppr2 cells but their mRNA levels were unchanged (Fig. 5).
PMID:38499131	PBO:0116339	We found that Rsv2, Zym1 and Gst2 were upregulated both at the mRNA and protein levels in Δppr2 cells in exponential phase (6 h after incubation) (Fig. 5). The protein levels of Sod2 was increased in Δppr2 cells but their mRNA levels were unchanged (Fig. 5).
PMID:38499131	PBO:0093796	We observed reduced growth of the ppr2 deletion mutant on glycerol- and galactose-containing media compared to on the glucose-containing media (Fig. 1A).
PMID:38499131	PBO:0093793	We observed reduced growth of the ppr2 deletion mutant on glycerol- and galactose-containing media compared to on the glucose-containing media (Fig. 1A).
PMID:38499152	GO:0097177	Mrh5C subunits no longer associate with each other. Mrh5 co-immunoprecipitated with the mtSSU as expected (Fig. 3A). Deletion of mtf2 dramatically reduced this association, suggesting that the whole complex is involved in mtSSU binding (Fig. 3A). |Mrh5C was predominantly associated with the mtSSU in WT cells (Fig. 3D)
PMID:38499152	PBO:0114755	(Fig. 1A)
PMID:38499152	PBO:0114790	(comment: CHECK ABOLISHED ********) These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C).
PMID:38499152	PBO:0114777	In control cells (Δpnu1[Δi]), the cox1 and cob1 mRNAs appeared in two peaks, a major peak (peak A) comigrating with the mtSSU and a second peak (peak B) comigrating with the mitoribosome (Fig. 4). In Δmtf2 cells, peak A was up-shifted to the lower-density regions and did not comigrate with the mtSSU, and peak B decreased dramatically (Fig. 4).
PMID:38499152	PBO:0114778	In control cells (Δpnu1[Δi]), the cox1 and cob1 mRNAs appeared in two peaks, a major peak (peak A) comigrating with the mtSSU and a second peak (peak B) comigrating with the mitoribosome (Fig. 4). In Δmtf2 cells, peak A was up-shifted to the lower-density regions and did not comigrate with the mtSSU, and peak B decreased dramatically (Fig. 4).
PMID:38499152	PBO:0114798	Immunoblot analysis of factions revealed that mutation of the DEAD-box of Mrh5 abolished the association of the cox1 mRNA with the mtSSU (Fig. 8).
PMID:38499152	PBO:0114797	Immunoblot analysis of factions revealed that mutation of the DEAD-box of Mrh5 abolished the association of the cox1 mRNA with the mtSSU (Fig. 8).
PMID:38499152	PBO:0114796	Immunoblot analysis of factions revealed that mutation of the DEAD-box of Mrh5 abolished the association of the cox1 mRNA with the mtSSU (Fig. 8).
PMID:38499152	PBO:0114776	In contrast, Mrh5C subunits no longer co-sedimented with the mtSSU in Δmtf2 cells (Fig. 3D)
PMID:38499152	PBO:0114779	A single Asp261 to Ala or Glu262 to Ala mutation gave rise to a substantially reduced level of cox1 mRNA but little or no reduction of the levels of other mt- mRNAs and mt-rRNAs (Fig. 5A).
PMID:38499152	FYPO:0002056	(comment: [35S]-methionine/cysteine labeling)
PMID:38499152	PBO:0114789	These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C).
PMID:38499152	PBO:0114754	Deletion of mrh5 did not reduce the protein level of Ppr4 (Fig. 1A)
PMID:38499152	PBO:0114793	These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C).
PMID:38499152	PBO:0114756	Additionally, the Mtf2 protein level was moderately reduced in Δmrh5 cells (Fig. 1A).
PMID:38499152	PBO:0114768	Mutations of the DEAD-box in Mrh5-Myc resulted in the dissociation of the Mrh5 mutants with the mtSSU (Figs. 7 and S6).
PMID:38499152	PBO:0114778	Immunoblot analysis of factions revealed that mutation of the DEAD-box of Mrh5 abolished the association of the cox1 mRNA with the mtSSU (Fig. 8).
PMID:38499152	PBO:0114777	Immunoblot analysis of factions revealed that mutation of the DEAD-box of Mrh5 abolished the association of the cox1 mRNA with the mtSSU (Fig. 8).
PMID:38499152	PBO:0114796	Immunoblot analysis of factions revealed that mutation of the DEAD-box of Mrh5 abolished the association of the cox1 mRNA with the mtSSU (Fig. 8).
PMID:38499152	PBO:0114797	Immunoblot analysis of factions revealed that mutation of the DEAD-box of Mrh5 abolished the association of the cox1 mRNA with the mtSSU (Fig. 8).
PMID:38499152	PBO:0114757	(Fig. 1A)
PMID:38499152	PBO:0114775	In contrast, Mrh5C subunits no longer co-sedimented with the mtSSU in Δmtf2 cells (Fig. 3D)
PMID:38499152	PBO:0114774	In contrast, Mrh5C subunits no longer co-sedimented with the mtSSU in Δmtf2 cells (Fig. 3D)
PMID:38499152	PBO:0114773	Deletion of mtf2 or other subunits of Mrh5C dramatically reduced the levels of mtSSU proteins but not the large subunit of the mitoribosome (mtLSU) proteins tested (Figure 3, B and C)
PMID:38499152	PBO:0114772	Deletion of mtf2 or other subunits of Mrh5C dramatically reduced the levels of mtSSU proteins but not the large subunit of the mitoribosome (mtLSU) proteins tested (Figure 3, B and C)
PMID:38499152	PBO:0114771	Deletion of mtf2 or other subunits of Mrh5C dramatically reduced the levels of mtSSU proteins but not the large subunit of the mitoribosome (mtLSU) proteins tested (Figure 3, B and C)
PMID:38499152	PBO:0114770	Deletion of mtf2 or other subunits of Mrh5C dramatically reduced the levels of mtSSU proteins but not the large subunit of the mitoribosome (mtLSU) proteins tested (Figure 3, B and C)
PMID:38499152	PBO:0114769	Deletion of mtf2 or other subunits of Mrh5C dramatically reduced the levels of mtSSU proteins but not the large subunit of the mitoribosome (mtLSU) proteins tested (Figure 3, B and C)
PMID:38499152	PBO:0114767	Mrh5C subunits no longer associate with each other. Mrh5 co-immunoprecipitated with the mtSSU as expected (Fig. 3A). Deletion of mtf2 dramatically reduced this association, suggesting that the whole complex is involved in mtSSU binding (Fig. 3A).
PMID:38499152	PBO:0114765	Similarly, deletion of ppr4 did not impair the interaction among Mrh5-Myc, Sls1-FLAG, and Mtf2-HA (Fig. 2E).
PMID:38499152	PBO:0114766	Similarly, deletion of ppr4 did not impair the interaction among Mrh5-Myc, Sls1-FLAG, and Mtf2-HA (Fig. 2E).
PMID:38499152	PBO:0114765	Deletion of mrh5 did not impair the interaction among Prp4-CBP, Sls1-FLAG, and Mtf2-HA (Fig. 2D).
PMID:38499152	PBO:0114764	Deletion of mrh5 did not impair the interaction among Prp4-CBP, Sls1-FLAG, and Mtf2-HA (Fig. 2D).
PMID:38499152	PBO:0114763	Co-immunoprecipitation experiments using anti-Myc beads revealed that loss of sls1 abolished the association of Mrh5-Myc with Prp4-CBP and Mtf2-HA (Fig. 2C).
PMID:38499152	PBO:0114762	Co-immunoprecipitation experiments using anti-Myc beads revealed that loss of sls1 abolished the association of Mrh5-Myc with Prp4-CBP and Mtf2-HA (Fig. 2C).
PMID:38499152	PBO:0114762	Co-immunoprecipitation experiments with anti-FLAG beads showed that deletion of mtf2 abolished the interaction of Sls1- FLAG with Mrh5-Myc and Ppr4-CBP (Fig. 2A).
PMID:38499152	PBO:0114761	Co-immunoprecipitation experiments with anti-FLAG beads showed that deletion of mtf2 abolished the interaction of Sls1- FLAG with Mrh5-Myc and Ppr4-CBP (Fig. 2A).
PMID:38499152	PBO:0114760	Co-immunoprecipitation experiments with anti-FLAG beads showed that deletion of mtf2 abolished the interaction of Sls1- FLAG with Mrh5-Myc and Ppr4-CBP (Fig. 2A).
PMID:38499152	PBO:0114755	In contrast, the deletion of ppr4 and mtf2 did not or only moderately affect the protein levels of other Mrh5C subunits (Fig. 1, C and D).
PMID:38499152	PBO:0114757	In contrast, the deletion of ppr4 and mtf2 did not or only moderately affect the protein levels of other Mrh5C subunits (Fig. 1, C and D).
PMID:38499152	FYPO:0002056	(comment: [35S]-methionine/cysteine labeling)
PMID:38499152	PBO:0114789	These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C)
PMID:38499152	PBO:0114798	Immunoblot analysis of factions revealed that mutation of the DEAD-box of Mrh5 abolished the association of the cox1 mRNA with the mtSSU (Fig. 8).
PMID:38499152	FYPO:0002056	(comment: [35S]-methionine/cysteine labeling)
PMID:38499152	PBO:0112960	It is likely that the abolishment of Cox1 synthesis results in the downregulation of OXPHOS complexes. Consistent with these results, cells harboring mrh5D261A-Myc or mrh5E262A-Myc could not grow on glycerol-containing medium, suggesting that they are respiratory-deficient (Fig. S5).
PMID:38499152	PBO:0112960	It is likely that the abolishment of Cox1 synthesis results in the downregulation of OXPHOS complexes. Consistent with these results, cells harboring mrh5D261A-Myc or mrh5E262A-Myc could not grow on glycerol-containing medium, suggesting that they are respiratory-deficient (Fig. S5).
PMID:38499152	PBO:0114795	Mutations of the DEAD-box in Mrh5-Myc resulted in the dissociation of the Mrh5 mutants with the mtSSU (Figs. 7 and S6).
PMID:38499152	PBO:0114754	In contrast, the deletion of ppr4 and mtf2 did not or only moderately affect the protein levels of other Mrh5C subunits (Fig. 1, C and D).
PMID:38499152	PBO:0114757	In contrast, the deletion of ppr4 and mtf2 did not or only moderately affect the protein levels of other Mrh5C subunits (Fig. 1, C and D).
PMID:38499152	PBO:0114755	In contrast, the deletion of ppr4 and mtf2 did not or only moderately affect the protein levels of other Mrh5C subunits (Fig. 1, C and D).
PMID:38499152	PBO:0114791	These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C).
PMID:38499152	PBO:0114758	Deletion of sls1 resulted in a drastic reduction in the protein level of Mtf2 (Fig. 1B). A
PMID:38499152	PBO:0114759	In contrast, the deletion of ppr4 and mtf2 did not or only moderately affect the protein levels of other Mrh5C subunits (Fig. 1, C and D).
PMID:38499152	PBO:0114790	These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C)
PMID:38499152	PBO:0114791	These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C)
PMID:38499152	PBO:0114792	These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C)
PMID:38499152	PBO:0114793	These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C)
PMID:38499152	PBO:0114792	These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C).
PMID:38598031	PBO:0037579	(Figure 5)
PMID:38598031	GO:0005737	(Figure 5)
PMID:38598031	GO:0005634	(Figure 5)
PMID:38598031	PBO:0112567	(Figure 4a)
PMID:38598031	PBO:0112566	(Figure 4)
PMID:38598031	GO:0005886	(Figure 4)
PMID:38598031	PBO:0112574	(Figure 6)
PMID:38598031	PBO:0112574	(Figure 6)
PMID:38598031	PBO:0112573	(Figure 6)
PMID:38598031	PBO:0112573	(Figure 6)
PMID:38598031	PBO:0093595	(Figure 3a)
PMID:38598031	PBO:0093594	(Figure 2)
PMID:38598031	PBO:0107560	(Figure 2)
PMID:38598031	PBO:0093595	(Figure 2)
PMID:38598031	PBO:0093595	(Figure 2)
PMID:38598031	PBO:0096587	(Figure 2)
PMID:38598031	PBO:0096587	(Figure 2)
PMID:38598031	PBO:0093594	(Figure 3a)
PMID:38598031	PBO:0107560	(Figure 3a)
PMID:38598031	PBO:0107568	(Figure 5)
PMID:38598031	PBO:0107568	(Figure 5)
PMID:38598031	PBO:0093594	(Figure 3b)
PMID:38598031	PBO:0107560	(Figure 2)
PMID:38598031	PBO:0093594	(Figure 2)
PMID:38598031	FYPO:0001020	(Figure 2)
PMID:38598031	FYPO:0005947	(Figure 2)
PMID:38598031	PBO:0107560	(Figure 1b)
PMID:38598031	PBO:0093594	(Figure 1a)
PMID:38598031	FYPO:0001020	(Figure 3b)
PMID:38598031	PBO:0093594	(Figure 3b)
PMID:38598031	PBO:0096587	(Figure 3a)
PMID:38598031	PBO:0096587	(Figure 3a)
PMID:38598031	PBO:0112568	(Figure 5)
PMID:38598031	PBO:0112569	(Figure 5)
PMID:38598031	PBO:0112572	(Figure 4a)
PMID:38598031	PBO:0112570	(Figure 6)
PMID:38598031	PBO:0107570	(Figure 6)
PMID:38598031	PBO:0112571	(Figure 6)
PMID:38598031	PBO:0112570	(Figure 6)
PMID:38598031	PBO:0107569	(Figure 6)
PMID:38598031	PBO:0107570	(Figure 6)
PMID:38598031	PBO:0112569	(Figure 5)
PMID:38598031	PBO:0107568	(Figure 5)
PMID:38598031	PBO:0107568	(Figure 5)
PMID:38598031	PBO:0112568	(Figure 5)
PMID:38598031	PBO:0093595	(Figure 3a)
PMID:38598031	PBO:0107565	(Figure 5)
PMID:38598031	PBO:0107562	(Figure 4)
PMID:38598031	GO:0005783	(Figure 4)
PMID:38598031	PBO:0107560	(Figure 3c) rst2∆ partially rescues the pps1∆ pka1∆ strain on CaCl2
PMID:38598031	PBO:0093595	(Figure 3c) rst2∆ partially rescues the pps1∆ pka1∆ strain on KCl
PMID:38598031	PBO:0107560	(Figure 3c)
PMID:38598031	PBO:0093594	(Figure 3c)
PMID:38598031	FYPO:0001020	(Figure 3c)
PMID:38598031	FYPO:0005947	(Figure 3c)
PMID:38598031	PBO:0112570	(Figure 6)
PMID:38598031	PBO:0112571	(Figure 6)
PMID:38598031	PBO:0107560	(Figure 3b)
PMID:38598031	PBO:0112570	(Figure 6)
PMID:38598031	PBO:0112574	(Figure 6)
PMID:38598031	PBO:0112574	(Figure 6)
PMID:38677290	PBO:0116456	Surprisingly, arginine substitutions of the hydrophobic residues (L101R, L108R, V141R, and V148R) led to degradation and insolubility of mutant proteins of spTbf1TRFH (Figures S3). | Consistently, all L101R, L108R, V141R, and V148R mutations resulted in great degradation of spTbf1 in cells (Figure 2E).
PMID:38677290	PBO:0116456	Surprisingly, arginine substitutions of the hydrophobic residues (L101R, L108R, V141R, and V148R) led to degradation and insolubility of mutant proteins of spTbf1TRFH (Figures S3). | Consistently, all L101R, L108R, V141R, and V148R mutations resulted in great degradation of spTbf1 in cells (Figure 2E).
PMID:38677290	PBO:0116456	Surprisingly, arginine substitutions of the hydrophobic residues (L101R, L108R, V141R, and V148R) led to degradation and insolubility of mutant proteins of spTbf1TRFH (Figures S3) | Consistently, all L101R, L108R, V141R, and V148R mutations resulted in great degradation of spTbf1 in cells (Figure 2E).
PMID:38677290	PBO:0116456	Surprisingly, arginine substitutions of the hydrophobic residues (L101R, L108R, V141R, and V148R) led to degradation and insolubility of mutant proteins of spTbf1TRFH (Figures S3) | Consistently, all L101R, L108R, V141R, and V148R mutations resulted in great degradation of spTbf1 in cells (Figure 2E).
PMID:38677290	PBO:0116457	urthermore, we found that all S100A, T104A, and N107A mutant proteins formed aggregation easily during concentration in our purification process, indicating that these three mutations also resulted in protein instability of spTbf1TRFH
PMID:38677290	PBO:0116457	urthermore, we found that all S100A, T104A, and N107A mutant proteins formed aggregation easily during concentration in our purification process, indicating that these three mutations also resulted in protein instability of spTbf1TRFH
PMID:38677290	FYPO:0005018	Interestingly, although the internal loop region (spTbf1loop, residues 320- 407) could not bind S. pombe telomeric DNA alone, it enhanced the binding affinity of both spTbf1TRFH and spTbf1Myb-L (Figure 4F), indicative of important roles of spTbf1loop in spTbf1 recognition of telomeric DNA. Consistently, deletion of the loop region (spTbf1Dloop) significantly reduced the binding affinity of spTbf1 with S. pombe telomeric DNA (Figure 4F).
PMID:38677290	GO:0003691	The spTbf1- TeloDNA complex exhibited a significant supershift, consistent with the previous report that spTbf1 binds S. pombe telomeric dsDNA with high affinity (Figure 4F).32
PMID:38692277	PBO:0112960	Strikingly, we observed a severe synthetic growth defect specifically on respiration-requiring media in the absence of Mmc1 and MICOS subunits (Figure 5D).
PMID:38692277	PBO:0112960	Strikingly, we observed a severe synthetic growth defect specifically on respiration-requiring media in the absence of Mmc1 and MICOS subunits (Figure 5D).
PMID:38692277	GO:0005739	Mmc1-FLAG was detected in the purified mitochondria by western analysis and was protected from Proteinase K digestion, suggesting the protein indeed localizes to mitochondria (Figure 2B
PMID:38692277	PBO:0112957	Approximately half of the Dmmc1 cells had abnormal mitochondrial morphology, and many cells contained the lamellar and ring-shaped mitochondria characteristic of cells with MICOS subunit deletions (Figures 2H and 2I)
PMID:38692277	FYPO:0005419	the absence of MICOS subunits caused characteristic alterations in mitochondrial morphology (Figure 1A).
PMID:38692277	FYPO:0005419	the absence of MICOS subunits caused characteristic alterations in mitochondrial morphology (Figure 1A).
PMID:38692277	FYPO:0005419	the absence of MICOS subunits caused characteristic alterations in mitochondrial morphology (Figure 1A).
PMID:38692277	FYPO:0003393	disruption of cristae architecture through loss of the core MICOS subunit Mic60 caused a growth defect specifically on media that requires respiration (Figure 1D).
PMID:38692277	FYPO:0005419	the absence of MICOS subunits caused characteristic alterations in mitochondrial morphology (Figure 1A).
PMID:38692277	GO:0044284	Both Mic60 and Mic26 appeared in a semi-punctate pattern distributed throughout the mitochondrial network (Figure 1E). These localization data are similar to observations in both budding yeast and human cells,26,38 suggesting that MICOS complexes also concentrate at cristae junctions in fission yeast.
PMID:38692277	GO:0044284	Both Mic60 and Mic26 appeared in a semi-punctate pattern distributed throughout the mitochondrial network (Figure 1E). These localization data are similar to observations in both budding yeast and human cells,26,38 suggesting that MICOS complexes also concentrate at cristae junctions in fission yeast.
PMID:38692277	GO:0061617	As expected, all core MICOS subunits were identified among the top hits by both Mic60 and Mic26 (Figures 1F and 1G, blue).
PMID:38692277	GO:0061617	As expected, all core MICOS subunits were identified among the top hits by both Mic60 and Mic26 (Figures 1F and 1G, blue).
PMID:38692277	GO:0061617	As expected, all core MICOS subunits were identified among the top hits by both Mic60 and Mic26 (Figures 1F and 1G, blue).
PMID:38692277	GO:0042407	(comment: complex member)
PMID:38692277	GO:0042407	(comment: complex member)
PMID:38692277	GO:0042407	(comment: complex member)
PMID:38692277	GO:0061617	As expected, all core MICOS subunits were identified among the top hits by both Mic60 and Mic26 (Figures 1F and 1G, blue).
PMID:38692277	FYPO:0003393	disruption of cristae architecture through loss of the core MICOS subunit Mic60 caused a growth defect specifically on media that requires respiration (Figure 1D).
PMID:38692277	GO:0099617	Instead, Mmc1-FLAG was only degraded after the combined addition of Proteinase K and the detergent Triton X-100, suggesting that the C terminus of Mmc1 localizes to the matrix. Mmc1 was found in the pellet fraction, indicating that it is an integral membrane protein (Figure 2C).
PMID:38692277	GO:0044284	. These data, in combination with previous immuno-EM-labeling experiments of MICOS subunits,31,38 suggest that Mmc1 concentrates at cristae junctions, where it associates in proximity with the MICOS complex.
PMID:38692277	GO:0042407	. Together, these data indicate that Mmc1 is a MICOS complex-associated protein required for normal cristae morphology.
PMID:38692277	PBO:0112958	(comment: CHECK ******NEW TERM REQUIRED ******)In contrast, in the absence of Mic10 and Mic26, which are constituents of a second MICOS subcomplex, Mmc1 lost its semi-punctate appearance and was more uniformly localized throughout the mitochondrial network (Figures 3A and 3B).
PMID:38692277	PBO:0112958	(comment: CHECK ******NEW TERM REQUIRED ******)In contrast, in the absence of Mic10 and Mic26, which are constituents of a second MICOS subcomplex, Mmc1 lost its semi-punctate appearance and was more uniformly localized throughout the mitochondrial network (Figures 3A and 3B).
PMID:38692277	PBO:0112959	the absence of MICOS subunits caused characteristic alterations in mitochondrial morphology (Figure 1A).
PMID:38692277	PBO:0112959	the absence of MICOS subunits caused characteristic alterations in mitochondrial morphology (Figure 1A).
PMID:38692277	FYPO:0003393	disruption of cristae architecture through loss of the core MICOS subunit Mic60 caused a growth defect specifically on media that requires respiration (Figure 1D).
PMID:38692277	FYPO:0003393	disruption of cristae architecture through loss of the core MICOS subunit Mic60 caused a growth defect specifically on media that requires respiration (Figure 1D).
PMID:3870979	FYPO:0002043	(comment: at 33.5 degrees, which is restrictive for cdc2-33 but allows sporulation)
PMID:3870979	FYPO:0001886	(comment: done in h- cells kinetics depend on medium composition (see fig 6B))
PMID:3870979	FYPO:0000583	(comment: at 33.5 degrees, which is restrictive for cdc10129 but allows sporulation)
PMID:3870979	FYPO:0000681	(comment: at 33.5 degrees, which is restrictive for cdc2-33 but allows sporulation)
PMID:3870979	FYPO:0002043	(comment: at 33.5 degrees, which is restrictive for cdc10-129 but allows sporulation)
PMID:38780300	PBO:0114553	(Fig. 7C)
PMID:38780300	PBO:0114553	(Fig. 1B)
PMID:38780300	PBO:0114553	(Fig. 1E)
PMID:38780300	PBO:0114553	(Fig. 1E)
PMID:38780300	PBO:0114553	(Fig. 1D)
PMID:38780300	PBO:0114540	(Fig. 1E)
PMID:38780300	PBO:0114540	(Fig. 1E)
PMID:38780300	FYPO:0000365	(Fig. 2)
PMID:38780300	FYPO:0005583	(Fig. 4B)
PMID:38780300	FYPO:0000365	(Fig. 2)
PMID:38780300	FYPO:0005583	(Fig. 4B)
PMID:38780300	FYPO:0002317	(Fig. 4D and E)
PMID:38780300	FYPO:0002235	(Fig. 4D and E)
PMID:38780300	FYPO:0002317	(Fig. 4D and E)
PMID:38780300	FYPO:0002235	(Fig. 4D and E)
PMID:38780300	FYPO:0000618	(Fig. 5)
PMID:38780300	FYPO:0005683	(Fig. 5)
PMID:38780300	FYPO:0006257	(Fig. 5)
PMID:38780300	FYPO:0004646	(Fig. 5)
PMID:38780300	PBO:0114553	(Fig. 1B)
PMID:38780300	PBO:0114554	(Fig. 3)
PMID:38780300	PBO:0114554	(Fig. 3)
PMID:38780300	PBO:0114554	(Fig. 3)
PMID:38780300	PBO:0114554	(Fig. 3)
PMID:38780300	PBO:0114555	(Fig. 3)
PMID:38780300	PBO:0114556	(Fig. 3)
PMID:38780300	PBO:0114557	(Fig. 3)
PMID:38780300	PBO:0114558	(Fig. 3)
PMID:38780300	PBO:0114559	(Fig. 3)
PMID:38780300	PBO:0114560	(Fig. 3)
PMID:38780300	PBO:0114561	(Fig. 3)
PMID:38780300	PBO:0114561	(Fig. 3)
PMID:38780300	PBO:0114561	(Fig. 3)
PMID:38780300	PBO:0114542	(Fig. 3)
PMID:38780300	PBO:0114562	(Fig. 3)
PMID:38780300	PBO:0114562	(Fig. 3)
PMID:38780300	PBO:0114543	(Fig. 3)
PMID:38780300	PBO:0114543	(Fig. 3)
PMID:38780300	PBO:0114543	(Fig. 3)
PMID:38780300	PBO:0114563	(Fig. 3)
PMID:38780300	PBO:0114544	(Fig. 3)
PMID:38780300	PBO:0114564	(Fig. 3)
PMID:38780300	PBO:0114564	(Fig. 3)
PMID:38780300	PBO:0114565	(Fig. 3)
PMID:38780300	PBO:0114545	(Fig. 3)
PMID:38780300	PBO:0114545	(Fig. 3)
PMID:38780300	PBO:0114545	(Fig. 3)
PMID:38780300	PBO:0114566	(Fig. 3)
PMID:38780300	PBO:0114547	(Fig. 3)
PMID:38780300	PBO:0114547	(Fig. 3)
PMID:38780300	PBO:0114547	(Fig. 3)
PMID:38780300	PBO:0114548	(Fig. 3)
PMID:38780300	PBO:0114548	(Fig. 3)
PMID:38780300	PBO:0114567	(Fig. 3)
PMID:38780300	PBO:0114550	(Fig. 3)
PMID:38780300	PBO:0114568	(Fig. 3)
PMID:38780300	PBO:0114566	(Fig. 3)
PMID:38780300	PBO:0114566	(Fig. 3)
PMID:38780300	PBO:0114569	(Fig. 3)
PMID:38780300	PBO:0114570	(Fig. 3)
PMID:38780300	PBO:0114558	(Fig. 3)
PMID:38780300	PBO:0114558	(Fig. 3)
PMID:38780300	PBO:0114555	(Fig. 3)
PMID:38780300	PBO:0114571	(Fig. 3)
PMID:38780300	PBO:0114556	(Fig. 3)
PMID:38780300	PBO:0114572	(Fig. 3)
PMID:38780300	PBO:0114573	(Fig. 3)
PMID:38780300	PBO:0114555	(Fig. 3)
PMID:38780300	PBO:0114555	(Fig. 3)
PMID:38780300	PBO:0114572	(Fig. 3)
PMID:38780300	PBO:0114572	(Fig. 3)
PMID:38780300	PBO:0114574	(Fig. 3)
PMID:38780300	PBO:0114574	(Fig. 3)
PMID:38780300	PBO:0114557	(Fig. 3)
PMID:38780300	PBO:0114557	(Fig. 3)
PMID:38780300	PBO:0114575	(Fig. 3)
PMID:38780300	PBO:0114560	(Fig. 3)
PMID:38780300	PBO:0114560	(Fig. 3)
PMID:38780300	PBO:0114560	(Fig. 3)
PMID:38780300	PBO:0114576	(Fig. 3)
PMID:38780300	PBO:0114577	(Fig. 3)
PMID:38780300	PBO:0114569	(Fig. 3)
PMID:38780300	PBO:0114569	(Fig. 3)
PMID:38780300	PBO:0114570	(Fig. 3)
PMID:38780300	PBO:0114570	(Fig. 3)
PMID:38780300	PBO:0114578	(Fig. 3)
PMID:38780300	PBO:0114567	(Fig. 3)
PMID:38780300	PBO:0114567	(Fig. 3)
PMID:38780300	PBO:0114579	(Fig. 3)
PMID:38780300	PBO:0114580	(Fig. 3)
PMID:38780300	PBO:0114578	(Fig. 3)
PMID:38780300	PBO:0114579	(Fig. 3)
PMID:38780300	PBO:0114568	(Fig. 3)
PMID:38780300	PBO:0114581	(Fig. 3)
PMID:38780300	PBO:0114582	(Fig. 3)
PMID:38780300	PBO:0114583	(Fig. 3)
PMID:38780300	PBO:0114584	(Fig. 3)
PMID:38780300	PBO:0114585	(Fig. 3)
PMID:38780300	PBO:0114586	(Fig. 3)
PMID:38780300	PBO:0114587	(Fig. 3)
PMID:38780300	PBO:0114588	(Fig. 3)
PMID:38780300	PBO:0114588	(Fig. 3)
PMID:38780300	PBO:0114588	(Fig. 3)
PMID:38780300	PBO:0114588	(Fig. 3)
PMID:38780300	PBO:0114588	(Fig. 3)
PMID:38780300	PBO:0114589	(Fig. 3)
PMID:38780300	PBO:0114589	(Fig. 3)
PMID:38780300	PBO:0114589	(Fig. 3)
PMID:38780300	PBO:0114589	(Fig. 3)
PMID:38780300	PBO:0114589	(Fig. 3)
PMID:38780300	PBO:0114589	(Fig. 3)
PMID:38780300	PBO:0114589	(Fig. 3)
PMID:38780300	PBO:0032923	(Fig. 6A)
PMID:38780300	PBO:0033358	(Fig. 6C)
PMID:38780300	PBO:0033178	(Fig. 6A)
PMID:38780300	PBO:0104391	(Fig. 6C)
PMID:38780300	PBO:0102384	(Fig. 6B)
PMID:38780300	PBO:0033937	(Fig. 6C)
PMID:38780300	PBO:0033270	(Fig. 6C)
PMID:38780300	PBO:0101179	(Fig. 6B)
PMID:38780300	PBO:0114590	(Fig. 6B)
PMID:38780300	PBO:0101179	(Fig. 6A)
PMID:38780300	PBO:0033073	(Fig. 7A)
PMID:38780300	PBO:0104391	(Fig. 7A)
PMID:38780300	PBO:0037887	(Fig. 7A)
PMID:38780300	PBO:0037887	(Fig. 7A)
PMID:38780300	PBO:0114540	(Fig. 1B)
PMID:38780300	PBO:0114541	(Fig. 3)
PMID:38780300	PBO:0114542	(Fig. 3)
PMID:38780300	PBO:0114543	(Fig. 3)
PMID:38780300	PBO:0114544	(Fig. 3)
PMID:38780300	PBO:0114545	(Fig. 3)
PMID:38780300	PBO:0114546	(Fig. 3)
PMID:38780300	PBO:0114547	(Fig. 3)
PMID:38780300	PBO:0114548	(Fig. 3)
PMID:38780300	PBO:0114549	(Fig. 3)
PMID:38780300	PBO:0114550	(Fig. 3)
PMID:38780300	PBO:0114551	(Fig. 6A)
PMID:38780300	PBO:0033073	(Fig. 6C)
PMID:38780300	PBO:0032852	(Fig. 6A)
PMID:38780300	PBO:0033071	(Fig. 6C)
PMID:38780300	PBO:0033074	(Fig. 6B)
PMID:38780300	PBO:0032995	(Fig. 6C)
PMID:38780300	PBO:0032923	(Fig. 6C)
PMID:38780300	PBO:0033066	(Fig. 6B)
PMID:38780300	PBO:0033067	(Fig. 6B)
PMID:38780300	PBO:0033073	(Fig. 6A)
PMID:38780300	PBO:0114552	(Fig. 7B)
PMID:38780300	PBO:0114552	(Fig. 7B)
PMID:38780300	PBO:0114553	(Fig. 7C)
PMID:38825008	FYPO:0002061	As predicted, the 4KRA mutant did not restore lethality upon shut-off, whereas the other three mutants did (Fig. 4C)
PMID:38825008	FYPO:0002060	As predicted, the 4KRA mutant did not restore lethality upon shut-off, whereas the other three mutants did (Fig. 4C)
PMID:38825008	FYPO:0002060	As predicted, the 4KRA mutant did not restore lethality upon shut-off, whereas the other three mutants did (Fig. 4C)
PMID:38825008	PBO:0120721	As expected, the number of cells with nuclear LDs increased in the cells overexpressing Bqt4-FL (Fig. 6, C and D; 65.9%; see arrowhead in FL) compared to the control cells under the suppressive conditions (0-0.3%).
PMID:38825008	PBO:0120722	Similar PA accumulation in the nucleus was observed in IDR-TM-overexpressing cells (IDR-TM in Figure 6, A and B for quantification).
PMID:38825008	FYPO:0006800	Overexpression of the GFP-IDR and GFP-IDR-TM fragments, but not GFP and GFP-KSE, caused dissociation of the centromeres from the NE and their declustering (Fig. 3, A and B).
PMID:38825008	PBO:0110251	All these fragments as well as wild-type Bqt4 (FL) were localized to the NE (Fig. 1C), suggesting that the lethality was not caused by the loss of NE localization.
PMID:38825008	PBO:0110251	All these fragments as well as wild-type Bqt4 (FL) were localized to the NE (Fig. 1C), suggesting that the lethality was not caused by the loss of NE localization.
PMID:38825008	FYPO:0004924	and the telomere anchoring (Fig. S1C).
PMID:38825008	FYPO:0000772	The DKSE mutant was expressed in lem2- shut-off bqt4D cells expressing GFP-GST-NLS, a nuclear protein marker, and nuclear protein leakage from the nucleus was assessed by calculating the fluorescence intensity ratio of the nucleus to the cytoplasm. Upon thiamine addition, GFP- GST-NLS severely leaked from the nucleus of DKSE mutant-expressing cells, but not from the nucleus of FL-expressing cells (Fig. 1, G and H), indicating NE rupture in the DKSE mutant-expressing cells. These results suggest that the KSE domain is vital for NE maintenance.
PMID:38825008	PBO:0093560	When GFP-IDR was overexpressed in S. pombe cells under the control of the nmt1 promoter, its overexpression resulted in severe growth defects in the spot assay (Fig. 2D).
PMID:38825008	FYPO:0001556	Under overexpression conditions, GFP-IDR was localized in the nucleoplasm, accompanied by a herniated structure adjacent to the nucleus (Fig. 2E, arrows). The Ish1 signal, which was localized in the NE under normal conditions, was distributed on cytoplasmic membranes besides the NE under overexpression conditions (Fig. 2E), suggesting that overexpression of GFP-IDR may cause abnormal membrane proliferation.
PMID:38825008	PBO:0119898	The Ish1 signal, which was localized in the NE under normal conditions, was distributed on cytoplasmic membranes besides the NE under overexpression conditions (Fig. 2E)
PMID:38825008	FYPO:0006800	Overexpression of the GFP-IDR and GFP-IDR-TM fragments, but not GFP and GFP-KSE, caused dissociation of the centromeres from the NE and their declustering (Fig. 3, A and B).
PMID:38825008	FYPO:0002360	This dissociation did not affect transcriptional silencing in the centromeric region (Fig. S6A).
PMID:38825008	FYPO:0006692	Consequently, the chromosome was missegregated during the next mitosis (Fig. 3C). Alternatively, the entire chromosome moved to one side or the cells showed a cut phenotype (untimely torn cell phenotype); these cells displayed nuclear membrane extrusion along the spindle microtubule (Movie S2).
PMID:38825008	FYPO:0002060	As predicted, the 4KRA mutant did not restore lethality upon shut-off, whereas the other three mutants did (Fig. 4C)
PMID:38825008	GO:0070300	To confirm the binding of PA to the IDR, we performed a liposome-mediated binding assay. Liposomes with different percentages of PA were prepared and incubated with purified GFP-IDR protein. After isolation of the liposomes via density gradient centrifugation, the proteins bound to the liposomes were electrophoresed and detected using silver staining. GFP-IDR co-sedimented with PA-containing liposomes but not with control liposomes (Fig. 4B). Therefore, we conclude that the IDR region directly binds to PA in vitro.
PMID:38825008	SO:0001534	(comment: This region was identified as a lipid binding region.)
PMID:38825008	PBO:0119896	Figure 2 Under overexpression conditions, GFP-IDR was localized in the nucleoplasm, accompanied by a herniated structure adja- cent to the nucleus (Fig. 2E, arrows).
PMID:38825008	FYPO:0002060	Upon shut-off of lem2, the cells expressing D1-140 and D259 to 383 fragments of Bqt4 did not grow, whereas the cells expressing D141 to 262 did (Fig. 1B)
PMID:38825008	FYPO:0002061	Upon shut-off of lem2, the cells expressing D1-140 and D259 to 383 fragments of Bqt4 did not grow, whereas the cells expressing D141 to 262 did (Fig. 1B)
PMID:38825008	FYPO:0002061	Upon shut-off of lem2, the cells expressing D1-140 and D259 to 383 fragments of Bqt4 did not grow, whereas the cells expressing D141 to 262 did (Fig. 1B)
PMID:38825008	PBO:0110251	All these fragments as well as wild-type Bqt4 (FL) were localized to the NE (Fig. 1C), suggesting that the lethality was not caused by the loss of NE localization.
PMID:38825008	PBO:0110251	All these fragments as well as wild-type Bqt4 (FL) were localized to the NE (Fig. 1C), suggesting that the lethality was not caused by the loss of NE localization.
PMID:38825008	PBO:0110251	All these fragments as well as wild-type Bqt4 (FL) were localized to the NE (Fig. 1C), suggesting that the lethality was not caused by the loss of NE localization.
PMID:38825008	FYPO:0002061	The deletion mutants D340 to 383 and D364 to 383, but not D340 to 363, showed growth defect in the lem2-shut-off bqt4D strain (Fig. 1E)
PMID:38825008	FYPO:0002061	The deletion mutants D340 to 383 and D364 to 383, but not D340 to 363, showed growth defect in the lem2-shut-off bqt4D strain (Fig. 1E)
PMID:38825008	FYPO:0002060	The deletion mutants D340 to 383 and D364 to 383, but not D340 to 363, showed growth defect in the lem2-shut-off bqt4D strain (Fig. 1E)
PMID:38825008	PBO:0110251	All these fragments as well as wild-type Bqt4 (FL) were localized to the NE (Fig. 1C), suggesting that the lethality was not caused by the loss of NE localization.
PMID:38825008	PBO:0119897	and retained interaction with Bqt3 (Fig. S1B)
PMID:38830897	FYPO:0001355	(comment: referring to growth defect) Mutating three other conserved residues in the Sororin domain of Sor1 (F299A, V302A and Y305A) resulted in a similar phenotype (Fig. 2e).
PMID:38830897	FYPO:0001355	(comment: referring to growth defect) Mutating three other conserved residues in the Sororin domain of Sor1 (F299A, V302A and Y305A) resulted in a similar phenotype (Fig. 2e).
PMID:38830897	GO:0005634	In an asynchronously growing culture, Sor1- GFP localized to the nucleus in most cells (Supplementary Fig. 2a)
PMID:38830897	GO:0007064	In metaphase, sor1Δ mutant cells showed a small, but significant, increase of split sister centromeres (Fig. 2a), indicative of a cohesion defect between sister centromeres.
PMID:38830897	PBO:0114891	Interestingly, the increase in split sister centromeres in sor1Δ mutant cells was prevented in sor1Δ wpl1Δ double mutants (compared to wild type), suggesting that similarly to mammalian cells wpl1 deletion reduces the sister chromatid cohesion defect caused by the sor1Δ mutation (Fig. 2a).
PMID:38830897	FYPO:0001355	(comment: referring to growth defect) Mutating three other conserved residues in the Sororin domain of Sor1 (F299A, V302A and Y305A) resulted in a similar phenotype (Fig. 2e).
PMID:38830897	PBO:0098329	Indeed, we observed a higher frequency of lagging chromosomes associated with a higher rate of chromosome mis-segregation in eso1-G799D sor1Δ and mis4-242 sor1Δ double mutants as compared to single mutants (Fig. 2b).
PMID:38830897	PBO:0114892	Sor1-D303A-Pk co-immunoprecipitated less efficiently with the Psm3-GFP protein, compared to wild-type Sor1- Pk, suggesting that the conserved residue D303 in the Sororin domain of Sor1 is important for the association of Sor1 with cohesin (Fig. 2d).
PMID:38830897	PBO:0097931	Indeed, we observed a higher frequency of lagging chromosomes associated with a higher rate of chromosome mis-segregation in eso1-G799D sor1Δ and mis4-242 sor1Δ double mutants as compared to single mutants (Fig. 2b).
PMID:38833506	PBO:0116462	Therefore, when Cdk9 was inactivated, transcription was slowed down [34,35]. We analyzed the splicing of the single intron of cbf11, which is one of the most affected in the Δsaf5 strain, with 60% of intron retention. The addition of the bulky ATP analog barely affected intron retention in a wild type or a Δsaf5 strains (Fig 5A). However, upon adding 3-MB-PP1 to the culture of the cdk9as Δsaf5 strain, splicing of the cbf11 intron was noticeably improved, with intron retention reduced to 25%. Splicing also improved in the cdk9as saf5+ strain (depicted by the pale orange bars), probably as the result of decreasing transcription rate and giving more time for the splicing to occur; however, this improvement was not statistically significant. When we analyzed how inactivation of Cdk9 affected the splicing of multi-intronic genes, such as atg5 or urm1 (Fig 5B and 5C), we consistently observed improvements in all introns 30 minutes after adding 3-MB-PP1
PMID:38833506	PBO:0109678	Among the 41 tested strains, three showed a markedly low YFP/RFP ratio when compared to the wild type strain: Δcwf12, Δsaf5 and Δsaf1. (Figure 2A)
PMID:38833506	PBO:0109678	Among the 41 tested strains, three showed a markedly low YFP/RFP ratio when compared to the wild type strain: Δcwf12, Δsaf5 and Δsaf1. (Figure 2A)
PMID:38833506	PBO:0109678	Among the 41 tested strains, three showed a markedly low YFP/RFP ratio when compared to the wild type strain: Δcwf12, Δsaf5 and Δsaf1. (Figure 2A)
PMID:38833506	FYPO:0003244	Of these candidates, only 4 were already known to be involved in the regulation of splicing (Cwf12, Saf5, Cwf19 and SPAC1705.02), whereas the remaining 33 were unrelated or not clearly assigned to the regulation of splicing
PMID:38833506	PBO:0116462	Of these candidates, only 4 were already known to be involved in the regulation of splicing (Cwf12, Saf5, Cwf19 and SPAC1705.02), whereas the remaining 33 were unrelated or not clearly assigned to the regulation of splicing
PMID:38833506	PBO:0109678	the effect observed in the Δmpn1 strain was comparable to that observed in Δsaf5 cells.
PMID:38833506	GO:1905746	(comment: highly expressed genes (or conditionally expressed))
PMID:38865179	PBO:0113843	Like ppa3∆, ppa3-D82N cells were viable and 9 rescued growth of cdc11-136, an indication that it is a loss-of-function ppa3 allele (Figure S3A)
PMID:38865179	FYPO:0001490	died as single elongated cells, consistent with SIN inactivation (Figure S2, C and D)
PMID:38865179	FYPO:0001490	died as single elongated cells, consistent with SIN inactivation (Figure S2, C and D)
PMID:38865179	FYPO:0001490	died as single elongated cells, consistent with SIN inactivation (Figure S2, C and D)
PMID:38865179	FYPO:0002061	Interestingly, we found that cells producing both Csc1-GFP and either Ppc89-GBP-mCherry (Figure S2A) or Sid4-GBP-mCherry (Figure 3A) were inviable.
PMID:38865179	FYPO:0002061	We found that cells producing both Csc1-R31A-GFP and Ppc89-GBP-mCherry (Figure S2B) or Sid4-GBP-mCherry (Figure 3B) were also inviable.
PMID:38865179	FYPO:0002061	Interestingly, we found that cells producing both Csc1-GFP and either Ppc89-GBP-mCherry (Figure S2A) or Sid4-GBP-mCherry (Figure 3A) were inviable.
PMID:38865179	PBO:0113841	is independent of the SIN because GFP- Csc1(FHA) expressed from the nmt81 promoter of pREP81 localized to mitotic SPBs marked by Sad1-mCherry in the SIN scaffold mutant sid4-SA1 cells at the restrictive temperature (Figure 1E).
PMID:38865179	PBO:0113841	GFP-Csc1(FHA) localized to SPBs in mitotic cells (Figure 1D).
PMID:38865179	PBO:0113923	ppa3-D82N cells producing Sid4-RFP displayed symmetric Sid1-GFP and Cdc7-GFP localization on anaphase SPBs whereas the localization is asymmetric in wild-type cells (Figure 4B). This further demonstrates that ppa3-D82N is a loss of function allele.
PMID:38865179	PBO:0113922	ppa3-D82N cells producing Sid4-RFP displayed symmetric Sid1-GFP and Cdc7-GFP localization on anaphase SPBs whereas the localization is asymmetric in wild-type cells (Figure 4B). This further demonstrates that ppa3-D82N is a loss of function allele.
PMID:38865179	PBO:0113841	In both wild-type and ppa3-D82N cells, Csc1-GFP localized to mitotic SPBs (Figure 4C).
PMID:38865179	PBO:0113923	we found that Cdc7 and Sid1 localized symmetrically to both SPBs during anaphase in contrast to its asymmetrical distribution to a single SPB in wild-type anaphase cells (Figure 2, A and B).
PMID:38865179	PBO:0113922	we found that Cdc7 and Sid1 localized symmetrically to both SPBs during anaphase in contrast to its asymmetrical distribution to a single SPB in wild-type anaphase cells (Figure 2, A and B).
PMID:38865179	PBO:0113836	We also did not detect Csc2-GFP, Csc3-GFP or Csc4-GFP at SPBs in csc1-R31A cells although these proteins were detected at SPBs in wild-type cells (Figure S1B).
PMID:38865179	PBO:0113838	We also did not detect Csc2-GFP, Csc3-GFP or Csc4-GFP at SPBs in csc1-R31A cells although these proteins were detected at SPBs in wild-type cells (Figure S1B).
PMID:38865179	PBO:0113835	we did not detect Csc1-R31A-GFP on SPBs at any point in the cell cycle (Figure 1C).
PMID:38865179	PBO:0093559	Thus, we tested whether csc1-R31A interacted negatively with cdc16-116 cells and found that it did (Figure 2C).
PMID:38865179	PBO:0093559	Thus, we tested whether csc1-R31A interacted negatively with cdc16-116 cells and found that it did (Figure 2C).
PMID:38865179	FYPO:0005258	SIP null mutants rescue cdc11- 136 (Singh et al., 2011) and we observed that csc1-R31A also did (Figure 2D).
PMID:38865179	FYPO:0005258	SIP null mutants rescue cdc11- 136 (Singh et al., 2011) and we observed that csc1-R31A also did (Figure 2D).
PMID:38865179	FYPO:0005258	Like ppa3∆, ppa3-D82N cells were viable and 9 rescued growth of cdc11-136, an indication that it is a loss-of-function ppa3 allele (Figure S3A)
PMID:38865179	FYPO:0005258	Like ppa3∆, ppa3-D82N cells were viable and 9 rescued growth of cdc11-136, an indication that it is a loss-of-function ppa3 allele (Figure S3A)
PMID:38865179	PBO:0113836	We found that this is also true for Csc4. Csc4-GFP was not detected at SPBs in csc1∆, csc2∆, csc3∆ or ppa3∆ cells (Figure S1A).
PMID:38865179	PBO:0113836	We found that this is also true for Csc4. Csc4-GFP was not detected at SPBs in csc1∆, csc2∆, csc3∆ or ppa3∆ cells (Figure S1A).
PMID:38865179	PBO:0113836	We found that this is also true for Csc4. Csc4-GFP was not detected at SPBs in csc1∆, csc2∆, csc3∆ or ppa3∆ cells (Figure S1A).
PMID:38865179	PBO:0113837	We also did not detect Csc2-GFP, Csc3-GFP or Csc4-GFP at SPBs in csc1-R31A cells although these proteins were detected at SPBs in wild-type cells (Figure S1B).
PMID:38889144	PBO:0114681	(Fig. 2)
PMID:38889144	PBO:0114681	(Fig. 2)
PMID:38889144	PBO:0114687	These results suggest that Ntp1-mediated trehalose degra­dation is required for cytoplasmic fluidization and rapid germi­nation through the cAMP-PKA pathway.
PMID:38889144	PBO:0114686	These results suggest that Ntp1-mediated trehalose degra­dation is required for cytoplasmic fluidization and rapid germi­ nation through the cAMP-PKA pathway.
PMID:38889144	PBO:0114685	(Fig. 4J)
PMID:38889144	PBO:0114684	(Fig. 4J)
PMID:38889144	PBO:0114683	(Fig. 4I and K)
PMID:38889144	PBO:0114683	(Fig. 4I and K)
PMID:38889144	FYPO:0002686	(Fig. 4C)
PMID:38889144	FYPO:0002686	(Fig. 4C)
PMID:38889144	FYPO:0000582	(Fig. 4D)
PMID:38889144	PBO:0114682	(Fig. 4I and K)
PMID:38889144	FYPO:0000582	(Fig. 2D)
PMID:38899862	FYPO:0001357	(Fig. 6D)
PMID:38899862	FYPO:0001357	(Fig. S4)
PMID:38899862	FYPO:0001357	(Fig. S4)
PMID:38899862	FYPO:0001357	(Fig. S4)
PMID:38899862	FYPO:0001357	(Fig. S4)
PMID:38899862	FYPO:0001357	(Fig. S4)
PMID:38899862	FYPO:0001357	(Fig. S4)
PMID:38899862	FYPO:0001357	(Fig. S4)
PMID:38899862	FYPO:0001357	(Fig. S4)
PMID:38899862	PBO:0113913	(Fig. S3)
PMID:38899862	PBO:0094833	(Fig. S3)
PMID:38899862	PBO:0094844	(Fig. S3)
PMID:38899862	PBO:0113918	(Fig. S3)
PMID:38899862	PBO:0113917	(Fig. S3)
PMID:38899862	PBO:0113916	(Fig. S3)
PMID:38899862	PBO:0113915	(Fig. S3)
PMID:38899862	PBO:0113914	(Fig. S3)
PMID:38899862	PBO:0113913	(Fig. S3)
PMID:38899862	PBO:0113912	(Fig. S3)
PMID:38899862	PBO:0113912	(Fig. S3)
PMID:38899862	PBO:0094850	(Fig. S3)
PMID:38899862	PBO:0113911	(Fig. S3)
PMID:38899862	PBO:0113911	(Fig. S3)
PMID:38899862	PBO:0113910	(Fig. S3)
PMID:38899862	PBO:0113910	(Fig. S3)
PMID:38899862	PBO:0113909	(Fig. S3)
PMID:38899862	PBO:0113908	(Fig. S3)
PMID:38899862	PBO:0113908	(Fig. S3)
PMID:38899862	PBO:0113907	(Fig. S3)
PMID:38899862	PBO:0113906	(Fig. S3)
PMID:38899862	PBO:0113907	(Fig. S3)
PMID:38899862	PBO:0113906	(Fig. S3)
PMID:38899862	PBO:0113905	(Fig. S3)
PMID:38899862	PBO:0113904	(Fig. S3)
PMID:38899862	PBO:0094831	(Fig. S3)
PMID:38899862	PBO:0113903	(Fig. S3)
PMID:38899862	PBO:0113903	(Fig. S3)
PMID:38899862	PBO:0094841	(Fig. S3)
PMID:38899862	PBO:0113902	(Fig. S3)
PMID:38899862	PBO:0113901	(Fig. S3)
PMID:38899862	PBO:0113900	(Fig. S3)
PMID:38899862	PBO:0113899	(Fig. S3)
PMID:38899862	PBO:0113898	(Fig. S3)
PMID:38899862	PBO:0113897	(Fig. S3)
PMID:38899862	PBO:0113896	(Fig. S3)
PMID:38899862	PBO:0113895	(Fig. S3)
PMID:38899862	PBO:0094841	(Fig. S3)
PMID:38899862	PBO:0113902	(Fig. S3)
PMID:38899862	PBO:0113901	(Fig. S3)
PMID:38899862	PBO:0113900	(Fig. S3)
PMID:38899862	PBO:0113899	(Fig. S3)
PMID:38899862	PBO:0113898	(Fig. S3)
PMID:38899862	PBO:0113897	(Fig. S3)
PMID:38899862	PBO:0113896	(Fig. S3)
PMID:38899862	PBO:0113895	(Fig. S3)
PMID:38899862	PBO:0113894	(Fig. S3)
PMID:38899862	PBO:0113894	(Fig. S3)
PMID:38899862	FYPO:0001357	(Fig. S2B)
PMID:38899862	FYPO:0001357	(Fig. S2B)
PMID:38899862	PBO:0093560	(Fig. S2A)
PMID:38899862	PBO:0093560	(Fig. S2A)
PMID:38899862	PBO:0113893	(Fig. S1B)
PMID:38899862	PBO:0093555	(Fig. S1A)
PMID:38899862	PBO:0113893	(Fig. S1B)
PMID:38899862	PBO:0093555	(Fig. S1A)
PMID:38899862	PBO:0113893	(Fig. S1B)
PMID:38899862	PBO:0093555	(Fig. S1A)
PMID:38899862	FYPO:0006658	(Fig. 12)
PMID:38899862	PBO:0113892	(Fig. 7)
PMID:38899862	PBO:0113892	(Fig. 7)
PMID:38899862	PBO:0113891	(Fig. 7)
PMID:38899862	PBO:0113891	(Fig. 7)
PMID:38899862	PBO:0113890	(Fig. 7)
PMID:38899862	PBO:0113889	(Fig. 7)
PMID:38899862	PBO:0113889	(Fig. 7)
PMID:38899862	PBO:0094808	(Fig. 7)
PMID:38899862	PBO:0094808	(Fig. 7)
PMID:38899862	PBO:0113888	(Fig. 7)
PMID:38899862	PBO:0113888	(Fig. 7)
PMID:38899862	PBO:0113887	(Fig. 7)
PMID:38899862	PBO:0113886	(Fig. 7)
PMID:38899862	PBO:0113886	(Fig. 7)
PMID:38899862	PBO:0113885	(Fig. 7)
PMID:38899862	PBO:0094791	(Fig. 7)
PMID:38899862	PBO:0113884	(Fig. 7)
PMID:38899862	PBO:0113883	(Fig. 7)
PMID:38899862	PBO:0113883	(Fig. 7)
PMID:38899862	PBO:0094804	(Fig. 7)
PMID:38899862	PBO:0094804	(Fig. 7)
PMID:38899862	PBO:0094798	(Fig. 7)
PMID:38899862	PBO:0113882	(Fig. 7)
PMID:38899862	PBO:0113882	(Fig. 7)
PMID:38899862	PBO:0113881	(Fig. 7)
PMID:38899862	PBO:0113881	(Fig. 7)
PMID:38899862	PBO:0094810	(Fig. 7)
PMID:38899862	PBO:0094810	(Fig. 7)
PMID:38899862	PBO:0113880	(Fig. 7)
PMID:38899862	PBO:0113880	(Fig. 7)
PMID:38899862	PBO:0113879	(Fig. 7)
PMID:38899862	PBO:0113879	(Fig. 7)
PMID:38899862	PBO:0094814	(Fig. 7)
PMID:38899862	PBO:0094814	(Fig. 7)
PMID:38899862	PBO:0094795	(Fig. 7)
PMID:38899862	PBO:0094795	(Fig. 7)
PMID:38899862	PBO:0094789	(Fig. 7)
PMID:38899862	PBO:0094789	(Fig. 7)
PMID:38899862	PBO:0094784	(Fig. 7)
PMID:38899862	PBO:0113878	(Fig. 7)
PMID:38899862	PBO:0113878	(Fig. 7)
PMID:38899862	PBO:0113877	(Fig. 7)
PMID:38899862	PBO:0113877	(Fig. 7)
PMID:38899862	PBO:0113876	(Fig. 7)
PMID:38899862	PBO:0113876	(Fig. 7)
PMID:38899862	PBO:0113875	(Fig. 7)
PMID:38899862	PBO:0113875	(Fig. 7)
PMID:38899862	PBO:0113874	(Fig. 7)
PMID:38899862	PBO:0113874	(Fig. 7)
PMID:38899862	PBO:0113873	(Fig. 7)
PMID:38899862	PBO:0113873	(Fig. 7)
PMID:38899862	PBO:0113872	(Fig. 7)
PMID:38899862	PBO:0113872	(Fig. 7)
PMID:38899862	PBO:0094773	(Fig. 7)
PMID:38899862	PBO:0094773	(Fig. 7)
PMID:38899862	PBO:0094772	(Fig. 7)
PMID:38899862	PBO:0094772	(Fig. 7)
PMID:38899862	PBO:0098283	(Fig. 7)
PMID:38899862	PBO:0098283	(Fig. 7)
PMID:38899862	PBO:0094793	(Fig. 7)
PMID:38899862	PBO:0094793	(Fig. 7)
PMID:38899862	FYPO:0001357	(Fig. 6D)
PMID:38899862	PBO:0108849	(Fig. 6E)
PMID:38899862	PBO:0108849	(Fig. 6E)
PMID:38899862	PBO:0094771	(Fig. 6E)
PMID:38899862	FYPO:0001357	(Fig. 6D)
PMID:38899862	FYPO:0001355	(Fig. 6D) (STF9)
PMID:38899862	PBO:0108849	SST-612 in Fig. 6B
PMID:38899862	FYPO:0001355	(Fig. 6A,D) (STF6)
PMID:38899862	FYPO:0001357	SST-612 in Fig. 6A
PMID:38899862	PBO:0094773	(Fig. 5)
PMID:38899862	PBO:0094773	(Fig. 5)
PMID:38899862	PBO:0098250	(Fig. 5)
PMID:38899862	PBO:0098250	(Fig. 5)
PMID:38899862	PBO:0098250	(Fig. 5)
PMID:38899862	PBO:0094775	(Fig. 5)
PMID:38899862	PBO:0094775	(Fig. 5)
PMID:38899862	PBO:0094772	(Fig. 5)
PMID:38899862	PBO:0094772	(Fig. 5)
PMID:38899862	PBO:0094775	(Fig. 5)
PMID:38899862	PBO:0094774	(Fig. 5)
PMID:38899862	PBO:0094774	(Fig. 5)
PMID:38899862	PBO:0094774	(Fig. 5)
PMID:38899862	PBO:0094776	(Fig. 5)
PMID:38899862	PBO:0094776	(Fig. 5)
PMID:38899862	PBO:0094771	(Fig. 4C)
PMID:38899862	PBO:0094771	(Fig. 4C)
PMID:38899862	PBO:0094738	(Fig. 4C, 6E)
PMID:38899862	PBO:0094738	(Fig. 4C, 6E)
PMID:38899862	PBO:0094738	(Fig. 4C)
PMID:38899862	PBO:0094738	(Fig. 4C)
PMID:38899862	PBO:0094738	(Fig. 4C)
PMID:38899862	PBO:0094738	(Fig. 4C)
PMID:38899862	PBO:0094738	(Fig. 4B)
PMID:38899862	PBO:0099749	(Fig. 4B)
PMID:38899862	PBO:0094738	(Fig. 4B)
PMID:38899862	PBO:0099749	(Fig. 4B)
PMID:38899862	FYPO:0002141	(Fig. 4A)
PMID:38899862	FYPO:0002141	(Fig. 4A)
PMID:38899862	FYPO:0000080	(Fig. 4A)
PMID:38899862	FYPO:0000080	(Fig. 4A)
PMID:38899862	FYPO:0001357	(Fig. 3A)
PMID:38899862	FYPO:0002141	(Fig. 3A)
PMID:38899862	FYPO:0000080	(Fig. 3A)
PMID:38899862	FYPO:0000080	(Fig. 3A)
PMID:38899862	FYPO:0000080	(Fig. 3A)
PMID:38899862	PBO:0094771	(Fig. 3B)
PMID:38899862	PBO:0094771	Moreover, snf22-(D996A-E997A) reversed the derepression of Pho1 accompanying deletion of erh1 (Fig. 3B), which results from precocious 3′-processing/termination of prt lncRNA synthesis (38).
PMID:38899862	PBO:0094771	(Fig. 3B)
PMID:38899862	PBO:0094771	(Fig. 3B)
PMID:38899862	PBO:0094738	Moreover, snf22-(D996A-E997A) reversed the derepression of Pho1 accompanying deletion of erh1 (Fig. 3B), which results from precocious 3′-processing/termination of prt lncRNA synthesis (38).
PMID:38899862	PBO:0094738	(Fig. 3B)
PMID:38899862	PBO:0094771	(Fig. 3B)
PMID:38899862	FYPO:0001357	(Fig. 3A, 4A)
PMID:38899862	PBO:0094771	Here we constructed a snf22∆ rad24∆ double mutant (Fig. 2A) and found that loss of Snf22 abolished Pho1 derepression by rad24∆ (Fig. 2B).
PMID:38899862	PBO:0094771	and (ii) snf22∆ suppressed the derepression of Pho1 by seb1-G476S (Fig. 2B).
PMID:38899862	PBO:0094771	Deletion of the Nudix-family pyrophosphatase Aps1 or the Duf89 phosphatase-pyro­ phosphatase also results in the derepression of Pho1 expression (15, 30), an effect that was suppressed by snf22∆ (Fig. 2B).
PMID:38899862	PBO:0094771	Deletion of the Nudix-family pyrophosphatase Aps1 or the Duf89 phosphatase-pyro­ phosphatase also results in the derepression of Pho1 expression (15, 30), an effect that was suppressed by snf22∆ (Fig. 2B).
PMID:38899862	PBO:0094738	Production of full-length interfering prt lncRNA is inhibited in rad24∆ cells (31) concomitant with increased production of pho1 mRNA and greatly increased Pho1 activity (as in Fig. 2B).
PMID:38899862	PBO:0094738	Pho1 expression is therefore derepressed in seb1-G476S cells (Fig. 2B). , 3B
PMID:38899862	PBO:0094738	(Fig. 2B)
PMID:38899862	PBO:0094738	(Fig. 2B)
PMID:38899862	PBO:0094777	The derepression of Pho1 seen in asp1-H397A cells was erased by snf22∆, to the extent that acid phosphatase activity in snf22∆ asp1-H397A cells was the same as that of the wild-type control (Fig. 2B).
PMID:38899862	PBO:0094738	The derepression of Pho1 seen in asp1-H397A cells was erased by snf22∆, to the extent that acid phosphatase activity in snf22∆ asp1-H397A cells was the same as that of the wild-type control (Fig. 2B).
PMID:38899862	PBO:0094771	snf22∆ elicited a sevenfold hyper-repression of Pho1 expression in phosphate-replete cells compared to the wild-type control (Fig. 2B, P value <0.0001).
PMID:38899862	FYPO:0001357	(Fig. 2A)
PMID:38899862	FYPO:0002141	(i) snf22∆ suppressed the cold-sensitive slow growth phenotype associated with seb1-G476S (Fig. 2A)
PMID:38899862	FYPO:0001357	(Fig. 2A)
PMID:38899862	FYPO:0001357	(Fig. 2A)
PMID:38899862	FYPO:0001357	(Fig. 2A)
PMID:38899862	FYPO:0000080	(Fig. 2A)
PMID:38899862	FYPO:0001357	(Fig. 2A)
PMID:38899862	FYPO:0001357	(Fig. 2A)
PMID:38899862	FYPO:0001357	(Fig. 2A)
PMID:38899862	FYPO:0001357	(Fig. 2A)
PMID:38899862	FYPO:0001357	snf22∆ cells grew similarly to wild-type cells on YES agar at all temperatures tested (Fig. 2A).
PMID:38899862	FYPO:0001357	The snf22∆ asp1-H397A double mutant grew well on YES agar at all temperatures from 20°C to 37°C (Fig. 2A)
PMID:38899862	PBO:0094738	(Fig. 1B)
PMID:38899862	FYPO:0001355	The STF7 (H686Y) pyrophosphatase domain mutation of asp1 elicits a severe growth defect at all temperatures (Fig. 1A).
PMID:38899862	PBO:0094738	(Fig. 1B). The asp1-STF7 pyrophosphatase mutation resulted in derepression of Pho1 expression, by 23-fold compared to the wild-type control.
PMID:38913087	PBO:0114445	(Fig. 5)
PMID:38913087	PBO:0114447	(Fig. 5)
PMID:38913087	PBO:0114446	(Fig. 5)
PMID:38913087	PBO:0114445	(Fig. 4)
PMID:38913087	PBO:0114451	(Fig. 4)
PMID:38913087	PBO:0114447	(Fig. 4)
PMID:38913087	PBO:0114447	(Fig. 4)
PMID:38913087	PBO:0114447	(Fig. 4)
PMID:38913087	PBO:0114447	(Fig. 4)
PMID:38913087	PBO:0114447	(Fig. 4)
PMID:38913087	PBO:0114447	(Fig. 4)
PMID:38913087	PBO:0114447	(Fig. 4)
PMID:38913087	PBO:0114447	(Fig. 4)
PMID:38913087	PBO:0114447	(Fig. 4)
PMID:38913087	PBO:0114447	(Fig. 4)
PMID:38913087	PBO:0114447	(Fig. 4)
PMID:38913087	PBO:0114447	(Fig. 4)
PMID:38913087	PBO:0114444	(Fig. 4)
PMID:38913087	PBO:0114446	(Fig. 4)
PMID:38913087	PBO:0114446	(Fig. 4)
PMID:38913087	PBO:0114446	(Fig. 4)
PMID:38913087	PBO:0114446	(Fig. 4)
PMID:38913087	PBO:0114446	(Fig. 4)
PMID:38913087	PBO:0114446	(Fig. 4)
PMID:38913087	PBO:0114446	(Fig. 4)
PMID:38913087	PBO:0114450	(Fig. 4)
PMID:38913087	PBO:0114449	(Fig. 4)
PMID:38913087	PBO:0114449	(Fig. 4)
PMID:38913087	PBO:0114449	(Fig. 4)
PMID:38913087	PBO:0114448	(Fig. 4)
PMID:38913087	PBO:0114448	(Fig. 4)
PMID:38913087	PBO:0114446	(Fig. 2)
PMID:38913087	PBO:0114447	(Fig. 2)
PMID:38913087	PBO:0114444	(Fig. 3)
PMID:38913087	PBO:0114448	(Fig. 3)
PMID:38913087	PBO:0114444	(Fig. 3)
PMID:38913087	PBO:0114447	(Fig. 2)
PMID:38913087	PBO:0114446	(Fig. 2)
PMID:38913087	PBO:0114445	(Fig. 2)
PMID:38913087	PBO:0114444	(Fig. 2)
PMID:38913087	PBO:0114442	(Fig. 6F)
PMID:38913087	FYPO:0000280	(Fig. 6J)
PMID:38913087	FYPO:0000280	(Fig. 6I)
PMID:38913087	FYPO:0000280	(Fig. 6H)
PMID:38913087	PBO:0114443	(Fig. 6G)
PMID:38913087	PBO:0114443	(Fig. 6D)
PMID:38913087	PBO:0114442	(Fig. 6C)
PMID:38913087	PBO:0114453	(Fig. 5)
PMID:38913087	PBO:0114453	(Fig. 5)
PMID:38913087	PBO:0114453	(Fig. 5)
PMID:38913087	PBO:0114446	(Fig. 5)
PMID:38913087	PBO:0114446	(Fig. 5)
PMID:38913087	PBO:0114446	(Fig. 5)
PMID:38913087	PBO:0114444	(Fig. 5)
PMID:38913087	PBO:0114444	(Fig. 5)
PMID:38913087	PBO:0114444	(Fig. 5)
PMID:38913087	PBO:0114444	(Fig. 5)
PMID:38913087	PBO:0114444	(Fig. 5)
PMID:38913087	PBO:0114448	(Fig. 5)
PMID:38913087	PBO:0114452	(Fig. 5)
PMID:38913087	PBO:0093825	(Fig. 6G)
PMID:38913087	FYPO:0001147	(Fig. 6G)
PMID:38913087	FYPO:0000280	(Fig. 6F)
PMID:38913087	FYPO:0007963	(Table 2)
PMID:38913087	PBO:0114456	(Table 2)
PMID:38913087	PBO:0114455	(Table 2)
PMID:38913087	PBO:0114454	(Table 2)
PMID:38913087	PBO:0114442	(Table 2)
PMID:38913087	PBO:0114442	(Table 2)
PMID:38913087	PBO:0114453	(Fig. 5)
PMID:38913087	PBO:0114453	(Fig. 5)
PMID:38913087	PBO:0114452	(Fig. 5)
PMID:38913087	PBO:0114445	(Fig. 5)
PMID:38913087	PBO:0114445	(Fig. 5)
PMID:38913087	PBO:0114445	(Fig. 5)
PMID:38913087	PBO:0114445	(Fig. 5)
PMID:38913087	PBO:0114445	(Fig. 5)
PMID:38917328	FYPO:0006320	(Fig. 5C)
PMID:38917328	PBO:0114212	The Ulp1 SUMO protease ensures an efficient initiation of restarted DNA synthesis. This mechanism requires the sequestration of Ulp1 at the NP which is coordinated by the Y complex and the nuclear basket nucleoporin Nup60
PMID:38917328	GO:0120292	The Ulp1 SUMO protease ensures an efficient initiation of restarted DNA synthesis. This mechanism requires the sequestration of Ulp1 at the NP which is coordinated by the Y complex and the nuclear basket nucleoporin Nup60
PMID:38917328	GO:0120292	The Ulp1 SUMO protease ensures an efficient initiation of restarted DNA synthesis. This mechanism requires the sequestration of Ulp1 at the NP which is coordinated by the Y complex and the nuclear basket nucleoporin Nup60
PMID:38917328	GO:0120292	Thus, Alm1 and Nup60 promote RDR in a preand post-anchoring manner, respectively.
PMID:38917328	PBO:0114198	(Fig. 3C)
PMID:38917328	PBO:0114199	(Fig. 2B)
PMID:38917328	PBO:0114199	(Fig. 2B)
PMID:38917328	FYPO:0006320	(Fig. 2B)
PMID:38917328	FYPO:0006320	(Fig. 2B)
PMID:38917328	PBO:0114200	(Fig. 6A and D)
PMID:38917328	PBO:0114199	(Fig. 5A)
PMID:38917328	PBO:0114201	(Fig. 5D and E)
PMID:38917328	PBO:0114202	(Fig. 5D)
PMID:38917328	PBO:0114202	(Fig. 5D)
PMID:38917328	PBO:0114199	(Fig. 5E)
PMID:38917328	PBO:0114200	(Fig. 6D)
PMID:38917328	PBO:0114200	(Fig. 6A)
PMID:38917328	FYPO:0006319	(Fig. 2D)
PMID:38917328	FYPO:0006319	(Fig. 2D)
PMID:38917328	FYPO:0006319	(Fig. 2D)
PMID:38917328	FYPO:0006319	(Fig. 2D)
PMID:38917328	PBO:0114204	(Fig. S6D)
PMID:38917328	PBO:0114205	(Fig. 3B)
PMID:38917328	PBO:0114205	(Fig. 3B)
PMID:38917328	PBO:0114206	(Fig. 3A and B)
PMID:38917328	PBO:0114198	(Fig. 3C)
PMID:38917328	PBO:0114207	(Fig. 4C)
PMID:38917328	PBO:0114208	(Fig. S6B)
PMID:38917328	PBO:0093614	(Fig. S1A)
PMID:38917328	FYPO:0007255	(Fig. 1B and C)
PMID:38917328	PBO:0093613	(Fig. S1A)
PMID:38917328	PBO:0093581	(Fig. S1A)
PMID:38917328	PBO:0093580	(Fig. S1A)
PMID:38917328	PBO:0093579	(Fig. S1A)
PMID:38917328	PBO:0093580	(Fig. S1A)
PMID:38917328	PBO:0093617	(Fig. S1A)
PMID:38917328	PBO:0093618	(Fig. S1A)
PMID:38917328	PBO:0093616	(Fig. S1A)
PMID:38917328	PBO:0093586	(Fig. S1A)
PMID:38917328	FYPO:0004003	(Fig. S1B)
PMID:38917328	FYPO:0004003	(Fig. S1B)
PMID:38917328	PBO:0114209	(Fig. 3A)
PMID:38917328	PBO:0114209	(Fig. 3A)
PMID:38917328	PBO:0114210	(Fig. 3A)
PMID:38917328	PBO:0114211	(Fig. 3A)
PMID:38917328	PBO:0114211	(Fig. 3A)
PMID:38917328	PBO:0093613	(Fig. S2A)
PMID:38917328	PBO:0093580	(Fig. S2A)
PMID:38917328	PBO:0093616	(Fig. S2A)
PMID:38917328	PBO:0093587	(Fig. S2A)
PMID:38917328	FYPO:0006320	(Fig. 5C)
PMID:38917328	FYPO:0006320	(Fig. 5C)
PMID:38940614	FYPO:0001357	(Fig. 10)
PMID:38940614	PBO:0093558	(Fig. S1)
PMID:38940614	PBO:0093558	(Fig. S1)
PMID:38940614	PBO:0093555	(Fig. S1)
PMID:38940614	PBO:0093555	(Fig. S1)
PMID:38940614	PBO:0093561	(Fig. S1)
PMID:38940614	PBO:0093561	(Fig. S1)
PMID:38940614	PBO:0114190	(Fig. 11)
PMID:38940614	PBO:0114190	(Fig. 11)
PMID:38940614	PBO:0114190	(Fig. 11)
PMID:38940614	PBO:0114194	(Fig. 11)
PMID:38940614	FYPO:0008285	(Fig. 11)
PMID:38940614	PBO:0114193	(Fig. 11)
PMID:38940614	PBO:0114193	(Fig. 11)
PMID:38940614	PBO:0114189	(Fig. 11)
PMID:38940614	PBO:0114192	(Fig. 11)
PMID:38940614	PBO:0114191	(Fig. 11)
PMID:38940614	PBO:0114191	(Fig. 11)
PMID:38940614	PBO:0114188	(Fig. 11)
PMID:38940614	PBO:0114188	(Fig. 11)
PMID:38940614	PBO:0114190	(Fig. 11)
PMID:38940614	PBO:0114189	(Fig. 11)
PMID:38940614	PBO:0114188	(Fig. 11)
PMID:38940614	FYPO:0001357	(Fig. 10)
PMID:38940614	FYPO:0001357	(Fig. 10)
PMID:38940614	PBO:0093559	(Fig. 10)
PMID:38940614	FYPO:0001575	(Fig. 10)
PMID:38940614	FYPO:0001575	(Fig. 10)
PMID:38940614	FYPO:0001357	(Fig. 10)
PMID:38940614	FYPO:0001357	(Fig. 9)
PMID:38940614	FYPO:0001357	(Fig. 10)
PMID:38940614	FYPO:0001357	(Fig. 10)
PMID:38940614	FYPO:0001357	(Fig. 10)
PMID:38940614	FYPO:0001357	(Fig. 10)
PMID:38940614	FYPO:0001357	(Fig. 10)
PMID:38940614	PBO:0114195	(Fig. 11)
PMID:38940614	PBO:0114195	(Fig. 11)
PMID:38940614	FYPO:0008285	(Fig. 11)
PMID:38940614	FYPO:0008285	(Fig. 11)
PMID:38940614	FYPO:0008286	(Fig. 11)
PMID:38940614	PBO:0114196	(Fig. 11)
PMID:38940614	PBO:0114197	(Fig. 11)
PMID:38940614	PBO:0114197	(Fig. 11)
PMID:38940614	PBO:0093559	(Fig. 9)
PMID:38940614	PBO:0093556	(Fig. 9)
PMID:38940614	FYPO:0005369	(Fig. 9)
PMID:38940614	FYPO:0005369	(Fig. 9)
PMID:38940614	PBO:0093561	(Fig. 9)
PMID:38940614	PBO:0093561	(Fig. 9)
PMID:38940614	PBO:0094777	(Fig. 8B)
PMID:38940614	PBO:0106693	(Fig. 8B)
PMID:38940614	PBO:0099750	(Fig. 8B)
PMID:38940614	PBO:0099750	(Fig. 8B)
PMID:38940614	FYPO:0005369	(Fig. 8A)
PMID:38940614	FYPO:0005369	(Fig. 8A)
PMID:38940614	PBO:0093559	(Fig. 8A)
PMID:38940614	PBO:0114187	(Fig. 7)
PMID:38940614	PBO:0114186	(Fig. 4A)
PMID:38940614	PBO:0114185	(Fig. 3A)
PMID:38940614	PBO:0114185	(Fig. 3A)
PMID:38940614	FYPO:0001357	(Fig. 9)
PMID:38940614	FYPO:0001357	(Fig. 9)
PMID:38940614	FYPO:0001357	(Fig. 9)
PMID:38940614	FYPO:0001357	(Fig. 9)
PMID:38940614	FYPO:0001357	(Fig. 9)
PMID:38940614	FYPO:0001357	(Fig. 9)
PMID:38940614	FYPO:0001357	(Fig. 9)
PMID:38940614	FYPO:0001357	(Fig. 9)
PMID:38940614	FYPO:0001357	(Fig. 9)
PMID:38940614	FYPO:0001357	(Fig. 9)
PMID:38940614	FYPO:0000674	(Fig. 9)
PMID:38940614	FYPO:0000674	(Fig. 9)
PMID:38940614	FYPO:0000674	(Fig. 9)
PMID:38940614	FYPO:0000674	(Fig. 9)
PMID:38940614	FYPO:0000674	(Fig. 9)
PMID:38940614	FYPO:0001357	(Fig. 8A)
PMID:38940614	FYPO:0001357	(Fig. 8A)
PMID:38940614	FYPO:0001357	(Fig. 8A)
PMID:38940614	GO:0052847	(Fig. 6C and 7)
PMID:38940614	FYPO:0001357	(Fig. 9)
PMID:38940614	FYPO:0001357	(Fig. 9)
PMID:38940614	FYPO:0001357	(Fig. 9)
PMID:38940614	PBO:0093558	(Fig. 9)
PMID:38940614	FYPO:0001357	(Fig. 9)
PMID:38940614	FYPO:0001357	(Fig. 9)
PMID:38940614	FYPO:0001575	(Fig. 10)
PMID:38940614	FYPO:0001575	(Fig. 10)
PMID:38940614	GO:0052846	(Fig. 6C and 7)
PMID:38940614	GO:0052845	(Fig. 6B and 7)
PMID:38940614	GO:0052843	(Fig. 5A, 6A and 7)
PMID:38940614	FYPO:0001357	(Fig. 8A)
PMID:38971312	FYPO:0008379	(Fig. 2A)
PMID:38971312	FYPO:0008380	(Fig. 5A)
PMID:38971312	FYPO:0008380	(Fig. 5B)
PMID:38971312	FYPO:0008380	(Fig. 5C)
PMID:38971312	PBO:0120682	(Fig. 1A and B)
PMID:38971312	PBO:0120682	(Fig. 1A, B and C and Fig. 5)
PMID:38971312	PBO:0120681	(Fig. 3C)
PMID:38971312	FYPO:0008380	(Fig. 5C)
PMID:38971312	FYPO:0008380	(Fig. 5D)
PMID:38971312	FYPO:0008380	(Fig. 5D)
PMID:38971312	FYPO:0008380	(Fig. 5C)
PMID:38971312	FYPO:0008380	(Fig. 5C)
PMID:38971312	FYPO:0008380	(Fig. 5E)
PMID:38971312	FYPO:0008380	(Fig. 5B)
PMID:38971312	FYPO:0008380	(Fig. 5C)
PMID:38971312	FYPO:0008380	(Fig. 5D)
PMID:38971312	FYPO:0008380	(Fig. 5D)
PMID:38971312	PBO:0120682	(Fig. 1B)
PMID:38971312	PBO:0120682	(Fig. 1B)
PMID:38971312	PBO:0120682	(Fig. 1B)
PMID:38971312	FYPO:0008380	(Fig. 5B)
PMID:38971312	FYPO:0008380	(Fig. 5B)
PMID:38971312	PBO:0120682	(Fig. 5E)
PMID:38971312	PBO:0120682	(Fig. 1B)
PMID:38971312	FYPO:0008379	(Fig. 2C)
PMID:38971312	PBO:0120682	(Fig. 1B)
PMID:38971312	PBO:0120683	(Fig. 1B)
PMID:38971312	PBO:0120683	(Fig. 1B)
PMID:38971312	FYPO:0008380	(Fig. 1D)
PMID:38971312	FYPO:0008380	(Fig. 1D)
PMID:38971312	FYPO:0001357	(Fig. 1E)
PMID:38971312	FYPO:0001357	(Fig. 1E)
PMID:38971312	PBO:0093561	(Fig. 1E)
PMID:38971312	PBO:0093615	(Fig. 1E)
PMID:38971312	PBO:0093561	(Fig. 1E)
PMID:38971312	PBO:0093559	(Fig. 1E)
PMID:38971312	PBO:0093613	(Fig. 1E)
PMID:38971312	PBO:0093613	(Fig. 1E)
PMID:38971312	PBO:0093613	(Fig. 1E)
PMID:38971312	PBO:0093614	(Fig. 1E)
PMID:38971312	FYPO:0008379	(Fig. 2A,B)
PMID:38971312	FYPO:0008379	(Fig. 2C)
PMID:38971312	FYPO:0008379	(Fig. 2C)
PMID:38971312	PBO:0120684	(Fig. 1A,3A)
PMID:38971312	PBO:0120681	(Fig. 3B)
PMID:38971312	PBO:0120685	(Fig. 3A)
PMID:38971312	PBO:0120684	(Fig. 1A,3A)
PMID:38971312	PBO:0120684	(Fig. 1A,3A)
PMID:38971312	FYPO:0008380	(Fig. 5A)
PMID:38971312	FYPO:0008380	(Fig. 5A)
PMID:38971312	FYPO:0008380	(Fig. 5C)
PMID:38971312	FYPO:0008380	(Fig. 5B)
PMID:38971312	FYPO:0008380	(Fig. 5B)
PMID:38971312	FYPO:0008380	(Fig. 5D)
PMID:38971312	FYPO:0008380	(Fig. 5D)
PMID:38971312	FYPO:0008380	(Fig. 5A)
PMID:38971312	FYPO:0008380	(Fig. 5A)
PMID:38971312	FYPO:0008380	(Fig. 5A)
PMID:38971312	PBO:0120685	(Fig. 3A)
PMID:38971312	PBO:0120685	(Fig. 3A)
PMID:38971312	FYPO:0008380	(Fig. 4A)
PMID:38971312	PBO:0120686	(Fig. 4B)
PMID:38971312	PBO:0120687	(Fig. 4B)
PMID:38985524	PBO:0114096	The Sid4 C-terminus interacts with the Ppc89 C-terminus (Rosenberg et al., 2006). Sid4- mCherry colocalized with endogenous Ppc89-GFP when FL or M+C were overexpressed, both forming enlarged SPBs (Figure 2). This is consistent with the idea that as additional Ppc89 C-termini becomes available at the SPB, more Sid4 can interact and localize there.
PMID:38985524	PBO:0114101	Ppc89 and Ppc89 M+C expressing cells exhibited the enlarged SPB phenotype (Figure 1D), as observed previously for FL Ppc89 (Rosenberg et al., 2006).
PMID:38985524	FYPO:0002061	(Figure 1B)
PMID:38985524	FYPO:0002061	(Figure 1B)
PMID:38985524	PBO:0114100	In contrast, Ppc89 N+M expressing cells displayed multiple foci of endogenous Ppc89-GFP (Figure 1D).
PMID:38985524	PBO:0114097	Pcp1 accumulated in enlarged Ppc89-containing structures upon overproduction of FL Ppc89 (Figure 3).
PMID:38985524	FYPO:0002061	(Figure 1B)
PMID:38985524	FYPO:0006431	Ppc89 and Ppc89 M+C expressing cells exhibited the enlarged SPB phenotype (Figure 1D), as observed previously for FL Ppc89 (Rosenberg et al., 2006).
PMID:38985524	PBO:0114095	Importantly, we also found that Pcp1-GFP could not localize to SPBs marked by Sad1-mCherry in cam1-E14 cells at the restrictive temperature (Figure 4E), suggest-ing that the PACT domain-Cam1 module directs SPB targeting.
PMID:38985524	PBO:0114094	We found that mNG-Cam1 could not localize to the SPB marked by Sad1-mCherry in pcp1-14 cells at the restrictive temperature (Figure 4D).
PMID:38985524	PBO:0114104	GFP-Ppc89(261-550) localized to SPBs marked by Sad1-mCherry
PMID:38985524	PBO:0114102	Similarly, we would expect overexpressed GFP-M+C to bind endogenous Pcp89 at the SPB to form larger SPBs and this was also observed (Supplemental Figure S1B).
PMID:38985524	PBO:0114105	but GFP-Ppc89(267-550-K299A) was diffuse in the cytoplasm and nucleus or present in foci that did not overlap with the SPB (Figure 6C).
PMID:38985524	PBO:0114105	Additionally, while GFP-Pcp1(PACT) localized at the SPB, GFP-Pcp1(PACT-I1151A) was diffuse throughout the cytosol and nucleus (Figure 6D)
PMID:38985524	PBO:0110446	When untagged Ppc89 N+M was overproduced, Sid4 was lost from the SPBs of cells that formed multiple Ppc89 foci (Figure 2). This result is consistent with the idea that N+M acts as a dominant negative, outcompeting endogenous Ppc89 at SPBs and diluting the Sid4-mCherry signal to such an extent that it can no longer be detected.
PMID:38985524	PBO:0114103	Like GFP-Pcp1 expressed from the weak nmt81 promoter, the GFP-PACT domain alone colocalized with Ppc89-mCherry (Figure 4B). Thus, Pcp1’s PACT domain is sufficient for SPB targeting.
PMID:38989013	FYPO:0002002	The phenotypes of the three mutants were comparable. At 25 ̊C, the percent of septated cells was 17-20 with none showing more than one septa and at 36 ̊C, all cells arrested with multiple septa and one or two nuclei (Figure 1H).
PMID:38989013	FYPO:0000082	All temperature-sensitive alleles grew less than wild-type at 36°C with the cdc16-C1 allele showing the greatest temperature-sensitivity (Figure 1I).
PMID:38989013	FYPO:0000118	(Figure 1H)
PMID:38989013	FYPO:0000082	All temperature-sensitive alleles grew less than wild-type at 36°C with the cdc16-C1 allele showing the greatest temperature-sensitivity (Figure 1I).
PMID:38989013	FYPO:0002002	(Figure 1H)
PMID:38989013	FYPO:0000082	A spot assay revealed that sid1-L2 had an intermediate restrictive temperature compared to sid1-125 and sid1-239 (Figure 1F).
PMID:38989013	FYPO:0001972	Nuclei and septa staining revealed predominantly a boomerang-shape phenotype that was often accompanied by cell lysis at septation (Figure 1E).
PMID:38989013	FYPO:0000082	A spot assay showed that the cdc14-E2 allele was comparable in its temperature sensitivity to cdc14-118 (Figure 1C).
PMID:38989013	FYPO:0000133	While cdc14-118 cells showed the classic sin phenotype of multinucleation and cell elongation at the non-permissive temperature, cdc14-E2 cells arrested uniformly at a very late stage of septation and frequently lysed (Figure 1B).
PMID:38989013	FYPO:0000082	A spot assay showed that the cdc14-E2 allele was comparable in its temperature sensitivity to cdc14-118 (Figure 1C).
PMID:38989013	FYPO:0003213	While cdc14-118 cells showed the classic sin phenotype of multinucleation and cell elongation at the non-permissive temperature, cdc14-E2 cells arrested uniformly at a very late stage of septation and frequently lysed (Figure 1B).
PMID:38989013	FYPO:0000082	All temperature-sensitive alleles grew less than wild-type at 36°C with the cdc16-C1 allele showing the greatest temperature-sensitivity (Figure 1I).
PMID:38989013	FYPO:0002049	(Figure 1E)
PMID:39010328	PBO:0093560	(Fig. 2B)
PMID:39010328	GO:0005774	As shown in Fig. 3B, GFP- Pib2 was detectable on vacuolar membranes, which can be visualized by the FM4-64 dye
PMID:39010328	FYPO:0001357	(Fig. 2A, 2B)
PMID:39010328	FYPO:0002672	(Fig. 2A)
PMID:39010328	PBO:0114118	(Fig. 3D)
PMID:39010328	PBO:0099989	(Fig. 1B)
PMID:39010328	PBO:0114119	(Fig. 1C)
PMID:39010328	FYPO:0001357	(Fig. 4A)
PMID:39010328	FYPO:0001357	(Fig. 4A)
PMID:39010328	PBO:0105134	(Fig. 2C)
PMID:39010328	PBO:0105134	(Fig. 4B)
PMID:39010328	PBO:0105134	(Fig. 4B)
PMID:39010328	PBO:0114120	(Fig. 3C)
PMID:39010328	PBO:0114118	(Fig. 3C)
PMID:39010328	PBO:0093560	(Fig. 2B)
PMID:39010328	PBO:0093560	(Fig. 2B)
PMID:39010328	PBO:0093560	(Fig. 2B)
PMID:39010328	PBO:0093560	(Fig. 2B)
PMID:39010328	PBO:0093560	(Fig. 2B)
PMID:39010328	PBO:0093560	(Fig. 2B)
PMID:39010328	PBO:0105131	(Fig. 2C)
PMID:39010328	PBO:0105131	(Fig. 2C)
PMID:39010328	PBO:0105131	(Fig. 2C)
PMID:39010328	PBO:0105131	(Fig. 2C)
PMID:39010328	PBO:0105131	(Fig. 2C)
PMID:39010328	PBO:0093560	(Fig. 4A)
PMID:39010328	PBO:0093560	(Fig. 4A)
PMID:39010328	PBO:0114121	(Fig. 4B)
PMID:39010328	PBO:0114121	(Fig. 4B)
PMID:39010328	PBO:0093561	(Fig. 4A)
PMID:39010328	PBO:0093561	(Fig. 4A)
PMID:39010328	PBO:0093560	(Fig. 2D)
PMID:39010328	PBO:0093560	(Fig. 2D)
PMID:39010328	PBO:0093561	(Fig. 2D)
PMID:39010328	PBO:0093561	(Fig. 2D)
PMID:39010328	PBO:0093561	(Fig. 2D)
PMID:39010328	PBO:0093561	(Fig. 2D)
PMID:39010328	PBO:0105134	(Fig. 4B)
PMID:39010328	PBO:0093561	(Fig. 2B)
PMID:39010328	PBO:0093561	(Fig. 2B)
PMID:39010328	PBO:0093561	(Fig. 2B)
PMID:39010328	FYPO:0001357	(Fig. 2A, 2B)
PMID:39010328	FYPO:0002672	(Fig. 2A)
PMID:39010328	FYPO:0001357	(Fig. 2B)
PMID:39010328	FYPO:0001357	(Fig. 2B)
PMID:39010328	FYPO:0001357	(Fig. 2B)
PMID:39010328	FYPO:0001357	(Fig. 2B)
PMID:39010328	FYPO:0001357	(Fig. 2B)
PMID:39010328	FYPO:0001357	(Fig. 2B)
PMID:39010328	PBO:0093559	(Fig. 2B)
PMID:39010328	PBO:0093559	(Fig. 2B)
PMID:39010328	FYPO:0001357	(Fig. 2B)
PMID:39010328	FYPO:0000047	(Fig. 2B)
PMID:39010328	FYPO:0001357	(Fig. 2B)
PMID:39010328	FYPO:0001357	(Fig. 2B)
PMID:39010328	PBO:0093561	(Fig. 2B)
PMID:39010328	PBO:0093561	(Fig. 2B)
PMID:39010328	PBO:0093559	(Fig. 2B)
PMID:39010328	PBO:0093559	(Fig. 2B)
PMID:39010328	PBO:0093561	(Fig. 2B)
PMID:39010328	PBO:0093560	(Fig. 2B)
PMID:39010328	PBO:0093560	(Fig. 2B)
PMID:39010328	PBO:0093560	(Fig. 2B)
PMID:39010328	PBO:0093560	(Fig. 2B)
PMID:39010328	PBO:0093560	(Fig. 2B)
PMID:39010328	PBO:0105134	(Fig. 2C)
PMID:39010328	PBO:0105134	(Fig. 2C)
PMID:39010328	PBO:0105131	(Fig. 2C)
PMID:39010328	FYPO:0001357	(Fig. 2B)
PMID:39010328	PBO:0093560	(Fig. 2B)
PMID:39010328	PBO:0093560	(Fig. 2B)
PMID:39012625	PBO:0114132	The pak1-ts cells are characteristically monopolar; however, we unexpectedly found that around 40% of these cells treated with CK-666 showed bipolar localization of Scd1-mNG (Fig. 5 A, asterisks).
PMID:39012625	PBO:0114129	(Fig. 4A)
PMID:39012625	PBO:0114128	(Fig. 4A)
PMID:39012625	PBO:0114127	(Fig. S1C and D)
PMID:39012625	GO:0045807	Interestingly, we also find that Pak1 is required for normal endocytic patch dynamics. Fig. 9
PMID:39012625	PBO:0114130	(Fig. 4A)
PMID:39012625	FYPO:0000422	(Fig. 9)
PMID:39012625	PBO:0114126	(Fig. S1A and B)
PMID:39012625	PBO:0114125	(Fig. 1)
PMID:39012625	PBO:0114124	(Fig. 7C and D)
PMID:39012625	PBO:0114123	(Fig. 7G)
PMID:39012625	GO:0061361	When the branched actin nucleator Arp2/3 complex is inhibited, Pak1 stabilizes at a cell end, preventing localization of the GEF and Scd1, and disrupting the positive and negative feedback loops needed for periodic Cdc42 activity at that end.
PMID:39012625	PBO:0114131	(Fig. 5A)
PMID:39012625	PBO:0114133	(Fig. 7A and B)
PMID:39016088	PBO:0114620	(comment: CHECK The defect was observed in rec12-deletion rec8-2A mutant background) Fig 3C.
PMID:39016088	FYPO:0000964	(Fig. 2) (comment: CHECK TBZ sensitivity testing for wild-type, 9A, and 9D)
PMID:39016088	FYPO:0000964	(Fig. 2) (comment: CHeCK TBZ sensitivity testing for wild-type, 9A, and 9D)
PMID:39016088	PBO:0114621	(comment: CHECK The defect was observed in the rec12-deletion rec8-2A mutation background. The defect of fta2-9D was less than that of fta2-9A) Fig 3C.
PMID:39094565	PBO:0114945	(Fig. 3G)
PMID:39094565	FYPO:0008327	(Fig. 3, Fig. S3)
PMID:39094565	FYPO:0008327	(Fig. S4)
PMID:39094565	PBO:0114944	(Fig. S2F)
PMID:39094565	PBO:0114943	(Fig. S2F)
PMID:39094565	PBO:0114942	(Fig. S2F)
PMID:39094565	PBO:0114660	(Fig. S2F)
PMID:39094565	PBO:0114941	(Fig. S2F)
PMID:39094565	PBO:0114940	(Fig. S2F)
PMID:39094565	PBO:0114939	(Fig. S2F)
PMID:39094565	PBO:0114658	(Fig. S2F)
PMID:39094565	PBO:0094263	(Fig. 1D and E)
PMID:39094565	PBO:0113949	(Fig. S1K)
PMID:39094565	PBO:0114932	(Fig. S6A)
PMID:39094565	PBO:0113940	(Fig. S6A)
PMID:39094565	PBO:0113949	(Fig. 5F)
PMID:39094565	PBO:0113940	(Fig. 7C)
PMID:39094565	PBO:0114933	(Fig. 5A)
PMID:39094565	PBO:0114932	(Fig. 4G)
PMID:39094565	PBO:0113940	(Fig. 1F, Fig. S1G and Fig. 2C)
PMID:39094565	PBO:0114931	(Fig. S1C)
PMID:39094565	PBO:0108812	(Fig. S2F)
PMID:39094565	PBO:0114936	(Fig. S2F)
PMID:39094565	PBO:0114659	(Fig. S2F)
PMID:39094565	PBO:0114934	(Fig. S2C)
PMID:39094565	PBO:0114935	(Fig. S2D)
PMID:39094565	PBO:0114935	(Fig. 2E)
PMID:39094565	PBO:0114934	(Fig. 2D)
PMID:39094565	PBO:0094265	(Fig. S2B)
PMID:39094565	PBO:0113940	(Fig. S1G)
PMID:39094565	PBO:0114937	(Fig. S2F)
PMID:39094565	PBO:0112523	(Fig. S1G)
PMID:39094565	PBO:0114938	(Fig. S2F)
PMID:39094565	PBO:0114934	(Fig. S1B)
PMID:39094565	PBO:0094265	(Fig. 1D and E)
PMID:39094565	PBO:0094264	(Fig. S1I and J)
PMID:39094565	PBO:0114947	(Fig. S7D)
PMID:39094565	PBO:0094264	(Fig. S6B)
PMID:39094565	PBO:0094263	(Fig. S6B)
PMID:39094565	PBO:0094265	(Fig. S6F)
PMID:39094565	PBO:0094264	(Fig. S7B)
PMID:39094565	PBO:0094263	(Fig. 5B, Fig. S6C)
PMID:39094565	PBO:0114946	(Fig. S7D)
PMID:39094565	PBO:0094265	(Fig. 4D and E)
PMID:39094565	PBO:0094263	(Fig. S6C)
PMID:39094565	PBO:0094264	(Fig. 4D and E)
PMID:39094565	PBO:0094265	(Fig. S1E and F)
PMID:39094565	PBO:0094263	(Fig. 1D and E)
PMID:39094565	FYPO:0004540	(Fig. S4)
PMID:39094565	FYPO:0004540	(Fig. 3)
PMID:39096900	PBO:0120618	(Fig. 5C, 5F, 5H)
PMID:39096900	PBO:0120609	(Fig. 5I)
PMID:39096900	FYPO:0007002	(Fig. 5I)
PMID:39096900	FYPO:0007002	(Fig. 5I)
PMID:39096900	FYPO:0007002	(Fig. 5I)
PMID:39096900	FYPO:0007002	(Fig. 5I)
PMID:39096900	FYPO:0007376	Expression of Snf5-CDx2 fusion protein abolished epigenetic inheritance of ectopic heterochromatin. (Fig. 6C, 6D)
PMID:39096900	PBO:0095651	(Fig. S1A)
PMID:39096900	PBO:0095653	(Fig. S1A)
PMID:39096900	PBO:0095653	(Fig. S1A)
PMID:39096900	PBO:0095984	(Fig. S4B)
PMID:39096900	PBO:0117342	(Fig. S5A)
PMID:39096900	PBO:0095984	(Fig. S5B)
PMID:39096900	PBO:0095984	(Fig. S5B)
PMID:39096900	PBO:0109209	(Fig. 1E, 1F)
PMID:39096900	PBO:0120613	(Fig. 5G)
PMID:39096900	PBO:0120613	(Fig. 5G)
PMID:39096900	PBO:0120613	(Fig. 5G)
PMID:39096900	FYPO:0007336	(Fig. S1B)
PMID:39096900	PBO:0109209	(Fig. 1E, 1F)
PMID:39096900	PBO:0095652	(Fig. S1B)
PMID:39096900	PBO:0095652	(Fig. S1B)
PMID:39096900	PBO:0120610	(Fig. 3E)
PMID:39096900	PBO:0120613	(Fig. 5G)
PMID:39096900	PBO:0120621	(Fig. 5F, 5H)
PMID:39096900	PBO:0120621	(Fig. 5F, 5H)
PMID:39096900	PBO:0120620	(Fig. 5F, 5H)
PMID:39096900	PBO:0120620	(Fig. 5F, 5H)
PMID:39096900	PBO:0120610	(Fig. 3E)
PMID:39096900	PBO:0120611	(Fig. 3E)
PMID:39096900	PBO:0095652	(Fig. S1B)
PMID:39096900	FYPO:0008364	(Fig. S1E)
PMID:39096900	PBO:0120610	(Fig. 3E)
PMID:39096900	FYPO:0005844	(Fig. 5D, 5G)
PMID:39096900	FYPO:0005844	(Fig. 5D, 5G)
PMID:39096900	PBO:0120619	(Fig. 5C, 5F, 5H)
PMID:39096900	PBO:0120609	(Fig. 5I)
PMID:39096900	PBO:0120615	(Fig. 5B)
PMID:39096900	PBO:0120628	(Fig. 1G)
PMID:39096900	GO:0120262	(Fig. 1)
PMID:39096900	PBO:0120627	(Fig. S2)
PMID:39096900	PBO:0109215	(Fig. S1E)
PMID:39096900	PBO:0120609	(Fig. 3E)
PMID:39096900	PBO:0109209	(Fig. S1E)
PMID:39096900	PBO:0120612	(Fig. 1C, 1D)
PMID:39096900	PBO:0109215	(Fig. 1E, 1F)
PMID:39096900	PBO:0109209	(Fig. S1E)
PMID:39096900	FYPO:0007336	(Fig. S5E)
PMID:39096900	PBO:0095651	(Fig. S5E)
PMID:39096900	PBO:0120622	(Fig. S6)
PMID:39096900	PBO:0109215	(Fig. S1E)
PMID:39096900	FYPO:0007336	(Fig. S1B)
PMID:39096900	PBO:0095653	(Fig. 1C)
PMID:39096900	PBO:0095653	(Fig. 1C)
PMID:39096900	FYPO:0007336	(Fig. 1C)
PMID:39096900	PBO:0120628	(Fig. 1G)
PMID:39096900	PBO:0120629	(Fig. 1G)
PMID:39096900	PBO:0120623	(Fig. S6)
PMID:39096900	FYPO:0004749	(Fig. 2D)
PMID:39096900	GO:0120262	(Fig. 1)
PMID:39096900	GO:0120262	Deletion of rsc1 promotes epigenetic heterochromatin inheritance. (Fig. S6)
PMID:39096900	GO:0120262	Targeting Mst2 to heterochromatin by expressing chromodomain-fused Mst2 (Mst2-CDx2) resulted in the loss of heterochromatin and gene silencing. (Fig. 4)
PMID:39096900	GO:0120262	Targeting SWI/SNF to heterochromatin by expressing chromodomain-fused Snf5 (Snf5-CDx2) resulted in the loss of heterochromatin and gene silencing. (Fig. 5)
PMID:39096900	GO:0120262	Targeting SWI/SNF to heterochromatin by expressing chromodomain-fused Snf59 (Snf59-CDx2) resulted in the loss of heterochromatin and gene silencing. (Fig. 5)
PMID:39096900	GO:0120262	Deletion of snf22 promotes epigenetic heterochromatin inheritance. (Fig. S6)
PMID:39096900	PBO:0120624	(Fig. 3B, 3D)
PMID:39096900	PBO:0120625	(Fig. 3C)
PMID:39096900	PBO:0120626	(Fig. 3D)
PMID:39096900	PBO:0120626	(Fig. 3D)
PMID:39096900	PBO:0120625	(Fig. 3C)
PMID:39096900	PBO:0120615	(Fig. 4D)
PMID:39096900	PBO:0120617	(Fig. 4H)
PMID:39096900	PBO:0109209	(Fig. 4G)
PMID:39096900	PBO:0120630	(Fig. 1G)
PMID:39096900	PBO:0109209	(Fig. 1E, 1F)
PMID:39096900	PBO:0109209	(Fig. 1E, 1F)
PMID:39096900	PBO:0120613	(Fig. 1E, 1F)
PMID:39096900	PBO:0120614	(Fig. 1C, 1D)
PMID:39096900	PBO:0120615	(Fig. 3A, 3C)
PMID:39096900	FYPO:0008327	(Fig. 2A-C)
PMID:39096900	FYPO:0007336	(Fig. S1D)
PMID:39096900	PBO:0095652	(Fig. S1D)
PMID:39096900	PBO:0095652	(Fig. S1D)
PMID:39096900	PBO:0120616	(Fig. 4B)
PMID:39096900	PBO:0120617	(Fig. 4C, 4H)
PMID:39096900	PBO:0109215	(Fig. 4E, 4G)
PMID:39096900	FYPO:0007336	(Fig. 4F)
PMID:39096900	PBO:0095652	(Fig. 4F)
PMID:39096900	PBO:0095652	(Fig. 4F)
PMID:39096900	PBO:0120615	(Fig. 5B)
PMID:39105351	FYPO:0007087	In contrast, in Δsdr1 diploid cells, almost no sporulation occurred under nitrogen or sulfur starvation, and the sporulation rate during phosphate starvation was also significantly less.
PMID:39105351	FYPO:0008321	In contrast, in Δsdr1 diploid cells, almost no sporulation occurred under nitrogen or sulfur starvation, and the sporulation rate during phosphate starvation was also significantly less.
PMID:39105351	PBO:0108843	We found that, similar to a phosphate-depleted environment (Ohtsuka et al., 2023), the expression levels in Δpho7 cells were significantly reduced under sulfur- depleted conditions (Figure 4).
PMID:39105351	PBO:0110728	We found that, similar to a phosphate-depleted environment (Ohtsuka et al., 2023), the expression levels in Δpho7 cells were significantly reduced under sulfur- depleted conditions (Figure 4).
PMID:39105351	FYPO:0008319	In Δfal1 cells, sulfur depletion induced the cleavage of GFP-Atg8, resulting in free-GFP, which confirms the occurrence of autophagy (Figure 2a).
PMID:39105351	FYPO:0007592	autophagy was triggered in ΔSPCC417.09c cells under nitrogen depletion but not under sulfur depletion.
PMID:39105351	PBO:0114819	Contrary to our prediction, the presence or absence of sdr1+ did not have significant effect on atg1+ and atg20+ induction by sulfur starvation.
PMID:39105351	FYPO:0008320	similar to sdr1+, overexpression of fal1+ did not rectify the morphological abnormalities of Δecl cells under sulfur depletion.
PMID:39105351	PBO:0114810	Additionally, we confirmed gene expressions that showed significant differences due to the deletion of sdr1+ through a real-time polymerase chain reaction (PCR) assay (Figure 3a).
PMID:39105351	FYPO:0001355	The induction of sdr1+ expression, yeast cell growth was significantly suppressed (Figure 2d), indicating that excessive expression of sdr1+ plays an active role in suppressing yeast cell growth.
PMID:39105351	FYPO:0007500	(Figure 2a). However, in ΔSPCC417.09c cells, sulfur depletion did not induce the cleavage of GFP-Atg8, indicating that autophagy was not induced.
PMID:39105351	PBO:0114860	These include mei2+, which encodes the master meiosis-regulator (Harigaya et al., 2006; Sugiyama et al., 2016), and phosphate depletion-responsive genes ecl3+, pho1+, and pho84+
PMID:39105351	PBO:0114859	These include mei2+, which encodes the master meiosis-regulator (Harigaya et al., 2006; Sugiyama et al., 2016), and phosphate depletion-responsive genes ecl3+, pho1+, and pho84+
PMID:39105351	PBO:0114813	(Figure 3a). However, dal51+ is an adjacent gene to sdr1+ (Figure S1). Therefore, the increased expression of dal51+ in Δsdr1 cells was potentially due to the loss of the regulatory sequence of dal51+ expression rather than the deletion of the sdr1+.
PMID:39105351	FYPO:0008320	Although the morphological abnormalities of Δsdr1 cells under sulfur depletion were rectified by overexpressing sdr1+, those of Δecls cells were not (Figure 5).
PMID:39105351	PBO:0114822	In this regard, we also confirmed that the sdr1+ deletion mutant exhibited a shorter CLS than the wild-type during the stationary phase in our assay system (Figure 6).
PMID:39105351	PBO:0114820	Contrary to our prediction, the presence or absence of sdr1+ did not have significant effect on atg1+ and atg20+ induction by sulfur starvation.
PMID:39105351	PBO:0114821	Additionally, we confirmed gene expressions that showed significant differences due to the deletion of sdr1+ through a real-time polymerase chain reaction (PCR) assay (Figure 3a).
PMID:39105351	PBO:0114817	Additionally, we confirmed gene expressions that showed significant differences due to the deletion of sdr1+ through a real-time polymerase chain reaction (PCR) assay (Figure 3a).
PMID:39105351	PBO:0114861	These include mei2+, which encodes the master meiosis-regulator (Harigaya et al., 2006; Sugiyama et al., 2016), and phosphate depletion-responsive genes ecl3+, pho1+, and pho84+
PMID:39105351	PBO:0114812	However, dal51+ is an adjacent gene to sdr1+ (Figure S1). Therefore, the increased expression of dal51+ in Δsdr1 cells was potentially due to the loss of the regulatory sequence of dal51+ expression rather than the deletion of the sdr1+.
PMID:39105351	PBO:0114811	Additionally, we confirmed gene expressions that showed significant differences due to the deletion of sdr1+ through a real-time polymerase chain reaction (PCR) assay (Figure 3a).
PMID:39105351	PBO:0114818	Additionally, we confirmed gene expressions that showed significant differences due to the deletion of sdr1+ through a real-time polymerase chain reaction (PCR) assay (Figure 3a).
PMID:39110593	PBO:0102525	(comment: CONDITION medium pH below 3.5)
PMID:39110593	PBO:0102525	medium pH below 3.5. In fact, scs2Dscs22D cells already showed compromised growth in highly acidic media, similarly to pma1-DCter cells that lacked the C-terminal R domain (Figure 6D).
PMID:39110593	PBO:0114925	Such interactions were required for its cortical localization, as Csr102 became cytosolic in the absence of both VAPs even when ER-PM contacts were artificially restored (Figures 2E and S2F).
PMID:39110593	PBO:0114918	Such reduction was enhanced when cells further lost either or both of csr102 and pdr16 in the background, whereas mutants with single or double deletion of csr102 and pdr16 remained WT-like (Figure 2D).
PMID:39110593	PBO:0114926	Notably, mutations of three previously reported conserved lysine residues (K36/38/43A,20,21 hereafter referred to as 3KA) in the VAP consensus sequence (VCS) within the MSP domain of either Scs2 or Scs22 abolished their ER-PM tethering capacity (asterisked by large PM regions devoid of the cER in Figure 1C)
PMID:39110593	FYPO:0008294	(Figure S3A) (left panel), ER-PM tethering is reduced in Scs2-2TA mutant at native locus
PMID:39110593	GO:0001786	(Figure 3D)
PMID:39110593	GO:0035091	(Figure 3D)
PMID:39110593	FYPO:0006330	(Figures 4B and S4B)
PMID:39110593	FYPO:0008294	ER-PM contact formation was however unaffected in pps1D (Figures 4B and S4B).
PMID:39110593	FYPO:0008330	We also saw augmented PM levels of PI4P and PI4,5P2 indicated by PHOsh2-GFP and PHNum1- GFP,5 respectively, in these cells (Figure S4A)
PMID:39110593	FYPO:0008329	Indeed, as previously shown,31 the PM pool of PS marked by GFP-Lact-C234 was absent in pps1D (Figure S4A).
PMID:39110593	GO:0001786	In fact, purified Scs2N-6His could bind both PI and PS liposomes. Such binding was enhanced with increased PI or PS concentration or by adding PI4P to respective liposomes (Figure S3C).
PMID:39110593	GO:0035091	In fact, purified Scs2N-6His could bind both PI and PS liposomes. Such binding was enhanced with increased PI or PS concentration or by adding PI4P to respective liposomes (Figure S3C).
PMID:39110593	PBO:0114928	Likewise, the cortical recruitment of Csr102 was fully rescued by Scs2-PM but not Scs23KA-PM (Figure S3B).
PMID:39110593	PBO:0114917	Such reduction was enhanced when cells further lost either or both of csr102 and pdr16 in the background, whereas mutants with single or double deletion of csr102 and pdr16 remained WT-like (Figure 2D).
PMID:39110593	PBO:0114916	Such reduction was enhanced when cells further lost either or both of csr102 and pdr16 in the background, whereas mutants with single or double deletion of csr102 and pdr16 remained WT-like (Figure 2D).
PMID:39110593	PBO:0114915	We found that both the PM and Golgi pools of PI4P decreased significantly in sec14D cells.
PMID:39110593	PBO:0114914	Scs2N bound specifically to PI and PS, and Scs2N2TA showed weaker binding to both, whereas Scs2N3KA exhibited significantly lower affinities for both (Figures 3C, S3D, and S3E). (liposome binding assay)
PMID:39110593	PBO:0114913	Scs2N bound specifically to PI and PS, and Scs2N2TA showed weaker binding to both, whereas Scs2N3KA exhibited significantly lower affinities for both (Figures 3C, S3D, and S3E). (Liposome binding assay)
PMID:39110593	FYPO:0006629	Surprisingly, like WT (Figure S1F), Scs2-PM was able to restore the PM PI4P level in scs2Dscs22D cells, while Scs23KA-PM again lost the competence (Figure 3B).
PMID:39110593	PBO:0114927	Fascinatingly, though not as fully efficient as WT, Scs2-PM was able to establish ER-PM contacts in a dose-dependent manner, which similarly required a functional MSP domain (Figure 3A).
PMID:39110593	PBO:0114926	(Figure S3A) (left panel), ER-PM tethering is reduced in Scs2-2TA mutant at native locus
PMID:39110593	FYPO:0008294	However, no reduction of ER-PM contacts was seen in csr102Dpdr16Dpil1D cells, and Scs2 could still establish ER-PM contacts at cortical regions devoid of Pma1 in the background (Figure 2G)
PMID:39110593	PBO:0114910	(Figure 3D)
PMID:39110593	GO:0120010	Such reduction was enhanced when cells further lost either or both of csr102 and pdr16 in the background, whereas mutants with single or double deletion of csr102 and pdr16 remained WT-like (Figure 2D). No detectable change of phosphatidylinositol 4,5-bisphosphate (PI4,5P2) levels was seen in all these mutants (data not shown). These data suggest that Sec14 family proteins contribute to PI4P homeostasis in S. pombe.
PMID:39110593	PBO:0114909	(Figure 3D)
PMID:39110593	PBO:0114912	(Figure 3D)
PMID:39110593	PBO:0114915	We found that both the PM and Golgi pools of PI4P decreased significantly in sec14D cells.
PMID:39110593	GO:0120010	Such reduction was enhanced when cells further lost either or both of csr102 and pdr16 in the background, whereas mutants with single or double deletion of csr102 and pdr16 remained WT-like (Figure 2D). No detectable change of phosphatidylinositol 4,5-bisphosphate (PI4,5P2) levels was seen in all these mutants (data not shown). These data suggest that Sec14 family proteins contribute to PI4P homeostasis in S. pombe.
PMID:39110593	GO:0120010	Such reduction was enhanced when cells further lost either or both of csr102 and pdr16 in the background, whereas mutants with single or double deletion of csr102 and pdr16 remained WT-like (Figure 2D). No detectable change of phosphatidylinositol 4,5-bisphosphate (PI4,5P2) levels was seen in all these mutants (data not shown). These data suggest that Sec14 family proteins contribute to PI4P homeostasis in S. pombe.
PMID:39110593	PBO:0114926	Notably, mutations of three previously reported conserved lysine residues (K36/38/43A,20,21 hereafter referred to as 3KA) in the VAP consensus sequence (VCS) within the MSP domain of either Scs2 or Scs22 abolished their ER-PM tethering capacity (asterisked by large PM regions devoid of the cER in Figure 1C)
PMID:39110593	PBO:0114926	Notably, mutations of three previously reported conserved lysine residues (K36/38/43A,20,21 hereafter referred to as 3KA) in the VAP consensus sequence (VCS) within the MSP domain of either Scs2 or Scs22 abolished their ER-PM tethering capacity (asterisked by large PM regions devoid of the cER in Figure 1C)
PMID:39110593	GO:0005635	Unlike Scs22 where its nuclear envelope (NE) localization was obvious, the NE pool of Scs2 was barely visible, suggesting likely stronger affinity of Scs2 toward the cell cortex (Figure 1C).
PMID:39110593	GO:0032541	(Figure 1C)
PMID:39110593	GO:0032541	(Figure 1C)
PMID:39110593	FYPO:0006330	Interestingly, ER-PM association was compromised when the open reading frames of scs2 and scs22 were swapped at their genomic loci (asterisked in Figure S1A), implying that two VAPs may intrinsically differ in ER-PM tethering function.
PMID:39110593	PBO:0114926	A previous study has shown that Scs2 plays a dominant role in ER-PM tethering over Scs22 in fission yeast,5 manifested by apparent ER-PM dissociation indicated by the luminal ER marker mCherry-ADEL18 in scs2D cells (see also Figure 1A).
PMID:39110593	SO:0001527	(comment: FFAT-like motif that binds VAPs (scs2))
PMID:39110593	GO:0035091	(comment: liposome binding assay)
PMID:39110593	PBO:0109538	Either the removal or genetic alterations of this presumed Scs2-interacting motif engendered inviable spores in S. pombe (Figure 6A), indicative of its necessity for Pma1 function.
PMID:39110593	PBO:0109538	Either the removal or genetic alterations of this presumed Scs2-interacting motif engendered inviable spores in S. pombe (Figure 6A), indicative of its necessity for Pma1 function.
PMID:39110593	PBO:0109538	Either the removal or genetic alterations of this presumed Scs2-interacting motif engendered inviable spores in S. pombe (Figure 6A), indicative of its necessity for Pma1 function.
PMID:39110593	PBO:0097202	(comment: CONDITION medium pH below 3.5) (Figure 6)
PMID:39110593	PBO:0097202	(comment: CONDITION medium pH below 3.5) (Figure 6)
PMID:39110593	PBO:0114911	(Figure 3D)
PMID:39110593	PBO:0102525	(comment: CONDITION medium pH below 3.5) (Figure 6)
PMID:39110593	PBO:0097202	(comment: CONDITION medium pH below 3.5) (Figure 6)
PMID:39156640	PBO:0117349	(Fig. 1B)
PMID:39156640	PBO:0117349	(Fig. 1B)
PMID:39156640	PBO:0117349	(Fig. 1B)
PMID:39156640	PBO:0117349	(Fig. 1B)
PMID:39156640	PBO:0117349	(Fig. 1D)
PMID:39156640	PBO:0117349	(Fig. 1D)
PMID:39156640	PBO:0117350	(Fig. 1A and B)
PMID:39156640	PBO:0117351	(Fig. 1A and C)
PMID:39156640	PBO:0117352	(Fig. 1A and C)
PMID:39156640	PBO:0093558	(Fig. 3B)
PMID:39156640	PBO:0093558	(Fig. 3B)
PMID:39156640	PBO:0117352	(Fig. 1C)
PMID:39156640	PBO:0117353	(Fig. 1E)
PMID:39156640	PBO:0117364	(Fig. 7F and G)
PMID:39156640	PBO:0117364	(Fig. 7F and G)
PMID:39156640	PBO:0117363	(Fig. 7F and G)
PMID:39156640	PBO:0117362	(Fig. 7A, C, D and E)
PMID:39156640	PBO:0117362	(Fig. 7B, C and D)
PMID:39156640	PBO:0117361	(Fig. 6A)
PMID:39156640	PBO:0117360	(Fig. 6A)
PMID:39156640	PBO:0117360	(Fig. 6A)
PMID:39156640	FYPO:0002942	(Fig. 5B)
PMID:39156640	FYPO:0002942	(Fig. 5B)
PMID:39156640	FYPO:0002942	(Fig. 5B)
PMID:39156640	FYPO:0002942	(Fig. 5B)
PMID:39156640	PBO:0093560	(Fig. 3B)
PMID:39156640	FYPO:0000674	(Fig. 3B)
PMID:39156640	FYPO:0000674	(Fig. 3B)
PMID:39156640	FYPO:0000674	(Fig. 3B)
PMID:39156640	GO:2000769	We show that Bgs1-synthetized linear b(1,3)glucan cooperates specifically with the Tea1-Tea4 complex, but not with the rest of polarisome proteins, and all together are essential for the control and maintenance of growth polarity and morphology (Figure 5C).
PMID:39156640	FYPO:0002652	(Fig. 6B)
PMID:39156640	PBO:0117366	(Fig. 6C, D and E)
PMID:39156640	PBO:0093558	(Fig. 3B)
PMID:39156640	PBO:0093558	(Fig. 3B)
PMID:39156640	PBO:0093559	(Fig. 3B)
PMID:39156640	PBO:0117349	(Fig. 3A)
PMID:39156640	PBO:0117349	(Fig. 3A)
PMID:39156640	PBO:0117349	(Fig. 3A)
PMID:39156640	PBO:0117349	(Fig. 3A)
PMID:39156640	PBO:0117349	(Fig. 3A)
PMID:39156640	PBO:0117349	(Fig. 3A)
PMID:39156640	PBO:0117365	(Fig. 7F and G)
PMID:39156640	PBO:0117354	(Fig. 2A)
PMID:39156640	PBO:0117355	(Fig. 2A)
PMID:39156640	PBO:0117356	(Fig. 2B)
PMID:39156640	PBO:0117353	(Fig. 1E)
PMID:39156640	PBO:0117353	(Fig. 1E)
PMID:39156640	PBO:0117359	(Fig. 3A)
PMID:39156640	PBO:0117358	(Fig. 2B)
PMID:39156640	PBO:0117358	(Fig. 2B)
PMID:39156640	PBO:0117357	(Fig. 2B and C)
PMID:39156640	PBO:0117357	(Fig. 2B and C)
PMID:39156640	PBO:0117356	(Fig. 2B)
PMID:39156640	PBO:0117352	(Fig. 1D)
PMID:39156640	PBO:0117352	(Fig. 1D)
PMID:39156640	PBO:0117353	(Fig. 1E)
PMID:39156640	PBO:0117353	(Fig. 1E)
PMID:39156640	PBO:0117352	(Fig. 1A and C)
PMID:39156640	PBO:0117353	(Fig. 1C)
PMID:39156640	PBO:0117353	(Fig. 1C)
PMID:39156640	PBO:0117352	(Fig. 1C)
PMID:39156640	FYPO:0001357	(Fig. 3B)
PMID:39156640	FYPO:0001357	(Fig. 3B)
PMID:39156640	FYPO:0001357	(Fig. 3B)
PMID:39156640	PBO:0093560	(Fig. 3B)
PMID:39156640	PBO:0093560	(Fig. 3B)
PMID:39156640	PBO:0093560	(Fig. 3B)
PMID:39156640	PBO:0117349	(Fig. 1D)
PMID:39156640	PBO:0117349	(Fig. 1D)
PMID:39156640	PBO:0117353	(Fig. 1E)
PMID:39156640	FYPO:0000135	(Fig. 4A)
PMID:39156640	FYPO:0002021	(Fig. 4A, 4B, Fig. S5B)
PMID:39156640	PBO:0117349	(Fig. 5A)
PMID:39156640	FYPO:0002021	(Fig. 5A)
PMID:39156640	PBO:0117349	(Fig. 1A and B)
PMID:39156640	PBO:0117349	(Fig. 1A and B)
PMID:39174851	PBO:0095390	(Fig. 3C)
PMID:39174851	PBO:0095386	(Fig. 3B)
PMID:39174851	FYPO:0004993	(Fig. 7D)
PMID:39174851	PBO:0114688	(Fig. 4A, Fig. EV2 and EV3)
PMID:39174851	PBO:0114689	(Fig. 3A, Fig. EV1A)
PMID:39174851	PBO:0106083	(Fig. 4A, Fig. EV2)
PMID:39174851	PBO:0114690	(Fig. EV4)
PMID:39174851	FYPO:0003891	(Fig. 3C)
PMID:39174851	PBO:0105184	(Fig. 3B)
PMID:39174851	FYPO:0004993	(Fig. 7D)
PMID:39174851	PBO:0114691	(Fig. 4A, Fig. EV2 and EV3)
PMID:39174851	PBO:0114692	(Fig. 3A, Fig. EV1A)
PMID:39174851	FYPO:0008303	(Fig. 4A, Fig. EV2)
PMID:39174851	PBO:0114690	(Fig. EV4)
PMID:39174851	PBO:0114693	(Fig. 7C)
PMID:39174851	PBO:0114694	The mobility shift observed in Phos-tag gels was almost completely abolished in this EGFP-Sfr1-7A mutant protein, indicating that it was related to modifications in these residues of the protein (Fig. 1D).
PMID:39174851	PBO:0101665	(Fig. S4A)
PMID:39174851	PBO:0114695	(Fig. S4B)
PMID:39174851	PBO:0106083	(Fig. 4, Fig. EV2)
PMID:39174851	PBO:0114696	(Fig. S4C)
PMID:39174851	PBO:0114697	(Fig. S3A and B)
PMID:39174851	PBO:0114697	(Fig. S3A and B)
PMID:39174851	PBO:0114697	(Fig. S3A and B)
PMID:39174851	PBO:0114698	(Fig. 3A)
PMID:39174851	PBO:0114699	(Fig. 7A)
PMID:39174851	PBO:0114700	(Fig. 7A)
PMID:39174851	PBO:0114700	(Fig. 7A)
PMID:39174851	PBO:0097898	(Fig. 7D)
PMID:39174851	PBO:0097898	(Fig. 7D)
PMID:39174851	PBO:0095337	(Fig. 7D)
PMID:39174851	PBO:0095337	(Fig. 7D)
PMID:39174851	PBO:0114701	(Fig. 7A)
PMID:39174851	PBO:0114701	(Fig. 7A)
PMID:39174851	PBO:0095338	(Fig. 7D)
PMID:39174851	FYPO:0000478	(Fig. 4A, Fig. S2)
PMID:39174851	FYPO:0008305	(Fig. 6)
PMID:39174851	PBO:0114702	(Fig. 1 and 5)
PMID:39174851	PBO:0092319	EGFP-Sfr1 protein was clearly detected from the end of S-phase (2.5 h after meiotic induction) to the entry into the first chromosome segregation (meiosis I, 4.5 h), with the highest levels during meiotic prophase (Fig. 1A).
PMID:39174851	PBO:0097905	(Fig. 7C)
PMID:39174851	PBO:0114693	(Fig. 7C)
PMID:39174851	PBO:0114703	(Fig. 1B and 2C)
PMID:39174851	PBO:0114704	This mobility shift was diminished in cells of the same culture treated in parallel with 1-NM- PP1, showing a 50% reduction in the slow-migrating band compared to DMSO-treated cells at 4 h after meiotic induction (n = 4, P value = 0.0337). This result suggests that Cdc2 is responsible for the phosphorylation of Sfr1 during meiotic prophase. (Fig. 2A)
PMID:39174851	FYPO:0000478	(Fig. 4A, Fig. S2)
PMID:39174851	FYPO:0000478	(Fig. 4A, Fig. S2)
PMID:39174851	PBO:0114705	(Fig. 5)
PMID:39174851	FYPO:0008305	(Fig. 6)
PMID:39174851	FYPO:0003176	(Fig. 7A)
PMID:39174851	FYPO:0003176	(Fig. 7A)
PMID:39174851	PBO:0114706	(Fig. 7A)
PMID:39174851	PBO:0114707	(Fig. 7A)
PMID:39174851	PBO:0114707	(Fig. 7A)
PMID:39174851	PBO:0114693	(Fig. 7C)
PMID:39174851	PBO:0114693	(Fig. 7C)
PMID:39174851	PBO:0097898	(Fig. 7D)
PMID:39174851	PBO:0097898	(Fig. 7D)
PMID:39174851	PBO:0114697	(Fig. S3C)
PMID:39174851	PBO:0114705	(Fig. 5)
PMID:39174851	PBO:0114697	(Fig. S3C)
PMID:39174851	PBO:0114691	(Fig. 5)
PMID:39174851	PBO:0114697	(Fig. S3C)
PMID:39174851	PBO:0097898	(Fig. 7D)
PMID:39239853	GO:0140268	Live-cell imaging revealed that they all localized either uniformly or in a punctate pattern along the lateral cell cortex and, all but Ist2 lacked any detectable localization at the cell division site (Fig. 3A)
PMID:39239853	GO:0140268	Live-cell imaging revealed that they all localized either uniformly or in a punctate pattern along the lateral cell cortex and, all but Ist2 lacked any detectable localization at the cell division site (Fig. 3A)
PMID:39239853	PBO:0114513	Live-cell imaging revealed that over-production of Duc1 indeed reduced Opy1-mNG at the PM by ~35% (Fig. 5C,D).
PMID:39239853	PBO:0114512	Live-cell imaging revealed that over-production of Duc1 indeed reduced Opy1-mNG at the PM by ~35% (Fig. 5C,D).
PMID:39239853	FYPO:0000339	Further, we noticed that over-production of Duc1, like overproduction of Opy1 (Snider et al., 2020), resulted in cells with off-centered septation (Fig. 5E,F), consistent with both of these proteins associating with PI(4,5)P2 and out-competing CR anchoring proteins for a limiting amount of PI(4,5)P2.
PMID:39239853	GO:0016328	Also, Opy1 and Its3 displayed localization along the cortex consistently throughout the cell cycle whereas Duc1 accumulated at different cortical sites depending on the cell-cycle stage (Fig. 1E). These results indicate that Duc1 may be proximal to Its3 and Opy1 at the PM only at certain times. || In scs2Δ scs22Δ cells, Duc1-mNG remained along the cell cortex, confirming its PM localization (Fig. 2A).
PMID:39239853	PBO:0114511	(comment: CHECK (mislocalized to division site).) As anticipated if these mutations successfully disrupted Duc1 association with Scs2 and Scs22, Duc1-Y374A,F375A-mNG localized at the division site (Fig. 4H).
PMID:39239853	PBO:0114510	Analysis of Duc1-mNG localization showed that, unlike in wild-type cells, Duc1- mNG localized at the septum in scs2-T39A,T40A scs22Δ cells (Fig. 4F).
PMID:39239853	PBO:0114510	In contrast to its exclusion from the division site in wild-type cells, Duc1- mNG localized along the septa in scs2Δ scs22Δ cells (Fig. 2A,B). This observation was confirmed by live-cell time-lapse imaging with CR and SPB markers (Fig. 2C). Thus, we conclude that Duc1 exclusion from the cell division site depends specifically on Scs2 and Scs22 and not ER-PM contact sites per se.
PMID:39239853	PBO:0114508	To dissect the contribution of each class of ER-PM contact to Duc1-mNG localization, we analyzed its distribution in hob2Δ, ltc2Δ, ist2Δ, and tcb1Δ tcb2Δ tcb3Δ strains. We found that Duc1-mNG was excluded from the cell division site in all four strains, as in wild-type cells (Fig. S2A).
PMID:39239853	PBO:0114509	The localizations of Scs2-mNG, Scs22-mNG and mCherry-AHDL all appeared unchanged in duc1Δ cells compared to wild-type cells (Figure S4B).
PMID:39239853	PBO:0114508	To dissect the contribution of each class of ER-PM contact to Duc1-mNG localization, we analyzed its distribution in hob2Δ, ltc2Δ, ist2Δ, and tcb1Δ tcb2Δ tcb3Δ strains. We found that Duc1-mNG was excluded from the cell division site in all four strains, as in wild-type cells (Fig. S2A).
PMID:39239853	PBO:0114507	check was plasma membrane /To dissect the contribution of each class of ER-PM contact to Duc1-mNG localization, we analyzed its distribution in hob2Δ, ltc2Δ, ist2Δ, and tcb1Δ tcb2Δ tcb3Δ strains. We found that Duc1-mNG was excluded from the cell division site in all four strains, as in wild-type cells (Fig. S2A).
PMID:39239853	PBO:0114508	We also examined if Scs2 or Scs22 alone was responsible for preventing Duc1 division site localization but, as in wild-type cells, Duc1- mNG was excluded from the cell division site in both single deletion strains (Fig. S2B).
PMID:39239853	PBO:0114508	We also examined if Scs2 or Scs22 alone was responsible for preventing Duc1 division site localization but, as in wild-type cells, Duc1- mNG was excluded from the cell division site in both single deletion strains (Fig. S2B).
PMID:39239853	PBO:0114517	The localizations of Scs2-mNG, Scs22-mNG and mCherry-AHDL all appeared unchanged in duc1Δ cells compared to wild-type cells (Figure S4B).
PMID:39239853	PBO:0114518	We detected no change in lateral cortex Efr3-mNG but a ~30% decrease in lateral cortex Its3-mNG in duc1Δ compared to wild-type cells (Fig 6G,H and Fig. S4C,D)
PMID:39239853	PBO:0114507	(comment: CHECK check was plasma menbrane/) To dissect the contribution of each class of ER-PM contact to Duc1-mNG localization, we analyzed its distribution in hob2Δ, ltc2Δ, ist2Δ, and tcb1Δ tcb2Δ tcb3Δ strains. We found that Duc1-mNG was excluded from the cell division site in all four strains, as in wild-type cells (Fig. S2A).
PMID:39239853	PBO:0114519	There was no change in Its3-mNG septum intensity in duc1Δ cells compared to wild-type, as expected (Fig. S4E).
PMID:39239853	GO:0032541	Live-cell imaging revealed that they all localized either uniformly or in a punctate pattern along the lateral cell cortex and, all but Ist2 lacked any detectable localization at the cell division site (Fig. 3A)
PMID:39239853	GO:0032541	Live-cell imaging revealed that they all localized either uniformly or in a punctate pattern along the lateral cell cortex and, all but Ist2 lacked any detectable localization at the cell division site (Fig. 3A)
PMID:39239853	GO:0032541	Live-cell imaging revealed that they all localized either uniformly or in a punctate pattern along the lateral cell cortex and, all but Ist2 lacked any detectable localization at the cell division site (Fig. 3A)
PMID:39239853	GO:0032541	Live-cell imaging revealed that they all localized either uniformly or in a punctate pattern along the lateral cell cortex and, all but Ist2 lacked any detectable localization at the cell division site (Fig. 3A)
PMID:39239853	GO:0032541	Live-cell imaging revealed that they all localized either uniformly or in a punctate pattern along the lateral cell cortex and, all but Ist2 lacked any detectable localization at the cell division site (Fig. 3A)
PMID:39239853	FYPO:0005289	However, a quantification of the ratio of short-to-long duc1Δ cells at septation demonstrated a significant fraction of duc1Δ cells divided asymmetrically (Fig. 6A,B). Wildtype cells formed a medial CR that slid in 1/13 cells examined, but duc1Δ cells formed a medial CR that slid along the cortex towards one cell end in 12/15 cells observed (Fig. 6C). Thus, Duc1 promotes proper CR anchoring.
PMID:39239853	FYPO:0006626	We confirmed a lack of change in lateral cortical PI(4,5)P2 signal but found that the PI(4,5)P2 signal was increased at the septum by ~20% in scs2Δ scs22Δ cells compared to wild-type (Fig. 7D-F).
PMID:39239853	PBO:0114516	Its3-mNG was increased at the septum in scs2Δ scs22Δ cells compared to wild-type cells by ~50% without a change in the lateral cortex levels (Fig. 7A-C).
PMID:39239853	PBO:0114515	We detected no change in lateral cortex Efr3-mNG but a ~30% decrease in lateral cortex Its3-mNG in duc1Δ compared to wild-type cells (Fig 6G,H and Fig. S4C,D)
PMID:39239853	FYPO:0006625	In contrast, lateral PM and septum PI(4,5)P2 levels, indicated by the GFP-2xPHPlc biosensor, were 36% and 48%, respectively, in duc1Δ compared to wild-type (Fig. 6D-F).
PMID:39239853	FYPO:0006629	There was no significant change in lateral cortex or septum PI4P levels, as determined by the GFP-P4CSidC biosensor (Fig. 6D-F).
PMID:39239853	PBO:0114514	(comment: CHECK (check was normal protein localization to plasma membrane)) We found that Duc1-mNG PM localization along the lateral cell cortex was diminished by ~25% in efr3Δ cells compared to wild-type (Fig. 5A,B).
PMID:39239853	PBO:0114513	Duc1-mNG levels were also reduced at the lateral PM in its3-1 cells at a semi-restrictive temperature compared to wild-type (Fig. 5A,B). These results are consistent with Duc1 requiring PM PI(4,5)P2 for its PM localization.
PMID:39239853	GO:0140268	Live-cell imaging revealed that they all localized either uniformly or in a punctate pattern along the lateral cell cortex and, all but Ist2 lacked any detectable localization at the cell division site (Fig. 3A)
PMID:39239853	GO:0140268	Live-cell imaging revealed that they all localized either uniformly or in a punctate pattern along the lateral cell cortex and, all but Ist2 lacked any detectable localization at the cell division site (Fig. 3A)
PMID:39289458	PBO:0114625	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	FYPO:0001940	Our results revealed a slight decrease in complex III enzyme activity in ∆shy1 cells compared to WT cells (Supplementary Fig. S5 online), suggesting that shy1 affects complex III in ways other than its assembly.
PMID:39289458	FYPO:0007624	The levels of supercomplexes III2IV2 and III2IV were found to be lower in ∆shy1 cells compared to WT cells, while the abundance of COA complexes increased (Fig. 7a), indicating that the formation of supercomplexes involving complex IV is influenced by deletion of shy1. In contrast, the abundance of III2 and V complexes was largely unchanged in ∆shy1 cells (Fig. 7a).
PMID:39289458	FYPO:0001164	Conversely, the growth reduction was marginal when cultured in glucose medium, which supports fermentative growth and thus necessitates moderate respiratory activity43.
PMID:39289458	PBO:0093796	The cell growth of the ∆shy1 mutant exhibited a notable decline when cultivated in glycerol medium in comparison to the wild-type (WT) strain (Fig. 5a).
PMID:39289458	GO:0097250	The levels of supercomplexes III2IV2 and III2IV were found to be lower in ∆shy1 cells compared to WT cells, while the abundance of COA complexes increased (Fig. 7a), indicating that the formation of supercomplexes involving complex IV is influenced by deletion of shy1. In contrast, the abundance of III2 and V complexes was largely unchanged in ∆shy1 cells (Fig. 7a).
PMID:39289458	GO:0005743	Collectively, our findings strongly indicate that Shy1 is affixed to the mitochondrial inner membrane./Fig. 6. Shy1 is localized in the mitochondrial inner membrane.
PMID:39289458	PBO:0114634	Our results showed that the expression of Cob1, Cox1, Cox2, Cox3, and Atp6 were greatly reduced in ∆shy1 cells (Fig. 5d).
PMID:39289458	PBO:0114633	Our results showed that the expression of Cob1, Cox1, Cox2, Cox3, and Atp6 were greatly reduced in ∆shy1 cells (Fig. 5d).
PMID:39289458	PBO:0114632	Our results showed that the expression of Cob1, Cox1, Cox2, Cox3, and Atp6 were greatly reduced in ∆shy1 cells (Fig. 5d).
PMID:39289458	PBO:0114622	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	PBO:0114623	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	PBO:0114624	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	PBO:0114630	Our results showed that the expression of Cob1, Cox1, Cox2, Cox3, and Atp6 were greatly reduced in ∆shy1 cells (Fig. 5d).
PMID:39289458	PBO:0114626	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	PBO:0114627	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	PBO:0114631	Our results showed that the expression of Cob1, Cox1, Cox2, Cox3, and Atp6 were greatly reduced in ∆shy1 cells (Fig. 5d).
PMID:39289458	PBO:0114628	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	PBO:0114629	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	PBO:0114654	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	PBO:0114655	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	PBO:0114644	As shown in Fig. 5c, the mtDNA copy number is slightly increased in ∆shy1 cells compared to that of in WT strain, indicating the observed reduction in mitochondrial RNA is not attributed to a decrease in mtDNA levels.
PMID:39330407	PBO:0117259	We acquired timelapse micrographs of ∆ain1 ∆myp2 cells expressing mEGFP-Myo2p to measure the duration of clumping when the onset of constriction is delayed. Forty-four percent of ∆ain1 ∆myp2 cells (n = 87 cells) showed the ring clumping phenotype, similar to ∆ain1 cells (Figure 1D).
PMID:39330407	FYPO:0000729	We measured the duration of clumps in ∆ain1 ∆myp2 cells and found that as expected, clumps last ~7 min longer in those cells (Figure 1E).
PMID:39330407	PBO:0117260	"node clumping, Myo2p marker Figure 1A-D ""The clumping phenotype suggests that nodes aggregate into clumps during contractile ring assembly in the absence of Ain1p."""
PMID:39330407	FYPO:0004653	The onset of contractile ring constriction is delayed by ~10 min in ∆ain1 ∆myp2 cells.
PMID:39330407	GO:0120104	3.4. Myo51 Localizes to the Inner Layer of the Contractile Ring during Constriction
PMID:39330407	PBO:0117257	During our investigation, we noticed that contractile ring shedding appeared premature and exaggerated in ∆ain1 ∆myo51 cells when compared to wild-type cells. In wild-type cells expressing mEGFP-Myo2p, shedding begins when the ring is 62% constricted (n = 38 cells), and the fragments that shed from the constricting contractile ring extend out along the septum without reaching the full width of the cell (Figures 2A and 3A-C)
PMID:39330407	PBO:0117258	(Figure 3) Contractile ring shedding is exaggerated and premature in ∆ain1 ∆myo51 cells.
PMID:39330407	PBO:0117258	(Figure 3) Contractile ring shedding is exaggerated and premature in ∆ain1 ∆myo51 cells.
PMID:39333464	GO:0060212	uridylation prevents excessive deadenylation which in turn protects mRNA from 3’ to 5’ exonucleolitic decay.
PMID:39333464	PBO:0116262	(Fig. 5A)
PMID:39333464	PBO:0093560	(Fig. 5C)
PMID:39333464	PBO:0093559	(Fig. 5C)
PMID:39333464	PBO:0093561	(Fig. 5C)
PMID:39333464	PBO:0093561	(Fig. 5C)
PMID:39333464	PBO:0116261	(Fig. 5B)
PMID:39333464	PBO:0116258	(Fig. 5B)
PMID:39333464	PBO:0116259	(Fig. 5B)
PMID:39333464	FYPO:0001357	(Fig. 5C)
PMID:39333464	FYPO:0001357	(Fig. 5C)
PMID:39333464	FYPO:0001357	(Fig. 5C)
PMID:39333464	PBO:0116260	(Fig. 4A)
PMID:39333464	PBO:0116258	(Fig. 4F)
PMID:39333464	PBO:0116256	(Fig. 4F)
PMID:39333464	PBO:0116258	(Fig. 4F)
PMID:39333464	PBO:0116256	(Fig. 4F)
PMID:39333464	PBO:0093559	(Fig. 4C, 4D)
PMID:39333464	PBO:0093559	(Fig. 4C, 4D)
PMID:39333464	PBO:0093559	(Fig. 4C, 4D)
PMID:39333464	PBO:0093559	(Fig. 4C, 4D)
PMID:39333464	PBO:0093561	(Fig. 4C, 4D)
PMID:39333464	PBO:0093561	(Fig. 4C, 4D)
PMID:39333464	PBO:0116259	(Fig. 4B)
PMID:39333464	PBO:0116259	(Fig. 4B)
PMID:39333464	PBO:0116258	(Fig. 4B, 4F)
PMID:39333464	PBO:0116257	(Fig. 4A)
PMID:39333464	PBO:0116256	(Fig. 4A, 4F)
PMID:39333464	FYPO:0001357	(Fig. S5B)
PMID:39333464	FYPO:0001357	(Fig. S5B)
PMID:39333464	FYPO:0001357	(Fig. S5B)
PMID:39333464	FYPO:0008339	(Fig. 3C, Fig. S4B)
PMID:39333464	FYPO:0008339	(Fig. 3C, Fig. S4B)
PMID:39333464	PBO:0116255	(Fig. 3C, Fig. S4)
PMID:39333464	FYPO:0008336	(Fig. 3A and B and Fig. S4B)
PMID:39333464	FYPO:0008336	(Fig. 3A and B and Fig. S4B)
PMID:39333464	PBO:0116254	(Fig. 3A and B and Fig. S4)
PMID:39333464	GO:1990074	(comment: CHECK ******uridylation dependent 3'-5' mRNA decay*******.) (Fig. 5)
PMID:39333464	GO:0036450	Under standard conditions, uridylation of short mRNA poly(A) tails by Cid1 helps to direct mRNA toward the 5’ to 3’ decay pathway by enhancing Lsm1-7 complex binding and protecting the 3’-end from extensive deadenylation.
PMID:39333464	PBO:0116253	mRNAs with shortened poly(A) tails are uridylated by Cid1, while completely deadenylated mRNAs are subjected to oligouridylation by Cid16. Cid1- mediated uridylation routes decay towards the 5’ to 3’ pathway, while Cid16-mediated oligouridylation facilitates 3’ to 5’ degradation.
PMID:39333464	GO:0000957	The highest number of oligo(U) tailed reads were detected for mitochondrial transcripts (Supplementary Fig. 4a), therefore, oligouridylation of mtRNA seems to be a main function of Cid16.
PMID:39333464	PBO:0116265	The highest number of oligo(U) tailed reads were detected for mitochondrial transcripts (Supplementary Fig. 4a), therefore, oligouridylation of mtRNA seems to be a main function of Cid16.
PMID:39333464	GO:1990074	(comment: CHECK ******uridylation dependent 3'-5' mRNA decay******) (Fig. 5)
PMID:39333464	FYPO:0002930	While the global tail profile did not change in the Δcid16 mutant, we noticed an increase in the fraction of short-tailed reads in Δcid1 and double deletion strains (Fig. 3e).
PMID:39333464	PBO:0116264	mRNAs with shortened poly(A) tails are uridylated by Cid1, while completely deadenylated mRNAs are subjected to oligouridylation by Cid16. Cid1- mediated uridylation routes decay towards the 5’ to 3’ pathway, while Cid16-mediated oligouridylation facilitates 3’ to 5’ degradation.
PMID:39333464	PBO:0116263	(Fig. 5A)
PMID:39333500	PBO:0094949	(Fig. 2H)
PMID:39333500	PBO:0093559	(Fig. 2H)
PMID:39333500	PBO:0114720	(Fig. 2B)
PMID:39333500	PBO:0114719	(Fig. 2E and F)
PMID:39333500	PBO:0114718	(Fig. 2E and F)
PMID:39333500	PBO:0114717	(Fig. 2B)
PMID:39333500	PBO:0114716	(Fig. 2B)
PMID:39333500	PBO:0098563	(Fig. 4C)
PMID:39333500	FYPO:0002059	(Fig. 2G)
PMID:39333500	PBO:0114715	(Fig. 2E)
PMID:39358553	FYPO:0008324	(Fig. 4E and F)
PMID:39358553	FYPO:0004706	(Fig. 4A and C)
PMID:39358553	GO:0005737	This analysis revealed that aal1 RNAs predominantly localize in the cytoplasm in multiple foci (Fig. 2B).
PMID:39358553	PBO:0095634	(Fig. EV2)
PMID:39358553	FYPO:0002062	(Fig. 1E)
PMID:39358553	PBO:0095685	(Fig. 1D)
PMID:39358553	PBO:0100665	(Fig. 1C)
PMID:39358553	PBO:0114900	(Fig. 1C)
PMID:39358553	PBO:0093531	(Fig. 1)
PMID:39358553	PBO:0114907	(Fig. 5)
PMID:39358553	PBO:0114905	(Fig. 5D)
PMID:39358553	FYPO:0008325	(Fig. 4E and F)
PMID:39358553	FYPO:0006036	(Fig. 4B and C)
PMID:39358553	PBO:0114903	(Fig. 1A)
PMID:39358553	PBO:0114904	(Fig. 1A)
PMID:39358553	PBO:0114904	(Fig. 1A)
PMID:39358553	PBO:0114903	(Fig. 1A)
PMID:39358553	PBO:0114903	(Fig. 1A)
PMID:39358553	PBO:0114903	(Fig. 1A)
PMID:39358553	PBO:0114903	(Fig. 1A)
PMID:39358553	PBO:0114902	(Fig. 1A)
PMID:39358553	PBO:0114902	(Fig. 1A)
PMID:39358553	PBO:0114901	(Fig. 4G)
PMID:39358553	PBO:0100665	(Fig. 5F)
PMID:39358553	PBO:0114900	(Fig. 5F)
PMID:39358553	PBO:0114906	(Fig. 5D)
PMID:39379376	FYPO:0008333	We then examined whether cytosolic ribosomes still tethered to mitochondria in Δdnm1 cells after prolonged glucose depletion. In situ cryo-ET imaging of Δdnm1 cells revealed that mitochondria remained elongated throughout glucose depletion (Fig. 4b). However, this morphological change did not prevent the tethering of cytosolic ribosomes to the OMM, with 98% of the imaged mitochondria (n = 100) being fully decorated with ribosomes at day 7 of glucose depletion (Fig. 4b, c, Supplementary Fig. 10 and Supplementary Movie 2).
PMID:39379376	FYPO:0009007	While Δcpc2 cells did not display discernible growth defects under nutrient-rich conditions, significant growth impairments were evident when these cells were cultivated in defined EMM media supplemented with either 2% or 0.5% glucose concentrations.
PMID:39379376	FYPO:0008334	We then used in situ cryo-ET to assess whether ribosomal tethering to mitochondria was affected in the Δcpc2 strain. The tomograms showed fragmented circular mitochondria, as observed in WT cells, while no ribosome tethering was observed after 7 days of cells growing at low glucose concentrations (Fig. 5c, d, Supplementary Fig. 10 and Supplementary Movie 3).
PMID:39387272	PBO:0093560	(Fig. S1C)
PMID:39387272	PBO:0093557	(Fig. S1C)
PMID:39387272	PBO:0093558	(Fig. S1C)
PMID:39387272	PBO:0093558	(Fig. S1C)
PMID:39387272	PBO:0093558	(Fig. S1C)
PMID:39387272	PBO:0093558	(Fig. S1C)
PMID:39387272	PBO:0093558	(Fig. S1C)
PMID:39387272	FYPO:0000674	(Fig. S1C)
PMID:39387272	FYPO:0000674	(Fig. S1C)
PMID:39387272	FYPO:0000674	(Fig. S1C)
PMID:39387272	PBO:0094205	(Fig. S1B)
PMID:39387272	PBO:0094205	(Fig. S1B)
PMID:39387272	FYPO:0001357	(Fig. S2B)
PMID:39387272	PBO:0093614	(Fig. S2B)
PMID:39387272	PBO:0093580	(Fig. S2B)
PMID:39387272	PBO:0093580	(Fig. S2B)
PMID:39387272	FYPO:0000957	(Fig. 2E)
PMID:39387272	PBO:0093616	(Fig. 2E)
PMID:39387272	PBO:0093613	(Fig. 2E)
PMID:39387272	PBO:0093614	(Fig. 2E)
PMID:39387272	PBO:0093613	(Fig. 2E)
PMID:39387272	PBO:0093615	(Fig. 2E)
PMID:39387272	PBO:0093581	(Fig. 2E)
PMID:39387272	PBO:0093579	(Fig. 2E)
PMID:39387272	PBO:0093580	(Fig. 2E)
PMID:39387272	PBO:0093560	(Fig. 2E)
PMID:39387272	PBO:0093579	(Fig. 2E)
PMID:39387272	PBO:0116423	(Fig. 2B)
PMID:39387272	PBO:0094205	(Fig. 2B)
PMID:39387272	PBO:0116422	(Fig. 1A)
PMID:39387272	PBO:0116422	(Fig. 1A)
PMID:39387272	PBO:0099929	(Fig. S1D)
PMID:39387272	PBO:0098709	(Fig. S1D)
PMID:39387272	PBO:0098709	(Fig. S1D)
PMID:39387272	PBO:0098709	(Fig. S1D)
PMID:39387272	PBO:0098709	(Fig. S1D)
PMID:39387272	PBO:0094205	(Fig. S1D)
PMID:39387272	PBO:0099929	(Fig. S1B)
PMID:39387272	PBO:0099929	(Fig. S1B)
PMID:39387272	PBO:0098709	(Fig. S1B)
PMID:39387272	PBO:0098709	(Fig. S1B)
PMID:39387272	PBO:0116426	(Fig. 5H)
PMID:39387272	PBO:0116426	(Fig. 5H)
PMID:39387272	PBO:0116428	(Fig. 5G)
PMID:39387272	PBO:0116427	(Fig. 5G)
PMID:39387272	PBO:0093579	(Fig. 5D)
PMID:39387272	PBO:0093579	(Fig. 5D)
PMID:39387272	PBO:0093559	(Fig. 5E)
PMID:39387272	PBO:0093559	(Fig. 5E)
PMID:39387272	PBO:0105329	These data strongly suggest that S60 is an additional Hhp1 and Hhp2 phosphorylation site, and that S60, S62, S75, and S87 are the primary sites on Arp8 that are targeted by Hhp1 and Hhp2.
PMID:39387272	PBO:0105329	These data strongly suggest that S60 is an additional Hhp1 and Hhp2 phosphorylation site, and that S60, S62, S75, and S87 are the primary sites on Arp8 that are targeted by Hhp1 and Hhp2.
PMID:39387272	PBO:0105329	These data strongly suggest that S60 is an additional Hhp1 and Hhp2 phosphorylation site, and that S60, S62, S75, and S87 are the primary sites on Arp8 that are targeted by Hhp1 and Hhp2.
PMID:39387272	PBO:0105329	These data strongly suggest that S60 is an additional Hhp1 and Hhp2 phosphorylation site, and that S60, S62, S75, and S87 are the primary sites on Arp8 that are targeted by Hhp1 and Hhp2.
PMID:39387272	GO:0035861	Hhp1 and Hhp2 localize diffusely across the nucleus and cytoplasm with a concentration at SPBs,38 but they did not co-localize with Rad52-GFP foci, even when genotoxic stress was induced (Supplementary material, Figure S2D).
PMID:39387272	GO:0035861	Hhp1 and Hhp2 localize diffusely across the nucleus and cytoplasm with a concentration at SPBs,38 but they did not co-localize with Rad52-GFP foci, even when genotoxic stress was induced (Supplementary material, Figure S2D).
PMID:39387272	PBO:0116426	(Fig. S2C)
PMID:39387272	PBO:0103021	(Fig. 4B)
PMID:39387272	PBO:0116425	(Fig. 4B)
PMID:39387272	PBO:0098835	(Fig. 4A)
PMID:39387272	PBO:0098835	(Fig. 4A)
PMID:39387272	PBO:0098836	(Fig. 4A)
PMID:39387272	PBO:0116424	(Fig. 3B)
PMID:39387272	PBO:0093557	(Fig. S2B)
PMID:39387272	PBO:0093557	(Fig. S2B)
PMID:39387272	FYPO:0001690	(Fig. S2B)
PMID:39387272	FYPO:0001357	(Fig. S2B)
PMID:39387272	PBO:0116421	(Fig. 1A)
PMID:39387272	PBO:0093559	(Fig. 2E)
PMID:39387272	PBO:0093580	(Fig. 2E)
PMID:39387272	PBO:0093613	(Fig. 2E)
PMID:39387272	PBO:0093616	(Fig. 2E)
PMID:39387272	PBO:0093580	(Fig. S2B)
PMID:39387272	PBO:0093613	(Fig. S2B)
PMID:39387272	PBO:0093580	(Fig. 2E)
PMID:39387272	PBO:0093613	(Fig. 2E)
PMID:39387272	PBO:0093580	(Fig. S2B)
PMID:39387272	PBO:0093558	(Fig. 5E)
PMID:39387272	PBO:0093558	(Fig. 5E)
PMID:39387272	FYPO:0001357	(Fig. S1C)
PMID:39387272	FYPO:0001357	(Fig. S1C)
PMID:39387272	FYPO:0001357	(Fig. S1C)
PMID:39387272	FYPO:0001357	(Fig. S1C)
PMID:39387272	PBO:0093561	(Fig. S1C)
PMID:39387272	PBO:0093561	(Fig. S1C)
PMID:39387272	PBO:0093559	(Fig. S1C)
PMID:39387272	PBO:0093559	(Fig. S1C)
PMID:39471327	FYPO:0001475	In ppc89-3 cells at the restrictive temperature, we noticed an increased proportion 14 of cells displaying 2 or 4 Ppc89-3-mNG and Sad1-mCherry foci, indicative of cytokinesis 15 failure (Figure 1G,H). In contrast, ppc89-4 cells displayed 3, 4, or ≥5 Ppc89-4-mNG and 16 Sad1-mCherry foci (Figure 1G,H), indicating that the integrity of the SPB as a whole is 17 disrupted in ppc89-4 cells whereas it appears to remain intact in ppc89-3 cells.
PMID:39471327	FYPO:0001475	Interestingly we found that the additional foci of Ppc89-4, 11 observed in 169/280 cells that progressed through mitosis during the movies, always 12 formed during anaphase by splitting off from one of the two SPBs (Figure 7A). By 13 determining the intensity of the two SPBs before and after foci appeared, we confirmed 14 that the fragments originated from one SPB because the fluorescence intensity of that 15 SPB always diminished relative to the second SPB (Figure 7B).
PMID:39471327	PBO:0114839	At 25°C, Sid4-GFP SPB intensity was reduced by 4 approximately 30% in ppc89-3 and 60% in ppc89-4 compared to wild-type (Figures 2A 5 and S2A). At 36°C, Sid4-GFP SPB intensity was further reduced by ~90% in ppc89-3 6 and ppc89-4 compared to wild-type (Figure 2A,B). These results indicate that the Sid4- 7 Ppc89 interaction is disrupted in both ppc89-3 and ppc89-4 cells at restrictive 8 temperatu re.
PMID:39471327	PBO:0114839	At 25°C, Sid4-GFP SPB intensity was reduced by 4 approximately 30% in ppc89-3 and 60% in ppc89-4 compared to wild-type (Figures 2A 5 and S2A). At 36°C, Sid4-GFP SPB intensity was further reduced by ~90% in ppc89-3 6 and ppc89-4 compared to wild-type (Figure 2A,B). These results indicate that the Sid4- 7 Ppc89 interaction is disrupted in both ppc89-3 and ppc89-4 cells at restrictive 8 temperatu re.
PMID:39471327	PBO:0114104	Both Ppc89(1-707)-mNG and Sid4-RFP 8 localized to the SPB with comparable intensity to wild-type at both 25 ̊C and 36°C 9 (Figure 3D,E).
PMID:39471327	PBO:0114840	Both Ppc89(1-707)-mNG and Sid4-RFP 8 localized to the SPB with comparable intensity to wild-type at both 25 ̊C and 36°C 9 (Figure 3D,E).
PMID:39471327	PBO:0114841	As expected, Dma1- 22 mNG, Cdc11-GFP and Mto1-mNG were lost from SPBs in ppc89-3 and ppc89-4 cells at 23 restrictive temperature, but Mto1-mNG localized normally to SPBs in ppc89(1-707) cells (Figures 4A-G; S2B and C)
PMID:39471327	PBO:0114841	As expected, Dma1- 22 mNG, Cdc11-GFP and Mto1-mNG were lost from SPBs in ppc89-3 and ppc89-4 cells at 23 restrictive temperature, but Mto1-mNG localized normally to SPBs in ppc89(1-707) cells (Figures 4A-G; S2B and C)
PMID:39471327	PBO:0114842	As expected, Dma1- 22 mNG, Cdc11-GFP and Mto1-mNG were lost from SPBs in ppc89-3 and ppc89-4 cells at 23 restrictive temperature, but Mto1-mNG localized normally to SPBs in ppc89(1-707) cells (Figures 4A-G; S2B and C)
PMID:39471327	PBO:0114842	As expected, Dma1- 22 mNG, Cdc11-GFP and Mto1-mNG were lost from SPBs in ppc89-3 and ppc89-4 cells at 23 restrictive temperature, but Mto1-mNG localized normally to SPBs in ppc89(1-707) cells (Figures 4A-G; S2B and C)
PMID:39471327	PBO:0114844	As expected, Dma1- 22 mNG, Cdc11-GFP and Mto1-mNG were lost from SPBs in ppc89-3 and ppc89-4 cells at 23 restrictive temperature, but Mto1-mNG localized normally to SPBs in ppc89(1-707) cells (Figures 4A-G; S2B and C)
PMID:39471327	PBO:0114844	As expected, Dma1- 22 mNG, Cdc11-GFP and Mto1-mNG were lost from SPBs in ppc89-3 and ppc89-4 cells at 23 restrictive temperature, but Mto1-mNG localized normally to SPBs in ppc89(1-707) cells (Figures 4A-G; S2B and C)
PMID:39471327	FYPO:0002150	We found 22 that ppc89-3 was synthetically lethal with sid4-SA1 and synthetically sick with spg1-106, 23 mob1-R4, and plo1-25 (Figure S1B,C).
PMID:39471327	FYPO:0002150	ppc89-4 was also synthetically lethal with sid4- 12 Downloaded from https://academic.oup.com/g3journal/advance-article/doi/10.1093/g3journal/jkae249/7848890 by guest on 01 November 2024 1 SA1 (Figure S1C)
PMID:39471327	FYPO:0002150	ppc89-4 was also synthetically lethal with sid4- 12 Downloaded from https://academic.oup.com/g3journal/advance-article/doi/10.1093/g3journal/jkae249/7848890 by guest on 01 November 2024 1 SA1 (Figure S1C)
PMID:39471327	FYPO:0000082	We found 22 that ppc89-3 was synthetically lethal with sid4-SA1 and synthetically sick with spg1-106, 23 mob1-R4, and plo1-25 (Figure S1B,C).
PMID:39471327	FYPO:0000082	We found 22 that ppc89-3 was synthetically lethal with sid4-SA1 and synthetically sick with spg1-106, 23 mob1-R4, and plo1-25 (Figure S1B,C).
PMID:39471327	FYPO:0000082	We found 22 that ppc89-3 was synthetically lethal with sid4-SA1 and synthetically sick with spg1-106, 23 mob1-R4, and plo1-25 (Figure S1B,C).
PMID:39471327	FYPO:0000082	We found 22 that ppc89-3 was synthetically lethal with sid4-SA1 and synthetically sick with spg1-106, 23 mob1-R4, and plo1-25 (Figure S1B,C).
PMID:39471327	FYPO:0002150	We found 22 that ppc89-3 was synthetically lethal with sid4-SA1 and synthetically sick with spg1-106, 23 mob1-R4, and plo1-25 (Figure S1B,C).
PMID:39471327	FYPO:0000082	We found 22 that ppc89-3 was synthetically lethal with sid4-SA1 and synthetically sick with spg1-106, 23 mob1-R4, and plo1-25 (Figure S1B,C).
PMID:39471327	FYPO:0000082	We found 22 that ppc89-3 was synthetically lethal with sid4-SA1 and synthetically sick with spg1-106, 23 mob1-R4, and plo1-25 (Figure S1B,C).
PMID:39471327	FYPO:0000082	ppc89-2, ppc89-3 and ppc89-4 grow 19 similarly to wild-type at 25°C but do not form colonies at 36°C (Figure 1B
PMID:39471327	FYPO:0000082	ppc89-2, ppc89-3 and ppc89-4 grow 19 similarly to wild-type at 25°C but do not form colonies at 36°C (Figure 1B
PMID:39471327	PBO:0093558	ppc89-2, ppc89-3 and ppc89-4 grow 19 similarly to wild-type at 25°C but do not form colonies at 36°C (Figure 1B
PMID:39471327	PBO:0093556	ppc89(1-707)-mNG cells were 7 viable but temperature-sensitive (Figure 3C).
PMID:39471327	PBO:0093556	ppc89-L756P,I770V was 3 temperature-sensitive and accumulated cells with one nucleus and a septum (Figure 4 6B-D), reminiscent of what we observed in ppc89-4 cells
PMID:39471327	FYPO:0000647	At 36°C, ppc89-2 and ppc89-3 displayed an increased proportion of binucleate cells with “kissing” nuclei in which nuclei return to the cell center after a failed cytokiness as well as cell lysis (Figure 1C,D)
PMID:39471327	FYPO:0000647	At 36°C, ppc89-2 and ppc89-3 displayed an increased proportion of binucleate cells with “kissing” nuclei in which nuclei return to the cell center after a failed cytokiness as well as cell lysis (Figure 1C,D)
PMID:39471327	PBO:0114837	. A 2 portion of ppc89-4 cells at 36°C showed an additional abnormal phenotype - cells with 3 a septum but only one nucleus (Figure 1C,D).
PMID:39471327	FYPO:0007652	Moreover, we found that 5 ppc89(1-707)-mNG cells accumulated mononucleated, septated cells and anucleate cell 6 compartments (Figure 6C,D) as well as multiple Ppc89 foci (Figure 6E and S4B).
PMID:39471327	FYPO:0007652	ppc89-L756P,I770V was 3 temperature-sensitive and accumulated cells with one nucleus and a septum (Figure 4 6B-D), reminiscent of what we observed in ppc89-4 cells| Moreover, we found that 5 ppc89(1-707)-mNG cells accumulated mononucleated, septated cells and anucleate cell 6 compartments (Figure 6C,D) as well as multiple Ppc89 foci (Figure 6E and S4B).
PMID:39471327	FYPO:0003245	At 36°C, ppc89-2 and ppc89-3 displayed an increased proportion of binucleate cells with “kissing” nuclei in which nuclei return to the cell center after a failed cytokiness as well as cell lysis (Figure 1C,D)
PMID:39471327	PBO:0114845	we also observed a reduction 3 in Mto2-mNG SPB signal at 36 ̊C in ppc89-3 and ppc89-4 compared to wild-type (Figure 4 S2D,E).
PMID:39471327	PBO:0114845	we also observed a reduction 3 in Mto2-mNG SPB signal at 36 ̊C in ppc89-3 and ppc89-4 compared to wild-type (Figure 4 S2D,E).
PMID:39471327	PBO:0114846	Neither Sfi1-mCherry nor 7 Sad1-mCherry signal were reduced in ppc89-3 or ppc89-4 cells (Figure S3A,B).
PMID:39471327	PBO:0114846	Neither Sfi1-mCherry nor 7 Sad1-mCherry signal were reduced in ppc89-3 or ppc89-4 cells (Figure S3A,B).
PMID:39471327	PBO:0114847	Pcp1 showed ~50% 9 reduction in pcp89-4 cells (Figure S3C)
PMID:39471327	FYPO:0000674	... so we tested whether tethering Sid4 to 23 Pcp1-GFP would rescue ppc89-3 and if so, ppc89-4 as well. ppc89-3 was rescued when Sid4 was tethered to Pcp1-GFP, as it had been when tethered to Ppc89-3 directly 2 (Figure S3D)
PMID:39471327	FYPO:0003245	At 36°C, ppc89-2 and ppc89-3 displayed an increased proportion of binucleate cells with “kissing” nuclei in which nuclei return to the cell center after a failed cytokinesis as well as cell lysis (Figure 1C,D)
PMID:39471327	PBO:0093557	Can grow at 32°C but not at 36°C | Sid4 tethered to 4 the SPB via Pcp1-GFP did not rescue growth of ppc89-4 cells at 36°C but the ppc89-4 5 pcp1-GFP sid4-mCherry strain grew at 32°C, and imaging confirmed that Sid4-GBP- 6 mCherry but not Sid4-mCherry was present at the SPB at 36 ̊C (Figures 5B and S4A).
PMID:39471327	PBO:0114848	The addition of the tagged sid4 and pcp1 alleles 13 exacerbated the cell growth (Figures 5B and S3D) and cell division defects of the ppc89 14 ts alleles (Figures 1C,D and 5C,D) In contrast, ppc89-4 cells with Sid4 tethered to the SPB displayed a significant 17 percentage of uninucleate cells with an off-center septum and also multiple Ppc89-4 foci 18 (Figures 5C,D and S4).
PMID:39471327	FYPO:0007742	We also determined 16 that the rarer off-center septum phenotype (9 of 280 cells) arose because a second 17 cytokinetic ring formed at the new cell end of one daughter cell after its birth (Figure 18 7C). In these cells, the cytokinetic ring appeared not to fully disassemble and one 19 daughter inherited this cortical material. Then, a second cytokinetic ring formed at 20 variable times relative to completion of the previous division where the first cytokinetic 21 ring remnants were located (Figure 7C).
PMID:39471327	GO:1905047	(Figure 7)
PMID:39471327	PBO:0114104	Ppc89-3-mNG localized to the 10 SPB at both permissive and restrictive temperatures similarly to Ppc89-mNG (Figures 11 1E, F and S1A).
PMID:39471327	PBO:0114838	In contrast, Ppc89-4-mNG showed a ~50% reduction in SPB 12 fluorescence intensity at both temperatures compared to wild-type (Figures 1E, F and 13 S1A).
PMID:39473973	PBO:0093558	(Fig. S3H)
PMID:39473973	FYPO:0004545	(Fig. 2D)
PMID:39473973	PBO:0119597	(Fig. S2E)
PMID:39473973	PBO:0093558	(Fig. S2C)
PMID:39473973	PBO:0119598	(Fig. S4A)
PMID:39473973	PBO:0119596	(Fig. 4A)
PMID:39473973	FYPO:0005382	(Fig. 3A)
PMID:39473973	PBO:0093558	(Fig. S3H)
PMID:39473973	PBO:0093558	(Fig. S4B)
PMID:39473973	PBO:0093558	(Fig. S4B)
PMID:39473973	GO:0080129	The increased proteasome activity correlates with the upregulation of the 20S CP assembly chaperone Ump1 and with an increase in proteasome assembly. Ump1 inactivation compromises 20S proteasome assembly, resulting in a drop in mature 26S/30S proteasomes.
PMID:39473973	PBO:0092185	(Fig. 1D)
PMID:39473973	PBO:0119584	(Fig. 1F)
PMID:39473973	PBO:0093558	(Fig. 2A and B)
PMID:39473973	PBO:0119585	(Fig. 5A)
PMID:39473973	PBO:0119586	(Fig. 4B)
PMID:39473973	PBO:0093558	(Fig. S3H)
PMID:39473973	PBO:0093558	(Fig. S3H)
PMID:39473973	PBO:0119587	(Fig. 4C and Fig. S4A)
PMID:39473973	PBO:0119588	(Fig. S3B)
PMID:39473973	PBO:0119589	(Fig. 4D)
PMID:39473973	PBO:0119589	(Fig. 4E)
PMID:39473973	PBO:0119586	(Fig. 5B)
PMID:39473973	PBO:0119586	(Fig. 5B)
PMID:39473973	PBO:0119590	(Fig. 2E)
PMID:39473973	PBO:0119591	(Fig. 2G)
PMID:39473973	PBO:0119586	(Fig. 5B)
PMID:39473973	PBO:0119586	(Fig. 5B)
PMID:39473973	PBO:0119586	(Fig. 5B)
PMID:39473973	PBO:0119591	(Fig. 5A)
PMID:39473973	PBO:0119592	(Fig. 5A)
PMID:39473973	FYPO:0000021	(Fig. S2A)
PMID:39473973	PBO:0093561	(Fig. S2B and C)
PMID:39473973	FYPO:0002774	(Fig. S2G)
PMID:39473973	PBO:0119588	(Fig. S3D)
PMID:39473973	PBO:0119588	(Fig. S3D)
PMID:39473973	PBO:0119593	(Fig. S3F)
PMID:39473973	PBO:0104699	(Fig. S3E)
PMID:39473973	PBO:0119594	(Fig. S3E)
PMID:39473973	PBO:0119589	(Fig. S3G)
PMID:39473973	PBO:0119589	(Fig. S3G)
PMID:39473973	PBO:0119595	(Fig. S4A)
PMID:39473973	PBO:0119595	(Fig. S4A)
PMID:39473973	PBO:0119595	(Fig. S4A)
PMID:39473973	PBO:0119595	(Fig. S4A)
PMID:39473973	PBO:0119598	(Fig. S4A)
PMID:39473973	FYPO:0004545	(Fig. 2)
PMID:39476757	PBO:0114983	(Table S1)
PMID:39476757	PBO:0114990	(Table S1)
PMID:39476757	PBO:0114989	(Table S1)
PMID:39476757	PBO:0114988	(Table S1)
PMID:39476757	PBO:0114987	(Table S1)
PMID:39476757	PBO:0114986	(Table S1)
PMID:39476757	PBO:0114985	(Table S1)
PMID:39476757	PBO:0114984	(Table S1)
PMID:39476757	PBO:0114982	(Table S1)
PMID:39476757	PBO:0114981	(Table S1)
PMID:39476757	PBO:0114980	(Table S1)
PMID:39476757	PBO:0114979	(Table S1)
PMID:39476757	PBO:0114978	(Table S1)
PMID:39476757	PBO:0114977	(Table S1)
PMID:39476757	PBO:0114976	(Table S1)
PMID:39476757	PBO:0114975	(Table S1)
PMID:39476757	PBO:0114974	(Table S1)
PMID:39476757	PBO:0114973	(Table S1)
PMID:39476757	PBO:0114972	(Table S1)
PMID:39476757	PBO:0114971	(Table S1)
PMID:39476757	PBO:0114970	(Table S1)
PMID:39476757	PBO:0114969	(Table S1)
PMID:39476757	PBO:0114968	(Table S1)
PMID:39476757	PBO:0114967	(Table S1)
PMID:39476757	PBO:0114966	(Table S1)
PMID:39476757	PBO:0114965	(Table S1)
PMID:39476757	PBO:0114964	(Table S1)
PMID:39476757	PBO:0114963	(Table S1)
PMID:39476757	PBO:0093561	(Fig. 1D, E and F)
PMID:39476757	PBO:0093556	(Fig. 1B)
PMID:39476757	FYPO:0001357	(Fig. 1B and E)
PMID:39476757	FYPO:0002141	(Fig. 1B)
PMID:39477503	FYPO:0005547	1 showed that the signal peptide and the transmembrane including DUF3844 domain were 2 essential for this function (Fig. 4A).
PMID:39477503	FYPO:0000080	Growth of the vps3844Δ strain was significantly inhibited at low temperature (Fig. 2B).
PMID:39477503	FYPO:0005547	To confirm that SPBC1709.03 is a VPS gene, extracellular leakage of CPY was assessed 17 by colony blot assay (Fig. 1C). Relative to wild type (WT), the SPBC1709.03 deletion strain 18 showed higher chemiluminescence intensity of CPY, indicating an increased occurrence of 19 CPY mis-sorting to the cell surface.
PMID:39477503	FYPO:0001423	1 showed that the signal peptide and the transmembrane including DUF3844 domain were 2 essential for this function (Fig. 4A).
PMID:39477503	FYPO:0001423	1 showed that the signal peptide and the transmembrane including DUF3844 domain were 2 essential for this function (Fig. 4A).
PMID:39477503	PBO:0114883	Although the Vps3844 protein is important for the transport of 26 CPY into the vacuole, Isp6-GFP and Psp3-GFP were found to localize in the vacuolar lumen 27 in vps3844Δ cells (Fig. S5).
PMID:39477503	PBO:0114884	Although the Vps3844 protein is important for the transport of 26 CPY into the vacuole, Isp6-GFP and Psp3-GFP were found to localize in the vacuolar lumen 27 in vps3844Δ cells (Fig. S5).
PMID:39477503	FYPO:0005547	1 showed that the signal peptide and the transmembrane including DUF3844 domain were 2 essential for this function (Fig. 4A).
PMID:39477503	FYPO:0005547	1 showed that the signal peptide and the transmembrane including DUF3844 domain were 2 essential for this function (Fig. 4A).
PMID:39485795	PBO:0116527	(Fig. 5C)
PMID:39485795	PBO:0093560	(Fig. 5D)
PMID:39485795	PBO:0093560	(Fig. 5D)
PMID:39485795	PBO:0093560	(Fig. 5D)
PMID:39485795	PBO:0103767	(Fig. 5E and F)
PMID:39485795	PBO:0116528	These results suggest that the only role of Bdf1 in Tdk1-mediated killing is to bridge an association between Tdk1 and acetylated histones, leading to the attachment of Tdk1 to chromosomes. (Fig. 6)
PMID:39485795	PBO:0116529	(Fig. S9C)
PMID:39485795	PBO:0116529	(Fig. S9D)
PMID:39485795	PBO:0093561	(Fig. S10A)
PMID:39485795	PBO:0116526	(Fig. 4D)
PMID:39485795	PBO:0116526	(Fig. 4K)
PMID:39485795	PBO:0116525	(Fig. 4K)
PMID:39485795	PBO:0116525	(Fig. 4K)
PMID:39485795	PBO:0116525	(Fig. 4K)
PMID:39485795	PBO:0116525	(Fig. 4K)
PMID:39485795	PBO:0116525	(Fig. 4K)
PMID:39485795	PBO:0116527	(Fig. 5C)
PMID:39485795	PBO:0116527	(Fig. 5C)
PMID:39485795	PBO:0103767	(Fig. 2B and C)
PMID:39485795	PBO:0093560	(Fig. S10A)
PMID:39485795	FYPO:0000579	(Fig. 3B and C)
PMID:39485795	PBO:0116525	(Fig. 4C)
PMID:39485795	PBO:0116525	(Fig. 4C)
PMID:39485795	FYPO:0001357	(Fig. 1B)
PMID:39485795	FYPO:0000579	(Fig. 1C)
PMID:39485795	PBO:0116527	(Fig. S10B)
PMID:39485795	PBO:0093561	(Fig. S10A)
PMID:39485795	PBO:0093561	(Fig. S10A)
PMID:39485795	GO:0110134	(Fig. 1C and D)
PMID:39485795	PBO:0116525	(Fig. 4D)
PMID:39485795	PBO:0116525	(Fig. 4D)
PMID:39485795	PBO:0116530	(Fig. 4E)
PMID:39485800	PBO:0109500	(Fig. 2A)
PMID:39485800	FYPO:0002150	(Fig. 6A and B)
PMID:39485800	PBO:0093560	(Fig. 3E)
PMID:39485800	PBO:0116537	(Fig. 3A)
PMID:39485800	PBO:0116537	(Fig. 3A)
PMID:39485800	PBO:0116537	(Fig. 3A)
PMID:39485800	PBO:0116538	(Fig. 3A)
PMID:39485800	PBO:0116539	(Fig. 3B)
PMID:39502420	PBO:0119822	yhm2+ works as a dosage suppressor of auxotrophic growth defect in the maa1 (glu1) mutant.
PMID:39502420	PBO:0119824	The glu1-NS176 mutation was rescued by sup3-5 (Figure 1E), a tRNASer (SPATRNASER.03) suppressor mutation that suppresses the TGAopal nonsense codon (Hottinger et al., 1982, Niwa et al., 1989). This is direct proof that the observed growth defect in the ammonium medium is caused by the maa1 gene nonsense mutation in the glu1- NS176 strain.
PMID:39502420	PBO:0119824	The glu1-NS176 mutation was rescued by sup3-5 (Figure 1E), a tRNASer (SPATRNASER.03) suppressor mutation that suppresses the TGAopal nonsense codon (Hottinger et al., 1982, Niwa et al., 1989). This is direct proof that the observed growth defect in the ammonium medium is caused by the maa1 gene nonsense mutation in the glu1- NS176 strain.
PMID:39502420	PBO:0119823	It catalyzes the transamination between oxaloacetate and glutamate, leading to the formation of aspartate and 2-oxoglutarate (Figure 1A). phenotypes support glutamate production. evidence also supports that this ebzyme would normally be other direction? on rich nitrogen source
PMID:39502420	PBO:0119825	In addition to glu1/maa1, the yhm2 gene (SPBC83.13) is a multicopy weak suppressor of the growth defect in the glu1-NS176 mutant. The glu1 mutant harboring the multicopy yhm2+ plasmid grew slower than the glu1-corrected, wild-type strain (maa1+ (integrated); Figure 1B). The Yhm2 homolog in Saccharomyces cerevisiae is a mitochondrial carrier protein that imports 2-oxoglutarate into the mitochondria (Castegna et al., 2010). Therefore, increasing the 2-oxoglutarate concentration in mitochondria may alleviate the ammonium utilization defect in the glu1-NS176 mutant. The yhm2∆ strain showed no growth defects under all medium conditions examined, whereas the glu1 and yhm2∆ mutations had an additive effect. The glu1-NS176 yhm2∆ double mutant grew slower than each single mutant in yeast extract medium (Figure 1F). The S. pombe glu1-NS176 yhm2∆ double mutant grew when amino acids, except aspartate and asparagine, were used as the sole nitrogen source (Figure 1F). Interestingly, all the tested amino acids, including glutamine, did not support the growth of double mutant in the presence of ammonium. S. cerevisiae mutants, which lack all mitochondrial 2-oxoglutarate carriers including Yhm2, cannot grow when ammonium is the sole nitrogen source, and importantly, this growth defect is rescued by the addition of glutamate (Palmieri et al., 2001, Castegna et al., 2010, Scarcia et al., 2017).
PMID:39502420	PBO:0119822	yhm2+ works as a dosage suppressor of auxotrophic growth defect in the maa1 (glu1) mutant.
PMID:39502420	PBO:0119822	The glu1 mutant grew when glutamate was used as the sole nitrogen source, although glutamate poorly supported its growth in the presence of ammonium (Figures 1B and F). ( In general, their availability is regulated by nitrogen catabolite repression; thus, it is greatly affected by the presence of ammonium, a high-quality nitrogen source.)
PMID:39502420	PBO:0119821	Arginine, glutamic acid, or proline weakly support growth with an ammonium nitrogen source. The mutant grows normally when these amino acids are used as the sole nitrogen source. The mutant cannot utilize aspartic acid and asparagine as the sole nitrogen source.
PMID:39502420	FYPO:0001357	Interestingly, glutamine efficiently rescues the growth defect of the glu1 mutant compared to glutamate, even in the presence of ammonium (Figure 1F, Barel and MacDonald 1993).
PMID:39509469	PBO:0116876	(Fig. 4B)
PMID:39509469	PBO:0116894	(Fig. 4C)
PMID:39509469	GO:0061245	Through Rho1 activation, Rgf1 stabilizes Tea4 at the cell ends, promoting its accumulation. Additionally, we described an alternative actin-dependent mechanism, driven by Rgf1 and Rho1, for marking the poles independently to the known MT- and Tea-dependent pathway.
PMID:39509469	PBO:0116879	(Fig. S4G)
PMID:39509469	PBO:0116875	(Fig. S4E)
PMID:39509469	PBO:0116876	(Fig. S4C)
PMID:39509469	PBO:0116880	(Fig. S4D)
PMID:39509469	PBO:0116869	(Fig. 5C)
PMID:39509469	PBO:0116869	(Fig. 5C)
PMID:39509469	PBO:0116895	(Fig. 4D)
PMID:39509469	PBO:0116896	(Fig. 5C)
PMID:39509469	PBO:0116897	(Fig. 5C)
PMID:39509469	PBO:0116897	(Fig. 5C)
PMID:39509469	PBO:0116898	(Fig. 5E)
PMID:39509469	PBO:0092160	(Fig. 5E)
PMID:39509469	PBO:0116899	(Fig. S5D)
PMID:39509469	PBO:0116900	(Fig. S5B)
PMID:39509469	PBO:0116901	(Fig. S5B)
PMID:39509469	PBO:0116881	(Fig. 2A)
PMID:39509469	FYPO:0000801	(Fig. S5C)
PMID:39509469	PBO:0116882	(Fig. S5G)
PMID:39509469	PBO:0116518	(Fig. S5H)
PMID:39509469	PBO:0116869	(Fig. S5J)
PMID:39509469	PBO:0116874	(Fig. S2A)
PMID:39509469	GO:0070273	(Fig. 3E)
PMID:39509469	PBO:0116883	(Fig. 1A, B and F)
PMID:39509469	PBO:0116874	(Fig. 1C)
PMID:39509469	PBO:0116884	(Fig. 1H)
PMID:39509469	PBO:0116885	(Fig. 2A)
PMID:39509469	PBO:0116886	(Fig. 2B)
PMID:39509469	PBO:0116887	(Fig. 2B)
PMID:39509469	PBO:0116888	(Fig. 2B)
PMID:39509469	PBO:0116888	(Fig. 2B)
PMID:39509469	PBO:0116889	(Fig. 2B)
PMID:39509469	PBO:0116886	(Fig. 2B)
PMID:39509469	PBO:0116867	(Fig. 2B)
PMID:39509469	PBO:0116867	(Fig. 2B)
PMID:39509469	PBO:0097435	(Fig. 2C)
PMID:39509469	PBO:0116890	(Fig. 2C)
PMID:39509469	PBO:0116891	(Fig. 3E)
PMID:39509469	PBO:0116892	(Fig. 3H)
PMID:39509469	PBO:0116893	(Fig. 3H)
PMID:39509469	PBO:0116875	(Fig. 4A)
PMID:39509469	PBO:0116875	(Fig. 4A)
PMID:39509469	PBO:0116875	(Fig. 4A)
PMID:39509469	PBO:0116874	(Fig. S1D)
PMID:39509469	PBO:0116873	(Fig. 3F)
PMID:39509469	PBO:0116872	(Fig. 2C)
PMID:39509469	PBO:0116872	(Fig. 2C)
PMID:39509469	PBO:0116876	(Fig. 4B)
PMID:39509469	PBO:0116877	(Fig. 4E)
PMID:39509469	PBO:0116878	(Fig. 4E)
PMID:39509469	PBO:0116871	(Fig. 3G)
PMID:39509469	PBO:0116870	(Fig. 1H)
PMID:39509469	FYPO:0007182	(Fig. 1G)
PMID:39509469	PBO:0116869	(Fig. S5J)
PMID:39509469	PBO:0116868	(Fig. 5B)
PMID:39509469	PBO:0116867	(Fig. 2B)
PMID:39509469	PBO:0116879	(Fig. S4G)
PMID:39509469	PBO:0116902	(Fig. S5B)
PMID:39520300	GO:0140693	(Figure 2)
PMID:39520300	GO:0140693	(Figure 1)
PMID:39520300	GO:0140693	(Figure 1)
PMID:39520300	GO:0140693	(Figure 2)
PMID:39520300	GO:0140693	(Figure 2)
PMID:39540318	PBO:0116924	(Fig. 2D)
PMID:39540318	PBO:0117282	(Fig. 2D)
PMID:39540318	PBO:0117282	(Fig. 2D)
PMID:39540318	PBO:0117281	(Fig. S2B)
PMID:39540318	PBO:0117280	(Fig. S2A)
PMID:39540318	PBO:0117279	(Fig. S5)
PMID:39540318	PBO:0117278	(Fig. S4B)
PMID:39540318	PBO:0117277	(Fig. 1B)
PMID:39540318	PBO:0116915	(Fig. 1I)
PMID:39540318	PBO:0117276	(Fig. 1D)
PMID:39540318	PBO:0117285	(Fig. 3C)
PMID:39540318	PBO:0117286	(Fig. 4C)
PMID:39540318	PBO:0117287	(Fig. 4C)
PMID:39540318	PBO:0117288	(Fig. 4C)
PMID:39540318	PBO:0117289	(Fig. S2B)
PMID:39540318	PBO:0117290	(Fig. 3A)
PMID:39540318	PBO:0117291	(Fig. 3B)
PMID:39540318	PBO:0117292	(Fig. 3C)
PMID:39540318	PBO:0117293	(Fig. S5C)
PMID:39540318	PBO:0117294	(Fig. S4D)
PMID:39540318	PBO:0117295	(Fig. S6A)
PMID:39540318	PBO:0117296	(Fig. S6A)
PMID:39540318	PBO:0117297	(Fig. S6B)
PMID:39540318	PBO:0117298	(Fig. 5B)
PMID:39540318	PBO:0117296	(Fig. S6A)
PMID:39540318	PBO:0117287	(Fig. 5A and 5C)
PMID:39540318	PBO:0117299	(Fig. S7A)
PMID:39540318	PBO:0117300	(Fig. S7A)
PMID:39540318	PBO:0117301	(Fig. 5C)
PMID:39540318	PBO:0117302	(Fig. 5C)
PMID:39540318	PBO:0117302	(Fig. 5C)
PMID:39540318	PBO:0117303	(Fig. S8A)
PMID:39540318	PBO:0117303	(Fig. S8A)
PMID:39540318	PBO:0117277	(Fig. 5E)
PMID:39540318	PBO:0117304	(Fig. 5F)
PMID:39540318	PBO:0117305	(Fig. S7A)
PMID:39540318	PBO:0117306	(Fig. 5C)
PMID:39540318	PBO:0117303	(Fig. 5G)
PMID:39540318	PBO:0117303	(Fig. 5G)
PMID:39540318	PBO:0117307	(Fig. 5I)
PMID:39540318	PBO:0117308	(Fig. 5I)
PMID:39540318	PBO:0117309	(Fig. 5H)
PMID:39540318	PBO:0117310	(Fig. S1C)
PMID:39540318	PBO:0117310	(Fig. S1C)
PMID:39540318	PBO:0117311	(Fig. S1A)
PMID:39540318	PBO:0117312	(Fig. S1A)
PMID:39540318	PBO:0096486	(Fig. S1B)
PMID:39540318	PBO:0117312	(Fig. S1D)
PMID:39540318	PBO:0117299	(Fig. S7A)
PMID:39540318	PBO:0117313	(Fig. S9D)
PMID:39540318	PBO:0117303	(Fig. S8C)
PMID:39540318	PBO:0117303	(Fig. S8C)
PMID:39540318	PBO:0117303	(Fig. 6E)
PMID:39540318	PBO:0117303	(Fig. 6E)
PMID:39540318	PBO:0117314	(Fig. 6C and D)
PMID:39540318	PBO:0117315	(Fig. S8B)
PMID:39540318	FYPO:0008374	(Fig. 7G)
PMID:39540318	PBO:0117309	(Fig. 7A)
PMID:39540318	PBO:0105762	(Fig. 2B)
PMID:39540318	PBO:0105762	(Fig. 2B)
PMID:39540318	FYPO:0001357	(Fig. 2B)
PMID:39540318	FYPO:0001357	(Fig. 2B)
PMID:39540318	PBO:0117316	(Fig. S10A)
PMID:39540318	PBO:0117309	(Fig. 7A)
PMID:39540318	PBO:0117317	(Fig. 7D)
PMID:39540318	PBO:0117318	(Fig. 7G)
PMID:39540318	PBO:0117309	(Fig. 7F)
PMID:39540318	PBO:0117319	(Fig. 7F)
PMID:39540318	PBO:0117320	(Fig. S9C)
PMID:39540318	PBO:0117321	(Fig. S9A)
PMID:39540318	PBO:0117322	(Fig. S9B)
PMID:39540318	PBO:0117309	(Fig. 1A and Fig. 4A)
PMID:39540318	PBO:0117323	(Fig. 1C)
PMID:39540318	PBO:0117324	(Fig. 1E)
PMID:39540318	PBO:0117325	(Fig. 1G)
PMID:39540318	PBO:0116916	(Fig. 1H)
PMID:39540318	FYPO:0001357	(Fig. 2B)
PMID:39540318	FYPO:0001357	(Fig. 2B)
PMID:39540318	FYPO:0001357	(Fig. 2B)
PMID:39540318	PBO:0117331	(Fig. 6B and Fig. 7G)
PMID:39540318	FYPO:0008374	(Fig. 7G)
PMID:39540318	FYPO:0008374	(Fig. 7G)
PMID:39540318	PBO:0117318	(Fig. 7G)
PMID:39540318	PBO:0117298	(Fig. S1D)
PMID:39540318	PBO:0117280	(Fig. S2A)
PMID:39540318	PBO:0117281	(Fig. S2B)
PMID:39540318	PBO:0117332	(Fig. S2C)
PMID:39540318	PBO:0117278	(Fig. S4B)
PMID:39540318	PBO:0117279	(Fig. S5)
PMID:39540318	PBO:0117333	(Fig. S6B)
PMID:39540318	PBO:0117320	(Fig. S9C)
PMID:39540318	PBO:0117330	(Fig. 7E)
PMID:39540318	PBO:0117330	(Fig. 7E)
PMID:39540318	PBO:0117303	(Fig. 6E)
PMID:39540318	PBO:0117329	(Fig. 6D)
PMID:39540318	PBO:0116926	(Fig. 5H)
PMID:39540318	PBO:0117303	(Fig. 5G)
PMID:39540318	PBO:0117328	(Fig. 5F)
PMID:39540318	PBO:0117327	(Fig. 5E)
PMID:39540318	PBO:0117302	(Fig. 5C)
PMID:39540318	PBO:0117312	(Fig. 5B)
PMID:39540318	PBO:0117326	(Fig. 2D)
PMID:39540318	PBO:0117283	(Fig. 3A)
PMID:39540318	PBO:0117284	(Fig. 3B)
PMID:39540318	PBO:0116924	(Fig. 2D)
PMID:39540318	PBO:0116924	(Fig. 2D)
PMID:39601909	GO:0005789	The confocal microscopic analysis using GFP tagged Bsd1 suggests a typical endoplasmic reticulum membranous localization of Bsd1-GFP (Fig. 2b, left panel) [32]. Interestingly, in the presence of tunicamycin, the Bsd1-GFP localization was more pronounced (Fig. 2b, right pane
PMID:39601909	PBO:0116549	The spotting assay analysis revealed that the bsd1Δ cells exhibit sensitivity against tunicamycin (Fig. 1c)
PMID:39601909	FYPO:0008365	Furthermore, we checked the growth of S. pombe cells in the presence of 2-deoxy-glucose and observed the concentration-dependent sensitivity of bsd1delta
PMID:39601909	FYPO:0000062	(Fig. 3) Tunicamycin exposure leads to apoptotic cell death and aberrant nuclear morphology.
PMID:39601909	FYPO:0000368	Interestingly, unlike wild type cells, the bsd1Δ cells showed punctate FM4-64 staining after tunicamycin exposure (Fig. 4), reminiscent of endosome like intermediate compartment previously has been reported in vps28 mutant cells that exhibit a defect in protein sorting process in budding yeast [34].
PMID:39601909	GO:0034976	Based on these results we speculate a protective role of Bsd1 in response to tunicamycin-induced ER stress.
PMID:39601909	PBO:0112122	The epistatic interaction analysis between bsd1Δ and ire1Δ cells revealed a relative increase in tunicamycin sensitivity in bsd1Δ ire1Δ double mutant as compared to each single mutant (Fig. 5a).
PMID:39601909	PBO:0112122	The epistatic interaction analysis between bsd1Δ and ire1Δ cells revealed a relative increase in tunicamycin sensitivity in bsd1Δ ire1Δ double mutant as compared to each single mutant (Fig. 5a).
PMID:39652606	PBO:0114568	(Fig. S2)
PMID:39652606	PBO:0114579	(Fig. S2)
PMID:39652606	PBO:0116559	(Fig. S2)
PMID:39652606	FYPO:0005995	(Fig. 2E)
PMID:39652606	PBO:0116560	(Fig. 3)
PMID:39652606	PBO:0116560	(Fig. 3)
PMID:39652606	FYPO:0006791	(Fig. 3)
PMID:39652606	FYPO:0006791	(Fig. 3)
PMID:39652606	FYPO:0006791	(Fig. 3)
PMID:39652606	FYPO:0008362	(Fig. 3)
PMID:39652606	FYPO:0008362	(Fig. 3)
PMID:39652606	FYPO:0008362	(Fig. 3)
PMID:39652606	PBO:0114564	(Fig. 2A, 2B)
PMID:39652606	PBO:0114566	(Fig. 2A, 2B)
PMID:39652606	PBO:0114542	(Fig. 2A, 2B)
PMID:39652606	PBO:0114549	(Fig. 2A, 2B)
PMID:39652606	PBO:0114547	(Fig. 2A, 2B)
PMID:39652606	PBO:0114543	(Fig. 2A, 2B)
PMID:39652606	PBO:0114545	(Fig. 2A, 2B)
PMID:39652606	PBO:0114561	(Fig. 2A, 2B)
PMID:39652606	PBO:0114158	(Fig. 3)
PMID:39652606	PBO:0093614	(Fig. 4)
PMID:39652606	PBO:0093564	(Fig. 4)
PMID:39652606	FYPO:0001357	(Fig. 4)
PMID:39652606	PBO:0093559	(Fig. 4)
PMID:39652606	PBO:0116562	(Fig. 5B)
PMID:39652606	PBO:0116563	(Fig. 5B)
PMID:39652606	PBO:0116564	(Fig. 5B)
PMID:39652606	PBO:0114566	(Fig. 2A, 2B)
PMID:39652606	PBO:0114568	(Fig. S2)
PMID:39652606	PBO:0116566	(Fig. S2)
PMID:39652606	PBO:0116559	(Fig. S2)
PMID:39652606	PBO:0116567	(Fig. S6A)
PMID:39652606	PBO:0116568	(Fig. S6A)
PMID:39652606	PBO:0116569	(Fig. S6B)
PMID:39652606	PBO:0116570	(Fig. S6B)
PMID:39652606	PBO:0116571	(Fig. S6A)
PMID:39652606	PBO:0116572	(Fig. S6A)
PMID:39652606	PBO:0116573	(Fig. S6A)
PMID:39652606	PBO:0116565	(Fig. 5B)
PMID:39652606	PBO:0114547	(Fig. 2A, 2B)
PMID:39652606	PBO:0114549	(Fig. 2A, 2B)
PMID:39652606	FYPO:0005995	(Fig. 2E)
PMID:39652606	FYPO:0005995	(Fig. 2E)
PMID:39652606	PBO:0114568	(Fig. S2)
PMID:39652606	PBO:0114579	(Fig. S2)
PMID:39652606	PBO:0116559	(Fig. S2)
PMID:39652606	PBO:0116574	(Fig. S6A)
PMID:39652606	PBO:0116575	(Fig. S6B)
PMID:39652606	PBO:0116576	(Fig. S6B)
PMID:39652606	PBO:0093559	(Fig. 4)
PMID:39652606	PBO:0093614	(Fig. 4)
PMID:39652606	PBO:0093614	(Fig. 4)
PMID:39652606	PBO:0093564	(Fig. 4)
PMID:39652606	PBO:0093564	(Fig. 4)
PMID:39652606	FYPO:0000164	(Fig. 1A)
PMID:39652606	FYPO:0000164	(Fig. 1A)
PMID:39652606	PBO:0116556	(Fig. 1)
PMID:39652606	PBO:0116557	(Fig. 1)
PMID:39652606	PBO:0116558	(Fig. 1)
PMID:39652606	PBO:0114561	(Fig. 2A, 2B)
PMID:39652606	PBO:0114564	(Fig. 2A, 2B)
PMID:39652606	PBO:0114542	(Fig. 2A, 2B)
PMID:39652606	PBO:0114543	(Fig. 2A, 2B)
PMID:39652606	PBO:0114545	(Fig. 2A, 2B)
PMID:39652606	PBO:0114566	(Fig. 2A, 2B)
PMID:39652606	PBO:0114547	(Fig. 2A, 2B)
PMID:39652606	PBO:0114549	(Fig. 2A, 2B)
PMID:39652606	PBO:0114561	(Fig. 2A, 2B)
PMID:39652606	PBO:0114564	(Fig. 2A, 2B)
PMID:39652606	PBO:0114542	(Fig. 2A, 2B)
PMID:39652606	PBO:0114543	(Fig. 2A, 2B)
PMID:39652606	PBO:0114545	(Fig. 2A, 2B)
PMID:39660919	FYPO:0006657	(Fig. 3C) (comment: Assayed activity using medium supernatant)
PMID:39660919	PBO:0097999	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PBO:0097999	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PBO:0097999	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PBO:0097999	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PBO:0097999	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PBO:0097999	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	FYPO:0001357	(Fig. 3A)
PMID:39660919	FYPO:0001357	(Fig. 3A)
PMID:39660919	PBO:0097999	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PBO:0097999	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PBO:0097999	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PBO:0097999	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PBO:0097999	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PBO:0097999	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PBO:0097999	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PBO:0116444	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	PBO:0116444	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	PBO:0116444	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	PBO:0116444	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	PBO:0116444	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	PBO:0116444	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	PBO:0116444	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	PBO:0116444	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	PBO:0116445	(Figure 5) It is apparent that Efn1 contributes a greater share of secreted 5'-nucleotidase activity against AMP, GMP, and UMP compared to Efn2.
PMID:39660919	PBO:0116445	(Figure 5) The Efn1:Efn2 activity ratio is 5.0 for AMP, 6.3 for GMP, and 4.1 for UMP (Fig. 5) However, the Efn1:Efn2 activity ratio for CMP hydrolysis is 1.3, suggesting that Efn2 displays a greater selectivity for CMP than does Efn1.
PMID:39660919	PBO:0116444	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	PBO:0116444	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	PBO:0116444	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	PBO:0116444	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	FYPO:0001310	(Fig. 6) We conclude that Pho1 acid phosphatase and extracellular 5'-nucleotidase activities, which are induced during acute phosphate starvation, are not important for survival during chronic phosphate starvation. It is likely that the lifespan-shortening effects of ablating Pho7 reflect its role in promoting the expression of several hundred other fission yeast genes (8).
PMID:39660919	PBO:0116444	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	FYPO:0008354	(Fig. 5)
PMID:39660919	FYPO:0008356	(Fig. 5)
PMID:39660919	FYPO:0008355	(Fig. 5)
PMID:39660919	FYPO:0008357	(Fig. 5)
PMID:39660919	FYPO:0008354	(Fig. 5)
PMID:39660919	FYPO:0008356	(Fig. 5)
PMID:39660919	FYPO:0008355	(Fig. 5)
PMID:39660919	FYPO:0008357	(Fig. 5)
PMID:39660919	FYPO:0001357	we generated a pho1∆ pho4∆ strain that grew as well as wild-type on YES agar medium (Fig. 3A).
PMID:39660919	FYPO:0008353	(Fig. 4C)
PMID:39660919	FYPO:0008352	(Fig. 4C)
PMID:39660919	FYPO:0008351	(Fig. 4C)
PMID:39660919	FYPO:0008350	(Fig. 4C)
PMID:39666777	FYPO:0002060	Exogenous expression of Nup211, Nup2111-863, or Nup2111-655 restored cell viability; however, expression of Nup2111-1033 only led to a partial recovery (Fig 4A)
PMID:39666777	FYPO:0000950	some cells failed to develop a septum during division (Fig 3B- a)
PMID:39666777	FYPO:0001406	Compared with wild type cells, a higher percentage of nup211 shut-off cells contained multiple and/or thicker septa (Fig 3C).
PMID:39666777	FYPO:0002060	Exogenous expression of Nup211, Nup2111-863, or Nup2111-655 restored cell viability; however, expression of Nup2111-1033 only led to a partial recovery (Fig 4A)
PMID:39666777	FYPO:0002060	(Fig. 4A)
PMID:39666777	PBO:0117455	(Figure 5C)
PMID:39666777	PBO:0117454	(Fig. 7) Nup211 regulates the expression of several genes involved in cytokinesis.
PMID:39666777	PBO:0117453	(Fig. 7) Nup211 regulates the expression of several genes involved in cytokinesis.
PMID:39666777	PBO:0117452	(Fig. 7) Nup211 regulates the expression of several genes involved in cytokinesis.
PMID:39666777	PBO:0117451	(Fig. 7) Nup211 regulates the expression of several genes involved in cytokinesis.
PMID:39666777	PBO:0117450	(Fig. 7) Nup211 regulates the expression of several genes involved in cytokinesis.
PMID:39666777	PBO:0117449	(Fig. 7) Nup211 regulates the expression of several genes involved in cytokinesis.
PMID:39666777	PBO:0117448	(Fig. 7) Nup211 regulates the expression of several genes involved in cytokinesis.
PMID:39666777	PBO:0117447	(Fig. 7) Nup211 regulates the expression of several genes involved in cytokinesis.
PMID:39666777	PBO:0117446	(Fig. 7) Nup211 regulates the expression of several genes involved in cytokinesis.
PMID:39666777	FYPO:0000134	(Figure 3B) Some cells appeared abnormally round, curved, bulged, or branched, indicating that Nup211 plays a role in maintaining proper cell shape (Fig 3B). Interestingly, nup211 shut-off cells also showed severe defects in septation and cytokinesis. These defects varied widely: some cells failed to develop a septum during division (Fig 3B- a), while others developed thicker (Fig 3B-b), misplaced (Fig 3B-c), or multiple septa (Fig 3B- d). Furthermore, septa were sometimes seen in shorter cells (Fig 3B-c), while other phenotypes like bulging (Fig 3B-c, 3B-e), branching (Fig 3B-e), curving, and swelling (Fig 3B-f) were also observed.
PMID:39705284	PBO:0119909	(Fig. 5C)
PMID:39705284	PBO:0119909	(Fig. 5C)
PMID:39705284	PBO:0119908	(Fig. 1D)
PMID:39705284	PBO:0117217	(Fig. 7A)
PMID:39705284	PBO:0117217	(Fig. 7A)
PMID:39705284	FYPO:0000581	(Fig. 7F)
PMID:39705284	PBO:0095337	(Fig. 7F and G)
PMID:39705284	PBO:0093824	(Fig. 7H)
PMID:39705284	PBO:0119917	(Fig. 5D)
PMID:39705284	PBO:0093823	(Fig. 7C)
PMID:39705284	PBO:0119914	(Fig. 7B)
PMID:39705284	PBO:0093825	(Fig. 7A)
PMID:39705284	PBO:0119917	(Fig. 5D)
PMID:39705284	FYPO:0006295	(Fig. 6C)
PMID:39705284	PBO:0093825	(Fig. 7A)
PMID:39705284	PBO:0119916	(Fig. 7B)
PMID:39705284	PBO:0119915	(Fig. 7B)
PMID:39705284	PBO:0119915	(Fig. 7B)
PMID:39705284	PBO:0119914	(Fig. 7B)
PMID:39705284	PBO:0119910	(Fig. 5C)
PMID:39705284	PBO:0119910	(Fig. 5C)
PMID:39705284	PBO:0119911	(Fig. 5C)
PMID:39705284	PBO:0119912	(Figure 5)
PMID:39705284	PBO:0119912	(Figure 5)
PMID:39705284	PBO:0119913	(Fig. 5D)
PMID:39705284	PBO:0119913	(Fig. 5D)
PMID:39705284	FYPO:0006294	(Fig. 6D)
PMID:39705284	FYPO:0004670	(Fig. 6C)
PMID:39705284	FYPO:0000573	(Fig. 6E)
PMID:39705284	FYPO:0000573	(Fig. 6A)
PMID:39705284	FYPO:0000573	(Fig. 6E)
PMID:39747188	PBO:0120586	while the nuclear localization of both TFs was preserved (Fig. 4h, Supplementary Fig. 5c)
PMID:39747188	PBO:0120833	On the other hand, when cwf10-1 was combined with swi6Δ, the double mutant cells showed a dramatic reduction in cenH siRNAs (Supplementary Fig. 7c).
PMID:39747188	PBO:0120832	A temperature-sensitive mutation in the conserved spliceosome component Cwf10EFTUD2 (cwf10-1)56 alone caused only a modest defect in the production of siRNAs that map to cenH (Sup- plementary Fig. 7c).
PMID:39747188	PBO:0120591	RNAPII occu- pancy increased at cenH in clr4Δ (Fig. 5e, f and Supplementary Fig. 6c). Removal of PhpC or Moc3, or the introduction of CCAATmut mutation in clr4Δ cells, resulted in a considerable reduction in RNAPII levels at cenH (Fig. 5e, f).
PMID:39747188	PBO:0120591	RNAPII occu- pancy increased at cenH in clr4Δ (Fig. 5e, f and Supplementary Fig. 6c). Removal of PhpC or Moc3, or the introduction of CCAATmut mutation in clr4Δ cells, resulted in a considerable reduction in RNAPII levels at cenH (Fig. 5e, f).
PMID:39747188	PBO:0120591	RNAPII occu- pancy increased at cenH in clr4Δ (Fig. 5e, f and Supplementary Fig. 6c). Removal of PhpC or Moc3, or the introduction of CCAATmut mutation in clr4Δ cells, resulted in a considerable reduction in RNAPII levels at cenH (Fig. 5e, f).
PMID:39747188	PBO:0120591	RNAPII occu- pancy increased at cenH in clr4Δ (Fig. 5e, f and Supplementary Fig. 6c). Removal of PhpC or Moc3, or the introduction of CCAATmut mutation in clr4Δ cells, resulted in a considerable reduction in RNAPII levels at cenH (Fig. 5e, f).
PMID:39747188	PBO:0120569	"(comment: vw: changed. ""GO:0140297 DNA-binding transcription factor BINDING"" to RNA polymerase II cis-regulatory region sequence-specific DNA binding. DNA-binding transcription factor binding is a term for proteins which bind transcription factors) We next investigated whether Php2 and Php3 bind at the het- erochromatic regions where Php5 is found. ChIP-seq analyses revealed that both proteins co-localized with Php5 at the cenH and dh repeats adjacent to siRNA hotspots, and this result was confirmed by ChIP- qPCR (Fig. 2c–f)."
PMID:39747188	PBO:0120570	"(comment: vw: changed. ""GO:0140297 DNA-binding transcription factor BINDING"" to RNA polymerase II cis-regulatory region sequence-specific DNA binding. DNA-binding transcription factor binding is a term for proteins which bind transcription factors) We next investigated whether Php2 and Php3 bind at the het- erochromatic regions where Php5 is found. ChIP-seq analyses revealed that both proteins co-localized with Php5 at the cenH and dh repeats adjacent to siRNA hotspots, and this result was confirmed by ChIP- qPCR (Fig. 2c–f)."
PMID:39747188	PBO:0120569	By using this method, we confirmed that Php5 and Moc3 were indeed enriched at both cenH and dh loci (Fig. 1d and Supplementary Fig. 1b). These results indicate that TFs can access repeat elements located within repressive het- erochromatin domains.
PMID:39747188	PBO:0120570	By using this method, we confirmed that Php5 and Moc3 were indeed enriched at both cenH and dh loci (Fig. 1d and Supplementary Fig. 1b). These results indicate that TFs can access repeat elements located within repressive het- erochromatin domains.
PMID:39747188	PBO:0120569	We next investigated whether Php2 and Php3 bind at the het- erochromatic regions where Php5 is found. ChIP-seq analyses revealed that both proteins co-localized with Php5 at the cenH and dh repeats adjacent to siRNA hotspots, and this result was confirmed by ChIP- qPCR (Fig. 2c–f).
PMID:39747188	PBO:0120570	We next investigated whether Php2 and Php3 bind at the het- erochromatic regions where Php5 is found. ChIP-seq analyses revealed that both proteins co-localized with Php5 at the cenH and dh repeats adjacent to siRNA hotspots, and this result was confirmed by ChIP- qPCR (Fig. 2c–f).
PMID:39747188	GO:0141194	*****************positive regulation. (comment: I removed GO:0031453 positive regulation of heterochromatin formation and GO:0010964 regulation of regulatory ncRNA-mediated heterochromatin formation, because if we make a positive regulation term it will cover both i.e the other terms will be ancestors ) Mutations in the php5 gene or its binding site, the CCAAT box located at cenH when combine with Swi6, result in a significant decrease in siRNA production at the mating type locus.
PMID:39747188	PBO:0120569	By using this method, we confirmed that Php5 and Moc3 were indeed enriched at both cenH and dh loci (Fig. 1d and Supplementary Fig. 1b). These results indicate that TFs can access repeat elements located within repressive het- erochromatin domains.
PMID:39747188	PBO:0120570	By using this method, we confirmed that Php5 and Moc3 were indeed enriched at both cenH and dh loci (Fig. 1d and Supplementary Fig. 1b). These results indicate that TFs can access repeat elements located within repressive het- erochromatin domains.
PMID:39747188	GO:0016602	For this, we performed immuno-affinity purification of GFP-tagged Php5 (Fig. 2a) and analyzed the purified fraction by mass spectroscopy. In addition to Php5, these analyses identified NF-YA and NF-YB orthologs, Php2 and Php3, respectively (Fig. 2b). Therefore, Php5 associates with Php3NF-YB and Php2NF-YA to form the Php complex (PhpC), as observed in other yeasts and humans.
PMID:39747188	GO:0141194	************************positive regulation (comment: vw: I removed GO:0031453 positive regulation of heterochromatin formation and GO:0010964 regulation of regulatory ncRNA-mediated heterochromatin formation, because if we make a positive regulation term it will cover both i.e the other terms will be ancestors ) Mutations in the Php3 gene or its binding site, the CCAAT box located at cenH, result in a significant decrease in siRNA production at the mating type locus.
PMID:39747188	PBO:0120572	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	PBO:0120573	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	PBO:0120573	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	PBO:0120572	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	PBO:0120572	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	PBO:0120572	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	PBO:0120572	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	PBO:0120572	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	PBO:0120572	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	PBO:0120572	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	PBO:0120572	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	GO:0141194	Small RNA sequencing data indicated that Swi6 is necessary for siRNA production, irrespective of PhpC and Moc3.
PMID:39747188	GO:0016602	For this, we performed immuno-affinity purification of GFP-tagged Php5 (Fig. 2a) and analyzed the purified fraction by mass spectroscopy. In addition to Php5, these analyses identified NF-YA and NF-YB orthologs, Php2 and Php3, respectively (Fig. 2b). Therefore, Php5 associates with Php3NF-YB and Php2NF-YA to form the Php complex (PhpC), as observed in other yeasts and humans.
PMID:39747188	GO:0016602	For this, we performed immuno-affinity purification of GFP-tagged Php5 (Fig. 2a) and analyzed the purified fraction by mass spectroscopy. In addition to Php5, these analyses identified NF-YA and NF-YB orthologs, Php2 and Php3, respectively (Fig. 2b). Therefore, Php5 associates with Php3NF-YB and Php2NF-YA to form the Php complex (PhpC), as observed in other yeasts and humans.
PMID:39747188	PBO:0120574	Consistent with the fact that Php2/3/5 forms a complex, loss of Php3 localization at cenH and dh elements was observed in the absence of php2 or php5 (Fig. 3a, b, and Supplementary Fig. 3a).
PMID:39747188	PBO:0120574	Consistent with the fact that Php2/3/5 forms a complex, loss of Php3 localization at cenH and dh elements was observed in the absence of php2 or php5 (Fig. 3a, b, and Supplementary Fig. 3a).
PMID:39747188	PBO:0120575	Consistent with the fact that Php2/3/5 forms a complex, loss of Php3 localization at cenH and dh elements was observed in the absence of php2 or php5 (Fig. 3a, b, and Supplementary Fig. 3a).
PMID:39747188	PBO:0120575	Consistent with the fact that Php2/3/5 forms a complex, loss of Php3 localization at cenH and dh elements was observed in the absence of php2 or php5 (Fig. 3a, b, and Supplementary Fig. 3a).
PMID:39747188	PBO:0120576	Interestingly, we also observed that Moc3 occupancy at both cenH and dh heterochromatic regions was contingent upon PhpC (Fig. 3a, c and Supplementary Fig. 3d).
PMID:39747188	PBO:0120577	Interestingly, we also observed that Moc3 occupancy at both cenH and dh heterochromatic regions was contingent upon PhpC (Fig. 3a, c and Supplementary Fig. 3d).
PMID:39747188	PBO:0120575	Moreover, the localization of PhpC subunits was compro- mised in moc3Δ cells (Fig. 3a, b and Supplementary Fig. 3b, c).
PMID:39747188	PBO:0120574	Moreover, the localization of PhpC subunits was compro- mised in moc3Δ cells (Fig. 3a, b and Supplementary Fig. 3b, c).
PMID:39747188	GO:0005721	Furthermore, the genome-wide distribution of Php3 and Moc3 remained largely unchanged in mitotic-arrested cells (Supplementary Data 4), indi- cating that PhpC and Moc3 maintain their association with hetero- chromatin outside of S-phase.
PMID:39747188	GO:0005721	Furthermore, the genome-wide distribution of Php3 and Moc3 remained largely unchanged in mitotic-arrested cells (Supplementary Data 4), indi- cating that PhpC and Moc3 maintain their association with hetero- chromatin outside of S-phase.
PMID:39747188	GO:0031934	Furthermore, the genome-wide distribution of Php3 and Moc3 remained largely unchanged in mitotic-arrested cells (Supplementary Data 4), indi- cating that PhpC and Moc3 maintain their association with hetero- chromatin outside of S-phase.
PMID:39747188	GO:0031934	Furthermore, the genome-wide distribution of Php3 and Moc3 remained largely unchanged in mitotic-arrested cells (Supplementary Data 4), indi- cating that PhpC and Moc3 maintain their association with hetero- chromatin outside of S-phase.
PMID:39747188	PBO:0120578	PhpC and Moc3 peaks at cenH and dh elements were mostly unchanged in cells lacking Clr4Suv39h (Fig. 4a–d and Supplementary Fig. 4a, b).
PMID:39747188	PBO:0120579	PhpC and Moc3 peaks at cenH and dh elements were mostly unchanged in cells lacking Clr4Suv39h (Fig. 4a–d and Supplementary Fig. 4a, b).
PMID:39747188	PBO:0120580	PhpC and Moc3 peaks at cenH and dh elements were mostly unchanged in cells lacking Clr4Suv39h (Fig. 4a–d and Supplementary Fig. 4a, b).
PMID:39747188	PBO:0120581	PhpC and Moc3 peaks at cenH and dh elements were mostly unchanged in cells lacking Clr4Suv39h (Fig. 4a–d and Supplementary Fig. 4a, b).
PMID:39747188	PBO:0120582	we investigated the dis- tribution of Php3 and Moc3 in cells devoid of both Gcn5, a subunit of the SAGA complex, and Mst2, a MYST acetyltransferase. Interestingly, we found that in those cells, both TFs can still localize to cenH and dh heterochromatic repeat elements, albeit with a slight reduction (Sup- plementary Fig. 4d, e).
PMID:39747188	PBO:0120583	we investigated the dis- tribution of Php3 and Moc3 in cells devoid of both Gcn5, a subunit of the SAGA complex, and Mst2, a MYST acetyltransferase. Interestingly, we found that in those cells, both TFs can still localize to cenH and dh heterochromatic repeat elements, albeit with a slight reduction (Sup- plementary Fig. 4d, e).
PMID:39747188	PBO:0120582	we investigated the dis- tribution of Php3 and Moc3 in cells devoid of both Gcn5, a subunit of the SAGA complex, and Mst2, a MYST acetyltransferase. Interestingly, we found that in those cells, both TFs can still localize to cenH and dh heterochromatic repeat elements, albeit with a slight reduction (Sup- plementary Fig. 4d, e).
PMID:39747188	PBO:0120583	we investigated the dis- tribution of Php3 and Moc3 in cells devoid of both Gcn5, a subunit of the SAGA complex, and Mst2, a MYST acetyltransferase. Interestingly, we found that in those cells, both TFs can still localize to cenH and dh heterochromatic repeat elements, albeit with a slight reduction (Sup- plementary Fig. 4d, e).
PMID:39747188	PBO:0120583	Specifically, we assessed TF localization in cells lacking the RSC subunit Rsc1, the SWI/SNF ATP-dependent chromatin remodeler Snf22 and/or bearing a mutation in the ATPase domain of Ino80 (i.e., ino80K873A). In all cases, we observed that Php3 and Moc3 binding to cenH and dh regions were only marginally reduced but nevertheless not abolished (Supplementary Fig. 4f–i).
PMID:39747188	PBO:0120582	Specifically, we assessed TF localization in cells lacking the RSC subunit Rsc1, the SWI/SNF ATP-dependent chromatin remodeler Snf22 and/or bearing a mutation in the ATPase domain of Ino80 (i.e., ino80K873A). In all cases, we observed that Php3 and Moc3 binding to cenH and dh regions were only marginally reduced but nevertheless not abolished (Supplementary Fig. 4f–i).
PMID:39747188	PBO:0120583	Specifically, we assessed TF localization in cells lacking the RSC subunit Rsc1, the SWI/SNF ATP-dependent chromatin remodeler Snf22 and/or bearing a mutation in the ATPase domain of Ino80 (i.e., ino80K873A). In all cases, we observed that Php3 and Moc3 binding to cenH and dh regions were only marginally reduced but nevertheless not abolished (Supplementary Fig. 4f–i).
PMID:39747188	PBO:0120582	Specifically, we assessed TF localization in cells lacking the RSC subunit Rsc1, the SWI/SNF ATP-dependent chromatin remodeler Snf22 and/or bearing a mutation in the ATPase domain of Ino80 (i.e., ino80K873A). In all cases, we observed that Php3 and Moc3 binding to cenH and dh regions were only marginally reduced but nevertheless not abolished (Supplementary Fig. 4f–i).
PMID:39747188	PBO:0120584	Remarkably, we observed that in both mutants, the binding of PhpC subunits Php3 and Php5 at cenH and dh heterochromatic repeats was drastically reduced (Fig. 4e–g, Supplementary Fig. 5b)...... Indeed, site- specific ChIP-qPCR analysis revealed a ~ 90% reduction in Php3 and a ~ 80% reduction in Php5 in HFD mutants compared to WT (Fig. 4g, Supplementary Fig. 5b).
PMID:39747188	PBO:0120585	Remarkably, we observed that in both mutants, the binding of PhpC subunits Php3 and Php5 at cenH and dh heterochromatic repeats was drastically reduced (Fig. 4e–g, Supplementary Fig. 5b),....... Indeed, site- specific ChIP-qPCR analysis revealed a ~ 90% reduction in Php3 and a ~ 80% reduction in Php5 in HFD mutants compared to WT (Fig. 4g, Supplementary Fig. 5b).
PMID:39747188	PBO:0120587	while the nuclear localization of both TFs was preserved (Fig. 4h, Supplementary Fig. 5c)
PMID:39747188	PBO:0120588	On the other hand, the global binding of Php3 at gene promoters, lncRNAs, and other ncRNAs, was reduced but not abolished in HFD mutant cells (Supplementary Fig. 5d, e, Supplemen- tary Data 4).
PMID:39747188	PBO:0113698	As expected, we observed increased cenH transcript levels in clr4Δ26 (Fig. 5a, b and Supplementary Fig. 6a, b). Interestingly, the lack of PhpC significantly decreased cenH transcript levels in clr4Δ (Fig. 5a, b).
PMID:39747188	PBO:0113714	As expected, we observed increased cenH transcript levels in clr4Δ26 (Fig. 5a, b and Supplementary Fig. 6a, b). Interestingly, the lack of PhpC significantly decreased cenH transcript levels in clr4Δ (Fig. 5a, b).
PMID:39747188	PBO:0113714	As expected, we observed increased cenH transcript levels in clr4Δ26 (Fig. 5a, b and Supplementary Fig. 6a, b). Interestingly, the lack of PhpC significantly decreased cenH transcript levels in clr4Δ (Fig. 5a, b).
PMID:39747188	PBO:0113714	As expected, we observed increased cenH transcript levels in clr4Δ26 (Fig. 5a, b and Supplementary Fig. 6a, b). Interestingly, the lack of PhpC significantly decreased cenH transcript levels in clr4Δ (Fig. 5a, b).
PMID:39747188	PBO:0113714	As expected, we observed increased cenH transcript levels in clr4Δ26 (Fig. 5a, b and Supplementary Fig. 6a, b). Interestingly, the lack of PhpC significantly decreased cenH transcript levels in clr4Δ (Fig. 5a, b).
PMID:39747188	PBO:0120589	As expected, we observed increased cenH transcript levels in clr4Δ26 (Fig. 5a, b and Supplementary Fig. 6a, b). Interestingly, the lack of PhpC significantly decreased cenH transcript levels in clr4Δ (Fig. 5a, b).
PMID:39747188	PBO:0120589	As expected, we observed increased cenH transcript levels in clr4Δ26 (Fig. 5a, b and Supplementary Fig. 6a, b). Interestingly, the lack of PhpC significantly decreased cenH transcript levels in clr4Δ (Fig. 5a, b).
PMID:39747188	PBO:0113714	Similar changes were observed in moc3Δ (Fig. 5a and Supplementary Fig. 6b)52.
PMID:39747188	PBO:0120590	RNAPII occu- pancy increased at cenH in clr4Δ (Fig. 5e, f and Supplementary Fig. 6c). Removal of PhpC or Moc3, or the introduction of CCAATmut mutation in clr4Δ cells, resulted in a considerable reduction in RNAPII levels at cenH (Fig. 5e, f).
PMID:39786922	GO:0000781	(Fig. 5)
PMID:39786922	PBO:0116935	(Fig. 6)
PMID:39786922	PBO:0116935	(Fig. 6)
PMID:39786922	PBO:0116936	(Fig. 7B and C)
PMID:39786922	PBO:0116937	(Fig. 7B and C)
PMID:39786922	PBO:0116938	(Fig. 7B and C)
PMID:39786922	PBO:0116939	(Fig. 6)
PMID:39786922	PBO:0116934	(Fig. 4)
PMID:39786922	PBO:0116927	(Fig. 2A)
PMID:39786922	PBO:0021459	Sl8-GFP colocalizes with nuclear periphery labeled by Cut11-mCherry (Fig. 4A)
PMID:39786922	PBO:0116928	Slx8-GFP colocalizes wih Mis6-RFP (Fig. 5)
PMID:39786922	PBO:0116929	(Fig. 5)
PMID:39786922	PBO:0116931	(Fig. 7B and C)
PMID:39786922	PBO:0095834	(Fig. 7A)
PMID:39786922	PBO:0093618	(Fig. S1A)
PMID:39786922	PBO:0095653	(Fig. 7A)
PMID:39786922	PBO:0116935	(Fig. 2B and C)
PMID:39786922	PBO:0116933	Slx8-GFP colocalizes with Sid4-RFP (Fig. 5)
PMID:39786922	PBO:0116932	(Fig. 7B and C)
PMID:39786922	PBO:0116935	(Fig. 2B and C)
PMID:39786922	PBO:0116935	(Fig. 2B, C and D)
PMID:39786922	PBO:0116932	(Fig. 7B and C)
PMID:39786922	PBO:0093615	(Fig. S1A)
PMID:39786922	PBO:0093581	(Fig. S1A)
PMID:39789818	PBO:0093614	Moreover, the rad52-S365D/E-YFP displayed higher sensitivities to HU, CPT, and MMS rather than cisPt (Figure 5a).
PMID:39789818	PBO:0093615	Interestingly, we found that dsk1Δ was highly sensitive to replication-associated DNA break agents like camptothecin (CPT), which is a topoisomerase I inhibitor, and was slightly sensitive to methyl methanesulfonate (MMS), which alkylates and breaks DNA during replication (Figure 1a and Figure S1c).
PMID:39789818	FYPO:0006567	After CPT release, the percentage of Rad52 foci in dsk1Δ decreased more slowly than that in dsk1+ (Figures 2a and S3a,b), indicating a compromised HR repair in dsk1Δ. Second, we exploited a transformation-based genetic system (Figure 2b)
PMID:39789818	FYPO:0004466	We exploited the YFP-tagged Rad52 strain and found that the percentage (45%) of Rad52-YFP fluorescent foci in dsk1Δ cells was elevated almost 100-fold relative to the percentage (0.5%) of that in WT cells under physiological conditions, suggesting more spontaneous DNA damage induced by dsk1Δ.
PMID:39789818	PBO:0093616	Moreover, we found that dsk1Δ together with mutations of PRR genes rhp18Δ (translesion synthesis) (Figure S2g) and ubc13Δ (template switching) (Figure S2h) were additively defective in response to CPT and MMS treatments, suggesting that Dsk1 and PRR are in parallel and distinct pathways in response to replication stress.
PMID:39789818	FYPO:0003906	However, dsk1Δ was not sensitive to Bleomycin (Bleo), Phleomycin (Phleo), and UV irradiation, which directly break DNA, as well as 6-Azauracil (6-AU) and Mycophenolic acid (MPA), which impair transcription (Figure S1d).
PMID:39789818	PBO:0093618	Interestingly, we found that dsk1Δ was highly sensitive to replication-associated DNA break agents like camptothecin (CPT), which is a topoisomerase I inhibitor, and was slightly sensitive to methyl methanesulfonate (MMS), which alkylates and breaks DNA during replication (Figure 1a and Figure S1c).
PMID:39789818	PBO:0093616	Moreover, we found that dsk1Δ together with mutations of PRR genes rhp18Δ (translesion synthesis) (Figure S2g) and ubc13Δ (template switching) (Figure S2h) were additively defective in response to CPT and MMS treatments, suggesting that Dsk1 and PRR are in parallel and distinct pathways in response to replication stress.
PMID:39789818	PBO:0093616	Moreover, we found that dsk1Δ together with mutations of PRR genes rhp18Δ (translesion synthesis) (Figure S2g) and ubc13Δ (template switching) (Figure S2h) were additively defective in response to CPT and MMS treatments, suggesting that Dsk1 and PRR are in parallel and distinct pathways in response to replication stress.
PMID:39789818	PBO:0093616	Moreover, we found that dsk1Δ together with mutations of PRR genes rhp18Δ (translesion synthesis) (Figure S2g) and ubc13Δ (template switching) (Figure S2h) were additively defective in response to CPT and MMS treatments, suggesting that Dsk1 and PRR are in parallel and distinct pathways in response to replication stress.
PMID:39789818	FYPO:0006437	Additionally, there were few septa when both dsk1+ and dsk1Δ were treated with MMS, and their number of septa was similarly increased after MMS release (Figure S2d). This result indicates that the cell cycle progression of dsk1Δ under MMS is arrested by functional checkpoints. To further support it biochemically, we tagged Chk1 with 3HA as we had no antibody against S. pombe Chk1. We found that the 3HA tag did not influence the genotoxic phenotype of chk1+ (Figure S2e). Immunoblots showed that Chk1-3HA in dsk1Δ was normally phosphorylated after MMS treatment (Figure S2f). Therefore, we conclude that dsk1Δ does not influence checkpoints activation.
PMID:39789818	PBO:0093613	However, dsk1Δ combined with mutations of DNA damage checkpoint effector chk1Δ and replication checkpoint effector cds1Δ, exhibited synergistic CPT and HU sensitivities (Figure S2b,c).
PMID:39789818	PBO:0093613	However, dsk1Δ combined with mutations of DNA damage checkpoint effector chk1Δ and replication checkpoint effector cds1Δ, exhibited synergistic CPT and HU sensitivities (Figure S2b,c).
PMID:39789818	PBO:0093613	However, dsk1Δ combined with mutations of DNA damage checkpoint effector chk1Δ and replication checkpoint effector cds1Δ, exhibited synergistic CPT and HU sensitivities (Figure S2b,c).
PMID:39789818	PBO:0093613	However, dsk1Δ combined with mutations of DNA damage checkpoint effector chk1Δ and replication checkpoint effector cds1Δ, exhibited synergistic CPT and HU sensitivities (Figure S2b,c).
PMID:39789818	PBO:0093615	Interestingly, we found that dsk1Δ was highly sensitive to replication-associated DNA break agents like camptothecin (CPT), which is a topoisomerase I inhibitor, and was slightly sensitive to methyl methanesulfonate (MMS), which alkylates and breaks DNA during replication (Figure 1a and Figure S1c).
PMID:39789818	PBO:0093613	Interestingly, we found that dsk1Δ was highly sensitive to replication-associated DNA break agents like camptothecin (CPT), which is a topoisomerase I inhibitor, and was slightly sensitive to methyl methanesulfonate (MMS), which alkylates and breaks DNA during replication (Figure 1a and Figure S1c).
PMID:39789818	FYPO:0000482	On the contrary, dsk1Δ cells displayed about a fivefold reduction in spontaneous recombination rate, mainly in the aspect of gene conversion rather than gene deletion (Figure 2g).
PMID:39789818	PBO:0120025	Consistent with the previous study (Hayashi et al. 2009), Dsk1-GFP localized in both the nucleus and cytoplasm. After CPT treatment, the percentage of Dsk1-GFP translocated from cytoplasm to nucleus was increased, and dominantly accumulated in the nucleus (Figures 3a and S3c).
PMID:39789818	GO:0005737	Consistent with the previous study (Hayashi et al. 2009), Dsk1-GFP localized in both the nucleus and cytoplasm. After CPT treatment, the percentage of Dsk1-GFP translocated from cytoplasm to nucleus was increased, and dominantly accumulated in the nucleus (Figures 3a and S3c).
PMID:39789818	PBO:0104838	(Figure 4) (comment: Dsk1 phosphorylates Rad52 in vitro and in vivo).
PMID:39789818	PBO:0120026	We also purified 6His-Rad52-S365A and 6His-Rad52-S367A proteins and found that the abundance of the phosphorylated peptide of Rad52-S367A was significantly higher than that of Rad52-S365A when incubated with GST- Dsk1 (Figure 4f,g). Together, these in vitro data strongly indicate that Dsk1 directly phosphorylates Rad52-Ser365. Together, these results suggest that Dsk1-mediated Rad52-Ser365 phosphorylation is probably one of the mechanisms for Dsk1 regulating HR repair.
PMID:39789818	PBO:0120027	We found that the levels of the indicated phosphorylated peptide of Rad52-YFP were substantially reduced in dsk1Δ, whereas no differences in the levels of unmodified peptides (Figure 4h). The remaining Rad52 phosphorylation in dsk1Δ suggests that there are redundant kinases of Rad52 in vivo. Moreover, Ser319 was predicted as the major phosphorylated residue in this indicated Rad52 peptide (Figure 4h).
PMID:39789818	PBO:0093616	The results of spot assays revealed that rad52Δ strain as a positive control grew slowly and exhibited pronounced sensitivities to all tested drugs. FIGURE 5 | The defective genotoxic and HR phenotypes of Rad52-Ser365 phosphorylation-defective and -mimicking mutants
PMID:39789818	PBO:0114146	Furthermore, a high percentage of spontaneous Rad52-YFP foci was observed in rad52-S365D-YFP, but not in rad52-YFP and rad52-S365A-YFP, suggesting genomic instability of rad52- S365D-YFP.
PMID:39789818	PBO:0093613	When combined with dsk1Δ, obviously synthetic effects were observed for CPT treatment, and slightly additive effects were observed for HU and MMS treatment (Figure 5a)
PMID:39789818	PBO:0093613	When combined with dsk1Δ, obviously synthetic effects were observed for CPT treatment, and slightly additive effects were observed for HU and MMS treatment (Figure 5a)
PMID:39789818	PBO:0093618	We then overexpressed dsk1+ from the constitutive adh21 promoter with medium strength at the lys1 locus of S. pombe genome (Chen et al. 2017). This made the cells highly sensitive to CPT and marginally sensitive to MMS (Figure 1g).
PMID:39789818	FYPO:0003912	As expected, the HR frequency of leu1 integration in rad51Δ cells was too low to be displayed. We also found that the HR frequency of leu1 integration in dsk1Δ cells was significantly reduced (Figure 2c), suggesting that Dsk1 may regulate the Rad52- and Rad51-dependent gene conversion sub-pathway of HR.
PMID:39789818	FYPO:0000829	Consistent with the phenotypes of deficiency of SKY1 and SRPKs, dsk1Δ also exhibited cisPt resistance.........(Figure 1a and Figure S1c).
PMID:39789818	PBO:0120028	We found that the association affinity between Rad52-YFP and Rad51 was marginally affected by dsk1Δ (Figure S7b).
PMID:39789818	PBO:0093579	In addition, dsk1Δ was consistently but marginally sensitive to HU. .........(Figure 1a and Figure S1c).
PMID:39789818	PBO:0093613	We then overexpressed dsk1+ from the constitutive adh21 promoter with medium strength at the lys1 locus of S. pombe genome (Chen et al. 2017). This made the cells highly sensitive to CPT and marginally sensitive to MMS (Figure 1g).
PMID:39789818	PBO:0093614	In line with this, the spacer truncation mutant was also sensitive to CPT (Figure 1e).
PMID:39789818	PBO:0093614	It showed CPT sensitivity compared with its isogenic dsk1-5FLAG control, but not as severe as dsk1Δ (Figure 1d). To avoid the negative effects of the FLAG tag, we created a dsk1-K110A mutant without the tag, and it also showed the sensitivity of CPT (Figure S1e)
PMID:39789818	FYPO:0007074	However, dsk1Δ was not sensitive to Bleomycin (Bleo), Phleomycin (Phleo), and UV irradiation, which directly break DNA, as well as 6-Azauracil (6-AU) and Mycophenolic acid (MPA), which impair transcription (Figure S1d).
PMID:39789818	FYPO:0005517	However, dsk1Δ was not sensitive to Bleomycin (Bleo), Phleomycin (Phleo), and UV irradiation, which directly break DNA, as well as 6-Azauracil (6-AU) and Mycophenolic acid (MPA), which impair transcription (Figure S1d).
PMID:39789818	PBO:0093613	When combined with dsk1Δ, obviously synthetic effects were observed for CPT treatment, and slightly additive effects were observed for HU and MMS treatment (Figure 5a)
PMID:39789818	PBO:0093613	When combined with dsk1Δ, obviously synthetic effects were observed for CPT treatment, and slightly additive effects were observed for HU and MMS treatment (Figure 5a)
PMID:39789818	PBO:0093613	When combined with dsk1Δ, obviously synthetic effects were observed for CPT treatment, and slightly additive effects were observed for HU and MMS treatment (Figure 5a)
PMID:39789818	PBO:0093613	When combined with dsk1Δ, obviously synthetic effects were observed for CPT treatment, and slightly additive effects were observed for HU and MMS treatment (Figure 5a)
PMID:39789818	PBO:0093617	Moreover, the rad52-S365D/E-YFP displayed higher sensitivities to HU, CPT, and MMS rather than cisPt (Figure 5a).
PMID:39789818	PBO:0093617	Moreover, the rad52-S365D/E-YFP displayed higher sensitivities to HU, CPT, and MMS rather than cisPt (Figure 5a).
PMID:39789818	PBO:0093581	Moreover, the rad52-S365D/E-YFP displayed higher sensitivities to HU, CPT, and MMS rather than cisPt (Figure 5a).
PMID:39789818	PBO:0093581	Moreover, the rad52-S365D/E-YFP displayed higher sensitivities to HU, CPT, and MMS rather than cisPt (Figure 5a).
PMID:39789818	PBO:0094311	The results of spot assays revealed that rad52Δ strain as a positive control grew slowly and exhibited pronounced sensitivities to all tested drugs. FIGURE 5 | The defective genotoxic and HR phenotypes of Rad52-Ser365 phosphorylation-defective and -mimicking mutants
PMID:39789818	PBO:0093580	The results of spot assays revealed that rad52Δ strain as a positive control grew slowly and exhibited pronounced sensitivities to all tested drugs. FIGURE 5 | The defective genotoxic and HR phenotypes of Rad52-Ser365 phosphorylation-defective and -mimicking mutants
PMID:39789818	PBO:0093613	The results of spot assays revealed that rad52Δ strain as a positive control grew slowly and exhibited pronounced sensitivities to all tested drugs. FIGURE 5 | The defective genotoxic and HR phenotypes of Rad52-Ser365 phosphorylation-defective and -mimicking mutants
PMID:39789818	PBO:0093615	The rad52-S365A-YFP was slightly sensitive to HU and CPT, but not to MMS and cisPt.
PMID:39789818	PBO:0093579	The rad52-S365A-YFP was slightly sensitive to HU and CPT, but not to MMS and cisPt.
PMID:39789818	FYPO:0001023	The rad52-S365A-YFP was slightly sensitive to HU and CPT, but not to MMS and cisPt.
PMID:39789818	FYPO:0000957	The rad52-S365A-YFP was slightly sensitive to HU and CPT, but not to MMS and cisPt.
PMID:39789818	FYPO:0000969	However, dsk1Δ was not sensitive to Bleomycin (Bleo), Phleomycin (Phleo), and UV irradiation, which directly break DNA, as well as 6-Azauracil (6-AU) and Mycophenolic acid (MPA), which impair transcription (Figure S1d).
PMID:39789818	FYPO:0003183	However, dsk1Δ was not sensitive to Bleomycin (Bleo), Phleomycin (Phleo), and UV irradiation, which directly break DNA, as well as 6-Azauracil (6-AU) and Mycophenolic acid (MPA), which impair transcription (Figure S1d).
PMID:39789818	PBO:0093614	Moreover, the rad52-S365D/E-YFP displayed higher sensitivities to HU, CPT, and MMS rather than cisPt (Figure 5a).
PMID:39878217	FYPO:0000085	(Fig. 1E)
PMID:39878217	FYPO:0000963	(Fig. 6E)
PMID:39878217	FYPO:0000963	(Fig. 6E)
PMID:39878217	FYPO:0001357	(Fig. S3D)
PMID:39878217	FYPO:0001357	(Fig. S3C, S3D)
PMID:39878217	FYPO:0001357	(Fig. S3C, S3D)
PMID:39878217	PBO:0093560	(Fig. S3C, S3D)
PMID:39878217	FYPO:0001357	(Fig. S3C, S3D)
PMID:39878217	FYPO:0001357	(Fig. S3C, S3D)
PMID:39878217	FYPO:0003247	(Fig. S3B)
PMID:39878217	FYPO:0003247	(Fig. S3B)
PMID:39878217	FYPO:0007158	(Fig. S3A)
PMID:39878217	FYPO:0007158	(Fig. 2E)
PMID:39878217	FYPO:0007158	(Fig. 2E)
PMID:39878217	FYPO:0008272	(Fig. 2E)
PMID:39878217	FYPO:0008272	(Fig. 2E)
PMID:39878217	FYPO:0003247	(Fig. 2E)
PMID:39878217	FYPO:0003247	(Fig. 2E)
PMID:39878217	FYPO:0003247	(Fig. 2E)
PMID:39878217	FYPO:0005751	(Fig. S7G)
PMID:39878217	FYPO:0005751	(Fig. S7G)
PMID:39878217	FYPO:0001690	(Fig. S7G)
PMID:39878217	FYPO:0001690	(Fig. S7G)
PMID:39878217	FYPO:0000957	(Fig. S7G)
PMID:39878217	FYPO:0000957	(Fig. S7G)
PMID:39878217	PBO:0102212	(Fig. S7G)
PMID:39878217	PBO:0093613	(Fig. S7G)
PMID:39878217	PBO:0093616	(Fig. S7G)
PMID:39878217	FYPO:0001357	(Fig. S7E)
PMID:39878217	PBO:0093560	(Fig. 5F)
PMID:39878217	PBO:0093560	(Fig. 5F)
PMID:39878217	PBO:0093559	(Fig. 5F)
PMID:39878217	PBO:0093556	(Fig. 5E)
PMID:39878217	PBO:0093558	(Fig. 5E)
PMID:39878217	FYPO:0008392	(Fig. 5A)
PMID:39878217	FYPO:0008392	(Fig. 5A)
PMID:39878217	FYPO:0005336	(Fig. 5A)
PMID:39878217	FYPO:0005336	(Fig. 5A)
PMID:39878217	FYPO:0007324	(Fig. 5A)
PMID:39878217	FYPO:0004578	(Fig. 5A)
PMID:39878217	PBO:0119312	(Fig. 4C, 4D)
PMID:39878217	PBO:0119311	(Fig. 4C, 4D)
PMID:39878217	PBO:0093560	(Fig. 3I)
PMID:39878217	PBO:0093560	(Fig. S3D)
PMID:39878217	PBO:0105880	(Fig. 1F)
PMID:39878217	PBO:0105880	(Fig. 1F)
PMID:39878217	PBO:0105880	(Fig. 1F)
PMID:39878217	FYPO:0008160	(Fig. 1F)
PMID:39878217	FYPO:0001690	(Fig. 1E)
PMID:39878217	FYPO:0000085	(Fig. 1E)
PMID:39878217	FYPO:0000089	(Fig. 1E)
PMID:39878217	PBO:0093581	(Fig. 1E)
PMID:39878217	FYPO:0001357	(Fig. 1E)
PMID:39878217	PBO:0093581	(Fig. 1E)
PMID:39878217	FYPO:0000089	(Fig. 1E)
PMID:39878217	FYPO:0000085	(Fig. 1E)
PMID:39878217	FYPO:0001357	(Fig. 1E)
PMID:39878217	FYPO:0000089	(Fig. 1E)
PMID:39878217	FYPO:0001357	(Fig. 1E)
PMID:39878217	PBO:0093581	(Fig. 1E)
PMID:39878217	PBO:0093581	(Fig. 1E)
PMID:39878217	FYPO:0001357	(Fig. 4A)
PMID:39878217	FYPO:0001357	(Fig. 4A)
PMID:39878217	FYPO:0001357	(Fig. 1B)
PMID:39878217	FYPO:0001357	(Fig. S3D)
PMID:39878217	FYPO:0001357	(Fig. 1B)
PMID:39878217	FYPO:0000957	(Fig. 1E)
PMID:39878217	FYPO:0001690	(Fig. 1E)
PMID:39878217	PBO:0119310	(Fig. 2)
PMID:39878217	PBO:0119309	(Fig. 2)
PMID:39878217	PBO:0119308	(Fig. 2)
PMID:39878217	PBO:0119307	(Fig. 2)
PMID:39878217	PBO:0119306	(Fig. 2)
PMID:39878217	PBO:0119305	(Fig. 2)
PMID:39878217	GO:0036205	Our study reveals that as a binding protein for the histone H3-H4 dimer, Djc9 acts with Hsp70 to promote the proteasomal degradation of excess histones. Its activity is restrained by the competitive binding of H3-H4 by Asf1, whose essential function in fission yeast is restricting histone degradation by Djc9. (Fig. 5 and Fig. 6)
PMID:39878217	FYPO:0004481	(Fig. S7E)
PMID:39878217	FYPO:0001357	(Fig. S1E)
PMID:39878217	PBO:0093579	(Fig. 1E, Fig. 6A, 6E)
PMID:39878217	FYPO:0001357	(Fig. S3D)
PMID:39878217	FYPO:0001357	(Fig. S3D)
PMID:39878217	PBO:0093560	(Fig. 7A)
PMID:39878217	PBO:0093560	(Fig. 7A)
PMID:39878217	FYPO:0000674	(Fig. S7E)
PMID:39878217	FYPO:0000674	(Fig. S7E)
PMID:39878217	FYPO:0000674	(Fig. S1E)
PMID:39878217	FYPO:0000674	(Fig. S1E)
PMID:39878217	FYPO:0000674	(Fig. S1E)
PMID:39878217	FYPO:0000674	(Fig. S1E)
PMID:39878217	PBO:0105880	(Fig. 1F)
PMID:39878217	FYPO:0002336	(Fig. S7B)
PMID:39878217	FYPO:0001357	(Fig. S3D)
PMID:39878217	FYPO:0001357	(Fig. S3D)
PMID:39878217	FYPO:0002336	(Fig. S7B)
PMID:39878217	FYPO:0004742	(Fig. S7A)
PMID:39878217	FYPO:0004742	(Fig. S7A)
PMID:39878217	FYPO:0000088	(Fig. S6A)
PMID:39878217	FYPO:0000088	(Fig. S6A)
PMID:39878217	FYPO:0000089	(Fig. 1E)
PMID:39878217	FYPO:0002061	(Fig. 1B)
PMID:39878217	PBO:0093561	(Fig. S3D)
PMID:39878217	PBO:0093559	(Fig. S3D)
PMID:39878217	PBO:0093559	(Fig. S3D)
PMID:39878217	FYPO:0001357	(Fig. S7E)
PMID:39878217	PBO:0093561	(Fig. S7E)
PMID:39878217	FYPO:0005751	(Fig. S7D)
PMID:39878217	FYPO:0005750	(Fig. S7D)
PMID:39878217	FYPO:0002336	(Fig. S7B)
PMID:39878217	PBO:0095653	(Fig. S7B)
PMID:39878217	PBO:0105770	(Fig. S7A)
PMID:39878217	FYPO:0006992	(Fig. S7A)
PMID:39878217	PBO:0093560	(Fig. S5F)
PMID:39878217	PBO:0093560	(Fig. S5F)
PMID:39878217	PBO:0093561	(Fig. S5E, S5F)
PMID:39878217	PBO:0093559	(Fig. S5E)
PMID:39878217	FYPO:0001357	(Fig. 3I)
PMID:39878217	PBO:0119313	(Fig. S1G)
PMID:39878217	PBO:0119313	(Fig. S1G)
PMID:39878217	PBO:0093558	(Fig. S1E)
PMID:39878217	FYPO:0000674	(Fig. S1E)
PMID:39878217	PBO:0093579	(Fig. 6E)
PMID:39878217	FYPO:0008391	(Fig. 6B)
PMID:39878217	FYPO:0008390	(Fig. 6B)
PMID:39880258	PBO:0098732	(kcat) was computed as 9.08 s-1. The Michaelis-Menten constant, KM was determined as 0.65 × 101 μM with a maximum velocity (Vmax) of 0.045 μM/s. The substrate specificity ratio, kcat/KM was calculated to be 1.39 × 106 M-1 s-1.
PMID:39910760	PBO:0117220	We investigated the effect of phosphorylation mutations of Ecl1 on the binding of TORC1 subunit Mip1 to Ecl1 (Figure 5i). Mip1-HA protein did not coprecipitate with GFP but did coprecipitate wild-type Ecl1 and with Ecl1 proteins with mutations at Thr7 or Ser22.
PMID:39910760	PBO:0105134	Furthermore, the Ecl1-overexpression reduced TORC1 activity regardless of the presence or absence of sulfur (Figure 5e,f). In other words, even during the logarithmic growth phase, when Thr7 is phosphorylated and Ecl function is suppressed, Ecl1 overexpression sufficiently reduces TORC1 activity. These results indicated that phosphorylation of the N-terminus of Ecl1 had little effect on TORC1 repression and that the expression of Ecl1, rather than starvation conditions, was important for TORC1 repression.
PMID:39910760	PBO:0105134	Furthermore, the Ecl1-overexpression reduced TORC1 activity regardless of the presence or absence of sulfur (Figure 5e,f). In other words, even during the logarithmic growth phase, when Thr7 is phosphorylated and Ecl function is suppressed, Ecl1 overexpression sufficiently reduces TORC1 activity. These results indicated that phosphorylation of the N-terminus of Ecl1 had little effect on TORC1 repression and that the expression of Ecl1, rather than starvation conditions, was important for TORC1 repression.
PMID:39910760	PBO:0117240	Ecl1, which physically interacts with Mip1, reduces TORC1 activity regardless of Thr7 mutation
PMID:39910760	PBO:0105131	TORC1 activity was reported to decrease in an ecl gene-dependent manner under conditions of sulfur or phosphate starvation (Ohtsuka et al., 2022a, 2023c) (Figure 5a).
PMID:39910760	PBO:0117218	This suggested that phosphorylation of the N-terminus of Ecl1 was unlikely to significantly affect the intracellular localization of Ecl1.
PMID:39910760	PBO:0117220	We investigated the effect of phosphorylation mutations of Ecl1 on the binding of TORC1 subunit Mip1 to Ecl1 (Figure 5i). Mip1-HA protein did not coprecipitate with GFP but did coprecipitate wild-type Ecl1 and with Ecl1 proteins with mutations at Thr7 or Ser22.
PMID:39910760	PBO:0100665	If CLS extension by Ecl1 is mediated by the same pathway as TORC1, no additive CLS extension would be observed if Ecl1 was overexpressed in a TORC1 subunit-deficient cell. Although wat1+ deletion or ecl1+ overexpression extended the CLS, overexpression of ecl1+ in the wat1-deficient cells did not result in further CLS extension, suggesting that Ecl1 and Wat1 function in CLS extension through the same pathway. (However, because Wat1 is a component of TORC1 and TORC2 (Ahamad et al., 2018), further experiments are required to clarify whether Ecl1-induced CLS extension is exclusively mediated by TORC1)
PMID:39910760	PBO:0117218	This suggested that phosphorylation of the N-terminus of Ecl1 was unlikely to significantly affect the intracellular localization of Ecl1.
PMID:39910760	GO:0005737	To investigate this, we observed the intracellular localization of the Ecl1-GFP fusion protein (Figure 4a). Regardless of mutations at Thr7 and Ser22, the Ecl1-GFP fusion protein was mainly localized in the nucleus during logarithmic growth and was also observed in the cytoplasm.
PMID:39910760	GO:0005634	To investigate this, we observed the intracellular localization of the Ecl1-GFP fusion protein (Figure 4a). Regardless of mutations at Thr7 and Ser22, the Ecl1-GFP fusion protein was mainly localized in the nucleus during logarithmic growth and was also observed in the cytoplasm.
PMID:39910760	FYPO:0000708	This suggested that the Ecl1-AA mutant protein activity was comparable to that of the wild-type Ecl1 protein. Meanwhile, when Ecl1-DD was expressed, the recovery was low, and the degree of recovery was significantly lower than that of Ecl1 and Ecl1-AA. This suggested that the activity or stability of the Ecl1-DD mutant protein, which mimics the phosphorylation of Thr7 and Ser22, was reduced compared with the wild-type Ecl1 protein. (comment: (vw: there was no WT assay, but compared to WT in the same background))
PMID:39910760	PBO:0117217	First, we investigated the conjugation rate in the stationary phase. Overexpression of wild-type Ecl1 and Ecl1-22D, but not the empty vector or Ecl1-7D, rescued the conjugation defect in the stationary phase of Δecls cells (Figure 3b), suggesting a significant loss of activity in Ecl1-7D.
PMID:39910760	FYPO:0005097	The number of cells in the G1 phase was considerably reduced in cells harboring pE- cl1-DD (Figure 2e)..
PMID:39910760	FYPO:0004085	In addition, Ecl1 fusion protein overexpression slowed the growth rate, similar to a previous report of Ecl1- overexpression (Ohtsuka et al., 2024a) (Figure 1c).
PMID:39910760	PBO:0093825	This suggested that the Ecl1-AA mutant protein activity was comparable to that of the wild-type Ecl1 protein. Meanwhile, when Ecl1-DD was expressed, the recovery was low, and the degree of recovery was significantly lower than that of Ecl1 and Ecl1-AA. This suggested that the activity or stability of the Ecl1-DD mutant protein, which mimics the phosphorylation of Thr7 and Ser22, was reduced compared with the wild-type Ecl1 protein. (comment: (vw: there was no WT assay, but compared to WT in the same background))
PMID:39910760	FYPO:0000708	This suggested that the Ecl1-AA mutant protein activity was comparable to that of the wild-type Ecl1 protein. Meanwhile, when Ecl1-DD was expressed, the recovery was low, and the degree of recovery was significantly lower than that of Ecl1 and Ecl1-AA. This suggested that the activity or stability of the Ecl1-DD mutant protein, which mimics the phosphorylation of Thr7 and Ser22, was reduced compared with the wild-type Ecl1 protein. (comment: (vw: there was no WT assay, but compared to WT in the same background))
PMID:39910760	PBO:0117217	When Δecls cells were cultured in EMM, mating did not occur, not even in the stationary phase, but this defect was restored by the expression of wild-type Ecl1 or Ecl1-AA proteins by plasmids (Figure 2b).
PMID:39910760	FYPO:0004085	In addition, Ecl1 fusion protein overexpression slowed the growth rate, similar to a previous report of Ecl1- overexpression (Ohtsuka et al., 2024a) (Figure 1c).
PMID:39910760	FYPO:0001309	Furthermore, the overexpression of the Ecl1 fusion protein using this plasmid led to CLS extension, suggesting that the protein was functional (Figure 1c).
PMID:39910760	PBO:0117216	GST protein purified from cultures under each condition revealed the phosphorylation of Thr7, Ser22, Ser61, Thr63, and Thr69 of Ecl1 protein in the nutrient-rich environment (Figure 1d; Figure S1). Under conditions of sulfur or metal starvation,...... but those of Thr7 and Ser22 (situated near the N-terminus) decreased.
PMID:39910760	PBO:0117215	GST protein purified from cultures under each condition revealed the phosphorylation of Thr7, Ser22, Ser61, Thr63, and Thr69 of Ecl1 protein in the nutrient-rich environment (Figure 1d; Figure S1). Under conditions of sulfur or metal starvation,...... but those of Thr7 and Ser22 (situated near the N-terminus) decreased.
PMID:39910760	PBO:0103668	If CLS extension by Ecl1 is mediated by the same pathway as TORC1, no additive CLS extension would be observed if Ecl1 was overexpressed in a TORC1 subunit-deficient cell. Although wat1+ deletion or ecl1+ overexpression extended the CLS, overexpression of ecl1+ in the wat1-deficient cells did not result in further CLS extension, suggesting that Ecl1 and Wat1 function in CLS extension through the same pathway.
PMID:39910760	PBO:0100665	If CLS extension by Ecl1 is mediated by the same pathway as TORC1, no additive CLS extension would be observed if Ecl1 was overexpressed in a TORC1 subunit-deficient cell. Although wat1+ deletion or ecl1+ overexpression extended the CLS, overexpression of ecl1+ in the wat1-deficient cells did not result in further CLS extension, suggesting that Ecl1 and Wat1 function in CLS extension through the same pathway.
PMID:39916665	PBO:0093558	(Fig. 1C)
PMID:39916665	FYPO:0004710	(Fig. S2)
PMID:39916665	FYPO:0001357	(Fig. S1A)
PMID:39916665	FYPO:0001357	(Fig. S1A)
PMID:39916665	PBO:0093560	(Fig. S1A)
PMID:39916665	PBO:0093558	(Fig. S1A)
PMID:39916665	FYPO:0009007	(Fig. 2A)
PMID:39916665	FYPO:0001357	(Fig. 1C)
PMID:39916665	FYPO:0001357	(Fig. 1C)
PMID:39916665	FYPO:0001357	(Fig. 1C)
PMID:39916665	PBO:0117462	(Fig. S3)
PMID:39916665	PBO:0117461	(Fig. S3)
PMID:39916665	PBO:0093558	(Fig. S1A)
PMID:39916665	PBO:0093558	(Fig. S1A)
PMID:39916665	FYPO:0000674	(Fig. 1C)
PMID:39916665	FYPO:0000674	(Fig. 1C)
PMID:39916665	PBO:0117460	(Fig. 4C, 4D)
PMID:39916665	PBO:0105459	(Fig. 4C, 4D)
PMID:39916665	PBO:0117459	(Fig. 3C, 3D)
PMID:39916665	PBO:0117458	(Fig. 3C, 3D)
PMID:39945308	PBO:0119781	(Fig. 4F)
PMID:39945308	PBO:0119782	(Fig. 4F)
PMID:39945308	PBO:0119783	(Fig. 4F)
PMID:39945308	PBO:0119783	(Fig. 4F)
PMID:39945308	PBO:0111026	(Fig. S1E)
PMID:39945308	FYPO:0002336	(Fig. 4D and 4E)
PMID:39945308	PBO:0095651	(Fig. 4D and 4E)
PMID:39945308	PBO:0095652	(Fig. 4C and 4E)
PMID:39945308	PBO:0095652	(Fig. 4C and 4E)
PMID:39945308	PBO:0112031	(Fig. 1F)
PMID:39945308	PBO:0095651	(Fig. 4C and 4E)
PMID:39945308	FYPO:0007334	(Fig. 1F)
PMID:39945308	PBO:0112031	(Fig. 1F)
PMID:39945308	PBO:0111026	(Fig. 1C)
PMID:39945308	FYPO:0002336	(Fig. 4C, 4D and 4E)
PMID:39945308	PBO:0095651	(Fig. 4D and 4E)
PMID:39945308	PBO:0119780	(Fig. 1D)
PMID:39945308	PBO:0119781	(Fig. 4F)
PMID:40015273	PBO:0119269	(Figure 7) (comment: CHECK decreased localization of chromatin region to nuclear periphery)
PMID:40015273	GO:0031491	Although histones were abundantly pulled down in all low stringency IPs, including the untagged control, this interaction was uniquely preserved for Pap1 and the heterodimeric TFs Atf1 and Pcr1 amongst TFs investigated under high stringency conditions (Figure 5C, Figure S5C)
PMID:40015273	PBO:0119268	Notably, Rad24 is known to negatively regulate Pho7- dependent pho1+ expression, with its deletion resulting in increased pho1+ levels even under phosphate-replete conditions82-84. Mechanistically, Rad24 has been linked to the regulation of an upstream long non-coding RNA (lncRNA), which is known to interfere with pho1+ expression in the absence of stress84,85. Our data suggests an alternative mechanism where Rad24, and potentially Rad25, directly interact with and negatively regulate Pho7, which would explain the de-repression of pho1+ in rad24Δ mutants. We identified two optimal 14-3-3 binding motifs78 in Pho7, corresponding to phosphorylated serine and threonine residues (RVCSAP (pS230) and RSFTNP (pT463))86-89 (Figure 6B). These motifs flank the Pho7 DBD, indicating that Rad24/Rad25 interactions could interfere with Pho7 DNA binding, similar to the mechanism proposed for the mammalian TF FOXO4
PMID:40015273	PBO:0119268	Notably, Rad24 is known to negatively regulate Pho7- dependent pho1+ expression, with its deletion resulting in increased pho1+ levels even under phosphate-replete conditions82-84. Mechanistically, Rad24 has been linked to the regulation of an upstream long non-coding RNA (lncRNA), which is known to interfere with pho1+ expression in the absence of stress84,85. Our data suggests an alternative mechanism where Rad24, and potentially Rad25, directly interact with and negatively regulate Pho7, which would explain the de-repression of pho1+ in rad24Δ mutants. We identified two optimal 14-3-3 binding motifs78 in Pho7, corresponding to phosphorylated serine and threonine residues (RVCSAP (pS230) and RSFTNP (pT463))86-89 (Figure 6B). These motifs flank the Pho7 DBD, indicating that Rad24/Rad25 interactions could interfere with Pho7 DNA binding, similar to the mechanism proposed for the mammalian TF FOXO4
PMID:40015273	GO:0031491	Although histones were abundantly pulled down in all low stringency IPs, including the untagged control, this interaction was uniquely preserved for Pap1 and the heterodimeric TFs Atf1 and Pcr1 amongst TFs investigated under high stringency conditions (Figure 5C, Figure S5C)
PMID:40015273	GO:0031491	Although histones were abundantly pulled down in all low stringency IPs, including the untagged control, this interaction was uniquely preserved for Pap1 and the heterodimeric TFs Atf1 and Pcr1 amongst TFs investigated under high stringency conditions (Figure 5C, Figure S5C)
PMID:40015273	PBO:0119269	(Figure 7) (comment: CHECK decreased localization of chromatin region to nuclear periphery)
PMID:40063661	PBO:0120671	(Table S2)
PMID:40063661	PBO:0120646	(Fig. 5A, 5B, 5E)
PMID:40063661	PBO:0120661	(Table S1)
PMID:40063661	FYPO:0007322	(Fig. 5D, 5E)
PMID:40063661	FYPO:0007322	(Fig. 5D, 5E)
PMID:40063661	FYPO:0007322	(Fig. 5D, 5E)
PMID:40063661	FYPO:0007323	(Fig. 4D, 4E)
PMID:40063661	FYPO:0007323	(Fig. 4D, 4E)
PMID:40063661	PBO:0120672	(Fig. 7D)
PMID:40063661	GO:0034063	(Fig 4D and 4E). Hence like their human orthologs, Cpn1 and Nxt3 are required to promote stress granule formation.
PMID:40063661	GO:0034063	(Fig 4D and 4E). Hence like their human orthologs, Cpn1 and Nxt3 are required to promote stress granule formation.
PMID:40063661	PBO:0120670	(Table S2)
PMID:40063661	PBO:0120669	(Table S2)
PMID:40063661	FYPO:0007322	(Fig. 4D, 4E)
PMID:40063661	FYPO:0007322	(Fig. 4D, 4E)
PMID:40063661	PBO:0037494	(Fig. 4B)
PMID:40063661	PBO:0037494	(Fig. 4B)
PMID:40063661	PBO:0037494	(Fig. 4A)
PMID:40063661	FYPO:0004744	(Fig. 3E)
PMID:40063661	FYPO:0004744	(Fig. 3E)
PMID:40063661	FYPO:0004744	(Fig. 3E)
PMID:40063661	FYPO:0004744	(Fig. 2A, 3E)
PMID:40063661	PBO:0120645	(Fig. 2H)
PMID:40063661	PBO:0120645	(Fig. 2H)
PMID:40063661	PBO:0120644	(Fig. 2H)
PMID:40063661	PBO:0120660	(Table S1)
PMID:40063661	PBO:0120659	(Table S1)
PMID:40063661	PBO:0120658	(Table S1)
PMID:40063661	PBO:0120657	(Table S1)
PMID:40063661	PBO:0120656	(Table S1)
PMID:40063661	PBO:0120655	(Table S1)
PMID:40063661	PBO:0120654	(Table S1)
PMID:40063661	PBO:0113664	(Table S1)
PMID:40063661	PBO:0094685	(Fig. S8D)
PMID:40063661	PBO:0097227	(Fig. 7C)
PMID:40063661	PBO:0094685	(Fig. 7A, 7B)
PMID:40063661	FYPO:0002350	(Fig. 5B)
PMID:40063661	FYPO:0002350	(Fig. 5B)
PMID:40063661	PBO:0120653	(Fig. 5B)
PMID:40063661	PBO:0120653	(Fig. 5B)
PMID:40063661	PBO:0120644	(Fig. 2H)
PMID:40063661	PBO:0120643	(Fig. 2H)
PMID:40063661	FYPO:0004749	(Fig. S4)
PMID:40063661	FYPO:0007226	(Fig. S2A)
PMID:40063661	PBO:0120642	(Fig. 2G)
PMID:40063661	FYPO:0007322	(Fig. 4D, 4E)
PMID:40063661	PBO:0120642	(Fig. 2G)
PMID:40063661	PBO:0120642	(Fig. 2G)
PMID:40063661	PBO:0120642	(Fig. 2G)
PMID:40063661	PBO:0120641	(Fig. 1E)
PMID:40063661	PBO:0120640	(Fig. 1E)
PMID:40063661	PBO:0120639	(Fig. 3F)
PMID:40063661	PBO:0108818	(Table S2)
PMID:40063661	PBO:0110728	(Table S2)
PMID:40063661	PBO:0108857	(Table S2)
PMID:40063661	PBO:0108801	(Table S2)
PMID:40063661	PBO:0108843	(Table S2)
PMID:40063661	PBO:0120668	(Table S2)
PMID:40063661	PBO:0120667	(Table S2)
PMID:40063661	PBO:0120666	(Table S2)
PMID:40063661	PBO:0120665	(Table S2)
PMID:40063661	PBO:0114658	(Table S2)
PMID:40063661	PBO:0110727	(Table S2)
PMID:40063661	PBO:0120664	(Table S2)
PMID:40063661	PBO:0120638	(Fig. 1E)
PMID:40063661	PBO:0120637	(Fig. 7E)
PMID:40063661	PBO:0120636	(Fig. 3F)
PMID:40063661	PBO:0120663	(Table S1)
PMID:40063661	PBO:0120662	(Table S1)
PMID:40063661	PBO:0120635	(Fig. 2H, 3F)
PMID:40063661	PBO:0120634	(Fig. 1F)
PMID:40063661	PBO:0120633	(Fig. 1F)
PMID:40063661	PBO:0120632	(Fig. 1F)
PMID:40063661	PBO:0120631	(Fig. 2A, 2C, 2D)
PMID:40063661	PBO:0120652	(Fig. 4A)
PMID:40063661	PBO:0021023	(Fig. 4A)
PMID:40063661	PBO:0120651	(Fig. S8A)
PMID:40063661	PBO:0120651	(Fig. 6C)
PMID:40063661	PBO:0120650	(Fig. 6D)
PMID:40063661	PBO:0094684	(Fig. S8B, S8C)
PMID:40063661	PBO:0094684	(Fig. S8B, S8C)
PMID:40063661	PBO:0094684	(Fig. S8D)
PMID:40063661	FYPO:0008414	(Fig. S7B, S7C)
PMID:40063661	FYPO:0008414	(Fig. S7B, S7C)
PMID:40063661	FYPO:0008414	(Fig. S7B, S7C)
PMID:40063661	FYPO:0008415	(Fig. 7F)
PMID:40063661	PBO:0120649	(Fig. 7D)
PMID:40063661	PBO:0094684	(Fig. 7C)
PMID:40063661	PBO:0094685	(Fig. 7C)
PMID:40063661	PBO:0094684	(Fig. 7C)
PMID:40063661	PBO:0094684	(Fig. 7A, 7B)
PMID:40063661	PBO:0094684	(Fig. 7A, 7B)
PMID:40063661	PBO:0094684	(Fig. 7A, 7B)
PMID:40063661	PBO:0094684	(Fig. 7A, 7B)
PMID:40063661	PBO:0120648	(Fig. 5A, 5B, 5E)
PMID:40063661	PBO:0120647	(Fig. 5A, 5B, 5E)
PMID:40093821	FYPO:0001309	(Fig. 1A-D)
PMID:40093821	PBO:0119776	(Fig. 1E)
PMID:40093821	PBO:0119775	(Fig. 1F)
PMID:40124504	GO:0005789	Like Oca3, localization of fluorescently tagged constructs of the putative orthologous S. pombe Emc3 (Pombase: ID SPBC1711.03), Emc5 (Pombase: ID SPAP4C9.02) and Emc6 (Pombase: ID SPCC1020.11c) is consistent with the ER structure in all these EMC subunits.
PMID:40124504	GO:0005789	Like Oca3, localization of fluorescently tagged constructs of the putative orthologous S. pombe Emc3 (Pombase: ID SPBC1711.03), Emc5 (Pombase: ID SPAP4C9.02) and Emc6 (Pombase: ID SPCC1020.11c) is consistent with the ER structure in all these EMC subunits.
PMID:40124504	PBO:0119865	As shown in Figure 1C, depletion of Oca3 leads to loss of Emc3, aggregation of Emc5, and normal ER localization, but reduced fluorescence levels of EMC6, revealing the requirement of Oca3 for the assembly of a functional EMC complex.
PMID:40124504	PBO:0119866	(comment: CHECK XXXXXX CHANGE TO ABOLISHED XXXXXXX) As shown in Figure 1C, depletion of Oca3 leads to loss of Emc3, aggregation of Emc5, and normal ER localization, but reduced fluorescence levels of EMC6, revealing the requirement of Oca3 for the assembly of a functional EMC complex.
PMID:40124504	FYPO:0003766	however, clumps of mitochondrial DNA (mtDNA) were present in the cytoplasm of these mutant cells (Figure 2A).
PMID:40124504	FYPO:0003769	Quantitative PCR analysis of target mtDNA sequences determined a 28% reduction in mtDNA molecules per cell in the mutant strain at 30C, exacerexacerbated at low temperature (37% reduction at 20C) (Figure 2B).
PMID:40124504	GO:0140268	In agreement with its localization in ER-PM and ER-vesicles previously described in fission yeast,17 Ltc1-GFP localizes to cortical and internal dots in the ER in wild-type cells (arrows in Figure 3), but MitoHealth co-localization indicates that this protein is also associated to ER-Mitochondrial contact sites in S. pombe cells (Figures 3 and S2), as reported in S. cerevisiae cells.24
PMID:40124504	FYPO:0005838	In comparison to wild-type cells, Oca3/Emc2 depletion results in a condensed mitochondrial structure that co-localize with abnormal mtDNA aggregations (Figure 2C).
PMID:40124504	FYPO:0003004	The accumulation of reactive oxygen species (ROS) is associated to mitochondrial dysfunctions.18 Remarkably, proliferating Oca3-depleted cells (at 30C) reach ROS levels similar to those found in wild-type cells subjected to oxidative stress (H2O2 treatment), indicating that EMC-deficient cells suffer mitochondrial stress (Figures S1A and S1B).
PMID:40124504	GO:0005789	As expected for an EMC component, in vivo fluorescence microscopy shows that Oca3-mCherry localizes to the ER (Figure 1A), co-localizing with the ER-reporter ADEL-GFP.
PMID:40124504	GO:0044233	In agreement with its localization in ER-PM and ER-vesicles previously described in fission yeast,17 Ltc1-GFP localizes to cortical and internal dots in the ER in wild-type cells (arrows in Figure 3), but MitoHealth co-localization indicates that this protein is also associated to ER-Mitochondrial contact sites in S. pombe cells (Figures 3 and S2), as reported in S. cerevisiae cells.24
PMID:40124504	PBO:0119869	In contrast to Mdm34-GFP, Ltc1-GFP lacks its normal ER-PM and ER-mitochondria localization (see Figure 3). This result indicates that Ltc1 localization is fully dependent on EMC activity.
PMID:40124504	FYPO:0002321	As shown in Figure 4A, loss of EMC results in a marked increase in the ergosterol content in the oca3D mutant strain at both temperatures when compared to levels in wild-type cells.
PMID:40124504	FYPO:0008408	As expected for the observed ergosterol overaccumulation (Figures 4A and 4B), the growth of Oca3/Emc2-depleted cells is sensitive to nystatin and resistant to ketoconazole (Figure 4C).
PMID:40124504	PBO:0093554	Likewise, the deletion of genes encoding the above predicted components of the S. pombe EMC (emc3D, emc5D and emc6D) renders a cold- sensitive phenotype too (Figure 1D).
PMID:40124504	PBO:0093554	Likewise, the deletion of genes encoding the above predicted components of the S. pombe EMC (emc3D, emc5D and emc6D) renders a cold- sensitive phenotype too (Figure 1D).
PMID:40124504	PBO:0119864	Localization of the Tts1-mCherry construct, enriched in the tubular structure of the ER14 indicates that the ER, ER-associated plasma membrane (PM) and nuclear membrane remain unaltered in oca3-null cells (the oca3D deletion strain) (Figure 1B).
PMID:40124504	GO:0044233	As shown in Figure 3, Mdm34-GFP co-localizes with mitochondrial membrane markers in wild-type cells, enriched at the ERMES ER-mitochondrial contact sites.
PMID:40124504	GO:0055092	Thus, as previously reported in S. cerevisiae cells,24 this protein may also facilitate ergosterol transfer from the ER to the mitochondria. Since Ltc1 depletion leads to ergosterol overaccumulation in S. pombe cells,17 it is likely that sterol transport from the PM to the ER and from the ER to the mitochondria by this protein is required to drain ergosterol excess in these cells.
PMID:40124504	FYPO:0008410	In contrast, BiP1-driven expression of mCherry-ADEL is greatly induced in Oca3/Emc2-depleted cells. The UPR senses the protein folding capacity of the ER,45 suggesting that EMC dysfunction may provoke the accumulation of ER-unfolded proteins in S. pombe cells (ER stressed cells).
PMID:40124504	PBO:0119867	As shown in Figure 1C, depletion of Oca3 leads to loss of Emc3, aggregation of Emc5, and normal ER localization, but reduced fluorescence levels of EMC6, revealing the requirement of Oca3 for the assembly of a functional EMC complex.
PMID:40124504	PBO:0093554	The oca3D strain produces compromised cells that can grow at 30°C but fail to grow at lower temperatures (routinely assessed at 20°C) (Figure 1D), a cold-sensitive phenotype that may reflect the loss of membrane lipid homeostasis,16,17 energy homeostasis,18,19 or other adaptive mechanisms required for growth at these environmental conditions.
PMID:40124504	PBO:0119863	Since Ltc1 requires EMC for its localization and function at ER-Plasma membrane and ER-mitochondria contact sites (Figure 3), we conclude that EMC regulates ergosterol homeostasis through the ER-assisted biogenesis of the sterol transfer protein Ltc1. ........These observations lead us to conclude that EMC assists membrane protein folding and insertion by direct action on client proteins (i.e., Ltc1), but also may facilitate the biogenesis of some other membrane proteins by providing optimal membrane fluidity (i.e., ERMES components).
PMID:40124504	FYPO:0008409	As expected for the observed ergosterol overaccumulation (Figures 4A and 4B), the growth of Oca3/Emc2-depleted cells is sensitive to nystatin and resistant to ketoconazole (Figure 4C).
PMID:40124504	FYPO:0000080	Likewise, the deletion of genes encoding the above predicted components of the S. pombe EMC (emc3D, emc5D and emc6D) renders a cold- sensitive phenotype too (Figure 1D).
PMID:40124504	PBO:0119863	Since Ltc1 requires EMC for its localization and function at ER-Plasma membrane and ER-mitochondria contact sites (Figure 3), we conclude that EMC regulates ergosterol homeostasis through the ER-assisted biogenesis of the sterol transfer protein Ltc1.
PMID:40124504	GO:0005789	Like Oca3, localization of fluorescently tagged constructs of the putative orthologous S. pombe Emc3 (Pombase: ID SPBC1711.03), Emc5 (Pombase: ID SPAP4C9.02) and Emc6 (Pombase: ID SPCC1020.11c) is consistent with the ER structure in all these EMC subunits.
PMID:40124504	PBO:0119868	In oca3D cells, most of the Mdm34-GFP is delocalized into the abnormal mitochondria, indicating that EMC disfunction may interfere the assembly of ERMES components.
PMID:40185772	PBO:0120766	(Fig. S6A)
PMID:40185772	PBO:0120741	(Fig. 4F)
PMID:40185772	PBO:0120767	(Fig. S6C)
PMID:40185772	PBO:0120768	(Fig. S6D)
PMID:40185772	PBO:0120746	(Fig. S4B)
PMID:40185772	PBO:0120767	(Fig. S6C)
PMID:40185772	PBO:0120768	(Fig. S6D)
PMID:40185772	PBO:0120731	(Fig. 4F)
PMID:40185772	PBO:0120731	(Fig. 4F)
PMID:40185772	PBO:0108630	(Fig. 4F)
PMID:40185772	PBO:0108632	(Fig. 4F)
PMID:40185772	GO:0031428	(Fig. 2C)
PMID:40185772	PBO:0108631	(Fig. 4F)
PMID:40185772	PBO:0120727	(Fig. 1B)
PMID:40185772	PBO:0120728	(Fig. 1B)
PMID:40185772	PBO:0120728	(Fig. 1B)
PMID:40185772	PBO:0120728	(Fig. 1B and C)
PMID:40185772	GO:0000027	From these experiments, we concluded that snR107 mediates 25S rRNA G2483 2’-O-Me and contributes to pre-rRNA processing and 60S subunit biogenesis in a Gm2483-independent fashion.
PMID:40185772	PBO:0093559	(Fig. S4D)
PMID:40185772	PBO:0120729	(Fig. 1B)
PMID:40185772	PBO:0120729	(Fig. 1B)
PMID:40185772	PBO:0120729	(Fig. 1B)
PMID:40185772	PBO:0120730	(Fig. 1)
PMID:40185772	PBO:0108631	(Fig. 4F)
PMID:40185772	PBO:0108632	(Fig. 4F)
PMID:40185772	PBO:0108632	(Fig. 4F)
PMID:40185772	PBO:0108630	(Fig. 4F)
PMID:40185772	FYPO:0001357	(Fig. S3G)
PMID:40185772	PBO:0120731	(Fig. 4F)
PMID:40185772	PBO:0120731	(Fig. 4F)
PMID:40185772	PBO:0108636	(Fig. 4F)
PMID:40185772	PBO:0108636	(Fig. 4F)
PMID:40185772	PBO:0108635	(Fig. 4F)
PMID:40185772	PBO:0108635	(Fig. 4F)
PMID:40185772	PBO:0108636	(Fig. 4F)
PMID:40185772	PBO:0120740	(Fig. 4D)
PMID:40185772	FYPO:0000590	(Fig. S5F)
PMID:40185772	FYPO:0001357	(Fig. S3G)
PMID:40185772	FYPO:0001357	(Fig. S3G)
PMID:40185772	FYPO:0001357	(Fig. S3G)
PMID:40185772	FYPO:0001357	(Fig. S3G)
PMID:40185772	PBO:0120778	(Fig. S6F)
PMID:40185772	PBO:0120777	(Fig. S6E)
PMID:40185772	PBO:0120775	(Fig. 5D)
PMID:40185772	PBO:0120743	(Fig. 5D)
PMID:40185772	PBO:0120776	(Fig. 5C)
PMID:40185772	PBO:0120775	(Fig. 5C)
PMID:40185772	PBO:0120754	(Fig. 4F)
PMID:40185772	PBO:0120774	(Fig. 4F)
PMID:40185772	PBO:0120773	(Fig. 4F)
PMID:40185772	PBO:0120772	(Fig. 4F)
PMID:40185772	PBO:0120771	(Fig. 3C)
PMID:40185772	PBO:0120770	(Fig. 2D)
PMID:40185772	GO:0005730	We further carried out smFISH analyses and found that snR107, as opposed to mamRNA 5’ exon, accumulated specifically in the nucleolus in wild type cells (Fig. 2d, e).
PMID:40185772	FYPO:0001135	(Fig. S3C)
PMID:40185772	PBO:0120742	(Fig. 5D)
PMID:40185772	PBO:0110962	(Fig. 4F)
PMID:40185772	PBO:0110947	(Fig. 4F)
PMID:40185772	PBO:0120754	(Fig. 4F)
PMID:40185772	PBO:0108630	(Fig. 4F)
PMID:40185772	PBO:0108630	(Fig. 4F)
PMID:40185772	PBO:0108632	(Fig. 4F)
PMID:40185772	PBO:0108632	(Fig. 4F)
PMID:40185772	PBO:0120740	(Fig. 4B, D and E)
PMID:40185772	PBO:0120738	(Fig. 3A, 3C)
PMID:40185772	PBO:0120730	(Fig. 1, Fig. 2D)
PMID:40185772	PBO:0120743	(Fig. 5D)
PMID:40185772	PBO:0120755	(Fig. 3D)
PMID:40185772	PBO:0108631	(Fig. 4F)
PMID:40185772	PBO:0120728	(Fig. 1B, 1C)
PMID:40185772	PBO:0120769	5’&3’SSmut cells also exhibited a strong increase in signal intensity and a redistribution of the lncRNA to the nucleolus, as determined by fluorescence overlap with the nucleolar marker Nop56 (Fig. 1d, e)
PMID:40185772	PBO:0120732	(Fig. 4F)
PMID:40185772	PBO:0120732	(Fig. 4F)
PMID:40185772	PBO:0108635	(Fig. 4F)
PMID:40185772	PBO:0108635	(Fig. 4F)
PMID:40185772	PBO:0120741	(Fig. 4F)
PMID:40185772	PBO:0120741	(Fig. 4F)
PMID:40185772	PBO:0108631	(Fig. 4F)
PMID:40185772	PBO:0108630	(Fig. 4F)
PMID:40185772	PBO:0120734	(Fig. S3F)
PMID:40185772	PBO:0108636	(Fig. 4F)
PMID:40185772	PBO:0120759	(Fig. 4F)
PMID:40185772	PBO:0120759	(Fig. 4F)
PMID:40185772	PBO:0120725	(Fig. S1A)
PMID:40185772	PBO:0120738	(Fig. 3C)
PMID:40185772	PBO:0120755	(Fig. 3D)
PMID:40185772	FYPO:0001135	(Fig. S3C)
PMID:40185772	PBO:0120748	(Fig. S3E)
PMID:40185772	PBO:0120734	(Fig. S3F)
PMID:40185772	PBO:0120740	(Fig. 4E)
PMID:40185772	FYPO:0001135	(Fig. S3C)
PMID:40185772	PBO:0120739	(Fig. 3D)
PMID:40185772	PBO:0120738	(Fig. 3A and C)
PMID:40185772	PBO:0120737	(Fig. 4B)
PMID:40185772	PBO:0120742	(Fig. 5C)
PMID:40185772	PBO:0120742	(Fig. 5E, 5F)
PMID:40185772	PBO:0120743	(Fig. 5C)
PMID:40185772	FYPO:0000590	(Fig. S5F)
PMID:40185772	PBO:0120753	(Fig. 4F)
PMID:40185772	PBO:0120752	(Fig. 5E)
PMID:40185772	PBO:0120751	(Fig. 5E)
PMID:40185772	PBO:0120748	(Fig. S3E)
PMID:40185772	PBO:0120735	(Fig. 4E)
PMID:40185772	PBO:0120738	(Fig. 3A, 3C)
PMID:40185772	PBO:0120750	(Fig. 6D)
PMID:40185772	PBO:0120749	(Fig. 6C)
PMID:40185772	PBO:0120748	(Fig. S1A)
PMID:40185772	PBO:0120748	(Fig. S1A)
PMID:40185772	PBO:0120747	(Fig. S2E)
PMID:40185772	PBO:0120747	(Fig. S2E)
PMID:40185772	PBO:0120735	(Fig. S4C)
PMID:40185772	PBO:0120735	(Fig. 4B)
PMID:40185772	PBO:0120734	(Fig. 2D)
PMID:40185772	PBO:0104073	(Fig. S2D)
PMID:40185772	PBO:0120733	(Fig. S2D)
PMID:40185772	PBO:0120726	(Fig. S2E)
PMID:40185772	PBO:0120735	(Fig. 4D)
PMID:40185772	PBO:0120736	(Fig. 4B)
PMID:40185772	PBO:0120732	(Fig. 4F)
PMID:40185772	PBO:0120749	(Fig. 6E)
PMID:40185772	PBO:0120743	(Fig. 5E, 5F)
PMID:40185772	PBO:0120756	(Fig. 6F)
PMID:40185772	PBO:0120757	(Fig. 6G)
PMID:40185772	PBO:0120732	(Fig. 4F)
PMID:40185772	PBO:0120758	(Fig. 6H)
PMID:40185772	PBO:0120748	(Fig. S3E)
PMID:40185772	PBO:0120735	(Fig. 4E)
PMID:40185772	PBO:0120755	(Fig. 3D)
PMID:40185772	PBO:0120760	(Fig. 3C)
PMID:40185772	FYPO:0001135	(Fig. S3C)
PMID:40185772	PBO:0108631	(Fig. 4F)
PMID:40185772	PBO:0120739	(Fig. S4E)
PMID:40185772	PBO:0120735	(Fig. S4F)
PMID:40185772	PBO:0120740	(Fig. 4D)
PMID:40185772	PBO:0120746	(Fig. S4B)
PMID:40185772	PBO:0120737	(Fig. 4D)
PMID:40185772	PBO:0120745	(Fig. S4B)
PMID:40185772	PBO:0120735	(Fig. 4D)
PMID:40185772	PBO:0120745	(Fig. S4B)
PMID:40185772	PBO:0120744	(Fig. S4B)
PMID:40185772	PBO:0120748	(Fig. S3E)
PMID:40185772	PBO:0120734	(Fig. S3F)
PMID:40185772	PBO:0120740	(Fig. 4E)
PMID:40185772	PBO:0120742	(Fig. 5F)
PMID:40185772	PBO:0120743	(Fig. 5E)
PMID:40185772	PBO:0120761	(Fig. 6E)
PMID:40185772	PBO:0120762	(Fig. 6F)
PMID:40185772	PBO:0120763	(Fig. 6G)
PMID:40185772	PBO:0120764	(Fig. 6H)
PMID:40185772	PBO:0120765	(Fig. S6B)
PMID:40185772	PBO:0120765	(Fig. S6B)
PMID:40193710	FYPO:0001355	(Fig. 2E)
PMID:40193710	GO:0008474	(Fig. 1)
PMID:40193710	PBO:0119794	our study suggested that Phi1 was a part of the cohesin loading machinery (Fig. 5)
PMID:40193710	GO:0034087	our study suggested that Phi1 was a part of the cohesin loading machinery (Fig. 5)
PMID:40193710	PBO:0093562	(Fig. 2A)
PMID:40193710	FYPO:0000964	(Fig. 2A)
PMID:40193710	PBO:0096828	(Fig. 2B)
PMID:40193710	FYPO:0000228	(Fig. 2C and D)
PMID:40193710	PBO:0119795	(Fig. 2E)
PMID:40193710	PBO:0119796	(Fig. 2E)
PMID:40193710	PBO:0119796	(Fig. 2E)
PMID:40193710	PBO:0119797	(Fig. 2E)
PMID:40193710	PBO:0119798	(Fig. 2E)
PMID:40193710	PBO:0119798	(Fig. 2E)
PMID:40193710	FYPO:0001355	(Fig. 2E)
PMID:40193710	PBO:0119806	(Fig. 5F)
PMID:40193710	PBO:0119807	(Fig. 5F)
PMID:40193710	PBO:0119805	(Fig. 5F)
PMID:40193710	PBO:0119804	(Fig. 5C)
PMID:40193710	PBO:0119803	(Fig. 5A)
PMID:40193710	PBO:0119808	(Fig. 5D and F)
PMID:40193710	PBO:0119809	(Fig. 5E and F)
PMID:40193710	PBO:0119802	(Fig. 4H and I)
PMID:40193710	FYPO:0004742	(Fig. 3E)
PMID:40193710	PBO:0119801	(Fig. 3C)
PMID:40193710	PBO:0119800	(Fig. 3D)
PMID:40193710	PBO:0119799	(Fig. 3A and B)
PMID:40193710	FYPO:0001355	(Fig. 2E)
PMID:40193710	FYPO:0001355	(Fig. 2E)
PMID:40385371	FYPO:0003440	A percentage of lysed cells were also detected for mob1-N1 and mob1-R4 (Figure 1C-D).
PMID:40385371	PBO:0093558	mob1-1 grew less well than wildtype at 32°C and 36°C and mob1-N1 grew less well than wildtype at 36°C (Figure 1B).
PMID:40385371	FYPO:0003440	A percentage of lysed cells were also detected for mob1-N1 and mob1-R4 (Figure 1C-D).
PMID:40385371	FYPO:0002049	At 36°C, mob1-1 cells were multinucleated with no septum present (Figure 1C), as has been previously reported (Hou et al., 2000).
PMID:40385371	PBO:0093556	mob1-R4 grew slightly less well than wildtype at both high (32°C and 36°C) and low (25°C) temperatures (Figure 1B).
PMID:40385371	PBO:0093556	mob1-N1 grew less well than wildtype at 36°C (Figure 1B).
PMID:40385371	PBO:0093553	mob1-R4 grew slightly less well than wildtype at both high (32°C and 36°C) and low (25°C) temperatures (Figure 1B).
PMID:40395999	PBO:0120559	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	PBO:0120559	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	PBO:0120559	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	PBO:0120559	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	PBO:0120559	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	PBO:0120559	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	PBO:0120559	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	PBO:0120559	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	PBO:0120559	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	PBO:0120562	Sulfur deficiency decreased the phosphorylation of the TORC1- phosphorylation site of Psk1. Conversely, in the absence of Ecl1-family genes, remarkable phosphorylation was observed with or without sulfur.
PMID:40395999	PBO:0120563	TORC1 activity of the ecls∆ cells was much higher than that of control cells even in the logarithmic growth phase (0 hour), suggesting that Ecl1-family proteins also partially inhibit TORC1 activity in this minimum medium condition.
PMID:40395999	PBO:0120563	TORC1 activity of the ecls∆ cells was much higher than that of control cells even in the logarithmic growth phase (0 hour), suggesting that Ecl1-family proteins also partially inhibit TORC1 activity in this minimum medium condition.
PMID:40395999	PBO:0120563	TORC1 activity of the ecls∆ cells was much higher than that of control cells even in the logarithmic growth phase (0 hour), suggesting that Ecl1-family proteins also partially inhibit TORC1 activity in this minimum medium condition.
PMID:40395999	PBO:0120564	Cdc13 is degraded during sulfur depletion, but the levels of its binding partner Cdc2 did not change (Fig. 1F and 1G), suggesting autophagy selectively degrades Cdc13 but not Cdc2 in this condition.
PMID:40395999	FYPO:0007086	Sulfur depletion results in Ecl1-family gene-dependent reduction of the cell size of S. pombe [12] (Fig. 1A and 1B). ecl1∆ ecl2∆ ecl3∆ (ecls∆) cells do not exhibit reduced cell size and develop abnormal deposits stained with aniline blue that stains the septum [28,29] (Fig. 1C).
PMID:40395999	PBO:0120559	Cdc13 levels declined in wild-type cells in response to sulfur depletion, but not in ecls∆ cells (Fig. 1F), suggesting that the abnormal morphology of ecls∆ cells during sulfur depletion is attributable to the failure of normal cyclin degradation.
PMID:40395999	PBO:0120559	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	PBO:0120559	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40406582	PBO:0120198	Gar2-GFP, a nucleolar marker and ortholog of human nucleolin (Gulli et al., 1995; Rutherford et al., 2024), localized normally within the nucleolus of nsk1∆ cells, as did two other nucleolar proteins, Nop2, a rRNA methyltransferase involved in ribosome biogenesis (Rutherford et al., 2024), and Nuc1 (Hirano et al., 1989) (Figure 1D).
PMID:40406582	PBO:0120199	Gar2-GFP, a nucleolar marker and ortholog of human nucleolin (Gulli et al., 1995; Rutherford et al., 2024), localized normally within the nucleolus of nsk1∆ cells, as did two other nucleolar proteins, Nop2, a rRNA methyltransferase involved in ribosome biogenesis (Rutherford et al., 2024), and Nuc1 (Hirano et al., 1989) (Figure 1D).
PMID:40406582	FYPO:0003216	For this, we monitored for de-repression of the ura4+ reporter gene that had been integrated into the normally silenced rDNA repeats (Jin et al., 2007; Thon and Verhein-Hansen, 2000). Depression of the ura4+ reporter in this context leads to enhanced growth on plates lacking exogenous uracil and increased sensitivity to 5-fluoroorotic acid (5-FOA). By this assay, we found that rDNA silencing was partially relieved in nsk1∆ cells (Figure 1A) and to the same extent as in dnt1∆ cells (Jin et al., 2007).
PMID:40406582	PBO:0120200	Gar2-GFP, a nucleolar marker and ortholog of human nucleolin (Gulli et al., 1995; Rutherford et al., 2024), localized normally within the nucleolus of nsk1∆ cells, as did two other nucleolar proteins, Nop2, a rRNA methyltransferase involved in ribosome biogenesis (Rutherford et al., 2024), and Nuc1 (Hirano et al., 1989) (Figure 1D).
PMID:40406582	PBO:0120201	Time-lapse imaging of 21 nsk1+ and 42 nsk1∆ cells showed that Gar2-GFP segregated equally and without lagging in all cells (Figure 1E).
PMID:40427588	PBO:0120213	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	PBO:0120216	However, the RNA level of var1, which encodes a mitochondrial ribosomal protein, remained stable in both mutants (Figure 2c)
PMID:40427588	PBO:0120207	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	PBO:0120218	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	PBO:0120217	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	PBO:0120216	However, the RNA level of var1, which encodes a mitochondrial ribosomal protein, remained stable in both mutants (Figure 2c).
PMID:40427588	PBO:0114823	Notably, deletion of the insertion domain resulted in a greatly decreased associ- ation of the translation initiation factors Mti2 and Mti3 with the mtSSU.
PMID:40427588	FYPO:0008434	Moreover, the deletion significantly reduced the association with assembled mitoribosomes and impaired mitoribosome assembly. Specifically, a distinct mitoribosome peak was observed in fraction 11 in the wild-type cells (Figure 4a) but was markedly diminished in the mti2∆insertion cells (Figure 4b), indicating a defect in mitoribosome assembly.
PMID:40427588	PBO:0120215	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	PBO:0120214	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	PBO:0120219	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	FYPO:0008434	Moreover, the deletion significantly reduced the association with assembled mitoribosomes and impaired mitoribosome assembly. Specifically, a distinct mitoribosome peak was observed in fraction 11 in the wild-type cells (Figure 4a) but was markedly diminished in the mti2∆insertion cells (Figure 4b), indicating a defect in mitoribosome assembly. This phenotype is similar Biomolecules 2025, 15, x FOR PEER REVIEW 11 of 16 to that observed in ∆mti2 cells (Figure 4c).
PMID:40427588	PBO:0120212	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	PBO:0120211	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	PBO:0120210	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	PBO:0120209	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	PBO:0120208	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	PBO:0120207	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes, including cob1 (complex III), cox1, cox2 and cox3 (complex IV) and atp6, atp8 and atp9 (ATP synthase).
PMID:40427588	FYPO:0000684	Compared to wild-type cells, the growth of mti2∆insertion and ∆mti2 cells was only marginally reduced in glucose media but was significantly impaired in glycerol media (Figure 2b). This result suggests that mitochondrial respiration is similarly inhibited in both mutants.
PMID:40427588	FYPO:0001357	Compared to wild-type cells, the growth of mti2∆insertion and ∆mti2 cells was only marginally reduced in glucose media but was significantly impaired in glycerol media (Figure 2b). This result suggests that mitochondrial respiration is similarly inhibited in both mutants.
PMID:40427588	PBO:0120212	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	PBO:0120213	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	PBO:0120209	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	PBO:0114824	Notably, deletion of the insertion domain resulted in a greatly decreased associ- ation of the translation initiation factors Mti2 and Mti3 with the mtSSU.
PMID:40427588	PBO:0120214	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	PBO:0120208	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	PBO:0120221	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	PBO:0120220	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	PBO:0120219	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	PBO:0120218	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	PBO:0120217	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	PBO:0120221	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	PBO:0120215	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	PBO:0120220	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	GO:0070124	These findings indicate that, similar to MTIF2 in humans, the insertion domain in S. pombe Mti2 promotes the efficiency of translation initiation by facilitating the association of initiation factors with the mitochondrial ribosome.
PMID:40427588	PBO:0120222	These findings indicate that, similar to MTIF2 in humans, the insertion domain in S. pombe Mti2 promotes the efficiency of translation initiation by facilitating the association of initiation factors with the mitochondrial ribosome.
PMID:40427588	FYPO:0000684	Compared to wild-type cells, the growth of mti2∆insertion and ∆mti2 cells was only marginally reduced in glucose media but was significantly impaired in glycerol media (Figure 2b).
PMID:40427588	PBO:0120211	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	PBO:0120210	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	FYPO:0001357	Compared to wild-type cells, the growth of mti2∆insertion and ∆mti2 cells was only marginally reduced in glucose media but was significantly impaired in glycerol media (Figure 2b).
PMID:40452482	GO:0042244	The isp3Δ mutant spores fail to partition into the hydrophobic polyethylene glycol (PEG) phase in aqueous two-phase systems (ATPSs), suggesting that Isp3 is required for proper spore wall assembly and surface hydrophobicity.
PMID:40452482	FYPO:0000175	The isp3Δ mutant spores fail to partition into the hydrophobic polyethylene glycol (PEG) phase in aqueous two-phase systems (ATPSs), suggesting that Isp3 is required for proper spore wall assembly and surface hydrophobicity.
PMID:40452482	GO:1990916	Isp3 is the major component of the outermost spore wall layer in S. pombe and is required for the surface hydrophobicity of mature spores.
PMID:4154968	GO:0004354	"(comment: well this is a slight fudge. The activity was assayed and present. We know this is glutamate dehydrogenase...so sone and will make ""published"")"
PMID:4309177	GO:0003938	(comment: activated by ATP)
PMID:4698209	GO:0004794	(comment: CHECK inhibited_by CHEBI:17191)
PMID:4698210	GO:0003984	(comment: CHECK inhibited_by CHEBI:27266)
PMID:4708672	GO:0019002	The enzyme is strongly inhibited by AMP and GMP. Whereas GMP seems to act by a direct competition for the GTP binding site, AMP appears as an allosteric effector, showing at non-saturating substrate concentrations a homotropic effect as well as a heterotropic effect upon the GTP and aspartate binding
PMID:4708672	GO:0016208	The enzyme is strongly inhibited by AMP and GMP. Whereas GMP seems to act by a direct competition for the GTP binding site, AMP appears as an allosteric effector, showing at non-saturating substrate concentrations a homotropic effect as well as a heterotropic effect upon the GTP and aspartate binding
PMID:4708672	GO:0004019	The enzyme is strongly inhibited by AMP and GMP. Whereas GMP seems to act by a direct competition for the GTP binding site, AMP appears as an allosteric effector, showing at non-saturating substrate concentrations a homotropic effect as well as a heterotropic effect upon the GTP and aspartate binding
PMID:4821071	GO:0003984	(comment: CHECK activated_by FAD , inhibited_by L-valine)
PMID:6094012	FYPO:0000134	(comment: CHECK actually this only occurs in 30% of cells.. I don't know if it is viable or inviable)
PMID:6094012	FYPO:0001972	(comment: CHECK parent child relationship with term above requested)
PMID:6526818	PBO:0114639	(comment: CHECK inhibited by methionine)
PMID:6828164	PBO:0095711	cell size at septation is 9.5µm in cdc2-1w (9.7µm in cdc2-2w)
PMID:6828164	FYPO:0000400	(Fig. 1A) The transition point for cdc2 (0.74) is not advanced using a cdc2.M35 wee1.6 mutant
PMID:6828164	FYPO:0000400	(Fig. 1A, Table 1) cdc13 transition point (0.78) is not advanced in a cdc13-117 wee1.6 mutant
PMID:6828164	FYPO:0000400	(Fig. 1A, Table 1) cdc13 transition point is 0.69 using a cdc13-117 mutant
PMID:6828164	FYPO:0003449	The transition point for cdc1 is advanced in a cdc1.P13 wee1.6 mutant from 0.62 to 0.33. An asynchronous population of a cdc1-P13 wee1.6 mutant was shifted from 25°C to the restrictive temperature of 36°C to inactivate the cdc1 gene and the number of cells that went on to divide was increased compared to a cdc1-7 mutant
PMID:6828164	FYPO:0000400	(Fig. 1A) The transition point for cdc2 (0.68) is not advanced using a cdc2.M63 wee1.6 mutant
PMID:6828164	FYPO:0000400	(Fig. 1A)
PMID:6828164	FYPO:0003449	The transition point for cdc2 is advanced from 0.65 to 0.53 using a cdc2.M26 wee1.6 mutant
PMID:6828164	FYPO:0003449	The transition point for cdc2 is advanced from 0.68 to 0.47 using a cdc2.L7 wee1.6 mutant
PMID:6828164	FYPO:0003449	(Fig. 1A) The transition point for cdc2 is advanced from 0.69 to 0.48 using a cdc2.33 wee1 [more...]
PMID:6828164	FYPO:0000400	(Fig. 1A) The transition point for cdc2 is 0.65 using cdc2.M55
PMID:6828164	FYPO:0000400	(Fig. 1A) The transition point for cdc2 is 0.66 using cdc2.M35
PMID:6828164	FYPO:0000400	(Fig. 1A) The transition point for cdc2 is 0.65 using cdc2.M26
PMID:6828164	FYPO:0000400	(Fig. 1A) The transition point for cdc2 is 0.70 using cdc2.M63
PMID:6828164	FYPO:0000400	(Fig. 1A) The transition point for cdc2 is 0.68 using cdc2.L7
PMID:6828164	FYPO:0000400	(Fig. 1A) The transition point for cdc2 is 0.65 using cdc2.33
PMID:6828164	FYPO:0003449	(Fig. 1A) The transition point for cdc27 is advanced from 0.63 to 0.22 in a cdc27-K3 wee1.6 mutant. An asynchronous population of a cdc1-7 wee1.6 mutant was shifted from 25°C to the restrictive temperature of 36°C to inactivate the cdc27 gene and the number of cells that went on to divide was increased compared to a cdc27-K3 mutant
PMID:6828164	FYPO:0000400	(Fig. 1A, Table 1) cdc27 transition point is 0.62 using a cdc27.K3 mutant
PMID:6828164	FYPO:0000400	"(Fig. 1A) (comment: EXP) The transition point for cdc1 is not advanced in a cdc1.7 cdc2-1w mutant (0.64). An asynchronous population of a cdc1-7cdc2-1w mutant was shifted from 25°C to the restrictive temperature of 36°C to inactivate the cdc1 gene and the number of cells that went on to divide was similar to a cdc1-7 mutant. The transition point for cdc1 (0.58) is not advanced in a cdc1.7 cdc2-2w mutant (comment: cdc2-2w is the same change as cdc2-1w, but also consider comment transferred from duplicate annotation: ""I think this allele cdc2-2w maybe a typo or a changed annotation since this paper was published and is actually cdc2-3w"")."
PMID:6828164	FYPO:0003449	(Fig. 1A) The transition point s advanced from 0.68 to 0.29 in a cdc1.7 wee1.6 mutant. An asynchronous population of a cdc1-7 wee1.6 mutant was shifted from 25°C to the restrictive temperature of 36°C to inactivate the cdc1 gene and the number of cells that went on to divide was increased compared to a cdc1-7 mutant
PMID:6828164	FYPO:0002516	(comment: TP. 0.33)
PMID:6828164	FYPO:0000400	(Fig. 1A) The cdc1 gene has a execution point of ~0.62 which means its function is completed just before entry into mitosis. An asynchronous population of the cdc1-7 mutant was shifted from 25°C to the restrictive temperature of 36°C to inactivate the gene and the number of cells that went on to divide was measured
PMID:6828164	FYPO:0002516	(comment: ???)
PMID:6828164	FYPO:0000400	(Fig. 1A) The cdc1 gene has a execution point of ~0.65 which means its function is completed just before entry into mitosis. An asynchronous population of the cdc1-7 mutant was shifted from 25°C to the restrictive temperature of 36°C to inactivate the gene and the number of cells that went on to divide was measured
PMID:6828164	PBO:0095711	cell size at septation is 8.7µm
PMID:6828164	PBO:0095711	cell size at septation is 8.9µm
PMID:6828164	PBO:0095711	cell size at septation is 8.5µm
PMID:6828164	PBO:0095711	cell size at septation is 8.9µm
PMID:6828164	PBO:0095711	cell size at septation is 8.4µm
PMID:6828164	PBO:0095711	cell size at septation is 10.3µm
PMID:6828164	PBO:0095711	cell size at septation is 9.6µm
PMID:6828164	PBO:0094266	cell size at separation is 22.4µm compared to 12.8µm for wild type
PMID:6828164	PBO:0093767	cell size at separation is 16.7µm compared to 12.8µm for wild type
PMID:689088	FYPO:0006822	(comment: CHECK at division)
PMID:6943408	FYPO:0003485	(comment: After release from HU block, cells can undergo one round of division without DNA replication)
PMID:6943408	FYPO:0001982	(comment: Cells unable to divide, even after DNA replication is completed)
PMID:6943408	FYPO:0003485	After release from HU block, cells can undergo one round of division without DNA replication)
PMID:6943408	FYPO:0001982	(comment: Cells unable to divide, even after DNA replication is completed)
PMID:6943408	FYPO:0003738	(comment: All nuclei took on a granular appearance and in some nuclei this granularity was clearly resolvable into three densely staining bodies resembling condensed chromosomes) (Fig. 3)
PMID:6943408	FYPO:0003485	(comment: After release from HU block, cells can undergo one round of division without DNA replication)
PMID:6943408	FYPO:0001248	(comment: CHECK abolished)
PMID:6943408	FYPO:0003485	(comment: DNA synthesis and cell number increase were rapidly inhibited (data not given but similar to the mitotic mutant cdc2 in Fig. 5 of Nurse et al. 1976))
PMID:6943408	FYPO:0003485	(comment: DNA synthesis and cell number increase were rapidly inhibited (data not given but similar to the mitotic mutant cdc 2 in Fig. 5 of Nurse et al. 1976))
PMID:6943408	FYPO:0003485	(comment: DNA synthesis and cell number increase were rapidly inhibited (data not given but similar to the mitotic mutant cdc 2 in Fig. 5 of Nurse et al. 1976))
PMID:6943408	FYPO:0003485	(comment: After release from HU block, cells can undergo one round of division without DNA replication)
PMID:6943408	FYPO:0000608	(comment: Cells able to undergo normal DNA replication and enter cell division, but fail to divide.)
PMID:6943408	FYPO:0003485	DNA synthesis and cell number increase were rapidly inhibited (data not given but similar to the mitotic mutant cdc 2 in Fig. 5 of Nurse et al. 1976)
PMID:6943408	FYPO:0000608	(comment: Cells able to undergo normal DNA replication and enter cell division, but fail to divide.)
PMID:6961452	GO:0004070	(comment: This was really IGI complemetnation of E-coli pyrB)
PMID:7262540	PBO:0101531	cells divide at 82% of wild diploid size at division
PMID:7262540	PBO:0101534	cells divide at 10% longer than wild diploid cells at division
PMID:7262540	PBO:0101536	cells divide at 6% longer than wild diploid cells at division
PMID:7262540	PBO:0101534	cells divide at 11% longer than wild diploid cells at division
PMID:7262540	PBO:0101531	Cells divide at 65% of wild type diploid cell length
PMID:7262540	PBO:0101534	cells divide at 16.7µm at 25°C
PMID:7262540	PBO:0101531	cells divide at 10.2µm at 25°C
PMID:7262540	PBO:0101532	cells divide at 22.4µm at 25°C
PMID:7262540	PBO:0101531	(comment: cdc2-1w was previously called wee2-1)
PMID:7262540	PBO:0101531	cells septate at 56% of wild type diploid length
PMID:7262540	PBO:0101531	cells septate at 58% of wild type diploid length
PMID:7262540	PBO:0101531	cells septate at 54% of wild type diploid length
PMID:7262540	PBO:0101534	cells divide at 11% longer than wild diploid cells at division
PMID:7262540	PBO:0101531	cells septate at 58% of wild type diploid length
PMID:7262540	PBO:0101531	cells septate at 52% of wild type diploid length
PMID:7262540	PBO:0101531	cells septate at 81% of wild type diploid length
PMID:7262540	PBO:0101535	cells divide at 7% longer than wild diploid cells at division
PMID:7262540	PBO:0101531	cells septate at 82% of wild type diploid length
PMID:7262540	PBO:0101536	cells divide at 8% longer than wild diploid cells at division
PMID:7262540	PBO:0101531	cells septate at 85% of wild type diploid length
PMID:7262540	PBO:0101531	cells septate at 77% of wild type diploid length
PMID:7262540	PBO:0101531	cells septate at 87% of wild type diploid length
PMID:7262540	FYPO:0002176	small cell size at division is partially suppressed in the presence of sup3-5 an opal nonsense suppressor mutation in the sup3 tRNA gene. Cells divide at 89% of control cell length at division so are not really normal size
PMID:7262540	PBO:0101531	cells divide at 56% of the size at division of wild type diploids
PMID:7262540	PBO:0101533	(comment: This mutation is probably allelic with cdc2-56. Cells divide at 10.0 µm. I think it is useful to have it annotated as it is in old literature and people may wonder what it is)
PMID:7262540	PBO:0101531	cells divide at 51% of control cell length at division
PMID:7262540	PBO:0101531	cells divide at 75% of wild type diploid cell length at division at 25°C
PMID:7262540	PBO:0101536	cells divide at 9% longer than wild diploid cells at division
PMID:7262540	PBO:0101534	cells divide at 10% longer than wild diploid cells at division
PMID:7262540	PBO:0101534	cells divide at 12% longer than wild diploid cells at division
PMID:7498507	GO:0004725	(comment: CHECK activated_by(CHEBI:16356))
PMID:7501024	FYPO:0001490	(comment: CHECK salt stress)
PMID:7501024	FYPO:0001490	(comment: CHECK salt stress)
PMID:7501024	FYPO:0001490	(comment: CONDITION non-ionic osmotic stress)
PMID:7501454	MOD:00046	(comment: CHECK hyperphosphorylated in late S phase; phosphorylated on different sites in S versus G2/M)
PMID:7501454	GO:0003887	constant throughout cell cycle
PMID:7501454	GO:0003697	(comment: higher affinity during S phase than G2/M)
PMID:7559598	FYPO:0000280	data not shown
PMID:7559598	PBO:0097547	data not shown
PMID:7596817	FYPO:0003695	(comment: polysome profile)
PMID:7596817	FYPO:0003696	(comment: polysome profile)
PMID:7622618	FYPO:0000280	(comment: evidence is essentially IC, as I inferred sterility from the lack of shmoo formation (h- cells))
PMID:7626804	MOD:00047	(Fig. 1D) peptide 2
PMID:7626804	PBO:0099201	(Fig. 1D) peptide 3 and peptide1
PMID:7626804	PBO:0094620	(Fig. 3) (comment: chk1 is not required for T14 phosphorylation by wee1)
PMID:7626804	PBO:0099202	(Table 2) (comment: cdc2-T14A is present on multicopy plasmid cells are viable but have a semi wee phenotype)
PMID:7626804	FYPO:0002176	(Table 2)
PMID:7626804	PBO:0099202	(Fig. 4A) (comment: cells average size 11.6µm)
PMID:7626804	PBO:0099208	(Fig. 7A, B)
PMID:7626804	PBO:0099209	(Fig. 7A, B)
PMID:7626804	FYPO:0001706	(Fig. 8)
PMID:7626804	MOD:00047	(Fig. 1D) peptide 3
PMID:7626804	PBO:0099200	(Fig. 1A)
PMID:7626804	PBO:0094619	(Fig. 1B, C and D) (comment: x = a small phospho peptide of T14Y15. T14 phosphorylation only occurs when wee1 is overexpressed)
PMID:7626804	PBO:0099210	data not shown
PMID:7626804	FYPO:0002102	(Fig. 8)
PMID:7626804	PBO:0093767	(Fig. 4A) (comment: cells average size 16.6µm)
PMID:7626804	PBO:0099203	(Fig. 4B)
PMID:7626804	PBO:0099204	(Fig. 4B)
PMID:7626804	PBO:0099205	(Fig. 4B)
PMID:7626804	PBO:0099206	(Fig. 4B)
PMID:7626804	PBO:0099207	(Fig. 5B) (comment: wee1 is necessary for T14 phosphorylation no peptide 3 is observed when wee1 is deleted)
PMID:7651412	FYPO:0003735	(comment: switches specificity from direct repeats to inverted repeats)
PMID:7651414	PBO:0105934	(comment: matmi and matpi)
PMID:7651414	PBO:0105934	(comment: matmi and matpi)
PMID:7651414	PBO:0105936	(comment: matmi and matpi)
PMID:7651414	PBO:0105935	(comment: matmi and matpi)
PMID:7651414	PBO:0105935	(comment: matmi and matpi)
PMID:7657164	PBO:0094488	(comment: residue not determined, but probably Y173)
PMID:7687541	GO:0005737	(Fig. 4)
PMID:7706287	FYPO:0002522	(comment: assayed for bulk poly(A)+ RNA)
PMID:7706287	FYPO:0000400	(comment: arrest point determined by H1 kinase activity peak)
PMID:7706287	FYPO:0000911	(comment: assayed for bulk poly(A)+ RNA)
PMID:7739540	FYPO:0001430	(Figure 3b)
PMID:7739540	FYPO:0001430	(Figure 3b)
PMID:7739540	FYPO:0001430	(Figure 3b)
PMID:7773104	FYPO:0005472	(comment: NADP-GDH-defective)
PMID:7774573	PBO:0037522	(comment: CHECK pREP5-DL45 is integrated. cdc2+ is expressed from its own promoter on a multi copy plasmid)
PMID:7774573	PBO:0097954	(comment: CHECK pRIP45DL45 is integrated). (Figure 6B) (comment: CHECK the 20% of cells that are in mitosis are probably cells that were in mitosis when the culture was shifted to the restrictive temperature)
PMID:7774573	PBO:0106642	(comment: CHECK Abnormal septum phenotype include misplace septum, multi septa and partially formed septa)
PMID:7774573	PBO:0037519	(comment: CHECK pREP41-DL50 is integrated)
PMID:7774573	PBO:0037520	(comment: 24% cells enter mitosis compared to 2% when cdc2+ is not over expressed but they did not say that it was a cut phenotype)
PMID:7774573	PBO:0037513	About 75% of cells do not enter mitosis in presence of HU Figure 6A, showing that this mutant does not disrupt normal controls regulating entry into mitosis. pRIP45cdc2-DL45 is integrated cdc2-DL41 has same phenotype but it is not clear if it is under the same conditions
PMID:7774573	PBO:0037512	(comment: CHECK pREP5cdc2-DL41 is integrated)
PMID:7774573	PBO:0037515	DNS
PMID:7774573	PBO:0037516	DNS
PMID:7774573	PBO:0037515	DNS
PMID:7774573	PBO:0095634	(comment: CHECK pIRT2suc1 multi copy plasmid partially rescues the pREP5cdc2-DL41 integrant mitotic arrest phenotype and allows formation of micro colonies) (comment: CHECK cdc2-DL45 is also partially rescued)
PMID:7774573	PBO:0037516	DNS
PMID:7774573	PBO:0037510	abnormal mitotic arrest with 4C DNA content Cells undergo an extra round of DNA replication without undergoing cytokinesis.
PMID:7774573	PBO:0037522	(comment: CHECK cdc2+ is expressed from its own promoter on a multi copy plasmid)
PMID:7774573	PBO:0037511	(comment: CHECK child term of abnormal regulation of mitotic metaphase/anaphase transition.)
PMID:7796804	PBO:0099447	(Figure 1, 4,5)
PMID:7796804	PBO:0099448	(Figure 1, 4,5)
PMID:7796804	PBO:0023774	(Figure 1, 4,5)
PMID:7796804	PBO:0104264	(Fig. 5B) (comment: CHECK cdc22-M45 blocked in G1/S)
PMID:7796804	PBO:0104264	(Fig. 5B) (comment: CHECK cdc22-M45 blocks in G1/S)
PMID:7796804	PBO:0104261	(Fig. 7A,8)
PMID:7796804	PBO:0104261	(Fig. 5A)
PMID:7796804	PBO:0097659	(Fig. 6 top panels, Fig7B panel 2) cells examined 7 hour after refeeding with nitrogen After 7 hour the cdc10-V50 cells start to leak through and this allows the mik1D wee1-50 cells to start entering mitosis
PMID:7796804	PBO:0100985	(Fig. 6 top panels, Fig7B panel 1) cells examined 7 hour after refeeding with nitrogen
PMID:7796804	PBO:0097558	(Fig. 6 middle panels Fig7B panel 3) cells examined 7 hour after refeeding with nitrogen
PMID:7796804	PBO:0104270	(Figure 1, 4,5)
PMID:7796804	PBO:0104269	(Fig. 7C)
PMID:7796804	PBO:0097659	(Fig. 6 middle panels Fig7B panel 4) cells examined 7 hour after refeeding with nitrogen
PMID:7796804	PBO:0097558	(Fig. 6 bottom panels Fig7B panel 5) cells nitrogen starved and examined 7 hour after refeeding with nitrogen
PMID:7796804	PBO:0097659	(Fig. 6 bottom panels Fig7B panel 6) cells examined 7 hour after refeeding with nitrogen
PMID:7796804	PBO:0104265	(comment: CHECK fypo/issues/3164) Fig 5C the cyclin cdc13 cdc2 complex are detected when cells are blocked at G1/S with cdc20-M10 mutant, complex precipitated with p13 beads
PMID:7796804	PBO:0104265	(comment: CHECK fypo/issues/3164) Fig 5C the cyclin cdc13 cdc2 complex are detected when cells are blocked at G1/S with cdc20-M45 mutant, complex precipitated with p13 beads
PMID:7796804	PBO:0097659	(Fig. 6, Fig 7B panel 8)
PMID:7796804	PBO:0104261	(Fig. 7A panel 2)
PMID:7796804	PBO:0104266	(Fig. 7A panel 1)
PMID:7796804	PBO:0104261	(Fig. 7A panel 4)
PMID:7796804	PBO:0104261	(Fig. 7A panel 6)
PMID:7796804	PBO:0102115	(Fig. 7A panel 3)
PMID:7796804	PBO:0104268	(Fig. 7B) It is the soluble form (upper panel) that disappears not the insoluble form (lower panel) which has implications for which form is allowing replication. I don't know whether to leave this annotation out
PMID:7796804	PBO:0102115	(Fig. 7A panel 5)
PMID:7796804	PBO:0104267	(Fig. 5B) (comment: CHECK cdc10-129 cells blocked in G1)
PMID:7796804	PBO:0037896	(Fig. 7C)
PMID:7796804	PBO:0037896	(Fig. 7C)
PMID:7796804	PBO:0104262	(Fig. 5A)
PMID:7796804	PBO:0104262	(Fig. 5A)
PMID:7796804	PBO:0104263	(Fig. 5C) cyclin cdc13 cdc2 complex are not detected when cells are blocked in G1 with cdc10-129 mutant complex precipitated with p13 beads
PMID:7798319	FYPO:0002303	Consistently, the phenotype of cut9-T98 was indistinguishable from that of cut9-665
PMID:7798319	FYPO:0003166	Consistently, the phenotype of cut9-T98 was indistinguishable from that of cut9-665
PMID:7798319	FYPO:0003165	Consistently, the phenotype of cut9-T98 was indistinguishable from that of cut9-665
PMID:7813446	FYPO:0001355	(comment: not arrested like wee1+ overexp alone)
PMID:7813446	FYPO:0001355	(comment: not arrested like wee1-50 overexp alone)
PMID:7813446	FYPO:0001355	(comment: not arrested like wee1-50 overexp alone)
PMID:7813446	PBO:0094967	(comment: higher than wee1 not overexp, but lower than wee1-50 overexp in wt bkg)
PMID:7859738	FYPO:0002060	(Figure 4)
PMID:7859738	FYPO:0002060	(Figure 4)
PMID:7859738	FYPO:0002060	(Figure 4)
PMID:7859738	FYPO:0002060	(Figure 4)
PMID:7859738	FYPO:0002060	(Figure 4)
PMID:7859738	FYPO:0002060	(Figure 4)
PMID:7859738	FYPO:0002060	(Figure 4)
PMID:7876257	MOD:00006	(comment: endoglycosidase-H cleaves N-linked glycosylation)
PMID:7883794	PBO:0106434	(Figure 3B)
PMID:7883794	PBO:0106430	(Figure 1A)
PMID:7883794	PBO:0102251	Table 1, Figure 1B appearance of IC peak at early timepoint
PMID:7883794	PBO:0106432	(Figure 2C)
PMID:7883794	FYPO:0005773	Data not shown
PMID:7883794	PBO:0023560	(Figure 3A)
PMID:7883794	PBO:0106429	(Fig. 1B)
PMID:7883794	PBO:0106431	(Figure 2B)
PMID:7883794	PBO:0106433	Table 1, Figure 2C
PMID:7889932	GO:0000287	(comment: crystal structure)
PMID:7903653	FYPO:0000249	(comment: CHECK ABOLISHED)
PMID:7903653	FYPO:0000249	(comment: CHECK ABOLISHED
PMID:7903653	FYPO:0000249	(comment: CHECK ABOLISHED)
PMID:7909513	PBO:0106920	the basal level of the 3.2 kb transcript was lower than that in h90 wild type cells, but the 3 kb transcript was properly induced upon nitrogen starvation
PMID:7909513	PBO:0106921	(comment: 3 kb transcript)
PMID:7916658	FYPO:0001492	(comment: constitutive cdc18+ expression)
PMID:7916658	FYPO:0000012	(comment: constitutive cdc18+ expression)
PMID:7916658	FYPO:0001355	(comment: constitutive cdc18+ expression)
PMID:7916658	PBO:0105614	(comment: inferred from combination of phenotype shown in this paper with background knowledge)
PMID:7923372	PBO:0103991	(comment: they interacted in the Y2H experiment, so inferring this relationship)
PMID:7957097	FYPO:0004922	(comment: no mitotic spindle)
PMID:7957097	PBO:0099590	(comment: CHECK inhibits)
PMID:7957098	FYPO:0001933	(comment: CHECK same as rad4 cut5 allele alone)
PMID:7957098	FYPO:0001933	(comment: CHECK same as rad4 cut5 allele alone)
PMID:7957098	FYPO:0001933	(comment: CHECK same as rad4 cut5 allele alone)
PMID:7957098	FYPO:0001933	(comment: CHECK same as rad4 cut5 allele alone)
PMID:7957098	FYPO:0001933	(comment: CHECK same as rad4 cut5 allele alone)
PMID:7957098	FYPO:0001933	(comment: CHECK same as rad4 cut5 allele alone)
PMID:7957098	FYPO:0001916	(comment: CHECK same as cdc25-22 alone)
PMID:7957098	FYPO:0001933	(comment: CHECK same as rad4 cut5 allele alone)
PMID:7957098	FYPO:0001933	(comment: CHECK same as rad4 cut5 allele alone)
PMID:7957098	FYPO:0001933	(comment: CHECK same as rad4 cut5 allele alone)
PMID:7957098	FYPO:0001916	(comment: CHECK same as cdc13-117 alone)
PMID:7957098	FYPO:0001916	(comment: CHECK same as cdc2-33 alone)
PMID:7957098	PBO:0097701	(comment: CHECK same as cdc10-129 alone)
PMID:7975894	PBO:0107866	increased transcriptional response to nitrogen starvation
PMID:7975894	PBO:0107869	(comment: CHECK increased transcription from TR box SO:0001858)
PMID:7975894	PBO:0107866	increased transcriptional response to nitrogen starvation
PMID:7983142	PBO:0104310	(comment: CONDITION 33 degrees) (comment: may be standard for them)
PMID:7983142	FYPO:0000021	(comment: CONDITION 33 degrees) (comment: may be standard for them); (comment: CHECK morphology same as ppe1delta alone)
PMID:7983142	FYPO:0001357	(comment: CONDITION 33 degrees) (comment: may be standard for them)
PMID:7983142	FYPO:0000280	(comment: CONDITION 33 degrees) (comment: may be standard for them)
PMID:7983142	FYPO:0001253	(comment: CONDITION 33 degrees) (comment: may be standard for them)
PMID:7983142	FYPO:0001253	(comment: CONDITION 33 degrees) (comment: may be standard for them)
PMID:7983142	PBO:0026157	(comment: CONDITION 33 degrees (comment: may be standard for them)
PMID:8006074	FYPO:0000479	(Fig. 8)
PMID:8006074	FYPO:0000477	(Fig. 8)
PMID:8006074	FYPO:0000477	(Fig. 8)
PMID:8006074	FYPO:0001043	(Fig. 8)
PMID:8026462	FYPO:0001384	(comment: CHECK assayed using casein)
PMID:8087848	PBO:0099433	cdc10-129 cells blocked in G1 over expressing cdc2 from integrated pREP5cdc2 and cdc13 from episomal pREP41-cdc13. The nmt1 promoter is derepressed Figure 4
PMID:8087848	PBO:0099432	cdc10-129 cells blocked in G1 over expressing cdc2 from integrated pREP5cdc2 and cdc13 from episomal pREP41-cdc13. The nmt1 promoter is derepressed Figure 4
PMID:8087848	FYPO:0005711	p34cdc2 cdc13-9 complex was pulled down using p13suc1 beads and then western blotted using anti cdc13 antibody SP4 to show reduced levels of Cdc13 complexed with cdc2 compared to the wild type control
PMID:8087848	PBO:0037893	(Table 1)
PMID:8087848	PBO:0037892	FACS analysis of germinating haploid cdc13delta spores. Up to 32C DNA content was observed by 19 hour after referring spores to allow germination Figure 2
PMID:8087848	PBO:0037895	(Table 1)
PMID:8087848	PBO:0026408	germinating haploid cdc13delta spores, observed by 14 hour after spores allowed to germination (Figure 2b). cdc13delete cells kept alive by a multicopy plasmid, pSM2-cdc13. Cell phenotype was observed after plasmid loss same phenotype as in Figure 2b
PMID:8087848	PBO:0037896	cdc13delete cells were kept alive by episomal pSM2 cdc13. Cell phenotype was observed after plasmid loss. Figure 2C
PMID:8087848	PBO:0037895	(Table 1)
PMID:8121488	PBO:0112244	(Fig. 4E,G) In cdc10-129 rum1 delta strain cells at 36 fail to activate the DNA replication checkpoint in the absence of rum1 and cells proceed into mitosis in the presence of HU and enter mitosis with reduced DNA content
PMID:8121488	FYPO:0007476	data not shown, cells become arrest in G2
PMID:8121488	FYPO:0001425	At both temperatures the DNA content per cell continued to increase, demonstrating that the G2-arrested cells were able to undergo further rounds of S phase (Fig. 2c and d, right) .
PMID:8121488	PBO:0112242	(Fig. 3a)
PMID:8121488	FYPO:0005097	(Fig. 4a) elongated cell, cells do not replicate DNA (never enter S phase), but keep growing
PMID:8121488	PBO:0112243	xpression results in a small delay of S phase onset until cells attain a higher mass, suggesting the rumr gene product may act as a transient inhibitor of progression through GI into S phase. The appearance of a small population of IC cells at 16 h is consistent with this interpretation (Fig. lb).
PMID:8121488	PBO:0112243	xpression results in a small delay of S phase onset until cells attain a higher mass, suggesting the rumr gene product may act as a transient inhibitor of progression through GI into S phase. The appearance of a small population of IC cells at 16 h is consistent with this interpretation (Fig. lb).
PMID:8121488	PBO:0112244	(Fig. 4d, f) In cdc10-129 rum1 delta strain cells fail to activate the DNA replication checkpoint in the absence of rum1 and cells proceed into mitosis in the absence of DNA replication and enter mitosis with reduced DNA content proce of DNA replication and
PMID:8121488	PBO:0112241	(comment: negative regulation/(I now think this is the same as G1 checkpoint).) expression results in a small delay of S phase onset until cells attain a higher mass, suggesting the rumr gene product may act as a transient inhibitor of progression through GI into S phase. The appearance of a small population of IC cells at 16 h is consistent with this interpretation (Fig. lb).
PMID:8121488	PBO:0112239	(Table 1)
PMID:8121488	PBO:0112238	(Fig. 2B) (comment: prestart)
PMID:8121488	PBO:0112237	(comment: CHECK in vitro assay) data not shown
PMID:8121488	PBO:0026408	(Fig. 1A) Overreplicating haploid cells become highly enlarged (Fig. la, left)
PMID:8121488	PBO:0112236	Table 1 (comment: CHECK increased cell size required for the G1/S transition.)
PMID:8121488	PBO:0037896	(comment: (transient expression)) most surviving cells generated diploid or tetraploid clones/ if rum was derepressed for only a short period, most surviving cells generated diploid or tetraploid clones, as would be expected if there were complete rounds of DNA replication. Fig1b
PMID:8121488	FYPO:0001425	(Fig. 1B) (comment: they give a pulse of rum1)
PMID:8121488	PBO:0112240	(Fig. 4A, B) In cdc10-129 rum1 delta strain cells fail to activate the DNA replication checkpoint in the absence of DNA replication and
PMID:8163505	GO:0004674	(comment: based on phenotype this annotation is possible)
PMID:8187760	FYPO:0000839	(comment: same as cdc2-33 alone)
PMID:8187760	FYPO:0004105	(comment: grows in three dimensions instead of just at cell ends)
PMID:8187760	FYPO:0000839	(comment: same as cdc25-22 alone)
PMID:8187760	FYPO:0001382	(comment: assayed in vitro using casein)
PMID:8223442	FYPO:0007564	(Fig. 1)
PMID:8223442	FYPO:0007565	(Fig. 1)
PMID:8227198	FYPO:0001665	(comment: response curve differs from wt and other git mutants)
PMID:8264625	GO:0043539	(comment: casein substrate (vw changed from GO:0004674 with contributes to))
PMID:8264625	GO:0004674	(comment: casein substrate)
PMID:8292390	PBO:0096647	(comment: CHECK same as cps8-185 alone)
PMID:8299169	FYPO:0002068	(comment: CHECK C868T (nt))
PMID:8319772	MOD:00046	(comment: present throughout cell cycle)
PMID:8334988	FYPO:0002987	binucleate fypo/issues/#2400 fypo/issues/#2401
PMID:8413241	PBO:0105255	(comment: tyrosine; residue not determined)
PMID:8413241	PBO:0105255	(comment: tyrosine; residue not determined)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	PBO:0019154	Table 1 (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0002061	Table 1 (comment: CHECK nmt1 promoter ON)
PMID:8437586	PBO:0019154	Table 1 (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0002061	Table 1 (comment: CHECK nmt1 promoter ON)
PMID:8437586	PBO:0019154	Table 1 (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0002061	Table 1, Fig 4 (comment: CHECK nmt1 promoter ON)
PMID:8437586	PBO:0019154	Table 1, Fig 4 (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0002061	(Fig. 4, Table 1) (comment: CHECK nmt1 promoter ON)
PMID:8437586	PBO:0019154	(Fig. 4, Table 1) (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0002061	Table 1 (comment: CHECK nmt1 promoter ON)
PMID:8437586	PBO:0019154	Table 1 (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0002061	(Fig. 4) (comment: CHECK nmt1 promoter ON)
PMID:8437586	PBO:0019154	(Fig. 4) (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0002061	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0001490	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0001490	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 no suppression)
PMID:8437586	FYPO:0002085	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0001490	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 no suppression)
PMID:8437586	FYPO:0002085	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0001490	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 no suppression)
PMID:8437586	FYPO:0002085	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0001490	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 no suppression)
PMID:8437586	FYPO:0002085	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0001490	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0001490	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 no suppression)
PMID:8437586	FYPO:0002085	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0001490	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype)
PMID:8437586	FYPO:0002085	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	(comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	PBO:0019154	(comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	(comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	PBO:0038194	Table1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0019154	(comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0000082	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 partially supresses the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype)
PMID:8437586	FYPO:0002061	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0093712	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0037209	Table 1, Fig 2 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0093712	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0001234	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 partially suppresses the ts phenotype)
PMID:8437586	PBO:0038194	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype)
PMID:8437586	PBO:0038194	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	PBO:0019154	(comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	(comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	PBO:0019154	(comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0093712	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0001234	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0099234	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 surpresses the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0000082	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 partially supresses the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	Table1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0093712	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype)
PMID:8437586	FYPO:0002061	Table 1 (comment: CHECK nmt1 promoter ON)
PMID:8437586	PBO:0097954	(Fig. 5) (comment: CHECK nmt1 promoter ON)
PMID:8437586	PBO:0097954	(Fig. 5) (comment: CHECK nmt1 promoter ON)
PMID:8437586	PBO:0097954	(Fig. 5) (comment: CHECK nmt1 promoter ON)
PMID:8437586	PBO:0100985	Table 1, Fig 4 (comment: CHECK nmt1 ON)
PMID:8437586	PBO:0019154	Cdc2 is only mildly over expressed as it is expressed from a multi copy plasmid pIRT2. This is much lower over expression than from the nmt1 promoter and for all the other annotations were the cdc2 mutant is expressed from pIRT2 I have said 'unknown' for expression level
PMID:8437586	FYPO:0002061	Cdc2 is only mildly over expressed as it is expressed from a multi copy plasmid pIRT2. This is much lower over expression than from the nmt1 promoter and for all the other annotations were the cdc2 mutant is expressed from pIRT2 I have said 'unknown' for expression level
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	FYPO:0002061	(comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0020446	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002060	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 give partial suppression)
PMID:8437586	FYPO:0000082	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0019143	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 partially supresses the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	(comment: mutant expressed from multi copy plasmid has dominant negative phenotype) Table 1
PMID:8437586	PBO:0019154	(comment: mutant expressed from multi copy plasmid has dominant negative phenotype) Table 1
PMID:8437586	FYPO:0002061	(comment: mutant expressed from multi copy plasmid has dominant negative phenotype) Table 1
PMID:8437586	PBO:0019154	(comment: mutant expressed from multi copy plasmid has dominant negative phenotype) Table 1
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant expressed from multi copy plasmid has dominant negative phenotype)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant expressed from multi copy plasmid has dominant negative phenotype)
PMID:8437586	FYPO:0002061	(comment: mutant expressed from multi copy plasmid has dominant negative phenotype) Table 1
PMID:8437586	PBO:0019154	(comment: mutant expressed from multi copy plasmid has dominant negative phenotype) Table 1
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0020446	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype)
PMID:8437586	FYPO:0000082	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	PBO:0038194	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0019154	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant expressed from multi copy plasmid pIRT2)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	PBO:0038194	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0107596	Table 1, Fig2 (comment: mutant gene expressed from multicopy plasmid pIRT2 partially suppresses the ts phenotype)
PMID:8437586	PBO:0093712	Table 1, Fig 2 (comment: mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype)
PMID:8437586	FYPO:0002061	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	PBO:0107595	(Fig. 5) increased duration of G1 phase
PMID:8463273	GO:0004699	(comment: kinase assay, and hybridization with S. cerevisiae PKC)
PMID:8485317	FYPO:0002060	(comment: like dis1-288 alone)
PMID:8485317	FYPO:0002061	(comment: like dis1-288 alone)
PMID:8496185	GO:0004017	(comment: CHECK inhibited by P(1),P(5)-bis(5'-adenosyl) pentaphosphate(5-)?)
PMID:8497322	FYPO:0002061	(Fig. 3)
PMID:8497322	PBO:0094950	(Fig. 2a) (comment: DROPS TO ZERO)
PMID:8497322	PBO:0094949	(Fig. 2c)
PMID:8497322	PBO:0093631	partial rescue of chk1, fig 2b
PMID:8497322	PBO:0093630	(Fig. 2a)
PMID:8497322	FYPO:0002060	(Fig. 3a)
PMID:8497322	PBO:0093629	(Fig. 2c)
PMID:8497322	FYPO:0006822	(Fig. 3) (comment: CHECK fypo/issues/2818)
PMID:8497322	FYPO:0001046	(Fig. 3) (comment: CHECK fypo/issues/2818)
PMID:8497322	PBO:0093630	(Fig. 2c)
PMID:8497322	FYPO:0001971	(Fig. 3) cells fail to separate and are clupmed together, multiple rounds of nuclear division
PMID:8497322	PBO:0094952	(Fig. 2c)
PMID:8497322	PBO:0093581	(Fig. 4)
PMID:8497322	FYPO:0002061	data not shown
PMID:8515818	FYPO:0002060	(Fig. 1b bottom R panel , bottom R)
PMID:8515818	PBO:0097560	(Fig. 2a lane 3)
PMID:8515818	PBO:0097561	(Fig. 4a,b, Fig. 2,3)
PMID:8515818	MOD:00046	(Fig. 2b)
PMID:8515818	MOD:00047	(Fig. 2b)
PMID:8515818	PBO:0019218	(Fig. 1b bottom R panel, top)
PMID:8515818	FYPO:0002060	(Fig. 1b top R panel bottom R)
PMID:8515818	PBO:0097558	(Fig. 1b top R panel bottom R)
PMID:8515818	PBO:0019218	(Fig. 1b top R panel, top)
PMID:8515818	PBO:0019218	(Fig. 1b top R panel bottom L)
PMID:8515818	FYPO:0006822	data not shown
PMID:8515818	MOD:00047	(Fig. 2b)
PMID:8515818	MOD:00046	(Fig. 2b)
PMID:8515818	FYPO:0002061	(Fig. 1b top R panel bottom L)
PMID:8515818	FYPO:0002061	(Fig. 1b top R panel, top)
PMID:8515818	FYPO:0002061	(Fig. 1b bottom R panel, top)
PMID:8515818	PBO:0019218	(Fig. 1b bottom R panel, bottom L)
PMID:8515818	FYPO:0002061	(Fig. 1b bottom R panel, bottom L)
PMID:8515818	PBO:0097558	(Fig. 1b bottom R panel , bottom R)
PMID:8515818	PBO:0097559	(Fig. 2a lane 1)
PMID:8521469	FYPO:0001425	(comment: CHECK same as cdc18+ oe alone)
PMID:8521469	FYPO:0001425	(comment: CHECK same as cdc18+ oe alone)
PMID:8521500	PBO:0101301	(Fig. 6) cdc2-cig1 complex is insensitive to inhibition by rum1. There is ~100% activity in the presence of 26nM rum
PMID:8521500	PBO:0101300	(comment: CHECK [ move to specific cyclin]) Fig6 2.6nM rum1 inhibits cig2 associated cdc2 kinase activity by ~50%
PMID:8521500	PBO:0101299	(Fig. 5B) over expression abolishes cdc13 associated kinase activity even in absence of added rum1 protein
PMID:8521500	PBO:0101298	(Fig. 5B) over expression reduces cdc2 kinase activity even in absence of added rum1 protein
PMID:8521500	PBO:0101297	(Fig. 5A)
PMID:8521500	PBO:0101296	(Fig. 5A)
PMID:8521500	PBO:0101295	(Fig. 3C)
PMID:8521500	PBO:0101294	(Fig. 3C)
PMID:8521500	PBO:0101293	(Fig. 4) (comment: rum1HA pulldown brings down both cdc13 and cdc2 to form rum1-cdc13-cdc2 complex. so I really need to add 3 proteins not two in the annotation extensions)
PMID:8521500	PBO:0101292	(Fig. 3B)
PMID:8521500	PBO:0101291	(Fig. 3B)
PMID:8521500	PBO:0101290	(Fig. 3A)
PMID:8521500	PBO:0101289	(Fig. 3A)
PMID:8521500	PBO:0101289	(Fig. 3A)
PMID:8521500	PBO:0101288	(Fig. 3A)
PMID:8521500	PBO:0101287	(Fig. 3A)
PMID:8521500	PBO:0101286	(Fig. 2C) (comment: rum1+ driven by nmt1 promoter in pREP6X is integrated)
PMID:8521500	PBO:0101285	(comment: CHECK [MOVE 'occurs at' TO M-PHASE CYCLIN]) Fig1 and 2B 0.26nM pRum1 inhibits in vitro cdc2-cdc13 kinase activity by ~80%, Fig3C ig5B,C, D addition of 2.6nM rum1 reduces cdc2 associated kinase activity
PMID:8521500	PBO:0096558	(Fig. 1) (comment: Histone H1 used as substrate)
PMID:8521500	PBO:0101284	(Fig. 1) (comment: Histone H1 used as substrate)
PMID:8522609	FYPO:0000647	(comment: same as orb3-167 alone)
PMID:8522609	FYPO:0001018	(comment: same as orb2-34 alone)
PMID:8522609	FYPO:0001018	(comment: same as orb2-34 alone)
PMID:8522609	FYPO:0000839	(comment: same as cdc2-33 alone)
PMID:8522609	FYPO:0001418	(comment: same as orb3-167 alone)
PMID:8522609	FYPO:0002021	(comment: same as orb3-167 alone)
PMID:8552670	PBO:0104786	(comment: CHECK activated_by(CHEBI:18420))
PMID:8557036	GO:0004693	assayed in S. cerevisiae cell extracts, with S.c. CDK2 substrate
PMID:8557036	GO:0008353	assayed in S. cerevisiae cell extracts, with S.c. CTD substrate
PMID:8557037	GO:0004693	(comment: CHECK activated_by(CHEBI:63041))
PMID:8569679	FYPO:0002061	(Fig. 2)
PMID:8569679	FYPO:0002061	(Fig. 2)
PMID:8569679	FYPO:0002061	(Fig. 2)
PMID:8569679	FYPO:0002061	(Fig. 2)
PMID:8569679	FYPO:0002061	(Fig. 2)
PMID:8569679	FYPO:0002061	(Fig. 2)
PMID:8569679	FYPO:0002061	(Fig. 2)
PMID:8569679	FYPO:0002061	(Fig. 2)
PMID:8590464	GO:0004043	(comment: CHECK inhibited_by L-lysine)
PMID:8590465	GO:0004151	(comment: cryptic dihydroorotase domain)
PMID:8590474	PBO:0095685	(comment: CHECK partial rescuie)
PMID:8599928	FYPO:0002060	Tetrad analysis showed that all four haploid spores of the heterozygous diploid produced colonies at 28°C, indicating that the wis2+ gene is non-essential for viability under normal growth conditions.
PMID:8599928	FYPO:0001124	Microscopic examination failed to detect any difference in cell size or morphology between wis2+-deleted cels (wis2A) and wild-type cels,over a range oftemperatures from 20 to 36°C.
PMID:8618924	PBO:0114929	(comment: also inferred from orthology to all other Orc1s in the world)
PMID:8621436	FYPO:0000158	(comment: they show it is not abnormal regulation of rereplication in cdc25 double mutant expts)
PMID:8621436	FYPO:0002303	(comment: transient phenotype, they then attempt to divide without segregation)
PMID:8621436	FYPO:0000158	(comment: they show it is not abnormal regulation of rereplication in cdc25 double mutant expts)
PMID:8621436	FYPO:0000620	(comment: transient phenotype, they then attempt to divide without segregation)
PMID:8621436	FYPO:0002303	(comment: transient phenotype, they then attempt to divide without segregation)
PMID:8621436	FYPO:0000620	(comment: transient phenotype, they then attempt to divide without segregation)
PMID:8649397	FYPO:0001122	(comment: Can't say if they are viable vegetative because it is in a pyp2+ background)
PMID:8654750	PBO:0099148	(comment: PHEROMONE)
PMID:8668131	GO:0006744	(comment: functionally complements S cerevisiae ABC1)
PMID:8688826	GO:0034399	(vw: changed from nuclear lumen to nuclear periphery)
PMID:872890	PBO:0093712	(Fig. 1) data not shown cdc2-1w is called wee 2-1 in this paper. Wee cells enter mitosis at a small cell size compared to wild type cells and thus daughter cells are born smaller than wild type cells. Wee cells have similar cell cycle timing (doubling time) to wild type cells
PMID:872890	FYPO:0006909	Table 1, DNA replication initiated at low protein content
PMID:872890	FYPO:0006909	(Table 1)
PMID:872890	PBO:0103505	(Fig. 6, Table 2) cell size measure by protein content per cell, cells need to reach ~7pg/cell. This measurement is also the same for wild type cells which are small after nitrogen starvation (Fig5)
PMID:872890	FYPO:0006905	(Fig. 2) This suggests that wee1-50 only has an indirect effect on the G1-S transition because when wee1-50 is shifted to the permissive temperature cells are still small, this is not affected by the presence of active wee1 and cells enter S-phase at the same size as they did at the restrictive temperature
PMID:872890	FYPO:0006906	(Fig. 2) This shows that wee1-50 has a direct effect on the G2-M transition because cells now at the permissive temperature (active wee1) detect that they are too small to enter mitosis and the G2/M transition is inhibited
PMID:872890	PBO:0103506	(Fig. 4, Table 2) cell size measure by protein content per cell, cells need to reach ~7pg/cell. This measurement is also the same for wild type cells which are small after spore germination (Fig3)
PMID:872890	FYPO:0006031	Table 1, Fig1
PMID:872890	PBO:0102251	Table 1, Fig1
PMID:8799335	PBO:0092041	(comment: present with ammonium, allantoin, or proline nitrogen source)
PMID:8799851	PBO:0101514	(Fig. 10)
PMID:8799851	PBO:0101511	Data not shown cdc13 protein level in asynchronous culture of wee1-50 cells at restrictive temperature is reduced by 40% compared to asynchronous culture of WT cells
PMID:8799851	PBO:0101513	(Fig. 9)
PMID:8799851	PBO:0101512	Uses elutriation synchrony. Fig5 cdc13 protein level in synchronous culture of wee1-50 cells at restrictive temperature is absent during longer G1 phase
PMID:8811082	GO:0000703	(comment: CHECK thymine glycols, urea)
PMID:8811082	GO:0140078	The capacity of Nth-Spo to generate strand breaks in a variety of damaged plasmid DNA substrates was investigated. Figure 4shows the activity of Nth-Spo and Nth-Eco in incising supercoiled damaged DNA. None of the proteins caused breaks in undamaged DNA.
PMID:8824588	PBO:0105349	(comment: also has AP1 binding site)
PMID:8834798	FYPO:0000117	abnormal septum forms on the surface from one side of the cell and then extends in a disorganized manner into the interior
PMID:8876193	PBO:0099352	data not shown, cells blocked in absence of septation, cells need to complete cell cycle to observe asymmetry
PMID:8876193	PBO:0099356	Fig. 3
PMID:8876193	PBO:0099355	Fig. 3
PMID:8876193	PBO:0099354	(Fig. 2) 1% of cells still have a short mitotic spindle after 5h at restrictive temperature
PMID:8876193	PBO:0099353	Fig. 2
PMID:8876193	PBO:0099352	data not shown, cells blocked in S phase, cells need to complete cell cycle to observe asymmetry
PMID:8876193	PBO:0099352	data not shown, cells blocked at G1/S, cells need to complete cell cycle to observe asymmetry
PMID:8876193	PBO:0099351	(comment: data not shown)
PMID:8876193	PBO:0099350	73% asymmetric distribution at old end by 5 hours asymmetric mitochondrial aggregation at old cell end
PMID:8876193	PBO:0099352	data not shown, cells blocked at G2/M, cells need to complete cell cycle to observe asymmetry
PMID:8876193	PBO:0099349	(Fig. 1) 77% asymmetric distribution by 5 hours, aggregation observed after 1 hour
PMID:8876193	GO:0048311	(Fig. 4)
PMID:8898110	FYPO:0006144	(Fig. 6)
PMID:8898110	FYPO:0006144	(Fig. 6)
PMID:8918598	FYPO:0005112	(comment: ubiquitin conjugate)
PMID:8918598	FYPO:0005112	(comment: ubiquitin conjugate)
PMID:8918880	FYPO:0002060	(Fig. 1)
PMID:8918880	FYPO:0002060	(Fig. 1)
PMID:8918880	FYPO:0002060	(Fig. 1)
PMID:8918880	FYPO:0002061	(Fig. 1)
PMID:8918880	GO:0005680	(Fig. 5)
PMID:8943330	PBO:0095167	(comment: tyrosine; position(s) not determined)
PMID:8943330	GO:0000196	(comment: CHECK not sure this annotation is 100% supported, can revise later if needed.)
PMID:8946912	FYPO:0003210	(Fig. 2a)
PMID:8946912	FYPO:0002070	(Fig. 2a)
PMID:8946912	FYPO:0001007	(Fig. 2a)
PMID:8946912	FYPO:0001234	(Fig. 3)
PMID:8978670	FYPO:0002023	(Figure 1)
PMID:8978670	FYPO:0002024	(Figure 1)
PMID:8978670	FYPO:0000417	(Figure 1)
PMID:8978670	FYPO:0001008	(Figure 1)
PMID:8978687	FYPO:0005393	(Fig. 7)
PMID:8978687	FYPO:0002060	(Figure 2)
PMID:8978687	FYPO:0002060	(Figure 1a)
PMID:8978687	FYPO:0001368	(Fig. 4b)
PMID:8978687	FYPO:0002018	(Figure 5)
PMID:8978687	FYPO:0002018	(Figure 5)
PMID:8978687	FYPO:0001705	(Figure 5)
PMID:8978687	FYPO:0004474	(Figure 5)
PMID:8978687	FYPO:0005371	(Figure 6)
PMID:8978687	PBO:0104407	(Fig. 6c)
PMID:8978687	FYPO:0004648	(Fig. 6a)
PMID:8978687	FYPO:0000729	(Fig. 6a)
PMID:8978687	FYPO:0003758	(Fig. 6a)
PMID:8978687	FYPO:0002049	(Fig. 7)
PMID:8978689	FYPO:0002060	A multicopy plasmid which conferred the ability to suppress ts sds22-181 was isolated.
PMID:8978689	FYPO:0006821	The cell division rates of Asds23 at the permissive temperatureswereexceedinglyslow.Thegenerationtimes inrichYPD mediumwere5.7(3.3)and4.3(2.2)hat26 and 33°C, respectively; the values in parenthesis are the generationtimesforthewild-typestrain.
PMID:8978689	FYPO:0000133	The cell division rates of Asds23 at the permissive temperatureswereexceedinglyslow.Thegenerationtimes inrichYPD mediumwere5.7(3.3)and4.3(2.2)hat26 and 33°C, respectively; the values in parenthesis are the generationtimesforthewild-typestrain.
PMID:8978689	FYPO:0002061	(Figure ID, -Thi, Dis2),which allows for colony formation. Cells producing the mutant T316A protein under the strong promoter, on the other hand, severely blocked colony formation (Figure ID,-Thi,Dis2T316A)
PMID:8978689	FYPO:0002060	A multicopy plasmid which conferred the ability to suppress ts sds22-181 was isolated.
PMID:8978689	PBO:0116400	A temperature shift (G2 block and release) experiment using the cdc25-22 mutant showed that the level of T316-phosphorylated Dis2 peaked in mitosis(Figure2A).
PMID:8978689	FYPO:0007303	(Figure 3A) because the spindle elongates in the absence of sister chromatid separation.
PMID:8978689	FYPO:0007664	(Figure 3A) abnormal cell cycle arrest in mitotic metaphase, condend chrosmosmes
PMID:8978689	FYPO:0004022	(Figure 3A) However, dis2-11 displayed an allele-specific mitotic phenotype with spindle elongation (Ohkura et al., 1989; see Figure 3A).
PMID:8978689	FYPO:0007664	(Figure 3A)
PMID:8978689	FYPO:0002061	Heterozygous diploids verified by Southern hybridization (lower panel) yielded four viable spores at 26 or 33°C with Ade+ segregating 2+:2-, indicating that the sds23+ gene was not essential for viability. Colonies were not formed at 22 or 36°C, however (Figure 6B), indicating that the gene-disrupted Asds23 causes cold and temperature sensitivity.
PMID:8978689	FYPO:0007303	In parallel with the increase in plasmid loss, cells containing condensed chromosomes with a short metaphase spindle dramatically increased (Figure 3C). After transferring the culture from selective to non-selective medium at 33°C, the fraction of these metaphase-arrested cells increased about nine times within 20 h (from 2 to 19%). We concluded, therefore, that the complete absence of PPI in fission yeast leads to the metaphase arrest, which is strikingly similar to the phenotype of sds22 mutants. More than 90% of the cells examined contained condensed chromosomes (Figure 3B, upper panel).
PMID:8978689	FYPO:0002061	(Figure 3A) abnormal cell cycle arrest in mitotic metaphase, condend chrosmosmes
PMID:8978689	FYPO:0002061	Heterozygous diploids verified by Southern hybridization (lower panel) yielded four viable spores at 26 or 33°C with Ade+ segregating 2+:2-, indicating that the sds23+ gene was not essential for viability. Colonies were not formed at 22 or 36°C, however (Figure 6B), indicating that the gene-disrupted Asds23 causes cold and temperature sensitivity.
PMID:8978689	FYPO:0002060	Heterozygous diploids verified by Southern hybridization (lower panel) yielded four viable spores at 26 or 33°C with Ade+ segregating 2+:2-, indicating that the sds23+ gene was not essential for viability. Colonies were not formed at 22 or 36°C, however (Figure 6B), indicating that the gene-disrupted Asds23 causes cold and temperature sensitivity.
PMID:9024682	PBO:0096483	(comment: severe when both cells are cpb1delta)
PMID:9034337	PBO:0096052	(Fig. 2B) (comment: Histone H1 used as cdc2 substrate Chk2 expressed from nmt1 promoter)
PMID:9034337	FYPO:0002085	Data not shown chk1+ over expression phenotype is suppressed by over expressing cdc25+ independently of cdr1
PMID:9034337	PBO:0106846	(Fig. 4)
PMID:9034337	PBO:0108717	(Fig. 5, 6)
PMID:9034337	PBO:0099201	(Fig. 6) GST wee1 has been phosphorylated in vitro by chk1. This assay shows that phosphorylation of wee1 by chk1 does not affect wee1 kinase activity
PMID:9034337	PBO:0095685	(Fig. 3B)
PMID:9034337	FYPO:0000444	(Fig. 2D)
PMID:9034337	FYPO:0001575	(Fig. 2A)
PMID:9034337	PBO:0106845	(Fig. 2C)
PMID:9034337	PBO:0108716	(Fig. 1)
PMID:9034337	PBO:0095634	(Fig. 3B)
PMID:9034337	FYPO:0002060	(Fig. 3A)
PMID:9034337	FYPO:0001974	(Fig. 3C) wee cell phenotype cell cycle distribution FACS profile of vegetatively growing wee cells show a cell cycle distribution with increased number of cells with a 1C DNA content compared to wild type cells. Note the increase in the G1 peak depends on the size of the cell and semi-wee cells do not always shown an increased G1 peak
PMID:9034337	PBO:0093712	(Fig. 3C) cell elongation as a result of chk1 over expression is dependent on wee1+
PMID:9034337	FYPO:0005773	(Fig. 2D)
PMID:9042863	FYPO:0007248	(comment: temperature restrictive for wee1-50)
PMID:9042863	FYPO:0001046	(comment: temperature permissive for wee1-50; un-irradiated)
PMID:9042863	GO:0072435	(comment: Activity inhibited in response to mitotic G2 DNA damage checkpoint)
PMID:9042863	PBO:0108718	(comment: dephosphorylation of Cdc2 Y15 by Cdc25 delayed in response to ionising radiation)
PMID:9055078	PBO:0112866	(Fig. 7A)
PMID:9055078	PBO:0112866	(Fig. 7A)
PMID:9055078	PBO:0112866	(Fig. 7A)
PMID:9055078	PBO:0112866	(Fig. 7A)
PMID:9062192	GO:0051728	(comment: mei2 promotes g1 arrest, premeiotic dna replication and meiosis I)
PMID:9078390	PBO:0096205	(Fig. 2C)
PMID:9078390	PBO:0096204	(Fig. 2C)
PMID:9078390	PBO:0096202	(Fig. 2C)
PMID:9078390	PBO:0096205	(Fig. 2C)
PMID:9078390	FYPO:0002061	(Fig. 3a)
PMID:9078390	FYPO:0002061	(Fig. 3a)
PMID:9078390	PBO:0037209	(Fig. 3a)
PMID:9078390	FYPO:0002061	(Fig. 3a)
PMID:9078390	PBO:0037209	(Fig. 3a)
PMID:9078390	PBO:0096202	(Fig. 2C)
PMID:9078390	PBO:0096203	(Fig. 2C)
PMID:9090050	PBO:0114483	inhibition by CCCP and DCCD
PMID:9092661	PBO:0109839	(comment: Cell survival assay)
PMID:9092661	PBO:0110294	(Figure 4)
PMID:9092661	PBO:0109839	(comment: Cell survival assay)
PMID:9092661	PBO:0106872	(comment: Cell survival assay)
PMID:9092661	PBO:0106872	(comment: Cell survival assay)
PMID:9092661	PBO:0110293	We found that the double mutant uvded rad2d was more resistant than a rad2d single mutant (Fig. 3).
PMID:9092661	PBO:0110295	Furthermore, a rad13d uvded rad2d triple disruptant had the same UV sensitivity as the rad13d uvded double disruptant.
PMID:9092661	PBO:0110294	(Figure 5)
PMID:9092661	PBO:0110293	We found that the double mutant uvded rad2d was more resistant than a rad2d single mutant (Fig. 3).
PMID:9092661	PBO:0110294	(Figure 4)
PMID:9092661	PBO:0110295	(Figure 4) The rad13d uvded double mutant cells were unable to remove either type of damage, even during 3 h post-UV incubation.
PMID:9092661	GO:0070914	We found that the double mutant uvded rad2d was more resistant than a rad2d single mutant (Fig. 3). This implies that the Rad2 protein is very important for processing nicks introduced by UVDE..........These results show that the Rad2 protein is involved only in the UVDE-mediated second pathway and that there are both rad2-dependent and rad2-independent components of the UVDE-mediated repair pathway.
PMID:9092661	PBO:0110293	(Figure 2) ...The uvde gene disruption made cells only mildly sensitive to UV, even after high doses.
PMID:9105045	PBO:0105900	(comment: cdc12 froms a cortical spot)
PMID:9111307	FYPO:0003241	(comment: CHECK not sure if this is the right term, sent a question)
PMID:9125114	PBO:0096500	(comment: CHECK also increased (WT overexppression)) (comment: CHECK normal (WT))
PMID:9135147	PBO:0095167	(comment: yrosine; residue not determined)
PMID:9135148	PBO:0094619	(comment: inferring that residue is Y15, though not shown experimentally)
PMID:9136929	PBO:0094396	(comment: not annotated to other stresses as subsequent papers show it is critical for assembly of signaling MAPKKK-MAPKKmodule)
PMID:9153313	PBO:0093629	(comment: same as crb2delta alone)
PMID:9153313	PBO:0093629	(comment: same as rad3delta alone)
PMID:9153313	PBO:0093629	(comment: same as rad26delta alone)
PMID:9154834	PBO:0095824	(comment: residue not determined, but probably Y173)
PMID:9154834	FYPO:0004254	(comment: doesn't resume normally)
PMID:9154834	PBO:0105229	(comment: residue not determined, but probably Y173)
PMID:9154838	PBO:0032853	(comment: has condensed chromosomes)
PMID:9177184	PBO:0098824	as cyclin-CDK complex with Cdc13 or Cig2
PMID:9182664	FYPO:0003413	(comment: CHECK swollen)
PMID:9182664	FYPO:0002845	(comment: this might be dumbbell ask Jacky)
PMID:9182664	FYPO:0002462	(comment: CHECK swollen)
PMID:9200612	PBO:0097436	data not shown
PMID:9200612	PBO:0097437	data not shown. 95% of cells re bent or T shaped but don't say the different percentages so I've left it as bent
PMID:9200612	FYPO:0002177	data not shown. tea1 on multi copy plasmid -R2 suppresses the cell shape defect of tea1 delta
PMID:9200612	PBO:0097438	(Fig. 2B, 2C)
PMID:9200612	PBO:0097439	(Fig. 2B, 2C)
PMID:9200612	FYPO:0001587	(Fig. 2C) protein localised to both cell tips
PMID:9200612	FYPO:0001587	(Fig. 2C) Protein localised to both cell tips during monopolar growth
PMID:9200612	FYPO:0001587	(Fig. 2D) Protein localised to both cell tips during monopolar growth
PMID:9200612	PBO:0097440	(Fig. 3A)
PMID:9200612	PBO:0097441	(Fig. 3A)
PMID:9200612	PBO:0097442	(Fig. 4A)
PMID:9200612	PBO:0097443	(Fig. 4A)
PMID:9200612	PBO:0097443	(Fig. 4A)
PMID:9200612	PBO:0097442	(Fig. 4A)
PMID:9200612	PBO:0037217	(Fig. 5) (comment: shown using TBZ treatment and wash out and by cold shock and relocalization)
PMID:9200612	PBO:0097444	(Fig. 5C)
PMID:9200612	PBO:0097445	(Fig. 5C)
PMID:9200612	PBO:0097446	(Fig. 5C)
PMID:9200612	PBO:0097445	(Fig. 5C) (comment: cells blocked in mitosis so have no interphase MTs)
PMID:9200612	PBO:0097447	(Fig. 6D)
PMID:9200612	PBO:0096501	(Fig. 6D)
PMID:9200612	PBO:0097448	(Fig. 1C ii)
PMID:9200612	PBO:0097449	(Fig. 1C iii)
PMID:9200612	PBO:0097433	(Fig. 1C ii)
PMID:9200612	PBO:0097434	(Fig. 1C iii)
PMID:9200612	PBO:0097435	(Fig. 1C iii)
PMID:9201720	PBO:0103195	(comment: not shown that it is ser/thr kinase activity, just that it is kinase activity)
PMID:9202173	FYPO:0003458	(Fig. 6)
PMID:9202173	FYPO:0001682	(Fig. 5)
PMID:9202173	FYPO:0003265	(Fig. 7)
PMID:9202173	FYPO:0003265	(Fig. 7)
PMID:9202173	FYPO:0003458	(Fig. 6)
PMID:9211982	FYPO:0003698	truncated Gar2 accumulates in this dense body
PMID:9252327	PBO:0098712	Cells look normal in early generation, but show many elongated cells in later generation due to telomere shortening.
PMID:9252327	PBO:0093560	Cell growth rate is reduced in later generation due to telomere shortening. In early generation, cells growth rate is not distingushiable from trt1+ cells.
PMID:9252327	PBO:0093560	This allele removes motif B' through E in reverse transcriptase domain of telomerase catalytic subunit. This allele showed similar delayed grow defect phenotype as trt1∆::his3+ allele that remove 99% of ORF.
PMID:9252327	PBO:0093637	Cells show progressive telomere shortening.
PMID:9252327	PBO:0093637	This allele removes motif B' through E in reverse transcriptase domain of telomerase catalytic subunit. This allele showed similar rate of telomere shortening as trt1∆::his3+ allele that remove 99% of ORF.
PMID:9252327	PBO:0098712	This allele removes motif B' through E in reverse transcriptase domain of telomerase catalytic subunit. This allele showed similar extent of delayed cell elongation phenotype as trt1∆::his3+ allele that remove 99% of ORF.
PMID:9278510	FYPO:0004259	(Fig. 1)
PMID:9278510	PBO:0037311	(Fig. 2b)
PMID:9278510	PBO:0037311	(Fig. 2b)
PMID:9285594	GO:0000796	(Fig. 1)
PMID:9285594	GO:0000796	(Fig. 1)
PMID:9285594	PBO:0101680	(comment: CHECK in vitro)
PMID:9301023	FYPO:0002519	(Figure 2b)
PMID:9301023	PBO:0098600	(Figure 2a)
PMID:9303310	PBO:0096940	(Fig. 2, Fig. 3)
PMID:9303310	PBO:0096942	(Fig. 8) (comment: added by cig1 associated CDK1)
PMID:9303310	PBO:0096943	(Fig. 7B)
PMID:9303310	FYPO:0000333	(Fig. 7A)
PMID:9303310	PBO:0096936	(Fig. 1) (comment: exponentially growing cells mainly in G2)
PMID:9303310	PBO:0096937	(Fig. 2)
PMID:9303310	PBO:0096936	(Fig. 1) cells blocked in G1 at the restrictive temp
PMID:9303310	PBO:0096938	(Fig. 2)
PMID:9303310	PBO:0096939	(Fig. 2, Fig. 3)
PMID:9303310	PBO:0096941	(Fig. 5)
PMID:9303312	PBO:0105921	(Fig. 8) Presence of MBF is correlated with cdc10 dependent transcription repression during G2
PMID:9303312	PBO:0037892	(Fig. 2B)
PMID:9303312	PBO:0101286	(Fig. 2B)
PMID:9303312	PBO:0105903	(Fig. 1B) (comment: cdc2-M26 has no detectable kinase activity in G1 at restrictive temperature)
PMID:9303312	PBO:0105902	(Fig. 1A, C) (comment: cdc18 transcription is not dependent on cdc2 function)
PMID:9303312	PBO:0101286	(Fig. 2B) cells do not undergo re replication at restrictive temperature
PMID:9303312	PBO:0105905	(Fig. 2A) cells do not undergo re replication at restrictive temperature but cdc18 transcript increases
PMID:9303312	PBO:0105902	(Fig. 2B)
PMID:9303312	PBO:0105906	(Fig. 3A) cdc18 transcript accumulates in absence of cig1, cig2 and cdc13
PMID:9303312	PBO:0105906	(Fig. 3A) cdc18 transcript accumulates in absence of cdc13
PMID:9303312	PBO:0105907	(Fig. 3B) cdc18 protein accumulates in absence of cig1, cig2 and cdc13
PMID:9303312	PBO:0105908	(Fig. 3C) no DNA replication in absence of all 3 cyclins
PMID:9303312	PBO:0105909	(Fig. 3C) DNA replication in presence of cig1 and cig2
PMID:9303312	PBO:0105910	(Fig. 3C) Abnormal DNA replication with cut DNA replication in absence cig1, cig2 and cdc13 promoter ON some cells have a cut phenotype. (comment: NOT sure the data warrants an annotation)
PMID:9303312	PBO:0105911	(Fig. 3C, D) Absence of cdc2 kinase activity in absence cig1, cig2 and cdc13
PMID:9303312	PBO:0105912	(Fig. 3C, D) cdc13 promoter ON cdc2 kinase activity acts after the accumulation of cdc18 protein to bring about the G1/S transition
PMID:9303312	PBO:0105906	(Fig. 4C) Cdc2 not required for active cdc10 dependent transcription during S phase
PMID:9303312	PBO:0105913	(Fig. 4C) Cdc18 transcript is low during G2
PMID:9303312	PBO:0105913	(Fig. 4C) Cdc18 transcript is low during G2
PMID:9303312	PBO:0105914	Cdc2 kinase activity is low during G2 data not shown
PMID:9303312	FYPO:0003246	(Fig. 4D)
PMID:9303312	FYPO:0003246	(Fig. 4D)
PMID:9303312	PBO:0098715	(Fig. 5A, B) decreased cdc18 transcript in HU block and on release
PMID:9303312	PBO:0098715	(Fig. 5A) decreased cdc18 transcript in HU block and on release
PMID:9303312	PBO:0098715	(Fig. 5A, B) decreased cdc18 transcript in HU block and on release
PMID:9303312	PBO:0105905	(Fig. 5A, B) level of cdc18 transcript does not decreased after release from HU block
PMID:9303312	FYPO:0004235	(Fig. 5C)
PMID:9303312	PBO:0105905	(Fig. 5C) rep2delta has no effect on cdc18 transcript levels in the absence of res2
PMID:9303312	PBO:0105915	(Fig. 6C)
PMID:9303312	PBO:0098713	(Fig. 6C)
PMID:9303312	PBO:0098716	(Fig. 6D)
PMID:9303312	PBO:0105915	(Fig. 6D)
PMID:9303312	PBO:0098716	(Fig. 6B)
PMID:9303312	PBO:0105915	(Fig. 6B)
PMID:9303312	PBO:0105913	Data not shown
PMID:9303312	PBO:0105916	(Fig. 7) (comment: CHECK res1 on multi copy pREP3X ON)
PMID:9303312	PBO:0105915	(Fig. 7) (comment: CHECK res1 on multi copy pREP3X ON)
PMID:9303312	PBO:0098713	(Fig. 7) (comment: CHECK res1 on multi copy pREP3X ON)
PMID:9303312	PBO:0105917	(Fig. 7)
PMID:9303312	PBO:0105913	(Fig. 7) (comment: CHECK res2 on multi copy pREP3X ON)
PMID:9303312	PBO:0105913	(Fig. 7) (comment: CHECK res2 on multi copy pREP3X ON)
PMID:9303312	PBO:0105918	(Fig. 8) (comment: DSC1 is now called MBF)
PMID:9303312	PBO:0105918	(Fig. 8B) (comment: DSC1 is now called MBF)
PMID:9303312	PBO:0105918	(Fig. 8) (comment: DSC1 is now called MBF)
PMID:9303312	PBO:0105918	(Fig. 8B) (comment: DSC1 is now called MBF)
PMID:9303312	PBO:0105919	(Fig. 5, 6, 7)
PMID:9303312	PBO:0105920	(Fig. 5, 6, 7)
PMID:9303312	PBO:0105921	(Fig. 8) Presence of MBF is correlated with cdc10 dependent transcription repression during G2
PMID:9303312	PBO:0105921	(Fig. 8) Presence of MBF is correlated with cdc10 dependent transcription repression during G2
PMID:9303312	PBO:0105921	(Fig. 8) Presence of MBF is correlated with cdc10 dependent transcription repression during G2
PMID:9303312	PBO:0105922	(Fig. 8C)
PMID:9303312	PBO:0105923	(Fig. 2B)
PMID:9303312	PBO:0094078	(Fig. 3C) Abnormal DNA replication with cut DNA replication in absence cig1, cig2 and cdc13 promoter ON some cells have a cut phenotype. (comment: NOT sure the data warrants an annotation)
PMID:9303312	PBO:0113868	(Fig. 4B)
PMID:9303312	PBO:0105904	(Fig. 1D) (comment: cdc2-M26 does not enter S phase even though cdc18 transcription is presence)
PMID:9312055	FYPO:0002061	(Fig. 2)
PMID:9312055	FYPO:0001946	(Fig. 1c)
PMID:9312055	FYPO:0003165	(Fig. 1c)
PMID:9312055	FYPO:0001946	(Fig. 1c)
PMID:9312055	FYPO:0003165	(Fig. 1c)
PMID:9312055	FYPO:0001946	(Fig. 1c)
PMID:9312055	FYPO:0002060	(Fig. 1b)
PMID:9312055	FYPO:0002061	(Fig. 1b)
PMID:9312055	FYPO:0002061	(Fig. 1b)
PMID:9312055	PBO:0095634	(Fig. 1b)
PMID:9312055	FYPO:0002061	(Fig. 1b)
PMID:9312055	PBO:0102752	(Fig. 9)
PMID:9312055	MOD:01148	(comment: poly...)
PMID:9312055	PBO:0020076	(Fig. 7)
PMID:9312055	PBO:0096939	(Fig. 6)
PMID:9312055	PBO:0102751	(Fig. 6)
PMID:9312055	PBO:0102750	(Fig. 4b-d)
PMID:9312055	PBO:0102749	(Fig. 4a)
PMID:9312055	PBO:0099779	(Fig. 4)
PMID:9312055	PBO:0102753	(Fig. 9)
PMID:9312055	FYPO:0002060	(Fig. 2) (comment: CHECK synthetic rescue)
PMID:9312055	FYPO:0003165	(Fig. 1c)
PMID:9312055	PBO:0102748	(Fig. 4)
PMID:9312055	FYPO:0002060	(Fig. 3b) (comment: CHECK rescue)
PMID:9312055	FYPO:0002061	(Fig. 3b) (comment: CHECK rescue)
PMID:9312055	FYPO:0002061	(Fig. 3b)
PMID:9312055	FYPO:0002061	(Fig. 3b)
PMID:9312055	FYPO:0002061	(Fig. 3b)
PMID:9312055	FYPO:0002060	(Fig. 2) (comment: CHECK synthetic rescue)
PMID:9315645	GO:0062038	"(comment: This one comes in ""from the side"", see Ladds, Bond post 2010 publication summary)"
PMID:9315645	PBO:0102572	(Fig. 7) (comment: sort of indirect - kinase dead mutant doesn't activate)
PMID:9321395	FYPO:0000082	(Figure 4)
PMID:9321395	PBO:0097481	data not shown
PMID:9321395	PBO:0097481	(Figure 5)
PMID:9321395	PBO:0097481	(Figure 5)
PMID:9321395	PBO:0097481	(Figure 5)
PMID:9321395	PBO:0097481	(Figure 5)
PMID:9321395	FYPO:0002177	data not shown
PMID:9321395	GO:0038066	An increased level of phosphotyrosine was detected on Spc1 in wis1+ cells overexpressing Wis4∆N, but not in wis1∆ cells, indicating that the action of Wis4 is Wis1- dependent.
PMID:9321395	FYPO:0001492	(Figure 4)
PMID:9321395	FYPO:0000271	(Figure 4)
PMID:9321395	FYPO:0001492	(Figure 4)
PMID:9325108	GO:0008821	(comment: CHECK activated_by(CHEBI:18420)| activated_by(CHEBI:29035))
PMID:9325304	FYPO:0006477	Figure 3B
PMID:9325304	FYPO:0000620	Figure 3B
PMID:9325316	PBO:0117201	(vw: author intent)
PMID:9325316	GO:0003677	(vw: binds DNA on its own)
PMID:9325316	GO:0003677	(vw: binds DNA in complex (2,3,11))
PMID:9325316	GO:0003677	(vw: binds DNA in complex (2,3,11))
PMID:9325316	PBO:0117201	(vw: author intent)
PMID:9325316	GO:0003677	(vw: binds DNA in complex (2,3,11))
PMID:9325316	PBO:0117201	(vw: author intent)
PMID:9325316	PBO:0117201	(vw: author intent)
PMID:9371883	PBO:0107554	(comment: two-hybrid assay)
PMID:9371883	PBO:0107553	(comment: two-hybrid assay)
PMID:9371883	PBO:0107554	(comment: two-hybrid assay)
PMID:9371883	PBO:0107553	(comment: two-hybrid assay)
PMID:9372936	FYPO:0000838	(comment: assayed using SV40 NLS-GFP-LacZ reporter protein)
PMID:9372936	FYPO:0001355	(comment: same as rae1-167 single mutant)
PMID:9372936	FYPO:0001355	(comment: same as rae1-167 single mutant)
PMID:9372936	FYPO:0000838	(comment: assayed using SV40 NLS-GFP-LacZ reporter protein)
PMID:9398669	FYPO:0000303	(comment: CHECK add penetrance?)
PMID:9398669	FYPO:0001425	(Fig. 5a)
PMID:9398669	PBO:0033959	(Fig. 5c) (comment: switched from conjugtion freqeuncy to sterility as can only capture penetance on cell phenotypes)
PMID:9398669	PBO:0095554	(comment: nitrogen induced arrest)
PMID:9398669	PBO:0095555	(comment: G1 phase nitrogen induced arrest)
PMID:9398669	PBO:0095551	because slp1 can bypass wee1 it must independently inhibit cd2
PMID:9398669	PBO:0095551	because slp1 can bypass wee1 it must independently inhibit cd2
PMID:9420333	PBO:0103695	(Fig. 2A) loss of cdc16 function does not affect cdc7 kinase activity
PMID:9420333	PBO:0110201	(comment: GTP bound)
PMID:9420333	PBO:0103703	(comment: GTP bound)
PMID:9420333	PBO:0103702	(comment: From this paper we don't actuallyyet know that it's the new one, that comes later, but ..)cdc7 is associated with both SPBs when a short spindle is present)
PMID:9420333	PBO:0103701	cdc7 is associated with both SPBs when a short spindle is present
PMID:9420333	PBO:0113864	(Fig. 6C) in late anaphase cdc7 is normally localized only one SPB
PMID:9420333	PBO:0113863	(Fig. 6A) in late anaphase cdc7 is normally localized only one SPB
PMID:9420333	PBO:0103698	(Fig. 5B)
PMID:9420333	PBO:0103697	(Fig. 5A)
PMID:9420333	PBO:0103697	(Fig. 5A)
PMID:9420333	PBO:0023023	(Fig. 3A,C) spg1-HA observed at SPB throughout the mitotic cell cycle
PMID:9420333	PBO:0018634	(Fig. 3A,C) spg1-HA observed at SPB throughout the mitotic cell cycle
PMID:9420333	PBO:0103695	(Fig. 2A) loss of spg1 function does not affect cdc7 kinase activity
PMID:9420333	PBO:0110202	(comment: GTP bound)
PMID:9420333	PBO:0103694	"(Fig. 1) (comment: vw interpretation for ""active form"")"
PMID:9428701	GO:0004722	(comment: MBP substrate),(comment: CHECK activated_by(CHEBI:29035))
PMID:9430640	PBO:0096362	(Fig. 1C) Peaks at the end of G2 40 min before peak of rum1 protein
PMID:9430640	PBO:0096369	(Fig. 7,8) cdc2-cig1 complex efficiently phosphorylates rum1 T58T62 residues in vivo . Phosphorylation by cdc2-cig2 or cdc2-cdc13 only observed after a very long exposure
PMID:9430640	PBO:0096377	(comment: this isn't quite the right way to capture this target, still thinking)
PMID:9430640	PBO:0096377	(comment: this isn't quite the right way to capture this target, still thinking)
PMID:9430640	PBO:0096372	(Fig. 4B) (comment: inhibitory for cdc2/cdc13 and cdc2/cig2 but not cdc2/cig1. Both Rum1+ and Rum1-A58A62 can inhibit cdk1 activity)
PMID:9430640	PBO:0092211	(Fig. 1B)
PMID:9430640	PBO:0096371	(Fig. 7B) rum1 A58A62 mutant protein is unable to be phosphorylated by cdc2/cig1
PMID:9430640	PBO:0096370	(Fig. 10)
PMID:9430640	PBO:0096369	(Fig. 7,8) cdc2-cig1 complex efficiently phosphorylates rum1 T58T62 residues in vivo . Phosphorylation by cdc2-cig2 or cdc2-cdc13 only observed after a very long exposure
PMID:9430640	PBO:0096368	(Fig. 6)
PMID:9430640	PBO:0096367	(Fig. 5B)
PMID:9430640	MOD:00047	(Fig. 3C)
PMID:9430640	PBO:0096366	(Fig. 4B) (comment: inhibitory for cdc2/cdc13 and cdc2/cig2 but not cdc2/cig1. Both Rum1+ and Rum1-A58A62 can inhibit cdk1 activity)
PMID:9430640	PBO:0096365	(Fig. 3C) (comment: integrated copy)
PMID:9430640	PBO:0095634	(Fig. 3B) (comment: CHECK: similar to rum1+OP more severe than either single mutant expressed from muliticopy plasmid. Colonies were integrants)
PMID:9430640	PBO:0094205	(Fig. 3) (comment: data not shown phenotype similar to rum+OP)
PMID:9430640	MOD:01148	(Fig. 2)
PMID:9430640	PBO:0096363	(Fig. 2)
PMID:9430640	PBO:0092393	(Fig. 1B)
PMID:9430640	PBO:0092114	(Fig. 1B)
PMID:9430640	PBO:0096361	(Fig. 5)
PMID:9450991	FYPO:0004702	(Figure 2A,B)
PMID:9450991	FYPO:0001418	30x Figure 4B
PMID:9450991	FYPO:0001490	(Figure 4B)
PMID:9450991	FYPO:0002061	(Fig. 4A)
PMID:9450991	FYPO:0003166	(Figure 1A)
PMID:9450991	FYPO:0000016	(Figure 1A)
PMID:9450991	PBO:0103183	(Figure 1A)
PMID:9450991	FYPO:0003166	(Figure 1A)
PMID:9450991	PBO:0033643	(Figure 1A)
PMID:9459302	PBO:0035607	(comment: CHECK is this OK? its aseptate?)
PMID:9468529	GO:0008444	(comment: CHECK inhibited_by CHEBI:29035)
PMID:9488736	PBO:0096790	(comment: looks very likely it is a ser/thr kinase, but if anything comes up that contradicts it this annotation can be made less specific)
PMID:9491802	FYPO:0002061	expressed Clostridium botulinum C3 protein to ADP-ribosylate Rho proteins including Rho1
PMID:9524127	PBO:0106211	(Fig. 3a)
PMID:9524127	PBO:0105150	(Fig. 3)
PMID:9524127	PBO:0106212	(Fig. 3a)
PMID:9524127	PBO:0106211	(Fig. 3a)
PMID:9524127	PBO:0105150	(Fig. 3a)
PMID:9524127	PBO:0106211	(Fig. 3a)
PMID:9524127	PBO:0106211	(Fig. 3a)
PMID:9524127	PBO:0106211	(Fig. 3a)
PMID:9524127	PBO:0106211	(Fig. 3a)
PMID:9531532	FYPO:0002061	(comment: over 35)
PMID:9531532	FYPO:0002061	(comment: over 25)
PMID:9531532	FYPO:0002060	(comment: over 25)
PMID:9531532	FYPO:0002061	(comment: over 25)
PMID:9531532	FYPO:0000276	(comment: over 25)
PMID:9535817	FYPO:0005288	(comment: inferred from FYPO:0000825, FYPO:0001117, FYPO:0005743, FYPO:0007674 phenotypes (including conditions))
PMID:9552380	GO:0000307	(comment: cig2-cdc2)
PMID:9560390	FYPO:0001122	(comment: CHECK osmotic stress)
PMID:9560390	FYPO:0001122	(comment: CHECK osmotic stress)
PMID:9571240	GO:2000134	Ste9 was indispensable for the growth of the wee1 cells, which had to lengthen the pre-Start G1 period to restrain DNA synthesis until the critical size to override Start control was attained....Ste9 might be required for maintenance of the Cdc2 kinase in a pre-Start form, suggested by the fact that overexpression of Ste9 induced rereplication of the genome due to reduction of the mitotic kinase activity of the Cdc13/Cdc2 complex, and rereplication in the cdc2ts strain was prevented by the ste9 mutation.
PMID:9571240	FYPO:0003012	(Figure 4e)
PMID:9571240	FYPO:0001054	(Figure 4e)
PMID:9571240	FYPO:0000398	(Fig. 3)
PMID:9572736	PBO:0112273	(Fig. 3C)
PMID:9572736	FYPO:0000963	(Fig. 5B)
PMID:9572736	PBO:0093580	(Fig. 5B)
PMID:9572736	PBO:0093580	(Fig. 5B)
PMID:9572736	PBO:0112267	(Fig. 1C)
PMID:9572736	PBO:0112268	(Fig. 1C)
PMID:9572736	PBO:0093581	(Fig. 5B)
PMID:9572736	FYPO:0005189	(Fig. 5A)
PMID:9572736	PBO:0112269	(Fig. 1C)
PMID:9572736	PBO:0112270	(Fig. 2A)
PMID:9572736	PBO:0112270	(Fig. 2A)
PMID:9572736	PBO:0112270	(Fig. 2A)
PMID:9572736	PBO:0112271	(Fig. 2B)
PMID:9572736	PBO:0112272	(Fig. 3B)
PMID:9572736	PBO:0092345	(Fig. 3C)
PMID:9572736	PBO:0112273	(Fig. 3C)
PMID:9572736	FYPO:0000088	(Fig. 3D)
PMID:9572736	FYPO:0001492	(Fig. 4)
PMID:9572736	FYPO:0005189	(Fig. 5A)
PMID:9572736	FYPO:0005189	(Fig. 5A)
PMID:9572736	FYPO:0003503	(Fig. 4)
PMID:9572736	FYPO:0003503	(Fig. 4)
PMID:9572736	FYPO:0001492	(Fig. 4)
PMID:9572736	FYPO:0001492	(Fig. 4)
PMID:9572736	FYPO:0003503	(Fig. 4)
PMID:9572736	FYPO:0003503	(Fig. 4)
PMID:9572736	FYPO:0003503	(Fig. 4)
PMID:9572736	FYPO:0003503	(Fig. 4)
PMID:9585506	FYPO:0001490	(comment: CHECK salt stress)
PMID:9585506	FYPO:0001490	(comment: CHECK salt stress)
PMID:9585506	FYPO:0001490	(comment: CHECK salt stress)
PMID:9585506	GO:0005515	(comment: western but we know this happens and I wanted to capture the extension)
PMID:9585506	GO:0005515	(comment: western but we know this happens and I wanted to capture the extension)
PMID:9585506	FYPO:0001490	(comment: CHECK salt stress)
PMID:9601094	PBO:0102019	(Fig. 4B)
PMID:9601094	PBO:0102018	(Fig. 4B)
PMID:9601094	FYPO:0003903	(Fig. 4B)
PMID:9601094	FYPO:0000964	dph1∆ cells were not hypersensitive to TBZ, compared to wild-type cells (Fig. 6C)
PMID:9601094	FYPO:0001399	(Figure 6)
PMID:9601094	FYPO:0001399	(Figure 6)
PMID:9601094	FYPO:0000620	(Fig. 3C) (comment: CHECK at metaphase/anaphase transiton)
PMID:9601094	PBO:0102017	(Fig. 2D)
PMID:9601094	FYPO:0001357	(Figure 6)
PMID:9601094	PBO:0102021	(Fig. 3C) (comment: CHECK at metaphase/anaphase transiton)
PMID:9601094	FYPO:0001357	(comment: medium level of mph1 OEX (high is lethal))
PMID:9601094	PBO:0093562	(Figure 4A)
PMID:9601094	PBO:0102020	(Fig. 4D)
PMID:9606213	PBO:0107898	(comment: DNS actin distributed in cytoplasm)
PMID:9606213	PBO:0099406	(slightly increased- In fact, more cells had staining at their tips than wild-type cells, probably indicating a prolonged attempt to conjugate, after which the protein delocalizes)
PMID:9606213	PBO:0099406	(slightly increased- In fact, more cells had staining at their tips than wild-type cells, probably indicating a prolonged attempt to conjugate, after which the protein delocalizes)
PMID:9606213	PBO:0107900	(Fig. 7)
PMID:9606213	PBO:0099406	In fact, more cells had staining at their tips than wild-type cells, probably indicating a prolonged attempt to conjugate, after which the protein delocalizes
PMID:9606213	PBO:0107899	Therefore, in a h90 mam2 strain, the P cells will attempt mating, but the M cells will be unable to respond due to the lack of the P-factor receptor and so the cells will fail to initiate fusion
PMID:9606213	PBO:0107897	polarization, during conjugation, in shmoo Fig1. We interpret the data as indicating that F-actin is first correctly localized to the tip in all fus1 mutants, but is then redistributed after a defective attempt to fuse. Thus, it is likely that Fus1 is required for the correct organization and stabilization of polarized F-actin at the tip, but is no
PMID:9606213	PBO:0107897	(commment: polarization, in shmoo DNS)
PMID:9606213	GO:0043332	By immunofluorescence, these antibodies stained a single dot at the very tip of each cell in wild-type pre-zygotes (Fig. 2, C and D).
PMID:9606213	FYPO:0000573	(Fig. 1)
PMID:9606213	FYPO:0000573	(Fig. 1)
PMID:9606213	FYPO:0000573	(Fig. 1)
PMID:9614176	PBO:0099126	(Fig. 5C)
PMID:9614176	GO:0031568	(Fig. 2B) after addition of P factor to nitrogen starved G1 arrested cells P factor does not further increase rum1 protein level. It is inferred that rum1 is required to maintain G1 arrest rather than bring it about.
PMID:9614176	PBO:0099130	(Fig. 4)
PMID:9614176	PBO:0099129	(Fig. 6A) (comment: CHECK transcript assayed was Mat1-Mm)
PMID:9614176	PBO:0099127	(Fig. 5C)
PMID:9614176	PBO:0099128	(Fig. 5C)
PMID:9614176	PBO:0099127	(Fig. 5C)
PMID:9614176	PBO:0099125	(Fig. 5B)
PMID:9614176	PBO:0099124	(Fig. 5A)
PMID:9614176	PBO:0099123	(Fig. 4) (comment: sows proteasome involvment as well)
PMID:9614176	PBO:0099121	(Fig. 3D) loss of cig2 does not restore P factor induced G1 arrest
PMID:9614176	PBO:0099122	(Fig. 3A) In absence of rum1 cdc2-cdc13 kinase activity remains high in presence of P factor
PMID:9614176	PBO:0099121	(Fig. 1A)
PMID:9614178	PBO:0106874	(comment: residue not determined experimentally, but probably Y173)
PMID:9614178	PBO:0100943	(comment: residue not determined experimentally, but probably Y173)
PMID:9614178	PBO:0100943	(comment: residue not determined experimentally, but probably Y173)
PMID:9614178	PBO:0095827	(comment: residue not determined experimentally, but probably Y173)
PMID:9614178	PBO:0103795	(comment: residue not determined experimentally, but probably Y173)
PMID:9614178	PBO:0103795	(comment: residue not determined experimentally, but probably Y173)
PMID:9622480	PBO:0097034	(comment: CHECK very mild as shown in xp)
PMID:9635190	PBO:0095292	(Figure 2b)
PMID:9635190	PBO:0095293	(Figure 2c)
PMID:9635190	FYPO:0000783	(Fig. 5) (comment: CHECK during mitosis)
PMID:9635190	FYPO:0001179	(comment: cytoplasm in interphase) (Figure 4a, I)
PMID:9635190	PBO:0033730	(Figure 4b)
PMID:9635190	FYPO:0000783	(Fig. 5) (comment: CHECK during mitotic M-phase)
PMID:9635190	FYPO:0000783	(Fig. 5) (comment: CHECK during mitotic M-phase)
PMID:9635190	FYPO:0000783	(Fig. 5) (comment: CHECK during mitotic M-phase)
PMID:9635190	FYPO:0000783	(Fig. 5) (comment: CHECK during mitotic M-phase)
PMID:9635190	FYPO:0005000	(Fig. 5) (comment: CHECK during interphase)
PMID:9635190	PBO:0095290	(Figure 2a)
PMID:9635190	PBO:0095288	(Fig. 1i)
PMID:9635190	PBO:0095291	(Fig. 1i)
PMID:9635190	FYPO:0004754	(Fig. 5) (comment: CHECK during mitotic M-phase)
PMID:9635190	FYPO:0001179	(comment: CHECK cytoplasm during interphase with nuclear localization)
PMID:9635190	FYPO:0000783	(Fig. 5) (comment: CHECK during mitotic M-phase)
PMID:9636183	PBO:0095711	(comment: same severity as wee1-50 alone)
PMID:9658208	FYPO:0002060	(comment: just to get the allele details of -P in the database)
PMID:9660817	FYPO:0000708	data not shown
PMID:9660817	FYPO:0001147	data not shown
PMID:9660817	PBO:0093824	data not shown
PMID:9660818	PBO:0093824	(comment: same severity when crossed with wild type or shk1delta)
PMID:9660818	PBO:0093825	(comment: when crossed with shk1delta overexpressing shk2+ or wild type)
PMID:9660818	PBO:0093825	(comment: when crossed with partner overexpressing shk1-deltaN; normal in cross with wild type)
PMID:9679144	PBO:0019143	(Fig. 3C) cell length does not affect branching showing its not because cells are longer at high temp
PMID:9679144	PBO:0095945	(Fig. 11) in the absence of microtubules and actin
PMID:9679144	PBO:0095946	(Fig. 5 C,D, Fig. 12) Normal protein localisation in presence of TBZ
PMID:9679144	PBO:0095944	(Fig. 9) tea1 can relocalise to cell ends in absence of microtubules
PMID:9679144	PBO:0095943	(Fig. 8A-D) Actin relocalisation to old or new cell end after microtubule disruption
PMID:9679144	FYPO:0007379	(Fig. 6) abnormal septum in branched cell
PMID:9679144	PBO:0095181	(Fig. 6) F-actin localised to branch site in presence of TBZ
PMID:9679144	PBO:0095945	(Fig. 11) absence of microtubules
PMID:9679144	PBO:0095942	(Fig. 5 C,D)
PMID:9679144	PBO:0095941	(Fig. 4) Short interphase microtubules located in the cell centre
PMID:9679144	PBO:0019143	(Fig. 3A-C) pre NETO blocked cells do not branch if TBZ is added at shift down
PMID:9679144	FYPO:0000672	(Fig. 2C) arrest released cells have NETO defect and do not branch.
PMID:9679144	PBO:0038218	(Fig. 2C) arrest released cells are pre NETO but only branch at low level.
PMID:9679144	PBO:0095940	(Fig. 2C) cells were pre NETO after temperature block about 5% cells are already branched at release
PMID:9679144	PBO:0095940	(Fig. 2C) cells were pre NETO after temperature block about 5% cells are already branched at release
PMID:9679144	PBO:0095939	(Fig. 2B) cells were pre NETO after temperature block
PMID:9679144	PBO:0095938	(Fig. 2B) cells were pre NETO after temperature block
PMID:9679144	PBO:0095936	(Fig. 2B) cells were pre NETO after temperature block
PMID:9679144	PBO:0095937	(Fig. 2A) cdc25-22 arrest released cells ie post NETO do not branch
PMID:9679144	PBO:0095936	(Fig. 1F,H) cells were pre NETO after temperature block
PMID:9693363	FYPO:0003694	(comment: increased 25S/18S ratio)
PMID:9693384	PBO:0095827	(comment: probably Y173, but not determined experimentally)
PMID:9693384	PBO:0097481	(comment: probably Y173, but not determined experimentally)
PMID:9693384	PBO:0097481	(comment: probably Y173, but not determined experimentally)
PMID:9718372	PBO:0100943	(comment: probably Y173, but not determined experimentally)
PMID:9718372	PBO:0100951	(comment: probably Y173, but not determined experimentally)
PMID:9718372	PBO:0095349	(comment: probably Y173, but not determined experimentally)
PMID:9722643	GO:0005634	Fig. 4
PMID:9722643	PBO:0103534	Fig. 3
PMID:9722643	FYPO:0002060	Fig. 1
PMID:9722643	FYPO:0000472	Fig. 2
PMID:9722643	FYPO:0001840	Table 2
PMID:9722643	FYPO:0000091	Fig. 5
PMID:9739083	PBO:0097659	(Fig. 2A) (comment: cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C)
PMID:9739083	PBO:0104511	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	PBO:0104511	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	PBO:0104512	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	PBO:0104513	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	PBO:0104514	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	PBO:0104513	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	PBO:0104515	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	PBO:0104511	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	PBO:0104509	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal.)
PMID:9739083	PBO:0104511	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal)
PMID:9739083	PBO:0104514	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal)
PMID:9739083	PBO:0104515	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal)
PMID:9739083	PBO:0104509	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal)
PMID:9739083	PBO:0104510	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	PBO:0104511	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	PBO:0104512	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	PBO:0100985	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	PBO:0104512	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	PBO:0104517	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	PBO:0104516	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	FYPO:0002061	(comment: cdc18-1-141 when expressed on multi copy plasmid does not rescue cdc18-K46)
PMID:9739083	FYPO:0002061	(comment: cdc18-150-577 when expressed on multi copy plasmid does not rescue cdc18-K46)
PMID:9739083	FYPO:0002061	(comment: cdc18-150-577(T374A) when expressed on multi copy plasmid does not rescue cdc18-K46)
PMID:9739083	FYPO:0002061	(comment: cdc1-577 (NTP) when expressed on multi copy plasmid does not rescue cdc18-K46)
PMID:9739083	PBO:0097659	(Fig. 2A) (comment: cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C)
PMID:9739083	PBO:0097659	(Fig. 2A) (comment: cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C)
PMID:9739083	PBO:0097659	(Fig. 2A) (comment: cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C)
PMID:9739083	PBO:0104510	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	PBO:0102340	(Fig. 2B) (comment: cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C)
PMID:9739083	PBO:0104505	(Fig. 2B) (comment: dc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C)
PMID:9739083	PBO:0096052	(Fig. 3) (comment: the kinase assay substrate used is Histone H1)
PMID:9739083	PBO:0096053	(Fig. 3) (comment: the kinase assay substrate used is Histone H1)
PMID:9739083	PBO:0096053	data not shown (comment: the kinase assay substrate used is Histone H1)
PMID:9739083	PBO:0096363	(Fig. 3) (comment: cdc18 expressed from pREP3X and assayed for 20 hours after removal of thiamine at 32°C)
PMID:9739083	PBO:0096363	(Fig. 3) (comment: cdc18 expressed from pREP3X and assayed for 20 hours after removal of thiamine at 32°C)
PMID:9739083	PBO:0104506	(Fig. 3) (comment: cdc18 expressed from pREP3X and assayed for 20 hours after removal of thiamine at 32°C)
PMID:9739083	PBO:0104507	(Fig. 3) (comment: not strictly a co-immunoprecitation experiment as they used suc1 beads to pull down cdc2 then a western blot)
PMID:9739083	PBO:0104508	(Fig. 3) (comment: not strictly a co-immunoprecitation experiment as they used suc1 beads to pull down cdc2 then a western blot)
PMID:9739083	FYPO:0005773	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0001122	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0001122	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0001122	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0001052	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0000402	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0000402	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0000402	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0000402	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	(Fig. 2A) (comment: cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C)
PMID:9739083	FYPO:0001052	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0000402	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0000402	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0000402	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0000402	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0002519	Data not shown (comment: Cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	FYPO:0002995	Data not shown (comment: Cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	PBO:0104509	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	PBO:0099432	(Fig. 6) (comment: and cell phenotype data not shown. cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	PBO:0104518	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	PBO:0104512	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9740803	GO:0008139	(comment: can't use IPI because we don't have identifiers for human importin alpha or the GST-NLS construct)
PMID:9740803	PBO:0103363	(comment: also assayed with GFP-NLS construct)
PMID:9745017	PBO:0095902	(comment: inferred from decreased nda3 mRNA level)
PMID:9745017	PBO:0095902	(comment: inferred from decreased nda3 mRNA level)
PMID:9755169	PBO:0107542	(Fig. 4C) cd18 N term deletion can accumulate in a metaphase arrest
PMID:9755169	PBO:0107538	(Fig. 2C) cdc10 dependent transcription occurs during mitotic exit
PMID:9755169	PBO:0107539	(Fig. 2C) cdc10 dependent transcription occurs during mitotic exit
PMID:9755169	PBO:0107542	(Fig. 4C) (comment: cd18 N term deletion can accumulate in a metaphase arrest)
PMID:9755169	PBO:0107541	(Fig. 3B) cdc10 is a cdc18 transcriptional regulator see Fig2C
PMID:9755169	PBO:0107541	(Fig. 3A) cdc10 is a cdc18 transcriptional regulator see Fig2C
PMID:9755169	PBO:0107542	(Fig. 5D)
PMID:9755169	PBO:0107540	(Fig. 2C) cdc10 dependent transcription occurs during mitotic exit
PMID:9755169	PBO:0107541	(Fig. 3B)
PMID:9755169	PBO:0107542	(Fig. 5C)
PMID:9755169	PBO:0096440	(Fig. 5B)
PMID:9755169	PBO:0107542	(Fig. 4E) cdc18 lacking cdc2 phosphorylation sites accumulates immediately as cells progress into mitosis
PMID:9771717	FYPO:0000678	data not shown
PMID:9774107	PBO:0108169	(Fig. 4a)
PMID:9774107	PBO:0094001	(Fig. 2e)
PMID:9774107	PBO:0095532	(Fig. 2)
PMID:9774107	PBO:0095532	(Fig. 2)
PMID:9774107	PBO:0094001	(Fig. 2e)
PMID:9774107	PBO:0108165	data not shown
PMID:9774107	PBO:0108165	(Fig. 2e)
PMID:9774107	PBO:0108166	(Fig. 2)
PMID:9774107	PBO:0108166	(Fig. 2)
PMID:9774107	PBO:0108168	(Fig. 4a)
PMID:9778252	PBO:0021058	Precise observation revealed that Mei2p dots could be visible in conjugating cells that completed cell fusion but did not undergo karyogamy yet.
PMID:9786952	PBO:0102010	(Fig. 6)
PMID:9786952	FYPO:0006802	(Fig. 2E)
PMID:9786952	FYPO:0005870	(Fig. 2B)
PMID:9786952	FYPO:0001406	(Fig. 2B)
PMID:9786952	PBO:0102009	(Fig. 4d,e)
PMID:9786952	FYPO:0001254	(Fig. 4a)
PMID:9786952	PBO:0102008	(Fig. 2A)
PMID:9786952	PBO:0032815	(Fig. 4a,b)
PMID:9786952	FYPO:0003500	(Fig. 4a)
PMID:9794798	PBO:0098699	mutant Cdc6 is not positively regulated by PCNA to the same extent as Cdc6+
PMID:9794798	PBO:0098699	mutant Cdc6 is not positively regulated by PCNA to the same extent as Cdc6+
PMID:9802907	FYPO:0002639	A striking feature in dis1 mutant cells was that the back-and-forth cen1 DNA movements seen in phase 2 of wild-type cells were entirely absent. After spindle elongation (the SPB distance, 􏰆8 􏰈m), the cen1 signals were fused again and moved to one of the SPBs. Such prolonged centromere splitting while the spindle was elongating was never seen in wild-type or any of the other mutant cells examined so far.
PMID:9802907	PBO:0018346	((comment: included because different/new method) To observe the SPB in living cells, GFP-tagged Sad1 (designated hereafter Sad1-GFP) was expressed and found to be bound to the SPB throughout the cell cycle (Figure 1A), identical to immunolocalization data (Hagan and Yanagida, 1995)
PMID:9802907	PBO:0018634	((comment: included because different/new method) To observe the SPB in living cells, GFP-tagged Sad1 (designated hereafter Sad1–GFP) was expressed and found to be bound to the SPB throughout the cell cycle (Figure 1A), identical to immunolocalization data (Hagan and Yanagida, 1995)
PMID:9808627	FYPO:0003241	(comment: G1 block)
PMID:9808627	PBO:0033703	(Fig. 2D)
PMID:9808627	PBO:0033704	(comment: G2 block)
PMID:9832516	PBO:0093579	(comment: severity estimated because wt (i.e. not overexpressing cdc25) not shown)
PMID:9832516	PBO:0093579	(comment: severity estimated because wt (i.e. not overexpressing cdc25) not shown)
PMID:9832516	PBO:0093579	(comment: severity estimated because wt (i.e. not overexpressing cdc25) not shown)
PMID:9832516	PBO:0093579	(comment: severity estimated because wt (i.e. not overexpressing cdc25) not shown)
PMID:9839953	PBO:0097089	(comment: low activity)
PMID:9839953	PBO:0097089	at the second position (Gal-Man-O)
PMID:9839953	PBO:0097092	at the second position (Gal-Man-O)
PMID:9843572	FYPO:0000712	(Figure 3A,B)
PMID:9843572	PBO:0103076	(Figure 9A)
PMID:9843572	PBO:0103075	(Figure 8)
PMID:9843572	PBO:0103075	(Figure 8)
PMID:9843572	PBO:0103074	(Figure 3B) (comment: additive)
PMID:9843572	PBO:0094266	(Figure 7A)
PMID:9843572	FYPO:0001491	(Figure 6B)
PMID:9843572	FYPO:0001124	(Figure 6A)
PMID:9843572	FYPO:0000711	(Figure 3A,B)
PMID:9843572	FYPO:0003481	(Figure 3B)
PMID:9843572	FYPO:0003481	(Figure 3B)
PMID:9843572	FYPO:0003481	(Figure 3B)
PMID:9843572	FYPO:0003481	(Figure 3B)
PMID:9843572	PBO:0098712	(Figure 1)
PMID:9843577	FYPO:0007137	single micrograph, so can't tell if they're viable
PMID:9843577	FYPO:0007136	single micrograph, so can't tell if they're viable
PMID:9843966	PBO:0026234	(comment: neutral wrt viability because data not shown, so don't know if aseptate mononucleate cells are the same ones that manage to survive and eventually divide)
PMID:9857040	GO:0070336	(comment: physiologically relevant?)
PMID:9857040	GO:0000403	(comment: physiologically relevant?)
PMID:9862966	PBO:0101179	(Fig. 3C, D)
PMID:9862966	PBO:0101180	(comment: CHECK https://github.com/pombase/fypo/issues/3931)
PMID:9864354	FYPO:0007125	(Fig. 2E)
PMID:9864354	FYPO:0000620	indicated by high level of H1 kinase activity
PMID:9864354	FYPO:0000229	(Fig. 2D)
PMID:9864354	FYPO:0007125	(Fig. 2E)
PMID:9872416	PBO:0103887	(Figure 2)
PMID:9872416	PBO:0103889	(Figure 2)
PMID:9872416	PBO:0103893	(Figure 2)
PMID:9872416	PBO:0103892	(Figure 2)
PMID:9872416	GO:0046316	(Figure 2)
PMID:9872416	PBO:0103888	(Figure 2)
PMID:9872416	PBO:0103890	(Figure 2)
PMID:9891039	FYPO:0001355	(comment: worse than cdc24-M38 alone -wt not shown)
PMID:9891039	FYPO:0001355	(comment: worse than cdc24-M38 alone -wt not shown)
PMID:9891039	FYPO:0001355	(comment: worse than cdc24-M38 alone -wt not shown)
PMID:9891039	FYPO:0001355	(comment: worse than cdc24-M38 alone -wt not shown)
PMID:9891047	FYPO:0002061	(comment: temperature permissive for single mutant without rad26delta)
PMID:9891047	PBO:0095859	(comment: temperature permissive for single mutant without rad2delta)
PMID:9891047	PBO:0095859	(comment: temperature permissive for single mutant without rad2delta)
PMID:9891047	PBO:0095857	(comment: temperature permissive for single mutant without rad2delta)
PMID:9891047	PBO:0095859	(comment: temperature permissive for single mutant without rad2delta)
PMID:9891047	PBO:0095859	(comment: temperature permissive for single mutant without rad2delta)
PMID:9891047	PBO:0095859	(comment: temperature permissive for single mutant without rad2delta)
PMID:9891047	PBO:0095857	(comment: temperature permissive for single mutant without rad2delta)
PMID:9891047	FYPO:0002061	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	PBO:0093560	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	PBO:0093561	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	PBO:0095859	(comment: temperature permissive for single mutant without rad2delta)
PMID:9891047	PBO:0093560	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	PBO:0095859	(comment: temperature permissive for single mutant without rad2delta)
PMID:9891047	PBO:0095859	(comment: temperature permissive for single mutant without rad2delta)
PMID:9891047	PBO:0093561	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	PBO:0095859	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	PBO:0093561	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	PBO:0095859	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	PBO:0093560	(comment: temperature permissive for single mutant without rad26delta)
PMID:9891047	PBO:0093560	(comment: temperature permissive for single mutant without rad26delta)
PMID:9891047	PBO:0093560	(comment: temperature permissive for single mutant without rad26delta)
PMID:9891047	PBO:0093561	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	PBO:0095857	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	PBO:0093560	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	PBO:0095857	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	FYPO:0002061	(comment: temperature permissive for single mutant without rad26delta)
PMID:9891047	FYPO:0002061	(comment: temperature permissive for single mutant without rad26delta)
PMID:9891047	FYPO:0002061	(comment: temperature permissive for single mutant without rad26delta)
PMID:9891047	FYPO:0002061	(comment: temperature permissive for single mutant without rad26delta)
PMID:9891047	FYPO:0002061	(comment: temperature permissive for single mutant without rad26delta)
PMID:9891047	FYPO:0002061	(comment: temperature permissive for single mutant without rad26delta)
PMID:9950674	FYPO:0002061	(Fig. 9)
PMID:9950674	FYPO:0003165	(Fig. 9)
PMID:9973368	FYPO:0001357	(comment: non-flocculating cells)