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:0003774	(comment: assayed using Tf1 transposon)
PMID:10022921	FYPO:0003772	(comment: assayed using Tf1 transposon)
PMID:10022921	FYPO:0003773	(comment: assayed using Tf1 transposon Gag and IN)
PMID:10022921	FYPO:0003775	(comment: assayed using Tf1 transposon plasmid construct)
PMID:10022921	FYPO:0000593	(comment: assayed using Tf1 transposon plasmid construct)
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	GO:0016020	These results suggested that Mok1 is an stable integral membrane pro- tein, which is consistent with the presence of several trans- membrane domains (Fig. 2 a).
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	FYPO:0002060	pck2delta rescues ags1 ox defect, we cant do this genetic interaction type in new interface
PMID:10087262	GO:0031520	combined localization and membrane fraction
PMID:10087262	FYPO:0006802	Fig. 1a 'delocalized actin'
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 di- vided cells associated side-by-side (12%), the cell wall of which appeared fragile and often lysed upon division.
PMID:10087262	PBO:0093772	data not shown
PMID:10087262	PBO:0099872	Fig. 1c
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	GO:0032178	combined localization and membrane fraction
PMID:10091325	GO:0004371	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:0098011	Csk1 activated both the monomeric and the Mcs2-bound forms of Mcs6.
PMID:10226032	PBO:0098010	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:0098012	Surprisingly, Csk1 also activated Cdc2 in complexes with either Cdc13 or Cig2 cyclins.
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:10364209	FYPO:0001357	DNS
PMID:10366596	FYPO:0004086	(comment: in zygotic nucleus)
PMID:10381387	PBO:0094917	(vw: it doesn't say old, but it is...)
PMID:10381387	PBO:0094917	(vw: it doesn't say old, but it is...)
PMID:10388806	FYPO:0001428	cdc18delta::p[nmt*.cdc18+-LEU2]
PMID:10388806	FYPO:0001430	cdc18delta::p[nmt*.cdc18+-LEU2]
PMID:10388806	PBO:0026408	Val: moved down from FYPO:0001429, its a fully penetrant inviable phenotype (anucleate)
PMID:10392445	FYPO:0000474	conditions under which pat1-114 alone induces meiosis & sporulation
PMID:10398679	GO:0038066	is response to heat a real process or should be resposne to denatured proteins or whatever?
PMID:10398680	FYPO:0006174	figure 3
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 (before phase 3 extension)
PMID:10398680	FYPO:0006190	Figure 2
PMID:10398680	FYPO:0006715	Figure 1, A and B All of these required passage through G1 (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	figue 4
PMID:10398680	FYPO:0007304	figure3
PMID:10398680	FYPO:0003788	fig 1a
PMID:10398680	FYPO:0003241	Figure 1F & 7B (second mitosis)
PMID:10398680	FYPO:0006190	Figure 1, A and B All of these required passage through G1 (second mitosis)
PMID:10428959	GO:0010971	figure 3
PMID:10428959	GO:0031139	table 2
PMID:10428959	FYPO:0001214	figure 3b
PMID:10428959	FYPO:0004481	figure 3b
PMID:10428959	PBO:0096484	(vw: sty1-atf1 pathway)
PMID:10428959	PBO:0096491	figure 7
PMID:10428959	PBO:0096492	figure 7
PMID:10428959	GO:0005515	Figure1/2
PMID:10428959	GO:0005515	Figure 1/2
PMID:10428959	PBO:0096485	(vw: sty1-atf1 pathway)
PMID:10428959	PBO:0022884	figure 2C (vw: not by sty1)
PMID:10428959	PBO:0096482	Figure 3 (vw severity 23.4 micron)
PMID:10428959	PBO:0096482	Figure 3 (vw: severity 20.2 micron)
PMID:10428959	GO:0010971	figure 3
PMID:10428959	PBO:0096486	Figure 5
PMID:10428959	PBO:0096487	Figure 5
PMID:10428959	GO:0038066	table 2
PMID:10428959	PBO:0096490	figure 7
PMID:10428959	FYPO:0002060	DNS
PMID:10428959	PBO:0096488	Figure 6
PMID:10428959	PBO:0096489	Figure 6B
PMID:10430583	PBO:0093619	same as rad51delta alone
PMID:10430583	PBO:0093619	same as rad51delta alone
PMID:10459013	GO:0044732	present throughout mitotic cell cycle
PMID:10462529	FYPO:0002061	fig2
PMID:10462529	PBO:0101463	fig 6
PMID:10462529	PBO:0101462	fig5
PMID:10462529	FYPO:0006038	fig3
PMID:10462529	FYPO:0001490	fig2
PMID:10462529	FYPO:0006822	fig7
PMID:10462529	FYPO:0000951	fig 7
PMID:10462529	PBO:0094621	extension, of cdc25 7b
PMID:10462529	FYPO:0001122	fig6
PMID:10462529	PBO:0101461	fig 6
PMID:10462529	FYPO:0003503	fig5
PMID:10462529	FYPO:0003503	fig5
PMID:10462529	FYPO:0002085	fig5
PMID:10462529	FYPO:0006038	4a
PMID:10462529	FYPO:0002085	Fig. 3
PMID:10462529	FYPO:0002061	Fig. 3
PMID:10462529	FYPO:0002061	fig2
PMID:10462529	GO:0002183	fig2
PMID:10462529	FYPO:0006037	fig1
PMID:10462529	FYPO:0006036	fig1
PMID:10473641	FYPO:0004539	broken
PMID:10521402	PBO:0096557	Fig 5A see Fig4A for control
PMID:10521402	PBO:0096552	Data not shown. kinetics same as pat1ts rad1delta diploid
PMID:10521402	PBO:0096558	Fig6C
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	Fig6A,D; 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:10521402	PBO:0096552	Fig 2 A,B
PMID:10521402	PBO:0096552	Fig 2 A,B
PMID:10521402	PBO:0096550	Fig 1B double cds1delta chk1 delta has same phenotype as single cds1delta/cds1 delta
PMID:10521402	PBO:0096551	Fig1B
PMID:10521402	PBO:0096551	Fig1B
PMID:10521402	FYPO:0006763	Fig1B cds1 is required for meiotic DNA replication checkpoint
PMID:10521402	PBO:0096550	Fig 1A rad1 is required for meiotic DNA replication checkpoint
PMID:10521402	PBO:0021428	Fig3B data not shown
PMID:10521402	PBO:0096553	Data not shown prophase arrest with horsetail nuclear morphology see fig3A for pat1ts control
PMID:10521402	PBO:0021428	Fig3B data not shown
PMID:10521402	FYPO:0000734	Fig3 B
PMID:10521402	FYPO:0004929	Fig3 B
PMID:10521402	FYPO:0001733	Fig3B
PMID:10521402	GO:0072441	Fig 4
PMID:10521402	PBO:0096554	Fig4 present during meiotic DNA replication checkpoint arrest
PMID:10521402	PBO:0096553	Data not shown prophase arrest with horsetail nuclear morphology see fig3A for pat1ts control
PMID:10521402	PBO:0096552	Data not shown. kinetics same as pat1ts rad1delta diploid
PMID:10521402	PBO:0096555	Fig5A see control in Fig4A
PMID:10521402	PBO:0096556	Fig5B see Fig4B for control
PMID:10521402	PBO:0096552	Data not shown. kinetics same as pat1ts rad1delta diploid
PMID:10521402	PBO:0096555	Fig5A see control in Fig4A
PMID:10521402	PBO:0096557	Fig 5A see Fig4A for control
PMID:10523629	PBO:0100796	Figure 1 a
PMID:10523629	PBO:0095532	Figure 1 a
PMID:10523629	PBO:0095532	Figure 1 a
PMID:10523629	PBO:0100796	Figure 1 a
PMID:10523629	PBO:0095532	Figure 1 a
PMID:10523629	PBO:0095532	Figure 1 a
PMID:10523629	PBO:0095532	Figure 1 a
PMID:10523629	PBO:0100796	Figure 1 a
PMID:10523629	PBO:0095532	Figure 1 a
PMID:10523629	PBO:0095532	Figure 1 a
PMID:10523629	PBO:0100796	Figure 1 a
PMID:10523629	PBO:0095532	Figure 1 a
PMID:10523629	PBO:0095532	Figure 1 a
PMID:10523629	PBO:0100803	Fig 5G
PMID:10523629	PBO:0100802	Fig 5C
PMID:10523629	PBO:0100801	Fig 5J
PMID:10523629	PBO:0093616	fig 4
PMID:10523629	PBO:0038186	fig 4
PMID:10523629	PBO:0100799	fig 3C
PMID:10523629	PBO:0094734	fig 2a
PMID:10523629	PBO:0100798	fig 2a
PMID:10523629	PBO:0095532	Figure 1 a
PMID:10526233	FYPO:0003166	(it basically the same as cut except the nucleus is not bisected)
PMID:10526233	FYPO:0003166	(it basically the same as cut except the nucleus is not bisected)
PMID:10545452	FYPO:0003931	Figure 1, 4 hr
PMID:10545452	FYPO:0001006	Figure 1, 8 hr
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	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 po- larity 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	FYPO:0002061	The drc1-191 mutation was found to be recessive, since cells of the genotype drc1􏰀/drc1- 191 resembled wild-type cells and were capable of colony formation under conditions in which the drc1-191 mu- tant was unable to form colonies (data not shown).
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:0002060	The drc1-191 mutation was found to be recessive, since cells of the genotype drc1􏰀/drc1- 191 resembled wild-type cells and were capable of colony formation under conditions in which the drc1-191 mu- tant was unable to form colonies (data not shown).
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 postana- phase array of microtubules (Figure 3A, 4 hr).
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:0003710	Figure 1, 0 hr
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:0001234	The drc1-191 rng2-D5 and drc1-191 cdc4-8 double mutants grew extremely poorly a
PMID:10545452	FYPO:0001234	The drc1-191 rng2-D5 and drc1-191 cdc4-8 double mutants grew extremely poorly a
PMID:10545452	FYPO:0001495	The drc1-191 rng2-D5 and drc1-191 cdc4-8 double mutants grew extremely poorly and showed cyto- kinesis 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	FYPO:0007541	The drc1-191 rng2-D5 and drc1-191 cdc4-8 double mutants grew extremely poorly and showed cyto- kinesis 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	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: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:0001368	i.e next round of replication
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:0004629	i.e next round of replication
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:10547441	FYPO:0003889	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	PBO:0096816	fig2d - number 7 and 8
PMID:10567589	PBO:0093769	fig2d - number 7 and 8
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:10567589	FYPO:0001929	3c
PMID:10574765	PBO:0096818	Figure 2c Boundary of the non growing cell end not maintained
PMID:10574765	PBO:0096817	Figure 2b Boundary of non growing cell end maintained
PMID:10574765	PBO:0096817	Figure 2a Boundary of non growing cell end maintained
PMID:10574765	PBO:0109946	"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:0096824	Figure 3 normal at non-growing end
PMID:10574765	PBO:0096824	Figure 3 normal at non-growing end
PMID:10574765	PBO:0096822	Figure 4 Ral3/cor-CGFP fusion is expressed from pMral3/cor-C
PMID:10574765	PBO:0096821	Figure 4 Ral3/cor-CGFP fusion is expressed from pMral3/cor-C
PMID:10574765	PBO:0096820	Figure 4 Ral3/cor-CGFP fusion is expressed from pMral3/cor-C
PMID:10574765	PBO:0096819	Figure 3 F actin is absent from non growing end
PMID:10581266	FYPO:0001493	fig9
PMID:10581266	FYPO:0002025	fig6
PMID:10581266	FYPO:0002729	fig6
PMID:10581266	FYPO:0003439	fig4
PMID:10581266	FYPO:0002061	fig9 high overexpression is lethal
PMID:10581266	FYPO:0002177	fig6
PMID:10588638	FYPO:0004372	inferred from Chk1 phosphorylation phenotypes
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), after 5 hours
PMID:10588653	PBO:0035615	DNS after 5 hours
PMID:10588653	FYPO:0001367	DNS
PMID:10588653	FYPO:0001357	DNS
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 8 A 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 8 A 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) 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: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:10591634	PBO:0101467	IPI and IMP evidence
PMID:10593886	GO:0004674	only in vitro data evidence
PMID:10641037	FYPO:0002060	DNS
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:0007912	figure 3b
PMID:10641037	FYPO:0002060	figure 2
PMID:10651902	PBO:0105062	appeared thicker
PMID:10651902	PBO:0099872	fig6
PMID:10651902	FYPO:0004104	normal volume?
PMID:10651902	PBO:0019176	fig6
PMID:10651902	GO:0005515	Rho1 GTP bound form pck2 HR1 domain
PMID:10651902	PBO:0105063	Rho1 appears to have a dual role in stabilizing and localizing Pck proteins
PMID:10683155	FYPO:0000229	cut if exposed to radiation during S phase, but not if exposed during G2
PMID:10683155	GO:0000785	constant level throughout cell cycle
PMID:10698951	FYPO:0002060	temperature restrictive for cdc27-P11 alone
PMID:10698951	FYPO:0002061	temperature restrictive for cdc27-P11 alone
PMID:10712506	PBO:0104977	from materials and methods
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:10718196	FYPO:0000337	DNS
PMID:10725227	PBO:0107278	Fig3B
PMID:10725227	PBO:0107289	Fig9
PMID:10725227	PBO:0107288	Fig10B
PMID:10725227	PBO:0107287	Fig10A
PMID:10725227	PBO:0107286	Fig9
PMID:10725227	FYPO:0001355	Fig7 B (comment: over expression of cig2+ cDNAI partially suppresses the rescue of cdc21-M68 by ded1-1D5)
PMID:10725227	FYPO:0002061	Fig7 B (comment: over expression of cig2+ cDNAII suppresses the rescue of cdc21-M68 by ded1-1D5)
PMID:10725227	FYPO:0002061	Fig7 B
PMID:10725227	PBO:0107284	Fig7C, D (comment: The protein and mRNA levels are compared to cDNA-I which is also expressed from medium strength nmt1 promoter ON)
PMID:10725227	PBO:0107283	Fig6 (comment: total protein translation not affected)
PMID:10725227	PBO:0107282	Fig6 (comment: total protein translation not affected)
PMID:10725227	PBO:0107281	Fig 5B 35S
PMID:10725227	PBO:0105174	Fig 5B 35S
PMID:10725227	PBO:0107280	Fig 5A 35S
PMID:10725227	GO:0005737	Fig4B
PMID:10725227	PBO:0107279	Fig3B
PMID:10725227	PBO:0107279	Fig. 3A
PMID:10725227	PBO:0107278	Fig. 3A
PMID:10725227	FYPO:0002060	Fig2D (comment: the semi permissive temperature 34.5C for ded1-D5 allows it to suppress cdc19-P1)
PMID:10725227	FYPO:0002060	Fig2B
PMID:10725227	FYPO:0002061	Fig. 2C
PMID:10725227	FYPO:0002061	Fig2C
PMID:10725227	FYPO:0002060	Fig2B
PMID:10725227	FYPO:0002060	Fig2B
PMID:10725227	FYPO:0002060	Fig2B
PMID:10725227	FYPO:0002060	Table 2
PMID:10725227	FYPO:0002060	Table 2
PMID:10725227	FYPO:0002060	Table 2
PMID:10725227	PBO:0097954	Fig 1B G1
PMID:10725227	PBO:0097954	Fig 1B
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:10733588	FYPO:0001840	Table2
PMID:10733588	FYPO:0001420	Fig. 3D and data not shown
PMID:10733588	FYPO:0001840	Table2
PMID:10748059	GO:0044750	inhibited_by(CHEBI:48828)
PMID:10749926	FYPO:0000228	figure 4
PMID:10749926	PBO:0106370	Fig 6
PMID:10749926	FYPO:0002061	figure 1B
PMID:10749926	FYPO:0000229	figure 4 (spindle is still present, normally disaaembld by cytokinesis)
PMID:10749926	FYPO:0000620	figure 1B
PMID:10749926	PBO:0106371	Fig 6
PMID:10757807	PBO:0093580	same as rqh1delta alone
PMID:10757807	PBO:0093580	same as cdc27-P11 alone
PMID:10757807	PBO:0093580	same as cds1delta alone
PMID:10766248	PBO:0095955	severity correlates positively with overexpression level
PMID:10766248	PBO:0095955	cdc18+ low level overexpression
PMID:10766248	PBO:0095955	severity correlates positively with overexpression level, and different isolates with same construct integrated show different Cdc18 levels
PMID:10769212	PBO:0094469	temperature restrictive for cdc4-8 alone
PMID:10769212	FYPO:0003389	temperature restrictive for cdc4-8 alone
PMID:10769212	PBO:0023726	early mitosis; independent of F-actin (assayed using Latrunculin A)
PMID:10769212	GO:0110085	dependent on F-actin (assayed using Latrunculin A)
PMID:10769212	FYPO:0002061	inviable at 37 degrees; some growth at 34 degrees
PMID:10769212	FYPO:0002061	inviable at 37 degrees; some growth at 34 degrees
PMID:10769212	FYPO:0002061	inviable at 34 or 37 degrees
PMID:10769212	FYPO:0002060	temperature restrictive for cdc4-8 alone
PMID:10769212	FYPO:0004652	temperature restrictive for cdc4-8 alone
PMID:10770926	GO:0003697	activated by ATP
PMID:10770926	GO:0003697	activated by ATP
PMID:10770926	GO:0003697	activated by ATP
PMID:10775265	PBO:0095731	Cdc7p cannot localize to the SPB(s) in cdc11 (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:0097834	I inferred new because it's asymmetric and we know sin is new
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	PBO:0097835	fig 3c
PMID:10775265	PBO:0097836	fig 3d
PMID:10775265	PBO:0095730	Figure4;TableI;datanotshown
PMID:10775265	PBO:0021078	I inferred new because it's asymmetric and we know sin is new
PMID:10775265	FYPO:0001493	dns
PMID:10775265	PBO:0095730	Figure4;TableI;datanotshown
PMID:10775265	PBO:0095730	Figure4;TableI;datanotshown
PMID:10775265	PBO:0095730	Figure4;TableI;datanotshown
PMID:10775265	PBO:0095730	Figure4;TableI;datanotshown
PMID:10775265	PBO:0095730	Figure4;TableI;datanotshown
PMID:10775265	PBO:0097839	Figure4;TableI;datanotshown
PMID:10775265	PBO:0097834	I inferred new because it's asymmetric and we know sin is new
PMID:10775265	PBO:0097839	Figure4;TableI;datanotshown
PMID:10775265	PBO:0097839	Figure4;TableI;datanotshown
PMID:10775265	PBO:0097839	Figure4;TableI;datanotshown
PMID:10775265	PBO:0097839	Figure4;TableI;datanotshown
PMID:10779336	FYPO:0002553	3B
PMID:10779336	FYPO:0001128	5.6%
PMID:10779336	FYPO:0002061	fig8
PMID:10779336	FYPO:0002092	4C
PMID:10779336	FYPO:0002060	2B
PMID:10779336	FYPO:0000141	2
PMID:10779336	FYPO:0001689	3B
PMID:10779336	FYPO:0000620	2B
PMID:10779336	FYPO:0003165	2B
PMID:10779336	FYPO:0000268	3A
PMID:10779336	FYPO:0000089	3B
PMID:10779336	FYPO:0000089	3B
PMID:10779336	FYPO:0000095	3B
PMID:10779336	FYPO:0000141	2B
PMID:10779336	FYPO:0001387	1A
PMID:10779336	FYPO:0001490	1A increased size?
PMID:10779336	FYPO:0000158	1B
PMID:10792724	GO:0004185	residue=S200
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:0104249	Western analysis showed that this decrease was not due to reduced Byr4 amounts
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: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: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: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:0104244	Figure 2E. These results show that Byr4 is re- quired to prevent septation in G1 cells.
PMID:10799520	PBO:0104243	This analysis of microtubule structures confirmed that mononucleate cells with Cdc7 local- ized to SPBs were in interphase and suggested that Byr4 was required to prevent septation during interphase.
PMID:10799520	FYPO:0001222	combine, other binucleates should unde new term
PMID:10799520	PBO:0104241	is this the right term?
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: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:0022584	Cdc7-HA was not localized to SPBs during interphase (Fig. 1C, 1),
PMID:10805744	PBO:0093825	same as cdc2delta alone
PMID:10805744	PBO:0094458	not sown it is ser/thr kinase activity
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: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	fig2
PMID:10850973	GO:0008441	activated_by(CHEBI:18420)| activated_by(CHEBI:29103)| inhibited_by(CHEBI:48607)| inhibited_by(CHEBI:26710)
PMID:10852821	PBO:0094468	fig8 myo2 clumped in nodes instead of ring
PMID:10852821	FYPO:0002050	Fig. 3B
PMID:10852821	FYPO:0004736	fig9 maintenance
PMID:10852821	FYPO:0002050	Fig. 3B
PMID:10852821	FYPO:0001368	fig8
PMID:10852821	FYPO:0001368	fig8
PMID:10852821	PBO:0094464	Fig 6
PMID:10852821	PBO:0094465	Fig 6
PMID:10852821	PBO:0094464	Fig 6
PMID:10852821	PBO:0094466	fig 7A
PMID:10852821	PBO:0094467	fig 7A (depends on actin)
PMID:10852821	PBO:0094465	Fig 6
PMID:10852821	PBO:0094464	Fig 6
PMID:10852821	FYPO:0000161	Fig. 3B
PMID:10852821	FYPO:0000161	Fig. 3B
PMID:10852821	PBO:0094469	fig8
PMID:10852821	PBO:0094469	fig8
PMID:10852821	PBO:0094468	fig8 myo2 clumped in nodes instead of ring
PMID:10852821	FYPO:0007127	fig9
PMID:10852821	PBO:0094464	Fig 6
PMID:10864871	FYPO:0000284	2nd division
PMID:10871341	FYPO:0002044	Fig. 1
PMID:10871341	PBO:0095590	Fig. 1
PMID:10871341	FYPO:0000474	Fig. 1
PMID:10871341	FYPO:0002044	Fig. 1
PMID:10879493	FYPO:0000081	2M glucose = 36% w/v = A LOT, so it is osmolarity rather than glucose itself I guess
PMID:10879493	FYPO:0000081	2M glucose = 36% w/v = A LOT, so it is osmolarity rather than glucose itself I guess
PMID:10886372	FYPO:0002059	don't know veg or spore
PMID:10905343	PBO:0098815	total alpha tubulin level reduced but not known whether from nda3 or atb2 or both
PMID:10905343	PBO:0098816	total alpha tubulin level reduced but not known whether from nda2 or atb2 or both
PMID:10921876	PBO:0105403	APC-Ste9 dependent protein destruction/11365/) I didn't do a phenotype for this becase they don't whow 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	FYPO:0001425	fig1 b
PMID:10921876	PBO:0100981	fig1a
PMID:10921876	PBO:0105409	fig1a
PMID:10921876	GO:1905785	APC-SLP1
PMID:10921876	PBO:0096939	fig3 cdc25-22 block and release
PMID:10921876	PBO:0105406	fig3 cdc25-22 block and release
PMID:10921876	PBO:0105405	fig3 cdc25-22 block and release
PMID:10921876	PBO:0105404	fig3 cdc25-22 block and release
PMID:10921876	PBO:0105405	fig 3 cdc25-22 block and release
PMID:10921876	PBO:0105404	fig 3 cdc25-22 block and release
PMID:10921876	PBO:0105402	APC-Ste9 dependent protein destruction/11365/) I didn't do a phenotype for this becase they don't whow 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:0104485	localized in an identical manner to wild-type mid1p (Figure 9A) and was fully functional (Figure 7 and Table 2).
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:0104487	diffuse cytoplsmic throughout the cell cycle
PMID:10930468	FYPO:0006638	diffuse cytoplsmic throughout the cell cycle
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: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: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: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	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	FYPO:0001234	and the generation time of the population was increased approximately two-fold (Figure 1C top).
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: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	FYPO:0008074	noNLS*-mid1p was detectable in the nucleus when expressed under the control of mid1 promoter (
PMID:10930468	PBO:0104484	no NLS*-mid1p was detectable in the nucleus when expressed under the control of mid1 promoter (
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	Tetrad dissection indicated that the mis3-224 dsk1 null double mutant failed to grow at any temperature.
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: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: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: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: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: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: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 pro- teins 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 ac- tivity 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:10950958	FYPO:0002061	Tetrad analysis of the heterozygous diploid showed two viable (Ura􏰄) and two inviable spores (Fig. 3D), indicating that the its3􏰀 gene is essential for cell growth.
PMID:10950958	FYPO:0006625	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	nterestingly, the level of PI(4)P was significantly higher than that of the wild-type cells.
PMID:10950958	FYPO:0006626	NOT PM
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:0001406	Micro- scopic 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: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:10954610	PBO:0099392	steady-state labeling assay; stability increases in wt but not sty1delta upon UV exposure
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:10970777	GO:0004081	there is another unknown gene with this activity
PMID:10970777	PBO:0096414	decreased
PMID:10978278	PBO:0097277	beta tubulin specific pathway
PMID:11007487	PBO:0038059	Fig 4F However, tip1p was observed at the tips of the astral microtubules that ema- nated 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	FYPO:0000224	Fig 1 tip1 expressed from pREP3X
PMID:11007487	FYPO:0004700	Fig 1 tip1 expressed from pREP3X
PMID:11007487	FYPO:0000015	Fig 1 tip1 expressed from pREP3X
PMID:11007487	FYPO:0000014	Fig 1 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 3 H (methanol fixation)
PMID:11007487	PBO:0038055	Fig 3D
PMID:11007487	PBO:0038056	Fig 3F (methanol fixation)
PMID:11007487	PBO:0037211	Figures 4C and 4G
PMID:11007487	PBO:0098916	( data for these cells not shown)
PMID:11007487	FYPO:0001400	Fig 3 K (methanol fixation)
PMID:11007487	PBO:0098915	Fig 3 K (methanol fixation)
PMID:11007487	PBO:0037218	Fig3I
PMID:11007487	FYPO:0001366	Fig 3I (Formaldehyde fixation)
PMID:11007487	PBO:0018345	Fig 4A & fig 3 G
PMID:11007487	PBO:0098917	Fig 4
PMID:11007487	PBO:0098918	Fig 6 (live cell imaging) GFP-tubulin expressed from nmt1 promoter on multi copy plasmid
PMID:11007487	FYPO:0005799	Fig 6 (live cell imaging) GFP-tubulin expressed from nmt1 promoter on multi copy plasmid
PMID:11007487	PBO:0098919	Fig 3 (methanol fixation)
PMID:11007487	PBO:0098920	Fig 3 C
PMID:11007487	FYPO:0001018	Fig 1 B
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	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	GO:0008017	figure 4H in vitro
PMID:11007487	PBO:0098921	(Figure 4I) I'm not sure if we knew it was the plus end then, but we do now ;)
PMID:11007487	PBO:0098922	(Figure 4I)
PMID:11014802	GO:0010515	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	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	PBO:0098938	Fig 2D
PMID:11018050	FYPO:0002760	Fig 3
PMID:11018050	PBO:0037206	Fig 2B
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:0095634	forms microcolonies
PMID:11018050	PBO:0037209	Fig 2G
PMID:11018050	PBO:0098939	Fig 8 and Fig 5 Tea2 is not completely delocalised but is has a more extended distribution along the microtubules
PMID:11018050	PBO:0037212	Fig 6 cell tip localisation increased compared to exponentially growing cells
PMID:11018050	PBO:0037211	Fig 5
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: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:0002060	growth assayed on agar plates at different temperature and media
PMID:11018050	FYPO:0005809	Data was not shown.
PMID:11018050	PBO:0037208	Fig 4
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	PBO:0098941	fig 8 c
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: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: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:0002060	growth assayed on agar plates at different temperature and media
PMID:11018050	PBO:0022298	Fig 5
PMID:11018050	PBO:0018421	Fig 6
PMID:11018050	PBO:0098940	Fig 8 (vw: I made this 'along micriotubule because we know its microtubule dept)
PMID:11018050	PBO:0037209	Fig 2
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:0002058	growth assayed on agar plates at different temperature and media
PMID:11027257	FYPO:0002061	temp semi-permissive for spp2-8 alone
PMID:11027257	PBO:0019630	mixed population
PMID:11027257	PBO:0023027	mixed population
PMID:11027257	FYPO:0002061	temp semi-permissive for spp2-8 alone
PMID:11027257	FYPO:0002061	temp semi-permissive for spp2-8 alone
PMID:11027257	FYPO:0002060	temp semi-permissive for spp2-8 alone
PMID:11027257	FYPO:0002061	higher temp, restrictive for spp2-8 alone
PMID:11027257	FYPO:0006822	higher temp, restrictive for spp2-8 alone
PMID:11027257	FYPO:0000062	higher temp, restrictive for spp2-8 alone
PMID:11027257	FYPO:0002061	temp semi-permissive for spp2-8 alone
PMID:11027257	FYPO:0002061	temp semi-permissive for spp2-8 alone
PMID:11027257	FYPO:0002061	temp semi-permissive for spp2-8 alone
PMID:11027257	FYPO:0002061	temp semi-permissive for spp2-8 alone
PMID:11027257	FYPO:0002061	temp semi-permissive for spp2-9 alone
PMID:11027257	FYPO:0002061	temp semi-permissive for spp2-9 alone
PMID:11027257	FYPO:0002060	temp semi-permissive for spp2-9 alone
PMID:11027257	FYPO:0002061	higher temp, restrictive for spp2-9 alone
PMID:11027257	FYPO:0006822	higher temp, restrictive for spp2-9 alone
PMID:11027257	FYPO:0000062	higher temp, restrictive for spp2-9 alone
PMID:11027257	FYPO:0002061	temp semi-permissive for spp2-9 alone
PMID:11027257	FYPO:0002061	temp semi-permissive for spp2-9 alone
PMID:11027257	FYPO:0002061	temp semi-permissive for spp2-9 alone
PMID:11027257	FYPO:0002061	temp semi-permissive for spp2-9 alone
PMID:11027257	FYPO:0002061	temp semi-permissive for spp2-9 alone
PMID:11027257	FYPO:0002061	temp semi-permissive for spp2-8 alone
PMID:11027257	FYPO:0002061	temp semi-permissive for spp2-9 alone
PMID:11027263	FYPO:0004672	same as hsk1-1312 alone
PMID:11027263	FYPO:0001355	temp. restrictive for hsk1-1312 alone; fudged a bit because assayed at 32
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:11030618	FYPO:0001690	Fig. 6
PMID:11030618	FYPO:0001690	Fig. 6
PMID:11030618	FYPO:0001690	Fig. 6
PMID:11030618	PBO:0093615	Fig. 6
PMID:11069657	FYPO:0000175	they form parts that fail to mature
PMID:11069779	FYPO:0001524	toxic aa-analog
PMID:11069779	FYPO:0002061	**SYNTHETIC LETHAL
PMID:11071923	FYPO:0007317	global translation, not a specific gene
PMID:11076964	GO:0030479	dependent on F-actin (assayed using Latrunculin A)
PMID:11080156	FYPO:0004537	SAC- fypo/issues/2310
PMID:11080156	FYPO:0003165	after passage through G1
PMID:11080156	PBO:0033364	with cut at second division
PMID:11080156	PBO:0033364	with cut
PMID:11084332	PBO:0102587	total protein in proteasome mutant
PMID:11084332	PBO:0097048	ubiquitinated
PMID:11084332	PBO:0102585	during anaphase
PMID:11084332	PBO:0102586	delayed during anaphase
PMID:11084332	PBO:0102590	ubiquitinated
PMID:11084332	FYPO:0000833	total ubiquitinated
PMID:11084332	PBO:0102589	during G1 arrest fig4 C right hand panel
PMID:11084332	PBO:0102588	during G1 arrest fig4 C right hand panel
PMID:11084332	PBO:0102587	total protein in proteasome mutant
PMID:11102508	PBO:0033981	WT 0.5%
PMID:11112691	PBO:0018339	Myo51 appears to be a component of the CAR.
PMID:11112691	FYPO:0001357	Myo51 were indistinguishable from an isogenic wild-type strain (Fig. 2A,B).
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	FYPO:0000650	septation index of 20%, twice that of wild type (Fig. 2A).
PMID:11112691	PBO:0095634	myo52∆ cells showed extremely slow growth at 36°C (Fig. 2C).
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:0018339	Myo52 formed a cap at the growing tips (Fig. 5C,D).
PMID:11112691	PBO:0020227	Myo52 formed a cap at the growing tips (Fig. 5C,D).
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:0112863	Mok1 was delocalised in myo52∆ (Fig. 8C)
PMID:11112691	PBO:0099929	Whereas Myo51 overproduction resulted in elongated cells with wispy, mis- oriented septal material (Fig. 4A)
PMID:11112691	FYPO:0000032	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: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:11134033	FYPO:0000337	figure 1 b
PMID:11134033	FYPO:0002060	(data not shown)
PMID:11134033	FYPO:0002946	figure 1 a
PMID:11134033	FYPO:0003302	figure 1 b
PMID:11134033	PBO:0037397	figure 1 b (I)
PMID:11134033	PBO:0096454	figure 1 b (I)
PMID:11134033	PBO:0037399	figure 1 C
PMID:11134033	GO:0005737	Fig. 2
PMID:11134033	PBO:0037400	indicated by decreased polysome to monosome ratio
PMID:11160827	PBO:0092751	present throughout mitotic cell cycle
PMID:11179424	PBO:0103795	residue not determined experimentally, but probably Y173
PMID:11226171	FYPO:0000267	same sensitivity as rhp54delta alone
PMID:11226171	FYPO:0000267	same sensitivity as rhp54delta alone
PMID:11226171	FYPO:0005370	sequencing
PMID:11226171	FYPO:0005370	sequencing
PMID:11231017	FYPO:0000106	fig1
PMID:11231017	FYPO:0001234	fig1
PMID:11231572	GO:0110085	dependent on F-actin (assayed using Latrunculin A)
PMID:11231572	GO:0030479	dependent on F-actin (assayed using Latrunculin A)
PMID:11238401	GO:0010515	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	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	FYPO:0007334	oss of association of Swi6 with centromeres should result in expression of a normally silent marker gene embedded in centro- meric 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	oss of association of Swi6 with centromeres should result in expression of a normally silent marker gene embedded in centro- meric 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	PBO:0111582	The ®ssion yeast S. pombe has an HP1 homologue Swi6, which contains a chromo domain that is closely related to those of HP1 family members1. 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	PBO:0111086	whereas the Clr4-G341D strain shows loss of localiza- tion from the nuclear periphery and accumulation of more diffuse staining over the nucleolus (Fig. 4c).
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	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:11248251	PBO:0110542	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	GO:0005759	These results further indicate that the C-terminal end of Cox15p, together with Yah1p, is located in the matrix com- partment. 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: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:11250892	PBO:0108092	figure 3
PMID:11250892	PBO:0108091	Fig 1
PMID:11250892	GO:0072686	Figure 1 C
PMID:11250892	PBO:0108093	fig 7
PMID:11252721	FYPO:0002061	facs and author comment about growth
PMID:11260263	FYPO:0000708	Fig 2 B
PMID:11260263	FYPO:0002061	0.75 M
PMID:11260263	FYPO:0002021	Fig 2 B
PMID:11260263	PBO:0093595	0.75 M
PMID:11263963	PBO:0094278	Fig. 3D
PMID:11263963	PBO:0093596	Fig. 3D
PMID:11263963	PBO:0093596	Fig. 3D
PMID:11263963	FYPO:0000961	Fig. 3D
PMID:11263963	FYPO:0001355	Fig. 3B and D
PMID:11263963	FYPO:0001357	Fig. 3B and D
PMID:11263963	FYPO:0001357	Fig. 3B and D
PMID:11263963	FYPO:0002459	Fig. 3A
PMID:11263963	FYPO:0002459	Fig. 3A
PMID:11263963	FYPO:0000648	Fig. 3A
PMID:11263963	FYPO:0001492	Fig. 3A
PMID:11263963	GO:0005886	Fig. 1B
PMID:11263963	FYPO:0000961	Fig. 3D
PMID:11263963	PBO:0112460	Fig. 4
PMID:11263963	PBO:0112429	Fig. 4
PMID:11263963	PBO:0094276	Fig. 3D
PMID:11263963	PBO:0094279	Fig. 3D
PMID:11263963	PBO:0112460	Fig. 4
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	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	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:11271422	PBO:0038207	Fig. 2A
PMID:11271422	FYPO:0005369	Fig. 3A
PMID:11271422	PBO:0104247	Fig. 1A
PMID:11271422	FYPO:0001315	Fig. 2B
PMID:11271422	FYPO:0002060	Fig. 3A
PMID:11271422	PBO:0107432	Fig. 2A
PMID:11271422	PBO:0112773	Fig. 1A
PMID:11271422	PBO:0097505	Fig. 2A
PMID:11271422	PBO:0097505	Fig. 2B
PMID:11271422	FYPO:0002060	Fig. 3A
PMID:11271422	PBO:0112774	Microscopy revealed occasional cells with an aberrant septum or with multiple nuclei. Fig. 2A
PMID:11271422	PBO:0097505	Fig. 2B
PMID:11271422	PBO:0112775	Fig. 1A
PMID:11271422	FYPO:0002049	Fig. 2B
PMID:11279037	FYPO:0002061	taf73 does not substitute for taf5
PMID:11290708	GO:0005634	qualifier=predominantly
PMID:11294895	PBO:0018421	localization requires F-actin (assayed using latrunculin A)
PMID:11294895	PBO:0100352	localization requires F-actin (assayed using latrunculin A)
PMID:11294895	PBO:0019716	localization requires F-actin (assayed using latrunculin A)
PMID:11294907	PBO:0018972	dependent on actin cytoskeleton (assayed using Latrunculin A)
PMID:11294907	GO:0110085	dependent on actin cytoskeleton (assayed using Latrunculin A)
PMID:11294907	PBO:0095173	dependent on actin cytoskeleton (assayed using Latrunculin A)
PMID:11294907	PBO:0095174	dependent on actin cytoskeleton (assayed using Latrunculin A)
PMID:11313455	GO:0003682	chromatin fractionation assay
PMID:11313455	GO:0003682	chromatin fractionation assay
PMID:11313455	GO:0003682	chromatin fractionation assay; increased during response to DNA damage by MMS or ionizing radiation; dissociates during response to HU
PMID:11313465	PBO:0106867	phosphorylates Cds1
PMID:11313465	PBO:0106866	cellular response to hydroxyurea
PMID:11313465	PBO:0106865	Rad3 phosphorylates T11 in response to hydroxyurea treatment
PMID:11331883	PBO:0098556	Consistently, Rec8 localization was indistinguishable from wildtype 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	FYPO:0005648	Fig. 2c and Table 1),
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:11331883	PBO:0109721	table1
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: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: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: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:11350031	PBO:0098377	all taf1 introns affected
PMID:11359920	PBO:0032993	30 degrees
PMID:11359920	PBO:0097499	30 degrees
PMID:11359920	PBO:0032998	30 degrees
PMID:11359920	FYPO:0001430	30 degrees
PMID:11359920	PBO:0094206	30 degrees
PMID:11359920	FYPO:0001933	30 degrees
PMID:11359920	PBO:0032994	30 degrees
PMID:11359920	PBO:0032997	30 degrees
PMID:11359920	PBO:0097500	30 degrees
PMID:11359920	PBO:0097498	30 degrees
PMID:11359928	PBO:0106452	fig 2 c
PMID:11359928	PBO:0019203	fig 8
PMID:11359928	PBO:0095312	fig 3a
PMID:11359928	PBO:0106454	Figure 4A
PMID:11359928	PBO:0106453	Figure 4A
PMID:11359928	PBO:0019203	fig 2 c
PMID:11369198	PBO:0023853	fig 2B
PMID:11369198	PBO:0018845	fig 2 B
PMID:11369198	FYPO:0002061	data not shown
PMID:11369198	PBO:0036768	Figure 5b
PMID:11369198	PBO:0022298	movie 1A
PMID:11369198	PBO:0097445	Figure 5b
PMID:11369198	FYPO:0004236	Figure 5b
PMID:11384993	PBO:0101548	barely above background for vector alone and Sid1C (Fig. 2B)
PMID:11384993	PBO:0101549	a significant reduction in kinase activity (􏰑40% of Sid1)
PMID:11387218	PBO:0095886	punctate in wild type, diffuse throughout nucleus in mutant
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:11387325	PBO:0111636	The key findings were that the S. pombe guany- lyltransferase 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:0111636	The key findings were that the S. pombe guany- lyltransferase 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 pep- tide or the Ser2-PO4 peptide (Fig. 3B).
PMID:11389847	FYPO:0006279	Fig. 5A
PMID:11389847	FYPO:0006279	Fig. 5A
PMID:11389847	PBO:0114389	Fig. 2
PMID:11389847	PBO:0114389	Fig. 5A
PMID:11389847	FYPO:0006279	Fig. 5A
PMID:11405625	PBO:0019133	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 resis- tants, which implicates that spSNW1 is an essential gene in S. pombe.
PMID:11432827	FYPO:0004317	1A
PMID:11432827	FYPO:0002638	ind mad2 mutant loses viability
PMID:11432827	GO:0000940	dependent on mitotic spindle (GO:0072686)
PMID:11432827	PBO:0093562	figure 4A
PMID:11432827	FYPO:0002060	2C
PMID:11432827	PBO:0033178	figure 4B
PMID:11432827	FYPO:0000276	Figure 1 C
PMID:11432827	FYPO:0006196	Figure 1 C
PMID:11432827	FYPO:0000141	Figure 1 A
PMID:11432827	FYPO:0000416	cut2 levels were reduced in alp14 mutant
PMID:11432827	FYPO:0001574	Figure 1 A
PMID:11432827	FYPO:0001491	2C
PMID:11432827	FYPO:0000131	1A
PMID:11432827	FYPO:0001734	Figure 1 C
PMID:11432827	FYPO:0004318	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	FYPO:0000324	3f
PMID:11432827	FYPO:0003165	Fig 3B
PMID:11432827	FYPO:0002061	Figure 3A, rapid loss of viability
PMID:11432827	FYPO:0002061	Table 1
PMID:11448769	PBO:0019801	(vw: sid2 phenotype indicates that Clp1 localization is independent of SIN)
PMID:11460168	FYPO:0009019	Fig. 4D
PMID:11460168	PBO:0112762	Fig. 3B
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:0112425	Fig. 2B
PMID:11460168	PBO:0112424	Fig. 1E and F
PMID:11460168	PBO:0112763	Fig. 3B
PMID:11460168	FYPO:0006660	Fig. 4E
PMID:11460168	PBO:0112429	Fig. 4A
PMID:11460168	FYPO:0001357	Fig. 4A
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	PBO:0112764	Fig. 4B
PMID:11460168	PBO:0112765	Fig. 4B
PMID:11460168	PBO:0112430	Fig. 4F
PMID:11493649	GO:0051447	negative regulation of meiotic exit
PMID:11493649	GO:0051446	positive regulation of meiotic cell cycle exit
PMID:11509236	FYPO:0000426	After 15 min, vacuoles were visible in all three strains, and this observa- tion demonstrates that, as in budding yeast [8, 9], endocy- tosis does not require a functional type V myosin.
PMID:11509236	FYPO:0000426	After 15 min, vacuoles were visible in all three strains, and this observa- tion demonstrates that, as in budding yeast [8, 9], endocy- tosis does not require a functional type V myosin.
PMID:11509236	FYPO:0002792	vacuoles in myo52
 were smaller (0.21  0.14 m). (Figure 1)
PMID:11514435	GO:0071944	Figure 5
PMID:11514435	PBO:0098114	figure 1 Figure 3B and 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	PBO:0098115	Figure 5D
PMID:11514435	PBO:0098115	Figure 5 E
PMID:11514435	PBO:0098116	Figure 5 E to membrane
PMID:11514435	GO:0052712	(Figure 7b) heterologous complementation
PMID:11514435	FYPO:0005485	figure 7b
PMID:11514435	FYPO:0005485	figure 7b
PMID:11514435	GO:0052714	(Figure 7D) assayed reaction products
PMID:11514435	GO:0046513	from MF
PMID:11514435	GO:0046521	from MF
PMID:11514435	PBO:0098117	fig 6
PMID:11514435	PBO:0098113	figure 1 & Figure 3B and Table 2
PMID:11514435	PBO:0098118	fig 6
PMID:11514435	GO:0005886	Figure 4D, lane 3 + figure 5
PMID:11514435	GO:0016020	Figure 4D, lane 3
PMID:11514436	FYPO:0001120	figure 4a
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	PBO:0105022	dns
PMID:11514436	FYPO:0002024	table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	figure 3biv
PMID:11514436	FYPO:0002061	figure 3a
PMID:11514436	FYPO:0002024	table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002061	figure 3a
PMID:11514436	FYPO:0002061	figure 3a
PMID:11514436	FYPO:0002024	figure 3biv
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: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	PBO:0094971	asymetric localization is normal
PMID:11514436	FYPO:0002024	table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	SID PHENOTYPE (Figure 2B).
PMID:11514436	FYPO:0002061	(Figure 2A).
PMID:11514436	FYPO:0006023	figure 2b
PMID:11514436	FYPO:0001357	(Figure 1C, lane 8
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:0113871	figure 4a
PMID:11553781	PBO:0103157	Rad3 phosphorylates S345 in response to DNA damage caused by ionizing radiation
PMID:11553781	PBO:0103159	vw: changed from response to chemical to part of DNA damage checkpoint signalling
PMID:11554922	FYPO:0000188	evidence: immunoblot using antibody that recognizes thymine dimers
PMID:11598020	GO:0005634	fig 4a
PMID:11598020	PBO:0106460	fig 4a
PMID:11598020	PBO:0106461	fig 4a
PMID:11598020	GO:0005721	fig 4a
PMID:11598020	GO:0005721	fig 4a
PMID:11600706	PBO:0111728	(vw: in vitro purification system)
PMID:11600706	PBO:0111727	(vw: in vitro purification system)
PMID:11600706	GO:0005515	fig 2B
PMID:11600706	GO:0005515	fig 2B
PMID:11600706	PBO:0111729	(vw: in vitro purification system)
PMID:11600706	MOD:01149	Figure 3B
PMID:11600706	FYPO:0005934	figure 1C
PMID:11600706	FYPO:0002778	figure 1C
PMID:11606752	PBO:0098344	level of mutant cdc18deltaCDK1-5 protein
PMID:1165770	PBO:0102251	Figure 3
PMID:1165770	PBO:0093712	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:0102250	Table 1, Figure 2
PMID:1165770	PBO:0102252	Table 1
PMID:1165770	PBO:0102253	Table 1
PMID:11676915	FYPO:0002912	fig 1 a
PMID:11676915	FYPO:0001368	fig 1 a
PMID:11676915	PBO:0095718	fig 1 a
PMID:11676915	PBO:0018634	figure 3 b
PMID:11676915	PBO:0018346	figure 3 b
PMID:11676915	PBO:0095723	fig 5a
PMID:11676915	PBO:0094089	fig 5c
PMID:11676915	FYPO:0000941	dns
PMID:11676915	PBO:0095724	scaffold, platform
PMID:11676915	PBO:0095725	scaffold, platform
PMID:11676915	PBO:0095726	scaffold, platform
PMID:11676915	PBO:0095727	scaffold, platform
PMID:11676915	PBO:0095721	figure 6
PMID:11676915	PBO:0095728	figure 6
PMID:11676915	PBO:0095729	figure 6
PMID:11676915	PBO:0095730	figure 6
PMID:11676915	PBO:0095731	figure 6
PMID:11676915	PBO:0094918	figure 6
PMID:11676915	PBO:0095732	figure 6
PMID:11676915	PBO:0095733	figure 6
PMID:11676924	GO:0000723	qualifier=same_pathway
PMID:11676924	GO:0140445	colocalizes with this region and taz1, abnormal localization in taz1-delta, and physically associates with taz1
PMID:11683390	PBO:0018677	Fig2A pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF)
PMID:11683390	PBO:0037404	Fig2A, B, Fig 4C, 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	Fig2A, B, Fig 4C, 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	Fig2A, B, Fig 4C, 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	Fig2A, B, Fig 4C, 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	Fig2A, B, Fig 4C, 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	Fig2A, B, Fig 4C, 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	Fig2A, B, Fig 4C, 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	Fig2A pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF)
PMID:11683390	PBO:0022133	Fig2A pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF)
PMID:11683390	PBO:0018999	Fig2A pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF)
PMID:11683390	PBO:0037148	Fig 2A b-c, Fig5D pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	PBO:0023023	Fig 2A b-c, Fig5D pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	PBO:0018634	Fig 2A b-c, Fig5D pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	PBO:0037408	Fig 2A b-c, Fig5 pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	PBO:0037148	Fig 2A b-c, Fig5 pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	PBO:0023023	Fig 2A b-c, Fig5 pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	PBO:0037409	Fig 2A b-c, Fig5 pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	PBO:0024116	Fig2A, B 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	Fig2A, B 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	Fig2A, B 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	Fig2A, B 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:0037410	Fig2A, B 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:0021770	Fig2A, B 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:0037411	Fig 2A, Fig 3, Fig5D pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	PBO:0021007	Fig 2A, Fig 3, Fig5D pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	PBO:0037411	Fig 2A, Fig3 Fig5D pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	PBO:0021007	Fig 2A, Fig3 Fig5D pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	PBO:0037412	Fig 2C, pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).
PMID:11683390	PBO:0106299	Figure 4A
PMID:11683390	PBO:0106300	Figure 4A. Cdc13YFP expressed from integrated pREP45
PMID:11683390	PBO:0106301	Figure 4A. Cdc13YFP expressed from integrated pREP45.
PMID:11683390	PBO:0106304	Data not shown. Cdc2 does not go prematurely to the SPB in a cut12 mutant (this is the stf1-1 mutant)
PMID:11683390	PBO:0106301	Figure 4B. Cdc13YFP expressed from integrated pREP45
PMID:11683390	PBO:0106300	Figure 4A. Cdc13YFP expressed from integrated pREP45. Decreased nuclear import of cdc2YFP compared to cdc13delta cig1delta mutant
PMID:11683390	PBO:0037419	Fig 6
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:0106305	Fig 6 Cdc13YFP and Cdc2YFP remain associated with spindle, SPB. Cdc13 is not recognised by defective APC
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:0037421	Fig 7 do not actually say it is associated with SPB just SPB region, i.e. telomere-SPB- centromere bouquet cluster
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:0037423	Fig 8
PMID:11683390	PBO:0037426	Fig 7
PMID:11683390	PBO:0106306	Fig 7
PMID:11683390	PBO:0106307	Fig 7
PMID:11685532	GO:0000776	mitotic, in meiosis it is only n the kinetochore during meitoic division(metaphase/anaphase) not during prophase
PMID:11694585	GO:0051015	assayed using purified rabbit skeletal muscle F-actin
PMID:11694585	FYPO:0002437	temperature permissive for cdc4-8
PMID:11694585	FYPO:0003315	temperature restrictive for cdc4-8
PMID:11694585	PBO:0019147	various abnormal shapes
PMID:11694585	FYPO:0002061	30 degrees C
PMID:11694585	FYPO:0002023	27 degrees C
PMID:11694585	FYPO:0004257	27 degrees C
PMID:11694585	FYPO:0004257	27 degrees C
PMID:11694585	FYPO:0002061	30 degrees C
PMID:11694585	PBO:0019147	various abnormal shapes
PMID:11694585	GO:0030479	dependent on actin cytoskeleton (assayed using Latrunculin A)
PMID:11694585	GO:0051017	in vitro bundling, detected by microscopy; Figure 2
PMID:11694585	GO:0032153	dependent on actin cytoskeleton (assayed using Latrunculin A)
PMID:11696322	PBO:0104462	igure 3b–g,i)
PMID:11696322	FYPO:0002021	figure 3b–g,i)
PMID:11696322	FYPO:0003315	figure 3b-g
PMID:11696322	PBO:0022665	figure 5bc
PMID:11696322	FYPO:0001234	data not shown
PMID:11696322	PBO:0018345	figure 5a
PMID:11696322	FYPO:0003193	table1
PMID:11696322	FYPO:0003225	table1
PMID:11696322	FYPO:0002401	Figure 4, table1
PMID:11696322	FYPO:0001367	Figure 3fg
PMID:11696322	PBO:0104463	figure 5e
PMID:11696322	FYPO:0000016	figure 3
PMID:11696322	FYPO:0001368	Figure 3fg
PMID:11717425	FYPO:0001095	filter binding assay
PMID:11719193	GO:0008821	magneisum activated_by(CHEBI:18420)
PMID:11737264	FYPO:0007436	population is viable but sick, and the elongated multiseptate cells are probably dead
PMID:11737264	FYPO:0005103	population is viable but sick; can't tell which individual cells are viable
PMID:11737264	PBO:0019176	population grows well, but very small cells look lysed
PMID:11737264	FYPO:0000021	population is viable but sick; can't tell which individual cells are viable
PMID:11737264	FYPO:0000647	population is viable but sick; can't tell which individual cells are viable, but very small cells look lysed
PMID:11737264	PBO:0019176	population is viable, but very small cells look lysed
PMID:11739790	FYPO:0004511	Figure 4, B&D
PMID:11739790	FYPO:0004511	Figure 4, B&D
PMID:11739790	PBO:0105588	arrested
PMID:11739790	FYPO:0002060	Figure 2 and Table 2
PMID:11739790	PBO:0105588	arrested
PMID:11739790	PBO:0105588	arrested
PMID:11777938	FYPO:0000620	NORMAL LENGTH
PMID:11777938	FYPO:0005322	figure 2
PMID:11780129	PBO:0112306	(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	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: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: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: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	PBO:0112300	shown), and the association with otr and KR was much reduced (Fig. 1d).
PMID:11780129	PBO:0110924	However, this mutation did not affect Swi6 localization at otr and KR (Fig. 1e).
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	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:0112302	Psc3 localization was strikingly disrupted in the swi6∆ strain at both loci (Fig. 1b).
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:0112307	we found that cohesin mutants (psc3-1T, psc3-2T, psc3-4T and rad21-K1) pro- duced switching-defective colonies at a rate nearly 100-fold that of the wild type (Fig.3a,b).
PMID:11780129	PBO:0112307	we found that cohesin mutants (psc3-1T, psc3-2T, psc3-4T and rad21-K1) pro- duced switching-defective colonies at a rate nearly 100-fold that of the wild type (Fig.3a,b).
PMID:11780129	PBO:0112307	we found that cohesin mutants (psc3-1T, psc3-2T, psc3-4T and rad21-K1) pro- duced switching-defective colonies at a rate nearly 100-fold that of the wild type (Fig.3a,b).
PMID:11780129	PBO:0112307	we found that cohesin mutants (psc3-1T, psc3-2T, psc3-4T and rad21-K1) pro- duced switching-defective colonies at a rate nearly 100-fold that of the wild type (Fig.3a,b).
PMID:11780129	PBO:0112308	(Fig. 3b, data not shown)
PMID:11780129	FYPO:0000228	Figure 2b
PMID:11780129	PBO:0112305	(Fig. 2a, b).
PMID:11781565	PBO:0096413	Fig7B res1S130A prevents the normal down regulation of MBF dependent transcription by res1+
PMID:11781565	FYPO:0006762	Fig2B
PMID:11781565	PBO:0106282	Fig1B
PMID:11781565	PBO:0106294	FIg4E
PMID:11781565	FYPO:0002060	Fig 5 res1-S130A can rescue the pat1-114 mutant at low levels of over expression
PMID:11781565	PBO:0106277	Fig1B
PMID:11781565	PBO:0106278	Fig1B
PMID:11781565	FYPO:0002061	Fig5 res1+ is unable to rescue the pat1-114 mutant at low levels of over expression
PMID:11781565	PBO:0106281	Fig1B
PMID:11781565	PBO:0106278	Fig1B
PMID:11781565	PBO:0105915	Fig6
PMID:11781565	PBO:0098713	Fig7B res1S130A prevents the normal down regulation of MBF dependent transcription by res1+
PMID:11781565	PBO:0096409	Fig7B res1S130A prevents the normal down regulation of MBF dependent transcription by res1+
PMID:11781565	PBO:0109006	Fig2B
PMID:11781565	PBO:0106291	Fig2B
PMID:11781565	PBO:0106286	Fig1C Shows 5 fold increase in presence of HU compared to no HU. res1 and lacZ fusion on episomal plasmids
PMID:11781565	PBO:0106283	Fig1B
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:0106280	Fig1B
PMID:11781565	PBO:0106287	Fig1C 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	Fig1C 5 fold increase in HU compared to no HU. res1 and lacZ fusion on episomal plasmids
PMID:11781565	PBO:0106288	Fig2B
PMID:11781565	PBO:0106289	Fig2B
PMID:11781565	PBO:0106290	Fig2B
PMID:11781565	PBO:0106279	Fig1B
PMID:11781565	PBO:0106292	Fig3A
PMID:11781565	PBO:0106292	Fig3B
PMID:11781565	PBO:0106292	Fig3B
PMID:11781565	PBO:0106293	Fig4D
PMID:11781565	PBO:0106293	Fig4D
PMID:11781565	PBO:0106293	Fig4D
PMID:11792803	PBO:0093462	fig6
PMID:11792803	FYPO:0004255	figure 2 b
PMID:11792803	FYPO:0005738	figure 2 b
PMID:11792803	FYPO:0003758	figure 2 a ( stretched chromaitn along elongating spindle at anaphase B)
PMID:11792803	PBO:0023853	fig8
PMID:11792803	PBO:0092680	fig8
PMID:11792803	FYPO:0005739	figure 2 b
PMID:11792803	FYPO:0000276	figure 2 b chromsome detached from spindle
PMID:11792803	PBO:0033839	fig8
PMID:11792803	PBO:0093462	fig6
PMID:11792803	PBO:0093462	fig6
PMID:11818066	FYPO:0002052	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:11818066	PBO:0111616	Rad24 sequesters phosphorylated Mei2, preventing Mei2 binding to meiRNA (sme2)
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: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: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: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: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: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: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: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: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: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: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	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	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: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	PBO:0110526	sar1, sec31 and pmm1 are essential genes 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:0110528	19% were septated, binucleated cells with condensed chromosomes. (vw:2c binucleate? should this be WT knockdown?)
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: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:11854402	PBO:0101937	during premeiotic DNA replication
PMID:11854402	PBO:0101936	during premeiotic DNA replication
PMID:11854402	PBO:0101936	during premeiotic DNA replication
PMID:11854402	PBO:0099076	during premeiotic DNA replication
PMID:11854402	PBO:0101936	during premeiotic DNA replication
PMID:11854409	GO:0005515	Figure 5B
PMID:11854409	GO:0005515	Figure 5C
PMID:11854409	GO:0005515	UPR
PMID:11854409	GO:0005515	UPR
PMID:11854409	GO:0005515	Figure 5A
PMID:11854409	GO:0005515	UPR
PMID:11854409	FYPO:0006558	fig 2, 3
PMID:11854409	PBO:0097222	fig 1A inviable
PMID:11854409	FYPO:0003440	fig 2, 3
PMID:11856374	FYPO:0002061	Loss of cia1+ led to a lethal phenotype
PMID:11861551	GO:0005634	fig 1a
PMID:11861551	FYPO:0004101	4
PMID:11861551	PBO:0022963	fig 1
PMID:11861551	FYPO:0000229	fig 7a
PMID:11861551	GO:0000776	igure 7
PMID:11861551	PBO:0023853	fig 1a
PMID:11861551	PBO:0035224	fig 3
PMID:11861551	FYPO:0002061	fig 7a
PMID:11861551	PBO:0097993	fig 3
PMID:11861551	FYPO:0003286	4c
PMID:11861551	FYPO:0000131	4
PMID:11861551	FYPO:0004101	4
PMID:11861551	GO:1990023	igure 7
PMID:11861551	PBO:0112057	fig 7
PMID:11861765	FYPO:0001779	fig 3D
PMID:11861765	PBO:0033209	fig 4B,C
PMID:11861765	FYPO:0000141	fig 4 D
PMID:11861765	FYPO:0001234	fig 4 D
PMID:11861765	PBO:0035685	fig 4B,C
PMID:11861765	FYPO:0003241	fig 4B
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	PBO:0033665	fig 3C
PMID:11861765	FYPO:0002061	fig 3B
PMID:11861765	PBO:0093562	fig 3A
PMID:11861765	FYPO:0002578	fig 2 B
PMID:11861765	PBO:0093586	fig 2 B
PMID:11861765	PBO:0093617	fig 2 B
PMID:11861765	PBO:0105969	fig 2 A
PMID:11861765	PBO:0093629	fig 2
PMID:11861765	FYPO:0002060	fig 1
PMID:11861765	PBO:0105971	fig 7C
PMID:11861765	PBO:0035688	fig 8A
PMID:11861765	FYPO:0002061	fig 8B
PMID:11861765	FYPO:0001234	fig 8B
PMID:11861765	FYPO:0000839	fig 8C
PMID:11861765	FYPO:0000141	fig 8C
PMID:11861765	FYPO:0000925	fig 5A
PMID:11861765	PBO:0105970	fig 7B
PMID:11861765	FYPO:0000581	fig 5B
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:11861905	PBO:0092180	figure 1a
PMID:11870212	PBO:0023853	Fig. 3B
PMID:11870212	PBO:0108184	Fig. 3B
PMID:11870212	PBO:0033837	Fig. 3B
PMID:11870212	PBO:0033837	Fig. 3B
PMID:11870212	PBO:0023853	Fig. 3B
PMID:11870212	PBO:0108184	Fig. 3B
PMID:11870212	FYPO:0000141	movement in anap[hase A
PMID:11882285	FYPO:0000639	fig 1
PMID:11882285	FYPO:0003307	fig 1
PMID:11882285	PBO:0102359	S1
PMID:11882285	FYPO:0001532	fig 1
PMID:11882285	FYPO:0000274	fig 1
PMID:11882285	PBO:0102361	fig 5a ie wt like
PMID:11882285	PBO:0102359	S1
PMID:11882285	PBO:0102359	S1
PMID:11882285	PBO:0092680	figure 3
PMID:11882285	FYPO:0000091	fig 2D
PMID:11882285	FYPO:0000091	fig 2D
PMID:11882285	PBO:0023558	fig4
PMID:11882285	PBO:0094474	fig 1 (3-4um normal metaphese lenght 2-2.5 um
PMID:11882285	PBO:0102358	fig 1C
PMID:11882285	PBO:0102360	fig 5a
PMID:11882285	PBO:0102359	S1
PMID:11884512	FYPO:0000097	data not shown
PMID:11884512	PBO:0099111	Of the inhibitors we tested, only iodoacetamide (10 mM) and NEM (10 mM) inhibited Ulp1 activity
PMID:11884512	PBO:0095634	data not shown
PMID:11884512	FYPO:0000268	Figure 3 C
PMID:11884512	PBO:0093629	same as rad17 single mutant, epistatic
PMID:11884512	FYPO:0001253	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:11884604	PBO:0114600	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:0098977	not much evidence of specificity for H3 vs. H4 or position
PMID:11884604	PBO:0114601	broad specificity; actually inferred from combination of phenotype and sequence similarity
PMID:11884604	PBO:0114602	broad specificity; actually inferred from combination of phenotype and sequence similarity
PMID:11884604	PBO:0114603	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	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:11884604	PBO:0114596	broad specificity; actually inferred from combination of phenotype and sequence similarity
PMID:11884604	PBO:0114597	broad specificity; actually inferred from combination of phenotype and sequence similarity
PMID:11884604	PBO:0114598	broad specificity; actually inferred from combination of phenotype and sequence similarity
PMID:11884604	PBO:0114599	broad specificity; 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	not (coincident_with(SO:0001789) | coincident_with(SO:0001795))
PMID:11886869	PBO:0093559	zhf strain were viable and showed only a minor reduction in growth rate under control conditions without any added heavy metal salts.
PMID:11886869	PBO:0111429	To determine whether the main pathway for Cd2
 de- toxification in S. pombe, the formation of phytochelatins, is required for the zhf-dependent protection, the zhf gene was disrupted in the pcs strain Sp27 (20). Toxicity assays showed that the protective effect was even more pronounced in this genetic background.
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 con- centration for wild-type cells of 100 
M, zhf cells were inhib- ited 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 zhf cells reached only 36% (3.5%).
PMID:11886869	PBO:0110448	In the presence of elevated Zn2
 levels, however, they were severely growth-inhibited (Fig. 1, A and B).
PMID:11886869	GO:0140209	storage
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:0002150	No mature ascospores were observed in the meu10∆mutant (Fig. 3C and see Fig. 4A).
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	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	Like the meu10∆ mutant, the spores from this mutantwere not viable (Fig. 8B)
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	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	FYPO:0000196	Like the meu10∆mutant (Fig. 3C), mature ascospores were not generatedby this mutant.
PMID:11895484	FYPO:0002043	We next measured the DNAcontent 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: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:11907273	FYPO:0000172	using chromosome III
PMID:11907273	GO:0005515	2-hybrid
PMID:11909965	FYPO:0003762	figure 3a cell cycle arrest in mitotic ametaphase
PMID:11909965	PBO:0096195	2B
PMID:11909965	PBO:0096197	figure 3a DECREASDED cell cycle arrest in mitotic anaphase
PMID:11909965	GO:0005515	figure 5
PMID:11909965	PBO:0023853	figure 5A
PMID:11909965	PBO:0096196	2B
PMID:11909965	PBO:0096196	2B
PMID:11909965	PBO:0033937	2B
PMID:11909965	FYPO:0004318	figure2C
PMID:11909965	FYPO:0004318	figure2C
PMID:11909965	FYPO:0003762	figure 3a cell cycle arrest in mitotic metaphase
PMID:11909965	FYPO:0000069	Fig 2A
PMID:11927555	PBO:0037408	Figure 5
PMID:11927555	FYPO:0000276	Figure 6
PMID:11927555	PBO:0093564	Figure 6
PMID:11927555	PBO:0093562	fig6
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:0093564	Figure 6
PMID:11927555	PBO:0101164	Figure 5
PMID:11927555	FYPO:0003738	fig6
PMID:11927555	FYPO:0000338	fig6
PMID:11927555	FYPO:0001489	fig6
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	PBO:0018346	Figure 5
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:0007566	These data show that Fin1p- mediated compaction of the chromosomes is not func- tionally 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 func- tionally 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 func- tionally 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 func- tionally related to mitotic chromosome condensation and the mechanism by which it occurs remains obscure.
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:11950879	FYPO:0003570	"indicated by ""majority of the Mad2-GFP was localized to the spindle"""
PMID:11950879	FYPO:0002638	"indicated by ""majority of the Mad2-GFP was localized to the spindle"""
PMID:11950879	PBO:0092680	(vw: nda3 tubulin mutant does not assemble spindle and shows Mad2 is localized to unattached kinetochores)
PMID:11950879	FYPO:0003570	"indicated by ""majority of the Mad2-GFP was localized to the spindle"""
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 4 F location alkso exists during mating
PMID:11950884	FYPO:0007563	Fig6B 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	Fig6B
PMID:11950884	FYPO:0007563	Fig6B
PMID:11950884	PBO:0102928	regulation of
PMID:11950884	FYPO:0000761	Fig6C
PMID:11950884	PBO:0102927	location is abolished during mating Fig4Dc and Fig4Ec
PMID:11950884	PBO:0102926	Fig6C
PMID:11950884	FYPO:0000761	Fig6C
PMID:11950884	FYPO:0006772	Fig8D,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	PBO:0102925	Fig6A
PMID:11950884	PBO:0102925	Fig6A
PMID:11950884	PBO:0102925	Fig6A
PMID:11950884	FYPO:0007810	Fig 5, Table 3,4
PMID:11950884	FYPO:0007810	Fig5 Table 3,4
PMID:11950884	FYPO:0007810	Fig5 Table 4
PMID:11950884	PBO:0102924	Fig2A
PMID:11950884	PBO:0102923	Fig2A
PMID:11950884	PBO:0102922	Fig2A
PMID:11950884	PBO:0102921	Fig1
PMID:11950927	FYPO:0000134	Figure 6A)
PMID:11950927	FYPO:0003165	Figure 1C
PMID:11950927	PBO:0098338	Figure2
PMID:11950927	PBO:0098340	Pic1– 765-924, which lacks the IN box, failed to bind Ark1p,
PMID:11950927	FYPO:0000134	fig 3c
PMID:11950927	FYPO:0001513	fig 3c
PMID:11950927	FYPO:0001357	fig4
PMID:11950927	FYPO:0001575	dominent negative effect
PMID:11950927	FYPO:0001575	dominent negative effect
PMID:11950927	FYPO:0001575	dominent negative effect
PMID:11950927	FYPO:0001234	Figure 6A)
PMID:11950932	PBO:0110443	GFP- Cdc11p(1– 630) was distributed throughout the cytoplasm (our unpublished results), but GFP-Cdc11p(631–1045) local- ized to SPBs (Figure 5A).
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:0018346	The single and merged images indicate that CAA20785 colocalizes with Sid4p to SPBs throughout the cell cycle (Figure 2B).
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: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:0110444	How- ever, its localization to the SPB was lost in the sid4-SA1 mutant at restrictive temperature (Figure 3).
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	GFP- Cdc11p(1– 630) was distributed throughout the cytoplasm (our unpublished results), but GFP-Cdc11p(631–1045) local- ized to SPBs (Figure 5A).
PMID:11950932	FYPO:0007569	nterestingly, we found that overproduction of GFP-Cdc11p(631–1045) gener-ated a sid phenotype (Figure 5A).
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 bind- ing site for Cdc11p, thus eliminating the opportunity for the full-length protein to localize to the SPB.
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:11952833	FYPO:0004537	premature SIN
PMID:11952833	PBO:0113865	even though cdc13 is present
PMID:11952833	PBO:0113866	even though cdc13 is present
PMID:11955632	FYPO:0003655	tRNA
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:0002060	figure S1 (20% longer)
PMID:11967147	FYPO:0002060	figure S1 (20% longer)
PMID:11967147	FYPO:0002060	figure S1 (20% longer)
PMID:11967147	FYPO:0006171	Figure 5D abolished pausing
PMID:11967147	PBO:0093767	figure S1
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	fig2d
PMID:11967147	PBO:0024749	fig2d
PMID:11967147	PBO:0103982	fig2a
PMID:11967147	PBO:0103982	fig2a
PMID:11967147	PBO:0020141	fig2b
PMID:11967147	PBO:0020141	fig2b
PMID:11967147	PBO:0103981	Fig 1D
PMID:11967147	PBO:0103981	Fig 1D
PMID:11967147	FYPO:0001840	DNS
PMID:11967147	FYPO:0001840	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
PMID:11967147	FYPO:0002060	figure S1
PMID:11972332	PBO:0109322	Figure 1A
PMID:11973289	FYPO:0001276	"Alleles with ""not specified"" expression were under nmt promoter, I think not induced (but I'm not sure how the resulting exp level compares with endogenous)."
PMID:11973289	FYPO:0001276	"Alleles with ""not specified"" expression were under nmt promoter, I think not induced (but I'm not sure how the resulting exp level compares with endogenous)."
PMID:11973289	FYPO:0001278	"Alleles with ""not specified"" expression were under nmt promoter, I think not induced (but I'm not sure how the resulting exp level compares with endogenous)."
PMID:11973289	FYPO:0002061	"Alleles with ""not specified"" expression were under nmt promoter, I think not induced (but I'm not sure how the resulting exp level compares with endogenous)."
PMID:11973289	FYPO:0002061	"Alleles with ""not specified"" expression were under nmt promoter, I think not induced (but I'm not sure how the resulting exp level compares with endogenous)."
PMID:11973289	FYPO:0002061	"Alleles with ""not specified"" expression were under nmt promoter, I think not induced (but I'm not sure how the resulting exp level compares with endogenous)."
PMID:11973289	FYPO:0002061	"Alleles with ""not specified"" expression were under nmt promoter, I think not induced (but I'm not sure how the resulting exp level compares with endogenous)."
PMID:12000964	FYPO:0000611	(vw: DNA checkpoint dept)
PMID:12000964	FYPO:0004588	(vw: delayed)
PMID:12000964	FYPO:0003438	(vw: I added this as an inference, because the checkpoint is never satisfied)
PMID:12000964	FYPO:0003545	(vw: I added this as an inference, because the checkpoint is never satisfied)
PMID:12006645	FYPO:0002059	tetrads only
PMID:12006658	GO:0005737	"can't capture punctate cytoplasmic localization during heat or osmotic stress, because there isn't a suitable GO CC term, and they wouldn't add something as vague as ""cytoplasmic focus"""
PMID:12006658	GO:0002183	taking authors' word that ribosome profiling phenotype is specific enough to infer role in translation initiation
PMID:12006658	PBO:0105174	assayed by incorporation of labeled methionine
PMID:12006658	PBO:0105175	assayed by incorporation of labeled methionine
PMID:12006658	FYPO:0003125	polysome profiling
PMID:12007420	PBO:0103185	Fig1 C
PMID:12007420	PBO:0101140	Fig1D
PMID:12007420	FYPO:0002452	Fig3B
PMID:12007420	PBO:0103192	Fig4A
PMID:12007420	PBO:0103192	Fig4C
PMID:12007420	PBO:0097442	Fig4B
PMID:12007420	PBO:0019143	Fig4D (jvh: 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	Fig3B
PMID:12007420	FYPO:0002061	Fig3B
PMID:12007420	FYPO:0002060	Fig3B
PMID:12007420	FYPO:0002060	Fig3B
PMID:12007420	FYPO:0002060	Fig3B
PMID:12007420	PBO:0103190	Fig3C
PMID:12007420	PBO:0103189	Fig2D (jvh: tea3GFP staining cell middle after nda3 block and release)
PMID:12007420	PBO:0103188	Fig2D (jvh: no tea3GFP staining cell middle in nda3 block)
PMID:12007420	PBO:0099942	Fig1
PMID:12007420	PBO:0101140	Fig1D
PMID:12007420	PBO:0103185	Fig1 C
PMID:12007420	FYPO:0003150	Fig1B
PMID:12007420	PBO:0103187	Fig2A
PMID:12007420	PBO:0103186	localisation of tea3 is a late event in septation
PMID:12007420	GO:0051285	localises at both ends, slightly enriched at non growing end
PMID:12007420	PBO:0103191	Fig 3D
PMID:12019258	FYPO:0005433	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:12019258	FYPO:0005431	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:12019258	FYPO:0005432	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:12019258	FYPO:0005431	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:12019258	FYPO:0005431	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:12019258	GO:0042138	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:12023299	PBO:0093619	(mah: same as rad51delta alone)
PMID:12023299	PBO:0093629	(mah: same as rad51delta alone)
PMID:12023299	PBO:0093629	(mah: same as rad51delta alone)
PMID:12023299	PBO:0093619	(mah: same as rad51delta alone)
PMID:12023299	PBO:0093619	(mah: same as rad51delta alone)
PMID:12023299	PBO:0100481	(mah: slighly more severe than rad50delta alone)
PMID:12023299	PBO:0101526	(mah: residue=T215)
PMID:12023299	PBO:0096052	(mah: assayed substrate: exogenous histone H1)
PMID:12023299	PBO:0101530	(mah: same as rad51delta alone)
PMID:12023299	PBO:0093619	(mah: same as rad51delta alone)
PMID:12023299	PBO:0101530	(mah: same as rad51delta alone)
PMID:12023299	PBO:0093620	(mah: sensitivity depends on how highly overexpressed top3+ is; more top3+ -> lower sensitivity)
PMID:12023299	PBO:0093620	(mah: same as rqh1delta alone)
PMID:12023299	GO:0000724	(mah: localization to DSB sites also contributes to inference)
PMID:12034771	PBO:0100778	Fig4B. 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:0103839	Fig6
PMID:12034771	PBO:0103838	Fig6
PMID:12034771	PBO:0103834	Fig3C
PMID:12034771	PBO:0103837	Fig6
PMID:12034771	PBO:0037574	Fig5B
PMID:12034771	PBO:0037573	Fig5B
PMID:12034771	PBO:0103834	Fig3C
PMID:12034771	PBO:0103834	Fig3C
PMID:12034771	PBO:0103833	Fig3C
PMID:12034771	PBO:0037573	Fig5B
PMID:12034771	FYPO:0003702	Fig5A
PMID:12034771	FYPO:0003702	Fig5A
PMID:12034771	PBO:0103832	Fig3C
PMID:12034771	PBO:0103831	Fig2C OUTSTANDING Q IS IT ALONG OR ON?
PMID:12034771	PBO:0103830	Figure 2A
PMID:12034771	PBO:0103835	Fig4B
PMID:12034771	PBO:0103831	Fig4A
PMID:12034771	PBO:0103829	used endogenous tea2 gene tagged at C term with GFP. Fig1A
PMID:12034771	PBO:0037211	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:0103836	Fig3C, Fig5A STILL TO ADD curved around cell end during mitotic interphase
PMID:12034771	PBO:0018421	used endogenous tea2 gene tagged at C term with GFP. Fig1A
PMID:12050156	PBO:0110449	FIG. 1. Zhf is required for growth on high and low zinc
PMID:12050156	FYPO:0000116	The growth of the resulting zym1 showed only a small but reproducible impairment in rich me- dium (YE5S) supplemented with 10 –100 
M zinc (Fig. 5A).
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: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:0110448	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	PBO:0110448	Most importantly, the zhf 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 
M ZnSO4 (Fig. 1C).
PMID:12050156	PBO:0110451	The abundance of zym1 transcripts was also re- duced in cells lacking Pcr1, a bZIP transcription factor that in conjunction with Atf1 functions downstream of Sty1 (41, 42) (Fig. 3C).
PMID:12050156	PBO:0110450	Both the basal and zinc-induced levels of zym1 transcripts were severely reduced in wis1 (Fig. 3C).
PMID:12050156	PBO:0110449	Zhf Is Required for Growth on Low Zinc
PMID:12058079	GO:0043139	activated_by(CHEBI:18420)
PMID:12062100	PBO:0092132	longer transcript
PMID:12062100	PBO:0097585	longer transcript
PMID:12062100	PBO:0097586	longer transcript
PMID:12065422	PBO:0095084	Figure 1B
PMID:12065422	PBO:0095085	Figures 1C and 2C
PMID:12065422	FYPO:0000620	Figure 2B and C
PMID:12065422	PBO:0095084	Figure 1C
PMID:12065422	FYPO:0001124	recessive, loss- of-function mutation
PMID:12065422	FYPO:0003481	Figure 2A; Table II
PMID:12065422	FYPO:0001124	Table II
PMID:12065422	FYPO:0003481	Table II
PMID:12065422	FYPO:0002061	DNS
PMID:12065422	FYPO:0002061	DNS
PMID:12065422	PBO:0095086	figure 5d
PMID:12065422	PBO:0095087	25 degrees figure5d
PMID:12065422	PBO:0095088	25 degrees figure 7
PMID:12065422	PBO:0095089	25 degrees figure 7
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	FYPO:0001399	recessive, loss- of-function mutation
PMID:12065422	PBO:0095084	Figure 1C
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:12074602	PBO:0111133	binds to 54-bp element at 1186-1239
PMID:12093738	PBO:0100985	Fig5B
PMID:12093738	PBO:0100982	Fig 3B no G1 peak is observed showing that S phase onset is not delayed
PMID:12093738	PBO:0019210	Fig 3 data not shown cell viability is reduced at late time points
PMID:12093738	PBO:0100983	Fig5A small peak of less that 1C DNA content
PMID:12093738	PBO:0100986	Fig 4A cells block normally with 1C DNA content even when cig2 is over expressed
PMID:12093738	PBO:0100990	Fig1D
PMID:12093738	PBO:0100988	fypo/issues/3165 Fig5C
PMID:12093738	PBO:0100989	Fig1D The protein cdc2 protein assayed is in complex with cig2 as there is no cdc2-cdc13 complex present
PMID:12093738	PBO:0100987	Fig5C
PMID:12093738	PBO:0024304	Fig1A
PMID:12093738	PBO:0100981	Fig 3C 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:0100977	Fig1C
PMID:12093738	PBO:0100978	Fig1C
PMID:12093738	PBO:0100979	Fig1C
PMID:12093738	PBO:0100980	Fig2C the cdc2-cig2 and cdc2-cdc13 complexe have no tyrosine 15 phosphorylation
PMID:12093738	PBO:0099888	Fig2C the cdc2-cig2 and cdc2-cdc13 complexes have increased kinase activity
PMID:12093738	PBO:0093769	fypo/issues/3165 Fig5B in the absence of cig2 there is a delay in the appearance of cut cells
PMID:12093738	FYPO:0000017	Fig5A lower panel used forward scatter to measure cell size
PMID:12093738	FYPO:0003449	Fig5A lower panel
PMID:12093738	PBO:0100984	Fig5A used forward scatter to measure cell size small peak of short cells
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: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:0001164	3.7. Association of SpRrn7h with rDNA core promoter sequences
PMID:12112233	FYPO:0003027	Figure 1
PMID:12112233	FYPO:0001357	Figure 1
PMID:12112233	FYPO:0002522	actually accumulation
PMID:12181326	FYPO:0006661	data not shown
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:0107193	fig7
PMID:12181336	PBO:0107189	fig 5
PMID:12181336	PBO:0107191	small amount
PMID:12181336	PBO:0107182	2 B
PMID:12181336	PBO:0107189	fig has 6
PMID:12181336	PBO:0107181	2B
PMID:12181336	PBO:0107183	Fig 3
PMID:12181336	PBO:0107183	Fig 3
PMID:12181336	PBO:0107184	Fig 3
PMID:12181336	PBO:0107189	fig 5
PMID:12181336	PBO:0107184	Fig 3
PMID:12181336	PBO:0107185	Fig 3
PMID:12181336	PBO:0107186	Fig 4
PMID:12181336	PBO:0107187	Fig 4
PMID:12181336	PBO:0107192	fig7
PMID:12181336	PBO:0107188	Fig 4
PMID:12181336	PBO:0107182	2 B
PMID:12185500	FYPO:0002060	25 degrees C
PMID:12185500	FYPO:0000082	restrictive temp 32
PMID:12185500	FYPO:0000082	restrictive temp 36
PMID:12185500	FYPO:0002061	29 degrees C
PMID:12185500	FYPO:0002061	27 degrees C
PMID:12185500	FYPO:0002061	29 degrees C
PMID:12185500	FYPO:0002061	27 degrees C
PMID:12185500	FYPO:0002061	25 degrees C
PMID:12185500	FYPO:0002061	25 degrees C
PMID:12185840	PBO:0101611	Figure 2C
PMID:12185840	GO:0005739	fig 2 C
PMID:12186944	GO:0032153	localization requires microtubules (assayed using thiabendazole or carbendazim) but not F-actin (assayed using latrunculin A)
PMID:12186947	PBO:0021453	penetrance low if cells exposed to UV
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: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 me- dium 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 me- dium 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 me- dium 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 me- dium 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:0107146	As expected, Swi6, which depends on histone modification for chromatin binding, was de- localized from the ura4
 transgenes (Fig. 3C).
PMID:12193640	PBO:0107146	As expected, Swi6, which depends on histone modification for chromatin binding, was de- localized from the ura4
 transgenes (Fig. 3C).
PMID:12193640	PBO:0107146	As expected, Swi6, which depends on histone modification for chromatin binding, was de- localized from the ura4
 transgenes (Fig. 3C).
PMID:12193640	FYPO:0003096	. In contrast, levels of K9 were greatly reduced.
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 me- dium lacking uracil and by Northern blots (Fig. 1, B) (21).
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: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: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 me- dium 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:12196391	PBO:0093637	same as rad26delta alone
PMID:12196391	PBO:0093633	same as either single mutant
PMID:12196391	PBO:0093637	same as rad3delta alone
PMID:12196391	PBO:0093637	same as rad3delta alone
PMID:12196391	PBO:0093637	same as rad3delta alone
PMID:12196391	PBO:0093637	same as rad3delta alone
PMID:12196391	PBO:0093633	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:0002946	fig 4 e
PMID:12242222	FYPO:0000647	fig 4
PMID:12242222	FYPO:0005870	fig 4
PMID:12242294	FYPO:0002390	fig 1a (maintenence of)
PMID:12242294	PBO:0103974	data not shown
PMID:12242294	PBO:0103973	data not shown
PMID:12242294	FYPO:0002061	fig8d
PMID:12242294	PBO:0103972	data not shown
PMID:12242294	PBO:0095634	fig8d
PMID:12242294	FYPO:0001355	fig 8b
PMID:12242294	FYPO:0001355	fig 8b
PMID:12242294	PBO:0034020	figure 9
PMID:12242294	PBO:0099328	data not shown
PMID:12242294	FYPO:0004085	fig 8a
PMID:12242294	FYPO:0002638	fig 8a
PMID:12242294	FYPO:0001355	fig 8a
PMID:12242294	FYPO:0002638	fig 8a
PMID:12242294	FYPO:0000324	fig 1a
PMID:12354095	PBO:0093558	Fig. 4B
PMID:12354095	PBO:0093558	Fig. 4B
PMID:12354095	PBO:0093558	Fig. 4B
PMID:12354095	PBO:0093557	Fig. 5A
PMID:12354095	PBO:0093557	Fig. 5B
PMID:12354095	PBO:0093558	Fig. 5B
PMID:12354095	PBO:0093558	Fig. 5B
PMID:12354095	PBO:0093641	Fig. 1
PMID:12354095	FYPO:0001357	Fig. 1
PMID:12354095	FYPO:0001357	Fig. 1
PMID:12354095	PBO:0094642	Fig. 2B
PMID:12354095	FYPO:0000674	Fig. 2C
PMID:12354095	PBO:0112776	Fig. 2B
PMID:12354095	PBO:0112781	Fig. 3C and D
PMID:12354095	PBO:0110822	Fig. 3A and D
PMID:12354095	FYPO:0001315	Fig. 2B
PMID:12354095	PBO:0112780	Fig. 3B and D
PMID:12354095	FYPO:0001315	Fig. 2B
PMID:12354095	PBO:0093557	Fig. 5A
PMID:12354095	PBO:0093558	Fig. 5A
PMID:12354095	PBO:0093557	Fig. 5B
PMID:12354095	PBO:0093558	Fig. 4A
PMID:12354095	FYPO:0001315	Fig. 2B
PMID:12354095	FYPO:0001315	Fig. 2B
PMID:12354095	PBO:0093558	Fig. 4B
PMID:12354095	PBO:0093557	Fig. 5A
PMID:12354095	FYPO:0001315	Fig. 2B
PMID:12354095	PBO:0104246	Fig. 2B
PMID:12354095	PBO:0095096	Fig. 5C and D
PMID:12354095	FYPO:0001406	Fig. 6
PMID:12354095	PBO:0112779	Fig. 3C and D
PMID:12354095	FYPO:0001470	Fig. 4A
PMID:12354095	FYPO:0001470	Fig. 4B
PMID:12354095	PBO:0093641	Fig. 4B
PMID:12354095	PBO:0112782	Fig. 3B and D
PMID:12354095	PBO:0112783	Fig. 3C and D
PMID:12354095	PBO:0112784	Fig. 3B and D
PMID:12354095	PBO:0112785	Fig. 3C and D
PMID:12354095	PBO:0093641	Fig. 4A
PMID:12354095	FYPO:0000118	Fig. 2B
PMID:12354095	PBO:0093641	Fig. 4B
PMID:12354095	PBO:0093641	Fig. 4B
PMID:12354095	PBO:0112778	Fig. 3B and D
PMID:12354095	PBO:0112777	Fig. 3A and D
PMID:12354095	FYPO:0000674	Fig. 2C
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	PBO:0101752	Fig. 1
PMID:12354095	PBO:0101752	Fig. 1
PMID:12354095	PBO:0093641	Fig. 1
PMID:12390246	PBO:0034017	penetrance is mentioned in EXP accompanying fig 6A
PMID:12390246	PBO:0034015	penetrance is mentioned in EXP accompanying fig 6A
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:12390246	PBO:0034015	Fig 6A
PMID:12390246	FYPO:0005349	fig 4a b
PMID:12390246	PBO:0034018	penetrance is mentioned in EXP accompanying fig 6A
PMID:12399381	PBO:0107305	fig5
PMID:12399381	FYPO:0001490	figure 3
PMID:12399381	PBO:0107303	figure 2C/D
PMID:12399381	FYPO:0000590	fig 5 CD
PMID:12399381	FYPO:0006822	table4
PMID:12399381	PBO:0107308	figure 6 b during x phase?
PMID:12399381	PBO:0094966	semi wee
PMID:12399381	PBO:0094730	figure 6A
PMID:12399381	PBO:0037055	figure 5 CD
PMID:12399381	GO:0034399	fig 5A
PMID:12399381	GO:0005737	fig 5A
PMID:12399381	PBO:0107304	figure 4 cdr phenotype
PMID:12399381	PBO:0107304	figure 4 cdr phenotype
PMID:12399381	PBO:0107302	figure 4 cdr phenotype
PMID:12399381	PBO:0107302	figure 4 cdr phenotype
PMID:12399381	PBO:0107302	figure 4 cdr phenotype
PMID:12399381	PBO:0107302	figure 4 cdr phenotype
PMID:12399381	GO:0005634	fig 5A
PMID:12399381	PBO:0107304	figure 4 cdr phenotype
PMID:12399381	PBO:0107305	fig5
PMID:12399381	PBO:0107305	fig5
PMID:12399381	PBO:0107304	figure 4 cdr phenotype
PMID:12399381	PBO:0095634	figure2a
PMID:12399381	PBO:0037050	figure2a
PMID:12399381	PBO:0095685	figure1
PMID:12399381	PBO:0095634	figure1
PMID:12399381	PBO:0107302	figure1 cdr phenotype
PMID:12399381	PBO:0037050	figure1
PMID:12399381	PBO:0107309	figure1 cdr phenotype
PMID:12411492	PBO:0107491	same as plo1-ts35 alone
PMID:12411492	PBO:0107489	same as plo1-ts35 alone
PMID:12411492	PBO:0107490	same as plo1-ts35 alone
PMID:12419251	PBO:0105826	normal binding periodicity over cell cycle
PMID:12419251	PBO:0105826	normal binding periodicity over cell cycle
PMID:12419251	PBO:0100913	actually ectopic expression, throughout cell cycle
PMID:12419251	FYPO:0000333	actually ectopic expression, throughout cell cycle
PMID:12419251	PBO:0097194	normal binding periodicity over cell cycle
PMID:12426374	PBO:0092680	Figure 1A and C
PMID:12426374	FYPO:0006179	(see rows 4±6 in Figure 1B)
PMID:12426374	FYPO:0006179	(see rows 4±6 in Figure 1B)
PMID:12426374	FYPO:0000141	figure 1 B
PMID:12426374	FYPO:0006190	(vw: assayed by increased mad2 at kinetochore - checkpoint active)
PMID:12426374	FYPO:0002638	(vw: assayed by increased mad2 at kinetochore - checkpoint active)
PMID:12426374	PBO:0092680	Figure 1A and C
PMID:12426374	FYPO:0006179	Figure 1B rows 4±6
PMID:12427731	GO:0007163	based just on this paper, candidate for involved_in_or_regulates qualifier
PMID:12427731	PBO:0097508	substrate myelin basic protein
PMID:12427731	GO:0004672	assayed using myelin basic protein; doesn't rule out tyrosine phosphorylation
PMID:12442907	FYPO:0007628	(Figs. 3A and 3B).
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: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: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: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: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:12455694	FYPO:0002061	32 degrees; mcl1-1 semi-permissive
PMID:12455694	FYPO:0002061	32 degrees; 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:0105161	Figures 3E and 3F)
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: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	GO:0031030	The observation that Clp1p/Flp1p is required for sep- tation in dma1􏰋 mutants is consistent with a model where Dma1p inhibits SIN activation
PMID:12479804	PBO:0105154	fig 1B
PMID:12479804	PBO:0105155	Figure 2A, panels 11 and 14
PMID:12479804	PBO:0105156	Figure 2A, panels 11 and 14
PMID:12479804	PBO:0100276	Figure 2D
PMID:12479804	PBO:0024374	(faintly) Figure 3A, panel 2, arrowhead
PMID:12479804	PBO:0105157	Figure 3A, panel 3
PMID:12479804	PBO:0022584	Figure 3A, panel 3
PMID:12479804	PBO:0105158	Figures 3E and 3F
PMID:12479804	PBO:0105159	Figures 3E and 3F
PMID:12479804	PBO:0096153	Figures 3E and 3F)
PMID:12479804	PBO:0105160	Figures 3E and 3F)
PMID:12479804	PBO:0105161	Figures 3E and 3F)
PMID:12479804	PBO:0105160	Figures 3E and 3F)
PMID:12479804	PBO:0105160	Figures 3E and 3F)
PMID:12479804	PBO:0105161	Figures 3E and 3F)
PMID:12479804	PBO:0105162	Figure 4A 10% (2/20) of anaphase cells displayed Dma1p-GFP SPB signal
PMID:12479804	FYPO:0005781	Table1
PMID:12479804	FYPO:0005781	Table1
PMID:12479804	FYPO:0005781	Table1
PMID:12479804	FYPO:0005781	Table1
PMID:12479804	FYPO:0005781	Table1
PMID:12479804	PBO:0105163	Figure 4A
PMID:12479804	PBO:0105160	Figure 4B)
PMID:12479804	PBO:0105164	igure 4C, bottom
PMID:12479804	PBO:0105165	igure 4C, bottom
PMID:12479804	GO:0005515	Fig4
PMID:12479804	PBO:0094087	Figure 5
PMID:12479804	PBO:0101132	Figure 5
PMID:12479804	PBO:0095090	fig 5
PMID:12479804	PBO:0096052	fig6
PMID:12479804	PBO:0096053	fig6
PMID:12479804	FYPO:0004106	Figure 2
PMID:12482946	PBO:0098309	Fig. 2B
PMID:12482946	PBO:0098310	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:0106607	fig3
PMID:12526748	PBO:0106604	fig3
PMID:12526748	PBO:0096039	D.N.S?
PMID:12526748	PBO:0106603	Pst1p colocalizes with the otr/imr region in a cell cycle-specific manner.
PMID:12526748	PBO:0106604	fig3
PMID:12526748	PBO:0106605	fig3
PMID:12526748	PBO:0096770	fig1
PMID:12526748	FYPO:0006993	fig1b
PMID:12526748	FYPO:0003411	Figure S1
PMID:12526748	FYPO:0002827	Figure S1
PMID:12526748	PBO:0096191	Figure S1
PMID:12526748	PBO:0106594	Figure S1
PMID:12526748	PBO:0106595	Figure 1C
PMID:12526748	PBO:0106596	figure1e
PMID:12526748	PBO:0106597	figure1e
PMID:12526748	PBO:0093562	fig1
PMID:12526748	PBO:0106602	D.N.S?
PMID:12526748	PBO:0096785	D.N.S?
PMID:12526748	PBO:0106606	fig3
PMID:12526748	PBO:0106607	fig3
PMID:12526748	PBO:0093562	fig1
PMID:12526748	PBO:0106598	figure1e
PMID:12526748	PBO:0093562	fig1
PMID:12526748	PBO:0106599	figure1e
PMID:12526748	PBO:0106600	figure1e
PMID:12526748	PBO:0106605	fig3
PMID:12526748	PBO:0106606	fig3
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	PBO:0094968	(Figure 1A) In a mob1-R4 byr4::ura4􏰀 mutant, and also in cdc16-116 grown for 5 hr at 36􏰁C, cdc11p accumulated in the hyperphosphorylated (3) form
PMID:12546793	PBO:0094968	(Figure 1A) In a mob1-R4 byr4::ura4􏰀 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::ura4􏰀, in which cdc7p is present on both spindle pole bodies, the hyperphosphorylated form (3) of cdc11p is more abundant.
PMID:12546793	PBO:0094969	(Figure 1B) n G2-arrested cdc2-17 cells overexpressing spg1p, cdc11p was predominantly in the hyperphosphorylated form
PMID:12546793	GO:0031028	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 accu- mulation of hyperphosphorylated cdc11p.
PMID:12546793	PBO:0094970	HYPERPHOSPHORYLATION (Figure 1C) In the mutant plo1-ts4, which is defective in SIN signaling but not spindle formation [10], hyperphosphorylated cdc11p was observed during mi- tosis, even though the cells were not septating .
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:0094972	(Figure 1C, and data not shown) Immunofluorescence indicated that both byr4p and cdc7p showed a normal, asymmetric distribution during mitosis
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:0094973	(Figure 3B). However, at 36􏰁C, when cdc11p is no longer associated with the SPB [3, 4], most of the cdc11p was hypophosphory- lated (form 1)
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	GO:0032991	SIN signalling complex
PMID:12546793	GO:0032991	SIN signalling complex
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 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 hypophos- phorylated forms (1 and 2) increased (Figure 1E). A simi- lar 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 hyper- phosphorylated form (3) (Figure 1F).
PMID:12546793	PBO:0094973	(Figure 1G) No significant hyperphosphorylation of cdc11p occurred at 36􏰁C.
PMID:12546793	PBO:0094973	(DNS)
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 hypophos- phorylated forms (1 and 2) increased
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:12565823	FYPO:0001035	Fig 4a
PMID:12565827	PBO:0018339	Fig. 2C
PMID:12565827	PBO:0018345	Fig. 2C
PMID:12569356	PBO:0093773	Treat- ment 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	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: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	FYPO:0003183	(Figure 4a). In contrast, treatment of hob3D cells did not produce a hypersensi- tive phenotype.
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	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:12589755	FYPO:0000268	same as crb2delta alone
PMID:12604790	GO:1904931	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	decreased rate of spindle phase I elongation (70 mins. vs 40 wt)
PMID:12606573	PBO:0099171	figure 7B
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:0111078	in vitro assay for activity, phenotype for process
PMID:12606573	FYPO:0005634	figure 7A
PMID:12606573	PBO:0099167	Figure 7A
PMID:12606573	PBO:0099172	Figure 7Ca
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:12606573	FYPO:0000091	Figure 3A during spindle checkpoint
PMID:12606573	FYPO:0005634	figure 7A
PMID:12606573	FYPO:0005634	figure 7A
PMID:12606573	PBO:0099171	figure 7B
PMID:12606573	FYPO:0005634	Figure 4E
PMID:12646585	GO:0071472	kinase activity increases in presence of salt
PMID:12653962	PBO:0035689	fig 6B
PMID:12653962	PBO:0106919	fig 6B
PMID:12653962	PBO:0106919	fig 6B
PMID:12653962	PBO:0035689	fig 6B
PMID:12654901	PBO:0101312	fig 7
PMID:12654901	PBO:0101309	fig2 maximum 3 septa
PMID:12654901	FYPO:0001971	fig2
PMID:12654901	FYPO:0004097	fig 3
PMID:12654901	FYPO:0001971	fig2
PMID:12654901	PBO:0101310	fig2 maximum 3 septa
PMID:12654901	FYPO:0001971	data not shown
PMID:12654901	FYPO:0006399	(Fig. 4, B and C)
PMID:12654901	GO:0032176	Fig 6
PMID:12654901	GO:0036391	Fig 6
PMID:12654901	GO:0032176	Fig 6
PMID:12654901	GO:0036391	Fig 6
PMID:12654901	PBO:0101311	fig7a
PMID:12654901	FYPO:0001971	fig7b
PMID:12654901	FYPO:0001420	not shown
PMID:12654901	FYPO:0000674	not shown
PMID:12654901	FYPO:0002141	not shown
PMID:12654901	FYPO:0001022	not shown
PMID:12654901	FYPO:0001037	not shown
PMID:12654901	FYPO:0004652	"""exhibited well- defined, normal actin rings"""
PMID:12654901	PBO:0098144	fig 8
PMID:12654901	PBO:0101313	fig 8
PMID:12654901	PBO:0101311	fig7c
PMID:12668659	GO:0031097	fig2a
PMID:12668659	FYPO:0001971	fig5
PMID:12668659	PBO:0102770	fig4
PMID:12668659	PBO:0106202	Fig. 3 C
PMID:12668659	PBO:0106202	Fig. 3 C
PMID:12668659	FYPO:0000132	Fig8
PMID:12668659	FYPO:0001234	Fig8
PMID:12668659	FYPO:0001492	Fig8
PMID:12668659	FYPO:0006821	Fig8
PMID:12668659	FYPO:0000021	Fig8
PMID:12668659	PBO:0094588	fig5
PMID:12668659	PBO:0098144	Fig. 7 D
PMID:12668659	PBO:0106209	fig5
PMID:12668659	PBO:0106209	fig5
PMID:12668659	PBO:0106209	fig5
PMID:12668659	FYPO:0001971	fig5
PMID:12668659	PBO:0106207	Fig3
PMID:12668659	PBO:0106206	Fig3
PMID:12668659	PBO:0106205	Fig3
PMID:12668659	PBO:0106204	Fig3
PMID:12668659	PBO:0106203	Fig. 3 A, lanes 1 and 7 (control)
PMID:12668659	FYPO:0001971	fig1
PMID:12668659	FYPO:0002060	fig1
PMID:12668659	PBO:0106202	Fig. 3 A, lanes 1 and 7
PMID:12668659	PBO:0106201	unpublished obsevation
PMID:12668659	PBO:0106201	unpublished obsevation
PMID:12668659	FYPO:0000339	fig1
PMID:12668659	FYPO:0001971	fig5
PMID:12668659	FYPO:0001971	fig5
PMID:12668659	GO:0036391	fig2a colocalizes with sep3
PMID:12668659	PBO:0101311	fig5
PMID:12668659	FYPO:0001971	fig5
PMID:12668659	PBO:0106208	fig4
PMID:12676088	PBO:0099284	telomerase regulator
PMID:12697806	FYPO:0002687	after 100 generations
PMID:12715160	PBO:0020891	salt stress
PMID:12715160	FYPO:0001490	salt stress
PMID:12719471	FYPO:0000732	at anaphase?
PMID:12719471	FYPO:0003217	abolished
PMID:12719471	FYPO:0000732	at anaphase?
PMID:12759375	FYPO:0000737	meiosis II
PMID:12764130	PBO:0093701	Fig3Biii Cells shown a normal tea1 delta morphology
PMID:12764130	PBO:0038195	Fig3B ii
PMID:12764130	PBO:0102652	Fig2B. 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:0038205	Fig 7B,C Penetrance refers to the penetrance of the NTR old-new end growth pattern
PMID:12764130	PBO:0101140	Fig 7A
PMID:12764130	PBO:0099010	Fig4C,D Cells shown a normal tea1 delta actin morphology
PMID:12764130	PBO:0103986	Fig 4E
PMID:12764130	PBO:0038199	Fig4F Cells have a similar defect to a tea1 delta cell wall defect
PMID:12764130	PBO:0038200	Fig 5B
PMID:12764130	PBO:0038202	Data not shown
PMID:12764130	PBO:0038203	Fig6D
PMID:12764130	PBO:0098304	Fig1 GST tea1 directly phosphorylated by Shk1 in vitro Fig2A GST-tea1 is phosphorylated in vivo in a Shk1 dependent manner
PMID:12764130	PBO:0038201	Fig 5C,D
PMID:12764130	PBO:0038206	Fig8. pREP3X tea1 is a multi copy plasmid and is over expressed from the nmt1 promoter
PMID:12764130	PBO:0103985	Fig 4B
PMID:12764130	PBO:0033269	Fig 6B,C
PMID:12764130	PBO:0103984	Fig 1B,C demonstrates in vitro kinase activity. 2A in vivo
PMID:12764130	PBO:0038196	Fig 4B
PMID:12764130	PBO:0035685	Fig5D
PMID:12764130	PBO:0038194	Fig3A tea1 delta is a temperature dependent suppressor of loss of skb15
PMID:12764130	PBO:0038207	Data not shown. pREP3X tea1 is a multi copy plasmid and is over expressed from the nmt1 promoter
PMID:12773390	MOD:00046	Figure 7A and B
PMID:12773390	FYPO:0002061	Fig 1 a
PMID:12773390	FYPO:0002061	figure 1 a
PMID:12773390	FYPO:0002106	figure 1 b (is described as a pair, but is cylindrical short and wide....
PMID:12773390	FYPO:0002060	figure 1 a
PMID:12773390	FYPO:0002061	figure 1 a
PMID:12773390	FYPO:0000113	figure 1 E
PMID:12773390	FYPO:0000113	figure 1 E
PMID:12773390	FYPO:0000113	figure 1 E
PMID:12773390	FYPO:0000113	figure 1 E
PMID:12773390	GO:0005515	figure 1 F
PMID:12773390	GO:0005515	figure 1 F
PMID:12773390	PBO:0092730	Fig 2
PMID:12773390	PBO:0025603	Fig 2
PMID:12773390	PBO:0093562	fig 3 a
PMID:12773390	PBO:0093562	fig 3 a
PMID:12773390	PBO:0093562	fig 3 a
PMID:12773390	FYPO:0000964	fig 3 a
PMID:12773390	FYPO:0000964	fig 3 a
PMID:12773390	PBO:0093562	fig 3 a
PMID:12773390	PBO:0106635	fig 3 b (WT 11%)
PMID:12773390	PBO:0106636	fig 3 b (WT 11%)
PMID:12773390	PBO:0100335	fig 4 a
PMID:12773390	PBO:0099328	fig 4 a
PMID:12773390	GO:1905560	Figure 4A and B
PMID:12773390	GO:0000785	Figure 5B
PMID:12773390	FYPO:0002060	Fig 6 a
PMID:12773390	FYPO:0002061	Fig 6 a
PMID:12773390	FYPO:0002060	Fig 1 a
PMID:12773390	MOD:00047	Figure 7A and B
PMID:12773390	PBO:0112007	Figure 4A and B
PMID:12773390	MOD:00046	Figure 7A and B
PMID:12773390	FYPO:0002060	Fig 1 a
PMID:12773392	PBO:0093629	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
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:0111994	Our analysis revealed that mutant strains display defects in the segregation, resolution and/or condensation of chromosomes during mitosis (Figure 6A), and mis-segre- gated 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:0103767	Our analysis revealed that mutant strains display defects in the segregation, resolution and/or condensation of chromosomes during mitosis (Figure 6A), and mis-segre- gated 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:0103767	Our analysis revealed that mutant strains display defects in the segregation, resolution and/or condensation of chromosomes during mitosis (Figure 6A), and mis-segre- gated 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:0103767	Our analysis revealed that mutant strains display defects in the segregation, resolution and/or condensation of chromosomes during mitosis (Figure 6A), and mis-segre- gated 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	GO:0140937	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:0031078	These data suggest that Clr6 and its associated factors are involved in the deacetylation of histones in vivo.
PMID:12773392	GO:0032129	These data suggest that Clr6 and its associated factors are involved in the deacetylation of histones in vivo.
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	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: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	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:0000892	Moreover, Dprw1 cells showed an increase in acetylation of H3 Lys9 and Lys14.
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: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	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: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	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: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: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: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:0005310	Moreover, Dprw1 cells showed an increase in acetylation of H3 Lys9 and Lys14.
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: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 tem- perature-sensitive (Ts±) growth defects (Figure 5B±D).
PMID:12773392	FYPO:0000082	and irreversible tem- perature-sensitive (Ts±) growth defects (Figure 5B±D).
PMID:12773392	FYPO:0000082	and irreversible tem- perature-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 tem- perature-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: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	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	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	GO:0004407	Af®nity-puri®ed Clr6-HA and control wild-type fractions were incubated with [3H]acetyl- labelled 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: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	normal spatial extent of heterochromatin assembly (JUST)
PMID:12773576	PBO:0104706	increased spatial extent of heterochromatin assembly (JUST)
PMID:12773576	PBO:0104707	outer repeats
PMID:12773576	PBO:0104706	increased spatial extent of heterochromatin assembly (JUST, not at prpote4in coding gene!)
PMID:12773576	FYPO:0004238	Figure 6C
PMID:12786945	PBO:0112181	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:0095629	Fig 3C
PMID:12791993	PBO:0094469	Fig 3C
PMID:12791993	PBO:0095631	Fig 3E, F.
PMID:12791993	PBO:0095196	Fig 3C
PMID:12791993	PBO:0094421	Fig 3E
PMID:12791993	PBO:0095632	Fig 3E
PMID:12791993	FYPO:0001400	Fig2 E,F
PMID:12791993	FYPO:0006005	Fig 4C (displacemetn is supressed by inhibiting membrane trafficking
PMID:12791993	FYPO:0006004	Fig1A
PMID:12791993	FYPO:0003245	Fig 4D, E, F
PMID:12791993	PBO:0095630	Fig 3C
PMID:12791993	FYPO:0005689	Fig 1B cell cycle arrest with post anaphase microtubule array
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	FYPO:0002026	Fig 4D
PMID:12791993	FYPO:0003303	Fig 4D, E, F
PMID:12791993	FYPO:0003838	Fig 1B, C Cells arrest with a stable actinomyosin ring and fail to undergo cytokinesis
PMID:12791993	FYPO:0003126	Fig2 E,F
PMID:12791993	PBO:0095628	Fig 3A
PMID:12791993	FYPO:0003126	Fig 1A
PMID:12796476	FYPO:0001493	figure 1D arrested after 􏰖24 h (Fig. 1 E)
PMID:12796476	GO:0051015	barbed end actin capping
PMID:12796476	GO:0051016	MF?
PMID:12796476	GO:0030041	fission yeast Cdc12 (FH1FH2)p purified from bacteria (Fig. 1 B) stimulated ac- tin polymerization, as detailed below (see Fig. 4). This is consistent with Cdc12(FH1FH2)p and MmCPcapping the barbed (fast depolymerizing) ends of the fila- ments with high affinity (Kd 􏰃 0.1 􏰂M), allowing dissocia- tion only from the slowly depolymerizing (Pollard, 1986) pointed ends (Caldwell et al., 1989)
PMID:12796476	PBO:0106850	actin binding inhibitor pointed end
PMID:12796476	FYPO:0002021	figure 1D but lacked both actin con- tractile rings and polarized actin patches (Fig. 1 D)
PMID:12796476	PBO:0024260	figure 1D but lacked both actin con- tractile rings and polarized actin patches (Fig. 1 D)
PMID:12796476	FYPO:0003210	abnormal (partial, broad, and misoriented) septa (Fig. 1 G)
PMID:12796476	FYPO:0001357	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 pres- ence of functional Cdc12p.
PMID:12796476	FYPO:0005853	figure 1D impressive enrichment of actin filaments in ab- errant thick cables and aster-like accumulations
PMID:12796476	FYPO:0002437	figure 1D impressive enrichment of actin filaments in ab- errant thick cables and aster-like accumulations
PMID:12805221	MOD:00046	referred to in PMID:33137119
PMID:12808043	PBO:0023748	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	FYPO:0001683	plo1.ts2 strains entered mitosis but did not form spindles
PMID:12815070	PBO:0100189	Figs.1A,4C)
PMID:12815070	PBO:0101129	his 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	PBO:0101128	Fig. 2A;
PMID:12815070	PBO:0101128	Fig. 2A;
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:0101130	Plo1-associatedkinaseactivityofextractsfromarrested cdc2.33cut12.s11cellswas2.4-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:0101131	Kinase assays of these mitotic samples indicated that the cut12.s11 mutation promoted a 1.6 (±0.18; n = 5) in-creaseinPlo1-specificactivityduringmitosis(Fig.4D).
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	PBO:0101137	Plo1.K65R,the“kinasedead”mutantprotein,onlyas- sociatedwithmitoticbutnotwithinterphaseSPBs(data not shown).
PMID:12815070	PBO:0101136	The extended and more random size of plo1.ts2cellsatdivisionsuggestedthatthismaybethe case. Despite the fact that these cells are able to enter mitosis,theyappeartobedoingsoinalessefficient,or more random manner (Fig. 8B).
PMID:12815070	PBO:0101135	Whereas cells in which the expres- sionoftheconstitutivelyactivemutantremainedre- pressed 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 pres- ence 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	FYPO:0002061	ability to form colonies o nrich medium at 36°C was indistin- guishable from that of wild-typec ells
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:0101128	Fig. 2A;
PMID:12815070	FYPO:0002060	ability to form colonies o nrich medium at 36°C was indistin- guishable from that of wild-typec ells
PMID:12815070	PBO:0101132	Western blot analysis showed that Plo1 levels in plo1.ts2cellswerenotradicallydifferentfromwildtype,
PMID:12815070	PBO:0101133	full-lengthproteinappearedtobelargely absent from plo1.ts19 on either minimal or rich medium at either 25°C or 36°C (Fig. 7B)
PMID:12815070	PBO:0101133	full-lengthproteinappearedtobelargely absent from plo1.ts19 on either minimal or rich medium at either 25°C or 36°C (Fig. 7B)
PMID:12815070	PBO:0101134	We concluded thatthePlo1-dependentkinaseactivityofbothplo1.ts2 andplo1.ts19wasgreatlyreduced.
PMID:12815070	PBO:0101134	We concluded thatthePlo1-dependentkinaseactivityofbothplo1.ts2 andplo1.ts19wasgreatlyreduced.
PMID:12815070	FYPO:0000276	plo1.ts2 strains entered mitosis but did not form spindles
PMID:12815070	FYPO:0000620	Unlike classic “cut” mutants (Hirano et al. 1986), septation did not always follow on from the mi- toticarrest.
PMID:12815070	FYPO:0002061	Fig 9A. cdc25.22 and cdc25.22 plo1.ts19 cells, on the other hand, could not form colo- nies on this medium at this temperature, but cdc25.22 cut12.s11 cells could
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 colo- nies on this medium at this temperature, but cdc25.22 cut12.s11 cells could
PMID:12815070	FYPO:0002061	triple cut12.s11 cdc25.22 plo1.ts19 cells were unable to grow (Fig. 9A).
PMID:12840005	FYPO:0005356	assayed using RTS1 mut2 or mut8 on plasmid
PMID:12840005	FYPO:0003084	assayed using RTS1 mut2 or mut8 on plasmid
PMID:12840005	PBO:0100889	assayed using RTS1 mut2 or mut8 on plasmid
PMID:12840005	FYPO:0003084	assayed using RTS1 mut2 or mut8 on plasmid
PMID:12840005	PBO:0100890	assayed using RTS1 mut2 or mut8 on plasmid
PMID:12840005	FYPO:0005356	assayed using RTS1 mut2 or mut8 on plasmid
PMID:12857865	FYPO:0000276	Fig4
PMID:12857865	FYPO:0002061	Figure 6A
PMID:12857865	FYPO:0005023	Figure 7 (this protrusion is opposite side of nucleus to the SPB)
PMID:12857865	FYPO:0002061	Fig4
PMID:12857865	GO:0061496	Fig 2/3
PMID:12857865	FYPO:0002061	data not shown
PMID:12857865	FYPO:0002061	data not shown
PMID:12857865	FYPO:0003165	Figure 6A
PMID:12857865	FYPO:0000608	Figure 7
PMID:12857865	FYPO:0003788	Figure 7 (this protrusion is opposite side of nucleus to the SPB)
PMID:12857865	FYPO:0003738	Fig4
PMID:12861005	FYPO:0005402	same as taz1d alone
PMID:12861005	FYPO:0005402	same as taz1d alone
PMID:12861005	PBO:0093616	same as rad51d alone
PMID:12861005	FYPO:0005402	same as taz1d alone
PMID:12861005	FYPO:0005402	same as taz1d alone
PMID:12861005	FYPO:0005402	same as taz1d alone
PMID:12861005	FYPO:0005402	same as taz1d alone
PMID:12861005	FYPO:0005402	same as taz1d alone
PMID:12867036	FYPO:0006681	Compared to wild-type cells, in sir2 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 sir2 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 sir2 cells carrying imr1R::ura4
 did not form colonies on FOA-containing plates, mutant cells carrying otr1R::ura4
 showed ap- preciable growth on FOA plates (Figure 2D). These re- sults 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 sir2 cells carrying imr1R::ura4
 did not form colonies on FOA-containing plates, mutant cells carrying otr1R::ura4
 showed ap- preciable growth on FOA plates (Figure 2D). These re- sults indicated that Sir2 was required for silencing at the S. pombe centromeric DNA regions.
PMID:12867036	FYPO:0006670	We combined the sir2 mutant with REII and found that the sir2 REII double mutant had a strong haploid meiosis phenotype (Figure 2E).
PMID:12867036	FYPO:0000470	We observed a strong reduction in staining of sir2 compared to sir2
 cells, which indicated a reduced rate of switching to the opposite mating type in sir2 cells (Figure 2E, column 1).
PMID:12867036	FYPO:0007336	In contrast, sir2 L(BglII)::ade6
 cells formed white colonies, indicating loss of silencing of the reporter gene (Figure 2C).
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:0111282	Moreover, the level of Swi6 associated with imr1R::ura4
 and otr1R::ura4
 report- ers was reduced 8- and 3-fold, respectively, in sir2 compared to wild-type cells (Figure 3B).
PMID:12867036	PBO:0097399	Histone H3-K9 methylation levels at Kint2::ura4
 and imr1R::ura4
 were strongly reduced in sir2 com- pared to sir2
 cells (32- and 13-fold, respectively) (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	GO:0046969	spSir2 efficiently deacetylated an H4 peptide with acetyl-lysine at position 16 (AcK16) and an H3 peptide with acetyl-lysine at posi- tion 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 posi- tion 9 (AcK9), compared to H4 peptides with acetyl- lysine at positions 5 (AcK5), 8 (AcK8), and 12 (AcK12) (Figure 1B).
PMID:12867036	PBO:0111016	ChIP analy- sis showed that the level of Swi6 associated with Kint2::ura4
 was reduced 47-fold in sir2 compared to wild-type cells (Figure 3B).
PMID:12867036	PBO:0104873	Moreover, the level of Swi6 associated with imr1R::ura4
 and otr1R::ura4
 report- ers was reduced 8- and 3-fold, respectively, in sir2 compared to wild-type cells (Figure 3B).
PMID:12867036	FYPO:0007633	Compared to wild-type cells, in sir2 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:0006815	Compared to wild-type cells, in sir2 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 sir2 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:12868054	FYPO:0000096	fig 7a
PMID:12868054	FYPO:0007286	fig 7 prevacuolar compartment membrane
PMID:12868054	FYPO:0005547	fig 6
PMID:12868054	FYPO:0000583	fig 5
PMID:12868054	FYPO:0003656	4 mM
PMID:12868054	FYPO:0000076	at 5 μg/ml
PMID:12868054	PBO:0096587	strong sensitiv- ity to 100 mM CaCl2 (Figure 4A)
PMID:12868054	FYPO:0004483	Fig3
PMID:12868054	FYPO:0000369	2b
PMID:12868054	FYPO:0002061	While both wild- type and vps33􏰗 cells grew at 26 ◦ C, vps33􏰗 cells exhibited a temperature-sensitive growth at 37 ◦C (Figure 2A).
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:12871901	FYPO:0000611	permissive for cdc25-22; restrictive for cdt2-M1
PMID:12871901	PBO:0096410	Northern blot
PMID:12888492	GO:0033214	IGI with cerevisiae
PMID:12893961	FYPO:0001234	fig3
PMID:12893961	FYPO:0002061	fig4
PMID:12893961	FYPO:0002061	fig4
PMID:12893961	FYPO:0002060	fig3
PMID:12893961	FYPO:0002060	fig4
PMID:12893961	FYPO:0002060	fig4
PMID:12893961	FYPO:0004009	fig5
PMID:12894167	PBO:0102429	"""These results indicate that Mal3 is required for the proper association of Tea2 with microtubules and sug- gest that Mal3 stabilizes the kinesin–microtubule interaction"""
PMID:12894167	PBO:0102431	LOCALIZES OK, IS NOT RETAINED
PMID:12925774	PBO:0097003	during mitotic DNA replication initiation
PMID:12951601	FYPO:0002061	Fig 1d
PMID:12951601	FYPO:0006346	fig 1a 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:12966087	GO:0000724	epistasis with Rhp51
PMID:12966087	GO:0000724	epistasis with Rhp51
PMID:12972434	GO:2000765	e pyruvate kinase, thiazole biosynthetic enzyme, and ribosomal protein L25-A
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	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:12972571	PBO:0101303	late anaphase
PMID:12972571	PBO:0104571	late anaphase
PMID:12972571	PBO:0100551	mcm4ts-td phenotype indicates that Cdc23 chromatin localization is independent of Mcm4
PMID:1314171	GO:0015385	inhibited by CCCP
PMID:1316996	FYPO:0004922	G2 arrest shown by FACS analysis.
PMID:1316996	FYPO:0001382	Hi used as substrate
PMID:1316996	PBO:0096052	HI used as substrate
PMID:1316996	FYPO:0001382	Hi used as substrate
PMID:1316996	FYPO:0002060	cdc2-E9 suppresses mitotic catastrophe at high temperature
PMID:1316996	FYPO:0002060	cdc2-E8 suppresses mitotic catastrophe at high temperature
PMID:1316996	FYPO:0002060	cdc2-A21 suppresses mitotic catastrophe at high temperature
PMID:1316996	PBO:0096052	HI used as substrate
PMID:1316996	FYPO:0000839	cells inviable at all temperatures in presence of wee1+
PMID:1316996	FYPO:0000839	G2 arrest shown by FACS analysis.
PMID:1316996	FYPO:0000839	crosses with this mutant generate a high level of diploids.
PMID:1324908	GO:0008444	regulated by inositol
PMID:1324908	FYPO:0000663	GO:0008444 CDP-DG synthase and GO:0003882 PS synthase
PMID:1324908	GO:0003882	regulated by inositol
PMID:1332977	MOD:00046	3 sites in N-terminus (1-75) and 7 in C-terminus (1221-1485), but positions not determined
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:1372994	PBO:0107331	val: I used this to link to process term even though it isn't shown directly in this paper
PMID:1372994	GO:0010972	AL added as BP since Val had added it involved_in on MF
PMID:1396704	PBO:0094498	activated_by(CHEBI:17234)
PMID:1427071	PBO:0019031	hydroxyurea absent
PMID:14519123	FYPO:0001712	fig3
PMID:14519123	FYPO:0000087	fig4
PMID:14519123	FYPO:0003270	fig4
PMID:14519123	FYPO:0000037	fig3
PMID:14519123	FYPO:0000103	fig4
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:14528010	GO:1990238	specific for dsDNA at ds/ssDNA junction
PMID:14532136	GO:0007129	there is good evidence for this, but not bullet proof
PMID:14585996	PBO:0103275	in presence of hydroxyurea
PMID:14585996	PBO:0094250	residue S604
PMID:14585996	PBO:0094250	residue S604
PMID:14585996	PBO:0103276	in presence of hydroxyurea
PMID:14585996	GO:0000785	phenotype indicates that mrc1/Phos:S604 has higher affinity for chromatin than Unphos:S604
PMID:14599746	GO:0070914	inferred from increased mutation rate upon UV exposure in mutant
PMID:14599746	GO:0006284	rationale: increased transversion frequency indicates that 8-oxoG persists more in mutant, but normal indel frequency suggests not NER
PMID:14602073	GO:0110085	dependent on F-actin (assayed using Latrunculin A)
PMID:14602073	PBO:0018844	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	GO:0110085	dependent on F-actin (assayed using Latruncilin A)
PMID:14602073	GO:0110085	dependent on F-actin (assayed using Latrunculin A)
PMID:14602073	GO:0110085	dependent on F-actin (assayed using Latrunculin A)
PMID:14602073	GO:0110085	dependent on F-actin (assayed using Latrunculin A)
PMID:14602073	PBO:0024047	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	PBO:0024047	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	PBO:0024047	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	PBO:0024047	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	PBO:0024047	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	GO:0110085	independent of F-actin (assayed using Latrunculin A)
PMID:14602073	GO:0110085	dependent on F-actin (assayed using Latrunculin A)
PMID:14602073	GO:0110085	dependent on F-actin (assayed using Latrunculin A)
PMID:14602073	PBO:0018470	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	PBO:0018470	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	PBO:0018470	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	PBO:0018470	late interphase; independent of F-actin (assayed using Latrunculin A)
PMID:14602073	PBO:0018677	before late interphase
PMID:14612233	GO:0004382	activated_by(CHEBI:29108)| activated_by(CHEBI:29035)
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	FYPO:0005947	fig1
PMID:14633985	PBO:0093578	fig1
PMID:14633985	PBO:0093578	fig1c
PMID:14633985	PBO:0093578	fig1c
PMID:14633985	PBO:0093612	fig1c
PMID:14633985	PBO:0094387	fig1c
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:0093577	fig1
PMID:14633985	PBO:0093578	fig1
PMID:14633985	PBO:0094758	the large increase in atf1+ mRNA that is induced by H2O2 in wildtype cells was abolished in csx1D cells.
PMID:14633985	PBO:0094759	This decrease correlated with a large drop in the amount of Atf1 protein (Figure 4C).
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: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:0094766	(Figure 6B) decreased stability in response to oxidative stress
PMID:14633985	PBO:0094767	Figure 7A
PMID:14633985	PBO:0094770	from genetics and Sty1 consensus. Later papers say Activated Sty1 also phosphorylates Csx1
PMID:14654689	PBO:0093621	same as rad11-D223Y alone
PMID:14654689	FYPO:0002239	same as rad11-D223Y alone
PMID:14654689	PBO:0093620	same as rad50delta alone
PMID:14663827	PBO:0110127	Figure 3
PMID:14663827	PBO:0110128	Figure 3
PMID:14663827	PBO:0110129	Figure 3
PMID:14663827	FYPO:0003150	Figure 2
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:0110135	Figure 4
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	PBO:0110126	Figure 3
PMID:14663827	PBO:0110127	Figure 3
PMID:14663827	PBO:0110137	figure5
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:0110123	Figure 1 about 30% from old end
PMID:14663827	PBO:0110124	Figure 1 about 60% from old end
PMID:14663827	PBO:0110124	Figure 1 about 60% from old end
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:0110134	Figure 4
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	PBO:0110125	Figure 3
PMID:14663827	PBO:0110135	Figure 4
PMID:14663827	PBO:0099081	Figure 3
PMID:14663827	PBO:0110136	figure5
PMID:14663827	PBO:0037207	figure5
PMID:14663827	PBO:0110136	figure5
PMID:14663827	PBO:0106644	figure5
PMID:14663827	PBO:0110137	figure5
PMID:14663827	PBO:0110137	figure5
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	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: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: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: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: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:14730319	PBO:0096804	Fig. 4c)
PMID:14730319	PBO:0104851	Fig. 4d
PMID:14730319	PBO:0104849	Fig. 4c)
PMID:14730319	PBO:0104848	Fig. 4d, e)
PMID:14730319	PBO:0104847	Fig. 4c)
PMID:14730319	FYPO:0000091	Fig. 4a)
PMID:14730319	FYPO:0002060	Fig. 4a)
PMID:14730319	PBO:0104845	fig 2 and 3d
PMID:14730319	PBO:0104843	Fig. 2c
PMID:14730319	PBO:0104842	Fig. 2c
PMID:14730319	FYPO:0005648	Fig. 2c
PMID:14730319	PBO:0112496	fig 2a
PMID:14730319	FYPO:0002219	fig 2a
PMID:14739927	GO:0005515	interaction increases during cellular response to UV
PMID:14739927	GO:0005515	proteins dissociate during cellular response to UV
PMID:14742702	PBO:0100542	Figure 3B
PMID:14742702	PBO:0100544	Figure 3B
PMID:14742702	PBO:0100545	Figure 4D
PMID:14742702	PBO:0100541	Figure 3B
PMID:14742702	PBO:0018346	Figure 2A
PMID:14742702	PBO:0100546	Figure 4D
PMID:14742702	PBO:0100547	Figure 4E
PMID:14742702	PBO:0094141	Figure 4F
PMID:14742702	GO:0070850	Figure 5A, lane 4
PMID:14742702	FYPO:0002638	Figure 1A inferred from increased duration of mitosis
PMID:14742702	PBO:0100539	Figure 4A
PMID:14742702	FYPO:0002400	Figure 8E
PMID:14742702	FYPO:0006195	Figure 8E
PMID:14742702	GO:0070850	Figure 5A, lane 4
PMID:14742702	GO:0005515	Figure 6A
PMID:14742702	GO:0005515	Figure 6A
PMID:14742702	PBO:0100548	Figure 6B
PMID:14742702	PBO:0100538	Figure 1D
PMID:14742702	PBO:0100544	8C
PMID:14742702	FYPO:0001978	Figure 8E
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, note chromosome missegregation in the cell of row 3, and see Supplementary Figure S1 for quantifica- tion of spindle intensity
PMID:14742702	FYPO:0000141	Figure 1C
PMID:14742702	FYPO:0000274	Figure 1A
PMID:14742702	FYPO:0005343	Figure 1B
PMID:14742702	FYPO:0006173	Figure 1B
PMID:14742702	PBO:0100543	Figure 3B
PMID:14742702	FYPO:0001733	Figure 8E
PMID:14742702	FYPO:0001355	Figure 8E
PMID:1475195	FYPO:0000470	other evidence = iodine staining
PMID:14766746	FYPO:0004386	filter binding assay
PMID:14766746	PBO:0097029	filter binding assay
PMID:14766746	FYPO:0004384	filter binding assay
PMID:14766746	PBO:0097028	filter binding assay
PMID:14972679	PBO:0106722	Figures 1B
PMID:14972679	FYPO:0005509	Figures 1A and 2
PMID:14972679	PBO:0106724	Figures 1A and 2
PMID:14972679	PBO:0106721	Figures 1B
PMID:14972679	PBO:0106725	Figures 1A and 2
PMID:14972679	FYPO:0004159	Figures 1A and 2
PMID:14972679	PBO:0106723	Figures 1B
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: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 􏰀sgo2 mutant binucleates was in- distinguishable from wild-type.
PMID:15004232	FYPO:0004766	Figure 5F
PMID:15040954	GO:0004022	qualifier=major
PMID:15047861	FYPO:0000650	fig6
PMID:15047861	FYPO:0000426	When the cells were labeled with FM4-64 for 60 min, the 􏰀apm1 cells were highly frag- mented compared with wild-type cells, consistent with the findings obtained by electron microscopy (Figure 7B)
PMID:15047861	FYPO:0002061	fig8c
PMID:15047861	FYPO:0002061	fig1
PMID:15047861	PBO:0093641	fig1
PMID:15047861	PBO:0093595	fig1
PMID:15047861	FYPO:0002061	fig1
PMID:15047861	FYPO:0002060	DNS
PMID:15047861	FYPO:0002061	fig1
PMID:15047861	PBO:0093595	fig1
PMID:15047861	FYPO:0002060	fig1
PMID:15047861	PBO:0093641	fig1
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:0002258	When the cells were labeled with FM4-64 for 60 min, the 􏰀apm1 cells were highly frag- mented compared with wild-type cells, consistent with the findings obtained by electron microscopy (Figure 7B)
PMID:15047861	FYPO:0003279	Figure 3B, a–c
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	FYPO:0000339	Fig. 1
PMID:15068790	FYPO:0002818	Fig. 7
PMID:15068790	PBO:0104133	Fig. 7
PMID:15068790	PBO:0104132	Fig. 7
PMID:15068790	PBO:0104131	Fig. 6
PMID:15068790	PBO:0104131	Fig. 6
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:0104125	Fig. 1
PMID:15068790	PBO:0104124	Fig. 1
PMID:15068790	PBO:0104123	Fig. 1
PMID:15068790	PBO:0104122	Fig. 1
PMID:15068790	PBO:0104134	Fig. 7
PMID:15121844	FYPO:0002357	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:0002134	three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site
PMID:15132994	PBO:0107121	We draw two conclu- sions 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	Fin1 binds Byr4. (A) Fin1 failed to associate with SPBs when the SIN was either inactive or hyperactive.
PMID:15132994	PBO:0033837	fig 1 c
PMID:15132994	FYPO:0006917	is this the correct term?
PMID:15132994	PBO:0018346	fig 1 c
PMID:15147872	PBO:0096456	fig 2
PMID:15147872	PBO:0037889	fig 4 abnormally segregating nuclear membrane #2863 PENDING
PMID:15147872	PBO:0037884	fig 1 a b
PMID:15147872	PBO:0037885	fig 1 c. figure 2
PMID:15147872	FYPO:0005342	fig 3a
PMID:15147872	PBO:0096453	table1
PMID:15147872	PBO:0096452	fig 1 a b
PMID:15147872	PBO:0096454	table1
PMID:15147872	PBO:0096455	table1
PMID:15155581	PBO:0103061	Fig 2
PMID:15155581	PBO:0103062	Fig 2
PMID:15155581	PBO:0103064	Fig 2
PMID:15155581	PBO:0103064	Fig 2
PMID:15155581	PBO:0093579	Fig 3
PMID:15155581	PBO:0093579	Fig 3
PMID:15155581	FYPO:0000267	Fig 3
PMID:15155581	PBO:0103063	Fig 4
PMID:15155581	PBO:0093579	Fig 3
PMID:15155581	FYPO:0003489	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:0103061	Fig 1
PMID:15155581	PBO:0094252	Fig 1
PMID:15155581	PBO:0103061	Fig 1
PMID:15155581	FYPO:0000267	Fig 3
PMID:15155581	PBO:0100318	Fig 5
PMID:15155581	PBO:0103066	Fig 5
PMID:15155581	PBO:0100317	Fig 5
PMID:15155581	PBO:0103071	basal phosphorylation on T412 & S423
PMID:15155581	PBO:0103066	Fig 5
PMID:15155581	PBO:0103063	Fig 4
PMID:15155581	PBO:0100318	Fig 5
PMID:15155581	PBO:0100317	Fig 5
PMID:15155581	PBO:0103065	Fig 4
PMID:15155581	PBO:0103065	Fig 4
PMID:15155581	PBO:0103065	Fig 4
PMID:15155581	PBO:0096806	Fig 3
PMID:15155581	FYPO:0003489	Fig 3
PMID:15155581	PBO:0093580	Fig 3
PMID:15155581	PBO:0093579	Fig 3
PMID:15155581	PBO:0097512	Fig 3
PMID:15155581	PBO:0096806	Fig 3
PMID:15155581	PBO:0093581	Fig 3
PMID:15155581	FYPO:0000267	Fig 3; same as either single mutant
PMID:15155581	PBO:0100925	Fig 2
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: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: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: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:0102382	residue T11
PMID:15173168	PBO:0094255	residue T11
PMID:15173168	PBO:0094255	residue T11
PMID:15173168	PBO:0094255	residue T11
PMID:15173168	PBO:0109147	inferred from phenotypes of mrc1delta, rad3delta, Cds1-Rad26 fusion, other cds1 alleles, and combinations thereof
PMID:15173168	PBO:0094255	residue T11
PMID:15173168	PBO:0094255	residue T11
PMID:15173168	PBO:0094255	residue T11
PMID:15173168	PBO:0094255	residue T11
PMID:15173168	PBO:0094255	residue T11
PMID:15173168	PBO:0094254	residue T11
PMID:15173168	PBO:0094255	residue T11
PMID:15173383	FYPO:0000444	TEV protease present; Cdc6 truncated
PMID:15173383	FYPO:0002061	TEV protease present; Cdc6 truncated
PMID:15175657	FYPO:0002060	dns
PMID:15177031	PBO:0108151	Fig 4C Tip1YFP is expressed from endogenous tip1 gene tagged with YFP
PMID:15177031	PBO:0103837	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 4A,B
PMID:15177031	PBO:0037217	Fig 1 live imaging of Tip1YFP and CFP tubulin
PMID:15177031	FYPO:0002060	Fig 2 same phenotype as tea2delta and tip1delta single mutants
PMID:15177031	PBO:0018345	colocalises with tip1
PMID:15177031	PBO:0108160	Fig6E
PMID:15177031	PBO:0108155	Fig6 E
PMID:15177031	PBO:0108159	Fig 6C,D GFPmal3 is mildly overexpressed from the repressed nmt1 promoter
PMID:15177031	PBO:0102694	Fig 6A,B GFPmal3 is mildly overexpressed from the repressed nmt1 promoter
PMID:15177031	PBO:0108157	Fig 5E,F tea2-GFP is mildly overexpressed from the repressed integrated nmt1 promoter
PMID:15177031	PBO:0108158	(plus end directed)
PMID:15177031	FYPO:0002760	Fig 2 same phenotype as tea2delta and tip1delta single mutants
PMID:15177031	FYPO:0002760	Fig 5E,F tea2-GFP is mildly overexpressed from the repressed integrated nmt1 promoter
PMID:15177031	PBO:0108156	Fig 5A,B Endogenous tea2 tagged with GFP
PMID:15177031	PBO:0103838	Fig 5A,B Endogenous tea2 tagged with GFP
PMID:15177031	PBO:0108155	Fig 5A,B Endogenous tea2 tagged with GFP
PMID:15177031	PBO:0108154	Fig 5C
PMID:15177031	PBO:0037218	Fig 2 same phenotype as tea2delta and tip1delta single mutants
PMID:15177031	PBO:0093701	Fig 2 same phenotype as tea2delta and tip1delta single mutants
PMID:15177031	PBO:0037217	co-localises with tip1
PMID:15177031	PBO:0108149	data not shown
PMID:15177031	PBO:0108150	data not shown
PMID:15177031	PBO:0108153	Fig 4I
PMID:15177031	PBO:0102425	Fig 4E-H
PMID:15177031	PBO:0108152	Fig 4C
PMID:15184401	PBO:0097802	fig 6F
PMID:15184401	PBO:0097801	fig 6F
PMID:15184401	PBO:0097799	Fig. 6 C . (G2)
PMID:15184401	PBO:0097800	Fig. 6 B (G2)
PMID:15184401	PBO:0097799	(G2) Fig. 6 B
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:0097592	Fig. 4 D
PMID:15184401	PBO:0097593	Fig. 4 D
PMID:15184401	PBO:0094424	Fig. 1 C/ Fig3
PMID:15184401	PBO:0094468	Fig. 1 C
PMID:15184401	FYPO:0001122	Fig 1E
PMID:15184401	FYPO:0001122	Fig 1E
PMID:15184401	PBO:0097592	Fig. 1 C
PMID:15184401	PBO:0097592	Fig. 1 C
PMID:15184401	PBO:0097593	Fig. 1 C
PMID:15184401	PBO:0097593	Fig. 1 C
PMID:15184401	PBO:0097801	fig 6F
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: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:15189983	PBO:0099906	fig 7
PMID:15189983	PBO:0099905	fig 7
PMID:15189983	PBO:0092140	Fig. 7 (lanes 1 and 2), we observed that both cgs1􏰀 and pka1􏰀 are transcriptionally induced by glucose starvation.
PMID:15189983	PBO:0095677	fig 6
PMID:15189983	PBO:0099903	fig 6
PMID:15189983	PBO:0093784	figure1
PMID:15189983	FYPO:0006141	figure1
PMID:15189983	PBO:0099904	table 3
PMID:15189983	PBO:0099904	table 3
PMID:15189983	FYPO:0006141	figure1
PMID:15189983	FYPO:0006141	figure1
PMID:15189983	FYPO:0001214	git2􏰇 strains themselves were severely defective for growth on YEA medium containing 1 M KCl (Fig. 1).
PMID:15189983	PBO:0093605	fig 6
PMID:15189983	PBO:0093605	fig 6
PMID:15189983	FYPO:0000245	fig 6
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:0093824	For cgs1-1 mu- tant 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 mu- tant 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 pres- ence of 2 M sorbitol, which is lethal to JSP12 (git2􏰇 spc1-12) and JSP29 (git2􏰇 wis1-29) cells. Therefore, the loss of adenyl- ate cyclase appears to confer a salt-sensitive, but not an os- motically sensitive, growth defect.
PMID:15189983	PBO:0099902	he FWP190 (git2􏰇) cells can grow in the pres- ence of 2 M sorbitol, which is lethal to JSP12 (git2􏰇 spc1-12) and JSP29 (git2􏰇 wis1-29) cells. Therefore, the loss of adenyl- ate cyclase appears to confer a salt-sensitive, but not an os- motically sensitive, growth defect.
PMID:15189983	PBO:0092140	Fig. 7 (lanes 1 and 2), we observed that both cgs1􏰀 and pka1􏰀 are transcriptionally induced by glucose starvation.
PMID:15189983	PBO:0099907	fig 7
PMID:15189983	PBO:0099908	fig 7
PMID:15189983	FYPO:0000961	he FWP190 (git2􏰇) cells can grow in the pres- ence of 2 M sorbitol, which is lethal to JSP12 (git2􏰇 spc1-12) and JSP29 (git2􏰇 wis1-29) cells. Therefore, the loss of adenyl- ate cyclase appears to confer a salt-sensitive, but not an os- motically sensitive, growth defect.
PMID:15189983	FYPO:0000961	he FWP190 (git2􏰇) cells can grow in the pres- ence of 2 M sorbitol, which is lethal to JSP12 (git2􏰇 spc1-12) and JSP29 (git2􏰇 wis1-29) cells. Therefore, the loss of adenyl- ate cyclase appears to confer a salt-sensitive, but not an os- motically sensitive, growth defect.
PMID:15189983	FYPO:0001490	figure2
PMID:15189983	FYPO:0001490	figure2
PMID:15189983	FYPO:0001490	figure2
PMID:15194812	PBO:0097127	Cdc45 reappears quickly after shift from restrictive to permissive temperature
PMID:15218150	PBO:0112683	Fig. 2A
PMID:15218150	GO:0141194	Fig. 3
PMID:15218150	GO:0141194	Fig. 3
PMID:15218150	PBO:0112700	Fig. 4B
PMID:15218150	PBO:0112699	Fig. 4B
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	FYPO:0005865	Fig. 2B
PMID:15218150	PBO:0112683	Fig. 2B
PMID:15218150	PBO:0112683	Fig. 2B
PMID:15218150	PBO:0112683	Fig. 2B
PMID:15218150	PBO:0112540	Fig. 2B
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:0097399	Fig. 2A
PMID:15218150	FYPO:0005865	Fig. 2A
PMID:15218150	PBO:0112683	Fig. 2A
PMID:15218150	PBO:0112683	Fig. 2A
PMID:15218150	PBO:0112683	Fig. 2A
PMID:15218150	PBO:0112540	Fig. 2A
PMID:15218150	PBO:0112540	Fig. 2A
PMID:15218150	PBO:0112698	Fig. 2A
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	FYPO:0002336	Fig. 2B
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. 2A
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	PBO:0097399	Fig. 1C
PMID:15218150	PBO:0097399	Fig. 1C
PMID:15218150	PBO:0097399	Fig. 1C
PMID:15218150	FYPO:0005865	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	PBO:0112540	Fig. 1C
PMID:15218150	PBO:0112540	Fig. 1C
PMID:15218150	PBO:0112540	Fig. 1C
PMID:15218150	PBO:0110928	Fig. 1C
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	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: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	PBO:0112698	Fig. 1B
PMID:15218150	PBO:0110928	Fig. 1B
PMID:15218150	PBO:0110928	Fig. 1B
PMID:15218150	PBO:0110928	Fig. 1B
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:0095651	Fig. 1C
PMID:15218150	PBO:0095651	Fig. 1C
PMID:15218150	PBO:0095651	Fig. 1C
PMID:15218150	FYPO:0002336	Fig. 1C
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. 1B
PMID:15218150	FYPO:0002336	Fig. 1B
PMID:15218150	FYPO:0002336	Fig. 1B
PMID:15218150	FYPO:0002336	Fig. 1B
PMID:15219990	GO:0051537	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:0004439	fig 1c
PMID:15249580	GO:0016314	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:15249580	PBO:0103033	mishapen
PMID:15249580	PBO:0109046	(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:15265986	PBO:0096461	in response to cytokinesis after mitosis checkpoint
PMID:15265986	PBO:0096462	in response to cytokinesis after mitosis checkpoint
PMID:15278909	PBO:0019995	during premeiotic DNA replication
PMID:15292231	PBO:0111986	Fig. 2B
PMID:15292231	PBO:0111992	Fig. 2B
PMID:15292231	PBO:0111977	Fig. 1B
PMID:15292231	PBO:0111976	Fig. 1 Similar to atf1 mutants, 
pcr1 showed reduced silencing, but the effect was weaker than that of 
atf1 or 
atf1
pcr1 (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:0111975	Fig. 1A In contrast, the atf1 deletion resulted in increased transcriptional repression at both centromeres and telomeres (Fig. 1A).
PMID:15292231	PBO:0111980	Fig. 2B
PMID:15292231	PBO:0111981	Fig. 2B
PMID:15292231	PBO:0111982	Fig. 2B
PMID:15292231	PBO:0111983	Fig. 2B
PMID:15292231	PBO:0111988	Fig. 2C
PMID:15292231	GO:0030466	RNAi-independent mechanism
PMID:15292231	GO:0030466	RNAi-independent mechanism
PMID:15292231	PBO:0111989	Fig. 6B
PMID:15292231	PBO:0111990	Fig. 6B
PMID:15292231	PBO:0111981	Fig. 6B
PMID:15292231	PBO:0111991	Fig. 6B
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	GO:0030466	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	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:0112047	ATF/CREB-binding
PMID:15292231	PBO:0112047	ATF/CREB-binding
PMID:15292231	PBO:0111978	Fig. 1
PMID:15292231	PBO:0111976	Fig. 3 Moreover, the ade6-off to ade6-on conversion in 
sty1 and 
wis1 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:0111976	Fig. 3
PMID:15292231	PBO:0111976	Fig. 3
PMID:15292231	PBO:0111979	Fig. 3
PMID:15292231	PBO:0111984	Fig. 2B
PMID:15292231	PBO:0111985	Fig. 2B
PMID:15292231	PBO:0111981	Fig. 2B
PMID:15292231	PBO:0111982	Fig. 2B
PMID:15292231	PBO:0111983	Fig. 2B
PMID:15292231	PBO:0111984	Fig. 2B
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:0111987	Fig. 2C
PMID:15292231	PBO:0111987	Fig. 2C
PMID:15297457	GO:0031573	would it be better/safer to annotate to parent (generic intra-S checkpoint term)?
PMID:15314153	FYPO:0002061	30 degrees
PMID:15314153	PBO:0093561	25 degrees
PMID:15316017	GO:0052658	activated_by(CHEBI:18420)| inhibited_by(CHEBI:29108)
PMID:15329725	FYPO:0002102	Fig. 1d and Fig. 1h
PMID:15329725	FYPO:0005429	Fig. 1h
PMID:15329725	FYPO:0005428	Fig. 1f)
PMID:1533272	PBO:0102314	Fig 4 Histone H1 used as substrate. Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid.
PMID:1533272	PBO:0104192	Fig 2. Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid.
PMID:1533272	PBO:0104193	Fig 5. Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid. Phosphorylation on threonine, but position(s) not determined.
PMID:1533272	PBO:0104194	Fig 7 Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid. Binds to cdc13 but this is reduced compared to binding of cdc2+ to cdc13
PMID:1533272	PBO:0097954	Fig 3. Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid.
PMID:1533272	FYPO:0001491	cdc13 expressed from own promoter on multi copy plasmid pUR18
PMID:15340008	PBO:0111724	Fig. 3A
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	FYPO:0002150	Fig. 5B
PMID:15340008	FYPO:0002150	Fig. 5B
PMID:15340008	PBO:0111726	Fig. 7
PMID:15340008	FYPO:0008162	Fig 1,3, & 4
PMID:15340008	FYPO:0003306	Fig. 1 C
PMID:15340008	PBO:0111722	Fig. 1
PMID:15340008	PBO:0111723	Fig. 1D &2
PMID:15340008	FYPO:0001761	Fig. 2
PMID:15340008	FYPO:0001513	Fig. 2
PMID:15340008	FYPO:0001513	Fig. 3
PMID:15340008	FYPO:0001513	Fig. 3
PMID:15340008	PBO:0020742	Fig. 3
PMID:15340008	PBO:0020742	Fig. 3
PMID:15340008	PBO:0102116	Fig. 3A
PMID:15340008	PBO:0102116	Fig. 3A
PMID:15340008	PBO:0111724	Fig. 3A
PMID:15359282	FYPO:0002150	Fig. 6A
PMID:15359282	GO:0005634	figure 2
PMID:15359282	PBO:0111734	Figure 3 (E2)
PMID:15359282	PBO:0111735	Figure 3 (E1, activating)
PMID:15359282	PBO:0093564	Fig. 4A
PMID:15359282	PBO:0111732	Fig. 3
PMID:15359282	PBO:0111731	Fig. 3A
PMID:15359282	PBO:0111730	Fig. 3A
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	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:0097301	Fig. 6A
PMID:15359282	PBO:0096188	Fig. 4C
PMID:15359282	PBO:0111733	Figure 3 (E3)
PMID:15359282	FYPO:0002687	Fig. 6B
PMID:15359282	FYPO:0002687	Fig. 6B
PMID:15359282	FYPO:0002687	Fig. 6B
PMID:15359282	PBO:0096189	Fig. 4C
PMID:15359282	PBO:0096191	Fig. 4C
PMID:15359282	PBO:0096191	Fig. 4C
PMID:15359282	PBO:0103455	Fig. 4B
PMID:15359282	PBO:0103456	Fig. 4B
PMID:15359282	PBO:0093562	Fig. 4A
PMID:15367656	PBO:0033073	no hydroxyurea
PMID:15369671	PBO:0101421	fig4
PMID:15369671	PBO:0096686	fig4
PMID:15369671	PBO:0101419	fig4
PMID:15371542	FYPO:0000964	fig 1a
PMID:15371542	FYPO:0000091	fig1
PMID:15371542	FYPO:0001840	fig1
PMID:15371542	FYPO:0001839	fig 1a
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	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	GO:0031508	Therefore, Chp1 protein was also involved in the production or processing of centromeric RNA transcripts, which might be linked to heterochromatin estab- lishment.
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: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: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: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: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 de- creased in the Dchp1 cells (Figures 2B and C, Dchp1)
PMID:15372076	PBO:0107146	In contrast, the centromeric localization of Swi6 or Chp2-13myc was specifically de- creased 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	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: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	PBO:0111009	fig 1
PMID:15372076	PBO:0107146	fig 1
PMID:15372076	PBO:0111013	fig 1
PMID:15372076	PBO:0111014	Figure 1
PMID:15372076	PBO:0111015	Figure 1
PMID:15372076	PBO:0111016	Figure 1
PMID:15372076	PBO:0111017	Figure 1
PMID:15372076	PBO:0111018	Figure 1
PMID:15372076	PBO:0111019	Figure 1
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	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	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	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	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 compar- able to that in Dclr4 (Figure 6A),
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 compar- able 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 compar- able to that in Dclr4 (Figure 6A),
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 compar- able to that in Dclr4 (Figure 6A),
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 compar- able 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 compar- able 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	FYPO:0003096	nexpectedly, the cen- tromeric H3-K9 methylation was also severely decreased in the Dchp1Dchp2 strain (Figure 5D, Dchp1Dchp2).
PMID:15372076	FYPO:0003097	Interestingly, we found that swi6þ dele- tion 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	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	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:15385632	GO:0005515	Figure 2A
PMID:15385632	GO:0005515	Figure 2A, Figure 2, D and E
PMID:15385632	PBO:0098863	Figure 6, A, D, and E
PMID:15385632	PBO:0098864	Figure 6, A, D, and E
PMID:15385632	FYPO:0006062	Figure 6, A, D, and E
PMID:15385632	PBO:0098862	Figure 6, A, D, and E
PMID:15385632	PBO:0098865	Figure 6, A, D, and E
PMID:15385632	PBO:0098864	Figure 6, A, D, and E
PMID:15385632	FYPO:0006062	Figure 6, A, D, and E
PMID:15385632	PBO:0098152	fig5
PMID:15385632	FYPO:0006062	fig 6
PMID:15385632	PBO:0098855	Figure 1H and Table 1
PMID:15385632	PBO:0098856	Figure 1I
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	GO:0005515	Figure 2, D and E
PMID:15385632	PBO:0098858	Figure 5 C
PMID:15385632	PBO:0098859	Figure 5
PMID:15385632	PBO:0098860	Figure 5
PMID:15385632	PBO:0098860	Figure 5
PMID:15385632	PBO:0098859	Figure 5
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 (Fig- ure 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	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:0005515	Figure 2A
PMID:15385632	GO:0005515	Figure 2A Figure 2, B and C)
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	FYPO:0001972	fig5
PMID:15385632	PBO:0098861	Figure 5
PMID:15385632	PBO:0098862	Figure 6, A, D, and E
PMID:15385632	FYPO:0006063	erexpression was the relative persistence of septin rings and the inhibition of mitotic progression, as determined by monitoring the for- mation of binucleates (Figure 8A). This result is consistent with our previous results, indicating that prolonged expres- sion 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 for- mation of binucleates (Figure 8A). This result is consistent with our previous results, indicating that prolonged expres- sion of Mid2p stabilizes septin ring structures and influences cell cycle progression (Tasto et al., 2003).
PMID:15385632	GO:0005515	Figure 2A
PMID:15385632	GO:0005515	Figure 2A,Figure 2, D and E
PMID:1538784	GO:0044732	throughout_cell_cycle
PMID:15470240	FYPO:0004256	fig2
PMID:15470240	FYPO:0002903	fig2
PMID:15470240	FYPO:0002903	fig2
PMID:15471884	GO:0003690	low affinity
PMID:15471884	GO:0070337	lower affinity than for Y-form DNA
PMID:15475954	PBO:0108389	Fig. 2B
PMID:15475954	GO:0031934	Fig. 1
PMID:15475954	GO:0140720	Fig. 1
PMID:15475954	GO:0005721	Fig. 1
PMID:15475954	GO:0031934	Fig. 1
PMID:15475954	GO:0031934	Fig. 1
PMID:15475954	GO:0140720	Fig. 1
PMID:15475954	GO:0140720	Fig. 1
PMID:15475954	GO:0005721	Fig. 1
PMID:15475954	GO:0005721	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:15475954	FYPO:0008011	Fig. 7C
PMID:15475954	FYPO:0008011	Fig. 7C
PMID:15475954	PBO:0108387	Fig. 7B
PMID:15475954	FYPO:0005865	Fig. 7B
PMID:15475954	PBO:0112901	Fig. 7B
PMID:15475954	PBO:0112900	Fig. 7B
PMID:15475954	FYPO:0008236	Fig. 7A
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	FYPO:0007336	Fig. 2C
PMID:15475954	PBO:0112683	Fig. 2C
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	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: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	PBO:0110928	Fig. 2B
PMID:15475954	FYPO:0005865	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	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:0002336	Fig. 2B
PMID:15485922	FYPO:0005402	same as taz1delta alone
PMID:15485922	FYPO:0005402	same as taz1delta alone
PMID:15504913	GO:0016460	Fig. 1
PMID:15504913	GO:0016460	Fig. 1
PMID:15504913	PBO:0112666	Fig. 3B and C
PMID:15504913	GO:0033275	Fig. 3
PMID:15504913	FYPO:0000161	Fig. 4A
PMID:15504913	FYPO:0000418	Fig. 4A
PMID:15504913	FYPO:0000161	Fig. 4B
PMID:15504913	FYPO:0008207	Table 1
PMID:15504913	PBO:0112668	Table 1
PMID:15504913	PBO:0112670	Table 1
PMID:15504913	PBO:0112670	Table 1
PMID:15504913	FYPO:0001367	Fig. 6C
PMID:15504913	PBO:0112668	Table 1
PMID:15504913	PBO:0112669	Table 1
PMID:15504913	FYPO:0000418	Fig. 4B
PMID:15504913	FYPO:0001252	Fig. 4A
PMID:15504913	FYPO:0001252	Fig. 4B
PMID:15504913	FYPO:0001252	Fig. 4C
PMID:15504913	PBO:0099316	Rng3p-GFP3 and Rng3p-YFP3 concentrated in contractile rings from anaphase B through constriction (Fig. 5).
PMID:15504913	FYPO:0008207	Table 1
PMID:15504913	FYPO:0008207	Table 1
PMID:15504913	PBO:0112669	Table 1
PMID:15504913	PBO:0107510	Rng3p-GFP3 and Rng3p-YFP3 concentrated in contractile rings from anaphase B through constriction (Fig. 5).
PMID:15504913	GO:0110085	Rng3p-GFP3 and Rng3p-YFP3 concentrated in contractile rings from anaphase B through constriction (Fig. 5).
PMID:15504913	FYPO:0000418	Fig. 4C
PMID:15504913	PBO:0112667	Fig. 6B
PMID:15504913	FYPO:0000161	Fig. 4C
PMID:15504913	FYPO:0001357	Fig. 6B
PMID:15504913	PBO:0112669	Table 1
PMID:15504913	PBO:0112669	Table 1
PMID:15504913	FYPO:0001357	Fig. 6B
PMID:15504913	PBO:0112669	Table 1
PMID:15504913	FYPO:0008207	Table 1
PMID:15504913	FYPO:0008207	Table 1
PMID:15504913	FYPO:0008207	Table 1
PMID:15507118	FYPO:0003763	inviable mononucleate aseptate vegetative cell with cell cycle arrest in mitotic G2 phase
PMID:15509783	PBO:0097814	table2
PMID:15509783	FYPO:0000229	Fig. 7D
PMID:15509783	FYPO:0004318	Fig. 7D
PMID:15509783	PBO:0097819	Fig. 7B
PMID:15509783	PBO:0097818	Fig. 7B
PMID:15509783	PBO:0097812	table2
PMID:15509783	PBO:0097811	table2
PMID:15509783	PBO:0023853	Figure 2A
PMID:15509783	FYPO:0000229	figure 1B
PMID:15509783	FYPO:0004318	figure 1B
PMID:15509783	PBO:0097815	table2
PMID:15509783	PBO:0097813	table2
PMID:15509783	PBO:0112055	checkpoint
PMID:15509865	FYPO:0004764	(Fig. 6B,C). in meiotic cells, shmooing cells
PMID:15509865	FYPO:0005814	(Fig. 6B,C). in meiotic cells, shmooing cells
PMID:15509865	FYPO:0005814	(Fig. 6B,C). in meiotic cells, shmooing cells
PMID:15509865	FYPO:0003066	data not shown , phenocopies ssm4 &dhc1
PMID:15509865	FYPO:0006130	meiosis
PMID:15509865	FYPO:0003179	(Table 2).leu1 and his2 loc, reduced 12 fold
PMID:15509865	FYPO:0004093	data not shown
PMID:15509865	FYPO:0000927	data not shown , phenocopies ssm4 &dhc1
PMID:15509865	FYPO:0006128	DURATION Fig. 2B,C
PMID:15509865	FYPO:0005383	Fig. 2B,C
PMID:15509865	GO:0005515	Fig. 3C).
PMID:15509865	FYPO:0000927	(Fig. 2A)
PMID:15509865	GO:0005515	Fig. 3B
PMID:15509865	GO:0005515	Fig. 3B
PMID:15509865	FYPO:0000927	(Fig. 2A)
PMID:15509865	PBO:0102573	(Table 3) assayed using pairing of his2 loci
PMID:15509865	FYPO:0000678	Add?
PMID:15509865	PBO:0033208	Table 3
PMID:15509865	FYPO:0004764	(Fig. 6B,C). in meiotic cells, shmooing cells
PMID:15509865	FYPO:0004731	(Fig. 6A-C), during meiotic prophase, shmooing
PMID:15509865	PBO:0033208	Table 3
PMID:15509865	PBO:0033208	Table 3
PMID:15525536	GO:0072479	only required when there are problems , possibly involved in repair of monoorientation
PMID:15537393	FYPO:0001190	Figure 3c
PMID:15537393	FYPO:0001082	Figure 3d
PMID:15537393	FYPO:0001082	Figure 3d
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	FYPO:0002196	figure 2f
PMID:15537393	PBO:0109439	figure 2f
PMID:15537393	PBO:0109438	figure 2f
PMID:15537393	PBO:0109437	figure 2e
PMID:15537393	PBO:0109436	figure 2e
PMID:15537393	PBO:0109435	figure 2e
PMID:15537393	PBO:0109434	figure 2e
PMID:15537393	PBO:0096587	figure 2e
PMID:15537393	FYPO:0001355	figure 2d
PMID:15537393	FYPO:0002061	figure 2d
PMID:15537537	PBO:0113769	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:0113768	Fig. 2G
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:15537537	FYPO:0002360	Fig. S1
PMID:15537537	FYPO:0002336	Fig. S1
PMID:15537537	PBO:0112663	Fig. 2G
PMID:15537537	GO:0031934	Fig. 2F
PMID:15537537	GO:0005634	Fig. 2B
PMID:15537537	PBO:0112927	Fig. 1A
PMID:15537537	PBO:0112927	Fig. 1A
PMID:15546915	FYPO:0002150	Fig. 3A
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: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	(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:0001123	Figure 3B indicates a bypass of cytokinesis checkpoint
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:0102105	Figure 5 These results indicate that Rgf3p acts as a specific Rho1p activator in S. pombe.
PMID:15546915	PBO:0101163	replace with cytokinetic phase
PMID:15546915	FYPO:0000647	(Fig. 1A
PMID:15546915	FYPO:0000951	Figure 3 C shrunken cell
PMID:15546915	FYPO:0000951	Figure 3 C shrunken cell
PMID:15546915	FYPO:0004892	Figure 4 GI Rho1 OEX rescues echinocandin sensitivity
PMID:15546915	FYPO:0002061	figure4
PMID:15546915	FYPO:0002159	(Fig. 1A
PMID:15548596	FYPO:0002134	three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site
PMID:15550243	PBO:0112168	figure 1
PMID:15550243	FYPO:0004217	Fig. 1
PMID:15550243	PBO:0112159	Fig. 1
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: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	PBO:0093613	Fig. 3
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:0112191	Fig. 4D
PMID:15550243	PBO:0093613	Fig. 3
PMID:15550243	PBO:0105171	Fig. 3
PMID:15550243	PBO:0105171	Fig. 3
PMID:15550243	PBO:0112167	figure 1
PMID:15550243	PBO:0112169	Fig. 1, 3 and 4
PMID:15550243	PBO:0112170	Fig. 1, 3 and 4
PMID:15550243	GO:0010468	Fig. 2B
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 g/ml) or temperatures (18C–36C) (Figure 2D
PMID:15550243	PBO:0093613	Fig. 3
PMID:15550243	PBO:0105171	Fig. 3
PMID:15550243	PBO:0105171	Fig. 3
PMID:15550243	PBO:0112163	Fig. 4D
PMID:15550243	PBO:0112163	Fig. 4D
PMID:15550243	PBO:0112163	Fig. 4D
PMID:15550243	GO:0042393	Fig. 1A
PMID:15550243	FYPO:0004126	Fig. 1
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	PBO:0112161	Fig. 4D
PMID:15550243	PBO:0112163	Fig. 4D
PMID:15550243	PBO:0112161	Fig. 4D
PMID:15550243	PBO:0112162	Fig. 5
PMID:15550243	PBO:0112161	Fig. 5B
PMID:15550243	PBO:0112163	Fig. 5B Clearly, this is not the case, as the sensitivity of the double crb2T215A-set9 mutant is much greater than either single mutant alone and equal to deletion of crb2 (Figure 5B).
PMID:15550243	PBO:0097793	Fig. 5
PMID:15550243	PBO:0097793	Fig. 5 Further, the double mutant displays a checkpoint defect equivalent to that of the crb2 mutant (Figure 5C).
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	PBO:0112158	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 set9 cells (Figure 1E).
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: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:0112165	Fig. 1, 3 and 4
PMID:15550243	PBO:0112176	figure 1
PMID:15572668	PBO:0112620	Table 2
PMID:15572668	PBO:0112617	Table 2
PMID:15572668	PBO:0112618	Table 2
PMID:15572668	PBO:0112619	Table 2
PMID:15572668	PBO:0112620	Table 2
PMID:15572668	PBO:0112620	Table 2
PMID:15572668	PBO:0112620	Table 2
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: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:0112637	Fig. 4A
PMID:15572668	PBO:0112631	Fig. 4A
PMID:15572668	PBO:0112636	Fig. 4A
PMID:15572668	PBO:0112635	Fig. 4A
PMID:15572668	PBO:0112634	Fig. 2D
PMID:15572668	PBO:0112633	Fig. 2D
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: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 con- centrated 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:0112627	Table 2
PMID:15572668	PBO:0112626	Table 2
PMID:15572668	PBO:0112625	Table 2
PMID:15572668	PBO:0112624	Table 2
PMID:15572668	PBO:0112623	Table 2
PMID:15572668	PBO:0112620	Table 2
PMID:15572668	PBO:0112622	Table 2
PMID:15572668	PBO:0112621	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:0112620	Table 2
PMID:15572668	PBO:0112620	Table 2
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: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:15607976	FYPO:0008011	Fig. 3D
PMID:15607976	FYPO:0008011	Fig. 3D
PMID:15607976	PBO:0112890	Fig. 3C
PMID:15607976	PBO:0112891	Fig. 3C
PMID:15607976	PBO:0112892	Fig. 3C
PMID:15607976	PBO:0112892	Fig. 3C
PMID:15607976	FYPO:0008011	Fig. 3D
PMID:15607976	FYPO:0008011	Fig. 3D
PMID:15607976	PBO:0112889	Fig. 2C and D
PMID:15607976	PBO:0112889	Fig. 2C and D
PMID:15607976	PBO:0098583	Fig. 2B
PMID:15607976	PBO:0098583	Fig. 2B
PMID:15607976	PBO:0098583	Fig. 2B
PMID:15607976	PBO:0096189	Fig. 2A
PMID:15607976	PBO:0096189	Fig. 2A
PMID:15607976	FYPO:0008235	Table 1
PMID:15607976	PBO:0096189	Fig. 6F
PMID:15607976	FYPO:0008235	Table 1
PMID:15607976	FYPO:0008235	Table 1
PMID:15607976	PBO:0112888	Table 1
PMID:15607976	PBO:0112888	Table 1
PMID:15607976	PBO:0112893	Fig. 6E
PMID:15607976	PBO:0112893	Fig. 6C and E
PMID:15607976	PBO:0096189	Fig. 6F
PMID:15607976	PBO:0096189	Fig. 6F
PMID:15607976	PBO:0110436	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:15615784	FYPO:0003000	assayed in vitro
PMID:15615784	FYPO:0003000	assayed in vitro
PMID:15615784	GO:0007163	based just on this paper, candidate for involved_in_or_regulates qualifier
PMID:15615784	GO:0007163	based just on this paper, candidate for involved_in_or_regulates qualifier
PMID:15615848	PBO:0104876	(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, rdp1􏰄, or dcr1􏰄 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, rdp1􏰄, or dcr1􏰄 cells
PMID:15615848	PBO:0104875	(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:0096476	(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	GO:0140720	Fig. 1A
PMID:15615848	GO:0031934	Fig. 1A CenH
PMID:15615848	GO:0005721	Fig. 1A 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	PBO:0104870	Fig. 1B
PMID:15615848	PBO:0108530	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	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:0104873	(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:0093562	hypersensitive to TBZ, indicating that chromosome segregation is not robust in these mutant cells (Fig. 3A).
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	FYPO:0008009	(Fig. 3 C 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 telo- meres to the nuclear periphery was unaffected
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 telo- meres to the nuclear periphery was unaffected (Fig. 3 C and D)
PMID:15615848	PBO:0110436	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: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 telo- meres to the nuclear periphery was unaffected (Fig. 3 C and D)
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, rdp1􏰄, or dcr1􏰄 cells
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 non- essential for cell growth under the conditions employed.
PMID:15616156	GO:0005730	Figure 2A
PMID:15616156	GO:0005674	e, we found that more Tfg3-H formed complexes with GST–Tfg3 (Figure 1D), con- firming 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	GO:0005654	Figure 2A
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	GO:0005737	Figure 2A
PMID:15625190	PBO:0100071	three-hybrid assay; also binds exogenous ESEs
PMID:15632064	FYPO:0007326	fig 1 The data sug- gest that the mutants are not deficient in termination effi- ciency.
PMID:15632064	PBO:0108882	trna chaperone
PMID:15632064	FYPO:0007326	fig 1 The data sug- gest that the mutants are not deficient in termination effi- ciency.
PMID:15632064	FYPO:0007008	fig 1 The data sug- gest that the mutants are not deficient in termination effi- ciency.
PMID:15632064	GO:0005666	Mutated Rpc11p subunits associate with Pol III and impair its RNA 3􏰌 cleavage activity.
PMID:15643072	FYPO:0001250	assayed in strain with cdc10-129 to synchronize
PMID:15647375	FYPO:0000252	fig 4
PMID:15647375	FYPO:0000229	fig 4
PMID:15647375	FYPO:0002303	fig4
PMID:15647375	PBO:0020141	GO:0051329 = mitotic interpase
PMID:15647375	PBO:0020565	GO:0000093 = mitotic telophase
PMID:15654094	GO:0042138	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:15654094	GO:0042138	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:15654094	GO:0042138	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:15654094	GO:0007131	assayed using 160-bp palindromic sequence inserted into ade6 locus
PMID:15665379	PBO:0103508	fig 2
PMID:15665379	PBO:0103509	fig 2
PMID:15665379	PBO:0103509	fig 2
PMID:15665379	PBO:0103510	fig 3b
PMID:15671491	FYPO:0003933	assayed using reporter based on S. cerevisiae MFA2
PMID:15671491	FYPO:0003934	assayed using reporter based on S. cerevisiae MFA2
PMID:15671491	FYPO:0003932	assayed using reporter based on S. cerevisiae MFA2
PMID:15671491	FYPO:0003933	assayed using reporter based on S. cerevisiae MFA2
PMID:15671491	FYPO:0003932	assayed using reporter based on S. cerevisiae MFA2
PMID:15689489	FYPO:0004395	Fig. 6
PMID:15689489	FYPO:0005722	Fig. 6
PMID:15689489	FYPO:0007304	Fig. 6
PMID:15689489	PBO:0106123	In metaphase the difference kinds of microtubules cannot be distinguished, but they can be distinguished during anaphase B
PMID:15689489	FYPO:0003481	Fig. 1
PMID:15689489	PBO:0106124	Fig. 1
PMID:15689489	PBO:0106125	Fig. 1
PMID:15689489	FYPO:0003840	Fig. 1
PMID:15689489	FYPO:0002401	Fig. 2
PMID:15689489	FYPO:0005558	Fig. 2
PMID:15689489	FYPO:0003302	Fig. 5
PMID:15689489	FYPO:0007981	Fig. 6
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: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:15710398	FYPO:0000492	Fig. 4B),
PMID:15710398	FYPO:0000492	Fig. 4B),
PMID:15710398	FYPO:0003807	the mitochondrial network appeared as highly interconnected tubules forming net-like structures (Fig. 5A).
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: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:0008108	In the Dmsp1Ddnm1 strain, mtDNA depletion (Fig. 5F) and lethality (not shown) did not occur
PMID:15710398	GO:0008053	MEMBRANE
PMID:15710398	PBO:0109717	In Msp1p overexpressing cells, more than 85% of the cells had an aggregated filamentous mitochondrial network.
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:0002061	while cells that expressed cytosolic Msp1pDMIS or CAT died.
PMID:15710398	FYPO:0008108	In the Dmsp1Ddnm1 strain, mtDNA depletion (Fig. 5F) and lethality (not shown) did not occur
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:0002061	while cells that expressed cytosolic Msp1pDMIS or CAT died.
PMID:15710398	FYPO:0003896	while cells that expressed cytosolic Msp1pDMIS or CAT died.
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: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: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: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:15716270	FYPO:0003699	18S rRNA position 1204
PMID:15716270	FYPO:0003699	25S rRNA positions 2216, 2220, 2351
PMID:15716270	FYPO:0003699	25S rRNA position 3017
PMID:15716270	FYPO:0003699	25S rRNA position 1074
PMID:15716270	FYPO:0003699	25S rRNA position 3069
PMID:15716270	FYPO:0003699	25S rRNA positions 2298, 2401
PMID:15716270	FYPO:0003699	25S rRNA position 1723
PMID:15716270	FYPO:0003699	25S rRNA position 1084
PMID:15716270	FYPO:0003699	18S rRNA position 1307
PMID:15716270	FYPO:0003699	18S rRNA positions 208, 2341
PMID:15728720	FYPO:0000209	increased centromere spindle pole body detachment during meiotic prophase fission-yeast-phenotype/2055/
PMID:15731009	PBO:0107072	same as orb3-167 alone
PMID:15731009	PBO:0107072	same as orb3-167 alone
PMID:15731009	GO:0007163	based just on this paper, candidate for involved_in_or_regulates qualifier
PMID:15731009	GO:0030950	based just on this paper, candidate for involved_in_or_regulates qualifier
PMID:15731009	GO:0004672	assayed using casein; doesn't quite rule out tyrosine phosphorylation
PMID:15731009	GO:0030479	dependent on F-actin (asayed using Latrunculin A); independent of microtubules (assayed using MBC)
PMID:15731009	GO:0110085	dependent on F-actin (asayed using Latrunculin A); independent of microtubules (assayed using MBC)
PMID:15743828	PBO:0111623	n contrast, cells lacking the RRM domain of Chp1 (RRMchp1-6xmyc) exhibited no loss of Chp1 function.
PMID:15743828	PBO:0111624	In contrast, CDchp1-6xmyc exhibited a diffuse faint spotty staining pattern throughout the nucleoplasm and was not as- sociated 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 centro- meric sequences.
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:0111626	Surprisingly, however, other foci of Chp1-6xmyc and Tas3- 13xmyc persisted in ago1 cells. Similar results were obtained in cells from which Dicer was deleted (Fig. 5A and B, right panels).
PMID:15743828	PBO:0110927	Surprisingly, however, other foci of Chp1-6xmyc and Tas3- 13xmyc persisted in ago1 cells. Similar results were obtained in cells from which Dicer was deleted (Fig. 5A and B, right panels).
PMID:15743828	PBO:0111626	Surprisingly, however, other foci of Chp1-6xmyc and Tas3- 13xmyc persisted in ago1 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	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	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 ago1 cells. Similar results were obtained in cells from which Dicer was deleted (Fig. 5A and B, right panels).
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:0111622	n contrast, cells lacking the RRM domain of Chp1 (RRMchp1-6xmyc) exhibited no loss of Chp1 function.
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:0111627	Tas3-13xmyc protein was essentially lost in chp1 cells, whereas it was present at normal levels in the ago1 cells (Fig. 6B) To address whether loss of Tas3-13xmyc protein in chp1 cells was due to suppression of tas3-13xmyc
 transcription, we performed quantitative RT-PCR using RNA prepared from wild-type, chp1, and ago1 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 post- transcriptional effect.
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 nucle- olus (Fig. 6A)
PMID:15743828	PBO:0111621	Importantly, cells lacking only the Chp1 chromodo- main (CDchp1-6xmyc) behaved similar to the chp1 null strain, with elevated transcription of the centromeric marker gene (Fig. 2C) and numerous mitotic chromosome segregation de- fects (Fig. 2D)
PMID:15743828	FYPO:0000141	Importantly, cells lacking only the Chp1 chromodo- main (CDchp1-6xmyc) behaved similar to the chp1 null strain, with elevated transcription of the centromeric marker gene (Fig. 2C) and numerous mitotic chromosome segregation de- fects (Fig. 2D)
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:15743909	PBO:0095173	dependent on F-actin (assayed using Latrunculin A)
PMID:15743909	FYPO:0003066	homozygous cross
PMID:15743909	FYPO:0003066	homozygous cross
PMID:15743909	FYPO:0003066	homozygous cross
PMID:15743909	PBO:0095174	dependent on F-actin (assayed using Latrunculin A)
PMID:15772152	FYPO:0000899	normal length
PMID:15797383	GO:0032936	fig1
PMID:15797383	PBO:0095815	fig2
PMID:15797383	GO:0032936	fig1
PMID:15797383	GO:0032933	fig2,3,4
PMID:15797383	GO:0032933	fig2,5
PMID:15797383	PBO:0095816	fig2 ln 11-12
PMID:15797925	FYPO:0004121	assayed using NLS-LacI-GFP construct
PMID:15797925	GO:0034399	punctate, similar to nuclear pore components; localization not dependent on microtubules
PMID:15800064	PBO:0106051	fig 5 a
PMID:15800064	PBO:0106051	fig 5 a
PMID:15800064	PBO:0106052	fig 5 b
PMID:15800064	FYPO:0003171	fig 6 B
PMID:15800064	FYPO:0002026	fig 6 c
PMID:15800064	PBO:0037745	figure 3A
PMID:15800064	GO:0005515	fig 1 C
PMID:15800064	PBO:0037148	fig 2 a,c 2D
PMID:15800064	FYPO:0004611	figure 3A
PMID:15800064	FYPO:0004624	figure 3A c
PMID:15800064	FYPO:0003126	figure 3A c
PMID:15800064	FYPO:0005688	Figure 3A
PMID:15800064	PBO:0106048	Figure 3 fypo/issues/2830
PMID:15800064	PBO:0106049	Figure 3 fypo/issues/2830
PMID:15800064	PBO:0106050	Figure 3 B fypo/issues/2830
PMID:15800064	FYPO:0004766	Figure 4
PMID:15800064	PBO:0022298	fig 2 a 2D
PMID:15800064	PBO:0023023	fig 2 a,c 2D
PMID:15800064	PBO:0037743	fig 2 a 2D
PMID:15800064	PBO:0037744	figure 3A
PMID:15809031	PBO:0097169	inferred from direct physical interactions between tea4,tea1 and tea4,for3, plus tea4delta phenotype
PMID:15827087	FYPO:0003150	Fig2A,B
PMID:15827087	FYPO:0002058	data not shown
PMID:15827087	PBO:0103538	Fig1B This distribution is only seen in cells with a rod shaped appearance
PMID:15827087	PBO:0037444	Table 2
PMID:15827087	PBO:0037443	Table 2 This distribution is only seen in cells with a rod shaped appearance
PMID:15827087	PBO:0019098	Fig4D
PMID:15827087	PBO:0037449	data for cdc25-22 block not shown but see also Fig4A
PMID:15827087	PBO:0103540	Fig 4B
PMID:15827087	PBO:0103541	data not shown, same as Fig 4C
PMID:15827087	PBO:0103541	Fig 4C
PMID:15827087	PBO:0018339	Fig4B
PMID:15827087	PBO:0103536	Table 2 This distribution is only seen in cells with a rod shaped appearance
PMID:15827087	PBO:0103535	Table 2 This distribution is only seen in cells with a rod shaped appearance
PMID:15827087	PBO:0037440	Fig1 Table 2
PMID:15827087	PBO:0037439	Fig1C Table 2
PMID:15827087	FYPO:0000021	Fig1
PMID:15827087	FYPO:0000224	Fig1. They describe cells as swollen in their middle region
PMID:15827087	FYPO:0000015	Fig1 permissive temperature is 25°C
PMID:15827087	FYPO:0001355	data not shown, permissive temperature 25°C
PMID:15827087	PBO:0094949	data not shown Non permissive temperature is 32°C and above
PMID:15827087	PBO:0103543	Fig2A and data not shown
PMID:15827087	FYPO:0001120	Fig1. They describe cells as swollen in their middle region
PMID:15827087	FYPO:0002058	data not shown
PMID:15827087	PBO:0099011	Fig3A,B Deletion of the talin domain suppresses the premature activation of bipolar growth in a cdc10 mutant in latA
PMID:15827087	FYPO:0003150	Fig2A and data not shown
PMID:15827087	FYPO:0000426	data not shown
PMID:15827087	PBO:0103539	Fig2A,B
PMID:15827087	PBO:0037448	Fig2D
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:15837798	FYPO:0004700	mto2 deletion strain, which yielded viable but slightly bent cells (Fig. 3 A)
PMID:15857958	FYPO:0000729	Fig. 3
PMID:15857958	PBO:0018346	Fig. 4
PMID:15857958	PBO:0023726	Fig. 4
PMID:15857958	FYPO:0002061	Fig. 5
PMID:15857958	FYPO:0002061	Fig. 5
PMID:15857958	FYPO:0004087	Fig. 2
PMID:15857958	FYPO:0000729	Fig. 3
PMID:15857958	FYPO:0002061	Fig. 7
PMID:15857958	PBO:0099464	Fig. 3 - mad2 signal.
PMID:15857958	FYPO:0002060	Fig. 5
PMID:15857958	FYPO:0006917	Fig. 3
PMID:15857958	PBO:0099462	Fig. 2
PMID:15857958	PBO:0099463	Fig. 2
PMID:15857958	FYPO:0002060	Fig. 5
PMID:15857958	FYPO:0000324	Fig. 2 and Fig. 3 (cdc13 signal)
PMID:15857958	FYPO:0006917	Fig. 3
PMID:15857958	PBO:0099477	Fig. 7
PMID:15857958	FYPO:0002061	Fig. 7
PMID:15857958	FYPO:0002061	Fig. 7
PMID:15857958	PBO:0099476	Fig. 7
PMID:15857958	PBO:0099475	Fig. 7
PMID:15857958	PBO:0099474	Fig. 6
PMID:15857958	PBO:0099473	Fig. 6
PMID:15857958	PBO:0099472	Fig. 7
PMID:15857958	PBO:0099471	Fig. 5
PMID:15857958	PBO:0099470	Fig. 5
PMID:15857958	PBO:0099470	Fig. 5
PMID:15857958	FYPO:0002060	Fig. 5
PMID:15857958	FYPO:0001355	Fig. 5
PMID:15857958	PBO:0099465	Fig. 5
PMID:15857958	PBO:0099465	Fig. 5
PMID:15857958	PBO:0037128	Fig. 5
PMID:15857958	PBO:0037128	Fig. 5
PMID:15857958	PBO:0099466	Fig. 5
PMID:15857958	PBO:0099466	Fig. 5
PMID:15857958	PBO:0099467	Fig. 5
PMID:15857958	PBO:0099467	Fig. 5
PMID:15857958	PBO:0099468	Fig. 5
PMID:15857958	PBO:0099469	Fig. 5
PMID:1588914	PBO:0093712	multicopy pwis4 does not suppress cdc2-3w phenotype
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	PBO:0097762	multicopy pwis2 does not suppress cdr1-34 phenotype
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: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: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: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	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: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:0100670	the wis2 gene on a multi copy plasmid pwis2 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
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:0093712	multicopy pwis2 does not suppress cdc2-1w phenotype
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	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	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	FYPO:0002061	multicopy pwis4 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 pwis3 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 pwis2 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 pwis1 does not suppress cdc13-117 ts phenotype
PMID:1588914	PBO:0019154	multicopy pwis1 does not suppress cdc2-33 ts phenotype
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	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	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: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 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	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: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:0008062	Figure 3 There was a 4- fold reduction of Cnp1 at cnt2 in hrp1D cells,
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	PBO:0033885	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:0007313	Figure 3
PMID:15908586	FYPO:0007314	Figure 3
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	PBO:0105928	Figure 2
PMID:15908586	PBO:0033665	Figure 2
PMID:15908586	PBO:0105931	Figure 3 There was a 4- fold reduction of Cnp1 at cnt2 in hrp1D cells,
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	FYPO:0004331	Figure 1
PMID:15908586	FYPO:0003412	Figure 1
PMID:15908586	FYPO:0004542	Figure 1
PMID:15908586	FYPO:0002827	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: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: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: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	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:15915339	PBO:0093629	more sensitive than either single mutant
PMID:15915339	PBO:0093580	more sensitive than either single mutant
PMID:15915339	PBO:0093616	more sensitive than either single mutant
PMID:15915339	PBO:0093587	more sensitive than either single mutant
PMID:15920625	GO:0036374	Proxy assay for hydrolase function used and IMP evidence for catalytic activity
PMID:15925945	PBO:0096148	assayed using AlF4- to mimic GTP-bound Gpa2
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	MOD:01148	These results indicate that Etd1p is polyubiquitinated and degraded through the ubiquitin-dependent 26S-proteasome pathway.
PMID:15933715	GO:0031028	suggesting that Etd1p is somehow necessary to maintain Spg1p activity during anaphase until the completion of cytokinesis
PMID:15933715	PBO:0107086	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	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	FYPO:0003838	However, in etd1-1 mutant cells, the medial ring marked with Cdc15p-GFP seems to fail constriction. To bette
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. (the anchor is using 2022 knowledge)
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: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: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: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: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	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	FYPO:0001493	Figure 1A and B).
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: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: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	FYPO:0007398	DNS
PMID:15936270	FYPO:0001357	DNS
PMID:15936270	PBO:0037676	(p;enetrance for m 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:0001018	2c Δwsh3 cells were found to grow exclusively in a monopolar fashion.
PMID:15937127	GO:0034399	Figure 3F-3
PMID:15937127	PBO:0107950	fig 5B
PMID:15937127	PBO:0107944	fig2
PMID:15937127	PBO:0100663	fig 4D
PMID:15937127	PBO:0107140	fig 4D
PMID:15937127	PBO:0100894	fig 4D
PMID:15937127	PBO:0107949	fig 4D
PMID:15937127	GO:0034399	Figure 3F-3
PMID:15937127	FYPO:0006338	DNA at the tips, telophase delay
PMID:15937127	GO:0005634	Figure 3F-3
PMID:15937127	GO:0005634	Figure 3F-3
PMID:15937127	FYPO:0002060	fig3
PMID:15937127	GO:0006606	fig2
PMID:15937127	GO:0006606	fig2
PMID:15937127	PBO:0107945	fig2
PMID:15937127	PBO:0107944	fig2
PMID:15937127	PBO:0107950	fig 5B
PMID:15937127	FYPO:0001355	fig3
PMID:15937127	PBO:0107946	fig3 B-2 (1.1% WT)
PMID:15937127	PBO:0107947	fig3 B-2 (never seen in WT)
PMID:15937127	FYPO:0003165	fig 3C
PMID:15941470	FYPO:0002061	Tev protease present; Cdc23 truncated
PMID:15941470	PBO:0101305	Tev protease present; Cdc23 truncated; Cdc23 C-terminal fragment not retained in nucleus
PMID:15941470	FYPO:0001430	Tev protease present; Cdc23 truncated; N starvation/recovery synchronizes cells
PMID:15941470	FYPO:0000611	Tev protease present; Cdc23 truncated; cells not synchronized
PMID:15941470	FYPO:0002060	Tev protease present; Cdc23 truncated
PMID:15941470	PBO:0101304	Tev protease present; Cdc23 truncated; Cdc23 C-terminal fragment not retained in nucleus
PMID:15957215	GO:0006265	from the catenated plasmid experiment (and failure to separate sisters)
PMID:15992541	PBO:0105631	promoter repressed
PMID:15992541	PBO:0105630	thiamine absent; expression level lower than with endogenous promoter but higher than when repressed
PMID:16055437	PBO:0109312	figure 1a
PMID:16079916	FYPO:0007632	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:0007632	protein-coding genes and intergenic regions
PMID:16079916	FYPO:0007631	protein-coding genes and intergenic regions
PMID:16079916	FYPO:0005309	protein-coding genes and intergenic regions
PMID:16079916	FYPO:0005310	protein-coding genes and intergenic regions
PMID:16079916	FYPO:0000892	protein-coding genes and intergenic regions
PMID:16079916	FYPO:0005310	protein-coding genes and intergenic regions
PMID:16079916	FYPO:0007632	assayed in intergenic regions
PMID:16079916	FYPO:0007631	assayed in intergenic regions
PMID:16079916	FYPO:0005309	assayed in intergenic regions
PMID:16079916	FYPO:0005310	assayed in intergenic regions
PMID:16079916	FYPO:0000892	protein-coding genes and intergenic regions
PMID:16079916	FYPO:0007631	protein-coding genes and intergenic regions
PMID:16079916	FYPO:0005309	protein-coding genes and intergenic regions
PMID:16079916	FYPO:0005310	protein-coding genes and intergenic regions
PMID:16079916	FYPO:0000892	protein-coding genes and intergenic regions
PMID:16085489	GO:0044878	clp1 cytoplasmic localization not maintained during cytokinetic stress. cdc7 localization to SPB not maintained during cytokinetic stress
PMID:16087707	GO:0030479	dependent on F-actin (assayed using Latrunculin A)
PMID:16087707	GO:0000147	also from timing of localization to patches
PMID:16087707	GO:0030479	dependent on F-actin (assayed using Latrunculin A)
PMID:16087707	GO:0071933	specific Arp2/3 complex subunit(s) not identified; authors use Myo1 tail as representative of whole protein
PMID:16087707	GO:0000147	also from timing of localization to patches
PMID:16087707	GO:0000147	also from synthetic lethality with myo1, timing of localization to patches, and vrp1 mutant phenotype
PMID:16087707	GO:0030479	dependent on F-actin (assayed using Latrunculin A)
PMID:16087707	GO:0000147	also from timing of localization to patches
PMID:16087707	GO:0071933	specific Arp2/3 complex subunit(s) not identified; authors use Myo1 tail as representative of whole protein
PMID:16087749	PBO:0111679	As shown in Fig. ​Fig.3D,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	FYPO:0001355	et2 cells grew nor- mally 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:0002060	et2 cells grew nor- mally 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:0002919	As shown in Fig. 4A, dele- tion of set2
 resulted in a complete abolishment of K36 meth- ylation (mono-, di-, and trimethylation), but not K4 methyl- ation or H3 K9 acetylation, in bulk histones
PMID:16087749	PBO:0111677	The results revealed that histone H3 was the only histone methylated (Fig. 3B).
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.3D,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: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.3D,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.3D,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:0018346	both SPBs in early mitosis
PMID:16096637	PBO:0102313	Pmo25 formed a complex with Nak1 and was required for both the localization and kinase activity of Nak1.
PMID:16111942	GO:0030989	arious exp, and ectoptic mitotic exprression
PMID:16111942	PBO:0018718	Fig 1A appeared at theSPB upon conjugation of haploid cells, persisted untilthe onset of meiosis I, and disappeared thereafter
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	GO:0032118	arious exp, and ectoptic mitotic exprression
PMID:16120966	GO:0003887	distributive; substrate preference: small gaps with a 5′-phosphate group
PMID:16120966	GO:0003899	can incorporate NTPs or dNTPs; changed from primase activity because not tested with unprimed template
PMID:16127433	PBO:0112655	Fig. 5A
PMID:16127433	PBO:0112654	Fig. 5A
PMID:16127433	FYPO:0001357	Fig. S3
PMID:16127433	FYPO:0001357	Fig. S3
PMID:16127433	FYPO:0007334	Fig. S3
PMID:16127433	PBO:0094283	Fig. S3
PMID:16127433	PBO:0094283	Fig. S3
PMID:16127433	FYPO:0007336	Fig. 2A
PMID:16127433	PBO:0112520	Fig. 5C
PMID:16127433	PBO:0098773	Fig. 2B
PMID:16127433	PBO:0112644	Fig. 2B
PMID:16127433	PBO:0094681	Fig. 2A
PMID:16127433	PBO:0112656	Fig. 5C
PMID:16127433	PBO:0112650	Fig. 2B
PMID:16127433	FYPO:0004745	Fig. 4B
PMID:16127433	FYPO:0004745	Fig. 4B
PMID:16127433	FYPO:0007334	Fig. 4A
PMID:16127433	PBO:0093561	Fig. 4A
PMID:16127433	FYPO:0003412	Fig. S3
PMID:16127433	PBO:0093560	Fig. S3
PMID:16127433	FYPO:0001357	Fig. S3
PMID:16127433	PBO:0110865	Fig. 5D
PMID:16127433	PBO:0112817	Fig. 4B
PMID:16127433	FYPO:0000468	Fig. 3C
PMID:16127433	FYPO:0001861	Fig. 3B
PMID:16127433	PBO:0095057	Fig. 3A
PMID:16127433	PBO:0112651	Fig. 2B
PMID:16127433	FYPO:0002331	Fig. 4B
PMID:16127433	FYPO:0002331	Fig. 4B
PMID:16127433	PBO:0112653	Fig. 4B
PMID:16127433	PBO:0112653	Fig. 4B
PMID:16127433	PBO:0112648	Fig. 2B
PMID:16127433	PBO:0112649	Fig. 2B
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: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:16141239	FYPO:0006341	endocytosis restricted to cell end
PMID:16141239	FYPO:0000426	Fig. 5A,B
PMID:16141239	FYPO:0000422	Fig. 5A,B
PMID:16141239	FYPO:0000034	endocytosis restricted to cell end
PMID:16141239	FYPO:0006341	endocytosis restricted to cell end
PMID:16141239	FYPO:0000422	Fig. 5A,B
PMID:16141239	FYPO:0006341	endocytosis restricted to cell end
PMID:16157682	PBO:0098583	Fig. 7
PMID:16157682	FYPO:0005063	Fig. 8C
PMID:16157682	FYPO:0005063	Fig. 8C
PMID:16157682	FYPO:0005063	Fig. 8C
PMID:16157682	FYPO:0006112	Fig. 8B
PMID:16157682	PBO:0112644	Fig. 8B
PMID:16157682	PBO:0112644	Fig. 8B
PMID:16157682	PBO:0094681	Fig. 7
PMID:16157682	PBO:0094681	Fig. 7
PMID:16157682	PBO:0094681	Fig. 7
PMID:16157682	PBO:0098583	Fig. 7
PMID:16157682	PBO:0098583	Fig. 7
PMID:16157682	FYPO:0002336	Fig. 7
PMID:16157682	PBO:0095653	Fig. 7
PMID:16157682	PBO:0095651	Fig. 7
PMID:16157682	PBO:0112643	Fig. 5
PMID:16157682	PBO:0112643	Fig. 5
PMID:16157682	PBO:0103456	Table 2 and Fig. 4
PMID:16157682	PBO:0103456	Table 2 and Fig. 4
PMID:16157682	FYPO:0007336	Fig. 2C
PMID:16157682	FYPO:0007336	Fig. 2C
PMID:16157682	PBO:0097950	Fig. 2B
PMID:16157682	PBO:0097950	Fig. 2B
PMID:16157682	PBO:0098583	Fig. 2A
PMID:16157682	PBO:0098583	Fig. 2A
PMID:16157682	FYPO:0000468	Fig. 1C
PMID:16157682	FYPO:0000468	Fig. 1C
PMID:16169489	FYPO:0002059	knocked out in diploid. Can't tell if it vegetative or spore?
PMID:16169489	FYPO:0002059	knocked out in diploid. Can't tell if it vegetative or spore?
PMID:16169489	FYPO:0000581	27% of spores produce viable colonies
PMID:1617727	GO:0045292	splicing of artificial construct with wt or mutated splice sites assayed in mutants
PMID:16199877	FYPO:0000266	DNS
PMID:16199877	FYPO:0000268	DNS
PMID:16199877	FYPO:0002061	fig 3A
PMID:16199877	FYPO:0000229	fig 3B
PMID:16199877	FYPO:0000284	Figure 4B
PMID:16199877	FYPO:0000228	Figure 4B
PMID:16199877	PBO:0106359	Fig. S1C
PMID:16199877	PBO:0106358	Fig. S1C
PMID:16199877	FYPO:0000229	Figure 4B
PMID:16199877	PBO:0106356	Figure 4B
PMID:16199877	FYPO:0000316	fig4
PMID:16199877	PBO:0106355	Fig 3C
PMID:16199877	FYPO:0008164	Fig 3C
PMID:16199877	PBO:0022134	Fig. 3C).
PMID:16199877	PBO:0023853	Fig. 3C).
PMID:16199877	FYPO:0000141	S1B
PMID:16199877	FYPO:0000316	S1A
PMID:16199877	FYPO:0001494	fig 3B
PMID:16199877	PBO:0112051	Fig 5DE
PMID:16199877	PBO:0023853	Fig. 3C).
PMID:16199877	FYPO:0001490	fig 3B
PMID:16199877	PBO:0022134	Fig. 3C).
PMID:16199877	FYPO:0002061	Fig 1A
PMID:16199877	FYPO:0001234	Fig 1D
PMID:16199877	FYPO:0000229	DNS
PMID:16199877	PBO:0106353	Fig 1E
PMID:16199877	PBO:0106353	Fig 1B
PMID:16199877	FYPO:0001234	Fig 1D
PMID:16199877	FYPO:0000091	DNS
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	PBO:0111663	At the mat locus, Clr3 is recruited at a specific site through a mechanism involving ATF/CREB family proteins
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:0008159	Our analyses revealed that a temper- ature-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	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: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	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:0005845	.....Interestingly, identical modifi- cation patterns were also observed in a swi6 mutant, consistent with Swi6 involvement in Clr3 spreading (Figure 5A).
PMID:16246721	FYPO:0005845	..... However, in clr3D cells, H3K9me3 was significantly reduced, while there was a substantial in- crease in H3K9me1. Furthermore, H3K9me2 levels were slightly elevated (Figure 5A).
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: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:0031934	Our results revealed that Clr3 is indeed enriched through- out 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:0111115	Remarkably, loss of Swi6 and Chp2 but not Chp1 completely abolished the localization of Clr3 at Kint2::ura4+ (Figure 1)
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:0111115	Remarkably, loss of Swi6 and Chp2 but not Chp1 completely abolished the localization of Clr3 at Kint2::ura4+ (Figure 1)
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 responsi- ble for RNAi-mediated targeting of heterochromatin to this region.
PMID:16246721	FYPO:0008157	mutant cells are de- fective in histone deacetylation and silencing at the mat2/3 locus (see Figure S1
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 se- verely affected (Figure 2A).
PMID:16246721	PBO:0109217	Surprisingly, except for a small but reproducible enrichment of Clr3 at the nu- cleation site, Clr3 was virtually absent from the entire mat2/3 region in a sir2D strain (Figure 2A).
PMID:16246721	GO:0030466	[NUCLEATION] Same pathway as clr3
PMID:16246721	GO:0030466	[NUCLEATION]
PMID:16246721	GO:0030466	[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 fac- tors, such as Chp2, involved in heterochromatin as- sembly.
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 com- pletely abolished in a clr3D dcr1D double mutant strain (Figure 4A).
PMID:16246721	PBO:0111115	[ vw specifically to REIII/ CAS, nucleation site] In double mutant cells lacking Pcr1 and Swi6, the localization of Clr3 was almost com- pletely abolished from REIII (Figure 3).
PMID:16246721	GO:0030466	[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 fac- tors, such as Chp2, involved in heterochromatin as- sembly.
PMID:16246721	GO:0030466	[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 fac- tors, such as Chp2, involved in heterochromatin as- sembly.
PMID:16246721	GO:0030466	[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 fac- tors, such as Chp2, involved in heterochromatin as- sembly. 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 localiza- tion at the mat locus in clr3-735 cells (see below; Figure S2),
PMID:16251348	GO:0005730	fig 2c
PMID:16251348	GO:0006364	fig3B
PMID:16252005	PBO:0093613	same as ddb1delta alone
PMID:16252005	GO:0006511	(regulation ) can also infer (IC) from GO:0030674
PMID:16252005	PBO:0093613	same as cdt2delta alone
PMID:16252005	PBO:0093613	same as pcu4delta alone
PMID:16252005	PBO:0093615	same as csn1delta alone
PMID:16252005	PBO:0093618	same as ddb1delta alone
PMID:16252005	PBO:0093618	same as cdt2delta alone
PMID:16252005	PBO:0093618	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	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	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: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: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:0001234	Therefore, sec9+ is essential for vegetative cell growth and spore germination.
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	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:0001234	Therefore, sec9+ is essential for vegetative cell growth and spore germination.
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:16291723	FYPO:0001367	fig 6
PMID:16291723	PBO:0096394	Figue 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	Figue 5C
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	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:0051286	Rgf1p-GFP was also detected at cell ends (Fig. 4B).
PMID:16291723	FYPO:0002061	Fig. 3C
PMID:16291723	PBO:0096392	Figue 5C
PMID:16291723	PBO:0096391	Fig. 3C
PMID:16291723	FYPO:0002200	Fig. 3C
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:0001366	Fig. 1A. All cells lysed while undergoing division and the daughter cells remained attached to one another.
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	FYPO:0003369	(50 mM)
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:0002060	Fig. 3C.
PMID:16291723	FYPO:0002060	rgf3+ is essential
PMID:16291723	FYPO:0001234	(Fig. 3C).
PMID:16291723	PBO:0020891	(Fig. 3C).
PMID:16291723	FYPO:0002061	rgf3+ is essential
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: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	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	FYPO:0002061	`SYNTHETIC LETHAL
PMID:16317005	PBO:0101093	activated_by CHEBI:15422 | inhibited_by CHEBI:16284
PMID:16317005	PBO:0101093	activated_by CHEBI:15422 | inhibited_by CHEBI:16284
PMID:16317047	PBO:0113822	Fig. 2B
PMID:16317047	MOD:01148	Fig. 4F
PMID:16317047	PBO:0113832	Fig. 5C
PMID:16317047	PBO:0113833	Fig. 5C
PMID:16317047	PBO:0095096	Fig. 3C
PMID:16317047	PBO:0095096	Fig. 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:0113825	Fig. 3A
PMID:16317047	PBO:0113825	Fig. 3A
PMID:16317047	FYPO:0006399	Fig. 2D
PMID:16317047	PBO:0113824	Fig. 2C
PMID:16317047	PBO:0113823	Fig. 2B
PMID:16317047	FYPO:0005115	Fig. 2A
PMID:16317047	PBO:0113820	Fig. 1G
PMID:16317047	PBO:0113820	Fig. 1G
PMID:16317047	PBO:0113821	Fig. 1F
PMID:16317047	PBO:0113821	Fig. 1E
PMID:16317047	PBO:0113821	Fig. 1D
PMID:16317047	PBO:0113820	Fig. 1B
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	FYPO:0006399	Fig. 3D
PMID:16317047	PBO:0113829	Fig. 3B and C
PMID:16317047	PBO:0113828	Fig. 3B and C
PMID:16317047	PBO:0113828	Fig. 3B and C
PMID:16317047	PBO:0033269	Fig. 3C
PMID:16317047	PBO:0033269	Fig. 3C
PMID:16317047	PBO:0032847	Fig. 3C
PMID:16317047	PBO:0113827	Fig. 3B and C
PMID:16317047	PBO:0113826	Fig. 3B and C
PMID:16317047	MOD:00696	Fig. 4E
PMID:16317047	PBO:0096598	Fig. 3C
PMID:16317047	PBO:0095096	Fig. 3C
PMID:16325576	PBO:0109784	S1
PMID:16325576	PBO:0109783	S1
PMID:16325576	PBO:0096955	Figure 5C However, the ChIP assay demonstrated intact lo- calization 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 lo- calization 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:0109782	Figure 2C
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:0096958	This hypothesis makes the key prediction that the in- crease of Rec8 at the centromeric central core would de- pend 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	FYPO:0004212	(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	FYPO:0004159	Figure 2C
PMID:16325576	PBO:0092319	induced
PMID:16325576	PBO:0096952	Whereas monopolar attachment is obviously impaired in moa1D rec12D meiosis I, the protection of centromere co- hesion also appears defective since almost all sister chroma- tids eventually separate.
PMID:16325576	FYPO:0004393	Whereas monopolar attachment is obviously impaired in moa1D rec12D meiosis I, the protection of centromere co- hesion also appears defective since almost all sister chroma- tids eventually separate.
PMID:16325576	FYPO:0005648	Figure 2D. Although deletion of moa1+ thus causes a centro- mere-specific defect, recombination appears to promote re- ductional 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	S2
PMID:16325576	PBO:0109786	S1
PMID:16325576	PBO:0109786	S1
PMID:16325576	PBO:0109786	S1
PMID:16325576	PBO:0109780	figure1
PMID:16325576	PBO:0109780	figure1
PMID:16325576	PBO:0109780	figure1
PMID:16325576	PBO:0109780	figure1
PMID:16325576	PBO:0109780	figure1
PMID:16325576	FYPO:0001894	figure2a
PMID:16325576	FYPO:0001894	figure2a
PMID:16325576	PBO:0109676	figure2b
PMID:16325576	PBO:0109781	Figure 2C
PMID:16325576	PBO:0109782	Figure 2C/3b
PMID:16325576	PBO:0109785	S1
PMID:16360688	PBO:0112587	, Sgo1 is seen as nuclear staining with punctate dots of fluores- cence along the spindle (Figure 1D and [2, 9]). This local- ization is abolished in a bub1D background but pre- served 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 pro- mote correct Sgo1 localization and function during MI.
PMID:16360688	PBO:0112587	, Sgo1 is seen as nuclear staining with punctate dots of fluores- cence along the spindle (Figure 1D and [2, 9]). This local- ization is abolished in a bub1D background but pre- served 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 pro- mote correct Sgo1 localization and function during MI.
PMID:16360688	PBO:0112576	figure 1c
PMID:16360688	PBO:0112588	figure1c a high frequency of sis- ter-chromatid nondisjunction during MII (Figure 1C), consistent with Sgo1’s being largely nonfunctional in this mutant background.
PMID:16360688	PBO:0112586	Similarly, we found that Sgo1 was mislocalized in a different allele (Figure 1D, K762M [6])
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: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: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	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 (approxi- mately 40% binucleated cells).
PMID:16360688	PBO:0100757	but homolog segregation was restored to a certain extent by the deletion of rec11 (approxi- mately 40% binucleated cells).
PMID:16360688	PBO:0112576	figure 1b
PMID:16360688	PBO:0112577	figure1a
PMID:16360688	PBO:0112577	figure 1a
PMID:16360688	PBO:0112578	figure 1a
PMID:16360688	PBO:0112579	figure1a
PMID:16360688	PBO:0112580	figure1a
PMID:16360688	PBO:0112581	figure1a
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:0112576	figure 1c
PMID:16360688	PBO:0112583	figure 1c
PMID:16360688	PBO:0112582	figure 1c
PMID:16360688	PBO:0112584	figure 1c
PMID:16360688	PBO:0112585	figure 1c
PMID:16360688	PBO:0112586	, Sgo1 is seen as nuclear staining with punctate dots of fluores- cence along the spindle (Figure 1D and [2, 9]). This local- ization is abolished in a bub1D background but pre- served 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 pro- mote correct Sgo1 localization and function during MI.
PMID:16360688	PBO:0112587	, Sgo1 is seen as nuclear staining with punctate dots of fluores- cence along the spindle (Figure 1D and [2, 9]). This local- ization is abolished in a bub1D background but pre- served 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 pro- mote correct Sgo1 localization and function during MI.
PMID:16394105	FYPO:0001357	fig 7 a
PMID:16394105	PBO:0102084	Figure 8 AB
PMID:16394105	PBO:0102085	Figure 8 C
PMID:16394105	FYPO:0001234	fig 7 b
PMID:16394105	FYPO:0001357	fig 7 a
PMID:16394105	PBO:0102080	Figure 1 B
PMID:16394105	PBO:0102079	Figure 1 B
PMID:16394105	PBO:0102078	Supplemental data
PMID:16394105	FYPO:0002638	Figure 1 B
PMID:16394105	PBO:0102077	Figure 1 B
PMID:16394105	PBO:0102076	Figure 1 B
PMID:16394105	PBO:0102086	Figure 8 D
PMID:16394105	PBO:0102086	Figure 8 D
PMID:16394105	PBO:0102086	Figure 8 D
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:0002060	table 4
PMID:16394105	FYPO:0002060	table 4
PMID:16394105	FYPO:0002061	table 4
PMID:16394105	FYPO:0002061	table 4
PMID:16394105	FYPO:0002060	fig 5 e
PMID:16394105	FYPO:0002061	fig 5 d
PMID:16394105	FYPO:0005706	fig 4
PMID:16394105	PBO:0037147	fig 3
PMID:16394105	PBO:0037146	fig 3
PMID:16394105	FYPO:0000899	morphology
PMID:16394105	FYPO:0002060	table 4
PMID:16394105	PBO:0037149	Figur 6 B,C
PMID:16394105	PBO:0037150	Figur 6 B,C
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	PBO:0094648	rga1􏰁 cells were severely impaired for growth, whereas rgf1􏰁rga1􏰁 exhibited a better growth pat- tern and resembled rgf1􏰁 cells.
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	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 expres- sion 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􏰃 overex- pression. This activity was fourfold higher than that ob- served 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	decreased gtp-bound gtpase (active)
PMID:16421249	PBO:0099856	increased gtp-bound gtpase (active)
PMID:16421249	PBO:0099855	rescue of multiseptate, swollen
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 pheno- type 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	positive regulation
PMID:16421249	PBO:0099854	Figure 2B regardless of the growth temperature 30 –35% of the cells were lysed,
PMID:16421249	GO:0051523	positive regulation
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	FYPO:0001366	Figure 3A at cell division site
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	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	GO:0090334	positive regulation
PMID:16421249	PBO:0099852	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:0099851	Figure 2B regardless of the growth temperature 30 –35% of the cells were lysed,
PMID:16421249	PBO:0099850	Figure 2A
PMID:16421249	PBO:0094648	(Figure 2A The resulting strain, rgf1􏰃, showed a slow growth pattern at 28°C
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	FYPO:0002691	Fig. 1
PMID:16428309	PBO:0114466	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:16428435	PBO:0112034	Fig. 2
PMID:16428435	FYPO:0002150	Thus, the carboxyl terminus of Cdk9 [...] is required for cell viability. Table 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	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. 3B and C
PMID:16428435	PBO:0112037	Fig. 3
PMID:16428435	PBO:0112187	Fig. 2D
PMID:16428435	PBO:0112186	Fig. 2D
PMID:16428435	PBO:0112036	Fig. 2C and D
PMID:16428435	PBO:0112035	Fig. 2B
PMID:16453724	FYPO:0000608	with re-replication
PMID:16453724	FYPO:0003758	ABOLISHED SEPARATION
PMID:16453724	FYPO:0003758	ABOLISHED SEPARATION
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:0000674	Table 1
PMID:16453733	FYPO:0000674	Table 1
PMID:16453733	FYPO:0000674	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:0000674	Table 1
PMID:1645660	GO:0016791	inhibited_by zinc(2+) activated_by magnesium(2+)
PMID:16467379	GO:0031097	localization dependent on F-actin (assayed using Latrunculin A)
PMID:16481403	GO:0008017	fig 1c
PMID:16481403	FYPO:0006195	Fig1 D (actually 2 bundles)
PMID:16481403	GO:0051415	emtoc
PMID:16481403	PBO:0020565	igure 5B
PMID:16481403	FYPO:0006397	from both ends
PMID:16481403	FYPO:0005558	from both ends
PMID:16481403	PBO:0101741	fig1
PMID:16483313	PBO:0102487	isn't really processing, cleavage
PMID:16489217	GO:0010515	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	FYPO:0001357	aerobic conditions
PMID:16537923	PBO:0098521	genes specified in extensions assayed in low-throughput Northern blots; additional genes assayed in high-throughput microarrays not listed
PMID:16537923	PBO:0098520	genes specified in extensions assayed in low-throughput Northern blots; additional genes assayed in high-throughput microarrays not listed
PMID:16537923	PBO:0098522	genes specified in extensions assayed in low-throughput Northern blots; additional genes assayed in high-throughput microarrays not listed
PMID:16541024	GO:0000159	fig.1
PMID:16541024	FYPO:0003176	Supplementary Fig. S2a
PMID:16541024	PBO:0097372	Fig. 2b
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:0097371	Fig. 4
PMID:16541024	PBO:0097371	Fig. 4
PMID:16541024	PBO:0097370	Fig. 2b
PMID:16541024	PBO:0097373	Fig. 4
PMID:16541024	PBO:0109336	Notably, we detected only a single combination of PP2A subunits associated with SpSgo1, namely SpPaa1A–SpPar1B′–SpPpa2C
PMID:16541024	PBO:0109333	this is an inference, but almost certainly true based on the genetics
PMID:16541024	PBO:0097370	Fig. 2b
PMID:16541024	PBO:0097370	Fig. 2b
PMID:16541024	PBO:0112501	Fig. 2b
PMID:16541024	PBO:0112501	Fig. 2b
PMID:16541024	PBO:0112500	Fig. 2b
PMID:16541024	PBO:0112500	Fig. 2b
PMID:16541024	FYPO:0002219	Fig. 2a
PMID:16541024	FYPO:0002219	Fig. 2a
PMID:16541024	PBO:0097367	Fig. 2a
PMID:16541024	FYPO:0002219	Fig. 2a
PMID:16541024	GO:0000159	fig.1
PMID:16541024	PBO:0097016	Supplementary Fig. S2a
PMID:16541024	PBO:0097366	Supplementary Fig. S2a
PMID:16541024	FYPO:0003176	Supplementary Fig. S2a
PMID:16541024	FYPO:0003176	Supplementary Fig. S2a
PMID:16541024	GO:0000159	fig.1
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)...both of these mutant cell types showed precocious centromeric dissociation after meiosis I, and random chromosome segregation following meiosis II
PMID:16541025	FYPO:0003182	(Supplementary Fig. 7)
PMID:16541025	FYPO:0003182	(Supplementary Fig. 7)
PMID:16541025	PBO:0109338	Fig. 5a
PMID:16541025	PBO:0102397	Fig. 5b however, it colocalizes with Sgo1 at centromeres during meiosis I
PMID:16541025	FYPO:0005648	(Supplementary Fig. 7).
PMID:16541025	PBO:0095117	dns
PMID:16541025	PBO:0102398	(Fig. 5b).
PMID:1655416	GO:0005515	ADD MODIFIED FORMS
PMID:1655416	FYPO:0000333	transient
PMID:1655416	FYPO:0000333	is delayed but the delay is reduced compared to the single mutant
PMID:1655416	PBO:0033741	figure 10 C
PMID:1655416	PBO:0033742	figure 10 C
PMID:1655416	PBO:0033737	LENgth
PMID:1657594	GO:0030552	fig 6
PMID:1657594	PBO:0099549	fig 6
PMID:16585273	FYPO:0000927	Fig. 4 E
PMID:16611237	PBO:0095920	indicates a G2 delay
PMID:16618806	PBO:0098128	assayed substrate myelin basic protein
PMID:16618806	PBO:0098128	assayed substrate myelin basic protein
PMID:16618806	PBO:0102093	effect of mutation in substrate Cds1 molecule
PMID:16618806	PBO:0093581	cells otherwise haploid
PMID:16618806	PBO:0093581	cells otherwise haploid
PMID:16618806	PBO:0093581	cells otherwise haploid
PMID:16618806	PBO:0102090	residue T11
PMID:16618806	PBO:0094206	assayed substrate myelin basic protein
PMID:16618806	PBO:0094255	residue T11
PMID:16618806	PBO:0102094	effect of mutation in substrate Cds1 molecule
PMID:16618806	PBO:0102095	effect of mutation in substrate Cds1 molecule
PMID:16618806	PBO:0099533	induced dimerization increases Cds1 autophosphorylation without prior phosphorylation on T11
PMID:16618806	PBO:0102092	residue T11
PMID:16618806	PBO:0102090	residue T11
PMID:16618806	PBO:0102096	abolished dimerization in kinase-dead cds1-D312E
PMID:16618806	PBO:0102097	assayed substrate myelin basic protein
PMID:16618806	PBO:0102097	assayed substrate myelin basic protein
PMID:16618806	PBO:0098128	assayed substrate myelin basic protein
PMID:16618806	PBO:0098128	assayed substrate myelin basic protein
PMID:16618806	PBO:0102090	residue T11
PMID:16618806	PBO:0102091	residue T11
PMID:16618806	PBO:0102097	assayed substrate myelin basic protein
PMID:16618806	PBO:0102097	assayed substrate myelin basic protein
PMID:16618806	PBO:0102098	has output PR:000037300
PMID:16618806	PBO:0098128	assayed substrate myelin basic protein
PMID:16618806	PBO:0098128	assayed substrate myelin basic protein
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 zy- gotes. 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 visu- alized 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	membrane anchor
PMID:16682348	PBO:0103025	G1 arrested cells
PMID:16682348	PBO:0101859	(G1 arrested cells)
PMID:16687577	PBO:0106114	Figure 6 asymetric during cytokinesis delay
PMID:16687577	PBO:0106113	Figure 5, D and E for maintenance of the actomyosin ring in response to cytokinesis delay upon
PMID:16687577	GO:1903475	different pathway
PMID:16687577	GO:1903475	different pathway
PMID:16687577	FYPO:0002026	fig4
PMID:16687577	PBO:0106109	fig4
PMID:16687577	PBO:0095196	fig 2
PMID:16687577	PBO:0095630	fig 1
PMID:16687577	PBO:0095630	fig 1
PMID:16687577	PBO:0095630	fig 1
PMID:16687577	PBO:0106108	fig4
PMID:16687577	PBO:0094433	fig 3
PMID:16687577	PBO:0106107	fig 3
PMID:16687577	PBO:0106106	fig 2
PMID:16687577	PBO:0106115	fig7
PMID:16687577	PBO:0106112	Figure 5, D and E for maintenance of the actomyosin ring in response to cytokinesis delay upon
PMID:16687577	PBO:0106111	fig 5 (during ectopic SIN activation)
PMID:16687577	PBO:0038073	fig 5
PMID:16687577	PBO:0106110	fig 5
PMID:16738311	FYPO:0001355	32 °C
PMID:16738311	FYPO:0001355	32 °C; very slightly worse than without cid12delta
PMID:16738311	FYPO:0001355	32 °C
PMID:16738311	FYPO:0001355	32 °C; better than without cid12delta
PMID:16738311	PBO:0093560	32 °C
PMID:16738311	PBO:0093560	32 °C; same as without cid12delta
PMID:16738311	FYPO:0001355	32 °C
PMID:16738311	FYPO:0001357	32 °C
PMID:16738311	FYPO:0002061	26 °C
PMID:16738311	FYPO:0002061	26 °C
PMID:16738311	FYPO:0002928	centromere outer repeat transcripts
PMID:16738311	FYPO:0001355	32 °C
PMID:16738311	PBO:0093560	32 °C
PMID:16762840	GO:0005721	heterochromatic loci, including centromeres, telomeres, and the mat locus (Figure 2A).
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 abol- ished, 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 abol- ished, such as in a Dclr4 background, loss of Epe1 had no detectable effect on transcript levels (Figure 5D).
PMID:16762840	PBO:0111030	Deletion of clr3 re- sults in a dramatic increase in Pol II occupancy at cenH element within silent mat domain.
PMID:16762840	PBO:0094684	However, abundant transcripts corresponding to cen- tromeric repeats and cenH are detectable in RNAi- defective Dago1 cells. We found that the levels of tran- scripts 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 ele- ments.
PMID:16762840	FYPO:0000862	Indeed, we found that loss of H3K9me2 in cells overexpressing Epe1 is de- pendent 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 re- sulted in considerable increase in H3K9me2 and H3K9me3 levels, concomitant with moderate increase in Swi6 binding at the ssm4 gene (Figures 6E and 6F).
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	FYPO:0002335	The Y307 mutation abolished the ability of Epe1 to destabilize heterochromatic silencing (Figure 6A).
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: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 inter- action 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 muta- tions 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 recruit- ment of Epe1 to these loci.
PMID:16762840	PBO:0111029	Moreover, ChIP analy- sis 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:0111028	Moreover, ChIP analy- sis 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	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:0111027	Moreover, ChIP analy- sis 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 de- tected 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 de- tected 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 de- tected 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 de- tected at certain meiotic genes, some of which are coated with heterochromatic markers (Figure 2A; [Cam et al., 2005]).
PMID:16762840	PBO:0111022	Moreover, Epe1 was de- tected at certain meiotic genes, some of which are coated with heterochromatic markers (Figure 2A; [Cam et al., 2005]).
PMID:16762840	PBO:0098231	Moreover, Epe1 was de- tected 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 re- vealed 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	PBO:0111021	Moreover, Epe1 was de- tected at certain meiotic genes, some of which are coated with heterochromatic markers (Figure 2A; [Cam et al., 2005]).
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	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:0110802	ChIP analysis showed that mutant protein is recruited to heterochromatic loci (Figure 6B), consis- tent with data showing that Y307A mutation has no ef- fect on Epe1 interaction with Swi6 in vitro (Figure 3D)
PMID:16762840	PBO:0094684	Our analysis revealed that Epe1 is required for the increase in transcription of repeats in Dclr3 back- ground, as suggested by the dramatic reduction in tran- script levels in Depe1 Dclr3 double mutant compared to Dclr3 single mutant (Figures 5A and 5B).
PMID:16762840	PBO:0097227	Our analysis revealed that Epe1 is required for the increase in transcription of repeats in Dclr3 back- ground, as suggested by the dramatic reduction in tran- script levels in Depe1 Dclr3 double mutant compared to Dclr3 single mutant (Figures 5A and 5B).
PMID:16762840	PBO:0097227	Our analysis revealed that Epe1 is required for the increase in transcription of repeats in Dclr3 back- ground, as suggested by the dramatic reduction in tran- script levels in Depe1 Dclr3 double mutant compared to Dclr3 single mutant (Figures 5A and 5B).
PMID:16762840	PBO:0097227	However, abundant transcripts corresponding to cen- tromeric repeats and cenH are detectable in RNAi- defective Dago1 cells. We found that the levels of tran- scripts in Depe1Dago1 double mutant cells were significantly reduced (Figures 5A and 5B), indicating that Epe1 facilitates transcription of the heterochromatic repeats.
PMID:16762840	PBO:0097227	However, abundant transcripts corresponding to cen- tromeric repeats and cenH are detectable in RNAi- defective Dago1 cells. We found that the levels of tran- scripts in Depe1Dago1 double mutant cells were significantly reduced (Figures 5A and 5B), indicating that Epe1 facilitates transcription of the heterochromatic repeats.
PMID:16775007	PBO:0098905	fig 5D
PMID:16775007	FYPO:0002061	Figure 5, A and B
PMID:16775007	GO:0005515	Figure 4C
PMID:16775007	GO:0044732	Fig 1A
PMID:16775007	GO:0005515	Fig 2A
PMID:16775007	PBO:0098902	Fig2A
PMID:16775007	FYPO:0002061	Figure 7A
PMID:16816948	FYPO:0004009	pulse/chase
PMID:16822282	PBO:0097358	caspase
PMID:16822282	FYPO:0001309	fig3A
PMID:16822282	FYPO:0002143	fig3A
PMID:16822282	FYPO:0002143	fig3A
PMID:16822282	FYPO:0004129	caspase
PMID:16822282	FYPO:0001310	fig3A
PMID:16822282	FYPO:0001310	fig3A
PMID:16822282	FYPO:0004129	caspase
PMID:16822282	FYPO:0002143	fig3A
PMID:16822282	FYPO:0001309	fig3A
PMID:16823445	PBO:0108615	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	might be abolished. Sometimes you see diploidization.
PMID:16914721	PBO:0097312	microarray data shows 111 genes affected
PMID:16914721	FYPO:0003917	assayed using ade6-M26
PMID:16914721	PBO:0097313	microarray data shows 111 genes affected
PMID:16914721	PBO:0097311	microarray data shows 111 genes affected
PMID:16914721	PBO:0094384	microarray data shows 111 genes affected
PMID:16914721	GO:0000184	These findings showed that Upf1 is re- quired for degradation of the ade6-M26 mRNA in S. pombe.
PMID:16914721	GO:0000184	These findings showed that Upf1 is re- quired for degradation of the ade6-M26 mRNA in S. pombe.
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: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 targets cdc18+ and ste9+ , is a G1-specific transcript (Figure 6D).
PMID:16916637	PBO:0113984	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:16920624	PBO:0106990	Figure 1C
PMID:16920624	PBO:0106989	figure 1B.
PMID:16920624	PBO:0106989	figure 1B.
PMID:16920624	FYPO:0002141	Figure 2A.
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	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	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-phosphory- lated form of Dis1)
PMID:16920624	PBO:0106993	These results established that phosphorylation of Dis1 by Cdc2 is required for the high-fidelity segregation of a minichromosome. (A little bit of curator licence here)
PMID:16920624	FYPO:0002061	Figure 2D. The double mutant mis12 Dis16A failed to produce colonies at 33
PMID:16920624	FYPO:0001355	Figure 2D. whereas mis12 Dis1N3A and mis12 Dis1C3A showed weak inhibition of colony formation
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 33􏰀C.
PMID:16920624	PBO:0023853	PHOSPHORYLATED. Fig3A The Dis1WT-GFP signals are seen as the kinetochore dots in metaphase. AND 4b
PMID:16920624	PBO:0106994	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 (ana- phase 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 mea- sured differences were within the boundaries of experi- mental error (Figure S1C)
PMID:16920624	FYPO:0004310	Measurements of the durations of phase 1 (prophase to metaphase), 2 (metaphase to anaphase), and 3 (ana- phase 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 mea- sured differences were within the boundaries of experi- mental 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	UNPHOSPHORYLATED. In anaphase, Dis1WT-GFP signals abruptly increased along the spindle and at the SPBs despite being absent from the central zone.
PMID:16920624	PBO:0018845	Because Dis1WT, Dis16A, and Dis16E all associated with anaphase SPBs, this as- sociation was independent of modification of the mole- cule on the Cdc2 phosphorylation sites.
PMID:16920624	FYPO:0000964	fig6
PMID:16920624	FYPO:0002061	In contrast, the Dis16E mutant, which shows the synthetic lethality with Dmtc1, dimin- ished 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:16921379	GO:0005515	sfr1 protein is not stable without swi5. swi5 alone does not bind rad51.
PMID:16921379	GO:0005515	sfr1 protein is not stable without swi5. swi5 alone does not bind rad51.
PMID:16921379	PBO:0105172	in complex with Swi5
PMID:16921379	PBO:0105172	in complex with Sfr1
PMID:16931764	PBO:0098772	Fig. 2C
PMID:16931764	PBO:0112807	Fig. 2C
PMID:16931764	PBO:0112807	Fig. 2C
PMID:16931764	PBO:0112806	Fig. 2B
PMID:16931764	PBO:0112805	Fig. 2B
PMID:16931764	PBO:0112804	Fig. 2A
PMID:16931764	PBO:0112800	Fig. 1C
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:0112803	Fig. 2A
PMID:16931764	PBO:0112800	Fig. 1C
PMID:16931764	PBO:0094684	Fig. 3C
PMID:16931764	PBO:0098772	Fig. 2C
PMID:16931764	PBO:0112804	Fig. 2A
PMID:16931764	PBO:0112803	Fig. 2A
PMID:16931764	FYPO:0002835	Fig. 1E
PMID:16931764	FYPO:0002835	Fig. 1E
PMID:16931764	PBO:0112802	Fig. 1D
PMID:16931764	PBO:0112801	Fig. 1D
PMID:16931764	PBO:0112802	Fig. 1D
PMID:16931764	PBO:0112801	Fig. 1D
PMID:16931764	PBO:0112802	Fig. 1D
PMID:16931764	PBO:0112801	Fig. 1D
PMID:16931764	PBO:0112802	Fig. 1D
PMID:16931764	PBO:0112801	Fig. 1D
PMID:16931764	PBO:0094684	Fig. 3C
PMID:16963626	GO:0016602	6b
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	PBO:0095322	Consistently, mutations in the php3􏰀 - and php5􏰀 -encoded CCAAT-binding proteins were phenocopies of php2􏰂
PMID:16963626	PBO:0095322	Consistently, mutations in the php3􏰀 - and php5􏰀 -encoded CCAAT-binding proteins were phenocopies of php2􏰂
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: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:0033573	figure2
PMID:17004072	FYPO:0002061	table 2
PMID:17004072	FYPO:0002060	figure 5 b
PMID:17004072	FYPO:0001861	figure 2a
PMID:17004072	FYPO:0001861	figure 2a
PMID:17005570	PBO:0104005	fig 7 A
PMID:17005570	GO:0005515	fig 1
PMID:17005570	PBO:0104002	fig3
PMID:17005570	PBO:0103998	Fig 1c lane 9
PMID:17005570	GO:0005515	fig 1
PMID:17005570	GO:0005515	fig 1
PMID:17005570	PBO:0104003	fig 5 A
PMID:17005570	PBO:0104003	fig 5 C
PMID:17005570	GO:0005515	fig 1
PMID:17005570	GO:0005515	fig 1
PMID:17005570	PBO:0104004	fig 6 A, lane 9
PMID:17005570	PBO:0104004	fig 6 B, lane 3
PMID:17005570	GO:0005515	fig 1
PMID:17005570	PBO:0104004	fig 6 B, lane 9
PMID:17005570	PBO:0104005	fig 7 A
PMID:17005570	GO:0005515	fig 1
PMID:17005570	PBO:0103998	fig 1 b
PMID:17005570	PBO:0103999	fig 1 b
PMID:17005570	PBO:0103999	fig 1 c
PMID:17005570	PBO:0104000	fig 1 d
PMID:17005570	GO:0005515	fig 1 F
PMID:17005570	PBO:0104001	fig 1 f
PMID:17005570	PBO:0104001	fig 1 f
PMID:17005570	PBO:0104000	fig3
PMID:17005570	PBO:0104000	fig3
PMID:17005570	PBO:0104000	fig3
PMID:17005570	PBO:0104002	fig3
PMID:17005570	PBO:0104002	fig3
PMID:1703321	FYPO:0002060	cdc2-F15 gene is expressed from episomal pIRT2
PMID:1703321	FYPO:0006822	cdc2-F15 gene is expressed from episomal pIRT2
PMID:1703321	PBO:0093712	cdc25 over expressed from the constitutive ADH promoter. Data not shown
PMID:1703321	PBO:0093712	data not shown
PMID:1703321	PBO:0097952	Figure 4D phospho amino acid analysis
PMID:1703321	PBO:0093712	data not shown
PMID:1703321	PBO:0097952	Figure 4D phospho amino acid analysis
PMID:1703321	PBO:0093712	I'm sure this has already been annotated. But previous annotations didn't come up, should they?
PMID:1703321	PBO:0093712	Also think this is previously annotated
PMID:1703321	PBO:0097952	Figure 4D phospho amino acid analysis
PMID:1703321	PBO:0097952	Figure 4 phospho amino acid analysis
PMID:1703321	PBO:0093712	cdc2-F15 gene is expressed from episomal pIRT2
PMID:1703321	FYPO:0002060	cdc2-F15 gene is expressed from episomal pIRT2
PMID:17035632	PBO:0103971	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: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: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	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:0018649	These 4 proteins share homology with the S. cerevisiae DASH com- plex, 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 com- plex, 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 com- plex, 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 com- plex, 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: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, dur- ing 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, dur- ing 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, dur- ing 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, dur- ing 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, dur- ing 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, dur- ing 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, dur- ing 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, dur- ing 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, dur- ing 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, dur- ing 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, dur- ing 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, dur- ing 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, dur- ing 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, dur- ing 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, dur- ing 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, dur- ing 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, dur- ing 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, dur- ing meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	PBO:0109097	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3).
PMID:17035632	PBO:0109098	In addition, their centromere localization depended on Mis6: Cnl2 and Fta7 proteins lost their centromere localization in a mis6-302 tem- perature-sensitive mutant at the restricted temperature of 36°C (Figure 1E)
PMID:17035632	PBO:0109099	In addition, their centromere localization depended on Mis6: Cnl2 and Fta7 proteins lost their centromere localization in a mis6-302 tem- perature-sensitive mutant at the restricted temperature of 36°C (Figure 1E)
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: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: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:17036054	PBO:0101891	Supplement
PMID:17036054	PBO:0101887	figure 1a
PMID:17036054	PBO:0101887	figure 1a
PMID:17036054	PBO:0101893	fig1b
PMID:17036054	FYPO:0005720	fig1b
PMID:17036054	PBO:0101889	figure 1a
PMID:17036054	PBO:0101888	figure 1a
PMID:17036054	PBO:0101893	fig1b
PMID:17036054	PBO:0101887	figure 1a
PMID:17036054	PBO:0101888	figure 1a
PMID:17036054	PBO:0101894	fig1b
PMID:17036054	PBO:0101890	figure 1a
PMID:17036054	PBO:0101893	fig1b
PMID:17036054	PBO:0101888	figure 1a
PMID:17038309	GO:0097680	i) xlf1 deletion is epistatic with lig4 deletion ii) IR sensitivity during spore state and inability to ligate linearised plasmids during vegetative state
PMID:17038309	GO:0003677	binds both circular and linear DNA fragments
PMID:17039252	PBO:0094400	especially during S and G2 phases
PMID:17039252	PBO:0094400	especially during S and G2 phases
PMID:17039252	PBO:0094400	especially during S and G2 phases
PMID:17039252	PBO:0094400	especially during S and G2 phases
PMID:17043360	PBO:0112857	Fig. 4C
PMID:17043360	PBO:0093579	Fig. 1B
PMID:17043360	PBO:0093581	Fig. 1B
PMID:17043360	FYPO:0000012	Fig. 1C
PMID:17043360	FYPO:0000650	Fig. 2
PMID:17043360	PBO:0112856	Fig. 4A
PMID:17046992	FYPO:0002060	cells stop growing at high temperature, but remain viable and resume growth and division when returned to standard temperature
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: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	30 degrees
PMID:17112379	PBO:0093561	25 degrees
PMID:17112379	PBO:0093561	25 degrees
PMID:17112379	PBO:0093559	25 degrees
PMID:17112379	FYPO:0002061	30 degrees
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	s 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	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	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	PBO:0097202	at 30 degrees// Tor1 becomes necessary for cell growth when Tor2 function is compromised.
PMID:17121544	PBO:0103531	at 30 degrees
PMID:17121544	FYPO:0000400	tor1∆tor2 -19 showed only the 2C peak, and no 1C peak appeared at 36 °C
PMID:17121544	FYPO:0002061	Figure 1B
PMID:17121544	FYPO:0002061	Figure 1B
PMID:17130122	FYPO:0003669	assayed using artificial reporter construct ura4 containing two introns and one exon from nda3
PMID:17130122	FYPO:0003669	assayed using artificial reporter construct ura4 containing two introns and one exon from nda3
PMID:17130122	FYPO:0003669	assayed using artificial reporter construct ura4 containing two introns and one exon from nda3
PMID:17130122	FYPO:0003669	assayed using artificial reporter construct ura4 containing two introns and one exon from nda3
PMID:17178839	PBO:0093630	fig 4A
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: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	not sure if this is correct....
PMID:17178839	PBO:0035373	fig 2 a/b
PMID:17178839	FYPO:0000671	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:0093586	fig 4A
PMID:17178839	FYPO:0002060	fig 3C
PMID:17178839	FYPO:0005435	fig 3c
PMID:17178839	FYPO:0002061	fig 3B
PMID:17178839	FYPO:0002060	fig 3A
PMID:17178839	PBO:0035374	fig 2 a/b
PMID:17178839	PBO:0093616	fig 4A
PMID:17178839	PBO:0093580	fig 4A
PMID:17190600	PBO:0111597	H4K20me2 modified histone binding
PMID:17190600	PBO:0111599	H4K20me2 modified histone binding
PMID:17190600	PBO:0111598	H4K20me2 modified histone binding
PMID:17192844	FYPO:0000488	The wildtype 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	binding by Pab2
PMID:17222800	FYPO:0003720	25S rRNA positions 2304, 2497
PMID:17276356	PBO:0092067	Expression of dap1+ mRNA was induced in the absence of oxygen in a Sre1-de- pendent manner (Figure 1A),
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:0008296	elevated amounts of the ergosterol biosynthetic inter- mediates 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)-tri- enol, and ergosta-5,7-dienol, Figure 1B. Ergo- sta-5,7-dienol is not a normal pathway intermediate, but forms when Erg5 is inhibited (Figure S1)
PMID:17276356	FYPO:0008298	elevated amounts of the ergosterol biosynthetic inter- mediates 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)-tri- enol, and ergosta-5,7-dienol, Figure 1B. Ergo- sta-5,7-dienol is not a normal pathway intermediate, but forms when Erg5 is inhibited (Figure S1)
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	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 con- ditions but .....
PMID:17276356	FYPO:0002321	...contained a reduced amount of ergosterol and elevated amounts of the ergosterol biosynthetic inter- mediates 24-methylene lanosterol, ergosta-5,7,24(28)-tri- enol, and ergosta-5,7-dienol, consistent with defects at the Erg11 and Erg5 enzymatic steps (Figure 1B).
PMID:17276356	FYPO:0008297	elevated amounts of the ergosterol biosynthetic inter- mediates 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)-tri- enol, and ergosta-5,7-dienol, Figure 1B. Ergo- sta-5,7-dienol is not a normal pathway intermediate, but forms when Erg5 is inhibited (Figure S1)
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	FYPO:0009071	sensitive to the inhibitors of sterol syn- thesis itraconazole and CoCl2 (Figure 1D).
PMID:17289569	GO:0000183	by TGS
PMID:17289569	GO:0000183	by TGS
PMID:17289569	GO:0000183	by TGS
PMID:17289569	GO:0030466	by TGS
PMID:17289569	GO:0030466	by TGS
PMID:17289569	GO:0030466	by TGS
PMID:17289569	GO:0031509	by TGS
PMID:17289569	GO:0031509	by TGS
PMID:17289569	GO:0031509	by TGS
PMID:17289569	GO:0031508	by TGS
PMID:17289569	GO:0031508	by TGS
PMID:17289569	GO:0031508	by TGS
PMID:17289569	GO:0000183	by TGS
PMID:17289569	GO:0030466	by TGS
PMID:17289569	PBO:0100960	pericentromeric repeats, the silent mat locus, telo- meres, 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:0100960	pericentromeric repeats, the silent mat locus, telo- meres, 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, telo- meres, 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, telo- meres, 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, telo- meres, 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, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
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: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	PBO:0094681	pericentromeric repeats, the silent mat locus, telo- meres, 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, telo- meres, 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, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
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:0095651	pericentromeric repeats, the silent mat locus, telo- meres, 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, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
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	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:0100952	part of tgs
PMID:17289569	PBO:0100953	4B clr3 at telomeres were reduced to the same extent in mutant strains disrupted for either Ccq1 or Taz1,
PMID:17289569	PBO:0100953	4B clr3 at telomeres were reduced to the same extent in mutant strains disrupted for either Ccq1 or Taz1,
PMID:17289569	PBO:0100954	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	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	4B
PMID:17289569	PBO:0100956	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	4B However, defect in RNAi pathway had no impact on Ccq1 localization
PMID:17289569	PBO:0100952	part of tgs
PMID:17289569	PBO:0100957	(Figure 4C), Levels of Clr3 and Mit1 were dramati- cally reduced at subtelomeres in swi6 mutant strains
PMID:17289569	PBO:0100958	In contrast to hetero- chromatic 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:0100959	In contrast to hetero- chromatic 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	GO:0031509	by TGS
PMID:17289569	FYPO:0000853	6E
PMID:17289569	FYPO:0001168	6D
PMID:17289569	FYPO:0003704	6D
PMID:17289569	GO:0031508	by TGS
PMID:17289569	PBO:0100960	pericentromeric repeats, the silent mat locus, telo- meres, 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, telo- meres, 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	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	6B
PMID:17289569	PBO:0094681	6B
PMID:17289569	PBO:0095651	(Figure 6B)
PMID:17289569	PBO:0095651	6B
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	pericentromeric repeats, the silent mat locus, telo- meres, 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, telo- meres, 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, telo- meres, 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, telo- meres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	PBO:0094283	(Figure 6A) both clr3D232N and mit1K587A mutant alleles alleviated silencing of a marker gene inserted at pericentromeric repeats
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:0111971	On the other hand, the nuclei of sfr1D cells contained Swi5-EGFP foci,
PMID:17304215	GO:0005634	Figure 2A
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: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	foci disappear in HU; without HU foci appear but with abnormal dynamics
PMID:17304223	FYPO:0005165	foci disappear in HU; without HU foci appear but with abnormal dynamics
PMID:17307401	PBO:0093613	worse than either single mutant
PMID:17307401	PBO:0093613	worse than either single mutant
PMID:17307401	PBO:0093616	worse than either single mutant
PMID:17307401	PBO:0093560	worse than either single mutant
PMID:17307401	PBO:0093629	worse than either single mutant
PMID:17307401	PBO:0093580	same as mus81delta alone
PMID:17307401	PBO:0093613	same as mus81delta alone
PMID:17307401	PBO:0093616	same as mus81delta alone
PMID:17307401	PBO:0093630	same as mus81delta alone
PMID:17307401	PBO:0093580	worse than either single mutant
PMID:17307401	PBO:0093616	worse than either single mutant
PMID:17307401	PBO:0093629	worse than either single mutant
PMID:17310250	FYPO:0004743	Fig. 6A
PMID:17310250	PBO:0095652	Fig. 1C
PMID:17310250	PBO:0098773	Fig. 1D
PMID:17310250	PBO:0105770	Fig. 1C
PMID:17310250	PBO:0105770	Fig. 1C
PMID:17310250	FYPO:0002835	Fig. 2C
PMID:17310250	GO:0005721	Fig. 2D and E
PMID:17310250	GO:0005721	Fig. 2E
PMID:17310250	PBO:0098773	Fig. 1D
PMID:17310250	GO:0005634	Fig. 3A
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	PBO:0095652	Fig. 1C
PMID:17310250	FYPO:0006992	Fig. 5B
PMID:17310250	PBO:0105770	Fig. 1C
PMID:17310250	FYPO:0004201	Fig. 5C
PMID:17310250	FYPO:0004201	Fig. 5C
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:0112830	Fig. 6A
PMID:17310250	PBO:0112830	Fig. 6A
PMID:17310250	PBO:0112830	Fig. 6A
PMID:17310250	PBO:0112831	Fig. 6A
PMID:17310250	PBO:0098760	Fig. 6A
PMID:17310250	PBO:0098773	Fig. 6A
PMID:17310250	PBO:0112827	Fig. 1D
PMID:17310250	PBO:0112827	Fig. 1D
PMID:17310250	FYPO:0004743	Fig. 6A
PMID:17310250	PBO:0112832	Fig. 6A
PMID:17310250	PBO:0112833	Fig. 6A
PMID:17310250	PBO:0112834	Fig. 6A
PMID:17310250	PBO:0112834	Fig. 6A
PMID:17317928	FYPO:0003075	assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25
PMID:17317928	FYPO:0001382	assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25
PMID:17317928	FYPO:0001382	assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25
PMID:17317928	FYPO:0002700	assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25
PMID:17317928	FYPO:0002700	assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25
PMID:17317928	FYPO:0002700	assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25
PMID:17339332	GO:0006357	same pathway
PMID:17352737	FYPO:0004439	anaphase, elongating beyond cell end resulting in long curved spindle, requested
PMID:17363370	PBO:0020446	Fig 1D
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	FYPO:0002360	Fig. 4, A and B
PMID:17363370	PBO:0107147	Fig. 4, A and B
PMID:17363370	FYPO:0002360	Fig. 4, A and B
PMID:17363370	PBO:0107147	Fig. 4, A and B
PMID:17363370	FYPO:0002360	Fig. 4, A and B
PMID:17363370	FYPO:0007843	(supplemental Fig. 2
PMID:17363370	PBO:0107146	Interestingly, levels of trim- ethylated 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:0002922	figur 2b
PMID:17363370	FYPO:0007844	Interestingly, levels of trim- ethylated 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 abro- gates silencing of the otr1::ura4􏰁 reporter, resulting in the loss of cell viability on medium supple- mented with FOA (Fig. 3A
PMID:17363370	FYPO:0006299	figur 2d 􏰀rhp6 resulted in enhanced silencing of the otr1::ura4􏰁, as shown by reduced growth on medium lacking uracil (Fig. 2D)
PMID:17363370	FYPO:0006299	figur 2d 􏰀rhp6 resulted in enhanced silencing of the otr1::ura4􏰁, as shown by reduced growth on medium lacking uracil (Fig. 2D)
PMID:17363370	FYPO:0002922	figur 2b
PMID:17363370	FYPO:0002922	figur 2b
PMID:17363370	FYPO:0006299	figur 2d 􏰀rhp6 resulted in enhanced silencing of the otr1::ura4􏰁, as shown by reduced growth on medium lacking uracil (Fig. 2D)
PMID:17363370	FYPO:0006299	figur 2d 􏰀rhp6 resulted in enhanced silencing of the otr1::ura4􏰁, as shown by reduced growth on medium lacking uracil (Fig. 2D)
PMID:17363370	FYPO:0002922	figur 2b
PMID:17363370	FYPO:0002922	figur 2b
PMID:17363370	PBO:0107148	fig 5D
PMID:17363370	FYPO:0005071	Interestingly, the H2B-K119R mutation sig- nificantly enhanced silencing of the otr1::ura4􏰁 (Fig. 5A),
PMID:17363370	PBO:0107149	fig 5D
PMID:17363370	PBO:0107147	Fig. 4, A and B
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:17363370	PBO:0020446	Fig 1D
PMID:17363370	PBO:0020446	Fig 1D
PMID:17363370	PBO:0020446	Fig 1D
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	FYPO:0005225	Fig. 4C
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: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:0006361	Fig. 5
PMID:17412958	FYPO:0001315	Fig. 3B
PMID:17412958	PBO:0093558	Fig. 3A
PMID:17412958	FYPO:0003210	Fig. 3D
PMID:17412958	FYPO:0003210	Fig. 3D
PMID:17412958	FYPO:0006213	Fig. 3D
PMID:17412958	FYPO:0003210	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:0093560	Fig. 3A
PMID:17412958	FYPO:0000123	Fig. 3B
PMID:17412958	FYPO:0000647	Fig. 3B
PMID:17434129	FYPO:0002061	data not shown
PMID:17434129	GO:0006338	also from localization and phenotypes
PMID:17434129	GO:0006338	also from localization and phenotypes
PMID:17434129	PBO:0100344	TEL2L only
PMID:17434129	PBO:0107043	TEL2L only
PMID:17434129	FYPO:0002061	data not shown
PMID:17434129	FYPO:0007508	TEL2L only
PMID:17440621	PBO:0108790	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	inferred from the fact growth is impaired in the double mutatn spc7-23/mad2 OR spc7-23/mph1 are growth impaired, so assumption is that spindle checkpoint is active in mutant
PMID:17450151	FYPO:0006361	bulk antisense transcripts
PMID:17450151	FYPO:0002355	bulk antisense transcripts
PMID:17450151	FYPO:0004137	bulk antisense transcripts
PMID:17450151	FYPO:0000888	bulk antisense transcripts
PMID:17450151	FYPO:0003547	bulk antisense transcripts
PMID:17450151	FYPO:0006987	bulk antisense transcripts
PMID:17450151	FYPO:0000887	bulk antisense transcripts
PMID:17450151	FYPO:0003557	bulk antisense transcripts
PMID:17450151	PBO:0095840	sense strand
PMID:17450151	PBO:0095841	sense strand
PMID:17450151	FYPO:0005523	bulk antisense transcripts
PMID:17450151	FYPO:0005315	bulk antisense transcripts
PMID:17452352	PBO:0099054	5d
PMID:17452352	PBO:0102190	fig7
PMID:17452352	PBO:0102191	fig7
PMID:17452352	PBO:0102192	"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:0102193	"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:0099051	5d
PMID:17452352	PBO:0102187	5a
PMID:17452352	PBO:0102187	fig7
PMID:17452352	PBO:0102191	fig7
PMID:17452352	PBO:0102186	5a
PMID:17452352	GO:0045944	bet this is a term Val hates :p
PMID:17452352	PBO:0099055	5c
PMID:17452352	PBO:0099054	5c
PMID:17452352	PBO:0099053	5c
PMID:17452352	PBO:0099052	5c
PMID:17452352	PBO:0099051	5c
PMID:17452352	PBO:0099050	5c
PMID:17452352	PBO:0099040	fig6
PMID:17452352	PBO:0102188	fig7
PMID:17452352	PBO:0102189	fig7
PMID:17452352	PBO:0099041	fig6
PMID:17452352	PBO:0099039	fig6
PMID:17452352	PBO:0099042	fig6
PMID:17452352	PBO:0102186	fig7
PMID:17452352	PBO:0102188	fig7
PMID:17452352	PBO:0099052	5d
PMID:17452352	PBO:0102186	fig7
PMID:17452352	PBO:0102189	fig7
PMID:17452352	PBO:0102190	fig7
PMID:17452352	PBO:0099055	5d
PMID:17452352	PBO:0099050	5d
PMID:17452352	PBO:0099053	5d
PMID:17452352	PBO:0102187	fig7
PMID:17452625	GO:1904530	regulates binding by myosin; assayed in vitro using rabbit actin and unspecified myosin motor domain
PMID:17486116	FYPO:0002638	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	PBO:0110931	Furthermore, consistent with a CTGS model for silencing of mat3M::ura4+, none of the tested mutants af- fected RNApII occupancy at this locus (Figure 3C).
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: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	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, respec- tively; Figure 5A) for polyadenylation activity in vitro and found that wild-type Cid14 was able to extend a synthetic oligo(A)15 RNAno ac- tivity 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, respec- tively; 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	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: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: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	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	FYPO:0002834	figure 2 &4
PMID:17512405	FYPO:0002834	figure 2 &4
PMID:17512405	FYPO:0002834	figure 2 &4
PMID:17512405	PBO:0110932	Consistent with a role for the exosome in degrad- ing heterochromatic ura4+ transcripts, we observed elevated ura4+ transcript levels in rrp6D compared to wild-type cells (Figures 4C–4E).
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	FYPO:0002335	We found that the deletion of air1+ had no effect on heterochromatic gene silencing (Figure S2
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	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	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:0110926	Surprisingly, in cid14D cells, neither Chp1 nor Swi6 binding was signifi- cantly reduced at several heterochromatic loci, includ- ing mat3M::ura4+, imr1R::ura4+, the subtelomeric tlh1+ gene, and cen-dg and cen-dh repeats, as assayed by chromatin immunoprecipitation experiments (ChIP) (Fig- ures 3A and 3B).
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	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:0110929	Surprisingly, in cid14D cells, neither Chp1 nor Swi6 binding was signifi- cantly reduced at several heterochromatic loci, includ- ing mat3M::ura4+, imr1R::ura4+, the subtelomeric tlh1+ gene, and cen-dg and cen-dh repeats, as assayed by chromatin immunoprecipitation experiments (ChIP) (Fig- ures 3A and 3B).
PMID:17512405	PBO:0110928	Surprisingly, in cid14D cells, neither Chp1 nor Swi6 binding was signifi- cantly reduced at several heterochromatic loci, includ- ing mat3M::ura4+, imr1R::ura4+, the subtelomeric tlh1+ gene, and cen-dg and cen-dh repeats, as assayed by chromatin immunoprecipitation experiments (ChIP) (Fig- ures 3A and 3B).
PMID:17512405	PBO:0110927	Surprisingly, in cid14D cells, neither Chp1 nor Swi6 binding was signifi- cantly reduced at several heterochromatic loci, includ- ing mat3M::ura4+, imr1R::ura4+, the subtelomeric tlh1+ gene, and cen-dg and cen-dh repeats, as assayed by chromatin immunoprecipitation experiments (ChIP) (Fig- ures 3A and 3B).
PMID:17512405	PBO:0110925	Surprisingly, in cid14D cells, neither Chp1 nor Swi6 binding was signifi- cantly reduced at several heterochromatic loci, includ- ing mat3M::ura4+, imr1R::ura4+, the subtelomeric tlh1+ gene, and cen-dg and cen-dh repeats, as assayed by chromatin immunoprecipitation experiments (ChIP) (Fig- ures 3A and 3B).
PMID:17512405	PBO:0110924	Surprisingly, in cid14D cells, neither Chp1 nor Swi6 binding was signifi- cantly reduced at several heterochromatic loci, includ- ing mat3M::ura4+, imr1R::ura4+, the subtelomeric tlh1+ gene, and cen-dg and cen-dh repeats, as assayed by chromatin immunoprecipitation experiments (ChIP) (Fig- ures 3A and 3B).
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:0105941	Like cid14D, Cid14 active site mutations had dramatically reduced centromeric siRNA levels (Fig- ure 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	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) (Fig- ure 5F).
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:17531813	PBO:0108392	Fig 1B
PMID:17531813	PBO:0108406	Fig 6B
PMID:17531813	PBO:0108409	Fig 1C
PMID:17531813	PBO:0108392	Fig 1B
PMID:17531813	PBO:0098712	Fig 1C
PMID:17531813	PBO:0108393	Fig 1C (vw data not shown, but assume are elongated)
PMID:17531813	PBO:0108392	Fig 1C
PMID:17531813	PBO:0108392	Fig 1C
PMID:17531813	PBO:0108394	Figure 2B lower right panel. rad3 is not present in the chromatin fraction in the absence of cdc18
PMID:17531813	PBO:0108395	Figure 2B upper right panel. In the cytosol rad3 is present in absence of cdc18
PMID:17531813	PBO:0108396	Figure 2C lower panel. cds1 is no longer phosphorylated because rad3 is absent in absence of cdc18
PMID:17531813	PBO:0108397	Figure 2D top of lower panel.
PMID:17531813	PBO:0108398	Fig3 top 2 two panels (ve jacky syuggested Presence of stalled replication forks after DNA checkpoint inactivation, i just used normal initiation Figure 3. Replication Structures Are Not Lost When Cdc18 Is Depleted)
PMID:17531813	PBO:0108399	Fig 4 A
PMID:17531813	PBO:0108399	Fig 4 A
PMID:17531813	PBO:0108400	Fig 4A
PMID:17531813	PBO:0108401	Fig 4A
PMID:17531813	PBO:0092600	2A; during mitotic DNA replication checkpoint
PMID:17531813	PBO:0108404	Fig 5B
PMID:17531813	PBO:0108405	Fig 6 B
PMID:17531813	PBO:0108402	Fig 4D In the absence of rad26, cdc18 is unable to stabilise rad3 on chromatin
PMID:17531813	PBO:0108403	Fig5A 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: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 com- plex was inhibited (Figure 5B)
PMID:17531813	PBO:0092600	2A
PMID:17531813	PBO:0094961	Fig 6B
PMID:17531816	FYPO:0004744	Tas3WG Cells Cannot Efficiently Establish De Novo Centromeric Heterochromatin
PMID:17531816	FYPO:0003098	Tas3WG Cells Cannot Efficiently Establish De Novo Centromeric Heterochromatin
PMID:17531816	GO:0031508	ESTABLISHMENT. 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:0003241	centromeric siRNAs were present in the F276Aago1 and tas3WG single mutants but were undetectable in the double mutant (Figure 2F).
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	PBO:0094684	the double mutant (tas3WG, F276Aago1) displayed markedly elevated levels of total centromeric transcripts (Figure 2E), similar to an ago1 null.
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:17538026	FYPO:0002061	table 2
PMID:17538026	FYPO:0002061	table 2
PMID:17538026	FYPO:0004506	fig1 B
PMID:17538026	GO:0005730	fig 3a
PMID:17538026	GO:0005730	igure 3, B and D
PMID:17538026	PBO:0033837	figure 3, B and D
PMID:17538026	FYPO:0002060	fig1 a
PMID:17538026	FYPO:0002060	fig1 a
PMID:17538026	PBO:0102471	fig 6 B
PMID:17538026	PBO:0102471	fig 6 B
PMID:17538026	FYPO:0002060	fig1 a
PMID:17538026	PBO:0037118	fig1 2
PMID:17538026	PBO:0037119	fig1 2
PMID:17538026	FYPO:0004506	fig1 B
PMID:17538026	PBO:0102470	fig 4
PMID:17538026	PBO:0102469	fig 4
PMID:17538026	FYPO:0002061	fig1a
PMID:17538026	PBO:0102469	fig 4
PMID:17556368	PBO:0096992	add note in curator feedback to get double mutant phenotypes
PMID:17556368	PBO:0096993	add note in curator feedback to get double mutant phenotypes
PMID:17556368	PBO:0096990	add note in curator feedback to get double mutant phenotypes
PMID:17556368	PBO:0096991	add note in curator feedback to get double mutant phenotypes
PMID:17561805	FYPO:0002638	tested through observing no de;ay when checkpoin is inactivated
PMID:17579515	FYPO:0001734	Figure 3A and 3B, and Video S3)
PMID:17579515	FYPO:0003787	Figure 2 C check (also nuclear envelope protrusion?
PMID:17579515	FYPO:0005380	Figure S4 /Figure 3A and 3B, and Video S3)
PMID:17579515	FYPO:0002061	S1
PMID:17579515	PBO:0033900	Figure 6C (ablated Nuclear envelope)
PMID:17579515	FYPO:0004396	Figure S4)
PMID:17579515	FYPO:0000619	(APC) activation occurred and chromosome cohesion was lost (Figure 1A and 1B).
PMID:17579515	FYPO:0004536	(APC) activation occurred and chromosome cohesion was lost (Figure 1A and 1B).
PMID:17579515	PBO:0096904	(Figure 1).
PMID:17579515	PBO:0096905	4G
PMID:17579515	PBO:0096906	Figure 6C
PMID:17596513	PBO:0112600	E. coli ispA mutant used as assay system
PMID:17596513	PBO:0113809	E. coli ispA mutant used as assay system
PMID:17596513	PBO:0112600	E. coli ispA mutant used as assay system
PMID:17614284	PBO:0113657	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:0093614	Fig. S6B
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:17614284	PBO:0113691	Table S1
PMID:17614284	PBO:0093554	Fig. 2A
PMID:17614284	PBO:0113656	Table S1
PMID:17614284	PBO:0113655	Table S1
PMID:17614284	PBO:0093557	Fig. 2A
PMID:17614284	PBO:0113654	Table S1
PMID:17614284	PBO:0104709	Fig. 2B
PMID:17614284	PBO:0113653	Table S1
PMID:17614284	PBO:0113671	Table S1
PMID:17614284	PBO:0113652	Table S1
PMID:17614284	PBO:0096188	Fig. 2B
PMID:17614284	PBO:0096191	Fig. 2B
PMID:17614284	PBO:0113672	Table S1
PMID:17614284	PBO:0113673	Table S1
PMID:17614284	PBO:0113674	Table S1
PMID:17614284	PBO:0095653	Fig. 2C
PMID:17614284	FYPO:0008265	Fig. 2C
PMID:17614284	FYPO:0003555	Fig. 2C
PMID:17614284	PBO:0095058	Fig. 3A and B
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:0113641	Fig. 3C
PMID:17614284	PBO:0113642	Fig. 3C
PMID:17614284	PBO:0113651	Table S1
PMID:17614284	PBO:0113650	Table S1
PMID:17614284	PBO:0113649	Table S1
PMID:17614284	PBO:0113648	Table S1
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:0113647	Table S1
PMID:17614284	PBO:0113646	Table S1
PMID:17614284	PBO:0113645	Table S1
PMID:17614284	PBO:0101148	Fig. S6D
PMID:17614284	PBO:0113644	Fig. S6D
PMID:17614284	PBO:0113644	Fig. S6D
PMID:17614284	PBO:0093631	Fig. S6C
PMID:17614284	PBO:0093581	Fig. S6A
PMID:17614284	PBO:0113670	Table S1
PMID:17614284	PBO:0110767	Table S1
PMID:17614284	PBO:0113669	Table S1
PMID:17614284	PBO:0113668	Table S1
PMID:17614284	PBO:0113667	Table S1
PMID:17614284	PBO:0113666	Table S1
PMID:17614284	PBO:0113665	Table S1
PMID:17614284	PBO:0110761	Table S1
PMID:17614284	PBO:0113664	Table S1
PMID:17614284	PBO:0110744	Table S1
PMID:17614284	PBO:0113663	Table S1
PMID:17614284	PBO:0110745	Table S1
PMID:17614284	PBO:0110737	Table S1
PMID:17614284	PBO:0110747	Table S1
PMID:17614284	PBO:0113662	Table S1
PMID:17614284	PBO:0113661	Table S1
PMID:17614284	PBO:0113660	Table S1
PMID:17614284	PBO:0113659	Table S1
PMID:17614284	PBO:0113658	Table S1
PMID:17614284	FYPO:0001357	Fig. 2A
PMID:17632059	PBO:0096119	fig3 V-shaped patterns indicating multiple spindles
PMID:17632059	PBO:0096120	fig3
PMID:17632059	PBO:0096121	fig3D
PMID:17632059	PBO:0096108	fig1B
PMID:17632059	PBO:0096118	fig3
PMID:17632059	PBO:0096117	fig3
PMID:17632059	PBO:0096107	fig1c
PMID:17632059	PBO:0096106	fig1b
PMID:17632059	PBO:0096103	fig1B
PMID:17632059	PBO:0096104	fig1B
PMID:17632059	PBO:0096105	fig1b
PMID:17632059	PBO:0096104	fig1B
PMID:17632059	PBO:0096103	fig1B
PMID:17632059	PBO:0096102	fig1B
PMID:17632059	FYPO:0004077	fig1b
PMID:17632059	FYPO:0000681	fig1c
PMID:17632059	PBO:0096101	fig1c
PMID:17632059	PBO:0096122	table S3
PMID:17632059	PBO:0096109	fig1B
PMID:17632059	PBO:0096110	fig1B
PMID:17632059	PBO:0096111	fig1B
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	fig3
PMID:17632059	PBO:0096130	table S3
PMID:17632059	FYPO:0000681	fig1e twice their share of DNA and SPBs.
PMID:17632059	FYPO:0006365	Matching synonym SPB detached from nucleuss fix syn
PMID:17632059	FYPO:0006383	fig1f
PMID:17632059	PBO:0096126	fig s4e movie S2
PMID:17632059	FYPO:0000927	S3
PMID:17632059	FYPO:0002890	S3
PMID:17632059	FYPO:0003835	S3
PMID:17632059	PBO:0096123	table S3
PMID:17632059	PBO:0096124	table S3
PMID:17632059	PBO:0096125	table S3
PMID:17632059	FYPO:0003835	S3
PMID:17632059	FYPO:0002890	S3
PMID:17632059	FYPO:0000927	S3
PMID:17632059	FYPO:0000927	S3
PMID:17632059	PBO:0096131	fig3D (I)
PMID:17677001	PBO:0100880	Figure 2B
PMID:17677001	PBO:0100884	Figure 3C spreading is still within the central domain, to the flanking tRNAs
PMID:17677001	PBO:0100883	Figure 3B
PMID:17677001	FYPO:0004331	Figure 3A EXP says increased, but is normal compared to WT (i.e ura4 insertion derepresses)
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: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:17677001	GO:0061638	Figure S1
PMID:17677001	PBO:0095962	Figure 4C
PMID:17677001	PBO:0100886	Figure S8
PMID:17677001	PBO:0100885	Figure 4B
PMID:17690116	PBO:0019114	Fig4C At the permissive temperature 25*C rad3 is active but checkpoint cannot be activated in absence of chk1
PMID:17690116	PBO:0094205	Fig9B, C rad52D reduces amount inappropriate recombination at DNA repeats leading to a reduction in cell elongation during checkpoint activation
PMID:17690116	PBO:0019114	Fig4C At 25°C rad3 is active but checkpoint cannot be activated in absence of rad26
PMID:17690116	PBO:0037515	Fig 5B
PMID:17690116	PBO:0102121	Fig5C
PMID:17690116	PBO:0102122	Fig5C
PMID:17690116	PBO:0102123	Fig6A,B
PMID:17690116	PBO:0037130	Fig1B This is the mutant form of pREP4X cdc18 from the screen At 25°C rad3 checkpoint is active and cells elongate, At 36°C rad3 is inactive and cells do not elongate when cdc18+ is expressed from pREP4X promoter,
PMID:17690116	PBO:0037130	Fig 2A when cdc18TA6 is overexpressed at 36°C (non permissive temperature for rad3ts ) cells continue to grow and divide normally ( permissive temperature for cdc18TA6)
PMID:17690116	PBO:0020446	Fig4C at the permissive temperature rad3ts is active and the checkpoint is activated in absence of mrc1
PMID:17690116	PBO:0102123	Fig6A,B
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	Fig3 and previous figs shows lack of re replication with moderate increase in cdc18 protein level
PMID:17690116	PBO:0102125	Fig3 and previous figs shows 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	Fig7A, 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	Fig9A
PMID:17690116	PBO:0098709	Fig9B, C reb1D reduces amount inappropriate recombination at DNA repeats leading to a reduction in cell elongation during checkpoint activation
PMID:17690116	PBO:0102125	The western 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	Fig3 This is the mutant form of pREP4X cdc18 from the screen
PMID:17690116	PBO:0102129	Fig1B 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:0037130	Fig 2A cells expressing cdc18T6A at 36°C do not elongate at the nonpermissive temperature for rad3ts due to inactivation of the mitotic DNA replication checkpoint
PMID:17690116	PBO:0020446	Fig4C at 25°C rad3ts is active and the checkpoint is activated in absence of cds1
PMID:17690116	PBO:0019114	Fig4C At 25°C rad3 is active but checkpoint cannot be activated in absence of crb2
PMID:17690116	PBO:0102117	Fig2 A,C cells arrested due to activation of the rad3 (permissive temperature) have normal nuclear to cell size ratio (NC ratio) compared to cdc25-22 at restrictive temp 2 hr
PMID:17690116	PBO:0102115	Fig1C 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:0102120	Fig 5A
PMID:17690116	PBO:0102119	Fig4A
PMID:17690116	PBO:0102118	Fig2D different to when pREP3X cdc18+ is over expressed in G2 block which show replicate intermediates and cells undergo re replication
PMID:17690116	PBO:0102117	Fig2 A,C cells arrested due to activation of the rad3 (permissive temperature) have normal nuclear to cell size ratio (NC ratio) compared to cdc25-22 at restrictive temp 2 hr
PMID:17690116	PBO:0102115	Fig2B 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	Fig1C 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:0019114	Fig4C At 25°C rad3 is active but checkpoint cannot be activated in absence of rad17
PMID:17690116	PBO:0102114	Fig1B 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:0102130	Fig3 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:0019114	Fig4C At 25°C rad3 is active but checkpoint cannot be activated in absence of rad1
PMID:17690116	PBO:0019114	Fig4C At 25°C rad3 is active but checkpoint cannot be activated in absence of rad9
PMID:17804800	PBO:0092665	emsa
PMID:17868468	GO:0006264	deleted existing genome maintence term, and annotated this instead, all things considered...
PMID:17881496	FYPO:0005719	ABOLISHED Figure 3 B
PMID:17881496	FYPO:0005719	Figure 3 A
PMID:17881496	FYPO:0000620	Figure 3 A
PMID:17881496	GO:1990942	Fig. 3A
PMID:17881496	FYPO:0003302	Fig. 1B
PMID:17881496	PBO:0038222	Fig. 1A
PMID:17881729	PBO:0105768	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:0016208	(site B)
PMID:17937917	GO:0005524	(site B)
PMID:17937917	GO:0043531	(site A)
PMID:18030666	FYPO:0002336	"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	spatial extent
PMID:18030666	FYPO:0002336	spatial extent
PMID:18030666	FYPO:0002336	spatial extent
PMID:18030666	FYPO:0007477	epigenetic variegation both 5-FOA-resistant and -sensitive colonies were found
PMID:18030666	FYPO:0002336	spatial extent
PMID:18030666	FYPO:0002336	spatial extent
PMID:18030666	FYPO:0002336	spatial extent
PMID:18030666	FYPO:0002336	"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	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	spatial extent
PMID:18042546	PBO:0102864	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: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:0102866	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:0102865	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:0101588	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	PBO:0102862	all microarray (table 1); arz1 also northern (fig 1)
PMID:18042546	PBO:0102861	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:0102863	all microarray (table 1); arz1 also northern (fig 1)
PMID:18057023	PBO:0112412	Fig. 1B
PMID:18057023	PBO:0112414	Fig. 2B
PMID:18057023	PBO:0112414	Fig. 2B
PMID:18057023	PBO:0095113	Fig. 3
PMID:18057023	PBO:0112415	Fig. 7A
PMID:18057023	PBO:0112416	Fig. 7A
PMID:18057023	PBO:0112417	Fig. 7A
PMID:18057023	PBO:0112415	Fig. 7A
PMID:18057023	PBO:0112416	Fig. 7A
PMID:18057023	PBO:0112417	Fig. 7A
PMID:18057023	PBO:0112415	Fig. 7A
PMID:18057023	PBO:0112416	Fig. 7A
PMID:18057023	PBO:0112417	Fig. 7A
PMID:18057023	PBO:0112415	Fig. 7A
PMID:18057023	PBO:0112416	Fig. 7A
PMID:18057023	PBO:0112423	Fig. 8B
PMID:18057023	PBO:0112410	Fig. 1B
PMID:18057023	PBO:0112410	Fig. 1B
PMID:18057023	PBO:0112409	Fig. 1B
PMID:18057023	FYPO:0001315	Fig. 1B
PMID:18057023	FYPO:0001315	Fig. 1B
PMID:18057023	FYPO:0001315	Fig. 1B
PMID:18057023	PBO:0112408	Fig. 1A
PMID:18057023	PBO:0112408	Fig. 1A
PMID:18057023	PBO:0112407	Fig. 1A
PMID:18057023	PBO:0112407	Fig. 1A
PMID:18057023	PBO:0112406	Fig. 1A
PMID:18057023	PBO:0112406	Fig. 1A
PMID:18057023	PBO:0112422	Fig. 8B
PMID:18057023	PBO:0112417	Fig. 7A
PMID:18057023	PBO:0112418	Fig. 8A
PMID:18057023	PBO:0112419	Fig. 8A
PMID:18057023	PBO:0112420	Fig. 8A
PMID:18057023	PBO:0112421	Fig. 8B
PMID:18057023	PBO:0112405	Fig. 1A
PMID:18057023	PBO:0112404	Fig. 1A
PMID:18057023	FYPO:0001315	Fig. 1A
PMID:18057023	FYPO:0001315	Fig. 1A
PMID:18057023	PBO:0112414	Fig. 2B
PMID:18057023	PBO:0112411	Fig. 1B
PMID:18057023	PBO:0112413	Fig. 1B
PMID:18059460	GO:0008574	speckles in Fig. 4A
PMID:18060866	GO:0051285	localization independent of actin cytoskeleton (assayed using latrunculin A) and microtubule cytoskeleton (assayed using carbendazim)
PMID:18061564	PBO:0099338	figure 6F
PMID:18061564	PBO:0099337	fig6
PMID:18061564	PBO:0099339	figure 6F
PMID:18079700	PBO:0098317	Figure 3 B
PMID:18079700	PBO:0098314	Figure 3 A (but not S phase)
PMID:18079700	PBO:0098313	Figure 3 B
PMID:18079700	PBO:0098316	Figure 3 C/E
PMID:18079700	PBO:0098316	Figure 3 C/E
PMID:18079700	PBO:0098318	Figure 3 C/E during G1
PMID:18079700	PBO:0098313	Figure 3 A
PMID:18079700	GO:0007064	maintenence
PMID:18079700	FYPO:0000450	Rad21
PMID:18079700	PBO:0098316	Figure 3C and E
PMID:18079700	PBO:0098315	Figure 3 A/B
PMID:18079700	FYPO:0002060	Supplementary Figure S2
PMID:18093330	FYPO:0007068	Fig8
PMID:18093330	FYPO:0001982	fig 1
PMID:18093330	FYPO:0007068	Fig8
PMID:18157149	MOD:00427	I guess this can be changed once we can do RNA mods
PMID:18157152	MOD:00427	this is a protein modification so should be changed once we can do RNA mods
PMID:18160711	FYPO:0002702	region between NsiI sites deleted
PMID:18160711	FYPO:0002702	truncated at PacI site
PMID:18160711	FYPO:0002702	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	PBO:0110558	(Figure 1B, left panel),
PMID:18184749	FYPO:0002872	(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	PBO:0110560	(Figure 1A, right panel). Figure 1C
PMID:18184749	PBO:0110559	(Figure 1A, right panel). Figure 1C
PMID:18184749	PBO:0110557	(Figure 1B, left panel),
PMID:18184749	PBO:0110556	(Figure 1B, left panel),
PMID:18184749	PBO:0110555	(Figure 1A, right panel). Figure 1C
PMID:18184749	GO:0032541	supp 1A
PMID:18184749	GO:0032541	supp 1A
PMID:18184749	GO:0042175	supp 1A
PMID:18184749	GO:0042175	supp 1A
PMID:18184749	FYPO:0002872	abnormal ER polarization (ectopic)
PMID:18184749	FYPO:0002872	(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:18203864	PBO:0114667	(Fig. 2B)
PMID:18203864	PBO:0114668	(Fig. 2B)
PMID:18223116	PBO:0107749	fig2
PMID:18223116	PBO:0107746	fig2
PMID:18223116	PBO:0107756	fig2
PMID:18223116	PBO:0111377	fig6, it doesn't bind dna according to later studies
PMID:18223116	PBO:0106352	fig2
PMID:18223116	PBO:0107748	fig2
PMID:18223116	PBO:0107745	fig2
PMID:18223116	PBO:0107015	fig2
PMID:18223116	PBO:0107753	fig2
PMID:18223116	PBO:0107754	fig2
PMID:18223116	PBO:0107751	fig2
PMID:18223116	PBO:0107755	fig2
PMID:18223116	PBO:0107747	fig2
PMID:18223116	PBO:0107750	fig2
PMID:18223116	PBO:0107752	fig2
PMID:18223116	PBO:0107016	fig2
PMID:18256284	PBO:0033846	figure 1A
PMID:18256284	PBO:0033845	figure 1B (plus end)
PMID:18256284	PBO:0033849	figure 1B (plus end)
PMID:18256284	PBO:0033842	figure 1A
PMID:18256284	PBO:0033843	figure 1B (plus end)
PMID:18256284	PBO:0033844	figure 1B (plus end)
PMID:18256290	PBO:0096598	increased more than pxl1delta alone
PMID:18256290	PBO:0096598	less levere than pxl1 null
PMID:18256290	PBO:0096598	increased more than pxl1delta alone
PMID:18256290	PBO:0096598	increased more than pxl1delta alone
PMID:18256290	PBO:0096598	increased more than pxl1delta alone
PMID:18256290	PBO:0096598	increased more than pxl1delta alone
PMID:18256290	GO:0110085	localization dependent on filamentous actin (GO:0031941); tested using latrunculin A
PMID:18256290	PBO:0096598	less levere than pxl1 null
PMID:18262494	FYPO:0000030	with extreme sister chromtid oscillations
PMID:18262494	FYPO:0001919	after chromosome segregation
PMID:18262494	PBO:0033440	(Fig. 1B)
PMID:18272786	FYPO:0001365	data from table; nothing more specific shown
PMID:18272786	GO:0110085	dependent on F-actin (assayed using Latrunculin A)
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:18276645	PBO:0107664	normal oxygen level
PMID:18276645	PBO:0109064	normal oxygen level
PMID:18303049	PBO:0096052	Fig. 2C
PMID:18303049	PBO:0114315	Table 2
PMID:18303049	PBO:0114315	Table 2
PMID:18303049	FYPO:0000252	Table 1
PMID:18303049	PBO:0114304	Fig. 1
PMID:18303049	PBO:0114308	Fig. 5
PMID:18303049	PBO:0114307	Fig. 3D
PMID:18303049	PBO:0114306	Fig. 3B
PMID:18303049	PBO:0114309	Table 2
PMID:18303049	FYPO:0001315	Fig. 3C
PMID:18303049	FYPO:0001315	Fig. 3C
PMID:18303049	PBO:0114307	Fig. 3D
PMID:18303049	PBO:0114305	Fig. 3B
PMID:18303049	PBO:0019301	Fig. 3A
PMID:18303049	PBO:0114310	Table 2
PMID:18303049	PBO:0114311	Table 2
PMID:18303049	PBO:0114312	Table 2
PMID:18303049	PBO:0114313	Fig. 6B
PMID:18303049	FYPO:0007743	Fig. 6C
PMID:18303049	PBO:0114314	Table 2
PMID:18303049	PBO:0114314	Table 2
PMID:18328707	PBO:0104856	Fig 1
PMID:18328707	PBO:0104865	GTP-bound Figure 4E
PMID:18328707	PBO:0104866	GTP-bound Figure 4E, polarization localization to both cell ends
PMID:18328707	PBO:0104858	Fig 1
PMID:18328707	PBO:0104860	Fig1SE to cell cortex of (newnon growing) cell tip from medial cortex
PMID:18328707	PBO:0104856	Fig 1
PMID:18328707	PBO:0104856	Fig 1
PMID:18328707	PBO:0096623	FigS1D
PMID:18328707	PBO:0104861	Fig1SE to cell cortex of (new) cell tip from medial cortex
PMID:18328707	PBO:0104861	Fig1SE to cell cortex of (new) cell tip from medial cortex
PMID:18328707	PBO:0104862	Fig 2C
PMID:18328707	PBO:0104858	Fig 1D (pom1 is catalytically active but not localized to cell ends)
PMID:18328707	PBO:0104857	Fig 1D
PMID:18328707	MOD:01455	fig 1D
PMID:18328707	PBO:0100644	Figure 3A
PMID:18328707	PBO:0104863	GTP bound
PMID:18328707	PBO:0020227	GTP bound active form
PMID:18328707	PBO:0103573	active GTP bound form
PMID:18328707	PBO:0104864	GTP bound fig 3C
PMID:18328707	FYPO:0000024	Figure 4E
PMID:18328707	PBO:0104858	Fig 1D
PMID:18328707	PBO:0104859	old end
PMID:18328707	PBO:0104868	*****OLD*****waiting for GO
PMID:18328707	GO:0005515	Figure 3B
PMID:18331722	PBO:0104195	in vitro assay
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 seques- ters 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:18337696	FYPO:0003118	at time 0. they don't look at nitrogen starvation for very long, only 60 mins
PMID:18344406	FYPO:0008161	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: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:0002061	However, every single repair mutant that we tested was synthetically sick in combination with hst4 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 hst4 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 hst4 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 hst4 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 hst4 when cells were grown on medium containing MMS (Fig. 3).
PMID:18344406	PBO:0093616	Interestingly, hst4 cells were sensitive to MMS and CPT (Fig. 1A)
PMID:18344406	FYPO:0002151	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2 and rad3 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 in- crease upon exposure to MMS (Fig. 2B).
PMID:18344406	FYPO:0002151	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2 and rad3 are shown in Fig. 2A
PMID:18344406	FYPO:0002151	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2 and rad3 are shown in Fig. 2A
PMID:18344406	FYPO:0000963	significantly sensitive to HU.
PMID:18344406	FYPO:0000502	Wild-type cells showed a peak of septation approximately 80 min after release, whereas the hst4 cells showed a delayed peak of septation at 120 min (see Fig. S2 in the supplemental material).
PMID:18344406	FYPO:0004928	Our fluorescence microscopic analysis also clearly indicated that a significant percentage of the hst4 cells in culture had fragmented DNA (see Fig. S1 in the sup- plemental material).
PMID:18344406	PBO:0093631	significantly sensitive to HU. less than that of wild-type cells but higher than that of checkpoint mutant rad3 cells (Fig. 1B).
PMID:18344406	FYPO:0002151	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2 and rad3 are shown in Fig. 2A
PMID:18344406	FYPO:0002151	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2 and rad3 are shown in Fig. 2A
PMID:18344406	FYPO:0001925	hst4 cells behaved as wild-type cells did and were able to survive exposure to gamma irradiation (Fig. 1C).
PMID:18344406	FYPO:0002060	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2 and rad3 are shown in Fig. 2A
PMID:18344406	FYPO:0002060	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2 and rad3 are shown in Fig. 2A
PMID:18344406	PBO:0093617	Interestingly, similar to the hst4 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:0093616	Interestingly, similar to the hst4 mutant, both K56R and K56Q mutants were sensitive to MMS and CPT.
PMID:18344406	FYPO:0003481	Like hst4 cells, both histone H3 mutant cells were very elongated, and a percentage of these cells exhibited abnormal DAPI staining (Fig. 7A).
PMID:18344406	PBO:0111114	Like hst4 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 hst4 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:0111111	If this signal is not generated, cells mutant go through the cell cycle with damage and eventually die.
PMID:18344406	FYPO:0002060	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2 and rad3 are shown in Fig. 2A
PMID:18344406	FYPO:0002060	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2 and rad3 are shown in Fig. 2A
PMID:18344406	PBO:0093613	Interestingly, hst4 cells were sensitive to MMS and CPT (Fig. 1A)
PMID:18344406	PBO:0093559	Both mutant strains were viable and able to grow at 32°C. However, like the hst4 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 hst4 strains were, indicating that Hst4 enzymatic activity was important for cells to be resistant to MMS.
PMID:18344406	FYPO:0007632	In the absence of Sir2, we observed elevated levels of histone H3 K9 and histone H4 K16, which was con- sistent with previous reports (17, 48).
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:0000871	In the absence of Sir2, we observed elevated levels of histone H3 K9 and histone H4 K16, which was con- sistent with previous reports (17, 48).
PMID:18344406	FYPO:0008160	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:18345014	PBO:0114331	Fig. 2A
PMID:18345014	GO:0140720	Fig. 1
PMID:18345014	GO:0005721	Fig. 1
PMID:18345014	PBO:0114329	Fig. 5D
PMID:18345014	PBO:0114329	Fig. 2A
PMID:18345014	PBO:0114330	Fig. 5D
PMID:18345014	PBO:0114331	Fig. 5D
PMID:18345014	GO:0033553	Fig. 1
PMID:18345014	GO:0033553	Fig. 1
PMID:18345014	PBO:0114482	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:0031934	Fig. 1
PMID:18345014	GO:0031934	Fig. 1
PMID:18345014	GO:0031934	Fig. 1
PMID:18345014	GO:0031934	Fig. 1
PMID:18345014	PBO:0114331	Fig. 5B
PMID:18345014	PBO:0114330	Fig. 5B
PMID:18345014	GO:0031934	Fig. 1
PMID:18345014	FYPO:0002355	Fig. 6A
PMID:18345014	GO:0140720	Fig. 1
PMID:18345014	PBO:0111016	Fig. 6A
PMID:18345014	GO:0140720	Fig. 1
PMID:18345014	PBO:0114339	Fig. 5B
PMID:18345014	PBO:0114329	Fig. 5B
PMID:18345014	PBO:0114334	Fig. 5C
PMID:18345014	PBO:0114334	Fig. 5A
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:0114333	Fig. 5C
PMID:18345014	FYPO:0002835	Fig. 2C
PMID:18345014	FYPO:0002836	Fig. 2C
PMID:18345014	PBO:0114335	Fig. 2B and D
PMID:18345014	PBO:0114334	Fig. 2B
PMID:18345014	PBO:0114333	Fig. 2B
PMID:18345014	PBO:0108529	Fig. 2B
PMID:18345014	PBO:0114332	Fig. 2A
PMID:18345014	PBO:0114330	Fig. 2A
PMID:18345014	PBO:0114333	Fig. 5A
PMID:18345014	PBO:0108531	Fig. 5A
PMID:18345014	PBO:0108529	Fig. 5A
PMID:18345014	FYPO:0008195	Fig. 4C
PMID:18345014	FYPO:0008195	Fig. 4C
PMID:18345014	PBO:0114340	Fig. 3B
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	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:0108531	Fig. S5
PMID:18345014	PBO:0108531	Fig. S5
PMID:18345014	PBO:0108531	Fig. S5
PMID:18345014	PBO:0108531	Fig. S5
PMID:18345014	FYPO:0002827	Fig. 2E
PMID:18345014	PBO:0108529	Fig. 5C
PMID:18345014	PBO:0114480	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:0114481	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:0114338	Fig. 2D
PMID:18345014	PBO:0114337	Fig. 2D
PMID:18345014	PBO:0114337	Fig. 2D
PMID:18345014	PBO:0114336	Fig. 2D
PMID:18345014	PBO:0114336	Fig. 2D
PMID:18345014	PBO:0114336	Fig. 2D
PMID:18378696	PBO:0093630	same as nbs1delta alone
PMID:18378696	PBO:0093586	same as either single mutant
PMID:18378696	PBO:0093586	same as nbs1delta alone
PMID:18378696	PBO:0093630	same as either single mutant
PMID:18378696	FYPO:0000089	same as nbs1delta alone
PMID:18378696	FYPO:0000088	same as nbs1delta alone
PMID:18378696	PBO:0093619	same as rad51delta alone
PMID:18378696	FYPO:0000089	same as either single mutant
PMID:18388861	FYPO:0003082	Fig. 5
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	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	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	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: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: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:0003612	The h90 exo1D mutant is viable. Fig. 2B. 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	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	PBO:0112927	The h90 rhp57D strain produces colonies with a mild defect in MT switching. Fig. 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: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	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	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	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:0000470	Table 1
PMID:18388861	FYPO:0000470	Table 1. Fig. 3C and D
PMID:18388861	FYPO:0000470	Table 1. Fig. 3C and D
PMID:18388861	PBO:0112927	None of the single helicase and essential topoisome- rase 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:0003612	Table 1, Fig. 3A, C and D
PMID:18388861	FYPO:0000316	Table 1. Fig. 3C and D
PMID:18388861	FYPO:0000316	Table 1. Fig. 3C and D
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:18388861	FYPO:0000316	Table 1
PMID:18388861	FYPO:0000316	Table 1
PMID:18388861	FYPO:0000316	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	Table 1
PMID:18388861	FYPO:0003082	Fig. 5
PMID:18388861	FYPO:0003082	Fig. 5
PMID:18391219	GO:0002143	"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:0000478	Fig. 3B
PMID:18397994	FYPO:0000346	Fig. 3A
PMID:18397994	PBO:0092176	Fig. 2B
PMID:18397994	PBO:0092330	Fig. 2A
PMID:18397994	GO:0032120	Fig. 5
PMID:18397994	FYPO:0000346	Fig. 6A
PMID:18397994	FYPO:0002708	Fig. 6A
PMID:18397994	FYPO:0002708	Fig. 6A
PMID:18397994	FYPO:0002708	Fig. 6A
PMID:18397994	PBO:0114353	Fig. 4
PMID:18397994	FYPO:0002708	Fig. 6A
PMID:18397994	GO:0005628	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	PBO:0114354	We found that Slk1 was also localized to the SPB during metaphase II and anaphase II. Fig. 7
PMID:18397994	FYPO:0002708	Fig. 8A
PMID:18397994	FYPO:0002708	Fig. 8A
PMID:18397994	FYPO:0002708	Fig. 8
PMID:18397994	FYPO:0002708	Fig. 8
PMID:18397994	FYPO:0000943	Fig. 9
PMID:18397994	FYPO:0000943	Fig. 9
PMID:18399988	PBO:0095423	they show transfer to a heterologous cytochrome p450 enzyme, but pombe doesn't have any mitochondrial ones.
PMID:18411246	PBO:0103896	(Fig. 3A)
PMID:18411246	FYPO:0004952	enclosure arrow in Figs 4Ci,ii)
PMID:18411246	FYPO:0001914	Fig. 5B
PMID:18411246	PBO:0103894	Fig. 2A
PMID:18411246	PBO:0103895	(Fig. 3A)
PMID:18411246	PBO:0023044	Fig. 2B
PMID:18414064	FYPO:0001387	same with or without TBZ
PMID:18414064	PBO:0098969	penetrance at 4 hours; increases upon longer time at restrictive temp
PMID:18414064	FYPO:0001387	same with or without TBZ
PMID:18414064	PBO:0098973	penetrance at 4 hours
PMID:18414064	PBO:0098974	penetrance at 4 hours
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	FYPO:0001660	git2-1 is effectively null, even though it isn't a complete deletion of the coding sequence
PMID:1849107	FYPO:0001869	git2-1 is effectively null, even though it isn't a complete deletion of the coding sequence
PMID:1849107	PBO:0103715	glycerol = derepressing for glucose repression also assayed using lacZ under fbp1 promoter (and maltose carbon source, also derepressing)
PMID:1849107	PBO:0103716	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103717	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103716	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103716	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103716	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103716	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103716	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103716	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103717	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103716	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103716	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103716	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103716	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103717	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103717	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103716	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103717	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103716	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103717	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103716	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103717	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103717	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103716	also assayed using lacZ under fbp1 promoter
PMID:1849107	PBO:0103717	also assayed using lacZ under fbp1 promoter
PMID:18493607	PBO:0094679	same as sir2+ overexpression alone
PMID:18493607	PBO:0093564	slighly more severe than sir2+ overexpression alone
PMID:18493607	PBO:0092751	present throughout mitotic cell cycle
PMID:18495844	PBO:0104278	Fig1B normal interphase MTs required to establish early orientation of mitotic spindle by aligning SPBs with long axis of cell
PMID:18495844	PBO:0104277	Fig1B
PMID:18495844	FYPO:0005691	Fig 2B
PMID:18495844	PBO:0104280	Fig3B,C
PMID:18495844	PBO:0104279	Fig3B
PMID:18495844	PBO:0104280	Fig3B,C As expected, the range of SPB trajectory angles was much wider than in wild-type cells (Fig. 2C, Fig. 3B,C
PMID:18495844	FYPO:0005691	Fig 2 A-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	PBO:0104281	Fig3B
PMID:18495844	PBO:0104278	Fig1B and 2B,C normal MTs required to establish early orientation of mitotic spindle by aligning SPBs with long axis of cell
PMID:18504300	PBO:0021460	Fig. 5
PMID:18504300	PBO:0099112	Fig. 5
PMID:18504300	PBO:0112312	Fig. 5
PMID:18504300	PBO:0112313	Fig. 5
PMID:18514516	PBO:0095386	same as either single mutant
PMID:18514516	PBO:0095390	same as either single mutant
PMID:18514516	PBO:0095386	same as either single mutant
PMID:18514516	PBO:0095390	same as either single mutant
PMID:18514516	PBO:0095386	same as either single mutant
PMID:18562692	FYPO:0006917	Fig. 6C
PMID:18562692	FYPO:0006917	Fig. 6C
PMID:18562692	FYPO:0006917	Fig. 6C
PMID:18562692	FYPO:0000324	Fig. 6C
PMID:18562692	FYPO:0000324	Fig. 6C
PMID:18562692	FYPO:0006917	Fig. 1
PMID:18562692	FYPO:0007388	Fig. 2
PMID:18562692	FYPO:0002022	Fig. 3
PMID:18562692	FYPO:0006917	Fig. 4
PMID:18562692	FYPO:0006917	Fig. 6C
PMID:18562692	FYPO:0001778	Fig. 5B
PMID:18562692	PBO:0099145	Fig. 5B
PMID:18562692	FYPO:0000324	Fig. 6C
PMID:18562692	PBO:0099146	Fig. 5A
PMID:18562692	PBO:0099147	Fig. 5A
PMID:18562692	FYPO:0000324	Fig. 1
PMID:18562692	FYPO:0007388	Fig. 2
PMID:18562692	FYPO:0000324	Table 1
PMID:18562692	FYPO:0000324	Fig. 5A
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:18562696	FYPO:0000583	Fig. 6B
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	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	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, Fig. 4F, Fig. 5A and B, Fig. 5E
PMID:18562696	PBO:0114363	Fig. 3D and E
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. 3G
PMID:18562696	PBO:0114363	Fig. 3G
PMID:18562696	PBO:0114363	Fig. 3F
PMID:18562696	PBO:0114363	Fig. 3F
PMID:18615848	FYPO:0002019	same as swi7-H4 alone, i.e. it's dominant
PMID:1863602	GO:0010515	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	in vitro
PMID:18653539	PBO:0096560	figure 1A, 8A
PMID:18653539	FYPO:0002060	figure 1A
PMID:18653539	FYPO:0003975	Fig 2 F during veg phase
PMID:18653539	FYPO:0006276	Fig. 1D, Fig. 1F
PMID:18653539	FYPO:0006275	Fig. 1D
PMID:18653539	FYPO:0004168	figure 8B
PMID:18653539	FYPO:0004168	figure 8B
PMID:18653539	FYPO:0004168	figure 8B
PMID:18653539	FYPO:0004168	figure 8B
PMID:18653539	FYPO:0006289	figure 2A
PMID:18653539	FYPO:0004695	figure 2A
PMID:18653539	FYPO:0005585	figure 2A
PMID:18653539	PBO:0096560	figure 1B
PMID:18653539	FYPO:0001673	figure 1 C
PMID:18658154	FYPO:0002567	nalysis revealed robust accumulation of the centromeric dg transcript in ers1 cells (Fig. 2A).
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-independ- ent silencing mechanisms.
PMID:18658154	FYPO:0007334	ers1 mutant is completely defective in the silencing of ura4
 genes placed in the inner or outer repeats of cen1.
PMID:18658154	FYPO:0003744	As shown in Fig. 1C, recruitment of RITS to both sites was abolished in ers1 cells.
PMID:18658154	FYPO:0000890	We found that ers1 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:0000878	We found that ers1 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:0006076	We observed an apparently complete defect in siRNA production (Fig. 2B).
PMID:18658154	FYPO:0000884	We found that ers1 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:0000888	We found that ers1 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:0003555	no defect in silencing of ura4
 reporter genes placed at mat3M or tel2R, where RNAi- dependent mechanisms act redundantly with RNAi-independ- ent silencing mechanisms.
PMID:18662319	GO:0034634	also L-gamma-glutamyl-L-cysteine
PMID:18667531	FYPO:0001234	synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81 (Figure 2, C and D).
PMID:18667531	FYPO:0002061	synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81 (Figure 2, C and D).
PMID:18667531	PBO:0104010	The Nse1-Nse3 interaction is not perturbed by dele- tion 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	PBO:0093556	The 􏰂RING, C197A, C199A, and C197A/C199A mutants were mildly temperature sensi- tive 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 sensi- tive 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 sensi- tive 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 sensi- tive 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 sensi- tive 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 sensi- tive but grew normally at 25°C (Figure 2A and data not shown)
PMID:18667531	FYPO:0000674	The C219A mutant was not temperature sensitive (Figure 2A).
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:0004329	nulcleolus inheritance
PMID:18667531	FYPO:0001234	synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81 (Figure 2, C and D).
PMID:18667531	FYPO:0002061	synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81 (Figure 2, C and D).
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	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:0000268	fig 4 a
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: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	FYPO:0000268	fig 4 a
PMID:18676809	PBO:0105612	Conversely, mutations disrupting dimerization did not disrupt -H2A.1 binding (Fig. 3C).
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 4 a
PMID:18676809	FYPO:0000085	fig 4 a
PMID:18676809	FYPO:0000085	fig 4 a
PMID:18676809	FYPO:0000268	fig 4 a
PMID:18676809	FYPO:0000088	fig 4 a
PMID:18676809	FYPO:0000006	fig 4 a
PMID:18676809	FYPO:0000088	fig 4 a
PMID:18676809	FYPO:0000088	fig 4 a
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:18716626	PBO:0096735	figure 1g 30% cells?
PMID:18716626	PBO:0112511	(Fig. 2a, b) As with sgo1D cells, swi6D cells undergo intact meiosis I but suffer a nondisjunction of sister chromatids in meiosis II
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: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, f) 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-defect- ive 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	FYPO:0003182	(Fig. 2a, b) As with sgo1D cells, swi6D cells undergo intact meiosis I but suffer a nondisjunction of sister chromatids in meiosis II
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	PBO:0096739	(Fig. 2e) Sgo1 localization is impaired in swi6D cells
PMID:18716626	PBO:0096740	(Fig. 2f) Sgo1–CD did indeed localize at the centromere regardless of swi6D
PMID:18716626	PBO:0112512	(Fig. 2a, b) As with sgo1D cells, swi6D cells undergo intact meiosis I but suffer a nondisjunction of sister chromatids in meiosis II
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: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	PBO:0112512	(Fig. 2a, b) 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	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: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: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:18769921	FYPO:0004437	during vegetative growth because non-sporulating strains used
PMID:18769921	FYPO:0000473	during vegetative growth because non-sporulating strains used
PMID:18769921	FYPO:0001839	during vegetative growth because non-sporulating strains used
PMID:18769921	FYPO:0001839	during vegetative growth because non-sporulating strains used
PMID:18769921	PBO:0093618	slightly more sensitive at low temperature than standard
PMID:18769921	FYPO:0001386	during vegetative growth because non-sporulating strains used
PMID:18769921	PBO:0093631	slightly worse than sfr1delta alone
PMID:18794373	FYPO:0007206	arrest at Ter2 and Ter3 sites abolished
PMID:18794373	FYPO:0007206	arrest at Ter2 and Ter3 sites abolished
PMID:18794373	FYPO:0007206	arrest at Ter2 and Ter3 sites abolished
PMID:18794373	FYPO:0007206	arrest at Ter2 and Ter3 sites abolished
PMID:18794373	GO:0110035	binds at Ter3 site
PMID:18794373	FYPO:0007206	arrest at Ter2 and Ter3 sites abolished
PMID:18794373	FYPO:0007206	arrest at Ter2 and Ter3 sites abolished
PMID:18809570	FYPO:0002360	Fig. 5A
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:0112679	Fig. 4D
PMID:18809570	PBO:0111115	Fig. 4D
PMID:18809570	PBO:0112679	Fig. 4D
PMID:18809570	PBO:0095652	Fig. 8H
PMID:18809570	PBO:0098583	Fig. 5A
PMID:18809570	PBO:0098583	Fig. 5A
PMID:18809570	PBO:0108390	Fig. 5A
PMID:18809570	PBO:0111587	Fig. 5A
PMID:18809570	PBO:0111587	Fig. 5A
PMID:18809570	PBO:0095651	Fig. 5B
PMID:18809570	PBO:0095651	Fig. 5B
PMID:18809570	PBO:0112680	Fig. 7B
PMID:18809570	PBO:0112681	Fig. 7A
PMID:18809570	GO:0005721	Fig. 7A
PMID:18809570	GO:0140720	Fig. 7A
PMID:18809570	GO:0031934	Fig. 7A
PMID:18809570	PBO:0111014	Fig. 7A
PMID:18809570	PBO:0112682	Fig. 7A
PMID:18809570	PBO:0101110	Fig. 7B
PMID:18809570	GO:0005721	Fig. 7B
PMID:18809570	GO:0140720	Fig. 7B
PMID:18809570	GO:0031934	Fig. 7B
PMID:18809570	PBO:0095651	Fig. 8D
PMID:18809570	PBO:0095653	Fig. 8D
PMID:18809570	PBO:0095652	Fig. 8D
PMID:18809570	PBO:0095653	Fig. 8D
PMID:18809570	PBO:0095652	Fig. 8H
PMID:18809570	PBO:0095653	Fig. 1B and C
PMID:18809570	PBO:0095651	Fig. 1B and C
PMID:18809570	PBO:0095651	Fig. 1D
PMID:18809570	FYPO:0002336	Fig. 1D
PMID:18809570	PBO:0095651	Fig. 1D
PMID:18809570	PBO:0095652	Fig. 1E
PMID:18809570	PBO:0112671	Fig. 2C
PMID:18809570	PBO:0112672	Fig. 2D
PMID:18809570	PBO:0095653	Fig. 2E
PMID:18809570	PBO:0095652	Fig. 2G
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:0112673	Fig. 4A
PMID:18809570	PBO:0112674	Fig. 4A
PMID:18809570	PBO:0109218	Fig. 4A
PMID:18809570	PBO:0112675	Fig. 4A
PMID:18809570	PBO:0112676	Fig. 4A
PMID:18809570	PBO:0112676	Fig. 4A
PMID:18809570	PBO:0112677	Fig. 4D
PMID:18809570	PBO:0112678	Fig. 4D
PMID:18809570	PBO:0111115	Fig. 4D
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 initi- ation events mediated by Atf1 is essential to convert chromatin to an RNAPII accessible state (Fig. 4B).
PMID:18820678	PBO:0111102	In the atf1- mutant, transcripts a and b are expressed normally, whereas tran- scripts c and d are absent (Fig. 4A).
PMID:18820678	PBO:0111103	In the atf1- mutant, transcripts a and b are expressed normally, whereas tran- scripts c and d are 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	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	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	FYPO:0008156	Expression of transcript c is not restored in the atf12tup112tup122 mutant, sug- gesting that Atf1 is essential to induce transcript c.
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:0111104	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 atf1- mutant, transcripts a and b are expressed normally, whereas tran- scripts c and d are absent (Fig. 4A).
PMID:18820678	PBO:0111101	In the atf1- mutant, transcripts a and b are expressed normally, whereas tran- scripts c and d are absent (Fig. 4A).
PMID:18849471	GO:0004585	qualifier=major
PMID:18854158	PBO:0100306	abolished interaction between wt and mutant; interaction partially restored if both copies are mutant
PMID:18854158	FYPO:0000267	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	FYPO:0000268	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	FYPO:0000268	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	FYPO:0000267	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	FYPO:0000085	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	FYPO:0000085	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	FYPO:0000268	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	FYPO:0000267	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	FYPO:0000085	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	FYPO:0000268	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	FYPO:0000267	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	FYPO:0000085	no extension because growth is decreased generally, making expressivity hard to judge
PMID:18854158	PBO:0100306	abolished interaction between wt and mutant; interaction partially restored if both copies are mutant
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	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: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	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:0003097	(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: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: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: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	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: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: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	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	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: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: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:18951025	PBO:0106929	one or more of mutated serine residues
PMID:18951025	PBO:0106929	one or more of mutated serine residues
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:0003682	GFP-Lid2 is resistant to detergent extraction indicating Lid2 is a chromatin-binding protein (Figure 2A).
PMID:18957202	PBO:0096189	ilencing 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	ilencing 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:0105543	As shown in Figure 5C, siRNA is barely detectable.
PMID:18957202	PBO:0096189	ilencing 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	FYPO:0000874	overexpressing Lid2 enhances H3K9 methylation (Figures 5G and H)
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	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	PBO:0101470	Figure 1A
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	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:0105541	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:0105541	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:0094673	drastic reduction of Swi6 binding (Figure 3D).
PMID:18957202	PBO:0105548	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	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	PBO:0105544	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:0103965	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	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	GO:0005634	Figure 2A
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	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	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	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:0105545	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	FYPO:0003481	WT and frequently exhibited an aberrant elongated cell shape (Figure 2C)
PMID:18957202	PBO:0093562	As shown in Figure 2E, lid2-j, like clr8Δ, is hypersensitive to TBZ
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	PBO:0105540	28% of the cells contained fragmented nuclear DNA (Figure 2D), indicating that the mutant nucleus is disorganized.
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	FYPO:0002151	tetrad analysis. 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:1899284	GO:0001228	also supported by complementation of S.c. deletion
PMID:19001497	PBO:0098084	supplementary material Fig. S1)
PMID:19001497	PBO:0098085	fig 4 F
PMID:19001497	PBO:0098086	fig 1 D
PMID:19001497	PBO:0098086	fig 1 D, 1 E
PMID:19001497	PBO:0098086	fig 1 D, 1 E
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	GO:0044732	fig 2 BC
PMID:19001497	PBO:0098075	fig 2 a (this fig also has expression level for mutant alleles)
PMID:19001497	FYPO:0004619	supplementary material Movies 2-4).
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:19001497	FYPO:0004511	Fig 1 E
PMID:19001497	FYPO:0004511	Fig 1 E
PMID:19001497	FYPO:0004511	Fig 1 E
PMID:19001497	PBO:0098074	fig 1 D, 1 E
PMID:19001497	PBO:0036769	fig 1 D, 1 E
PMID:19001497	PBO:0036769	fig 1 D, 1 E
PMID:19001497	PBO:0036769	fig 1 D
PMID:19001497	PBO:0019206	fig 1 C
PMID:19001497	PBO:0019223	fig 1 C
PMID:19001497	PBO:0019206	fig 1 C
PMID:19001497	PBO:0019206	fig 1 C
PMID:19001497	FYPO:0005696	Fig4D
PMID:19001497	PBO:0098083	Fig4c
PMID:19001497	FYPO:0002112	Fig4c
PMID:19001497	PBO:0098082	Fig4a
PMID:19001497	PBO:0098081	fig3
PMID:19001497	PBO:0098081	fig3
PMID:19001497	PBO:0098080	fig3
PMID:19001497	PBO:0094143	Fig 2 D-F
PMID:19001497	PBO:0094143	Fig 2 D-F
PMID:19001497	PBO:0098079	Fig 2 D-F
PMID:19001497	PBO:0098078	Fig 2 D-F
PMID:19001497	PBO:0098078	Fig 2 D-F
PMID:19001497	PBO:0098077	Fig 2 D-F
PMID:19001497	PBO:0094146	Fig 2 D-F
PMID:19001497	PBO:0094146	Fig 2 D-F
PMID:19001497	PBO:0098076	Fig 2 D-F
PMID:19001497	PBO:0098076	Fig 2 D-F
PMID:19001497	GO:0031021	fig 2 BC
PMID:19001497	GO:0000923	fig 2 BC
PMID:19001497	FYPO:0005699	Fig4D
PMID:19001497	FYPO:0005696	Fig 1 E
PMID:19001497	PBO:0098084	supplementary material Fig. S1)
PMID:19001497	PBO:0098085	fig 4 F
PMID:19023408	FYPO:0005136	Southern blot
PMID:19023408	GO:0035861	ChIP
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:19023408	FYPO:0005911	Southern blot
PMID:19023408	FYPO:0005136	microarray
PMID:19023408	FYPO:0005136	Southern blot
PMID:19023408	FYPO:0005911	Southern blot
PMID:19026779	PBO:0107732	Figure 4D
PMID:19026779	PBO:0107730	Figure 4D
PMID:19026779	PBO:0107731	Figure 4D
PMID:19026779	PBO:0112758	Figure 4D
PMID:19026779	PBO:0107734	Figure 4D
PMID:19026779	PBO:0107730	Figure 4D
PMID:19026779	PBO:0107730	Figure 4D
PMID:19026779	PBO:0107732	Figure 4D
PMID:19026779	PBO:0107733	Figure 4D
PMID:19026779	PBO:0107733	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:0107730	Figure 4D
PMID:19026779	PBO:0107732	Figure 4D
PMID:19026779	PBO:0107730	Figure 4D
PMID:19026779	PBO:0094855	Figure 4D
PMID:19026779	PBO:0107733	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:0107730	Figure 4D
PMID:19026779	PBO:0107732	Figure 4D
PMID:19026779	PBO:0107730	Figure 4D
PMID:19026779	PBO:0107730	Figure 4D
PMID:19026779	PBO:0107732	Figure 4D
PMID:19033384	PBO:0100016	Use of Western blot to assay phosphorylation levels GO:0071494= cellular response to UVC GO:1990253 = cellular response to leucine starvation (TG freeform submission) GO:0070301 = cellular repsonse to H2O2
PMID:19033384	PBO:0021985	Use of Western blot to assay phosphorylation levels GO:0071494= cellular response to UVC GO:1990253 = cellular response to leucine starvation (TG freeform submission) GO:0070301 = cellular repsonse to H2O2
PMID:19033384	PBO:0021987	Use of Western blot to assay phosphorylation levels GO:0071494= cellular response to UVC GO:1990253 = cellular response to leucine starvation (TG freeform submission) GO:0070301 = cellular repsonse to H2O2
PMID:19033384	PBO:0033378	Use of Western blot to assay phosphorylation levels GO:0071494= cellular response to UVC GO:1990253 = cellular response to leucine starvation (TG freeform submission) GO:0070301 = cellular repsonse to H2O2
PMID:19033384	PBO:0021984	Use of Western blot to assay phosphorylation levels GO:0071494= cellular response to UVC GO:1990253 = cellular response to leucine starvation (TG freeform submission) GO:0070301 = cellular repsonse to H2O2
PMID:19033384	PBO:0033377	Use of Western blot to assay phosphorylation levels GO:0071494= cellular response to UVC GO:1990253 = cellular response to leucine starvation (TG freeform submission) GO:0070301 = cellular repsonse to H2O2
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:19033384	PBO:0033376	Use of Western blot to assay phosphorylation levels GO:0071494= cellular response to UVC GO:1990253 = cellular response to leucine starvation (TG freeform submission) GO:0070301 = cellular repsonse to H2O2
PMID:19033384	PBO:0021986	Use of Western blot to assay phosphorylation levels GO:0071494= cellular response to UVC GO:1990253 = cellular response to leucine starvation (TG freeform submission) GO:0070301 = cellular repsonse to H2O2
PMID:19037096	GO:0008574	Figure 4, A and B, and Supplemen- tal Movie S1
PMID:1905818	FYPO:0000280	haploid, either mating type
PMID:1905818	GO:0003924	(changed to GTPase from signal transducer)
PMID:19075108	PBO:0112551	Fig. 2B and C
PMID:19075108	FYPO:0008204	Fig. 2 and 3
PMID:19075108	FYPO:0008204	Fig. 2 and 3
PMID:19075108	FYPO:0006005	Fig. 2B
PMID:19075108	PBO:0112551	Fig. 2B and C
PMID:19075108	PBO:0112548	Fig. 2A and C
PMID:19075108	PBO:0112554	These results furthered the notion that the function of Mid1p and corti- cal nodes was important for organization of normal actomy- osin rings in early mitosis.
PMID:19075108	PBO:0112551	Fig. 2B and C
PMID:19075108	PBO:0112549	Fig. 2A and C
PMID:19075108	FYPO:0007827	Fig. 5D
PMID:19075108	PBO:0112553	Fig. 5A, B and C
PMID:19075108	PBO:0112545	Fig. 1A
PMID:19075108	PBO:0112544	Fig. 1A
PMID:19075108	PBO:0112543	Fig. 1A
PMID:19075108	PBO:0112548	Fig. 2A and C
PMID:19075108	PBO:0112550	Fig. 2B and C
PMID:19075108	PBO:0112550	Fig. 2B and C
PMID:19075108	PBO:0112552	Fig. 4
PMID:19075108	FYPO:0007827	Fig. 5D
PMID:19075108	PBO:0112550	Fig. 2B and C
PMID:19075108	PBO:0112551	Fig. 2B and C
PMID:19075108	PBO:0112546	Fig. 1A
PMID:19075108	PBO:0112550	Fig. 2B and C
PMID:19075108	PBO:0112547	Fig. 2A and C
PMID:19111658	GO:0003723	binds centromeric transcripts
PMID:19117951	FYPO:0001234	mat1Msmto REIIdelta mat2::ura4
PMID:19117951	FYPO:0001886	mat1Msmto REIIdelta mat2::ura4
PMID:19117951	FYPO:0000156	mat1Msmto REIIdelta mat2::ura4 gave dark staining with iodine, metastable and switch to the opposite state at a low rate
PMID:19117951	FYPO:0002355	mat1Msmto REIIdelta mat2::ura4
PMID:19117951	PBO:0108056	heterochromatin
PMID:19117951	PBO:0108055	mat1Msmto REIIdelta mat2::ura4
PMID:19117951	PBO:0098599	mat1Msmto REIIdelta mat2::ura4
PMID:19117951	FYPO:0002346	mat1Msmto REIIdelta mat2::ura4
PMID:19117951	FYPO:0000156	gave dark staining with iodine,switch to the opposite state at a low rate
PMID:19117951	FYPO:0000156	gave dark staining with iodine,switch to the opposite state at a low rate
PMID:19117951	FYPO:0000877	mat1Msmto REIIdelta mat2::ura4
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	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:0097399	Similarly, H3K9me on Kint2::ura4 was diminished in dcr1Dckb1D but still retained in atf1Dckb1D cells (Fig. 1D). T
PMID:19136623	PBO:0111989	Similarly, H3K9me on Kint2::ura4 was diminished in dcr1Dckb1D but still retained in atf1Dckb1D cells (Fig. 1D). T
PMID:19136623	GO:0090055	Therefore, Clr3 and Ckb1 function similarly in Atf1/Pcr1-dependent heterochromatin formation at the mating locus.
PMID:19136623	GO:0030466	Therefore, Clr3 and Ckb1 function similarly in Atf1/Pcr1-dependent heterochromatin formation at the mating locus.
PMID:19136623	PBO:0092711	Similarly, CK2 efficiently phos- phorylated bacteria-prepared Swi6 in a Ckb1-dependent manner, resulting in slower migrating bands in SDS- PAGE (Fig. 2C).
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 path- way (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 path- way (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:19136623	PBO:0112915	Similarly, Clr3 and Mit1 localization was decreased in ckb1D and swi6-S18-117A mutants, al- though 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, al- though 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, al- though 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, al- though 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	PBO:0113571	whereas mutant Swi6 harboring S18A and S24A showed a slight mobility change,
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	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:19139265	PBO:0102283	fig8
PMID:19139265	PBO:0096679	fig9
PMID:19139265	FYPO:0002061	Fig. S5
PMID:19139265	FYPO:0002061	Fig. S5
PMID:19150433	PBO:0094912	covalent binding between topoisomerase and DNA
PMID:19150433	PBO:0094913	covalent binding between topoisomerase and DNA
PMID:19150433	PBO:0094916	covalent binding between topoisomerase and DNA
PMID:19150433	PBO:0094913	covalent binding between topoisomerase and DNA
PMID:19150433	PBO:0094912	covalent binding between topoisomerase and DNA
PMID:19150433	PBO:0094913	covalent binding between topoisomerase and DNA
PMID:19150433	PBO:0094915	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	"closest we can get to ""at stalled fork"" with available terms"
PMID:19164572	PBO:0112540	Fig. 4B
PMID:19164572	PBO:0112527	Table S1
PMID:19164572	FYPO:0008203	Fig. 1G
PMID:19164572	FYPO:0006299	Fig. 2A
PMID:19164572	FYPO:0000887	Fig. 2B
PMID:19164572	FYPO:0000863	Fig. 1F
PMID:19164572	PBO:0112519	Fig. 1E
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:0112520	Fig. 1H
PMID:19164572	PBO:0112522	Table S1
PMID:19164572	PBO:0112521	Table S1
PMID:19164572	PBO:0112523	Table S1
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:0112530	Table S1
PMID:19164572	PBO:0112529	Table S1
PMID:19164572	PBO:0112528	Table S1
PMID:19164572	PBO:0112538	Fig. 2C
PMID:19164572	PBO:0112518	Fig. 1D
PMID:19164572	PBO:0112517	Fig. 1C
PMID:19164572	PBO:0112524	Table S1
PMID:19164572	FYPO:0003412	Fig. 2A
PMID:19164572	PBO:0112539	Fig. 3
PMID:19164572	PBO:0112525	Table S1
PMID:19164572	FYPO:0003412	Fig. 2A
PMID:19164572	PBO:0112526	Table S1
PMID:19164572	PBO:0112516	Fig. 1B
PMID:19185548	GO:0000724	qualifier=different_pathway
PMID:19185548	GO:0000724	qualifier=different_pathway
PMID:19189958	FYPO:0002061	Figue 5B As expected for the rgf31 shut-off, the cells died in the presence of thiamine (promoter off).
PMID:19189958	FYPO:0002061	Figue 5B As expected for the rgf31 shut-off, the cells died in the presence of thiamine (promoter off).
PMID:19189958	FYPO:0002060	Figue 5B How- ever, 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	FYPO:0000590	Figure 2
PMID:19189958	PBO:0102195	Figure 2b
PMID:19189958	PBO:0102196	Figure 2A
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:0007905	Figure 3A
PMID:19189958	PBO:0102202	47% of cells
PMID:19189958	PBO:0102203	10% of cells
PMID:19189958	FYPO:0007436	cells were larger than wild-type cells and displayed multiple abnormal septa.
PMID:19189958	GO:0140748	"Figure 3 ""This result indicates that Rgf2p is in- volved 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	PBO:0102197	Figure 4c positive
PMID:19189958	PBO:0102196	Figure 2A
PMID:19189958	FYPO:0002060	Figue 5B How- ever, their growth was rescued in the presence of sorbitol
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	PBO:0102196	Figure 2A
PMID:19189958	GO:0005632	Figure 3B
PMID:19189958	PBO:0102198	the amount of active Rho1p increased considerably in the strain over- expressing Rgf2p as compared with the wild-type strain (Figure 4B
PMID:19189958	FYPO:0000478	Figure 2A
PMID:19189958	FYPO:0004927	Figure 2A
PMID:19189958	FYPO:0000121	Figure 2
PMID:19189958	FYPO:0002177	Asexpected,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: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	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	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: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	FYPO:0002060	Figure 5B viable and phenotypically in- distinguishable from the ehs2-1 mutant
PMID:19202278	FYPO:0002447	absent beta 1,3 gal
PMID:19202289	GO:0032120	(Fig. 2B)
PMID:19202289	GO:0032120	(Fig. 3B)
PMID:19202289	GO:0032120	(Fig. 3B)
PMID:19202289	FYPO:0000590	(Fig. 3A and B)
PMID:19202289	FYPO:0000590	(Fig. 3A and B)
PMID:19202289	FYPO:0002060	(Fig. 3C)
PMID:19202289	FYPO:0002060	(Fig. 3C)
PMID:19202289	GO:0005628	(Fig. 2D)
PMID:19202289	GO:0005886	(Fig. 2D)
PMID:19202289	FYPO:0000307	(Fig. 2B)
PMID:19202289	FYPO:0003905	(data not shown).
PMID:19202289	FYPO:0002061	Fig. 1B
PMID:19202289	FYPO:0003798	Fig. 1B
PMID:19202289	FYPO:0003563	Fig. 1B
PMID:19202289	FYPO:0003563	Fig. 1A
PMID:19202289	FYPO:0000121	Fig. 1A
PMID:19205745	PBO:0093561	temp semi-permissive for pol1-1 alone
PMID:19205745	PBO:0093581	temp semi-permissive for cdc6-23 alone
PMID:19205745	PBO:0093561	temp semi-permissive for cdc6-23 alone
PMID:19205745	PBO:0093561	temp semi-permissive for cdc20-M10 alone
PMID:19205745	PBO:0093581	temp semi-permissive for cdc6-23 alone
PMID:19205745	PBO:0093561	temp semi-permissive for cdc6-23 alone
PMID:19214192	PBO:0105817	present in late S, as late as pols alpha & delta
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
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 S phase
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 late S phase
PMID:19214192	PBO:0105817	present in late S
PMID:19214192	GO:0140445	present at roughly constant level throughout cell cycle
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
PMID:19217404	FYPO:0003740	abolished, fig1 d
PMID:19217404	FYPO:0003740	abolished, fig1 d
PMID:19217404	FYPO:0003740	abolished, fig1 d
PMID:19217404	FYPO:0003740	abolished, fig1 d
PMID:19217404	FYPO:0003740	abolished, fig1 d
PMID:19217404	PBO:0099221	fig S10
PMID:19217404	FYPO:0003740	abolished, fig1 d
PMID:19250904	PBO:0093619	same as either single mutant
PMID:19250904	PBO:0093629	same as either single mutant
PMID:19250904	PBO:0093619	same as either single mutant
PMID:19250904	PBO:0093629	same as either single mutant
PMID:19250904	PBO:0093619	same as either single mutant
PMID:19250904	PBO:0093629	same as either single mutant
PMID:19250904	PBO:0093629	same as either single mutant
PMID:19250904	PBO:0093619	same as either single mutant
PMID:19250904	PBO:0093630	same as either single mutant
PMID:19250904	PBO:0093620	same as either single mutant
PMID:19250904	GO:0042393	assayed using purified HeLa histone octamers
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 ac- tivity 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:19279143	PBO:0105388	fig 4F
PMID:19279143	PBO:0105387	fig 4F
PMID:19279143	PBO:0105385	"""Thus, Nrd1 di- rectly binds with Cdc4 mRNA in vivo and in vitro"""
PMID:19328067	PBO:0095887	(All at eng2 CDS)
PMID:19328067	PBO:0103633	"Mcs6 ""primes"" Rpb1 for phosphorylation by cdk9"
PMID:19328067	PBO:0095887	(All at eng2 CDS)
PMID:19328067	PBO:0114260	positive regulation
PMID:19328067	PBO:0103629	(All at eng2 CDS)
PMID:19328067	PBO:0103631	(All at eng2 CDS)
PMID:19328067	PBO:0103630	(All at eng2 CDS)
PMID:19330768	FYPO:0000802	in arrested cells, indicating independent of cell cycle progression
PMID:19330768	FYPO:0000141	G1 temperature shift
PMID:19330768	FYPO:0004588	G2 temperature shift
PMID:1934126	FYPO:0000681	same as cdc25-22 single mutant
PMID:1934126	FYPO:0000681	same as cdc25-22 single mutant
PMID:1934126	FYPO:0000681	same as cdc25-22 single mutant
PMID:1934126	FYPO:0000681	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: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	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	FYPO:0004742	+ . In contrast, the F61Achp1; F276Aago1 mutant strain showed no defect in the silencing of the reporter (Figure 4D).
PMID:19362535	FYPO:0007334	d loss of maintenance of heterochromatin was seen in cells expressing both Tas3WG and E23Vchp1, unlike cells expressing either single mutant
PMID:19362535	FYPO:0007334	d loss of maintenance of heterochromatin was seen in cells expressing both Tas3WG and E23Vchp1, unlike cells expressing either single mutant
PMID:19362535	FYPO:0007334	d loss of maintenance of heterochromatin was seen in cells expressing both Tas3WG and E23Vchp1, unlike cells expressing either single mutant
PMID:19362535	FYPO:0004742	d loss of maintenance of heterochromatin was seen in cells expressing both Tas3WG and E23Vchp1, unlike cells expressing either single mutant
PMID:19362535	PBO:0111400	******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	*******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	*******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	*******reassembly/nucleation********* 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	*******reassembly/nucleation********* 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	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	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	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: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	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: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	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: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	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	FYPO:0004201	. 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: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	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: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	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: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	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	PBO:0112174	TheSwi6 V82E mutant bound H3K9me2 with 5-fold higher affinity than wild-type Swi6 (Table 1; Figure S2A),
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: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: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: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	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:0112171	*A third class showed a more profound reduction in binding affinity: the E23V,V24M mutant reduced binding affinity 40 fold,
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: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	PBO:0111583	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: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:0111584	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:0111582	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	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: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: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: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: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:0002150	Figure 5
PMID:19363481	FYPO:0001234	Figure 5
PMID:19363481	GO:0005515	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:19366728	FYPO:0006518	fragmented
PMID:19366728	FYPO:0006518	fragmented
PMID:19366728	FYPO:0006518	fragmented
PMID:19366728	FYPO:0006518	fragmented
PMID:19366728	FYPO:0006518	fragmented
PMID:19366728	FYPO:0006518	fragmented
PMID:19366728	FYPO:0006518	fragmented
PMID:19366728	FYPO:0006518	fragmented
PMID:19366728	FYPO:0006518	fragmented
PMID:19366728	FYPO:0006518	fragmented
PMID:19366728	FYPO:0006518	fragmented
PMID:19366728	FYPO:0006518	fragmented
PMID:19366728	FYPO:0006518	fragmented
PMID:19373772	PBO:0019716	during mitotic M phase?
PMID:19373772	PBO:0019715	"happens during mitotic M phase? term will be renames ""mitochondrial membrane fission"""
PMID:19373772	PBO:0019714	"happens during mitotic M phase? term will be renames ""mitochondrial membrane fission"""
PMID:19373772	FYPO:0000251	non fermentable carbon source
PMID:19394293	FYPO:0003411	Figure 3.
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	FYPO:0003411	Figure 3. tas3-TAM Mutations Cause a Dramatic Loss of ura4+ Silencing at imr1 but Only a Modest Loss at otr1 (A) Schematic diagram of S. pombe centromere (cen) 1. The
PMID:19394293	PBO:0101404	(Figure 3C).
PMID:19394293	PBO:0101404	(Figure 3C).
PMID:19394293	PBO:0101404	(Figure 3C).
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: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: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:0003411	Figure 3. tas3-TAM Mutations Cause a Dramatic Loss of ura4+ Silencing at imr1 but Only a Modest Loss at otr1 (A) Schematic diagram of S. pombe centromere (cen) 1. The
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 (A) Schematic diagram of S. pombe centromere (cen) 1. The
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 (A) Schematic diagram of S. pombe centromere (cen) 1. The
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	FYPO:0001355	figure 5A
PMID:19417105	PBO:0102568	(Supplemental Table S1).
PMID:19417105	GO:0018444	figure 1
PMID:19417105	PBO:0102568	(Supplemental Table S1).
PMID:19417105	PBO:0102566	(Supplemental Table S1).
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	PBO:0102566	Supplemental Table S1; Supplemental Fig. S3
PMID:19417105	PBO:0102566	Supplemental Table S1; Supplemental Fig. S3
PMID:19417105	PBO:0102567	(Supplemental Table S1).
PMID:19417105	FYPO:0001645	(Fig. 5B)
PMID:19417105	FYPO:0001645	(Fig. 5B)
PMID:19417105	PBO:0102566	(Supplemental Table S1).
PMID:19417105	FYPO:0001645	(Fig. 5B)
PMID:19417105	FYPO:0001355	figure 5A
PMID:19417105	FYPO:0002061	figure 5A
PMID:19417105	PBO:0102566	(Supplemental Table S1).
PMID:19417105	PBO:0102566	(Supplemental Table S1).
PMID:19422421	FYPO:0001357	actually 25 degrees, but calling it low to make distinction from inviable at 30
PMID:19422421	PBO:0093616	25 degrees (permissive for hsk1-89)
PMID:19422421	FYPO:0002061	30 degrees
PMID:19422421	PBO:0093631	25 degrees, but calling it low to make distinction from inviable at 30
PMID:19422421	PBO:0093581	25 degrees, but calling it low to make distinction from inviable at 30
PMID:19422421	PBO:0093580	25 degrees (permissive for hsk1-89)
PMID:19422421	PBO:0093617	25 degrees, but calling it low to make distinction from inviable at 30
PMID:19422421	PBO:0093629	25 degrees (permissive for hsk1-89)
PMID:19422421	PBO:0103154	actually 25 degrees, but calling it low to make distinction from inviable at 30
PMID:19422421	PBO:0103155	actually 25 degrees, but calling it low to make distinction from inviable at 30
PMID:19422421	PBO:0093559	25 degrees (permissive for hsk1-89)
PMID:19422421	PBO:0093580	25 degrees (permissive for hsk1-89)
PMID:19422421	PBO:0093616	25 degrees (permissive for hsk1-89)
PMID:19422421	PBO:0093561	25 degrees (permissive for hsk1-89)
PMID:19422421	GO:0000785	increased chromatin association in presence of HU
PMID:19427212	GO:1902408	Fig. 4
PMID:19427212	PBO:0112457	We conclude that fission yeast cytokinesis uses two over- lapping 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:0112456	Fig. 3C and D
PMID:19427212	PBO:0112455	Fig. 3C and D
PMID:19427212	PBO:0112454	Fig. 3C and D
PMID:19427212	PBO:0112449	Fig. 3B
PMID:19427212	PBO:0112449	Fig. 3B
PMID:19427212	PBO:0112453	Fig. 3A
PMID:19427212	PBO:0112452	Fig. 2D
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:19430462	GO:0036450	urg1, gar2, act1, adh1, pof9 and hcn1 mRNAs were shown to be direct targets by cRACE sequence analysis.
PMID:19430466	PBO:0104402	Fig. 1f ATP-dependent Supplementary Information, Movie 1)
PMID:19430466	GO:0005872	homodimer
PMID:19430466	PBO:0104404	Fig. 2j
PMID:19430466	PBO:0104403	Fig. 2d, lane 4
PMID:19430466	PBO:0104404	Fig. 2j
PMID:19430466	GO:0008017	Fig. 2c
PMID:19431238	GO:0005938	ocalization independent of actin cytoskeleton (assayed using latrunculin A) and microtubule cytoskeleton (assayed using carbendazim)
PMID:19431238	GO:0051285	ocalization independent of actin cytoskeleton (assayed using latrunculin A) and microtubule cytoskeleton (assayed using carbendazim)
PMID:1943699	PBO:0098027	assay construct also has nt change G36C to distinguish from snu2+ transcript
PMID:1943699	PBO:0098027	assay construct also has nt change G36C to distinguish from snu2+ transcript
PMID:1943699	PBO:0098027	assay construct also has nt change G36C to distinguish from snu2+ transcript
PMID:1943699	PBO:0106466	assay construct also has nt change G36C to distinguish from snu2+ transcript
PMID:1943699	PBO:0098027	assay construct also has nt change G36C to distinguish from snu2+ transcript
PMID:1944266	FYPO:0001759	assayed substrate: rabbit muscle phosphorylase
PMID:19443688	PBO:0114416	Fig. S3A
PMID:19443688	PBO:0114417	Fig. S3B
PMID:19443688	PBO:0094679	Fig. S5
PMID:19443688	PBO:0094283	Fig. 2D
PMID:19443688	PBO:0094283	Fig. 1
PMID:19443688	PBO:0094679	Fig. 1
PMID:19443688	PBO:0094282	Fig. 1
PMID:19443688	PBO:0114414	Fig. 3D
PMID:19443688	PBO:0114415	Fig. S3A
PMID:19443688	PBO:0094282	Fig. 4C
PMID:19443688	PBO:0094679	Fig. 4C
PMID:19443688	PBO:0094283	Fig. 4C
PMID:19454013	PBO:0095499	Rad21
PMID:19454013	PBO:0095500	Rad21
PMID:19474789	PBO:0108327	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	PBO:0096312	fig3
PMID:19474789	PBO:0103732	all data These data indi- cate 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:0103729	Figure 4 d
PMID:19474789	PBO:0096314	Supplementary Table 2 These experiments support the pom1 gradient model, pom1 is delocalized in tea1 delete
PMID:19474789	PBO:0095711	Supplementary Table 2 These experiments support the pom1 gradient model, pom1 is delocalized in tea1 delete
PMID:19474789	PBO:0096312	Supplementary Table 2 These experiments support the pom1 gradient model, pom1 is delocalized in tea1 delete
PMID:19474789	PBO:0107817	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	PBO:0107817	Supplementary Fig. 6
PMID:19474789	PBO:0107428	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	PBO:0107428	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	PBO:0018540	Fig. 2c,d,e
PMID:19474789	FYPO:0003481	Supplementary Table 1
PMID:19474789	PBO:0094428	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	PBO:0108328	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	PBO:0024116	Fig. 2c,d,e
PMID:19474789	PBO:0096311	Supplementary Table 2
PMID:19474789	PBO:0107661	all data These data indi- cate 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:0018346	Fig. 2c,d,e
PMID:19474789	PBO:0096314	fig3
PMID:19474789	PBO:0018540	Fig. 1c and Supplementary Fig. 2a
PMID:19474789	PBO:0018540	Fig 1 a,b
PMID:19474789	PBO:0018540	Fig 1 a,b
PMID:19474789	GO:0031569	all data These data indi- cate 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 indi- cate 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:0096314	fig3
PMID:19474789	PBO:0018540	Fig 1 a,b
PMID:19474789	PBO:0107426	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	PBO:0110567	Supplementary Fig. 6
PMID:19474789	PBO:0108330	Fig. 3a
PMID:19474789	PBO:0107426	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	PBO:0107426	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	PBO:0107426	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	PBO:0107426	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	PBO:0108331	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	PBO:0108331	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	PBO:0108332	Supplementary Figure S8
PMID:19474789	PBO:0108333	Supplementary Figure S8
PMID:19474789	PBO:0108334	Supplementary Figure S8
PMID:19474789	PBO:0108335	Supplementary Figure S8
PMID:19474789	PBO:0095712	fig3
PMID:19474789	PBO:0096311	fig3
PMID:19474789	PBO:0096314	fig3
PMID:19474789	PBO:0096314	fig3
PMID:19474789	PBO:0096314	fig3
PMID:19474789	PBO:0096314	fig3
PMID:19474789	PBO:0107426	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	PBO:0107426	Fig. 2a and Supplementary Fig. 3a
PMID:19474789	PBO:0096314	fig3
PMID:19474789	PBO:0094619	Supplementary Fig. 10
PMID:19474789	PBO:0095711	fig3
PMID:19474789	PBO:0095711	fig3
PMID:19474789	PBO:0096314	fig3
PMID:19474792	GO:0051285	Supplementary Fig. 2
PMID:19474792	PBO:0024047	Supplementary Fig. 3
PMID:19474792	PBO:0024047	Supplementary Fig. 3
PMID:19474792	PBO:0103728	Supplementary Fig. 4
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:0103730	cortex
PMID:19474792	FYPO:0001355	fig 1b
PMID:19474792	FYPO:0001355	fig 1b
PMID:19474792	FYPO:0001357	or is this reduced with low exressivity?
PMID:19474792	PBO:0103732	Fig. 1e in vitro link from epistastis and delayed cdc2 phosphorylation
PMID:19474792	FYPO:0003736	(Fig. 3b).
PMID:19474792	FYPO:0003481	Table 1 and Fig. 2d
PMID:19474792	FYPO:0001234	Table 1 and Fig. 2d
PMID:19474792	PBO:0103731	Table 1 and Fig. 2d
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	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	FYPO:0003736	(Fig. 3b).
PMID:19474792	PBO:0096311	Table 1
PMID:19474792	PBO:0094966	table1
PMID:19474792	PBO:0094966	table1
PMID:19474792	FYPO:0003736	(Fig. 3b).
PMID:19474792	FYPO:0003307	(Fig. 3b).
PMID:19474792	FYPO:0002516	(Fig. 3b).
PMID:19474792	PBO:0103725	fig 1d ie not blocked in g2
PMID:19474792	PBO:0103726	Fig. 1e Fig. 1f)
PMID:19474792	PBO:0103727	Fig. 1e in vitro link from epistastis and delayed cdc2 phosphorylation
PMID:19474792	PBO:0096180	fig 1g
PMID:19474792	GO:0051285	Supplementary Fig. 2
PMID:19486165	PBO:0093574	(Fig. 7B)
PMID:19486165	PBO:0093574	(Fig. 7B)
PMID:19486165	PBO:0097639	(Fig. 7B)
PMID:19486165	PBO:0097639	(Fig. 7B)
PMID:19486165	PBO:0097639	(Fig. 7B)
PMID:19486165	FYPO:0000110	figure 7 A
PMID:19486165	PBO:0097638	Fig. 6C
PMID:19486165	FYPO:0000046	Fig. 5C
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 4 C
PMID:19486165	FYPO:0000046	Figure 4 C
PMID:19486165	FYPO:0002061	Figure 4 C
PMID:19486165	FYPO:0000650	(Fig. 4B)
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:19487457	PBO:0107111	(Fig. 4 C and Video 3)
PMID:19487457	FYPO:0007428	monopolar
PMID:19487457	FYPO:0007428	monopolar
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: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: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: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	insertion
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:19487461	FYPO:0001425	Fig5A
PMID:19487461	FYPO:0006822	Fig1A BrdU incorporation wee1-50 strain analysed at 32°C
PMID:19487461	PBO:0021770	Fig 1B
PMID:19487461	PBO:0100211	Fig1G 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:19502236	PBO:0114270	Fig. 7B
PMID:19502236	PBO:0114263	Fig. 1A
PMID:19502236	PBO:0114264	Fig. 1B
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:0114266	Fig. 7C
PMID:19502236	PBO:0114271	Fig. 9A
PMID:19502236	PBO:0114272	Fig. 9A
PMID:19502236	PBO:0114271	Fig. 9A
PMID:19502236	PBO:0114271	Fig. 9A
PMID:19502236	PBO:0114273	Fig. 9A
PMID:19502236	PBO:0114272	Fig. 9A
PMID:19523829	FYPO:0002638	increased dlocalization of mad2 to kinetochore
PMID:19543678	PBO:0099033	(Fig. 3)
PMID:19543678	PBO:0099031	from PM (Fig. 3c
PMID:19543678	PBO:0099032	(Fig. 3)
PMID:19546237	GO:0010971	during recovery from stress
PMID:19567474	PBO:0093560	Fig. 3A
PMID:19567474	PBO:0114392	Fig. 4
PMID:19567474	PBO:0093560	Fig. 3A
PMID:19567474	PBO:0093560	Fig. 3A
PMID:19567474	PBO:0114391	Fig. 4
PMID:19570908	GO:1902404	request and use GO:new positive regulation of (MF) microfilament motor activity instead? depends on ancestry of motor activity branch
PMID:19570908	PBO:0095205	25 degrees C, i.e. lower end of normal temp. range; penetrance higher at 29 degrees C
PMID:19570908	FYPO:0005904	myo2
PMID:19570908	FYPO:0005904	myo2
PMID:19571115	PBO:0108194	fig1
PMID:19571115	PBO:0108193	fig1
PMID:19571115	FYPO:0002060	Fig. 5B
PMID:19571115	FYPO:0000411	Fig. 5B
PMID:19571115	PBO:0108195	fig5D
PMID:19571115	FYPO:0007572	Fig. 5a
PMID:19592249	GO:1902426	fig2
PMID:19592249	PBO:0095923	figure 1E apc complex binding
PMID:19592249	PBO:0095922	figure 1E apc complex binding
PMID:19592249	GO:0090267	fig1
PMID:19592249	PBO:0095921	figure 1a
PMID:19592249	PBO:0095920	figure 1a
PMID:19592249	PBO:0095925	figure 2a abolished
PMID:19592249	FYPO:0002638	figure2
PMID:19592249	FYPO:0002638	figure2
PMID:19592249	PBO:0095924	figure 2a abolished
PMID:19605557	PBO:0100329	figure 6
PMID:19605557	PBO:0100329	figure 6
PMID:19605557	PBO:0100329	figure 6
PMID:19605557	PBO:0100329	figure 6
PMID:19605557	FYPO:0007797	However, GII activity is significantly reduced in the microsomal fraction of 􏰄GII􏰀 cells (Figure 2B), suggesting that GII􏰀 is involved in ER localization of GII􏰁
PMID:19605557	GO:0106407	GII􏰀 Is Required for an Efficient In Vitro Glucose Trimming from G2M9 and G1M9
PMID:19606211	SO:0001531	Sequence LVIAMDQLNL mentioned in the text
PMID:19606211	SO:0001528	See Fig. 1
PMID:19624755	PBO:0093720	Dapl2 and Dapm1 cells were more sensitive when exposed to 34 °C or to 5 mM VPA com- pared 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 com- pared 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 com- pared 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:19624755	PBO:0106298	localized to large endosomal structures
PMID:19624755	PBO:0106298	localized to large endosomal structures
PMID:19624755	PBO:0106298	localized to large endosomal structures
PMID:19624755	PBO:0107027	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	localized to large endosomal structures
PMID:19624755	PBO:0106298	localized to large endosomal structures
PMID:19624755	PBO:0106298	localized to large endosomal structures
PMID:19624755	PBO:0106298	localized to large endosomal structures
PMID:19624755	GO:0005768	Fig. 6a, wt, arrowheads
PMID:19624755	GO:0005886	Fig. 6a, wt, arrowheads
PMID:19624755	PBO:0107026	fig5
PMID:19624755	PBO:0107026	fig5
PMID:19624755	PBO:0107025	fig5
PMID:19624755	PBO:0107025	fig5
PMID:19624755	PBO:0107025	fig5
PMID:19624755	PBO:0107024	fig5
PMID:19624755	PBO:0107023	fig5
PMID:19624755	PBO:0107023	fig5
PMID:19624755	GO:0005794	Fig4. 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 com- pared 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 com- pared with those of Dapl4 and Daps1 cells
PMID:19625445	PBO:0101774	Fig 2A
PMID:19625445	PBO:0101750	Fig 1 16.5 +/- 0.78
PMID:19625445	FYPO:0002106	Fig 1 IS THIS SMALL OR STUBBY? 11.6 +/- 0.45
PMID:19625445	FYPO:0000223	Fig 1
PMID:19625445	PBO:0101750	Fig 1
PMID:19625445	PBO:0101750	Fig 1
PMID:19625445	PBO:0032799	Fig 1
PMID:19625445	PBO:0033281	Fig 1
PMID:19625445	PBO:0093576	figure 6a
PMID:19625445	PBO:0101784	Figure 7
PMID:19625445	FYPO:0002444	fig8
PMID:19625445	FYPO:0007525	fig8
PMID:19625445	PBO:0101785	fig9A
PMID:19625445	PBO:0097115	Figure 9B
PMID:19625445	PBO:0101786	Figure 9B
PMID:19625445	PBO:0095212	Figure 9
PMID:19625445	PBO:0101775	Figure9
PMID:19625445	PBO:0101775	Figure 5A
PMID:19625445	PBO:0095212	Figure 5A
PMID:19625445	PBO:0099872	Fig 1C
PMID:19625445	PBO:0099872	Fig 1C
PMID:19625445	FYPO:0007520	Fig 1 C
PMID:19625445	PBO:0099871	Fig 1C
PMID:19625445	PBO:0099872	Fig 1C
PMID:19625445	PBO:0101751	fig 1D
PMID:19625445	PBO:0101751	fig 1D
PMID:19625445	PBO:0101752	fig 1D
PMID:19625445	PBO:0101752	fig 1D
PMID:19625445	PBO:0101753	Fig 2A
PMID:19625445	PBO:0101754	Fig 2A
PMID:19625445	PBO:0101755	Fig 2A
PMID:19625445	FYPO:0007520	Fig 2B
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:19625445	PBO:0101760	Fig 2D
PMID:19625445	PBO:0093578	figure 6a
PMID:19625445	PBO:0093578	figure 6a
PMID:19625445	PBO:0093612	figure 6a
PMID:19625445	FYPO:0001037	figure 6a
PMID:19625445	PBO:0099902	figure 6a
PMID:19625445	PBO:0101781	figure 6c,d
PMID:19625445	PBO:0101782	Figure 7
PMID:19625445	PBO:0095501	Fig 2D
PMID:19625445	PBO:0101761	Figure 3D
PMID:19625445	PBO:0101762	figure 4A
PMID:19625445	PBO:0099926	figure 4A IS THIS NORMAL OR EVEN HIGHER THAN WT?
PMID:19625445	PBO:0101763	figure 4A IS THIS NORMAL OR EVEN HIGHER THAN WT? (this is higher than wis1DD-cpc2delet so must be increased
PMID:19625445	PBO:0101783	Figure 7
PMID:19625445	PBO:0097115	Figure 3D
PMID:19625445	PBO:0101764	Figure 3D
PMID:19625445	PBO:0101765	Figure 3D
PMID:19625445	PBO:0101766	Figure 3D
PMID:19625445	PBO:0101767	Figure 4B
PMID:19625445	PBO:0101768	Figure 4B
PMID:19625445	PBO:0101769	Figure 4B
PMID:19625445	PBO:0101770	Figure 4B
PMID:19625445	PBO:0101771	Figure 4B
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:0101778	Figure 5B
PMID:19625445	PBO:0101777	Figure 5B
PMID:19625445	PBO:0094763	Figure 5B
PMID:19625445	PBO:0101776	Figure 5B
PMID:19625445	FYPO:0000961	figure 6a
PMID:19625445	PBO:0093577	figure 6a
PMID:19625445	PBO:0101772	Figure 4c
PMID:19625445	PBO:0101773	Figure 4c
PMID:19625445	PBO:0101774	Fig 2A
PMID:19627505	GO:0070867	localization requires F-actin (assayed using latrunculin A) and membrane rafts (assayed using filipin)
PMID:19636559	PBO:0103845	not shown, from text
PMID:19636559	FYPO:0004481	not shown, from text
PMID:19636559	PBO:0103845	not shown, from text
PMID:19643199	FYPO:0001423	fig 1 d
PMID:19643199	PBO:0095556	fig 1 c
PMID:19643199	FYPO:0001423	fig 1 d this term should really be trafficing
PMID:19643199	FYPO:0006266	fig 1 d
PMID:19646873	PBO:0105340	2f
PMID:19646873	PBO:0095264	2f
PMID:19646873	PBO:0105341	2f
PMID:19646873	PBO:0105342	2f
PMID:19646873	PBO:0095264	S2
PMID:19680287	FYPO:0005684	Fig. 2A assayed with plo1 GFP
PMID:19680287	PBO:0105465	Fig. 3E, S9
PMID:19680287	PBO:0096322	Fig. 1B, S3
PMID:19680287	PBO:0105458	Fig. 1B, S3
PMID:19680287	PBO:0096316	Fig. 1B, S3
PMID:19680287	PBO:0096315	Fig. 1B, S3
PMID:19680287	PBO:0105465	Fig. 3E, S9
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:0105464	Fig. 3E
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:19680287	FYPO:0006428	(Fig 3C), showed a similar fraction of mono-oriented chromosomes as wild-type cells
PMID:19680287	FYPO:0004396	Fig. S10
PMID:19680287	PBO:0105464	Fig. 3E
PMID:19680287	PBO:0105463	Fig. 3E
PMID:19680287	PBO:0105462	Fig. 3B/C
PMID:19680287	PBO:0105460	Fig. 3B/C moved down from congresssion to abnormal mitotic sister chromatid biorientation ?
PMID:19680287	PBO:0105461	Fig. 3B/C. SEE ABOVE
PMID:19680287	PBO:0105459	Fig. 2B
PMID:19680287	PBO:0037150	Fig. 2B
PMID:19680287	PBO:0105466	Fig. S7
PMID:19680287	PBO:0096323	Fig. S6C/D
PMID:19680287	PBO:0096323	Fig. S6C/D
PMID:19680287	PBO:0096322	Fig. S6A/B
PMID:19680287	FYPO:0003762	Fig. S2B
PMID:19680287	FYPO:0004318	Fig. S2B
PMID:19680287	FYPO:0004318	Fig. S2B
PMID:19680287	FYPO:0003762	Fig. S2A
PMID:19680287	FYPO:0004318	Fig. S2A
PMID:19680287	FYPO:0004318	Fig. S2A
PMID:19686686	PBO:0095697	Figure 3 D
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:0109478	interacts with unmodified Ase1 PR:000027520
PMID:19686686	PBO:0033572	interphase, prophase, metaphase,anaphase A
PMID:19686686	PBO:0033573	interphase, prophase, metaphase,anaphase A
PMID:19686686	PBO:0033574	interphase, prophase, metaphase,anaphase A
PMID:19686686	PBO:0022963	mitotic anaphase B
PMID:19686686	FYPO:0005342	fig 1e
PMID:19686686	FYPO:0005342	fig 1e
PMID:19686686	FYPO:0000620	with monopolar spindle
PMID:19686686	PBO:0033575	mitotic anaphase B, mitotic telophase
PMID:19686686	PBO:0033576	mitotic anaphase B, mitotic telophase
PMID:19686686	GO:1990023	fig 4 a
PMID:19686686	GO:1990023	fig 4 a
PMID:19686686	PBO:0095690	cdc2 dependent phophorylation (fig. 4B)
PMID:19686686	PBO:0094040	cdc2 dependent phophorylation (fig. 5B)
PMID:19686686	PBO:0095694	Fig. 5C
PMID:19686686	FYPO:0003268	Fig. 5C
PMID:19686686	FYPO:0005343	Fig. 5C
PMID:19686686	PBO:0095689	Fig. 5C
PMID:19686686	PBO:0095696	Figure 3 D
PMID:19686686	PBO:0095696	Figure 3 D
PMID:19686686	PBO:0095696	Figure 3 D
PMID:19686686	PBO:0095697	Figure 3 D
PMID:19686686	PBO:0109478	interacts with unmodified Klp9 PR:000027705
PMID:19686686	PBO:0021821	interphase, prophase, metaphase,anaphase A
PMID:19693008	PBO:0110854	affected chromatin association of Swr1, distribution of H2A.Z across the genome (Supplementary Fig. 2c).
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:0110855	At euchromatic loci, H2A.Z localizes preferentially in intergenic regions (Supplementary Fig. 3b)
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: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	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	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: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 transcrip- tion (RT–PCR; Fig. 1f).
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:19696784	PBO:0106851	fig 1 c
PMID:19696784	PBO:0106853	Fig 2A,B
PMID:19696784	PBO:0106855	(Fig 3B)
PMID:19696784	PBO:0106856	(Fig 3B)
PMID:19696784	PBO:0106857	(Fig 3B)
PMID:19696784	PBO:0106858	figure5
PMID:19696784	PBO:0106859	supplementary Fig S6 online
PMID:19696784	PBO:0106852	fig 1 c
PMID:19713940	GO:0051015	assayed using N-terminal Rng2-Ns fragment or calponin homology domain (CHD) fragment
PMID:19713940	PBO:0095570	observed after short-duration overexpression
PMID:19713940	FYPO:0002437	temperature restrictive for cdc25-22
PMID:19713940	FYPO:0002437	temperature restrictive for cdc25-22
PMID:19713940	FYPO:0002437	temperature restrictive for cdc25-22
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: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: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: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	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: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: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: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: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: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: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: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: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: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: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: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: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: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: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: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: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: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	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: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	FYPO:0001357	yox1D cells were viable and did not show any overall growth defect (Figure 4B).
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	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:0113994	Another example is map1, encoding a MADS-box transcription factor involved in the transcriptional response during mating
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: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: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: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: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: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: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	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: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	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: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: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: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: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: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: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: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: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: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: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: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: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: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:19723888	PBO:0093629	figure 1B
PMID:19723888	PBO:0093629	figure 1B
PMID:19723888	PBO:0093630	figure 1B
PMID:19723888	PBO:0093629	fig1A
PMID:19723888	PBO:0093580	fig1C,D
PMID:19723888	PBO:0093629	figure 1B
PMID:19723888	PBO:0093631	figure 1B
PMID:19723888	PBO:0093631	figure 1B
PMID:19723888	PBO:0093581	fig1C
PMID:19723888	PBO:0093629	fig1A
PMID:19723888	PBO:0093630	fig1A
PMID:19723888	PBO:0093630	fig1A
PMID:19723888	PBO:0093630	fig1A
PMID:19723888	PBO:0093580	fig1C
PMID:19723888	PBO:0093630	fig1A
PMID:19723888	PBO:0093581	fig1C
PMID:19723888	PBO:0093580	fig1C
PMID:19723888	PBO:0093629	fig1A
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	PBO:0093629	fig1A
PMID:19723888	FYPO:0001903	Fig 2A III
PMID:19723888	PBO:0093581	fig1C
PMID:19723888	PBO:0093630	fig1A
PMID:19723888	PBO:0093629	fig1A
PMID:19723888	PBO:0093629	fig1A
PMID:19723888	PBO:0093581	fig1D
PMID:19723888	FYPO:0000650	Fig 2A III
PMID:19723888	PBO:0097772	fig1D
PMID:19723888	PBO:0095096	Fig 2A III
PMID:19723888	PBO:0097772	fig1D
PMID:19723888	PBO:0093580	fig1C
PMID:19723888	PBO:0093581	fig1C
PMID:19723888	PBO:0093629	fig1A
PMID:19723888	PBO:0097773	fig1C
PMID:19723888	PBO:0097773	fig1C
PMID:19723888	PBO:0093629	figure 1B
PMID:19723888	PBO:0093630	fig1A
PMID:19723888	PBO:0093629	figure 1B
PMID:19723888	PBO:0093629	figure 1B
PMID:19736319	FYPO:0001493	Fig. S1 C, arrows
PMID:19736319	FYPO:0005369	Fig. S1 B and not depicted
PMID:19736319	PBO:0108322	2% fig 6a
PMID:19736319	PBO:0113925	2% fig 6a. to dauughter
PMID:19736319	PBO:0018345	Fig. 4 B and not depicted
PMID:19736319	PBO:0108321	fig 4d
PMID:19736319	FYPO:0005055	arrested normal size (multiple rounds of cytokinesis) in interphase
PMID:19736319	FYPO:0002000	add to def, septated in interphase. one compartment is anucleate
PMID:19736319	PBO:0021746	Fig. 4 B and not depicted
PMID:19758558	PBO:0103657	Fig. S3D
PMID:19798055	FYPO:0005452	decreased overall
PMID:19804755	MOD:01455	residues include one or more of S77, T78, T79, S87, and T89, and other(s)
PMID:19804755	PBO:0100522	ctp-Phosphorylated
PMID:19879140	FYPO:0006725	MT spindown assay.
PMID:19879140	FYPO:0001944	MT spindown assay
PMID:19879140	GO:0008017	Biochemistry
PMID:19915592	GO:0000812	figure2b
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:19915592	FYPO:0002061	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	figure2b
PMID:19915592	GO:0000812	figure2b
PMID:19915592	GO:0000812	figure2b
PMID:19915592	GO:0000812	figure2b
PMID:19915592	GO:0000812	figure2b
PMID:19915592	GO:0000812	figure2b
PMID:19915592	GO:0000812	figure2b
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	GO:0000812	figure2b
PMID:19915592	GO:0000812	figure2b
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	GO:0000812	figure2b
PMID:19915592	GO:0000812	figure2b
PMID:19915592	GO:0000812	figure2b
PMID:19915592	GO:0000812	figure2b
PMID:19915592	GO:0000812	figure2b
PMID:19915592	FYPO:0000283	(iii) entanglement leading to breakage, where broken pieces of chromatin with no kinetochore lag on the spindle (Fig. 4b).
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: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:19942659	PBO:0108463	minor
PMID:19942659	FYPO:0003728	Like the gms1D mutant, neither the uge1D strain nor the uge1Dgal10D strain reacted with PNA (Fig. 2b
PMID:19942659	GO:0003978	major
PMID:19942852	PBO:0102700	fig3
PMID:19942852	PBO:0102701	fig3
PMID:19942852	PBO:0102702	fig3
PMID:19942852	FYPO:0005380	1D
PMID:19942852	PBO:0102699	1D
PMID:19942852	PBO:0102699	1D
PMID:19942852	FYPO:0000274	1D
PMID:19942852	PBO:0019218	fig1
PMID:19942852	FYPO:0006593	1D
PMID:19942852	FYPO:0005380	1D
PMID:19942852	PBO:0102705	fig6a
PMID:19942852	FYPO:0002061	fig1
PMID:19942852	PBO:0102698	S2 &3
PMID:19942852	PBO:0102698	S2 &3
PMID:19942852	FYPO:0006593	1D
PMID:19942852	PBO:0019218	fig1
PMID:19942852	FYPO:0002061	fig1
PMID:19942852	FYPO:0000274	1D
PMID:19942852	PBO:0102706	fig6a
PMID:19948483	FYPO:0002061	Fig. 3
PMID:19948483	FYPO:0005045	Fig. 3
PMID:19948483	PBO:0101996	Fig. 3
PMID:19948483	FYPO:0008007	Fig. 3
PMID:19948484	PBO:0095347	this is an adaptor
PMID:19948484	PBO:0095335	they say periphery in the text but it has TM domains
PMID:19948484	PBO:0095336	they say periphery in the text but it has TM domains
PMID:19965387	PBO:0102063	Fig. 3A
PMID:19965387	FYPO:0006423	Fig. S3
PMID:19965387	FYPO:0006423	Fig. S3
PMID:19965387	FYPO:0006423	Fig. S3
PMID:19965387	PBO:0102063	Fig. S3
PMID:19965387	PBO:0112750	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:0102073	fusion experiments (Figure 3)
PMID:19965387	PBO:0102072	Fig. 4G
PMID:19965387	PBO:0102072	Fig. 4G
PMID:19965387	PBO:0102072	Fig. 4G
PMID:19965387	PBO:0102071	Fig. 4G
PMID:19965387	PBO:0102059	Fig. 3A
PMID:19965387	PBO:0102059	Fig. 3A
PMID:19965387	PBO:0102070	4c
PMID:19965387	PBO:0101329	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: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	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:0102063	Fig. S3
PMID:19965387	FYPO:0005634	Fig. 2E
PMID:19965387	FYPO:0005634	Fig. 2E
PMID:19965387	FYPO:0005634	Fig. 2E
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:0102059	Fig. 3A
PMID:19965387	PBO:0102059	Fig. 3A
PMID:19965387	PBO:0102060	Fig. 3A
PMID:19965387	PBO:0102061	Fig. 3A
PMID:19965387	PBO:0102062	Fig. 3A
PMID:19965387	PBO:0102060	Fig. 3A
PMID:19965387	PBO:0102061	Fig. 3A
PMID:19965387	PBO:0102062	Fig. S5
PMID:19965387	FYPO:0006423	Fig. S3
PMID:20062003	FYPO:0006076	2D
PMID:20062003	FYPO:0007009	4
PMID:20062003	FYPO:0007009	4
PMID:20062003	FYPO:0007009	4
PMID:20062003	FYPO:0007009	4
PMID:20062003	FYPO:0007009	4
PMID:20062003	FYPO:0007009	S1
PMID:20062003	FYPO:0007009	S1
PMID:20062003	FYPO:0007009	S1
PMID:20062003	FYPO:0007010	3
PMID:20062003	FYPO:0007009	4
PMID:20075862	FYPO:0001408	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	Forms gamma H2A dependent nuclear foci when over-expressed
PMID:20110347	FYPO:0004430	25 degrees
PMID:20110347	PBO:0101716	32 degrees; semi-permissive for cdc8-27 alone
PMID:20110347	FYPO:0001355	25 or 32 degrees; latter semi-permissive for cdc8-27 alone
PMID:20110347	FYPO:0001355	32 degrees
PMID:20110347	FYPO:0001357	25 degrees
PMID:20110347	PBO:0104411	32 degrees
PMID:20110347	FYPO:0004895	32 degrees
PMID:20110347	FYPO:0004895	25 degrees
PMID:20110347	FYPO:0003339	25 degrees
PMID:20123974	FYPO:0000485	also ctp1,rec12,rad22,rti1,rad51,dmc1 unequal sister chromatid recombination (USCR)
PMID:20123974	FYPO:0000487	increased unequal sister chromatid recombination
PMID:20123974	FYPO:0000487	increased unequal sister chromatid recombination
PMID:20123974	FYPO:0000487	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: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:0114327	. Grow- ing 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 (Fig- ure 7) (n  20). The GEF activity of SpSpo13 is therefore required for FSM assembly in S. pombe.
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:0106748	full-length Rad3 or Rad3-kd-delta
PMID:20140190	PBO:0106743	same as nbs1-c60-delta alone
PMID:20140190	PBO:0106743	same as nbs1-c60-delta alone
PMID:20140190	PBO:0101083	full-length Rad3 or Rad3-kd-delta
PMID:20164182	PBO:0106771	unstressed cells
PMID:20164182	PBO:0095167	unstressed cells
PMID:20164182	PBO:0108243	unstressed cells
PMID:20164182	PBO:0106771	unstressed cells
PMID:20164182	PBO:0108243	unstressed cells
PMID:20164182	PBO:0108243	unstressed cells
PMID:20164182	PBO:0095167	unstressed cells
PMID:20164182	PBO:0095167	unstressed cells
PMID:20164182	PBO:0095167	unstressed cells
PMID:20164182	PBO:0108243	unstressed cells
PMID:20164182	PBO:0095167	unstressed cells
PMID:20164182	PBO:0108243	unstressed cells
PMID:20164182	PBO:0095167	unstressed cells
PMID:20164182	PBO:0106771	unstressed cells
PMID:20164182	PBO:0095167	unstressed cells
PMID:20164182	PBO:0108243	unstressed cells
PMID:20164182	PBO:0095167	unstressed cells
PMID:20164182	PBO:0095167	unstressed cells
PMID:20211136	FYPO:0004170	abolished at exogenous RNA polII transcribed gene
PMID:20211136	PBO:0098760	this is the endogenous dg repeat
PMID:20211136	PBO:0112179	not sure which clrc subunit it binds to?
PMID:20211136	FYPO:0003412	endogenous ade6
PMID:20226666	FYPO:0000229	Figure 1 in interphase
PMID:20226666	FYPO:0007664	Figure 1 in interphase
PMID:20226666	PBO:0102628	Figure 1
PMID:20226666	PBO:0102629	Figure 1
PMID:20230746	PBO:0108901	involved in negative regulation of transcription via transcription factor catabolism
PMID:20299449	PBO:0113963	Fig. 1F
PMID:20299449	PBO:0113969	Fig. 4D
PMID:20299449	PBO:0113968	Fig. 4F
PMID:20299449	PBO:0113967	Fig. 4E
PMID:20299449	PBO:0113966	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	FYPO:0002837	Fig. 1E
PMID:20299449	PBO:0113963	Fig. 1F
PMID:20299449	PBO:0104709	Fig. 1C
PMID:20299449	PBO:0104710	Fig. 1B and C
PMID:20299449	PBO:0104710	Fig. 1B and C
PMID:20299449	PBO:0020274	IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT
PMID:20299449	MOD:00723	IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT
PMID:20299449	PBO:0020274	IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT
PMID:20299449	PBO:0096407	IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT
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	FYPO:0001442	Fig. 2A
PMID:20299449	FYPO:0004240	Fig. 2A
PMID:20299449	FYPO:0004239	Fig. 2B
PMID:20299449	FYPO:0000892	Fig. 2A
PMID:20299449	FYPO:0008270	Fig. 2A
PMID:20299449	FYPO:0004238	Fig. 2A
PMID:20299449	FYPO:0002837	Fig. 1E
PMID:20299449	PBO:0113964	Fig. 1F
PMID:20299449	PBO:0113963	Fig. 1F
PMID:20299449	PBO:0094283	Fig. 1B and C
PMID:20356456	GO:0008379	The peroxidase activity of BCP (bacterioferritin comigratory protein) was similar to that of TPx.
PMID:20360683	FYPO:0003917	assayed using GFP reporter with or without premature stop codons
PMID:20360683	FYPO:0003917	assayed using GFP reporter with or without premature stop codons
PMID:20360683	FYPO:0003947	assayed using ypt3 reporter with or without premature stop codons
PMID:20360683	FYPO:0003947	assayed using ypt3 reporter with or without premature stop codons
PMID:2038306	PBO:0024304	Data not shown. pMNScdc2-DL5 is integrated
PMID:2038306	PBO:0037126	pMNScdc2-DL5 is integrated cells observed after 30 hours over expression Figure 2. In the paper they call this plasmid pMNSDL5 I have added cdc2-DL5 for clarity . The pMNS21L plasmid used for isolating this cdc2 mutant has since been rename pREP1.
PMID:2038306	PBO:0037125	pMNScdc2-DL5 is an episomal plasmid.
PMID:2038306	PBO:0037130	the endogenous copy of cdc2 has been replaced by cdc2 from human cells CDC2HS. 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	pMNScdc2-DL5 is integrated. Cells observed after 12 hours over expression Figure 2. In the paper they call this plasmid pMNSDL5 I have added cdc2-DL5 for clarity . The pMNS21L plasmid used for isolating this cdc2 mutant has since been rename pREP1.
PMID:2038306	PBO:0102101	cdc2-DL5 is over expressed from episomal pMNScdc2DL5. 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 lane pMNSDL5-
PMID:2038306	PBO:0096052	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	cdc2-DL5 is expressed from episomal pMNScdc2DL5. CDC2HS is not recognised by anti cdc2 antibody 4711 and so does not contribute to the level of cdc2-DL5 kinase activity Figure 4A lane pMNSDL5-
PMID:2038306	PBO:0102100	CDC2HS is not recognised by anti cdc2 antibody 4711 and so does not contribute to the level of kinase activity assayed. S. pombe cdc2+ is on a multi copy plasmid pMNScdc2 Figure 4A lane 1
PMID:2038306	PBO:0093712	CDC2HS complements cdc2delete phenotype Figure 4B
PMID:2038306	PBO:0037125	pMNScdc2-DL5 fails to rescue cdc2-33 mutant at the restrictive temperature. Do not say how this was assayed
PMID:2038306	PBO:0024451	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	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:0037128	pMNScdc2-DL5 is integrated
PMID:2038306	PBO:0037127	Data not shown. pMNScdc2-DL5 is integrated
PMID:20383139	PBO:0101009	Fig 1e
PMID:20383139	PBO:0109330	fig3a
PMID:20383139	PBO:0109329	fig3a par1, the regulatory subunit was used in the assay
PMID:20383139	PBO:0101028	Fig. 5c
PMID:20383139	PBO:0101025	Fig. 5b
PMID:20383139	PBO:0101027	fig 5c
PMID:20383139	PBO:0101026	fig 5B
PMID:20383139	PBO:0101025	Fig. 5b
PMID:20383139	PBO:0101025	Fig. 5b
PMID:20383139	PBO:0101024	Fig. S5
PMID:20383139	PBO:0101024	Fig. S5
PMID:20383139	PBO:0101023	fig 4 c
PMID:20383139	PBO:0101021	separation
PMID:20383139	PBO:0101019	fig 3 c
PMID:20383139	PBO:0101018	fig 3 c
PMID:20383139	PBO:0101017	fig3a
PMID:20383139	PBO:0101017	fig3a
PMID:20383139	PBO:0101016	Fig. 2b
PMID:20383139	PBO:0101015	Fig. 2b
PMID:20383139	PBO:0101014	Fig. 2b
PMID:20383139	PBO:0101013	Fig. 2b
PMID:20383139	PBO:0033208	Fig. S1a
PMID:20383139	FYPO:0001513	fig 1d
PMID:20383139	PBO:0101010	fig1e
PMID:20383139	FYPO:0001355	fig1b
PMID:20383139	FYPO:0001357	fig1b
PMID:20383139	FYPO:0001357	fig1b
PMID:20383139	FYPO:0001357	fig1b
PMID:20383139	PBO:0101008	Fig 1d
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: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: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: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	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	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: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	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: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: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: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: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: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:20434336	PBO:0100842	figure S1B
PMID:20434336	PBO:0100841	Fig1
PMID:20434336	PBO:0100840	Fig1
PMID:20434336	PBO:0100841	Fig 1
PMID:20434336	PBO:0100849	fig3
PMID:20434336	PBO:0100840	Fig 1
PMID:20434336	PBO:0100849	fig3
PMID:20434336	PBO:0100848	fig3
PMID:20434336	GO:0005635	Fig1
PMID:20434336	PBO:0100841	Fig 1
PMID:20434336	PBO:0100840	Fig 1
PMID:20434336	PBO:0019716	Fig 1
PMID:20434336	PBO:0100847	fig3
PMID:20434336	PBO:0019716	Fig 1
PMID:20434336	PBO:0100846	Fig 2D tubular/cortical
PMID:20434336	GO:0005635	Fig1
PMID:20434336	PBO:0100845	Figures2A and 2B cortical/tubular
PMID:20434336	PBO:0100845	Figures2A and 2B
PMID:20434336	PBO:0100843	Figures2A and 2B
PMID:20434336	PBO:0100844	Figures2A and 2B
PMID:20434336	PBO:0100844	Figures2A and 2B
PMID:20434336	PBO:0100843	Figures2A and 2B
PMID:20434336	PBO:0099441	Figures2A and 2B
PMID:20434336	PBO:0100842	figure S1C
PMID:20434336	PBO:0019716	Fig 1
PMID:20434336	PBO:0095196	Fig3 C
PMID:20434336	PBO:0100852	Fig3 C
PMID:20434336	PBO:0100851	Fig3 C protein distributed in cortex
PMID:20434336	PBO:0098959	(Figure S3A)
PMID:20434336	PBO:0100850	fig3
PMID:20434336	PBO:0100850	fig3
PMID:20434336	PBO:0100853	Fig 4E
PMID:20434336	PBO:0100842	figure S1C
PMID:20434336	GO:1990608	data not shown
PMID:20434336	PBO:0100845	Figures2A and 2B cortical/tubular
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	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:20452294	FYPO:0005221	PCNA trimerization
PMID:20517925	FYPO:0001011	Fig. S1
PMID:20517925	FYPO:0006207	Fig. 3D
PMID:20517925	PBO:0099013	Fig. 3D
PMID:20517925	FYPO:0004964	Fig. 1B
PMID:20517925	FYPO:0002022	formation
PMID:20517925	FYPO:0004652	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 unaf- fected.
PMID:20517925	FYPO:0005430	Fig. 1B
PMID:20547592	PBO:0102400	(Figure 7A)
PMID:20547592	FYPO:0002060	fig 1
PMID:20547592	PBO:0023812	figure 6 a
PMID:20547592	PBO:0037741	fig 5 b
PMID:20547592	FYPO:0001487	Figure 8A and B (fairly similar expression orofiles)
PMID:20547592	FYPO:0002350	(Figure 7B)
PMID:20547592	PBO:0037736	fig 1
PMID:20547592	PBO:0037737	fig 1 nuclear
PMID:20547592	FYPO:0000158	fig 1 c
PMID:20547592	PBO:0037494	fig 2 e suggesting that Vgl1 might escort RNA from ER-associated polyribosomes to the cytosol under thermal stress.
PMID:20547592	FYPO:0005488	fig 5 e
PMID:20547592	FYPO:0001387	figure 4
PMID:20547592	PBO:0037494	Figure 6E)
PMID:20547592	FYPO:0002350	fig 6 c
PMID:20547592	PBO:0037738	Figure 5A
PMID:20547592	PBO:0021023	fig 5 a
PMID:20547592	PBO:0023514	fig 5 b
PMID:20547592	FYPO:0002350	fig 6 D
PMID:20547592	PBO:0037739	Figure 5A
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:0103382	at ste11
PMID:20605454	PBO:0103376	at ste11
PMID:20605454	PBO:0103383	at ste11
PMID:20605454	PBO:0103376	at ste11
PMID:20605454	PBO:0103375	at act1 & sam1
PMID:20605454	PBO:0103369	polII CTD; probably S5 but can't rule out effect on S7
PMID:20605454	PBO:0103369	pol II CTD; probably S2 but can't rule out effect on S7
PMID:20605454	PBO:0103375	at act1 & sam1
PMID:20622008	FYPO:0002353	at genes
PMID:20622014	PBO:0103350	pol II localization to sme2 locus
PMID:20622014	PBO:0103339	temperature restrictive for mmi1-ts3
PMID:20622014	PBO:0103343	temperature restrictive for mmi1-ts3
PMID:20622014	PBO:0103340	temperature restrictive for mmi1-ts3
PMID:20622014	PBO:0103342	temperature restrictive for mmi1-ts3
PMID:20622014	PBO:0103337	temperature restrictive for mmi1-ts3
PMID:20623139	PBO:0093641	high expressivity
PMID:20623139	PBO:0093645	low expressivity
PMID:20624975	FYPO:0005423	fig 5C
PMID:20624975	FYPO:0000904	depolymerization (cytoplasmic?)
PMID:20624975	FYPO:0005423	Fig. S5 B–E
PMID:2065367	PBO:0020025	incomplete penetrance due to translational frameshifting
PMID:2065367	PBO:0020024	incomplete penetrance due to translational frameshifting
PMID:2065367	PBO:0020022	incomplete penetrance due to translational frameshifting
PMID:2065367	FYPO:0000684	severity is variable, and segregates over successive generations (but not 2:2)
PMID:2065367	PBO:0020023	incomplete penetrance due to translational frameshifting
PMID:2065367	PBO:0020021	incomplete penetrance due to translational frameshifting
PMID:2065367	PBO:0020020	incomplete penetrance due to translational frameshifting
PMID:20661445	PBO:0023775	Rad3 dependent
PMID:20661445	PBO:0096219	Phosphorylated at centromeres during S-phase, Rad3 dependent
PMID:20661445	PBO:0023773	Phosphorylated at centromeres during S-phase, Rad3 dependent
PMID:20661445	PBO:0096219	Phosphorylated at centromeres during S-phase, Rad3 dependent
PMID:20661445	PBO:0023773	Phosphorylated at centromeres during S-phase, Rad3 dependent
PMID:20661445	PBO:0096220	Phosphorylated at Tf2-type retrotransposons and wtf elements during S-phase
PMID:20661445	PBO:0023774	Rad3 dependent
PMID:20661445	PBO:0023775	Rad3 dependent
PMID:20661445	PBO:0023774	Rad3 dependent
PMID:20661445	PBO:0023773	Rad3 dependent
PMID:20661445	PBO:0096209	Rad3 dependent
PMID:20661445	PBO:0023773	Rad3 dependent
PMID:20661445	PBO:0096218	Phosphorylated at mating type locus during S-phase in Rad3 dependent manner
PMID:20661445	PBO:0096218	Phosphorylated at mating type locus during S-phase, Rad3-dependent
PMID:20661445	PBO:0021093	ChIP
PMID:20661445	PBO:0033541	Phosphorylated at Tf2-type retrotransposons and wtf elements during S-phase
PMID:20661445	PBO:0096210	Phosphorylated at Tf2-type retrotransposons and wtf elements during S-phase, Rad3-dependent
PMID:20661445	PBO:0096208	Rad3 dependent
PMID:20661445	PBO:0096208	Rad3 dependent
PMID:20661445	PBO:0096209	Rad3 dependent
PMID:20679485	PBO:0103260	Crb2 binds phosphorylated histone H2A (Hta1 Serine-129 and Hta2 Serine-128) through its C-terminal BRCT domains
PMID:20679485	PBO:0111564	Crb2 binds phosphorylated histone H2A (Hta1 Serine-129 and Hta2 Serine-128) through its C-terminal BRCT domains
PMID:20705466	PBO:0098637	temperature semi-permissive for cdc8-27
PMID:20705466	PBO:0106972	temperature semi-permissive for cdc8-27
PMID:20705466	PBO:0098637	temperature semi-permissive for cdc8-27
PMID:20705466	PBO:0106975	temperature semi-permissive for cdc8-27
PMID:20705471	PBO:0098637	temperature permissive for cdc8-27
PMID:20736315	PBO:0102340	Fig4
PMID:20736315	PBO:0102342	Fig1B
PMID:20736315	PBO:0102341	Fig1B
PMID:20739936	FYPO:0001007	The cdc13-M7 mutant is suppressed by bir1-8D
PMID:20739936	PBO:0098639	fig 1c
PMID:20739936	PBO:0098640	fig1d,k
PMID:20739936	PBO:0098641	fig1c
PMID:20739936	PBO:0098642	fig 1k
PMID:20739936	PBO:0093562	fig1
PMID:20739936	FYPO:0003503	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	fig1j
PMID:20739936	PBO:0096770	fig1j
PMID:20739936	PBO:0098648	fig1S4/ figS5
PMID:20739936	PBO:0098649	fig2a,b. figS5
PMID:20739936	PBO:0098650	fig2a
PMID:20739936	PBO:0098651	fig2a
PMID:20739936	PBO:0111964	figS6
PMID:20739936	PBO:0095380	figS6
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	fig2a,b. figS5
PMID:20739936	PBO:0098649	fig2a,b. figS5
PMID:20739936	PBO:0098654	Supplementary Fig. 8a)
PMID:20799962	PBO:0093561	same as rid2-1 alone
PMID:20799962	PBO:0093560	same as rid1-1 alone
PMID:20805322	PBO:0098351	assayed substrate casein
PMID:20805322	PBO:0098352	assayed substrate MBP
PMID:20805322	PBO:0098352	assayed substrate MBP
PMID:20805322	PBO:0098352	assayed substrate MBP
PMID:20805322	PBO:0098357	Fig. 1 A and Table I)
PMID:20805322	PBO:0098359	assayed substrate MBP
PMID:20805322	PBO:0098359	assayed substrate MBP
PMID:20805322	PBO:0098360	assayed substrate MBP
PMID:20805322	PBO:0098361	assayed substrate MBP
PMID:20805322	GO:0032956	negative reg of polarization/remodelling
PMID:20807799	PBO:0106964	"vw: I used ""added by naa20 which is the catalytic subunit for naa25"""
PMID:20807799	PBO:0097713	PR:000037081= tropomyosin cdc8, acetylated form (fission yeast)
PMID:20807799	PBO:0020501	GO:0051329= mitotic interphase
PMID:20807799	PBO:0106962	acetylated Cdc82 so could use PR:000037081
PMID:20826461	PBO:0100787	fig 2C
PMID:20826461	PBO:0100787	fig 2C
PMID:20826461	PBO:0100782	(Fig. 1F
PMID:20826461	PBO:0033557	fig 2A
PMID:20826461	PBO:0100783	fig 2A
PMID:20826461	PBO:0100784	fig 2A
PMID:20826461	GO:0043332	(Fig. 1C
PMID:20826461	PBO:0035494	Fig. 1
PMID:20826461	PBO:0037653	Fig. 1
PMID:20826461	PBO:0100782	(Fig. 1F
PMID:20826461	PBO:0100794	fig 6
PMID:20826461	PBO:0113920	fig 5
PMID:20826461	PBO:0037648	fig 6
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:0100786	fig 2C
PMID:20826461	PBO:0100785	fig 2B
PMID:20826461	PBO:0100786	fig 2C
PMID:20826805	PBO:0021076	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	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	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	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	PBO:0018576	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:20829365	PBO:0099781	figure 3
PMID:20829365	FYPO:0001168	figure 3
PMID:20829365	PBO:0099780	figure 2 a
PMID:20829365	FYPO:0001103	figure 2 a
PMID:20829365	FYPO:0001420	figure 1 a
PMID:20829365	FYPO:0001158	figure 3
PMID:20829365	FYPO:0004874	figure 3
PMID:20829365	FYPO:0007098	figure 5
PMID:20829365	FYPO:0001309	figure 1 a
PMID:20829365	PBO:0099782	figure 3
PMID:20833892	PBO:0035495	fig 3 B WT 10%
PMID:20854854	PBO:0038207	fig 1a
PMID:20854854	FYPO:0001420	fig 1b
PMID:20854854	FYPO:0001234	fig 1b
PMID:20854854	FYPO:0000106	fig 1c
PMID:20854854	FYPO:0002637	fig 1c
PMID:20854854	FYPO:0002447	fig 3
PMID:20854854	PBO:0103040	I don't understand the chemistry well enough to know how the HPLC shows this but I think this is enough evidence?
PMID:20854854	FYPO:0002061	fig 1c
PMID:20854854	FYPO:0002447	fig 3
PMID:20854854	PBO:0103039	fig 1a
PMID:20854854	PBO:0019806	fig 1a
PMID:20876564	PBO:0093558	Fig. 4B
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	FYPO:0000674	Fig. 4B
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: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	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	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	FYPO:0000674	Fig. 4A
PMID:20876564	PBO:0093558	Fig. 4A
PMID:20876564	FYPO:0000674	Fig. 4A
PMID:20876564	FYPO:0000674	Fig. 4A
PMID:20876564	PBO:0093556	Fig. 4A
PMID:20876564	PBO:0112770	Fig. 3A
PMID:20876564	PBO:0112770	Fig. 3A
PMID:20876564	PBO:0112769	Fig. 3A
PMID:20876564	PBO:0112768	Fig. 3A
PMID:20876564	FYPO:0006117	Fig. 2B
PMID:20876564	FYPO:0002177	Fig. 2B
PMID:20876564	FYPO:0004481	Fig. 2A
PMID:20876564	PBO:0093556	Fig. 2A
PMID:20876564	PBO:0093558	Fig. 2A
PMID:20876564	PBO:0093560	Fig. 2A
PMID:20876564	PBO:0093560	Fig. 2A
PMID:20876564	FYPO:0001357	Fig. 2A
PMID:20876564	GO:0044732	Fig. 1C
PMID:20876564	FYPO:0000841	Fig. 1B
PMID:20876564	FYPO:0004103	Fig. 1A
PMID:20876564	FYPO:0004103	Fig. 1A
PMID:20876564	FYPO:0004103	Fig. 1A
PMID:20876564	FYPO:0002024	Fig. 1A
PMID:20876564	FYPO:0001357	Fig. 1A
PMID:20876564	FYPO:0001357	Fig. 1A
PMID:20876564	FYPO:0001357	Fig. 1A and B
PMID:20876564	PBO:0093560	Fig. 1A
PMID:20885790	PBO:0093580	less sensitive than ssb3delta alone
PMID:20890290	PBO:0104007	Second, eRF1 and Dom34 increase the bind- ing 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 bind- ing 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:0108926	phosphorylated
PMID:20929775	PBO:0104309	K9-mehtylated
PMID:20929775	PBO:0108926	phosphorylated
PMID:20929775	PBO:0104309	K9 methyl;ated
PMID:20929775	PBO:0104309	K9-mehtylated
PMID:20929775	PBO:0108926	phosphorylated
PMID:20935472	PBO:0023853	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	PBO:0097626	Fig1A,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:0100727	Fig6D,E in presence of LatA + MBC there is no SPB separation compared to + MBC only where SPBs can separate
PMID:20967237	FYPO:0004318	Fig2B in this case (high temp + MBC) cells can proceed through cell cycle and replicate their DNA
PMID:20967237	FYPO:0007862	Fig5A
PMID:20967237	PBO:0100723	Fig4E
PMID:20967237	PBO:0100726	Fig4C followed the presence of clp1 in the nucleolus to monitor cen3
PMID:20967237	PBO:0100725	data not shown
PMID:20967237	PBO:0100724	Fig4B
PMID:20967237	PBO:0100723	Fig4D
PMID:20967237	PBO:0100722	Fig4A
PMID:20967237	PBO:0095672	Fig3G suggests nuclear fission is independent of spindle checkpoint
PMID:20967237	FYPO:0007859	video S3
PMID:20967237	PBO:0100721	Fig3E
PMID:20967237	PBO:0100720	Fig 3F
PMID:20967237	FYPO:0007859	Fig3 D
PMID:20967237	FYPO:0000133	Fig3C
PMID:20967237	FYPO:0002004	Fig3B just a short microtubule stub remains
PMID:20967237	FYPO:0007858	Fig2c in presence of MBC cells re-enter S phase earlier than in the absence of MBC
PMID:20967237	FYPO:0004367	Fig2c
PMID:20967237	FYPO:0003762	Fig2B 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	PBO:0100719	Fig2 A
PMID:20967237	PBO:0097954	Fig1D; microtubules absent
PMID:20967237	PBO:0100718	Fig1D
PMID:20967237	PBO:0100718	Fig1D
PMID:20967237	FYPO:0007858	Fig1D
PMID:20967237	PBO:0100718	Fig1E
PMID:20967237	PBO:0100718	Fig1C
PMID:20974849	PBO:0093559	Fig. 3B
PMID:20974849	PBO:0096312	Fig. 5E
PMID:20974849	PBO:0096314	Fig. 5E
PMID:20974849	PBO:0096832	Fig. 5C
PMID:20974849	PBO:0112442	Fig. 5D
PMID:20974849	PBO:0112441	Fig. 5D
PMID:20974849	PBO:0112440	Fig. 5C
PMID:20974849	PBO:0112439	Fig. 5B
PMID:20974849	PBO:0112438	Fig. 5A
PMID:20974849	PBO:0112437	Fig. 4C
PMID:20974849	PBO:0112436	Fig. 4C
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:0112431	Fig. 5G
PMID:20974849	PBO:0112433	Fig. 3C
PMID:20974849	PBO:0112433	Fig. 3C
PMID:20974849	PBO:0112432	Fig. 3C
PMID:20974849	PBO:0112432	Fig. 3C
PMID:20974849	PBO:0096312	Fig. 3B
PMID:20974849	PBO:0096311	Fig. 3B
PMID:20974849	FYPO:0000405	Fig. 3A
PMID:20974849	PBO:0096314	Fig. 3A
PMID:20974849	PBO:0112431	Fig. 3A
PMID:20974849	PBO:0096311	Fig. 3A
PMID:20974849	GO:2000045	Fig. 2
PMID:20974849	FYPO:0004481	Fig. 1C
PMID:20974849	PBO:0093558	Fig. 1C
PMID:20974849	PBO:0093556	Fig. 1C
PMID:20974849	PBO:0093561	Fig. 1C
PMID:20974849	PBO:0093559	Fig. 1C
PMID:20974849	PBO:0093559	Fig. 1C
PMID:20974849	PBO:0096314	Fig. 1D
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:20980623	PBO:0100821	Supplemental Figure S3
PMID:20980623	FYPO:0000587	the initiation of spore formation was delayed for 􏰃2 h com- pared 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:0100822	several types of defects in FSM de- velopment in dma1􏰁 cells (Figure 6B). These defects roughly fell into three classes: (1) initially FSM formation was normal and appeared as sphere structure, but subse- quently 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 com- pletely unable to sporulate under conditions in which single spg1-106 or mob1-1 mutants were not apparently compro- mised 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 com- pletely unable to sporulate under conditions in which single spg1-106 or mob1-1 mutants were not apparently compro- mised 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 com- pletely unable to sporulate under conditions in which single spg1-106 or mob1-1 mutants were not apparently compro- mised for sporulation (Figure 8, A and B), suggesting that Dma1 might function in parallel with Spg1 and Mob1 in sporulation.
PMID:20980623	PBO:0111998	Figure 3B Figure 4B the initiation of spore formation was delayed for 􏰃2 h com- pared 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	GO:0035974	fig2
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:21035342	PBO:0107586	"vw: 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). I agree the data supports this model."
PMID:21035342	PBO:0107586	"vw: 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). I agree the data supports this model."
PMID:21035342	PBO:0111686	"(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:21035342	GO:0019887	vw: bit 61 is importabt for torc2 regulation by ryh1
PMID:21095590	GO:0045739	phosphorylation of rad9 by DDK releases rad9 from damaged chromatin and allows repair factors to come in. fig6
PMID:21095590	GO:0045739	phosphorylation of rad9 by DDK releases rad9 from damaged chromatin and allows repair factors to come in. fig6
PMID:21095590	PBO:0110104	phosphorylation of rad9 by DDK releases rad9 from damaged chromatin and allows repair factors to come in. fig6
PMID:21095590	FYPO:0001931	fig 5b
PMID:21095590	FYPO:0001931	fig 5b
PMID:21098122	FYPO:0000267	no expressivity extension because of decreased growth when untreated
PMID:21098122	FYPO:0000267	no expressivity extension because of decreased growth when untreated
PMID:21098122	FYPO:0000268	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	no expressivity extension because of decreased growth when untreated
PMID:21098122	FYPO:0000268	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:0000085	no expressivity extension because of decreased growth when untreated
PMID:21098122	PBO:0104121	nuclease-dead allele
PMID:21098122	FYPO:0000268	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:0102368	25 degrees
PMID:21099360	PBO:0093581	same as hsk1-89 alone
PMID:21099360	PBO:0093581	same as hsk1-89 alone
PMID:21099360	PBO:0093581	same as hsk1-89 alone
PMID:21099360	PBO:0100922	30 degrees
PMID:21099360	PBO:0100922	30 degrees; same as hsk1-89 alone
PMID:21099360	PBO:0102368	25 degrees, same as hsk1-89 alone
PMID:21099360	FYPO:0001357	30 degrees; restrictive for hsk1-89 alone
PMID:21099360	PBO:0100922	30 degrees; same as hsk1-89 alone
PMID:21099360	PBO:0102368	25 degrees, same as hsk1-89 alone
PMID:21099360	PBO:0100922	30 degrees; same as hsk1-89 alone
PMID:21099360	PBO:0102368	25 degrees, same as hsk1-89 alone
PMID:21099360	PBO:0100922	30 degrees; same as hsk1-89 alone
PMID:21099360	PBO:0102368	25 degrees, same as hsk1-89 alone
PMID:21099360	PBO:0102370	in SQ/TQ clusters . , activated_by(CHEBI:29035)
PMID:21099360	PBO:0102371	not in SQ/TQ clusters
PMID:21099360	PBO:0100905	at ars2004 and oriChr2-1266, during early S phase
PMID:21099360	GO:0031573	hsk1 phenotypes more informative than mrc1 itself
PMID:21099360	FYPO:0001355	30 degrees
PMID:21099360	PBO:0094250	30 degrees
PMID:21099360	PBO:0102364	25 degrees
PMID:21099360	FYPO:0001382	MBP substrate
PMID:21107719	GO:0071944	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: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:21118717	GO:0047555	Active against both cAMP and cGMP based on its ability to confer resistance to exogenous cyclic nucleotides. Fig. 1A, B
PMID:21131906	PBO:0098869	un- ubiquitinated
PMID:21148300	PBO:0097265	Cdc42-GTP assayed with CRIB
PMID:21148300	PBO:0097265	Cdc42-GTP assayed with CRIB
PMID:21148300	PBO:0097265	Cdc42-GTP assayed with CRIB
PMID:21148300	PBO:0097265	Cdc42-GTP assayed with CRIB
PMID:21151114	PBO:0097281	independent of Clr4
PMID:21151114	PBO:0097131	independent of Clr4
PMID:21151114	PBO:0020366	SO:0000286 = LTR
PMID:21151114	PBO:0020366	SO:0000286 = LTR
PMID:21151114	PBO:0097280	independent of Clr4
PMID:21151114	PBO:0098170	independent of Clr4
PMID:21151114	PBO:0103746	independent of Clr4
PMID:21151114	PBO:0026298	independent of Clr4
PMID:21151114	PBO:0103747	independent of Clr4
PMID:21151114	PBO:0103748	independent of Clr4
PMID:21151114	PBO:0026298	independent of Clr4
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
PMID:21182284	MOD:00046	i) unknown kinase ii) asynchronous cells iii) unknown
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: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	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	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	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: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	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: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: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	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	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: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: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	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	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: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	GO:0033696	not sue if this is quite the correct term, but it is the old spreading term
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: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:0000089	We also found that asf1-1 cells were hypersensitive to genotoxic agents such as bleomycin, camptothecin and methylmethane sulfonate (Figure S6)
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: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	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	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	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: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:21256022	PBO:0102183	affecting dis1
PMID:21256022	GO:0005515	binding site L405 ndc80 loop
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	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: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	FYPO:0001355	fig7
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	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	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	PBO:0095159	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: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:0094506	Fig. 2A and E
PMID:21376600	PBO:0112276	Fig. 1B
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	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	PBO:0112296	Fig. S3H
PMID:21376600	PBO:0112294	Fig. S3H
PMID:21376600	PBO:0112297	Fig. 4B
PMID:21376600	PBO:0112298	Fig. 4B
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: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:21389117	PBO:0107807	fig2A
PMID:21389117	PBO:0107794	I'm not completely sure if the Slp1-APC degrades mes1 or only ubiquitinates it, but this is most likely correct?...
PMID:21389117	FYPO:0000587	fig 1B: 4 nuclei appear later than normal.
PMID:21389117	FYPO:0003379	fig 1c, no tetranucleates
PMID:21389117	GO:0005515	fig 7A
PMID:21389117	GO:0005515	fig 7A
PMID:21389117	FYPO:0005382	also fzr3
PMID:21389117	FYPO:0004994	fig2B
PMID:21389117	GO:1990950	i changed this to +ve reg /AL
PMID:21389117	FYPO:0005382	also fzr2 &3
PMID:21389117	FYPO:0001000	fig 1B: 4 nuclei appear later than normal.
PMID:21389117	FYPO:0003379	fig2B
PMID:21389117	FYPO:0003380	fig2B
PMID:21389117	FYPO:0005412	fig 1B: 4 nuclei appear later than normal.
PMID:21389117	PBO:0104199	fig 6C
PMID:21389117	PBO:0104199	fig 6C
PMID:21389117	FYPO:0003379	fig2A
PMID:21389117	PBO:0107804	fig2A
PMID:21389117	GO:0005515	fig 7A
PMID:21389117	GO:0005515	fig 7A
PMID:21422229	PBO:0114258	Rng2 subsequently recruits the myosin­II subunits Myo2 and Rlc1.
PMID:21429938	PBO:0095337	cross between h+ and h- deletions, allowed to sporulate immediately
PMID:21429938	PBO:0095338	cross between h+ and h- deletions, allowed to sporulate immediately
PMID:21429938	FYPO:0002485	cross between h+ and h- deletions, allowed to sporulate immediately
PMID:21429938	PBO:0097898	cross between h+ and h- deletions, allowed to sporulate immediately
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	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: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	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	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	FYPO:0004201	Interestingly, mlo3-A caused a decrease in levels of centromeric siRNA as compared to WT (Fig. 2D).
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	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:0110846	Recombinant Clr4 could methylate the carboxy- terminal 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	GO:0140746	[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	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	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:21437270	FYPO:0005371	ch16
PMID:21441914	FYPO:0000268	no expressivity extension because of decreased growth when untreated
PMID:21441914	FYPO:0000085	no expressivity extension because of decreased growth when untreated
PMID:21441914	FYPO:0000267	no expressivity extension because of decreased growth when untreated
PMID:21441914	FYPO:0000268	no expressivity extension because of decreased growth when untreated
PMID:21441914	FYPO:0000088	no expressivity extension because of decreased growth when untreated
PMID:21441914	FYPO:0000085	no expressivity extension because of decreased growth when untreated
PMID:21441914	FYPO:0000267	no expressivity extension because of decreased growth when untreated
PMID:21441914	FYPO:0000268	no expressivity extension because of decreased growth when untreated
PMID:21441914	FYPO:0000088	no expressivity extension because of decreased growth when untreated
PMID:21441914	FYPO:0000085	no expressivity extension because of decreased growth when untreated
PMID:21441914	FYPO:0000267	no expressivity extension because of decreased growth when untreated
PMID:21441914	FYPO:0000088	no expressivity extension because of decreased growth when untreated
PMID:21441914	FYPO:0000088	no expressivity extension because of decreased growth when untreated
PMID:21441914	FYPO:0000085	no expressivity extension because of decreased growth when untreated
PMID:21441914	FYPO:0000088	no expressivity extension because of decreased growth when untreated
PMID:21441914	FYPO:0000268	no expressivity extension because of decreased growth when untreated
PMID:21441914	FYPO:0000267	no expressivity extension because of decreased growth when untreated
PMID:21441914	FYPO:0000085	no expressivity extension because of decreased growth when untreated
PMID:21441914	FYPO:0000267	no expressivity extension because of decreased growth when untreated
PMID:21441914	FYPO:0000268	no expressivity extension because of decreased growth when untreated
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:0112688	(with ofd1)
PMID:21481773	PBO:0112689	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:0112690	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:0112684	Ofd1 was enriched in the nucleus with little cytosolic staining consistent with previous findings (Fig. 3A)(
PMID:21481773	PBO:0112685	Ofd1 was enriched in the nucleus with little cytosolic staining consistent with previous findings (Fig. 3A)(
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:0112757	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:21518960	PBO:0105449	comment assayed at ars1 and ars2004
PMID:21518960	PBO:0105448	assayed elongation from ars1 and ars2004 (early-firing origins)
PMID:21518960	FYPO:0001249	assayed at ars1 and ars2004 (early-firing origins)
PMID:21518960	FYPO:0005108	assayed elongation from ori1-200
PMID:21518960	PBO:0100905	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:0005107	comment assayed at ars1 and ars2004
PMID:21518960	PBO:0105447	assayed at ars1 and ars2004 (early-firing origins)
PMID:21518960	FYPO:0001249	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:21536008	GO:0016651	"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:0035577	t-shift on mitotic entry fig1d
PMID:21540296	PBO:0035593	figure 7c, no rescue of cnd-2
PMID:21540296	FYPO:0002061	fig 1a
PMID:21540296	FYPO:0002061	figure 7c, no rescue of cnd-2
PMID:21540296	PBO:0035578	t-shift on mitotic entry fig1d
PMID:21540296	PBO:0035579	t-shift on mitotic entry fig1c
PMID:21540296	PBO:0035579	t-shift on mitotic entry fig1c
PMID:21540296	FYPO:0001513	t-shift on mitotic entry fig1c
PMID:21540296	PBO:0103824	t-shift on mitotic entry fig1c
PMID:21540296	FYPO:0005424	t-shift on mitotic entry fig1c
PMID:21540296	PBO:0035583	fig 4
PMID:21540296	MOD:00046	fig 5c
PMID:21540296	PBO:0035592	fig 7a
PMID:21540296	FYPO:0002061	fig 1a
PMID:21540296	FYPO:0002060	fig 1a
PMID:21540296	PBO:0035591	fig 7a
PMID:21540296	PBO:0035590	fig 7a
PMID:21540296	PBO:0035590	fig 7a
PMID:21540296	PBO:0035590	fig 7a
PMID:21540296	PBO:0035594	figure 7e
PMID:21540296	PBO:0035592	fig 7a
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	sulphate
PMID:21633354	PBO:0093730	condensin, which subunit assayed?
PMID:21633354	PBO:0093730	all tested chromosome loci (Fig. 2g).
PMID:21633354	PBO:0093730	all tested chromosome loci (Fig. 2g).
PMID:21633354	FYPO:0003286	decreased along arms
PMID:21633354	PBO:0107914	H3-pS10 used to detect ark1 activity
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: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	PBO:0107913	centromeric
PMID:21652630	FYPO:0000421	see S5A
PMID:21652630	FYPO:0002858	in fig s4b there is septal material hanging around one cell end
PMID:21664573	FYPO:0002060	(Figure 1D, Supplemental Figure 2A)
PMID:21664573	FYPO:0002060	(Supplemental Figure 2B)
PMID:21664573	FYPO:0002061	(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	PBO:0036897	in vitro (Figure 1C & 2D)
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:0111958	fig 1A
PMID:21664573	PBO:0111957	fig 1A
PMID:21664573	PBO:0111956	fig 1A
PMID:21664573	FYPO:0002060	(Supplemental Figure 2B)
PMID:21664573	FYPO:0002060	(Supplemental Figure 2B)
PMID:21664573	FYPO:0002060	(Supplemental Figure 2B)
PMID:21664573	FYPO:0005726	fig 2 b c
PMID:21664573	FYPO:0005727	fig 2 b
PMID:21664573	FYPO:0005727	fig 3 b
PMID:21664573	FYPO:0000168	ABOLISHED Fig 2 C
PMID:21664573	PBO:0036897	Figure 5B
PMID:21664573	FYPO:0005727	fig 3 b
PMID:21664573	FYPO:0005728	Fig 4c NORMAL SILENCING
PMID:21664573	FYPO:0005728	Fig 4d NORMAL SILENCING
PMID:21664573	FYPO:0005728	Fig 4d NORMAL SILENCING
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 3 b
PMID:21676862	GO:0071933	Fig 1
PMID:21693583	PBO:0102393	Fig. 8B
PMID:21693583	GO:0030036	MF? myo1
PMID:21693583	PBO:0102392	Fig. 8A
PMID:21693583	FYPO:0001234	Fig. 8B
PMID:2170029	FYPO:0006822	high temp is permissive
PMID:2170029	FYPO:0001234	high temp is permissive
PMID:2170029	PBO:0095579	std temp is restrictive
PMID:2170029	PBO:0095578	high temp is permissive
PMID:2170029	FYPO:0001234	temperature restrictive for dis2cs alone
PMID:2170029	FYPO:0001234	temperature restrictive for dis2cs alone
PMID:2170029	FYPO:0001234	temperature restrictive for dis2cs alone
PMID:2170029	FYPO:0002061	temperature permissive for dis2cs alone
PMID:2170029	FYPO:0001234	temperature restrictive for dis2cs alone
PMID:2170029	FYPO:0002061	temperature restrictive for dis2cs alone
PMID:21703453	GO:0051285	Requires auto-phosphorylation to be restricted to cell tips (not restricted to cell tips for Pom1-6A and Pom1-KD allele)s
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	GO:0051286	Requires auto-phosphorylation to be restricted to cell tips (not restricted to cell tips for Pom1-6A and Pom1-KD allele)s
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: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	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	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	MOD:00046	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	GO:0051286	Requires auto-phosphorylation to be restricted to cell tips (not restricted to cell tips for Pom1-6A and Pom1-KD allele)s
PMID:21703453	PBO:0096617	(comment: required for detachment from plasma membrane)
PMID:21703453	PBO:0096616	(comment: required for detachment from plasma membrane)
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	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: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	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	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:2172964	FYPO:0000761	both partners cyr1delta
PMID:21775631	PBO:0101474	Figure S2A
PMID:21775631	PBO:0101474	Figure S2A
PMID:21775631	PBO:0097865	Figure S2B
PMID:21775631	FYPO:0001915	Figure 1A Figure 5D
PMID:21775631	PBO:0101474	Figure S2A
PMID:21775631	PBO:0101475	Figure S2B
PMID:21775631	PBO:0100820	Figure S2B
PMID:21811607	FYPO:0001460	basal transcription is meaningless because emm contains calcium
PMID:21813639	GO:1902969	candidate for involved_in_or_involved_in_regulation_of qualifier
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: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: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:0113558	Fig. 3
PMID:21828039	PBO:0113559	Fig. 3
PMID:21828039	PBO:0100415	Fig. 4B
PMID:21828039	PBO:0100415	Fig. 4B
PMID:21828039	PBO:0100415	Fig. 4B
PMID:21828039	PBO:0113560	Fig. 4B
PMID:21828039	PBO:0108340	Fig. 4G
PMID:21828039	PBO:0113561	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: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	endosomal localization requires F-actin (assayed using latrunculin A)
PMID:21847092	GO:0008270	bound by the C-terminal dsrbd domain
PMID:21849474	PBO:0098573	Fig5
PMID:21849474	PBO:0098574	Fig 6A fusion protein driven from nmt41 promoter
PMID:21849474	FYPO:0006616	Fig 1B
PMID:21849474	PBO:0098572	Fig5
PMID:21849474	FYPO:0006616	Fig 1B
PMID:21849474	PBO:0098564	Fig 3 cell width is wider than either of the single mutants
PMID:21849474	PBO:0098563	Fig 3 increased cell width compared to single mutants
PMID:21849474	PBO:0098563	Fig 3 increased cell width compared to single mutants
PMID:21849474	FYPO:0001294	Fig 2 C
PMID:21849474	FYPO:0001294	Fig 2 C
PMID:21849474	FYPO:0001293	Fig2B
PMID:21849474	FYPO:0006616	Fig 1A
PMID:21849474	PBO:0098580	Fig4D
PMID:21849474	FYPO:0006616	Fig 1B
PMID:21849474	FYPO:0006616	Fig 1B
PMID:21849474	FYPO:0006616	Fig 1B
PMID:21849474	FYPO:0006616	Table 1 not suppressed by sorbitol
PMID:21849474	FYPO:0006617	Table 1A
PMID:21849474	FYPO:0006617	Fig 1A
PMID:21849474	FYPO:0006617	Fig 1A
PMID:21849474	FYPO:0006616	Table 1 not suppressed by sorbitol
PMID:21849474	FYPO:0006616	Fig 1B
PMID:21849474	FYPO:0006616	Table 1 not suppressed by sorbitol
PMID:21849474	FYPO:0006617	Fig 1A
PMID:21849474	FYPO:0006616	Table 1 not suppressed by sorbitol
PMID:21849474	FYPO:0006616	Table 1 not suppressed by sorbitol
PMID:21849474	FYPO:0006616	Table 1 not suppressed by sorbitol
PMID:21849474	FYPO:0006616	Table 1 not suppressed by sorbitol
PMID:21849474	FYPO:0006616	Table 1 not suppressed by sorbitol
PMID:21849474	FYPO:0006616	Table 1 not suppressed by sorbitol
PMID:21849474	FYPO:0006616	Table 1 not suppressed by sorbitol
PMID:21849474	FYPO:0002104	Table 1 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	PBO:0098571	Fig5
PMID:21849474	FYPO:0006616	Fig 1B
PMID:21849474	PBO:0098568	Fig4B
PMID:21849474	GO:0031520	Fig4B, Fig8 localisation is actin dependent
PMID:21849474	GO:0031520	Fig4B, Fig8 localisation is actin dependent
PMID:21849474	GO:0016328	Fig4A
PMID:21849474	PBO:0098569	Fig4C
PMID:21849474	PBO:0098570	Fig4D
PMID:21849474	FYPO:0001293	Fig2B
PMID:21849474	GO:0031520	Fig9 cdc42-CRIB-GFP localisation is actin dependent and sensitive to low levels (10mM) Lat A
PMID:21849474	PBO:0098579	Fig7A, 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	PBO:0098578	Fig7A, B
PMID:21849474	PBO:0098577	Fig6C
PMID:21849474	PBO:0098575	Fig 6B fusion protein driven from nmt41 promoter
PMID:21849474	PBO:0098576	Fig6C
PMID:21849474	FYPO:0006617	Fig 1A
PMID:21849474	FYPO:0006617	Fig 1A
PMID:21849474	FYPO:0006617	Fig 1A Fig2A
PMID:21849474	FYPO:0006617	Fig 1A
PMID:21849474	PBO:0098567	Fig4B
PMID:21849474	FYPO:0006617	Fig1A Fig2A
PMID:21849474	FYPO:0006617	Fig 1A
PMID:21849474	PBO:0098566	Figure 4 A
PMID:21849474	PBO:0098565	Figure 4 A
PMID:21849474	PBO:0098565	Figure 4 A
PMID:21849474	FYPO:0006616	Fig 3 no increase in cell width compared to single mutants
PMID:21849474	FYPO:0006616	Fig 1B
PMID:21885283	FYPO:0002061	TAble II
PMID:21885283	FYPO:0000422	Figure 2A
PMID:21885283	FYPO:0000422	Figure 2A
PMID:21885283	GO:0072583	Figure 2A
PMID:21885283	GO:0030139	Figures 1A, 1B and S1B - S1I; TableI
PMID:21885283	PBO:0099724	Figure S1K
PMID:21885283	PBO:0107961	Figure S1K
PMID:21885283	FYPO:0002060	Table I
PMID:21885283	GO:0072583	Figure 2A
PMID:21885283	FYPO:0002060	Table I
PMID:21885283	PBO:0018844	Figures 1A, 1B and S1B - S1I; TableI
PMID:21885283	FYPO:0002061	TAble II
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	FYPO:0000082	TAble II
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:0018470	Figures 1A, 1B and S1B - S1I; TableI
PMID:21885283	PBO:0097713	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:0018345	Figures 1A, 1B and S1B - S1I; TableI
PMID:21885283	PBO:0018345	Figures 1A, 1B and S1B - S1I; TableI
PMID:21885283	PBO:0097629	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	GO:0034314	Figure 2A
PMID:21885283	PBO:0107966	Figure 3G
PMID:21885283	PBO:0107965	Figure 3D
PMID:21885283	PBO:0107964	Figure 3C
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	FYPO:0002060	Table I
PMID:21885283	FYPO:0002060	Table I
PMID:21885283	FYPO:0002060	Table I
PMID:21885283	FYPO:0002060	Table I
PMID:21885283	PBO:0098289	Figures 1A, 1B and S1B - S1I; TableI
PMID:21892171	FYPO:0006992	(Supplementary Fig. 1)
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:21892171	PBO:0093562	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	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	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	FYPO:0004065	and changes in the distribution of RNAPII at body of genes (Supplementary Fig. 3c)
PMID:21892171	PBO:0104709	resulted in variegated suppression of silencing defects in ago1Δ and dcr1Δ mutants (Fig. 2b and Supplementary Fig. 2b)
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:0097401	In contrast, mlo3Δ resulted in considerable restoration of H3K9me at centromeres in clr3Δ ago1Δ cells (Fig. 3b).
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: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	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: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:0105770	***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	(Fig. 1a).
PMID:21892171	FYPO:0006992	(Supplementary Fig. 1)
PMID:21892183	PBO:0104112	microtubule sliding brake https://www.ebi.ac.uk/interpro/entry/InterPro/IPR007882/#PUB00070924
PMID:21920317	PBO:0097918	Fig 6
PMID:21920317	PBO:0109779	fig 4B
PMID:21920317	PBO:0112506	fig 4
PMID:21920317	PBO:0112505	>inc merotelic kinetochore attachment
PMID:21920317	PBO:0112504	Fig 4 B
PMID:21920317	FYPO:0005383	Fig 4 A
PMID:21920317	PBO:0109773	fig 1D
PMID:21920317	PBO:0035389	( Figure S3 A)
PMID:21920317	PBO:0037712	( Figure 1 A) 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:0037711	fig 1D although sister kinetochore sometimes split, segregation ends up mostly normal
PMID:21920317	PBO:0112502	fig 1D
PMID:21920317	GO:0031619	prevents bipolar attachment (Ask Takeshi if this fits better rec role)
PMID:21920317	GO:0031619	prevents bipolar attachment
PMID:21920317	GO:0031619	prevents bipolar attachment
PMID:21920317	PBO:0035382	( Figure 1 A) continuous rate of spindle elongation (I)
PMID:21920317	PBO:0097907	( Figure 1B)
PMID:21920317	FYPO:0005512	( Figure 1B) We found that virtually all rec12D cells (n = 240) eventually relo- calized Ark1 to the spindle (Figure 1B), indicating that the SAC ultimately becomes satisfied in achiasmate meiosis.
PMID:21920317	FYPO:0003177	Figure 1C, 1D bipolar attachment of univalents
PMID:21920317	PBO:0112502	fig 1D
PMID:21920317	PBO:0109773	fig 1D
PMID:21920317	PBO:0037711	fig 1D although sister kinetochore split, segregation ends up mostly normal
PMID:21931816	PBO:0099311	Ser-2 of the heptad repeat
PMID:21945095	GO:0043596	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	PBO:0100906	during replication fork processing
PMID:21945095	PBO:0100906	during replication fork processing
PMID:21945095	PBO:0100906	during replication fork processing
PMID:21945095	PBO:0100905	during mitotic DNA replication initiation
PMID:21945095	PBO:0100905	during mitotic DNA replication initiation
PMID:21945095	GO:0031261	also inferred from interaction with Cdc23 and from timing of localization to chromatin at origins
PMID:21945095	PBO:0100906	during replication fork processing
PMID:21945095	PBO:0100905	during mitotic DNA replication initiation
PMID:21949882	GO:0016706	moved down from GO:0016706 30/8/2014 . activated_by(CHEBI:29033)
PMID:21965289	GO:1902425	dis2 is required for the retreival of unclustered kinetochores in nsk delete (additive chromosome segregation defects)
PMID:21979813	PBO:0096909	1B
PMID:21979813	PBO:0096911	2C
PMID:21979813	PBO:0096912	2C
PMID:21979813	PBO:0096914	Fig 4AB
PMID:21979813	FYPO:0000209	2B abolished mono orientation at meiosis I
PMID:21979813	PBO:0096911	2C
PMID:21979813	PBO:0096911	2C
PMID:21979813	PBO:0096915	4E decreased kinetochore mono orientation at meiosis I
PMID:21979813	PBO:0096915	4E decreased kinetochore mono orientation at meiosis I
PMID:21979813	PBO:0096915	4E decreased kinetochore mono orientation at meiosis I
PMID:21979813	FYPO:0000209	2B abolished kinetochore mono orientation at meiosis I
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:0110278	In agreement with the direct role of Rpl30-1 in the control of rpl30-2 expression, excess Rpl30-1 re- sulted 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	XXXXXXXinresponse to high termperatureXXXXXXX. 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. Accord- ingly, 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	XXXXXXXinresponse to high termperatureXXXXXXX. 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	Impor- tantly, 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	Impor- tantly, 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	Similarly, a Pab2 variant in which the 11 arginine resi- dues within the arginine/glycine-rich domain were substituted to alanine (R-to-A) showed no poly(A) binding (Figure S3)
PMID:21981922	FYPO:0002926	he 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: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:0110274	Consistent with this, rpl30-2 expression levels were unaffected in the rrp6D strain when rpl30-2 was ex- pressed from the intronless construct (Figure 1B, lanes 4 and 6), similar to results using the pab2D mutant (Figure 1B, lane 5).
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	PBO:0110274	Similar results were obtained with a conditional strain in which the genomic copy of mtr4 is expressed from the thiamine-sensi- tive nmt1+ promoter: depletion of Mtr4 did not affect rpl30-2 pre- mRNA and mRNA levels (Figure 2D, compare lanes 3 and 7)
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	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	In contrast, no cumulative increase in the levels of rpl30-2 tran- scripts 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: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: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	Northern blot analysis of RNA prepared from the rrp6D strain revealed robust upregu- lation of rpl30-2 mRNA and pre-mRNA, 5- and 18-fold, respec- tively (Figure 2A, lane 7, and Figures 2B and 2C),
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: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: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 slower- migrating rpl30-2 transcript is the unspliced pre-mRNA (Fig- ure 1A, lane 4).
PMID:22017871	PBO:0104135	ubiquitin dependent due to need for rhp6 -AL
PMID:22017871	PBO:0104142	vw updated
PMID:22017871	PBO:0104138	fig 7c shows direct dna binding
PMID:22017871	PBO:0104136	ubiquitin dependent due to need for rhp6 -AL
PMID:22017871	PBO:0104135	ubiquitin dependent due to need for rhp6 -AL
PMID:22024164	FYPO:0002061	30 degrees
PMID:22024164	FYPO:0001249	early-firing origins; HU absent
PMID:22024164	FYPO:0001250	genome-wide detection
PMID:22024164	FYPO:0001249	at late-firing or dormant origins; genome-wide detection
PMID:22024164	PBO:0098899	genome-wide detection
PMID:22024164	FYPO:0001387	"30 degrees, ""high"" compared to 25 degrees"
PMID:22024164	FYPO:0001250	assayed using ars2004; not abolished as in hsk1delta alone (but single mutant not shown)
PMID:22024164	FYPO:0001250	assayed using ars2004; not abolished as in hsk1delta alone (but single mutant not shown)
PMID:22024164	FYPO:0001357	actually 25 degrees, but calling it low to make distinction from inviable at 30
PMID:22024164	FYPO:0002061	30 degrees
PMID:22024164	FYPO:0001249	at late-firing or dormant origins; genome-wide detection
PMID:22024167	PBO:0095671	vw >50% activity
PMID:22033972	GO:0032798	structure
PMID:2203537	PBO:0098343	Figure 3 A
PMID:2203537	PBO:0105792	Figure 3 A
PMID:2203537	PBO:0037182	30% at 120 min. (archery bow)
PMID:2203537	PBO:0035360	85% at 160 min
PMID:2203537	PBO:0035363	Figure 3 A
PMID:22042620	FYPO:0007426	Fig. 3 and Fig. S3, for comparative images of an inserted pro-metaphase wild-type SPB, see Fig. S1 B
PMID:22042620	FYPO:0002328	Fig. S5 B
PMID:22042620	GO:0006998	fig7
PMID:22042620	GO:0006998	fig7
PMID:22042620	FYPO:0000135	Fig. 7 indicated by NDB cholesterol
PMID:22042620	GO:0006643	fig7
PMID:22042620	FYPO:0002328	Fig. S5 B
PMID:22042620	FYPO:0002237	Fig. S5 B
PMID:22042620	FYPO:0002328	Fig. S5 B
PMID:22042620	FYPO:0002328	Fig. S5 B
PMID:22042620	FYPO:0000338	Fig. S5 B
PMID:22042620	GO:0090307	not required after insertion
PMID:22042620	PBO:0104497	Fig. S2, B and C
PMID:22042620	PBO:0104497	Fig. 1, A and B;
PMID:22042620	FYPO:0002237	Fig. S5 B
PMID:22042869	PBO:0113784	Fig. 6C
PMID:22042869	PBO:0113785	Abp1 bound to the swi2 pro- moter region facilitates preferential targeting of Mc, which normally binds an M-box sequence motif to activate M-specific genes
PMID:22042869	PBO:0113783	Fig. 6A
PMID:22042869	PBO:0113782	Fig. 6A and B
PMID:22042869	PBO:0106419	Abp1 is localized at the swi2 promoter (Fig. 6A), in addition to its localization at LTRs.
PMID:22042869	PBO:0113776	Abp1 is localized at the swi2 promoter (Fig. 6A), in addition to its localization at LTRs.
PMID:22042869	PBO:0112663	Fig. 5
PMID:22042869	PBO:0113781	Fig. 4B
PMID:22042869	PBO:0113780	Fig. 4A
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:0113779	Fig. 3B
PMID:22042869	PBO:0113778	Fig. 3B
PMID:22042869	PBO:0113777	Fig. 3B
PMID:22042869	PBO:0113776	Fig. 3B
PMID:22042869	PBO:0112929	Fig. 2B
PMID:22042869	FYPO:0000472	Fig. 2A
PMID:22042869	FYPO:0000472	Fig. 2A
PMID:22042869	PBO:0112929	Fig. 2A
PMID:22042869	PBO:0112929	Fig. 2A and B
PMID:22042869	PBO:0112929	Fig. 2B
PMID:22064476	FYPO:0003244	tested using several genes, and reporter construct to test mutations at or near splice sites
PMID:22065639	PBO:0022135	GO:0000236= mitotic prometaphase
PMID:22081013	PBO:0107598	3f In marked contrast, subtelomeric tlh transcripts (Figure 3a) accumulated in chp1ΔC strains (Figure 3b,e Supplementary Figure 9).
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	3g
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:22081013	PBO:0107597	3f
PMID:22084197	GO:0006284	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	PBO:0095396	(Figure 6A)
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:22093869	FYPO:0003928	The phenotype is assessed by the high-throughput sequencing.
PMID:22093869	FYPO:0003928	The phenotype is assessed by the high-throughput sequencing.
PMID:22093869	FYPO:0003928	The phenotype is assessed by the high-throughput sequencing.
PMID:22093869	FYPO:0003928	The phenotype is assessed by the high-throughput sequencing.
PMID:22119525	FYPO:0001226	fig 2A
PMID:22132152	PBO:0096345	fig 8 increased calcinurin activity
PMID:22132152	GO:0005789	n agreement, the corresponding fractions 15–22 iso- lated from the fission yeast strain expressing GFP-tagged Cta4p were immuno-reactive with anti-GFP antibodies
PMID:22132152	PBO:0107589	fig 6
PMID:22132152	FYPO:0001457	fig 5
PMID:22132152	FYPO:0000843	fig 5
PMID:22132152	FYPO:0006707	fig 2, 4
PMID:22132152	FYPO:0006706	fig 2
PMID:22132152	FYPO:0001198	fig 1, 7
PMID:22132152	PBO:0107591	fig 6
PMID:22132152	PBO:0107590	fig 6
PMID:22134091	FYPO:0000964	fig S2
PMID:22134091	FYPO:0006180	fig 1c
PMID:22134091	FYPO:0003307	22.3%
PMID:22134091	PBO:0100712	fig2B
PMID:22134091	PBO:0100713	fig2AB
PMID:22134091	PBO:0100714	fig2
PMID:22134091	FYPO:0000274	Fig. S3A
PMID:22134091	FYPO:0003566	Fig.
PMID:22134091	FYPO:0000276	ig. S1B-j
PMID:22134091	FYPO:0000903	fig3
PMID:22134091	FYPO:0000903	fig3
PMID:22134091	FYPO:0005681	in vitro
PMID:22134091	FYPO:0005681	in vitro
PMID:22134091	FYPO:0005681	in vitro
PMID:22134091	FYPO:0005681	in vitro
PMID:22134091	FYPO:0001943	increased affinity
PMID:22134091	FYPO:0002636	fig7F
PMID:22134091	FYPO:0002636	fig7F
PMID:22140232	PBO:0102621	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:0102610	same as ssp2delta alone
PMID:22140232	FYPO:0001176	same as ssp2delta alone
PMID:22140232	PBO:0093796	same as ssp2delta alone
PMID:22140232	PBO:0093796	same as ssp2delta alone
PMID:22140232	PBO:0102609	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:22140232	PBO:0102612	same as ssp2delta alone
PMID:22140232	FYPO:0005742	same as ssp2delta alone
PMID:22140232	PBO:0102616	same as ssp2delta alone
PMID:22140232	PBO:0102611	same as ssp2delta alone
PMID:22144463	GO:1902801	negative ::
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:1902794	during vegetative growth, near genes normally expressed in meiotic cell cycle
PMID:22144463	GO:1902794	during vegetative growth, near genes normally expressed in meiotic cell cycle
PMID:22144909	PBO:0106387	(serine 2)
PMID:22172946	PBO:0037495	fig3
PMID:22172946	PBO:0037494	fig 2
PMID:22172946	PBO:0037494	fig 2
PMID:22172946	PBO:0093678	fig 1 a
PMID:22172946	PBO:0093678	fig 1 a
PMID:22173095	PBO:0102374	fig 7 sdj mutant is unstable
PMID:22173095	PBO:0102372	abolished homodimerization Fig. 6,
PMID:22173095	PBO:0102373	fig 7
PMID:22173095	PBO:0102374	fig 7 sdj mutant is unstable
PMID:22180499	FYPO:0003335	floculation inhibited by galactose
PMID:22184248	FYPO:0002061	fig 1a
PMID:22184248	FYPO:0002061	fig 1a
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 ac- tivation. We speculate that partially degraded Mph1-KD pro- teins (Fig. S2B) might be toxic to some extent.
PMID:22184248	FYPO:0002060	figure 1a
PMID:22184248	FYPO:0002060	figure 1a
PMID:22184248	FYPO:0002060	figure 1a
PMID:22184248	FYPO:0002060	figure 1a
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 ac- tivation. We speculate that partially degraded Mph1-KD pro- teins (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: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 ac- tivation. We speculate that partially degraded Mph1-KD pro- teins (Fig. S2B) might be toxic to some extent.
PMID:22184248	FYPO:0000620	As shown in Fig. 3A, ex- pression of Mph1-Ndc80-GFP from pREP81 caused an arrest in the wild-type background.
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	PBO:0099035	recruitment (is this the right way around?)
PMID:22184248	GO:0005515	recruitment
PMID:22184248	FYPO:0000620	As shown in Fig. 3A, ex- pression of Mph1-Ndc80-GFP from pREP81 caused an arrest in the wild-type background.
PMID:22235339	PBO:0103123	also assayed using bulk histones from calf thymus
PMID:22235339	PBO:0103125	also assayed using bulk histones from calf thymus
PMID:22235339	PBO:0103124	also assayed using bulk histones from calf thymus
PMID:22267499	GO:0005737	Both the GFP-Ypa1p and GFP-Ypa2p proteins showed a uniform cyto- plasmic localization and a faint nuclear signal.
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: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	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: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:0002061	Figure 1 A
PMID:22267499	PBO:0095634	Figure 1 A
PMID:22267499	FYPO:0001357	Figure 1 A
PMID:22267499	FYPO:0001357	Figure 1 A
PMID:22267499	PBO:0094648	Figure 1 A
PMID:22267499	PBO:0094648	Figure 1 A
PMID:22267499	GO:0005737	Both the GFP-Ypa1p and GFP-Ypa2p proteins showed a uniform cyto- plasmic localization and a faint nuclear signal.
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	FYPO:0002061	The double mutant wee1-50 ypa2–D was syntheti- cally lethal, with the germinating spore giving rise to one or two small, rounded cells at 29 (DNS)
PMID:22267499	FYPO:0002280	The double mutant wee1-50 ypa2–D was syntheti- cally lethal, with the germinating spore giving rise to one or two small, rounded cells at 29 (DNS)
PMID:22267499	PBO:0111473	Table 3
PMID:22267499	PBO:0111474	Table 3
PMID:22267499	PBO:0111475	Table 3
PMID:22267499	PBO:0111476	Table 3
PMID:22267499	PBO:0111477	Table 3
PMID:22267499	PBO:0111478	Table 3
PMID:22267499	PBO:0111479	Table2
PMID:22267499	PBO:0111480	Table2
PMID:22267499	FYPO:0006802	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	FYPO:0000648	Figure 4b
PMID:22267499	FYPO:0000648	Figure 4b
PMID:22267499	FYPO:0004103	Figure 4b
PMID:22267499	FYPO:0004103	Figure 4b
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	GO:0031029	These data therefore implicate Ypa2p and Ppa2p in establishing SIN protein asymmetry during anaphase.
PMID:22268381	PBO:0096783	localization of Dcr1-GFP and GFP-Ago1 was not affected by the loss of Sal3 activity (Figure S1).
PMID:22268381	PBO:0096782	ocalization of Dcr1-GFP and GFP-Ago1 was not affected by the loss of Sal3 activity (Figure S1).
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	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:0096787	fig 5
PMID:22268381	PBO:0096786	fig 5
PMID:22268381	FYPO:0001513	fig 5
PMID:22268381	PBO:0096785	fig 5
PMID:22268381	FYPO:0000091	fig 4
PMID:22268381	FYPO:0000091	fig 4
PMID:22268381	FYPO:0000220	Pericentric transcript levels are increased in sal3 mutants
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:22279046	FYPO:0000085	same as hsk1-89 alone
PMID:22279046	FYPO:0000268	same as hsk1-89 alone
PMID:22279046	FYPO:0000088	same as hsk1-89 alone
PMID:22279046	FYPO:0001249	same as hsk1-89 alone
PMID:22279046	FYPO:0000088	same as hsk1-89 alone
PMID:22279046	FYPO:0000089	same as hsk1-89 alone
PMID:22279046	FYPO:0000085	same as hsk1-89 alone
PMID:22279046	FYPO:0000089	same as hsk1-89 alone
PMID:22279046	FYPO:0000268	same as hsk1-89 alone
PMID:22291963	PBO:0097785	mild expressivity
PMID:22291963	GO:0005634	in asf1-33 at higher temperature
PMID:22292001	PBO:0104342	5c
PMID:22292001	PBO:0104345	5
PMID:22292001	FYPO:0000674	5
PMID:22292001	PBO:0104342	5c
PMID:22292001	PBO:0104344	5c
PMID:22292001	FYPO:0007102	5d
PMID:22292001	FYPO:0007102	5d
PMID:22292001	PBO:0093558	5
PMID:22292001	PBO:0093557	5
PMID:22292001	PBO:0093558	5
PMID:22292001	FYPO:0000678	fig4
PMID:22292001	FYPO:0007105	fig3e
PMID:22292001	FYPO:0007105	fig3e
PMID:22292001	FYPO:0006419	fig3d
PMID:22292001	FYPO:0007104	fig2
PMID:22292001	FYPO:0006426	fig2
PMID:22292001	FYPO:0000678	fig2
PMID:22292001	FYPO:0007103	1d
PMID:22292001	FYPO:0007102	1d
PMID:22292001	FYPO:0000913	1a
PMID:22292001	FYPO:0007102	5d
PMID:22292001	FYPO:0007101	during meiosis I
PMID:22292001	FYPO:0007101	1d
PMID:22292001	GO:0000712	"strong contender for GO's ""acts upstream of or within"" (RO:0002264) gp-term relation"
PMID:22292001	GO:0000712	"strong contender for GO's ""acts upstream of or within"" (RO:0002264) gp-term relation"
PMID:22292001	FYPO:0007101	during meiosis I
PMID:22292001	FYPO:0007101	during meiosis I
PMID:22292001	PBO:0093557	5
PMID:22292001	PBO:0104343	5c
PMID:22328580	FYPO:0002350	fig 4 D
PMID:22328580	FYPO:0002350	Figure 4, A and B,
PMID:22328580	FYPO:0002350	Figure 4, A and B,
PMID:22328580	FYPO:0002350	Figure 4, A and B,
PMID:22328580	FYPO:0002350	Figure 4, A and B,
PMID:22328580	PBO:0021023	fig 1
PMID:22328580	FYPO:0002350	Fig. 3B Figure 4, A and B,
PMID:22328580	FYPO:0002350	Fig. 3B Figure 4, A and B,
PMID:22328580	PBO:0105472	Fig 3A
PMID:22328580	PBO:0105473	Fig 3A
PMID:22328580	FYPO:0002350	Figure 4, A and B,
PMID:22328580	FYPO:0002350	fig 4 D
PMID:22328580	PBO:0021023	Figure Figures 5D, 6C
PMID:22328580	PBO:0021023	Figure Figures 5D, 6C
PMID:22328580	FYPO:0002350	fig 4 D
PMID:22328580	PBO:0021023	Figure Figures 5D, 6C
PMID:22328580	PBO:0021023	Figure 2D
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	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:0097468	*****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:22344254	PBO:0108023	***********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	GO:0000329	fig6
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: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	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 and Fig. 1C, respectively Gtr2, and in particular Gtr1, inhibit sexual differentiation in rich medium.
PMID:22344254	FYPO:0003031	Fig. 1B and Fig. 1C, respectively Gtr2, and in particular Gtr1, inhibit sexual differentiation in rich medium.
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	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: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: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	FYPO:0000280	fig 4a
PMID:22344254	FYPO:0000280	fig 4a
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	PBO:0097468	********nitrogen replete/with aa
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: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	PBO:0108022	These results suggest that Vam6 functions upstream of Gtr1, possibly by acting as a GEF.
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	FYPO:0002716	FM4-64 stained only small vesicles in the cytoplasm of vam6D cells, confirming a defect in vacuolar fusion in these cells.
PMID:22344694	PBO:0106009	not shown direct binding but want to capture the fact that it binds the oxidised form
PMID:22344694	PBO:0106009	not shown direct binding but want to capture the fact that it binds the oxidised form
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: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	FYPO:0004045	figure 2c
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: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:0005634	Consistent with a role in chromatin modification, all three proteins localized to the nucleus (Figure 4A).
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: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	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	PBO:0105071	Northern blots revealed no defect in the accumulation of mature messengers (Figure 5B)
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	5E
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:0105066	Figure 1C
PMID:22349564	GO:0005739	Figure S4A, B, C
PMID:22349564	FYPO:0001437	Figure 1A
PMID:22349564	FYPO:0001437	Figure 1A
PMID:22349564	FYPO:0003730	Figure 1A
PMID:22349564	FYPO:0003730	Figure 1A
PMID:22349564	FYPO:0003730	Figure 1A
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	PBO:0105065	Figure 1C
PMID:22349564	PBO:0105064	Figure 1C
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	FYPO:0007623	Figure 1B
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:0007623	Figure 1B
PMID:22349564	FYPO:0000441	Figure 1A
PMID:22354040	PBO:0098697	Fig 7 B
PMID:22354040	GO:0042162	Fig 7
PMID:22354040	PBO:0098696	Fig 7 A
PMID:22354040	FYPO:0002239	figure 8 A
PMID:22354040	PBO:0098698	fig 7 c
PMID:22354040	PBO:0095770	Fig 7B
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: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	( positive). 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:0010514	( positive). AMPK is required for proper advance entry into mitosis in nitrogen-starved cells and arrest in G1 before Start.
PMID:22375066	GO:0010514	positive
PMID:22375066	GO:0140648	( positive). AMPK is required for proper advance entry into mitosis in nitrogen-starved cells and arrest in G1 before Start.
PMID:22375066	GO:0010514	positive
PMID:22375066	GO:0010514	( positive). 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:22419817	GO:0031028	"vw deleted ""+ve regulation of"""
PMID:22426534	PBO:0101049	genes in extensions are assayed as represntative of highly transcribed genes
PMID:22426534	PBO:0101053	genes in extensions are assayed as represntative of highly transcribed genes
PMID:22426534	PBO:0101050	genes in extensions are assayed as represntative of highly transcribed genes
PMID:22426534	PBO:0101052	genes in extensions are assayed as represntative of highly transcribed genes
PMID:22426534	PBO:0101051	genes in extensions are assayed as represntative of highly transcribed genes
PMID:22427686	PBO:0114249	Fig. 3B
PMID:22427686	PBO:0114252	Fig. 4F
PMID:22427686	PBO:0114251	Fig. 4D
PMID:22427686	PBO:0099471	Fig. 4C
PMID:22427686	PBO:0099471	Fig. 4C
PMID:22427686	PBO:0112294	Fig. 4C
PMID:22427686	PBO:0099470	Fig. 4C
PMID:22427686	PBO:0099471	Fig. 4C
PMID:22427686	PBO:0112293	Fig. 4C
PMID:22427686	PBO:0112293	Fig. 4C
PMID:22427686	PBO:0114250	Fig. 4C
PMID:22427686	PBO:0112293	Fig. 4C
PMID:22427686	PBO:0032815	Fig. 4C
PMID:22427686	PBO:0032815	Fig. 4C
PMID:22427686	PBO:0112296	Fig. 4C
PMID:22427686	PBO:0114248	Fig. 3B
PMID:22427686	PBO:0114249	Fig. 3B
PMID:22427686	PBO:0114248	Fig. 3B
PMID:22427686	PBO:0114254	Fig. 6H
PMID:22427686	PBO:0114254	Fig. 6H
PMID:22427686	PBO:0114256	Fig. 6H
PMID:22427686	PBO:0114247	Fig. 3B
PMID:22427686	PBO:0114256	Fig. 6H
PMID:22427686	PBO:0112452	Fig. S2A
PMID:22427686	FYPO:0001368	Fig. 2H
PMID:22427686	FYPO:0001368	Fig. 2H
PMID:22427686	FYPO:0001368	Fig. 2H
PMID:22427686	PBO:0112639	Fig. 2C
PMID:22427686	PBO:0114231	Fig. 2C
PMID:22427686	PBO:0114246	Fig. 2C
PMID:22427686	PBO:0112639	Fig. 2C
PMID:22427686	PBO:0114245	Fig. 1B and Table 1
PMID:22427686	PBO:0114244	Fig. 1B and Table 1
PMID:22427686	PBO:0114243	Fig. 1B and Table 1
PMID:22427686	PBO:0094136	Fig. 1B and Table 1
PMID:22427686	PBO:0114242	Fig. 1B and Table 1
PMID:22427686	PBO:0033280	Fig. 1B and Table 1
PMID:22427686	PBO:0032796	Fig. 1B and Table 1
PMID:22427686	PBO:0032817	Fig. 1B and Table 1
PMID:22427686	PBO:0114241	Fig. 1B and Table 1
PMID:22427686	PBO:0114240	Fig. 1B and Table 1
PMID:22427686	PBO:0114239	Fig. 1B and Table 1
PMID:22427686	PBO:0114238	Fig. 1B and Table 1
PMID:22427686	PBO:0114237	Table 1
PMID:22427686	PBO:0114236	Fig. 1B and Table 1
PMID:22427686	PBO:0114235	Fig. 1B and Table 1
PMID:22427686	PBO:0114234	Fig. 1B and Table 1
PMID:22427686	PBO:0114233	Fig. 1B and Table 1
PMID:22427686	PBO:0114226	Fig. 1B and Table 1
PMID:22427686	PBO:0099470	Fig. 1B and Table 1
PMID:22427686	PBO:0114232	Fig. 1B and Table 1
PMID:22427686	PBO:0107134	Table 1
PMID:22427686	PBO:0032816	Fig. 6E
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:0103459	Table 1
PMID:22427686	PBO:0032816	Fig. 6E
PMID:22427686	FYPO:0002253	Fig. 6E
PMID:22427686	FYPO:0002253	Fig. 6E
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:0114222	Table 1
PMID:22427686	PBO:0114222	Table 1
PMID:22427686	PBO:0114222	Table 1
PMID:22427686	PBO:0114224	Table 1
PMID:22427686	PBO:0114224	Table 1
PMID:22427686	PBO:0114231	Fig. 2C
PMID:22427686	FYPO:0002253	Fig. 1B and Table 1
PMID:22427686	FYPO:0002253	Fig. 1B and Table 1
PMID:22427686	FYPO:0002253	Fig. 1B and Table 1
PMID:22427686	PBO:0107134	Table 1
PMID:22427686	PBO:0103459	Table 1
PMID:22427686	PBO:0114222	Table 1
PMID:22427686	PBO:0114230	Fig. 1B and Table 1
PMID:22427686	PBO:0114229	Fig. 1B and Table 1
PMID:22427686	PBO:0107134	Table 1
PMID:22427686	PBO:0103459	Table 1
PMID:22427686	PBO:0114222	Table 1
PMID:22427686	PBO:0114228	Fig. 1B and Table 1
PMID:22427686	PBO:0114227	Fig. 1B and Table 1
PMID:22427686	PBO:0104485	Fig. 6F and G
PMID:22427686	PBO:0104485	Fig. 6F and G
PMID:22427686	FYPO:0003338	Fig. 6A
PMID:22427686	FYPO:0003338	Fig. 6B
PMID:22427686	PBO:0114255	Fig. 5D
PMID:22427686	PBO:0114254	Fig. 5B and C
PMID:22427686	PBO:0114253	Fig. 4F
PMID:22427686	PBO:0103459	Table 1
PMID:22427686	PBO:0114222	Table 1
PMID:22427686	PBO:0114226	Fig. 1B and Table 1
PMID:22427686	PBO:0114225	Fig. 1B and Table 1
PMID:22427686	PBO:0114224	Table 1
PMID:22427686	PBO:0114223	Fig. 1B and Table 1
PMID:22427686	PBO:0032843	Fig. 1B and Table 1
PMID:22427686	PBO:0114222	Table 1
PMID:22427686	PBO:0114221	Fig. 1B and Table 1
PMID:22427686	FYPO:0002253	Fig. 1B and Table 1
PMID:22427686	PBO:0114220	Fig. 2C
PMID:22427686	PBO:0032798	Fig. 1B and Table 1
PMID:22427686	FYPO:0002253	Fig. 1B and Table 1
PMID:22431512	PBO:0102102	localization independent of Ago1
PMID:22431512	PBO:0102103	localization independent of Ago1
PMID:22431512	PBO:0102103	SO:0001843 =ATF1/CRE; localization independent of Ago1
PMID:22431512	PBO:0102102	localization independent of Ago1
PMID:22438582	PBO:0101883	6A
PMID:22438582	GO:1990395	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	S6
PMID:22438582	FYPO:0000583	S6
PMID:22438582	PBO:0101879	Figure 1
PMID:22438582	PBO:0101879	Figure 1
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	FIG 4B
PMID:22438582	PBO:0022389	Figure 1
PMID:22438582	PBO:0101884	6A
PMID:22438582	PBO:0101878	5A
PMID:22438582	PBO:0101877	5A
PMID:22438582	PBO:0101882	5A
PMID:22438582	PBO:0101882	5
PMID:22438582	PBO:0101882	5
PMID:22438582	PBO:0101885	6A
PMID:22438582	PBO:0101886	6A
PMID:22438582	PBO:0101874	5F
PMID:2245912	FYPO:0001492	Table 5 no genetic interaction with stf1-1.
PMID:2245912	FYPO:0001492	Table 5 This mutant is a revertant of cdc2-M35
PMID:2245912	FYPO:0000674	Table 4 suppressor of cdc25-22
PMID:2245912	FYPO:0000674	Table 3 suppressor of cdc25-22
PMID:2245912	PBO:0097657	the restrictive temperature for a cdc25-22 diploid is 32°C
PMID:2245912	PBO:0020446	cells heterozygous for stf1-1 are more elongated that stf1-1 homozygous cells
PMID:2245912	FYPO:0000674	Table 4 suppressor of cdc25-22
PMID:2245912	PBO:0020446	cells homozygous for stf1-1 are not as elongated as stf1-1 heterozygous cells at restrictive temperature
PMID:2245912	PBO:0097658	cells homozygous for stf1-1 form small colonies at restrictive temperature ~20-200 cells
PMID:2245912	PBO:0097659	stf1-1/stf1-2 cells are not as elongated as stf1-1 heterozygous cells at restrictive temperature
PMID:2245912	PBO:0097658	stf1-1/stf1-3 cells form small colonies at restrictive temperature ~20-200 cells
PMID:2245912	FYPO:0001492	Table 5 This mutant is a revertant of cdc2-M35
PMID:2245912	FYPO:0006822	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	FYPO:0001490	dis2+ over expression reverses the stf1-1 suppression cdc25-22
PMID:2245912	PBO:0097658	cells heterozygous for stf1-1 form small colonies at restrictive temperature ~20-200 cells
PMID:2245912	FYPO:0000674	Table 4 stf1-1 is a suppressor of cdc25-M51
PMID:2245912	FYPO:0000674	Table 4 suppressor of cdc25-disruption occasional cdc- cells observed
PMID:2245912	FYPO:0001490	Table 5 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:0006822	Table 5 no genetic interaction with stf1-1
PMID:2245912	PBO:0020446	same phenotype as cells homozygous for stf1-1
PMID:2245912	PBO:0097658	same phenotype as cells homozygous for stf1-1
PMID:2245912	FYPO:0001492	Table 4 suppressor of cdc25-22
PMID:2245912	FYPO:0001492	Table 4 suppressor of cdc25-22
PMID:2245912	FYPO:0006822	Table 5 no genetic interaction with stf1-1
PMID:2245912	FYPO:0006822	Table 5 cdc2-3w and stf1-1 have additive effect on cdc25-22 cell size at restrictive temperature
PMID:2245912	FYPO:0001492	Table 5 cdc2-1w rescues cdc25-22 but cells are long
PMID:2245912	FYPO:0006822	Table 5 cdc2-1w and stf1-1 have additive effect on cdc25-22 cell size at restrictive temperature
PMID:2245912	FYPO:0006822	Table 6 wee1-50 and stf1-1 have an additive effect to suppress cdc25-22 phenotype at the restrictive temperature
PMID:2245912	FYPO:0006822	Table 6
PMID:2245912	PBO:0093770	Table 7 Cells are slightly shorter at high temperature when stf1-1 present
PMID:2245912	PBO:0093770	Table 7 Cells are slightly shorter at high temperature when stf1-1 present
PMID:2245912	FYPO:0001492	Table 4 stf1-1 is a suppressor of cdc25-M51
PMID:2245912	FYPO:0001492	Table 4 suppressor of cdc25-disruption occasional cdc- cells observed
PMID:2245912	FYPO:0001490	Table 8 no genetic interaction with stf1-1
PMID:2245912	FYPO:0001492	Table 8 no genetic interaction with stf1-1
PMID:2245912	FYPO:0001491	Table 5
PMID:2245912	PBO:0020446	stf1-1/stf1-3 cells are not as elongated as stf1-1 heterozygous cells at restrictive temperature
PMID:2245912	PBO:0097660	Table 4
PMID:2245912	FYPO:0001490	Table 5 no genetic interaction with stf1-1
PMID:2245912	FYPO:0001490	Table 5 no genetic interaction with stf1-1
PMID:2245912	FYPO:0001490	Table 5 no genetic interaction with stf1-1
PMID:22474355	PBO:0111710	The localizations of Hrr1-Flag and Rdp1-Flag at centro- meric repeats were also found to be severely compromised in both ers1Δ and swi6Δ mutant cells (Fig. 5 A and B).
PMID:22474355	PBO:0111708	sug- gesting that a physical association with Swi6, but not the other CD proteins, was required for the heterochromatic localization of Ers1.
PMID:22474355	PBO:0111707	To test the hypothesis that the nu- clear 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 nu- clear 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:0111706	To test the hypothesis that the nu- clear 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: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: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 locali- zation 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: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:0111711	The localizations of Hrr1-Flag and Rdp1-Flag at centro- meric 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 centro- meric 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 con- sistent 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 de- creased in swi6Δ and clr4Δ cells (Fig. S5A).
PMID:22474355	PBO:0111713	ChIP analyses showed that Ers1 localization at the mating type locus (cenH) and telomeres was severely de- creased 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 de- creased 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 de- creased 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: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:0111710	The localizations of Hrr1-Flag and Rdp1-Flag at centro- meric repeats were also found to be severely compromised in both ers1Δ and swi6Δ mutant cells (Fig. 5 A and B).
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:22484924	PBO:0104297	fig 2c
PMID:22484924	FYPO:0000423	fig4 (I moved this down from abnormal endocytisis, is that OK?)
PMID:22484924	PBO:0104296	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	(protein)
PMID:22484924	PBO:0099384	fig 5c
PMID:22484924	FYPO:0004482	fig 4
PMID:22496451	PBO:0023351	"allele tyep ""unknown"" because neither nt nor aa position 324 is A"
PMID:22508988	PBO:0099624	fig 3B
PMID:22508988	PBO:0099623	fig 3B
PMID:22508988	PBO:0099622	fig 2d Spt5-T1P (CTD repeat 1 residue)
PMID:22508988	PBO:0099622	fig 2d Spt5-T1P (CTD repeat 1 residue)
PMID:22508988	FYPO:0007074	fig 2c
PMID:22508988	PBO:0099621	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 un- known (34)
PMID:22508988	FYPO:0001357	fig 2c
PMID:22508988	FYPO:0002141	fig 2c
PMID:22508988	PBO:0093560	fig 2c
PMID:22508988	PBO:0093554	fig 2c
PMID:22508988	PBO:0093560	fig 2c
PMID:22508988	PBO:0093554	fig 2c
PMID:22508988	FYPO:0006821	fig 2b
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),(is this an physiological substrate?)
PMID:22508988	PBO:0099619	fig 1a
PMID:22508988	GO:0005515	fig1 carboxy terminal region
PMID:22508988	PBO:0099618	fig 1a in vitro /in vivo
PMID:22508988	PBO:0099618	fig 1a
PMID:22508988	GO:0005515	fig1 carboxy terminal region
PMID:22508988	PBO:0111962	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:22508988	PBO:0103373	S. pombe Cdk9 also generated Ser2-P and Ser5-P signals but was relatively inefficient at phosphorylating Ser7.
PMID:22508988	PBO:0099620	fig 1e in vitro
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:0111962	(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:0103372	(Fig. 6C) Immunoblot analysis indicated that Mcs6 phosphorylates Ser2, Ser5, and Ser7
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:0099626	fig 4 A/B
PMID:22508988	PBO:0099625	fig 4 A/B
PMID:22558440	PBO:0109949	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	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	PBO:0098286	fig 2a
PMID:22573890	PBO:0098290	fig S2
PMID:22573890	FYPO:0000651	fig 6
PMID:22573890	FYPO:0000650	fig 6
PMID:22573890	FYPO:0006559	fig 5 6 min late
PMID:22573890	FYPO:0006187	fig 5
PMID:22573890	FYPO:0004895	fig 5
PMID:22573890	FYPO:0004653	fig 5
PMID:22573890	PBO:0097713	fig 3 A
PMID:22573890	PBO:0018345	fig 3 A
PMID:22573890	PBO:0098289	fig 3 A
PMID:22573890	PBO:0098288	figure 2 B/C
PMID:22573890	PBO:0111999	fig 2a (WT 10% @36degrees)
PMID:22582262	GO:0007129	"rec12 phenotype indicates that Sme2 role in synapsis is independent of meiotic recombination; 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; NEEDS TO BE REGULATION OF SYNAPSISa change to the GO ""pairing"" definition requested""https://sourceforge.net/p/geneontology/ontology-requests/10607/"
PMID:22645648	FYPO:0002061	Figure1a
PMID:22645648	FYPO:0002672	Figure1a
PMID:22645648	FYPO:0002060	Figure1a
PMID:22645648	GO:0038202	TOR kinase activity was measured using immunoprecipitated proteins (Fig.2)
PMID:22645648	FYPO:0002061	Figure 1a/6a
PMID:22645648	FYPO:0002061	Figure 6
PMID:22645648	FYPO:0002672	Figure6
PMID:22645648	FYPO:0002060	Figure 6
PMID:22645648	FYPO:0001019	Figure 4d
PMID:22645648	FYPO:0001122	Figure4e
PMID:22645648	FYPO:0000012	Figure4ab
PMID:22645648	FYPO:0005430	Figure4d
PMID:22645654	FYPO:0004031	Fig1f (evidence:immunoblot using anti-thymine dimer anitbodies)
PMID:22645654	FYPO:0002060	fig 2b,c
PMID:22645654	FYPO:0001926	fig 2b,c
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:0001930	Fig1d
PMID:22645654	FYPO:0000089	Fig1d
PMID:22645654	FYPO:0000085	Fig1d
PMID:22645654	FYPO:0001387	Fig1h
PMID:22645654	FYPO:0003844	Fig1g
PMID:22645654	FYPO:0004385	Fig7
PMID:22645654	FYPO:0000088	Fig1d
PMID:22645654	FYPO:0000268	Fig2e
PMID:22645654	FYPO:0002573	Fig3a-g (evidence: immunpflouresence)
PMID:22645654	FYPO:0002573	Fig4
PMID:22645654	FYPO:0004385	Fig5
PMID:22645654	FYPO:0005438	Fig5
PMID:22645654	FYPO:0000268	Fig.1d, e, f
PMID:22645654	FYPO:0000088	Fig2e
PMID:22658721	PBO:0095271	small
PMID:22658721	PBO:0095272	bulky
PMID:22658721	FYPO:0004371	NMeed to check, its decreased duration of replication arrest?
PMID:22660415	PBO:0112092	Fig. 4B
PMID:22660415	PBO:0112210	Fig. 4C
PMID:22660415	PBO:0112234	Fig. 5A
PMID:22660415	PBO:0112234	Fig. 5A
PMID:22660415	PBO:0112233	Fig. 5A
PMID:22660415	PBO:0112233	Fig. 5A
PMID:22660415	PBO:0112233	Fig. 5A
PMID:22660415	PBO:0112234	Fig. 5A.
PMID:22660415	PBO:0112234	Fig. 5A.
PMID:22660415	PBO:0112094	Fig. 5B
PMID:22660415	PBO:0112094	Fig. 5B
PMID:22660415	PBO:0112094	Fig. 5B
PMID:22660415	PBO:0112105	Fig. 5B
PMID:22660415	PBO:0112106	Fig. 5B
PMID:22660415	PBO:0112211	Fig. 5B
PMID:22660415	PBO:0112233	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:0103768	Fig. 5C
PMID:22660415	PBO:0096163	Fig. 5C
PMID:22660415	PBO:0096163	Fig. 5C
PMID:22660415	PBO:0103767	Fig. 5C
PMID:22660415	PBO:0103767	Fig. 5C
PMID:22660415	PBO:0093559	Fig. 5E
PMID:22660415	PBO:0093559	Fig. 5E
PMID:22660415	PBO:0093562	Fig. 5E
PMID:22660415	PBO:0093562	Fig. 5E
PMID:22660415	PBO:0093562	Fig. 5E
PMID:22660415	PBO:0093563	Fig. 5E
PMID:22660415	FYPO:0001357	Fig. 5F
PMID:22660415	PBO:0093563	Fig. 5F
PMID:22660415	PBO:0093563	Fig. 5F
PMID:22660415	PBO:0103768	Fig. 5F
PMID:22660415	PBO:0103768	Fig. 5F
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:0112085	Fig. 2G
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:0112086	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:22660415	PBO:0112094	Fig. 5B
PMID:22660415	PBO:0093559	Fig. 5E
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:0097991	Fig. 1A
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:0112095	Fig. 1D
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: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:0112097	Fig. 2I
PMID:22660415	PBO:0112097	Fig. 2I
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:0112108	Fig. 5E
PMID:22660415	PBO:0112109	although the kinetochore localization of Spc7-12A protein was intact (Fig. 2f),
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:0112099	Fig. 2I
PMID:22660415	PBO:0112101	Fig. 2I
PMID:22660415	PBO:0112101	Fig. 2I
PMID:22660415	PBO:0112098	Fig. 2I
PMID:22660415	PBO:0112098	Fig. 2I
PMID:22660415	PBO:0112100	Fig. 2I
PMID:22660415	PBO:0112102	Fig. 2I
PMID:22660415	PBO:0112102	Fig. 2I
PMID:22660415	PBO:0112091	Fig. 4B
PMID:22661707	PBO:0102208	more specific term required, during GO:0034599)
PMID:22665807	PBO:0096304	Table S1 and Figure S1
PMID:22665807	PBO:0096303	Table S1 and Figure S1
PMID:22665807	PBO:0096303	Table S1 and Figure S1
PMID:22665807	PBO:0096303	Table S1 and Figure S1
PMID:22665807	PBO:0096303	Table S1 and Figure S1
PMID:22665807	PBO:0096303	Table S1 and Figure S1
PMID:22665807	PBO:0096304	Table S1 and Figure S1
PMID:22665807	PBO:0096308	2A
PMID:22665807	PBO:0096308	2A
PMID:22665807	PBO:0096307	2A
PMID:22665807	PBO:0096308	1d
PMID:22665807	FYPO:0006822	figure 2A
PMID:22665807	PBO:0096307	2A
PMID:22665807	PBO:0096306	1d
PMID:22665807	PBO:0096308	2A
PMID:22665807	PBO:0096308	2A
PMID:22665807	PBO:0096308	2A
PMID:22665807	PBO:0096310	3a
PMID:22665807	FYPO:0004474	3b
PMID:22665807	PBO:0096311	4b
PMID:22665807	PBO:0096311	4b
PMID:22665807	PBO:0096311	4b
PMID:22665807	PBO:0096311	4b
PMID:22665807	PBO:0096311	4b
PMID:22665807	PBO:0096312	4b
PMID:22665807	PBO:0096312	4b
PMID:22665807	PBO:0096312	4b
PMID:22665807	PBO:0096312	4b
PMID:22665807	PBO:0096314	4b
PMID:22665807	PBO:0096305	1c
PMID:22665807	PBO:0096304	Table S1 and Figure S1
PMID:22665807	PBO:0096304	Table S1 and Figure S1
PMID:22665807	PBO:0096303	Table S1 and Figure S1
PMID:22665807	PBO:0096303	Table S1 and Figure S1
PMID:22682245	FYPO:0002061	implies that dna2 E560A alone is inviable
PMID:22682245	FYPO:0002060	implies that dna2 K961T alone is viable
PMID:22682245	GO:1990601	cleaves unpaired nascent DNA in replication forks (vw replaced GO:0045145)
PMID:22683269	GO:0003723	assayed using bulk RNA
PMID:22684255	PBO:0100303	Figure 2f lanes 1, 2
PMID:22684255	PBO:0100302	Figure 2f lanes 1, 2
PMID:22684255	PBO:0100301	Figure 1g
PMID:22684255	PBO:0100301	Figure 1g
PMID:22684255	PBO:0097831	Figure 1b
PMID:22684255	PBO:0097831	Figure 1b
PMID:22684255	PBO:0092296	fig 1a
PMID:22684255	PBO:0100305	upstream of pom1
PMID:22684255	FYPO:0000400	fig 4d
PMID:22684255	FYPO:0000400	fig 4d
PMID:22684255	FYPO:0000400	fig 4d
PMID:22684255	FYPO:0000400	fig 4d
PMID:22684255	FYPO:0000400	fig 4d
PMID:22684255	FYPO:0000400	fig 4d
PMID:22684255	FYPO:0000400	fig 4d
PMID:22684255	FYPO:0003306	fig 4d
PMID:22684255	FYPO:0000400	fig 4d
PMID:22684255	FYPO:0000405	fig 4d
PMID:22684255	FYPO:0000405	fig 4d
PMID:22684255	GO:0010971	(Figure 4b) confirming that each kinase promotes mitotic commitment.
PMID:22684255	GO:0010971	"""mitotic commitment'"
PMID:22684255	FYPO:0003481	Figure 3a. t (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. t (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	FYPO:0003306	Figure 3a
PMID:22684255	PBO:0100302	Figure 2f lanes 1, 2
PMID:22696680	FYPO:0002760	Figure 1
PMID:22696680	GO:0061863	Figure 3, Supplemental Table S2, and Supplemental Figure S4
PMID:22696680	FYPO:0002112	Figure 2A
PMID:22696680	FYPO:0004731	Figure 1
PMID:22696680	FYPO:0004731	Figure 1
PMID:22696680	FYPO:0002818	Figure 2B
PMID:22696680	PBO:0037217	(growing) fig 1A
PMID:22696680	PBO:0018346	fig 1A
PMID:22696680	PBO:0019801	fig 1A
PMID:22696680	FYPO:0005797	Figure 2C
PMID:22696680	FYPO:0005681	Figure 2D Figure 2F
PMID:22696680	FYPO:0001234	Figure 2A
PMID:22696680	FYPO:0005682	Figure 2D Figure 2F
PMID:22696680	PBO:0103479	Supplemental Figure S1, C–E
PMID:22696680	PBO:0098921	Supplemental Figure S1, C–E
PMID:22696680	PBO:0103480	Supplemental Figure S1, C–E
PMID:22696680	FYPO:0002760	Figure 1
PMID:22705791	FYPO:0003164	not sure if it is endo, exo or both? so went with more general term
PMID:22705791	GO:0004518	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:22711988	PBO:0103997	implies that MIND complex is required for Sos7 to localize to the kinetochore
PMID:22711988	GO:0000776	kinetochore localization requires MIND complex
PMID:22718908	PBO:0103928	inferred from localization of proteins distal to origin
PMID:22718908	FYPO:0006728	BrdU incorporation
PMID:22718908	FYPO:0006727	BrdU incorporation
PMID:22718908	PBO:0103920	inferred from localization of proteins distal to origin
PMID:22718908	FYPO:0006728	BrdU incorporation
PMID:22718908	PBO:0103909	inferred from localization of proteins distal to origin
PMID:22718908	FYPO:0006728	BrdU incorporation
PMID:22718908	PBO:0103909	inferred from localization of proteins distal to origin
PMID:22718908	FYPO:0006726	inferred from normal localization of CMG proteins at origin
PMID:22723423	GO:0000400	Fml1 binds to the four-way junction at a displacement (D) loop.
PMID:22723423	GO:0009378	Fml1 catalyses the dissociation of displacement (D) loops
PMID:22727667	PBO:0111539	binds H3K9me
PMID:22727667	PBO:0111540	binds H3K9me
PMID:22727667	PBO:0111538	binds H3K9me
PMID:22737087	PBO:0093561	data not shown decreased aneuploid cell viability during vegetative growth
PMID:22737087	FYPO:0007391	Fig 4 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 This strain is disomic for Chromosome 3
PMID:22737087	PBO:0104055	Table 2 This strain is disomic for Chromosome 3
PMID:22737087	PBO:0104054	Fig1, Table1 affects C1 type colonies
PMID:22737087	PBO:0104054	Fig1, Table1 affects C1 type colonies
PMID:22737087	PBO:0104054	Fig1, Table1 affects C1 and C2 type colonies
PMID:22737087	PBO:0093560	Fig6. reduced growth may not be specific to aneuploidy as it also interacts with gtb1-93
PMID:22737087	PBO:0093560	Fig6
PMID:22737087	PBO:0093560	Fig6
PMID:22737087	PBO:0093560	Fig6
PMID:22737087	PBO:0093560	Fig6.
PMID:22737087	PBO:0093560	Fig6.
PMID:22737087	PBO:0104055	Table 2 This strain is disomic for Chromosome 3
PMID:22737087	PBO:0104055	Table 2 This strain is disomic for Chromosome 3
PMID:22737087	FYPO:0001326	All the genes affect by at least 1.5 fold (17) are reported in Table S2
PMID:22737087	FYPO:0001326	All the genes affect by at least 1.5 fold (61) are reported in Table S2
PMID:22737087	FYPO:0001326	All the genes affect by at least 1.5 fold (141) are reported in Table S2
PMID:22737087	PBO:0093560	Fig2.
PMID:22737087	PBO:0104054	Fig1, Table1 affects C1 more than C2 type colonies
PMID:22737087	PBO:0104054	Fig2.
PMID:22737087	PBO:0093560	Fig S1 decreased aneuploid cell viability during vegetative growth
PMID:22737087	PBO:0093561	Fig S1, decreased aneuploid cell viability during vegetative growth
PMID:22737087	PBO:0093559	Fig S1, decreased aneuploid cell viability during vegetative growth
PMID:22737087	PBO:0093560	Fig2. decreased aneuploid cell viability during vegetative growth
PMID:22737087	PBO:0104055	Fig 3B This strain is disomic for Chromosome 3
PMID:22737087	PBO:0093558	Fig 3A This strain is disomic for Chromosome 3
PMID:22737087	PBO:0104055	Fig 3B This strain is disomic for Chromosome 3
PMID:22737087	PBO:0093558	Fig 3A This strain is disomic for Chromosome 3
PMID:22737087	PBO:0104054	Table1 Fig1 affects C1 and C2 type colonies
PMID:22737087	PBO:0093559	Fig2. reduced growth may not be specific to aneuploidy as it also interact with gtb1 though looks quite good to me
PMID:22737087	PBO:0093560	Fig2. reduced growth may not be specific to aneuploidy as it also interacts with gtb1
PMID:22737087	FYPO:0007391	data not shown
PMID:22737087	PBO:0093560	Fig2. decreased aneuploid cell viability during vegetative growth
PMID:22737087	FYPO:0007391	data not shown
PMID:22737087	FYPO:0007391	data not shown
PMID:22737087	FYPO:0007391	data not shown
PMID:22737087	PBO:0093560	Fig2. decreased aneuploid cell viability during vegetative growth
PMID:22737087	FYPO:0001357	Fig2 normal population growth in presence of aneuploid cells
PMID:22737087	FYPO:0001357	Fig2 normal population growth in presence of aneuploid cells
PMID:22737087	PBO:0093560	Fig2.
PMID:22737087	PBO:0104054	Fig1, Table1 affects C1 and C2 type colonies
PMID:22768388	FYPO:0000674	S1 E
PMID:22768388	FYPO:0000674	S1 E
PMID:22768388	FYPO:0000674	S1 E
PMID:22768388	FYPO:0002672	S1 E
PMID:22768388	FYPO:0000082	fig 1 A
PMID:22768388	FYPO:0001357	figure 1c
PMID:22768388	FYPO:0001234	Figur 1 c
PMID:22768388	FYPO:0001234	Figur 1 c
PMID:22768388	FYPO:0001357	figure 1c
PMID:22768388	FYPO:0001357	figure 1c
PMID:22768388	FYPO:0000674	S1 E
PMID:22768388	FYPO:0002672	S1 E
PMID:22768388	FYPO:0002672	S1 E
PMID:22768388	FYPO:0002672	S1 E
PMID:22768388	FYPO:0003503	data not shown
PMID:22768388	PBO:0104835	fig 4C
PMID:22768388	FYPO:0005177	Figures S1C
PMID:22768388	FYPO:0001492	Figures 1B
PMID:22768388	FYPO:0001492	Figures 1B
PMID:22768388	FYPO:0000118	Figures 1B
PMID:22768388	FYPO:0003218	Figures S1C and S1D
PMID:22768388	FYPO:0002360	data not shown
PMID:22768388	FYPO:0000082	fig 1 A
PMID:22768388	FYPO:0002834	fig S4
PMID:22768388	FYPO:0000118	Figures 1B
PMID:22768388	FYPO:0001234	Figur 1 c
PMID:22768388	FYPO:0000082	fig 1 A
PMID:22768388	FYPO:0000082	fig 1 A
PMID:22768388	FYPO:0000082	fig 1 A
PMID:22792081	PBO:0104543	This interaction depends on the phosphorylation of Crb2 on the T73 and S80 residues.
PMID:22792081	PBO:0111547	This interaction depends on the phosphorylation of Crb2 on the T73 and S80 residues.
PMID:22792081	GO:0005515	This interaction depends on the phosphorylation of Crb2 on the T73 and S80 residues.
PMID:22809626	PBO:0022949	"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	"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	"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	"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:0096316	Fig. 4A and S8
PMID:22825872	PBO:0096315	Fig. 4A and S7
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	ditto
PMID:22825872	FYPO:0003762	The shorter truncation (Mph1-D1-150) maintained kinetochore localization and SAC signaling,
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	PBO:0096318	Mph1 localizes to unattached kinetochores in bub3D cells (Fig. 2A).
PMID:22825872	PBO:0096320	Fig. 4B Fig. 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.3A. 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	This is 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	This is S4B and C
PMID:22825872	PBO:0096325	This is S4B and C
PMID:22825872	PBO:0096326	This is S4B and C
PMID:22825872	PBO:0096327	(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	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	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	GO:0090267	Together this suggests that Ark1 is directly and continuously required to maintain Mph1 localization to kinetochores.
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:0096331	(Fig. S9F)
PMID:22825872	FYPO:0003307	(Fig. 3C) (inhibiting Ark1 does not rescue the Mph1-kinetochore targeting, arguing that Ark1 is upstream)
PMID:22825872	FYPO:0003307	(Fig. 3C)increased mitotic index (Fig. S4A)
PMID:22848669	PBO:0101760	(Figure 3B)
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	PBO:0095501	Notably, overex- pression 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, overex- pression 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, overex- pression 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:0093641	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: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	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:0093641	(Figure 2)
PMID:22848669	PBO:0101760	(Figure 2)
PMID:22848669	PBO:0096587	(Figure 2)
PMID:22848669	PBO:0112961	(Figure 2)
PMID:22848669	PBO:0112962	(Figure 2)
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 3B)
PMID:22848669	PBO:0112962	(Figure 3B)
PMID:22848669	PBO:0112962	(Figure 3B)
PMID:22848669	PBO:0112962	(Figure 3B)
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: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	****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: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	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: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: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:22891259	GO:0032153	fig1 /figs1?
PMID:22891259	GO:0032153	fig1 /figs1?
PMID:22891259	GO:0031671	Explosive cell separation due to a weak primary septum. Absence of a secondary septum.
PMID:22891259	GO:0005886	Localized at cell tips, actomyosin contractile ring and septum
PMID:22891673	FYPO:0000650	septation index constantly high
PMID:22891673	FYPO:0000639	decreased septum closure
PMID:22891673	FYPO:0000230	At the end of ring constriction Filamentous projections from the unclosed ring toward the cytoplasm
PMID:22891673	FYPO:0000424	Assayed by FM4-64 uptake
PMID:22891673	FYPO:0002438	Weak actin cables
PMID:22891673	FYPO:0002526	assayed at 32C, which is semi-permissive for sec3-913
PMID:22891673	FYPO:0000639	decreased/delayed septum closure
PMID:22891673	PBO:0018345	normal localization in several mutants indicates that Sec3 localization is independent of exocytosis and vesicle-mediated transport along microtubules
PMID:22891673	FYPO:0000650	septation index increased gradually over time
PMID:22895252	GO:0030466	Fig. S2
PMID:22905165	PBO:0022652	Cdc15-GFP However, we observed that a number of the Cdc15-GFP and the GFP-Cdc4 rings were asymmetric or broken.
PMID:22905165	PBO:0018345	GFP-Cfh3 figure 1 A
PMID:22905165	PBO:0105436	S1
PMID:22905165	PBO:0105435	S1
PMID:22905165	PBO:0105434	S1
PMID:22905165	PBO:0105433	S1
PMID:22905165	PBO:0105441	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, A protein distributed in cortex
PMID:22905165	PBO:0105439	GFP-Bgs1
PMID:22905165	PBO:0096859	GFP-Bgs1
PMID:22905165	PBO:0035602	Cdc15-GFP supplemental figure S3
PMID:22905165	PBO:0035602	Cdc15-GFP
PMID:22905165	PBO:0098289	GFP-Cfh3 figure 1 A
PMID:22905165	PBO:0022652	(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	1B
PMID:22905165	PBO:0105442	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:22912768	PBO:0095155	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:22912768	PBO:0095154	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:22912768	PBO:0096135	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:22912768	PBO:0096136	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:22912768	PBO:0096134	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:22912768	PBO:0096133	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:22912768	PBO:0096132	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:22918943	PBO:0095813	Figure 5, I, J, and L
PMID:22918943	FYPO:0004594	Figure 7
PMID:22918943	PBO:0095812	Figure 5, I, J, and L
PMID:22918943	PBO:0095811	Figure 5, I, J, and L
PMID:22918943	GO:0071341	Figure 1A, 2A
PMID:22918943	GO:0110115	Figure 1A, 2A
PMID:22918943	PBO:0095814	Figure 7
PMID:22918943	FYPO:0001364	Figure 3A
PMID:22918943	FYPO:0003339	Figure 3A
PMID:22918952	PBO:0099901	unspecfied RxxS site(s)
PMID:22918952	PBO:0099900	unspecfied RxxS site(s)
PMID:22918954	PBO:0099647	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 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:0099646	Figure 4
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: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: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	at Ser/Thr-Pro site
PMID:22959349	PBO:0103680	at Ser/Thr-Pro site
PMID:22959349	PBO:0103680	at Ser/Thr-Pro site
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: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: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:22976295	PBO:0025355	blotted for rps601 & rps602 simultaneously
PMID:22976295	PBO:0025357	blotted for rps601 & rps602 simultaneously
PMID:22976295	PBO:0025356	blotted for rps601 & rps602 simultaneously
PMID:22976295	GO:0038202	"I guess everything in the signaling cascade that isn't the ""final effector"" is part of the signaling cascade?"
PMID:22976295	PBO:0097477	in vitro assay using rps602 so I am inferring rps601
PMID:22976295	PBO:0097459	not shown
PMID:22976295	PBO:0110437	in vitro assay using rps602 so I am inferring rps601
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:0097454	both rps proteins in extension because blot is for both of them
PMID:22976295	PBO:0097453	both rps proteins in extension because blot is for both of them
PMID:22976295	PBO:0097452	both rps proteins in extension because blot is for both of them
PMID:22976295	PBO:0097451	both rps proteins in extension because blot is for both of them
PMID:22976295	PBO:0097450	both rps proteins in extension because blot is for both of them
PMID:22976295	PBO:0025357	blotted for rps601 & rps602 simultaneously
PMID:22976295	PBO:0025356	blotted for rps601 & rps602 simultaneously
PMID:22976295	PBO:0097469	both rps proteins in extension because blot is for both of them
PMID:22976295	PBO:0025355	blotted for rps601 & rps602 simultaneously
PMID:22976295	PBO:0097468	both rps proteins in extension because blot is for both of them
PMID:22976295	PBO:0097469	both rps proteins in extension because blot is for both of them
PMID:22976295	PBO:0097468	both rps proteins in extension because blot is for both of them
PMID:22976295	PBO:0097469	both rps proteins in extension because blot is for both of them
PMID:22976295	PBO:0097468	both rps proteins in extension because blot is for both of them
PMID:22976295	PBO:0097468	both rps proteins in extension because blot is for both of them
PMID:22976295	PBO:0097454	both rps proteins in extension because blot is for both of them
PMID:22976295	PBO:0097454	both rps proteins in extension because blot is for both of them
PMID:22976295	PBO:0097469	both rps proteins in extension because blot is for both of them
PMID:22976295	GO:0038202	"I guess everything in the signaling cascade that isn't the ""final effector"" is part of the signaling cascade?"
PMID:22987637	PBO:0104501	"for evidence, ""BrdU incorporation assay evidence used in manual assertion"" (ECO:0001155) would be applicable."
PMID:22987637	FYPO:0005758	"for evidence, ""BrdU incorporation assay evidence used in manual assertion"" (ECO:0001155) would be applicable."
PMID:22988247	PBO:0097487	This gene has been named as otg2 in the article.
PMID:22988247	PBO:0097487	This gene has been named as otg3 in the article.
PMID:22988247	FYPO:0003354	This gene has been named as otg1 in the article.
PMID:22990236	PBO:0034977	SO:0001899 = dh repeat
PMID:23028377	GO:0140713	move down to histone chaperone (H3-?)
PMID:23032292	FYPO:0000854	spacing is wrong as well as occupancy
PMID:23051734	GO:0070648	localization
PMID:23051734	GO:0070649	required for wildtype rates of actin cable retrograde flow in myo52∆ cells
PMID:23066505	PBO:0099504	ire1 breaks down mRNAs during ER stress, however bip1 is unusual in that ire1 cleavage stabilizes it
PMID:23066505	GO:0036498	RIDD? - there is no RIDD term in GO, Val wants to wait with this
PMID:23071723	FYPO:0000972	throughout cell cycle, with peak at M/G1
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	FYPO:0004890	As previously shown, telomere tethering was significantly compromised in rap1Δ and bqt4Δ cells (Figure S2C; Chikashige et al., 2009).
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: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:0007270	(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	GO:0099115	1A
PMID:23084836	GO:0005721	1A
PMID:23084836	PBO:0101844	1A
PMID:23084836	FYPO:0007270	(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: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 and S2B)
PMID:23084836	PBO:0101845	(Figures S2A and 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	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: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	Figures 6A and 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:0007270	Figures 6A and 6B) see above
PMID:23084836	FYPO:0005545	Figures 6A and 6B) see above
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: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	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: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: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 and 6B) see above
PMID:23084836	FYPO:0005545	Figures 6A and 6B), see above
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: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:23093942	FYPO:0003588	assayed in strain with RTS1 replication fork barrier inserted near ori3006/7
PMID:23093942	FYPO:0001740	assayed by PCR in strain with RTS1 replication fork barrier inserted near ori3006/7
PMID:23093942	FYPO:0001740	assayed in strain with RTS1 replication fork barrier inserted near ori3006/7
PMID:23093942	FYPO:0003587	assayed by PCR in strain with RTS1 replication fork barrier inserted near ori3006/7
PMID:23093942	FYPO:0003587	assayed by PCR in strain with RTS1 replication fork barrier inserted near ori3006/7
PMID:23093943	PBO:0099938	fig 3c
PMID:23093943	PBO:0102282	Figure 1F–1G
PMID:23093943	PBO:0102281	fiigure S1B–S1C
PMID:23093943	PBO:0097167	fiigure S1B–S1C
PMID:23093943	PBO:0102280	fiigure S1B–S1C
PMID:23093943	PBO:0102279	fig 1b fig2
PMID:23093943	FYPO:0003535	fig 1b
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	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	PBO:0102296	Figure S5B
PMID:23093943	PBO:0102296	Figure S5B
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:0102288	fig 4c/ figure 6a
PMID:23093943	GO:1902404	Consistent with early cytokinesis events proceeding appropri- ately 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: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	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: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:0099938	fig S3F
PMID:23093943	PBO:0102290	fig 4c
PMID:23093943	PBO:0102289	fig 4c
PMID:23093943	PBO:0102288	fig 4c
PMID:23093943	FYPO:0000026	Figure 4A–4C and Figure S3A–S3B
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 and Figure S3A–S3B
PMID:23093943	PBO:0102285	Figure 3G
PMID:23093943	PBO:0102284	fFigure 3D–3F
PMID:23093943	PBO:0102283	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:23093943	FYPO:0001355	S1F
PMID:23093943	FYPO:0001355	S1F
PMID:23093943	FYPO:0002061	S1F
PMID:23112169	GO:0032132	binds O6-alkylguanine, 2-aminopurine and 2,6-diaminopurine
PMID:23115244	FYPO:0002010	evidence=mas spec, can I wang this into another evidence code or should we add it (or something similar?)
PMID:23122962	GO:2001178	******mediator L complex asembly******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 inter- action between Cdk8 and either the Med27 or Med4 phos- phorylation mutants was specifically lost (Figure 4B, right panel). In contrast, the phosphorylation mutants of Med27 and Med4 still interacted with the middle subunit Med7 (Fig- ure 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:2001178	*****mediator L complex assembly******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 inter- action between Cdk8 and either the Med27 or Med4 phos- phorylation mutants was specifically lost (Figure 4B, right panel). In contrast, the phosphorylation mutants of Med27 and Med4 still interacted with the middle subunit Med7 (Fig- ure 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: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 tran- scription, together with its nuclear localization and copurifica- tion 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	PBO:0111120	in contrast to Mcs6 (the Cdk7 ortholog), which readily phosphor- ylated the GST-CTD fusion in vitro (Figure 1E) (Drogat and Her- mand, 2012)
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 phos- phorylation level of these two residues in vivo, the absence of cdk11 had no effect (Figure 1F).
PMID:23122962	PBO:0107732	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 phos- phorylation level of these two residues in vivo, the absence of cdk11 had no effect (Figure 1F).
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. I (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 (Fig- ure 2D).
PMID:23122962	PBO:0111120	in contrast to Mcs6 (the Cdk7 ortholog), which readily phosphor- ylated the GST-CTD fusion in vitro (Figure 1E) (Drogat and Her- mand, 2012)
PMID:23122962	PBO:0111452	Therefore, we found no evidence of Cdk11 being a genuine CTD kinase in fission yeast.
PMID:23122962	PBO:0096825	in contrast to Mcs6 (the Cdk7 ortholog), which readily phosphor- ylated the GST-CTD fusion in vitro (Figure 1E) (Drogat and Her- mand, 2012)
PMID:23122962	GO:0000307	A tandem affinity purification (TAP) identified physical partners of Cdk11, including an unchar- acterized cyclin (SPAC1296.05c) that was confirmed to bind Cdk11 in independent coimmunoprecipitation experiments (Fig- ure 1C and 1D).
PMID:23122962	GO:0000307	A tandem affinity purification (TAP) identified physical partners of Cdk11, including an unchar- acterized cyclin (SPAC1296.05c) that was confirmed to bind Cdk11 in independent coimmunoprecipitation experiments (Fig- ure 1C and 1D).
PMID:23122962	GO:0005634	Fluorescence microscopy revealed that Cdk11 was expressed and mainly concentrated in the nucleus (Figure 1A).
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 demon- strated that Cdk11 phosphorylates Med4 on three residues (Fig- ure 3B: S115, S204, and S218
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 demon- strated that Cdk11 phosphorylates Med4 on three residues (Fig- ure 3B: S115, S204, and S218
PMID:23128140	GO:0051010	NMR + substrate
PMID:23133674	GO:0005515	bqt1 is fused to the activation domain
PMID:23133674	GO:0005515	fig1 only bqt1 is fused to the activation domain (that's why I am not adding this function to bqt2)
PMID:23133674	GO:0005515	fig1 Y2H
PMID:23133674	GO:0005515	fig1 Y2H
PMID:23133674	GO:0005515	Y2H fig 1
PMID:23166349	GO:0005515	Coimmunoprecipitation, yeast-two-hybrid
PMID:23166349	PBO:0109468	Further supported by PMID:25057016
PMID:23188080	FYPO:0004287	affects intermolecular, but not intramolecular, end joining
PMID:23188080	FYPO:0004287	affects intermolecular, but not intramolecular, end joining
PMID:23188080	FYPO:0004287	affects intermolecular, but not intramolecular, end joining
PMID:23188080	FYPO:0004287	affects intermolecular, but not intramolecular, end joining
PMID:23188080	FYPO:0004287	affects intermolecular, but not intramolecular, end joining
PMID:23188080	FYPO:0004287	affects intermolecular, but not intramolecular, end joining
PMID:23188080	FYPO:0004287	affects intermolecular, but not intramolecular, end joining
PMID:23200991	PBO:0038209	Observed with probe for active Cdc42 (CRIB)
PMID:23200991	GO:1902917	inferred from localization plus GTPase activity
PMID:23200991	PBO:0037256	Observed with probe for active Cdc42 (CRIB)
PMID:2320127	PBO:0107935	Fig4a. Cells blocked in G2
PMID:2320127	MOD:00046	Fig1c Serine is the major phosphoamino acid
PMID:2320127	MOD:00047	Fig1c threonine is the minor phosphoamino acid
PMID:2320127	PBO:0107935	Fig4a. Cells blocked in mitosis
PMID:23209828	PBO:0099849	MBC resistance phenotype and pap1 ubiquitylation phenotype
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	PBO:0099842	Pap1 is ubiquitylated by Rhp6 and Ubr1
PMID:23209828	PBO:0099843	Pap1 is ubiquitylated by Rhp6 and Ubr1
PMID:23209828	GO:0061631	MBC resistance phenotype and pap1 ubiquitylation phenotype
PMID:23211746	PBO:0095371	same as exo1delta alone
PMID:23211746	FYPO:0002553	gel electrophoresis + southern blot
PMID:23211746	FYPO:0000268	same as chk1delta alone
PMID:23211746	FYPO:0000089	same as exo1delta alone
PMID:23211746	FYPO:0000089	same as chk1delta alone
PMID:23211746	PBO:0095371	same as rad2delta alone
PMID:23211746	FYPO:0000089	same as rad2delta alone
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: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: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: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: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: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: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:23231582	PBO:0100021	also inferred from chromatin localization and reporter gene expression
PMID:23231582	PBO:0100048	at pho1+ and SPBC1271.09
PMID:23231582	GO:0000122	represses Pho7-mediated transcription activationin phosphate-replete conditions; does not regulate Pho7 DNA binding
PMID:23236291	FYPO:0003335	Figure 8B (PMID:23236291)
PMID:23236291	FYPO:0001252	Figure 8E (PMID:23236291)
PMID:23236291	FYPO:0005277	Figure 8E (PMID:23236291)
PMID:23236291	GO:1900735	Figure 6A and 6C (PMID:23236291)
PMID:23236291	FYPO:0005504	Figure 6A (PMID:23236291)
PMID:23236291	FYPO:0004153	Figure 7A (PMID:23236291)
PMID:23236291	FYPO:0004153	Figure 7A (PMID:23236291)
PMID:23236291	FYPO:0003335	Figure 8D (PMID: 23236291)
PMID:23236291	FYPO:0003776	Figure 8D (PMID: 23236291)
PMID:23236291	PBO:0107311	Requested new term from Sequence Ontology: CArG-box
PMID:23236291	FYPO:0000155	Figure 8D (PMID: 23236291)
PMID:23236291	GO:1900735	Figure 1A and 1B (PMID: 23236291)
PMID:23236291	FYPO:0003335	Figure 1A (PMID: 23236291)
PMID:23236291	FYPO:0003318	Figure 1B (PMID: 23236291)
PMID:23236291	FYPO:0000155	Figure 3 (PMID: 23236291)
PMID:23236291	FYPO:0000155	Figure 3 (PMID: 23236291)
PMID:23236291	FYPO:0000155	Figure 3 (PMID: 23236291)
PMID:23236291	FYPO:0000155	Figure 3 (PMID: 23236291)
PMID:23236291	FYPO:0000155	Figure 3 (PMID: 23236291)
PMID:23236291	FYPO:0000155	Figure 3 (PMID: 23236291)
PMID:23236291	FYPO:0000155	Figure 3 (PMID: 23236291)
PMID:23236291	FYPO:0000155	Figure 3 (PMID: 23236291)
PMID:23236291	FYPO:0000155	Figure 8D (PMID: 23236291)
PMID:23236291	FYPO:0000155	Figure 8D (PMID: 23236291)
PMID:23236291	FYPO:0000155	Figure 8D (PMID: 23236291)
PMID:23236291	FYPO:0000155	Figure 8D (PMID: 23236291)
PMID:23236291	FYPO:0003318	Figure 8B (PMID: 23236291)
PMID:23236291	FYPO:0003335	Figure 8A (PMID: 23236291)
PMID:23236291	FYPO:0003318	Figure 8B (PMID:23236291)
PMID:23245849	GO:0003905	A. 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	PBO:0093616	fig 1D
PMID:23245849	FYPO:0000957	fig 1D
PMID:23245849	PBO:0093616	fig 1D
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	GO:0006307	multiple experiments
PMID:23245849	GO:0005634	Figure 1C
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: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: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	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: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 galactosyla- tion of cell-surface proteins
PMID:23254763	FYPO:0006807	Fig 3. galactose-specific HRP-PNA staining was used to detect quantitative differences in the galactosyla- tion of cell-surface proteins
PMID:23254763	FYPO:0002061	FIgure 2. +25 μg/ml Hyg.B
PMID:23254763	FYPO:0002061	FIgure 2. +25 μg/ml Hyg.B
PMID:23254763	PBO:0093561	FIgure 2. +25 μg/ml Hyg.B
PMID:23254763	PBO:0093561	FIgure 2. +25 μg/ml Hyg.B
PMID:23254763	PBO:0093561	FIgure 2. +25 μg/ml Hyg.B
PMID:23254763	PBO:0093561	FIgure 2. +25 μg/ml Hyg.B
PMID:23254763	PBO:0093561	FIgure 2. +25 μg/ml Hyg.B
PMID:23254763	PBO:0093561	FIgure 2. +25 μg/ml Hyg.B
PMID:23254763	PBO:0093561	FIgure 2.
PMID:23254763	PBO:0093561	FIgure 2.
PMID:23254763	PBO:0095407	complemented by S. cerevisiae GAL2
PMID:23254763	PBO:0095408	FIgure 2. +25 μg/ml Hyg.B
PMID:23254763	PBO:0095408	FIgure 2
PMID:23254763	PBO:0095408	FIgure 2
PMID:23254763	PBO:0095408	FIgure 2
PMID:23254763	PBO:0093561	FIgure 2. +25 μg/ml Hyg.B
PMID:23260662	GO:0071515	Fig. 3A
PMID:23260662	GO:0071515	inferred directness from effects of different alleles and of mutations elsewhere (swi1delta, clr4delta, or mat1-SS2)
PMID:23260662	GO:0011000	inferred directness from effects of different alleles and of mutations elsewhere (swi1delta, clr4delta, or mat1-SS2)
PMID:23260662	GO:1902681	inferred indirectness from author description and different effect of swi1delta
PMID:23260662	PBO:0104354	same as lsd1-E918 single mutant
PMID:23260662	PBO:0104354	same as lsd1-E918 single mutant
PMID:23260662	PBO:0104354	same as lsd1-E918 single mutant
PMID:23260662	PBO:0104354	same as lsd1-E918 single mutant
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:00047	T123 and S334 were 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	S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	Phosphorylation site S265 was identified by mass spectrometry.
PMID:23297348	MOD:00046	S332, S700, and S732 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S332, S700, and S732 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S332, S700, and S732 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00047	S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00047	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	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	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	S267 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S321 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00047	T297 and S364 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S303 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S57 and S206 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S57 and S206 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S183 and S372 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S183 and S372 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S674 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S502 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S196 and S252 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S196 and S252 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S345 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00047	S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00047	S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00047	S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S411 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00047	T554 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S372 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S436 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S220 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00047	T106 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S148 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S65 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S216 and S298 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S216 and S298 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S301 and S499 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S301 and S499 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S558 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S74 and S95 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S74 and S95 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S370 was identified as phosphorylation sites by mass spectrometry.
PMID:23297348	PBO:0101808	serine residues, presumably some or all of those mutated
PMID:23297348	PBO:0101808	serine residues, presumably some or all of those mutated
PMID:23297348	PBO:0101808	serine residues, presumably some or all of those mutated
PMID:23297348	MOD:00047	S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00047	T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00047	T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	T297 and S364 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	T123 and S334 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	T123 and S334 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.
PMID:23297348	MOD:00046	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	non-flocculating cells
PMID:23314747	PBO:0097201	AACCCT box, subtelomere
PMID:23314747	PBO:0095974	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	AACCCT box, subtelomere
PMID:23333317	PBO:0100177	Fig5B plo1 increased specific activity
PMID:23333317	PBO:0100178	Fig5B
PMID:23333317	PBO:0100179	Fig5B
PMID:23333317	PBO:0100193	Fig1H cdc25-22 cut12R531STOP can grow at higher temperature in presence of cut12. G71V mutation. (vw changed form increased to normal, compared to WT)
PMID:23333317	PBO:0093557	Fig1. 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:0093557	Fig1. 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	Fig1. Rescue of cdc25-22 but not restored to full growth (partial rescue)
PMID:23333317	PBO:0093556	Fig1. Rescue of cdc25-22 but not restored to full growth (partial rescue)
PMID:23333317	FYPO:0000674	Fig2E
PMID:23333317	PBO:0100194	T75T78
PMID:23333317	PBO:0111088	T75
PMID:23333317	PBO:0100195	Fig 1b, F and G. (T75T78 UNPHOSPHORYLATED FORM)
PMID:23333317	PBO:0100196	Fig 1b, F and G. (T75T78 PHOSPHORYLATED FORM)
PMID:23333317	PBO:0100157	Fig1 C 2 hybrid
PMID:23333317	PBO:0100158	Fig1c 2-hybrid
PMID:23333317	PBO:0100160	Fig1 C 2 hybrid
PMID:23333317	PBO:0100160	Fig1C 2 hybrid
PMID:23333317	PBO:0100160	Fig1C 2 hybrid
PMID:23333317	PBO:0100198	Fig2H
PMID:23333317	PBO:0100199	Fig2H (VWI added this and man=de the original 'abnormal cell size' small (variable size at division, mixed sized see #3800)
PMID:23333317	PBO:0100193	Fig1H cdc25-22 cut12R531STOP can grow at higher temperature in presence of cut12. G71V mutation. (vw changed form increased to normal, compared to WT)
PMID:23333317	FYPO:0000674	Fig 2E phospho mimetic cdc12 mutant rescues cdc25 mutant
PMID:23333317	FYPO:0000674	Fig 2E phospho mimetic cdc12 mutant rescues cdc25 mutant
PMID:23333317	PBO:0100158	Fig1c 2-hybrid
PMID:23333317	PBO:0100158	Fig1D
PMID:23333317	PBO:0100159	Fig1D
PMID:23333317	PBO:0100158	Fig1D
PMID:23333317	PBO:0100157	Fig1 D & E
PMID:23333317	PBO:0100181	Fig5B plo1 increased specific activity
PMID:23333317	PBO:0100179	Fig5B
PMID:23333317	PBO:0100177	Fig5B plo1 increased specific activity
PMID:23333317	PBO:0100178	Fig5B
PMID:23333317	PBO:0100179	Fig5B
PMID:23333317	PBO:0100192	Fig5B
PMID:23333317	PBO:0100188	Fig5B DELAYED
PMID:23333317	PBO:0100189	Fig5B
PMID:23333317	PBO:0100190	Fig5B plo1 increased specific activity
PMID:23333317	PBO:0100184	Fig5B
PMID:23333317	PBO:0100180	Fig5B
PMID:23333317	PBO:0100190	Fig5B plo1 increased specific activity
PMID:23333317	PBO:0100184	Fig5B
PMID:23333317	PBO:0100191	Fig5B
PMID:23333317	PBO:0100187	Fig5B plo1 decreased specific activity
PMID:23333317	PBO:0100188	Fig5B DELAYED
PMID:23333317	PBO:0100192	Fig5B
PMID:23333317	PBO:0100182	Fig5B
PMID:23333317	PBO:0100159	Fig1C increased interaction in 2 hybrid
PMID:23333317	PBO:0100160	Fig1 E
PMID:23333317	PBO:0100160	Fig1E
PMID:23333317	PBO:0100160	Fig1E
PMID:23333317	PBO:0100161	Fig1E
PMID:23333317	PBO:0100162	Fig1 E
PMID:23333317	FYPO:0000674	"Fig1A, 2A. vw""Fig 1. Rescue of cdc25-22 but not restored to full growth (partial rescue)"""
PMID:23333317	FYPO:0000674	Fig2G
PMID:23333317	PBO:0097660	Fig2H
PMID:23333317	FYPO:0000674	Fig 2E phospho mimetic cdc12 mutant rescues cdc25 mutant
PMID:23333317	FYPO:0004481	Fig 2E unphosphorylatable cut12 mutants are unable to rescue cdc25 mutant (vw changed from decreased to abolished?)
PMID:23333317	PBO:0093557	Fig2E 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:0093557	Fig2E single mutant T75D does not rescue cdc25-22 as well as double T75DT78D or singleT78D mutants. (vw: changed to decreased)
PMID:23333317	PBO:0100163	Fig2I single mutant cut12. T75A binds dis2
PMID:23333317	PBO:0100163	Fig2I single mutant cut12.T78A binds Dis2
PMID:23333317	PBO:0100164	Fig2I single mutant cut12. T75D reduces dis2 binding
PMID:23333317	PBO:0100164	Fig2I single mutant cut12. T78D reduces dis2 binding
PMID:23333317	PBO:0100165	Fig2I Fig3C double mutant cut12.T75A T78A binds dis2
PMID:23333317	PBO:0100166	Fig4A HU arrest Fig4E synchronous culture
PMID:23333317	PBO:0100166	Fig4A fin1 activation is dependent on sid1
PMID:23333317	PBO:0100167	Fig4A an antibody that recognized Cut12 when phosphorylated on T75 [Figure S2C] alone established that MPF phosphorylates T75 in vitro [Figure 4D]).
PMID:23333317	PBO:0100168	Fig4E in absence of fin1 activity dis2 remains bound to cut 12
PMID:23333317	PBO:0100171	Fig4F dis2 remains bound to cut12
PMID:23333317	PBO:0100172	Fig4F T75 T78 no longer phosphorylated and dis2 remains bound to cut12
PMID:23333317	PBO:0100173	Fig5A No increase in recruitment of plo1 to SPB when fin1 is active if T75 T78 mutated to A
PMID:23333317	PBO:0100174	vw: could this one be abolished? Fig5A No change in recruitment of plo1 to SPB when fin1 is inactivated T75 T78 mutated to D
PMID:23333317	PBO:0100175	Fig5A plo1 localisation to SPB is dependent on fin1 activity
PMID:23333317	PBO:0100176	Fig5A plo1 localisation to SPB is dependent on fin1 activity
PMID:23333317	PBO:0100177	Fig5B plo1 increased specific activity
PMID:23333317	PBO:0100178	Fig5B. premature recruitment of protein to the mitotic SPB
PMID:23333317	PBO:0100179	Fig5B
PMID:23333317	PBO:0100177	Fig5B plo1 increased specific activity
PMID:23333317	PBO:0100178	Fig5B
PMID:23333317	PBO:0100179	Fig5B
PMID:23333317	PBO:0100177	Fig5B plo1 increased specific activity
PMID:23333317	PBO:0100178	Fig5B
PMID:23333317	PBO:0100180	Fig5B
PMID:23333317	PBO:0100181	Fig5B plo1 increased specific activity
PMID:23333317	PBO:0100182	Fig5B
PMID:23333317	PBO:0100179	Fig5B
PMID:23333317	PBO:0100181	Fig5B plo1 increased specific activity
PMID:23333317	PBO:0100182	Fig5B
PMID:23333317	PBO:0100183	Fig5B
PMID:23333317	PBO:0100181	Fig5B plo1 increased specific activity
PMID:23333317	PBO:0100182	Fig5B
PMID:23333317	PBO:0100183	Fig5B
PMID:23333317	PBO:0100187	Fig5B plo1 decreased specific activity
PMID:23333317	PBO:0100188	Fig5B DELAYED
PMID:23333317	PBO:0100189	Fig5B
PMID:23333317	PBO:0100187	Fig5B plo1 decreased specific activity
PMID:23348717	PBO:0099730	assayed using cell growth with AspRec8c–FGFP–Mei2SATA construct (degradation frees Mei2SATA to arrest cell cycle)
PMID:23348717	FYPO:0003299	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:23348717	PBO:0099730	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 AspRec8c–FGFP construct
PMID:23349636	PBO:0099925	more specifically, response to mitotic DNA replication checkpoint signaling
PMID:23349808	PBO:0097713	during cytokinesis
PMID:23349808	PBO:0024047	during G2 phase of mitotic cell cycle
PMID:23349808	PBO:0024047	during G2 phase of mitotic cell cycle
PMID:23349808	PBO:0024047	during G2 phase of mitotic cell cycle
PMID:23349808	PBO:0024047	during G2 phase of mitotic cell cycle
PMID:23394829	GO:0044732	also present in early anaphase; disappears by late anaphase
PMID:23394829	PBO:0023023	also present in early anaphase; disappears by late anaphase
PMID:23395004	FYPO:0003615	ChIP-CHIP, rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag)
PMID:23395004	PBO:0101944	rec27-205::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	PBO:0101943	rec25-204::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	PBO:0101942	mug20::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	PBO:0101942	mug20::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	PBO:0101942	mug20::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	PBO:0101942	mug20::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	FYPO:0004585	ChIP-CHIP, rec27-205::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	FYPO:0004585	rec25-204::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	FYPO:0004585	mug20::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	FYPO:0004585	mug20::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	FYPO:0004585	mug20::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	FYPO:0004585	mug20::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	PBO:0101941	ChIP-CHIP, rec27-205::GFP-kanMX6(C-terminal GFP tag)
PMID:23395004	FYPO:0003615	ChIP-CHIP, rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag)
PMID:23395004	FYPO:0003615	ChIP-CHIP, rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag)
PMID:23395004	FYPO:0003615	ChIP-CHIP, rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag)
PMID:23395004	FYPO:0003181	ChIP-CHIP, rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag)
PMID:23427262	PBO:0111961	vw after attachment
PMID:23427262	PBO:0111960	vw after attachment
PMID:23442800	GO:1902426	required for ubiquitination of Slp1
PMID:23462181	GO:0000935	Fig. 2A and B
PMID:23462181	PBO:0018346	Fig. 2A and B
PMID:23462181	PBO:0018634	Fig. 2A and B
PMID:23462181	GO:0005730	Fig. 2A and B
PMID:23462181	GO:0051286	Fig. 2A and B
PMID:23496905	FYPO:0002060	Figure 1
PMID:23496905	PBO:0099397	Figure 3
PMID:23496905	PBO:0099397	Figure 3
PMID:23496905	PBO:0099396	fig 2
PMID:23496905	PBO:0099399	fig 4 (40% act remaining)
PMID:23496905	PBO:0099399	fig 4 (60%)
PMID:23496905	PBO:0099398	Figure 2
PMID:23496905	FYPO:0002060	Figure 1
PMID:23496905	GO:0000338	fig 2
PMID:23496905	PBO:0099396	fig 2
PMID:23496905	FYPO:0002060	Figure 1
PMID:23496905	PBO:0099397	Figure 3
PMID:23496905	PBO:0099397	Figure 3
PMID:23496905	PBO:0099396	fig 2
PMID:23496905	FYPO:0002060	Figure 1
PMID:23496905	PBO:0099396	fig 2
PMID:23496905	FYPO:0002060	Figure 1
PMID:23503588	FYPO:0002064	in vitro
PMID:23551936	PBO:0021255	cellular response to rapamycin = GO:0072752 cellular response to caffeine =GO:0071313
PMID:23551936	PBO:0021256	cellular response to rapamycin = GO:0072752 cellular response to caffeine =GO:0071313
PMID:23555033	PBO:0092698	occurs_at CSL_response_element, overexpression, in vitro
PMID:23555033	PBO:0096541	major region affecting localization between aa 395–465
PMID:23555033	PBO:0092698	occurs_at CSL_response_element in vivo
PMID:23555033	GO:0045944	overexpression
PMID:23555033	PBO:0096540	to CSL_response_element
PMID:23555033	PBO:0096538	to CSL_response_element
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	GO:0140767	binds the non trimmed part of the N-glycan
PMID:23609449	PBO:0103289	figure 10 (check specificty). 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:23609449	PBO:0103289	figure 10 (check specificty)
PMID:23615450	PBO:0104673	complements deletion Figure 6A
PMID:23615450	PBO:0104674	complements deletion Figure 6A
PMID:23615450	FYPO:0001496	Figure 4F
PMID:23615450	PBO:0104670	Figure 4C
PMID:23615450	PBO:0104671	Figure 4C
PMID:23615450	PBO:0104672	complements deletion Figure 6A
PMID:23615450	FYPO:0000639	complements deletion Figure 6A
PMID:23615450	FYPO:0000161	(Figure 3).
PMID:23615450	FYPO:0002061	(Figure 3).
PMID:23615450	FYPO:0002061	(Figure 3).
PMID:23615450	GO:0005515	Supple- mental Figure S9C)
PMID:23615450	PBO:0104676	in interphase
PMID:23615450	PBO:0096761	complements deletion Figure 6A
PMID:23615450	PBO:0101822	Figure 1E and Supplemental Figure S1C
PMID:23615450	PBO:0101823	Figure 1E and Supplemental Figure S1C
PMID:23615450	PBO:0104666	Figure 1E and Supplemental Figure S1C
PMID:23615450	PBO:0104667	Figure 1C and Supplemental Figure S1C
PMID:23615450	PBO:0104668	Figure 1D
PMID:23615450	FYPO:0002060	complements deletion
PMID:23615450	FYPO:0002060	complements deletion
PMID:23615450	FYPO:0002060	complements deletion
PMID:23615450	FYPO:0001368	complements deletion
PMID:23615450	FYPO:0004097	complements deletion
PMID:23615450	FYPO:0002060	complements deletion
PMID:23615450	GO:0051015	Kd ≈ 20 μM Supplemental Figure S5B
PMID:23615450	FYPO:0001368	complements deletion
PMID:23615450	FYPO:0004653	fig 5
PMID:23615450	PBO:0101816	complements deletion
PMID:23615450	FYPO:0001357	Figure 4F
PMID:23615450	PBO:0104669	Figure 4F inferred penetrance because growth not m,uch affected
PMID:23628763	PBO:0101103	binds chromatin at promoter, and phenotypes suggest this
PMID:23628763	PBO:0101100	fig3c
PMID:23628763	PBO:0101099	fig3c
PMID:23628763	FYPO:0002773	fig2
PMID:23628763	GO:0045944	boosts expression of the APC activator Fzr1/Mfr1
PMID:23658229	PBO:0103135	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:23658229	PBO:0095151	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:23658229	PBO:0103138	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:23658229	PBO:0096136	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:23658229	PBO:0095154	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:23658229	PBO:0095155	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:23658229	PBO:0103137	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:23658229	PBO:0103136	deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05)
PMID:23671279	PBO:0099242	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	FYPO:0001097	same as cpc2delta alone
PMID:23671279	FYPO:0001097	same as either single mutant
PMID:23671279	PBO:0099243	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: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	GO:0140469	vw edited
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:0099241	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: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:0099237	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:0099236	RNA level increases upon amitrole exposure in wild type but not mutant
PMID:23671279	PBO:0099254	worse than cpc2delta alone
PMID:23671279	PBO:0099244	same as gcn2delta alone
PMID:23671279	PBO:0099253	same as cpc2delta alone
PMID:23677513	FYPO:0000102	same as rad9delta alone
PMID:23677513	FYPO:0000102	same as hus1delta alone
PMID:23677513	FYPO:0000095	same as rad9delta alone
PMID:23677513	FYPO:0000095	same as hus1delta alone
PMID:23677513	FYPO:0002345	same as rad9delta alone
PMID:23677513	FYPO:0002345	same as hus1delta alone
PMID:23677513	FYPO:0002344	same as rad9delta alone
PMID:23677513	FYPO:0002344	same as hus1delta alone
PMID:23687372	PBO:0102418	occurs_during(G1 to G0 transition)
PMID:23687372	FYPO:0000708	homothallic h90
PMID:23687372	FYPO:0000708	homothallic h90
PMID:23687372	PBO:0102422	occurs_during(G1 to Go transition)
PMID:23687372	PBO:0102420	occurs_during(G1 to G0 transition)
PMID:23687372	PBO:0102419	occurs_during(G1 to G0 transition)
PMID:23687372	FYPO:0000712	move down to G1, nitrogen induced
PMID:23695302	FYPO:0000223	they don't say whether the OEP populations continue to grow like normal (viable/inviable). Also data not shown.
PMID:23754748	FYPO:0002059	fig s1, can't tell after germination or before
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	FYPO:0007112	Fig 2 b-d involved in kinetochore retrieval during meiotic prophase
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:0100773	The Nuf2 complex interacts with the Alp7-Alp14 complex phosphorylated by the polo kinase Plo1
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	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:23770679	FYPO:0007107	meiosis I
PMID:23770679	FYPO:0007108	figure 2a
PMID:23770679	PBO:0100756	fig 2g
PMID:23770679	FYPO:0007112	Fig 2 b-d nvolved in kinetochore retrieval during meiotic prophase
PMID:23770679	PBO:0100757	fig 2G
PMID:23770679	PBO:0100758	Fig 3b
PMID:23770679	FYPO:0007109	fig 3d
PMID:23770679	FYPO:0007108	fig 3d
PMID:23770679	PBO:0100759	Is this phase correct
PMID:23770679	PBO:0100759	Is this phase correct
PMID:23770679	FYPO:0007110	fig 4c
PMID:23770679	FYPO:0007110	fig 4c
PMID:23770679	PBO:0100760	fig 4d
PMID:23770679	PBO:0100761	fig 4d
PMID:23770679	FYPO:0007108	figure 4c
PMID:23770679	PBO:0100762	figure 4
PMID:23770679	FYPO:0006427	fig 5b
PMID:23770679	PBO:0100763	Fig 5. d,e (unattached)
PMID:23770679	FYPO:0000209	fig 5b
PMID:23770679	PBO:0100764	Fig 6a
PMID:23770679	PBO:0100765	Figure 6 b/d (d used chromosome tethered polo mutants, I did not curate these phenotypes)
PMID:23770679	PBO:0100759	Is this phase correct
PMID:23770679	PBO:0100766	polo consensus fig 6b
PMID:23770679	PBO:0100767	Supp Fig S6
PMID:23770679	PBO:0100768	Supp Fig S6
PMID:23770679	PBO:0100769	Fig 6c or abolished?
PMID:23770679	PBO:0100770	Fig 7
PMID:23770679	FYPO:0000209	fig 7c
PMID:23851719	GO:0140673	results in retaining specifically modified histone H3 at the genes in question
PMID:23874237	PBO:0021601	The SO ID's correspond to tRNA lys/gln/glu
PMID:23874237	PBO:0021600	The SO ID's correspond to tRNA lys/gln/glu
PMID:23874237	PBO:0021602	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	GO:0005886	Mtl2p-GFP showed an even membrane distribution with little intra- cellular signals.
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	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	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 cul- tures.
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 cul- tures.
PMID:23907979	GO:0031520	Wsc1p-GFP was found along the entire plasma membrane, but appeared much more concen- trated in patches at the cell ends. We also noted that Wsc1p-GFP accumulated in intracellular compartments (Fig. 3C and D).
PMID:23907979	PBO:0102604	. Interest- ingly, 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:0102605	. Interest- ingly, 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	. Interest- ingly, 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	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 cul- tures.
PMID:23907979	PBO:0101751	wsc1D cell growth was inhibited above 2 lg/mL of Csp (Fig. 1C)
PMID:23907979	PBO:0101752	mtl2D cells were unable to grow on plates sup- plemented 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:0102600	~8% of the cells in the wsc1D mutant and 15% of the cells in mtl2D were lysed (Fig. 1B)
PMID:23907979	PBO:0093590	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:0094276	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:0093626	Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1).
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 incorpo- rated in the cell wall as compared with wild-type cells (30% in wild-type cells and 25% in mtl2D). The differ- ence 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:0102601	We found that GS activity was slightly reduced in mtl2D null cells (Fig. 1D)
PMID:23907979	FYPO:0000760	The mating rate was not affected in mtl2Dh+ 9 mtl2Dh
 or wsc1Dh+ 9 wsc1Dh
 homozygous crosses,
PMID:23907979	FYPO:0000760	The mating rate was not affected in mtl2Dh+ 9 mtl2Dh
 or wsc1Dh+ 9 wsc1Dh
 homozygous crosses,
PMID:23907979	FYPO:0000647	Repres- sion of mtl2+ promoted cell lysis and the cells shrunk without the release of cytoplasmic material.
PMID:23907979	FYPO:0007910	Repres- sion 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 concen- trated 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 sup- plemented 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 sup- plemented 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 expres- sion of a constitutively active form of Rho1p or overex- pression 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. Interest- ingly, 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:23936074	PBO:0095821	assayed using minichromosomes and internal telomeric repeat arrays
PMID:23936074	PBO:0112081	increased staining of all chromatin
PMID:23956092	FYPO:0001496	was branched, elongated, multiseptate cell
PMID:23962284	PBO:0103049	recombinant hal3 not a strong inhibitor in vitro
PMID:23962284	FYPO:0002059	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:23966468	PBO:0099784	FYPO_EXT:0000001=high penetracne
PMID:23977061	GO:0006887	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 (but assayed acid phosphatase activity in medium, so can't tell which gene(s))
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. 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	PBO:0108019	Fig 1
PMID:23986474	FYPO:0002061	DNS
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: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	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	FYPO:0002061	fig 3c
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	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	FYPO:0006917	fig 4c.
PMID:23986474	FYPO:0000620	dns
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: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: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:24003116	FYPO:0001552	Grown in EMM + 200uM ZnSo4. Measurements made via ICP-MS.
PMID:24003116	FYPO:0001534	Grown in EMM + 200uM ZnSo4. Measurements made via ICP-MS.
PMID:24003116	GO:0005634	Visualized via Florescence using an integrated LOZ1::GFP construct grown in EMM +/- ZnSo4
PMID:24003116	FYPO:0001552	Grown in EMM + 200uM ZnSo4. Measurements made via ICP-MS.
PMID:24003116	PBO:0100861	directly regulates adh4
PMID:24003116	PBO:0100862	Via EMSA binds directly to adh4 promoter.
PMID:24006256	GO:0010971	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) (mah 2015-11-06)
PMID:24006256	FYPO:0006822	wee1-50 epistatic to dnt1delta; shows that cell cycle regulation by Dnt1 depends on Wee1
PMID:24006488	PBO:0098802	fig4
PMID:24006488	PBO:0098804	localizes the MBF complex
PMID:24006488	PBO:0098801	fig4
PMID:24006488	PBO:0098802	fig4
PMID:24006488	PBO:0098794	Serine 720 and Serine 732 are phosphorylated by Chk1 Phosphorylation releases MBF from DNA and represses transcription of MBF-dependent genes.
PMID:24006488	PBO:0098794	Serine 720 and Serine 732 are phosphorylated by Chk1 Phosphorylation releases MBF from DNA and represses transcription of MBF-dependent genes.
PMID:24006488	MOD:00696	Serine 114 and Threonine 115 are phosphorylated by Cds1 upon activation of the DNA replication checkpoint. Yox1 phosphorylation by Cds1 releases Yox1 from MBF and activates MBF-dependent transcription.
PMID:24006488	PBO:0098799	fig4
PMID:24006488	PBO:0098800	fig4
PMID:24006488	PBO:0098801	fig4
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	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	GO:0031508	siRNA independent
PMID:24013500	GO:0031508	siRNA independent
PMID:24013500	GO:0031508	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	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	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: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	PBO:0096189	A strain harboring a ura4+ reporter gene inserted into the innermost repeat (imr) region of centro- mere 1 displays reduced growth on 5-FOA when harboring the seb1-1 allele (Fig. 1C). I
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: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	FYPO:0002837	seb1-1 displays normal levels of pericentromeric siRNA accu- mulation (Fig. 2A)
PMID:24013500	FYPO:0000220	In con- trast, 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	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	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	FYPO:0002335	We found that all three mutations are required to produce a silencing defect on 5- FOA medium (Fig. 1B).
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: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: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: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: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:0112918	Together, these data support our hypothesis that Seb1 acts by recruiting SHREC to pericentromeric heterochromatin.
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:0004170	Strikingly, while the levels of H3K9me2 are reduced by only threefold to fivefold in the single mu- tants, 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	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:0002335	We found that all three mutations are required to produce a silencing defect on 5- FOA medium (Fig. 1B).
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:24013500	GO:0031508	siRNA independent
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:24013504	FYPO:0003107	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: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: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-
NTE 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	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: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	PBO:0113765	In the cwf10-
NTE 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	GO:0000974	Table 1
PMID:24014766	GO:0000974	Table 1
PMID:24014766	PBO:0113764	In the cwf10-
NTE 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	GO:0000974	Table 1
PMID:24014766	GO:0000974	Table 1
PMID:24014766	GO:0000974	Table 1
PMID:24014766	GO:0000974	Table 1
PMID:24014766	PBO:0113763	In the cwf10-
NTE 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-
NTE 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-
NTE cells grown at 25°C accumulate unspliced tran- script (Fig. 2C). retrotransposon silencing by mRNA destabilization
PMID:24014766	FYPO:0001234	The cwf10-
NTE 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-
NTE 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 2–135
 aligns with snu114
N (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: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: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	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-
NTE ver- sus 2.0  0.3 for cwf10 2–23
), while the ratio in the wild-type strain was 9.7  1.5 (Fig. 6H). Th
PMID:24014766	GO:0005686	Table 1
PMID:24021628	GO:0006360	heterologous complemetation of S. c HMO1
PMID:24039245	PBO:0107152	in vitro assay with purified proteins
PMID:24047646	FYPO:0006822	Fig3, Table 1
PMID:24047646	FYPO:0005207	Fig 6, shows pom1delta cells still have G2-M size control
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	PBO:0103987	Fig1 In early G2 nif1 localisation is monopolar and in late G2 it is bipolar
PMID:24047646	PBO:0103989	Fig1
PMID:24047646	PBO:0103988	Fig1
PMID:24047646	GO:0071341	Fig1
PMID:24047646	FYPO:0006822	Fig3, Table 1
PMID:24047646	FYPO:0006822	Fig3, Table 1
PMID:24047646	PBO:0103988	Fig1
PMID:24055157	PBO:0094510	Although mutating S278 to alanine abolished Sid4 ubiquitination (Figure 1D)
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: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	FYPO:0004537	cells bypassed the arrest after 5 hrs (Figure 2C).
PMID:24055157	PBO:0106627	mutating S278 to a glutamate did not affect Sid4 ubiquitination (Figure 1D).
PMID:24055157	PBO:0094517	Although Dma1-GFP still localized to SPBs in sid4(T275A) mutant cells (Figure S1F),
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:0106630	Hhp1-GFP localization at SPBs is Sid4 independent (Figure S3E)
PMID:24055157	PBO:0106629	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	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:2406029	FYPO:0001916	same as cdc2-ww single mutant
PMID:24074952	MOD:00047	residue=T235 | residue=T187, annotation_extension=added_by(CDK COMPLEX, CDC2 AND CDC13) | residue=T215
PMID:24074952	MOD:00047	residue=T235 | residue=T187, annotation_extension=added_by(CDK COMPLEX, CDC2 AND CDC13) | residue=T215
PMID:24074952	MOD:00047	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:0101060	has substrates centromere outer repeat transcripts and polyA mRNA. Activated by mg2+
PMID:24095277	PBO:0108681	has substrates centromere outer repeat transcripts and polyA mRNA. Activated by mg2+
PMID:24095277	GO:0016891	does it produce 5' monoesters?
PMID:24115772	PBO:0018470	during(GO:0051329)
PMID:24115772	GO:1903475	dependent on septation initiation signaling (GO:0031028)
PMID:24118096	GO:1990355	Trx1's involvement in tis process is to recycle mxr1 for met-O conversion to met
PMID:24127216	GO:1903475	Truncation of Cdc12 at N-terminus leads to a requirement of For3 actin assembly for contractile ring assembly.
PMID:24127216	FYPO:0003001	fig3e
PMID:24127216	FYPO:0001368	figS1a
PMID:24127216	PBO:0104781	figs2a
PMID:24127216	FYPO:0003014	fig2a
PMID:24127216	PBO:0099316	Depends on Cdc15 to localize to the contractile ring during Anaphase A. Viewed by fluorescent fusion protein. AL - exists during anaphase A and anaphase B
PMID:24127216	FYPO:0003001	fig3e
PMID:24127216	FYPO:0002998	fig 1h
PMID:24127216	FYPO:0003000	fig 1d-g
PMID:24127216	FYPO:0001365	fig2a
PMID:24127216	GO:0030041	fig 1D-G
PMID:24127216	PBO:0104780	Depends on Cdc15 to localize to the contractile ring during Anaphase A. Viewed by fluorescent fusion protein. AL - exists during anaphase A and anaphase B
PMID:24127216	FYPO:0003000	fig 1d-g
PMID:24127216	PBO:0096493	fig1b
PMID:24127216	PBO:0096493	fig1b
PMID:24127216	FYPO:0002998	fig1a
PMID:24127216	GO:1903475	Truncation of Cdc12 at N-terminus leads to a requirement of For3 actin assembly for contractile ring assembly. AL -also see fig 2fgh
PMID:24146635	PBO:0020826	prolonged heat exposure (more than ~45 min)
PMID:24146635	PBO:0020826	prolonged heat exposure (more than ~45 min)
PMID:24146635	PBO:0020826	prolonged heat exposure (more than ~45 min)
PMID:24146635	FYPO:0001326	Global gene expression profile (RNAseq) of deletion similar to that of heat-stressed wild type.
PMID:24146635	PBO:0020826	prolonged heat exposure (more than ~45 min)
PMID:24146635	FYPO:0000082	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	PBO:0099108	"""Both Gef1-3YFP and Scd1-GFP exhibited bipolar localization in majority of late wild type cells"""
PMID:24146635	PBO:0023812	punctate; shorter duration of heat exposure (up to ~45 min)
PMID:24146635	PBO:0020827	shorter duration of heat exposure (up to ~45 min)
PMID:24146635	PBO:0020827	shorter duration of heat exposure (up to ~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:0020827	shorter duration of heat exposure (up to ~45 min)
PMID:24146635	PBO:0020826	prolonged heat exposure (more than ~45 min)
PMID:24146635	PBO:0020826	prolonged heat exposure (more than ~45 min)
PMID:24147005	FYPO:0006538	6A
PMID:24147005	FYPO:0006539	7c
PMID:24155978	PBO:0093578	5S
PMID:24155978	PBO:0102935	5X
PMID:24155978	PBO:0102936	all independent of Sty1 (effects of H2O2 & NAC unchanged in sty1delta)
PMID:24161933	PBO:0112079	30% of endogenous mad3 level, Fig. S4
PMID:24161933	PBO:0112074	500% of endogenous mad1 level, Fig. S4
PMID:24161933	PBO:0112080	40% of endogenous slp1 level, Fig. S4
PMID:24161933	PBO:0112078	65% of endogenous mad2 level, Fig. S4
PMID:24161933	PBO:0112077	10% of endogenous mad2 level, Fig. S4
PMID:24161933	PBO:0112076	30% of endogenous mad1 level, Fig. S4
PMID:24161933	PBO:0112075	10% of endogenous mad1 level, Fig. S4
PMID:24161933	PBO:0112074	300% of endogenous mad1 level, Fig. S4
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:0099162	(Fig. 2d)
PMID:24161933	FYPO:0004318	abundances of 40% or lower, cells lacked checkpoint activity.
PMID:24161933	PBO:0099161	5a.
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:0018530	fig1
PMID:24167631	FYPO:0001178	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.) -mah
PMID:24186976	GO:0005515	supp fig7
PMID:24186976	GO:0005515	supp fig7
PMID:24224056	GO:0045944	in response to carbon source change from glucose to maltose regulates agl1
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 regulates agl1
PMID:24239120	PBO:0094480	Fig. 3
PMID:24239120	PBO:0094480	Fig. 3
PMID:24239120	PBO:0094479	Fig. 3
PMID:24239120	FYPO:0007961	Fig. 4
PMID:24239120	PBO:0094478	Fig. 3
PMID:24239120	FYPO:0006917	Fig. S1 (This is a rescue of FYPO:0000324)
PMID:24239120	PBO:0094476	Fig. S1 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 (This is a rescue of FYPO:0004395)
PMID:24239120	FYPO:0000324	Fig. S1 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 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 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:0007960	Fig. S1
PMID:24239120	FYPO:0007959	Fig. S1
PMID:24239120	FYPO:0006259	Fig. 1
PMID:24239120	FYPO:0006259	Fig. 1
PMID:24239120	FYPO:0006259	Fig. 1
PMID:24239120	FYPO:0006259	Fig. 1
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	FYPO:0004307	Fig. 1
PMID:24239120	PBO:0094477	Fig. 3
PMID:24239120	FYPO:0006259	Fig. 2 (This is a rescue of FYPO:0004395)
PMID:24239120	FYPO:0006917	Fig. 2 (This is a rescue of FYPO:0000324)
PMID:24239120	PBO:0094474	Fig. S1 (This is a partial rescue of FYPO:0004307)
PMID:24239120	FYPO:0006917	Fig. S1 (This is a rescue of FYPO:0000324)
PMID:24239120	PBO:0094481	Fig. 4
PMID:24240238	FYPO:0002687	Southern blot to detect telomeric sequence
PMID:24240238	FYPO:0002687	Southern blot to detect telomeric sequence
PMID:24240238	FYPO:0002019	Southern blot to detect telomeric sequence
PMID:24240238	FYPO:0002019	Southern blot to detect telomeric sequence
PMID:24240238	FYPO:0004744	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:0004742	silencing normal as long as heterochromatin assembly can take place normally
PMID:24240238	FYPO:0002687	Southern blot to detect telomeric sequence
PMID:24240238	FYPO:0002687	Southern blot to detect telomeric sequence
PMID:24240238	FYPO:0002687	Southern blot to detect telomeric sequence
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	decreased. (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	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:0096788	Our data indicates thatRng3p 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	I think this is real i.e. downregulation of growth to allow differentiation
PMID:24268782	PBO:0105248	vw: fixed extensions to link F-P and to delete GO:0051091 vw: move up to from thioredoxin-disulfide reductase activity
PMID:24268782	PBO:0105247	vw: fixed extensions to link F-P and to delete GO:0051091
PMID:24291789	GO:0007064	(Fig. 2e) Fig. 2f) Fig. 3a,b).
PMID:24291789	GO:0032116	Fig. 1a
PMID:24291789	GO:0032116	Fig. 1a
PMID:24291789	PBO:0114852	Fig. 1c,d (part_of extension is 'positive regulation of mitotic cohesin loading'
PMID:24291789	GO:0030892	Fig. 2a,b and Extended Data Fig. 2a
PMID:24291789	GO:0030892	Fig. 2a,b and Extended Data Fig. 2a
PMID:24291789	GO:0030892	Fig. 2a,b and Extended Data Fig. 2a
PMID:24291789	GO:0003690	Fig. 2a,b and Extended Data Fig. 2a
PMID:24291789	GO:0003690	Fig. 2a,b and Extended Data Fig. 2a
PMID:24291789	GO:0030892	Fig. 2a,b and Extended Data Fig. 2a
PMID:24291789	GO:0003690	Fig. 2a,b and Extended Data Fig. 2a
PMID:24291789	PBO:0114853	fig 4 b part_of extension is 'positive regulation of mitotic cohesin loading'
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	GO:0007064	(Fig. 2e) Fig. 2f) Fig. 3a,b). contributes to, mis4 is sufficient?
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:0114852	Fig. 1c,d part_of extension is 'positive regulation of mitotic cohesin loading'
PMID:24291789	GO:0003690	Fig. 2a,b and Extended Data Fig. 2a
PMID:24297439	GO:0005515	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:24297439	GO:0005515	Two hybrid interaction using Gpa2K270E activated protein with Sck1.
PMID:24297439	PBO:0106128	it's a bit indirect, but they show this via consensus site mutations....I think it is borderline ok
PMID:24313451	GO:0101005	assayed using cell extract, overexpressed protien and synthetic UB conjugate
PMID:24314397	GO:0030378	inhibited by α-(hydroxymethyl)serine (CHEBI:28187)
PMID:24316795	GO:0031569	Cdr2 phosphorylated by Pom1 at the CTD negatively regulates its activity
PMID:24316795	PBO:0103727	Phosphorylates cdr2 at S755 in vitro
PMID:24316795	FYPO:0001124	moderate overexpression
PMID:24316795	FYPO:0003481	high overexpression
PMID:24316795	PBO:0103729	high concentration (1 uM) 3MB-PP1
PMID:24316795	FYPO:0000339	high concentration (1 uM) 3MB-PP1
PMID:24316795	FYPO:0001018	high concentration (1 uM) 3MB-PP1
PMID:24316795	FYPO:0003150	low concentration (<0.25 uM) 3MB-PP1
PMID:24316795	PBO:0107141	low concentration (<0.25 uM) 3MB-PP1
PMID:24316795	FYPO:0006822	low concentration (<0.25 uM) 3MB-PP1
PMID:24316795	FYPO:0006822	high concentration (1 uM) 3MB-PP1
PMID:24316795	FYPO:0006822	low concentration (<0.25 uM) 3MB-PP1
PMID:24316795	GO:0010971	Negatively regulated by Pom1 via phosphorylation of C-ter
PMID:24316795	PBO:0094966	same as cdr2-S755A-758A alone
PMID:24316795	PBO:0094966	same as cdr2-S755A-758A alone
PMID:24316795	PBO:0096622	Pom1-as1 protein may preferentially localize to non-growing end.
PMID:24327658	GO:0005515	Binds specifically to active Sre1 transcription factor and not full-length precursor
PMID:24327658	FYPO:0003251	Ok as a single mutant despite sre1-N mutant?
PMID:24327658	GO:0010895	hhp2 deletion increases steady-state ergosterol
PMID:24327658	GO:0000122	accelerates degradation of active Sre1 transcription factor
PMID:24327658	PBO:0096022	in vitro kinase assay using recombinant Sre1 aa 1-440
PMID:24327658	PBO:0096021	in vitro kinase assay using recombinant Sre1 aa 1-440
PMID:24327658	PBO:0108902	in vitro kinase assay using recombinant Sre1 aa 1-440
PMID:24344203	PBO:0101640	same as isp7+ overexpression alone
PMID:24344203	PBO:0101636	isp7+ overexpression decreases Gad8's kinase activity towards substrate Fkh2
PMID:24344203	PBO:0101640	same as isp7+ overexpression alone
PMID:24475199	FYPO:0002834	Expression level up 2 times
PMID:24475199	FYPO:0002834	Expression level up 2 times
PMID:24475199	FYPO:0002834	Expression level up 2 times
PMID:24475199	FYPO:0002827	Expression level up 25 times
PMID:24475199	FYPO:0002827	Expression level up 23 times
PMID:24475199	FYPO:0002827	Expression level up 38 times
PMID:24475199	FYPO:0002827	Expression level up 43 times
PMID:24475199	FYPO:0002827	Expression level up 31 times
PMID:24475199	FYPO:0002827	Expression level up 22 times
PMID:24475199	FYPO:0002834	Expression level up 3 times
PMID:24475199	FYPO:0002834	Expression level up 2 times
PMID:24475199	FYPO:0002827	Expression level up 8 times.
PMID:24475199	FYPO:0002827	Expression level up 35 times
PMID:24475199	FYPO:0002834	Expression level up 2.5 times
PMID:24477934	PBO:0104987	Fig S1I
PMID:24477934	PBO:0104996	. 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	Fif 3F
PMID:24477934	FYPO:0004318	(Fig (Fig 2D and E). mad1 localized did not rescue,
PMID:24477934	FYPO:0004318	Fig 2B
PMID:24477934	PBO:0104994	Fig 1H
PMID:24477934	PBO:0104993	Fig 1H
PMID:24477934	PBO:0095479	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	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:0104986	Fig S1I
PMID:24477934	PBO:0104985	Fig S1B
PMID:24477934	PBO:0096320	Fig S1B
PMID:24477934	PBO:0095474	Fig 3D
PMID:24477934	PBO:0095474	Fig 3 D
PMID:24477934	PBO:0104984	Fig3 B/C
PMID:24477934	PBO:0104984	Fig3 B/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	Fig1C/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	Fig1F
PMID:24477934	FYPO:0004318	Fig1F
PMID:24477934	FYPO:0004318	fig1F
PMID:24477934	FYPO:0004318	(Fig 1F
PMID:24477934	FYPO:0005781	Fig S4a
PMID:24477934	FYPO:0005781	Fig S4a
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:0096319	Fig S4a
PMID:24477934	FYPO:0003762	Fig S4a
PMID:24477934	FYPO:0003762	Fig S4a
PMID:24477934	FYPO:0003762	Fig S4a
PMID:24477934	FYPO:0003762	Fig S4a
PMID:24477934	FYPO:0003762	Fig S4a
PMID:24477934	FYPO:0003762	Fig S4a
PMID:24478458	PBO:0108730	phosphorylates rgf1 during HU response, part of maintenance of protien lcoation in nucleus
PMID:24493644	PBO:0096066	fig5
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: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	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:0113631	Also, Pmk1 hyperactivation triggered by rho2+ overexpression is fully attenuated in mutants lacking Pck2 (Figure 1A).
PMID:24498240	PBO:0113632	Also, Pmk1 hyperactivation triggered by rho2+ overexpression is fully attenuated in mutants lacking Pck2 (Figure 1A).
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:24498240	PBO:0113634	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:0113639	Figure 3A indicates that deletion of rho2+ gene alleviated the increased Pmk1 basal phosphorylation present in pck1D cells.
PMID:24498240	PBO:0113640	(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:0113638	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	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: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:0113634	Rho1 GTPase might modulate the activity Pmk1 by acting upstream of Pck2 because it has been described that overexpres- sion of wild type or a constitutively active allele of rho1+ (G15V mutant) induced a marked hyperactivation of Pmk1 (Figure 1B
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: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: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	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:24514900	PBO:0105619	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	high penetrance
PMID:24521463	PBO:0093576	low expressivity
PMID:24521463	PBO:0094264	high expressivity (strong phenotype)
PMID:24521463	PBO:0097692	mild phenotype
PMID:24521463	FYPO:0002060	decreased cell pop is not a child of this term
PMID:24521463	PBO:0094265	mild expressivity
PMID:24554432	GO:2000114	sufficient to trigger cell shape change when targeted to cell sides by fusion with Cdr2
PMID:24554432	GO:2000114	necessary to trigger cell shape change upon Tea4 targeting to cell sides by fusion with Cdr2
PMID:24554432	GO:0030010	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	necessary to trigger cell shape change upon Tea4 targeting to cell sides by fusion with Cdr2
PMID:24554432	GO:2000784	sufficient to trigger cell shape change when targeted to cell sides by fusion with Cdr2
PMID:24569997	PBO:0105209	changed from transcription because mrna measured fig2 (copper excess)
PMID:24569997	PBO:0105211	changed from transcription because mrna measured fig2
PMID:24569997	PBO:0105208	changed from transcription because mrna measured (fig 1)
PMID:24569997	PBO:0105207	changed from transcription because mrna measured (fig 1)
PMID:24569997	PBO:0105206	changed from transcription because mrna measured (fig 1)
PMID:24569997	PBO:0105209	*******during copper excess****** changed from transcription because mrna measured fig2
PMID:24569997	PBO:0025347	Observed at this location during spore maturation by indirect immunofluorescence
PMID:24569997	PBO:0105204	figur 5B
PMID:24569997	PBO:0105204	figure 5B
PMID:24583014	PBO:0105365	Fig. 1B,
PMID:24583014	FYPO:0000274	Fig. S1B,C
PMID:24583014	PBO:0105367	Fig. 3A,B,E, securin abnormally stabilized during anaphase
PMID:24583014	FYPO:0006646	Fig. 2B,C
PMID:24583014	FYPO:0005684	Fig. 2B,C
PMID:24583014	FYPO:0007403	Fig. 2A, , complex seen here in anaphase although it normally forms in prometaphase and disassembles before anaphase
PMID:24583014	PBO:0101464	Fig. 1D,E
PMID:24583014	PBO:0105366	Fig. 1A
PMID:24583014	FYPO:0004301	figure S1B
PMID:24583014	PBO:0105364	Fig. 1A
PMID:24583014	PBO:0105363	Fig. 1A
PMID:24583014	PBO:0105362	Fig. 1A indicating that CDK1 activity remained high
PMID:24586893	PBO:0093563	the extension means that the phenotype has low expressivity (i.e. weak sensitivity)
PMID:24637836	PBO:0093563	sensitivity is weak
PMID:24637836	PBO:0093563	sensitivity is weak.
PMID:24637836	PBO:0093579	sensitivity is weak.
PMID:24637836	PBO:0093563	weak sensitivity
PMID:24637836	GO:0005737	Fluorescence microscopy of Sec13 tagged with GFP at either its N-terminal or C-terminal end.
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:0093579	sensitivity is weak.
PMID:24652833	GO:0009262	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	no MF possible
PMID:24662054	PBO:0097229	binds both DNA and histone. Not sure if the H3 preference is an artefact of in vitro system
PMID:24662054	GO:0140750	binds both DNA and histone. Not sure if the H3 preference is an artefact of in vitro system
PMID:24663817	PBO:0093617	1D, Fig. 2B
PMID:24663817	PBO:0093617	1D,Fig. 2B
PMID:24663817	PBO:0093617	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	1D, Fig. 2B
PMID:24663817	PBO:0093581	1D, Fig. 2B
PMID:24663817	PBO:0093581	1D,Fig. 2B
PMID:24663817	PBO:0093581	1D,Fig. 2B
PMID:24663817	PBO:0093581	1D
PMID:24663817	PBO:0093581	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)The slight decrease in Cds1 phosphorylation may be caused indirectly by a minor defect in DNA replication
PMID:24663817	PBO:0100314	C13Y and K56R mutations completely eliminated the phosphorylation of Chk1 in MMS-treated cells (Fig. 3A)
PMID:24663817	PBO:0093616	3D
PMID:24663817	PBO:0093616	3D
PMID:24663817	PBO:0093580	3D
PMID:24663817	PBO:0093580	3D
PMID:24663817	PBO:0093617	f3
PMID:24663817	PBO:0100313	C13Y and K56R mutations completely eliminated the phosphorylation of Chk1 in MMS-treated cells (Fig. 3A)
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	f3
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:0100316	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:0100318	C13Y-K56R mutation abolished the interaction with Crb2 (Fig. 5C), not Rad9 (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	Fig. 5A and B
PMID:24663817	PBO:0100319	3a/b
PMID:24663817	PBO:0100320	3a/b. cds1-T11
PMID:24663817	PBO:0100321	3a/b
PMID:24663817	MOD:00696	affected by rad4
PMID:24663817	PBO:0100323	(phosphorylated rad9)
PMID:24696293	FYPO:0000087	supp fig
PMID:24710126	FYPO:0005071	central core
PMID:24710126	FYPO:0003410	convert to double mutant (cnp1 overexpression)
PMID:24710126	FYPO:0005071	central core
PMID:24713849	PBO:0095161	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	PBO:0101244	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	PBO:0101243	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	PBO:0095160	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	GO:1990477	Observed in cells undergoing vegetative growth.
PMID:24713849	GO:1990477	Observed in cells undergoing vegetative growth.
PMID:24713849	GO:1990477	Observed in cells undergoing vegetative growth.
PMID:24713849	GO:1990477	Observed in cells undergoing vegetative growth.
PMID:24713849	GO:1990477	Observed in cells undergoing vegetative growth.
PMID:24713849	PBO:0094859	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	PBO:0095143	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	PBO:0094861	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	PBO:0094862	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	PBO:0094862	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	PBO:0094860	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	PBO:0101249	"[Term] id: FYPO_EXT:0000003 name: low def: ""small fraction of cells (penetrance) or weak phenotype (expressivity)"" [PomBase:curators]"
PMID:24713849	PBO:0101245	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	GO:1990477	Observed in cells undergoing vegetative growth.
PMID:24713849	PBO:0094859	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	PBO:0094860	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	PBO:0095143	mei4 ssm4 crs1 rec8 spo5
PMID:24713849	PBO:0094861	mei4 ssm4 crs1 rec8 spo5
PMID:24741065	PBO:0097925	tor2 phosphorylates mei2. Phosphorylated mei2 is ubiquitylated which targets it for degradation via the proteasome.
PMID:24741065	PBO:0097921	phosphorylation of mei2 targets it for degradation via the proteasome
PMID:24755092	GO:0010494	SPAC12G12.09-mCherry localizes to stress granules
PMID:24755092	GO:0010494	Exo2-GFP localizes to stress granules
PMID:24758716	GO:0019172	qualifier=major
PMID:24758716	GO:0019172	qualifier=minor Hsp3106 (synonym: spDJ-1) has a lower in vitro glyoxalase III activity than Hsp3101 and Hsp3102
PMID:24758716	GO:0019172	qualifier=major
PMID:24768994	FYPO:0001407	Figure 5
PMID:24768994	FYPO:0000684	Figure 5
PMID:24768994	FYPO:0000684	Figure 5
PMID:24768994	GO:0005634	Figure 3
PMID:24768994	PBO:0104274	Figure 2C
PMID:24768994	GO:0005737	Figure 3
PMID:24768994	GO:0005515	Figure 2B
PMID:24768994	GO:0005635	Figure 2A
PMID:24768994	GO:0005515	Figure 2B
PMID:24774534	FYPO:0002061	fig6
PMID:24774534	FYPO:0002061	fig6
PMID:24774534	FYPO:0002060	fig6
PMID:24774534	FYPO:0002060	fig6
PMID:24774534	FYPO:0002060	fig6
PMID:24774534	FYPO:0002060	fig6
PMID:24774534	FYPO:0002060	fig6
PMID:24774534	FYPO:0002060	fig6
PMID:24774534	FYPO:0002060	fig6
PMID:24774534	FYPO:0002060	fig6
PMID:24774534	FYPO:0002060	fig6
PMID:24774534	PBO:0100347	add other complex members
PMID:24787148	PBO:0103362	ubiquitin monmomer inhibits sst2
PMID:24790093	PBO:0108213	Yeast two hybrid
PMID:24790095	GO:0110085	exists_during( metaphase? anaphase A????)
PMID:24790095	PBO:0024047	mitotic interphase
PMID:24790095	GO:0110085	exists_during( metaphase? anaphase A????)
PMID:24798735	PBO:0019669	"this annotation extension means ""small fraction of cells"""
PMID:24798735	PBO:0019539	"this annotation extension means ""small fraction of cells"""
PMID:24798735	PBO:0020891	"this annotation extension means ""small fraction of cells"""
PMID:24798735	PBO:0023418	"this annotation extension means ""small fraction of cells"""
PMID:24806815	PBO:0111551	Mdb1 binds to Hta1 phosphorylated on Ser-129. PR:000027566 = H2A phosphorylated on S129
PMID:24806815	GO:0035861	This localisation requires phosphorylated histone H2A.
PMID:24815688	FYPO:0003743	"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	FYPO:0000104	figure 1D
PMID:24818994	GO:0005737	Figures 3 and 6
PMID:24818994	PBO:0101445	Figures 3 and 6
PMID:24818994	PBO:0101445	Figures 3 and 6
PMID:24818994	GO:0070139	Figure 1 A
PMID:24818994	GO:0005634	Figures 3 and 6
PMID:24818994	PBO:0101444	Figure 5A, +
PMID:24818994	GO:0005737	minor
PMID:24818994	FYPO:0002061	figure 1D
PMID:24818994	FYPO:0000088	figure 1D
PMID:24818994	PBO:0099111	figure 1 A
PMID:24818994	GO:0016929	Figure 1 A
PMID:24818994	PBO:0101443	Figure 1 A
PMID:24831008	PBO:0099223	fig4
PMID:24831008	PBO:0099222	Fig 2
PMID:24831008	PBO:0099222	Fig 2
PMID:24831008	PBO:0099222	Fig 2
PMID:24831008	PBO:0099224	fig1
PMID:24831008	PBO:0099224	fig1
PMID:24831008	PBO:0099225	fig 4g
PMID:24831008	PBO:0099226	fig2
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: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: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:24831008	PBO:0099223	fig4
PMID:24847916	FYPO:0003928	The phenotype is assessed by the high-throughput sequencing.
PMID:24876389	PBO:0096283	have guessed at deleted residues
PMID:24876389	PBO:0096271	ubiquitinated probably at K263.
PMID:24876389	PBO:0096272	SPBC18H10.20c protein appears to have a function as arrestin-related trafficking adaptor, which is involved in ubiquitination of membrane transporters and subcellular localization of them. val, I changed the 'with' field to pub1, but I want to also add *****
PMID:24876389	PBO:0096275	internalization abolished
PMID:24876389	PBO:0096275	abolished internalization
PMID:24876389	PBO:0096275	abolished internalization
PMID:24876389	PBO:0096275	abolished internalization
PMID:24920274	PBO:0104594	figS1
PMID:24920274	PBO:0104608	at sme2 locus (one of several exosome foci in nucleus during vegetative growth)
PMID:24920274	PBO:0104608	at sme2 locus (one of several exosome foci in nucleus during vegetative growth)
PMID:24920274	PBO:0104604	"the def includes ""maintenance of lcoalization WITHIN nucleus"" so it fits the def, but maybe the term looks weird"
PMID:24920274	PBO:0104604	"the def includes ""maintenance of lcoalization WITHIN nucleus"" so it fits the def, but maybe the term looks weird"
PMID:24920274	PBO:0104603	fig3
PMID:24920274	PBO:0104602	fig3
PMID:24920274	PBO:0104603	fig3
PMID:24920274	PBO:0104602	fig3
PMID:24920274	PBO:0094908	abnormal RNA localization to chromatin
PMID:24920274	PBO:0095590	figS1
PMID:24920274	PBO:0104600	figS1
PMID:24920274	FYPO:0000583	figS1
PMID:24920274	FYPO:0000583	figS1
PMID:24920274	PBO:0104597	figS1
PMID:24920274	PBO:0104596	figS1
PMID:24920274	PBO:0104595	figS1
PMID:24920274	PBO:0104599	figS1
PMID:24920274	PBO:0104598	figS1
PMID:24920274	PBO:0104597	figS1
PMID:24920274	PBO:0104596	figS1
PMID:24920274	PBO:0104595	figS1
PMID:24920274	PBO:0104594	figS1
PMID:24920823	PBO:0093475	S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1)
PMID:24920823	PBO:0019669	low penetrance
PMID:24920823	PBO:0103495	targets Byr4 at S248A, S326A, T412A, T429A, S499A, T502A, S533A, results in Byr4 removal from metaphase spindle pole bodies
PMID:24920823	PBO:0093476	S326, T429, S499: added by cyclin-dependent kinase (Cdk1)
PMID:24920823	PBO:0103496	Cdk1-dependent, Cdk1 non-phosphorylatable Byr4 localizes to one or both SPBs in >90% of metaphase cells
PMID:24920823	PBO:0093476	S326, T429, S499: added by cyclin-dependent kinase (Cdk1)
PMID:24920823	PBO:0113865	affecting Cdc7
PMID:24920823	GO:0031031	Term name: supports establishment of SIN asymmetry Definition: characterized by asymmetric localization of the SIN initiator kinase Cdc7 in anaphase
PMID:24920823	PBO:0093475	S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1)
PMID:24920823	FYPO:0004562	results from collapse of actomyosin contractile ring
PMID:24920823	PBO:0094078	medium penetrance
PMID:24920823	PBO:0019671	anaphase B
PMID:24920823	PBO:0093475	S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1)
PMID:24920823	PBO:0093475	S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1)
PMID:24925530	FYPO:0003107	starts with longer telomeres than wild type, which then shorten
PMID:24928430	FYPO:0006103	Fig. 4 - minor rescue
PMID:24928430	FYPO:0006103	Fig. 4 - minor rescue
PMID:24928430	FYPO:0009001	Fig. 3 - minor rescue
PMID:24928430	FYPO:0009001	Fig. 3 - minor rescue
PMID:24928430	FYPO:0006103	Fig. 3 - minor rescue
PMID:24928430	FYPO:0006103	Fig. 3 - minor rescue
PMID:24928430	FYPO:0009001	Fig. 3
PMID:24928430	FYPO:0006103	Fig. 3
PMID:24928430	FYPO:0000899	Fig. 2
PMID:24928430	FYPO:0009000	Fig. 1
PMID:24928430	FYPO:0008008	Fig. 1
PMID:24928510	PBO:0096003	Phosphorylation assayed in vitro
PMID:24928510	PBO:0096003	protein phosphorylation assayed in vitro
PMID:24928510	PBO:0096003	protein phosphorylation assayed in vitro
PMID:24928510	PBO:0096003	Phosphorylation assayed in vitro
PMID:24928510	PBO:0101351	Phosphorylation assayed in vitro
PMID:24928510	PBO:0096003	Phosphorylation assayed in vitro
PMID:24928510	PBO:0096003	Phosphorylation assayed in vitro
PMID:24928510	PBO:0106561	Protein phosphorylation assayed in vitro
PMID:24928510	PBO:0106561	Protein phosphorylation assayed in vitro
PMID:24928510	PBO:0106563	protein phosphorylation assayed in vitro
PMID:24928510	PBO:0096003	Phosphorylation assayed in vitro
PMID:24928510	PBO:0106563	protein phosphorylation assayed in vitro
PMID:24928510	PBO:0106579	protein phosphorylation assayed in vitro
PMID:24928510	PBO:0106579	protein phosphorylation assayed in vitro
PMID:24928510	PBO:0106580	protein phosphorylation assayed in vitro
PMID:24928510	PBO:0106579	protein phosphorylation assayed in vitro
PMID:24928510	PBO:0106582	protein phosphorylation assayed in vitro
PMID:24936793	GO:0071218	also inferrable (IC) from GO:0051787
PMID:24937146	PBO:0094143	affecting Pcp1 and Alp4
PMID:24937146	PBO:0098527	affecting Alp7
PMID:24937146	PBO:0098529	affecting Pcp1 and Alp4
PMID:24939935	FYPO:0008181	Fig. 1G
PMID:24939935	PBO:0093559	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:0002061	Fig. 4D
PMID:24939935	FYPO:0002061	Fig. 4D
PMID:24939935	FYPO:0008182	Fig. 4E
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 phosphor- ylation.
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 phosphor- ylation.
PMID:24939935	PBO:0093557	Fig. 4D
PMID:24939935	FYPO:0004481	Fig. 4D
PMID:24939935	PBO:0093560	Fig. 4D
PMID:24939935	FYPO:0002061	Fig. 4D
PMID:24939935	FYPO:0008181	Fig. 1G
PMID:24939935	PBO:0093561	Fig. 1D
PMID:24939935	PBO:0093561	Fig. 4D
PMID:24939935	PBO:0093561	Fig. 1D
PMID:24939935	PBO:0093558	Fig. 1D
PMID:24939935	PBO:0093557	Fig. 1D
PMID:24939935	FYPO:0002061	Fig. 1D
PMID:24939935	FYPO:0002061	Fig. 1D
PMID:24939935	PBO:0093558	Fig. 1D
PMID:24939935	PBO:0093556	Fig. 1D
PMID:24939935	PBO:0093557	Fig. 1D
PMID:24939935	PBO:0093558	Fig. 1D
PMID:24939935	FYPO:0002061	Fig. 1D
PMID:24945319	GO:0005847	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	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	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:0098152	Fig 6 B.
PMID:24947517	FYPO:0002060	Fig 6 B.
PMID:24947517	PBO:0035611	Fig. 3A
PMID:24947517	GO:0032153	Fig. 5A
PMID:24947517	FYPO:0001357	Fig. 1B
PMID:24947517	FYPO:0001357	Fig. 1B
PMID:24947517	FYPO:0001315	Fig. 1B
PMID:24947517	FYPO:0000650	Fig. 1C
PMID:24947517	FYPO:0005628	Fig 1 D (decreased rate of cell separation)
PMID:24947517	FYPO:0000673	Fig 1 D
PMID:24947517	PBO:0098140	Fig 1 E
PMID:24947517	PBO:0098140	Fig 1 E
PMID:24947517	PBO:0098141	fig 1 F
PMID:24947517	PBO:0097059	Fig 1 F
PMID:24947517	PBO:0035615	Fig 1 F
PMID:24947517	PBO:0019669	fig 1 F
PMID:24947517	PBO:0098142	Figure 3 C
PMID:24947517	PBO:0098142	Figure 3 C
PMID:24947517	PBO:0098143	Data not shown
PMID:24947517	PBO:0098144	Data not shown
PMID:24947517	PBO:0098145	Fig. 3F
PMID:24947517	PBO:0098145	Fig. 3F
PMID:24947517	PBO:0098145	Fig. 3F
PMID:24947517	PBO:0098146	Data not shown
PMID:24947517	PBO:0098147	Data not shown
PMID:24947517	PBO:0098148	Fig 4 A
PMID:24947517	PBO:0035620	Fig 4 A
PMID:24947517	PBO:0098148	Fig 4 A
PMID:24947517	PBO:0098148	Fig 4 A
PMID:24947517	PBO:0092529	Fig. 4A
PMID:24947517	PBO:0098149	Fig. 4A
PMID:24947517	GO:0005515	Fig 4 C,D,E
PMID:24947517	GO:0005886	Fig. 5A
PMID:24947517	PBO:0098150	Fig 5 A
PMID:24947517	PBO:0098151	Fig 5 B
PMID:24947517	FYPO:0002061	Fig. 6A
PMID:24947517	FYPO:0002061	Fig. 6A
PMID:24947517	FYPO:0002061	Fig 6 B.
PMID:24947517	GO:0016192	(Fig. 6D)
PMID:24947517	PBO:0098155	Fig 6 D.
PMID:24947517	PBO:0095634	Fig 6 C, D
PMID:24947517	FYPO:0002061	Fig 6 C.
PMID:24947517	PBO:0098154	Fig 6 B.
PMID:24947517	PBO:0098153	Fig 6 B.
PMID:24947517	FYPO:0002060	Fig 6 B.
PMID:24954052	PBO:0111560	GO:0051286 = cell tip PR:000037082 = ID for unacetylated form of cdc8
PMID:24954052	PBO:0111559	PR:000037081= ID for acetylated form of cdc8
PMID:24954111	PBO:0102137	bipolar/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:0102133	fig1 In wild-type cells, monopolar or nonpolar spindles were not observed (Fig. 4C).
PMID:24954111	PBO:0102132	fig1
PMID:24954111	PBO:0102138	spindle defects caused by the loss of telomere clustering were rescued by stopping nuclear movement.
PMID:24954111	PBO:0102131	fig1
PMID:24954111	FYPO:0000678	Fig 6 A,B even in the presence of the bipolar spindle
PMID:24954111	FYPO:0006366	never observed 54/54
PMID:24954111	FYPO:0006366	never observed 37/37
PMID:24957674	PBO:0100330	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	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:0100331	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	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	PBO:0099264	(GO:0000279) = mitotic M-phase
PMID:24963130	FYPO:0002636	(comment: 2 sub populations spindle elongation delayed during anaphase. A spindle elongation delayed during anaphase B)
PMID:24997422	FYPO:0001164	). Interestingly, growth of transformants over- expressing truncated Fxn1 with a disrupted mitochondrial localization sequence (Fxn1Δ2–11) is similar to pREP3X at all concentrations of thi- amine (Fig. 1A). These observations demonstrate that the growth inhi- bition resulting from Fxn1 overexpression is related to mitochondrial levels or improper processing of Fxn1.
PMID:25002536	PBO:0097280	LTR and ncRNA
PMID:25002536	PBO:0097281	occurs at LTR and ncRNA
PMID:25002536	GO:0000785	occurs at LTR and ncRNA
PMID:25002536	GO:0000785	occurs at LTR and ncRNA
PMID:25002536	PBO:0097281	LTR and ncRNA
PMID:25002536	PBO:0097280	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:0102768	same as spt20delta alone
PMID:25015293	PBO:0102774	multinucleate inferred from DNA content
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	GO:0005737	punctate
PMID:25015293	PBO:0102768	same as spt20delta alone
PMID:25015293	PBO:0102762	multinucleate inferred from DNA content
PMID:25015293	PBO:0102768	same as spt20delta alone
PMID:25040903	FYPO:0000024	Figure S1C
PMID:25040903	FYPO:0001492	Figure S1C
PMID:25040903	PBO:0099500	Figure S1E
PMID:25040903	PBO:0099499	Figure S1E
PMID:25057016	PBO:0109495	Fig. 4
PMID:25057016	PBO:0093565	Fig. 1
PMID:25057016	PBO:0109494	Fig. 4
PMID:25057016	FYPO:0003840	Fig. 1
PMID:25057016	PBO:0109494	Fig. 3
PMID:25057016	PBO:0109493	Fig. S1D
PMID:25057016	FYPO:0003566	Fig. 2
PMID:25057016	FYPO:0003566	Fig. 2
PMID:25057016	PBO:0109495	Fig. 4
PMID:25057016	PBO:0109497	Fig. 4 (BiFC)
PMID:25057016	FYPO:0003840	Fig. 4
PMID:25057016	FYPO:0003566	Fig. 4
PMID:25057016	FYPO:0009114	Fig. 4
PMID:25057016	PBO:0109494	Fig. 4
PMID:25057016	PBO:0109497	Fig. 4 (BiFC)
PMID:25057016	PBO:0109497	Fig. 4
PMID:25057016	PBO:0109497	Fig. 4
PMID:25057016	PBO:0109496	Fig. 3
PMID:25057016	PBO:0109495	Fig. 3
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	FYPO:0000228	Fig. 6
PMID:25057016	FYPO:0000228	Fig. 6
PMID:25057016	FYPO:0000228	Fig. 6
PMID:25057016	PBO:0109498	Fig. S5D
PMID:25057016	FYPO:0003840	Fig. 4
PMID:25057016	FYPO:0003566	Fig. 4
PMID:25057016	FYPO:0009114	Fig. 4
PMID:25066056	GO:0045547	nus1 was shown to be indispensable subunit of dehydrodolichyl diphosphate synthase. It is not active cis-prenyltransferase by itself but it forms active enzyme with rer2 (SPAC4D7.04c)
PMID:25066056	FYPO:0002061	The heterozygous deletion h+/ h+ strains with exchanged one copy of SPBC2A9.06c ORFs for kanMX4 cassette (Genome-wide Deletion Mutant Library (Bioneer) was able to produce viable spores only when transformed with plasmid expressing Giardia lamblia cis-prenyltransferase but not carrying empty vector.
PMID:25066056	GO:0045547	rer2 was shown to be indispensable subunit of dehydrodolichyl diphosphate synthase. It is not active cis-prenyltransferase by itself but it forms active enzyme with nus1
PMID:25081204	GO:0106057	prz1 is the pombe equivalent to NFAT (functional equivalent rather than orholog)
PMID:25081204	FYPO:0001122	the pop grows more slowly but I guess they are viable en large
PMID:25081204	PBO:0097246	cmk1 seems to phosphorylate prz1 which makes prz1 cytoplasmic. During response to calcium, calcineurin dephosphorylates prz1 and it goes to the nucleus.
PMID:25081204	GO:0106057	prz1 is the pombe equivalent to NFAT (functional equivalent rather than orholog)
PMID:25103238	GO:0140480	Failure of NE fenestration during mitosis in the double tts1del cut1-6 mutant
PMID:25103238	PBO:0022383	large fraction of cells = annotation_extension=has_penetrance(FYPO_EXT:0000001)
PMID:25106870	GO:1990516	Incision of ribonucleotides paired to 8oxoguanine in the DNA
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). changed from dna repair to translesion synthesis. /AL
PMID:25106870	GO:0003887	fig 1
PMID:25106870	GO:0070716	RER should probably be a child of this
PMID:25106870	GO:0004523	fig5
PMID:25109267	GO:1990748	Ricinoleic acid, RA moieties from phospholipids
PMID:25122751	FYPO:0003908	At stress response genes
PMID:25195688	GO:1990536	transmembrane import into Golgi lumen
PMID:25195688	GO:1990536	transmembrane import into Golgi lumen
PMID:25203555	GO:0005515	not sure
PMID:25203555	PBO:0100996	regulator of structure-specific DNA nuclease
PMID:25204792	PBO:0107951	defect in sexual development in response to zinc or iron limitation
PMID:25204792	PBO:0107954	defect in sexual development in response to zinc or iron limitation
PMID:25245948	FYPO:0003555	cDNA; no introns
PMID:25245948	PBO:0102503	cDNA; no introns
PMID:25245948	PBO:0102504	cDNA; no introns
PMID:25245948	PBO:0102504	cDNA; no introns
PMID:25245948	GO:0031509	Fig. 1
PMID:25245948	PBO:0094688	cDNA; no introns
PMID:25245948	PBO:0102503	cDNA; no introns
PMID:25254656	FYPO:0006893	figure 3C the N erminal domain has a dominent -ve effect in in vitro assay (not expression should ne n/a)
PMID:25254656	FYPO:0003328	Figure 3A
PMID:25254656	FYPO:0005682	Figure 4A)
PMID:25254656	FYPO:0005485	figure 3C
PMID:25254656	FYPO:0000091	Figure S2A
PMID:25254656	FYPO:0003328	Figure S15
PMID:25254656	FYPO:0005799	igure 3B Figure 3C
PMID:25254656	FYPO:0006892	figure 3C
PMID:25254656	GO:0052843	in vitro Figure S1A, right pane
PMID:25254656	GO:0000828	in vitro Figure S1A, right pane
PMID:25254656	PBO:0096502	Figure 4E
PMID:25254656	PBO:0096501	Figure 4E
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:0001355	permissive temperature for bbl1-9
PMID:25318672	FYPO:0000674	Mutant cells grow normally in liquid minimal medium supplemented with ethanolamine.
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	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:0006934	Determined by thin layer chromatography (TLC)
PMID:25318672	FYPO:0000674	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	FYPO:0006934	Determined by thin layer chromatography (TLC)
PMID:25318672	FYPO:0000674	Mutant cells grow normally in liquid minimal medium supplemented with choline.
PMID:25318672	FYPO:0002061	restrictive temperature for bbl1-9
PMID:25318672	FYPO:0001357	restrictive temperature for bbl1-9
PMID:25318672	PBO:0095685	restrictive temperature for bbl1-9
PMID:25318672	FYPO:0006934	Determined by thin layer chromatography (TLC)
PMID:25318672	PBO:0096383	Determined by thin layer chromatography (TLC)
PMID:25318672	PBO:0096381	The endoplasmic reticulum is wrapped around the abnormally large lipid droplets
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-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: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:0003107	Tpz1-L439R,L445R disrupts interaction with Ccq1 but retain interactions with Pot1 and Poz1 based on co-IP experiments.
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:0110012	Fig. 3
PMID:25348260	PBO:0110012	Fig. 3
PMID:25348260	PBO:0110012	Fig. 3
PMID:25348260	PBO:0110015	Fig. 3
PMID:25348260	PBO:0110013	Fig. 3
PMID:25348260	PBO:0110015	Fig. 3
PMID:25348260	PBO:0110013	Fig. 3
PMID:25348260	PBO:0110014	Fig. 3
PMID:25348260	PBO:0110014	Fig. 3
PMID:25356590	PBO:0113715	Fig. 3E
PMID:25356590	PBO:0113699	Fig. 3E
PMID:25356590	PBO:0102526	Fig. 3D
PMID:25356590	PBO:0113698	Fig. 3D
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	PBO:0113714	Fig. 3D
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: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:0113722	Fig. S5
PMID:25356590	PBO:0113722	Fig. S5
PMID:25356590	PBO:0113721	Fig. 4A
PMID:25356590	PBO:0113720	Fig. 4A
PMID:25356590	PBO:0113718	Fig. 4A
PMID:25356590	PBO:0113719	Fig. 4A
PMID:25356590	PBO:0113719	Fig. 4A
PMID:25356590	PBO:0113719	Fig. 4A
PMID:25356590	PBO:0113718	Fig. 4A
PMID:25356590	PBO:0113717	Fig. 3E
PMID:25356590	PBO:0113716	Fig. 3E
PMID:25356590	PBO:0113716	Fig. 3E
PMID:25356590	PBO:0113716	Fig. 3E
PMID:25356590	PBO:0113699	Fig. 3E
PMID:25356590	PBO:0113693	Fig. 1D
PMID:25356590	PBO:0113696	Fig. 1D
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: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. 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:0113707	Fig. 2C
PMID:25356590	PBO:0113706	Fig. 2A
PMID:25356590	PBO:0113706	Fig. 2A
PMID:25356590	PBO:0113705	Fig. 2A
PMID:25356590	PBO:0113705	Fig. 2A
PMID:25356590	PBO:0113704	Fig. 2A
PMID:25356590	FYPO:0008252	Fig. 1C
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	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:0113699	Fig. 1F
PMID:25356590	PBO:0113699	Fig. 1F
PMID:25356590	FYPO:0008246	Fig. 1E
PMID:25356590	PBO:0102526	Fig. 1E
PMID:25356590	PBO:0113698	Fig. 1E
PMID:25356590	PBO:0113698	Fig. 1E
PMID:25356590	PBO:0113698	Fig. 1E
PMID:25356590	PBO:0113694	Fig. 1D
PMID:25356590	PBO:0113698	Fig. 1E
PMID:25356590	PBO:0113698	Fig. 1E
PMID:25356590	PBO:0113695	Fig. 1D
PMID:25356590	FYPO:0002917	Fig. 1B
PMID:25356590	FYPO:0002917	Fig. 1B
PMID:25356590	FYPO:0002917	Fig. 1B
PMID:25356590	PBO:0113697	Fig. 1D
PMID:25356590	PBO:0113697	Fig. 1D
PMID:25356590	FYPO:0002917	Fig. 1B
PMID:25356590	FYPO:0002917	Fig. 1B
PMID:25356590	PBO:0113692	Fig. 1B
PMID:25356590	FYPO:0005311	Fig. 1B
PMID:25356590	PBO:0113693	Fig. 1D
PMID:25356590	PBO:0113722	Fig. S5
PMID:25356590	PBO:0113698	Fig. 3D
PMID:25356590	PBO:0113713	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:25375240	PBO:0095421	indicated by increased mad2 on unattached kinetochores
PMID:25375240	PBO:0095416	figure 5E
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	PBO:0095418	Figure 7D
PMID:25375240	FYPO:0001270	Figure 4G
PMID:25375240	FYPO:0002060	Figure 7D
PMID:25378562	FYPO:0000116	Sensitive to 3 mM ZnCl2. Suppressed by overexpression of budding yeast VAM7.
PMID:25378562	FYPO:0001423	mutants defective in vacuolar sorting do not deliver SpCPY to the 185 vacuole but rather to the outside of the cells.
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 185 vacuole but rather to the outside of the cells.
PMID:25378562	FYPO:0000116	Sensitive to 3 mM ZnCl2
PMID:25392932	GO:0006386	Our data only demonstrate that this true for RNA Polymerase III // MOVED UP TO 'REGULATION' FROM NEG REG BASED ON NEW PUBLICATION
PMID:25392932	PBO:0098562	SO:0001272 = tRNA gene
PMID:25392932	PBO:0098562	SO:0001272 = tRNA gene
PMID:25402480	PBO:0104436	"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:0104435	"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	"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:0104438	"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:0104437	"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: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:0106682	Table 2
PMID:25404562	PBO:0106686	Table 2
PMID:25404562	PBO:0106687	Table 2
PMID:25404562	PBO:0106688	Table 2
PMID:25404562	PBO:0106689	Table 2
PMID:25404562	PBO:0106690	Table 2
PMID:25404562	PBO:0106691	Table 2
PMID:25404562	PBO:0106692	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:0106681	Table 2
PMID:25404562	PBO:0106686	Table 2
PMID:25404562	PBO:0106687	Table 2
PMID:25404562	PBO:0106690	Table 2
PMID:25404562	PBO:0106681	Table 2
PMID:25404562	PBO:0106686	Table 2
PMID:25404562	PBO:0106687	Table 2
PMID:25404562	PBO:0106689	Table 2
PMID:25404562	PBO:0106688	Table 2
PMID:25404562	FYPO:0001357	Fig. 3A
PMID:25404562	FYPO:0001234	Fig. 2A (11 days for visible colonies)
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	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:0114479	specific term requested
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:0106685	specific term requested
PMID:25410910	PBO:0098171	yes it looks like pol II?! (val: changed to DNA binding term)
PMID:25411334	FYPO:0000026	Supp S2A
PMID:25411334	FYPO:0000026	Supp S2A
PMID:25411334	FYPO:0000026	Supp S2A
PMID:25411338	GO:0031520	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: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:0024683	during cellular response to glucose starvation
PMID:25411338	PBO:0094264	strong phenotype = has_severity(FYPO_EXT:0000001)
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: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: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	PBO:0094264	strong phenotype = has_severity(FYPO_EXT:0000001)
PMID:25411338	GO:0031520	during cellular response to glucose starvation
PMID:25411338	GO:0031520	during cellular response to glucose starvation
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:25414342	FYPO:0000581	13.87% of wild-type spore viability (Table S6)
PMID:25414342	FYPO:0005659	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	6.87% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6E, Table S6)
PMID:25414342	FYPO:0002485	20.15% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S6)
PMID:25414342	FYPO:0000581	31.18% of wild-type spore viability (Table S6)
PMID:25414342	FYPO:0005658	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	9.88% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6E, Table S6)
PMID:25414342	FYPO:0002485	30.92% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	FYPO:0000581	7.8% of wild-type spore viability, synergistic relationship (Table S6)
PMID:25414342	FYPO:0005660	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	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.6E, Table S6)
PMID:25414342	FYPO:0002485	55.49% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	FYPO:0000581	20.24% of wild-type spore viability (Table S6)
PMID:25414342	FYPO:0005659	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	15.59% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig.6D, Table S6)
PMID:25414342	FYPO:0002485	45.45% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	FYPO:0000581	21.46% of wild-type spore viability, synergistic relationship (Table S6)
PMID:25414342	FYPO:0005658	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	10.34% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6D, Table S6)
PMID:25414342	FYPO:0002485	38.89% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	FYPO:0004993	91.68% of wild-type spore viability, epistatic relationship (Table S6)
PMID:25414342	FYPO:0005659	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	27.08% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6D, Table S6)
PMID:25414342	FYPO:0002485	49.8% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	FYPO:0000581	21.45% of wild-type spore viability, synergistic relationship (Table S6)
PMID:25414342	FYPO:0005659	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	7.33% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6C, Table S6)
PMID:25414342	FYPO:0002485	59.57% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	FYPO:0000581	37.75% of wild-type spore viability, epistatic relationship (Table S6)
PMID:25414342	FYPO:0005659	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	8.33% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6C, Table S6)
PMID:25414342	FYPO:0002485	32.13% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	FYPO:0000581	73.46% of wild-type spore viability, epistatic relationship (Table S6)
PMID:25414342	FYPO:0005658	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	52.08% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Table S6)
PMID:25414342	FYPO:0002485	46.52% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	FYPO:0005658	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	36.88% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6C, Table S6)
PMID:25414342	FYPO:0002485	69.41% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	FYPO:0000581	4.11% of wild-type spore viability (Table S6)
PMID:25414342	FYPO:0005659	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	12.19% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6B, Table S6)
PMID:25414342	FYPO:0002485	15.53% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	FYPO:0000581	3.68% of wild-type spore viability, synergistic relationship (Table S6)
PMID:25414342	FYPO:0005659	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	8.87% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6B, Table S6)
PMID:25414342	FYPO:0002485	15.19% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	FYPO:0000581	53.76% of wild-type spore viability, epistatic relationship (Table S6)
PMID:25414342	FYPO:0005659	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	35.42% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6B, Table S6)
PMID:25414342	FYPO:0002485	55.62% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, partial rescue from rad55Δ levels (Table S6)
PMID:25414342	FYPO:0005659	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	3.55% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig.6A, Table S6)
PMID:25414342	FYPO:0002485	28.85% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	FYPO:0000581	54.78% of wild-type spore viability, epistatic relationship (Table S6)
PMID:25414342	FYPO:0005659	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	2.55% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship (Fig.6A, Table S6)
PMID:25414342	FYPO:0002485	25.9% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	FYPO:0005659	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	24.3% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6)
PMID:25414342	FYPO:0003179	7.4% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6A, Table S6)
PMID:25414342	FYPO:0000581	60.64% of wild-type spore viability, epistatic relationship (Table S6)
PMID:25414342	FYPO:0005659	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	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	76.1% of wild-type recombination assayed between ade6-3083 and ade6-469 (Table S6)
PMID:25414342	FYPO:0000581	15.4% of wild-type spore viability, synergistic relationship (Table S6)
PMID:25414342	FYPO:0000581	50.7% of wild-type spore viability, synergistic relationship (Table S5)
PMID:25414342	FYPO:0005660	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	31.1% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Table S5)
PMID:25414342	FYPO:0002485	54.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S5)
PMID:25414342	FYPO:0000581	55.5% of wild-type spore viability, synergistic relationship (Fig. 4D, Table S5)
PMID:25414342	FYPO:0005660	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	21.1% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	65.3% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Fig. 4B, Table S5)
PMID:25414342	FYPO:0000581	9.9% of wild-type spore viability, synergistic relationship (Fig. 4D, Table S5)
PMID:25414342	FYPO:0005657	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	2.1% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, synergistic relationship (Fig. 4B, Table S5)
PMID:25414342	FYPO:0000581	76.9% of wild-type spore viability, epistatic relationship (Fig. 4D, Table S5)
PMID:25414342	FYPO:0005660	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	25.7% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	26.4% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Fig. 4B, Table S5)
PMID:25414342	FYPO:0000581	93.8% of wild-type spore viability, epistatic relationship (Fig. 4D, Table S5)
PMID:25414342	FYPO:0005660	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	14.2% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	33.5% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Fig. 4B, Table S5)
PMID:25414342	FYPO:0000581	13.0% of wild-type spore viability, synergistic relationship (Fig. 4D, Table S5)
PMID:25414342	FYPO:0005660	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	2.5% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	4.5% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, synergistic relationship (Fig. 4B, Table S5)
PMID:25414342	FYPO:0000581	3.7% of wild-type spore viability, synergistic relationship (Fig. 4D, Table S5)
PMID:25414342	FYPO:0003179	0.42% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, synergistic relationship (Fig. 4B, Table S5)
PMID:25414342	FYPO:0004993	104.8% of wild-type spore viability (Fig. 3D, Table S4)
PMID:25414342	FYPO:0005660	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	44.4% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig. 3A, Table S4)
PMID:25414342	FYPO:0002485	55.5% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Fig. 3B, Table S4)
PMID:25414342	FYPO:0004993	117.1% of wild-type spore viability (Fig. 3D, Table S4)
PMID:25414342	FYPO:0005660	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	32.3% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig. 3A, Table S4)
PMID:25414342	FYPO:0002485	48.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Fig.3B, Table S4)
PMID:25414342	FYPO:0000581	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	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	36.3% of wild-type recombination assayed between ade6-3083 and ade6-469 (Table S3)
PMID:25414342	FYPO:0002485	58.1% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S3)
PMID:25414342	FYPO:0000581	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	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	57.9% of wild-type recombination assayed between ade6-3083 and ade6-469 (Table S3)
PMID:25414342	FYPO:0002485	6.4% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S3)
PMID:25414342	FYPO:0000581	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	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	30.1% of wild-type recombination assayed between ade6-3083 and ade6-469 (Table S3)
PMID:25414342	FYPO:0002485	26.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S3)
PMID:25414342	FYPO:0000581	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	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	2.2% of wild-type recombination assayed between ade6-3083 and ade6-469 (Table S3)
PMID:25414342	FYPO:0002485	19.1% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S3)
PMID:25414342	FYPO:0000581	47% of wild-type spore viability (Fig. 2A, Table S3), 18.3-fold higher spore viability than mus81 single mutant
PMID:25414342	FYPO:0005660	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	12.3% of wild-type recombination assayed between ade6-3083 and ade6-469 (Table S3)
PMID:25414342	FYPO:0002485	0.9% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S3)
PMID:25414342	FYPO:0000581	43.6% of wild-type spore viability (Table S6)
PMID:25414342	FYPO:0005657	(Fig. 5, Table S6)
PMID:25414342	FYPO:0003179	8.0% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 6, Table S6)
PMID:25414342	FYPO:0002485	31.4% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S6)
PMID:25414342	FYPO:0000581	77.7% of wild-type spore viability (Fig. 4D, Table S5)
PMID:25414342	FYPO:0005660	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	9.7% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	16.3% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Fig. 4B, Table S5)
PMID:25414342	FYPO:0004993	133.5% of wild-type spore viability (Fig. 3D, Table S4)
PMID:25414342	FYPO:0005660	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	49.2% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 3A, Table S4)
PMID:25414342	FYPO:0002485	49.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Fig. 3B, Table S4)
PMID:25414342	FYPO:0004993	108.5% of wild-type spore viability (Fig. 3D, Table S4)
PMID:25414342	FYPO:0005660	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	27.7% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 3A, Table S4)
PMID:25414342	FYPO:0002485	48.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Fig. 3B, Table S4)
PMID:25414342	FYPO:0004993	95.2% of wild-type spore viability (Fig. 3D, Table S4)
PMID:25414342	FYPO:0005660	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	42.4% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 3A, Table S4)
PMID:25414342	FYPO:0002485	61.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Fig. 3B, Table S4)
PMID:25414342	FYPO:0000581	61.1% of wild-type spore viability (Fig. 4D, Table S5)
PMID:25414342	FYPO:0005660	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	39.7% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	28.9% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Fig. 4B, Table S5)
PMID:25414342	FYPO:0000581	78.4% of wild-type spore viability (Table S2)
PMID:25414342	FYPO:0005659	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	83.9% of wild-type spore viability (Fig. 4D, Table S5)
PMID:25414342	FYPO:0005657	(Fig. 4C, Table S5)
PMID:25417108	FYPO:0004820	Affecting Rad52 enrichment at rDNA
PMID:25417108	PBO:0095377	occurs at tDNA
PMID:25417108	FYPO:0004818	affecting antisense transcription at tDNA
PMID:25417108	FYPO:0004817	affecting antisense transcription at rDNA
PMID:25417108	FYPO:0004819	Affecting Rad52 enrichment at rDNA
PMID:25417108	FYPO:0004814	affecting: highly transcribed genes antisense transcription of tDNA and rDNA
PMID:25417108	GO:0006369	occurs at rDNA, tRNA gene, protein coding gene
PMID:25417108	FYPO:0004813	affecting: highly transcribed genes antisense transcription of tDNA and rDNA
PMID:25417108	FYPO:0003103	Affecting Dcr1-terminated genes
PMID:25417108	FYPO:0004812	affecting: highly transcribed genes antisense transcription of tDNA and rDNA
PMID:25417108	GO:0006363	occurs at rDNA, tRNA gene, protein coding gene
PMID:25417108	GO:0006386	occurs at rDNA, tRNA gene, protein coding gene
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: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: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:0111000	We therefore conclude that tgp1(+) is regulated by transcriptional interference.
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: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	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: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	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	Trun- cations 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: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	Trun- cations 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: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: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: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: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:25428987	PBO:0020227	mitotic interphase
PMID:25451933	FYPO:0001366	The fission yeast lacking Aip1 have normal appearing actin patches, cables, and contractile rings (Fig. 5B).
PMID:25451933	FYPO:0006187	igs. 6B and C and Table 3
PMID:25451933	GO:0003786	competatively with cofilin
PMID:25451933	FYPO:0007573	Surprisingly, contractile rings began to constrict earlier in 􏰀aip1 cells than wild type cells (Fig. 7, A and B, and Table 3), foreshortening the maturation period before constriction
PMID:25451933	FYPO:0007573	As a result, ring constriction in 􏰀aip1 cells takes 􏰅 5 min less than in wild type cells (Table 3). Overall, cytokinesis was 􏰅16 min (24%) faster in 􏰀aip1 cells than wild type cells, because the maturation period was shorter and the rings constricted faster.
PMID:25451933	GO:0051014	SpAip1 dramatically stimulated severing by 100 nM cofilin, with a maximum rate at 1.5 􏰋M 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 distin- guish from filament depolymerization.
PMID:25471935	FYPO:0005764	assayed Cdc20 recruitment
PMID:25472718	FYPO:0000674	fig 1A
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	PBO:0101235	Fig. 4A,B
PMID:25472718	FYPO:0004307	Fig. 5D
PMID:25472718	FYPO:0006259	Fig. 5D
PMID:25472718	PBO:0101239	Overall, our data suggest that Klp5–Klp6 delivers PP1 to the attached kinetochores, thereby promoting SAC silencing.
PMID:25472718	FYPO:0001387	Fig. 5A
PMID:25472718	PBO:0101239	Overall, our data suggest that Klp5–Klp6 delivers PP1 to the attached kinetochores, thereby promoting SAC silencing.
PMID:25472718	FYPO:0001387	fig S2B
PMID:25472718	PBO:0101242	Fig. 5A
PMID:25472718	FYPO:0001387	fig S2B
PMID:25472718	PBO:0093556	fig 2 A
PMID:25472718	FYPO:0000674	fig 2 A
PMID:25472718	FYPO:0002061	(supplementary material Fig. S1A
PMID:25472718	PBO:0037884	Fig 1A
PMID:25472718	PBO:0101238	(Fig. 1C–E; Type I
PMID:25472718	FYPO:0004310	Fig. 5A
PMID:25472718	PBO:0101237	(Fig. 1C–E; Type I
PMID:25472718	PBO:0101236	(Fig. 1C–E; Type I
PMID:25472718	PBO:0093561	Fig 1A
PMID:25472718	PBO:0094476	Fig. 1C; Fig. 3D
PMID:25472718	FYPO:0001905	Fig. 4C,D)
PMID:25472718	PBO:0101233	Fig. 4E reduced by >70%
PMID:25472718	PBO:0101232	fig 3 d
PMID:25472718	FYPO:0001387	fig 2A
PMID:25472718	PBO:0101231	Fig. 2C,D
PMID:25472718	PBO:0101234	Fig. 4A,B
PMID:25472718	PBO:0097264	fig 3C
PMID:25472718	PBO:0097264	fig 3A
PMID:25472718	FYPO:0000674	fig 3A
PMID:25472718	FYPO:0000674	fig 3A
PMID:25472718	FYPO:0000674	fig 3A
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:25473118	PBO:0102105	fig6
PMID:25473118	FYPO:0003339	the ring seems to start off forming normally but maturation is delayed, this leads to delayed constriction.
PMID:25473118	PBO:0018576	independent of actin
PMID:25473118	PBO:0102181	fig6
PMID:25487150	GO:0005515	unphosphorylated form
PMID:25500221	PBO:0099955	secretion of acid phosphatase
PMID:25500221	PBO:0099955	secretion of acid phosphatase
PMID:25501814	PBO:0107514	(Fig. 3C).
PMID:25501814	PBO:0107510	fig1
PMID:25501814	PBO:0107511	fig1c
PMID:25501814	PBO:0107512	fig 2g
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:0023023	fig1
PMID:25501814	PBO:0018634	fig1
PMID:25501814	PBO:0099316	fig1
PMID:25501814	PBO:0018845	fig1
PMID:25501814	PBO:0018845	fig1
PMID:25519804	PBO:0106417	high suppression of phenotype
PMID:25519804	FYPO:0003911	efficient suppression of ade6-M26; very poor suppression of ade6-M375
PMID:25519804	PBO:0106417	high suppression of phenotype
PMID:25519804	FYPO:0003911	suppresses ade6-M26 efficiently; suppresses ade6-M375 weakly
PMID:25519804	PBO:0106418	low suppression of phenotype
PMID:25520186	PBO:0097184	full-length Cut14 present; not sure how to interpret this, check
PMID:25520186	FYPO:0002061	I only captured the OEX experiment
PMID:25520186	PBO:0097184	full-length Cut14 present; not sure how to interpret this, check
PMID:25520186	PBO:0097183	of condensin complex
PMID:25520186	FYPO:0002060	I only captured the OEX Experiment
PMID:25520186	PBO:0097182	of condensin complex
PMID:25520186	MOD:00047	Auto-phosphorylation occurred in the presence of ATP in vitro
PMID:25520186	MOD:00047	Auto-phosphorylation occurred in the presence of ATP in vitro
PMID:25520186	MOD:00047	Auto-phosphorylation occurred in the presence of ATP in vitro
PMID:25520186	MOD:00047	Auto-phosphorylation occurred in the presence of ATP in vitro
PMID:25520186	MOD:00047	Auto-phosphorylation occurred in the presence of ATP in vitro
PMID:25520186	MOD:00583	Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro
PMID:25520186	MOD:00046	Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro
PMID:25520186	MOD:00046	Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro
PMID:25520186	MOD:00046	Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro
PMID:25520186	MOD:00046	Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro
PMID:25520186	MOD:00046	Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro
PMID:25520186	MOD:00046	Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro
PMID:25520186	MOD:00046	Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro
PMID:25520186	PBO:0097184	full-length Cut14 present; not sure how to interpret this, check
PMID:25533340	PBO:0103462	phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining S192
PMID:25533340	PBO:0022125	This looks like direct regulation because it phosphorylates xlf1
PMID:25533340	FYPO:0000482	leu1
PMID:25533340	FYPO:0003584	increased end-joining activity in vegetative cells
PMID:25533340	PBO:0103465	phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining T180
PMID:25533340	PBO:0103464	phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining T180
PMID:25533340	PBO:0103463	phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining S192
PMID:25533348	PBO:0098715	WT 3%
PMID:25533348	PBO:0098717	fig 3 A
PMID:25533348	PBO:0098722	fig 3 A
PMID:25533348	PBO:0098724	fig 3 A
PMID:25533348	PBO:0098707	greater range of legths
PMID:25533348	PBO:0098708	greater range of legths
PMID:25533348	PBO:0098721	fig 3 A
PMID:25533348	PBO:0098720	fig 3 A
PMID:25533348	PBO:0098707	greater range of legths
PMID:25533348	PBO:0033097	WT 3%
PMID:25533348	PBO:0033098	WT 3%
PMID:25533348	PBO:0033099	WT 3%
PMID:25533348	PBO:0098725	fig 3 A
PMID:25533348	PBO:0098719	fig 3 A
PMID:25533348	PBO:0098718	fig 3 A
PMID:25533348	PBO:0098726	fig 3 A
PMID:25533348	PBO:0098723	fig 3 A
PMID:25533348	PBO:0098727	fig 3 A
PMID:25533956	PBO:0105398	fig5 e
PMID:25533956	PBO:0105397	fig5 e
PMID:25533956	PBO:0105399	RECRUITS
PMID:25543137	GO:0005634	Nuclear localization at 30°C
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	FYPO:0004808	A prionogenic reporter (S. cerevisiae Sup35 prion domain) aggregates in cytoplasmic inclusions in dcr1Δ
PMID:25543137	PBO:0104384	Dcr1 is not released from cytoplasmic inclusions at 37°C in hsp104Δ
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	GO:0005737	Diffuse cytoplasmic localisation at 37°C, no stress granules
PMID:25543137	GO:0005634	Nuclear localization at 30°C
PMID:25590601	PBO:0101539	strong phenotype = has_severity(FYPO_EXT:0000001)
PMID:25590601	PBO:0101537	iii) decreased during glucose starvation
PMID:25590601	PBO:0023218	ii) in the presence of glucose
PMID:25590601	PBO:0023217	ii) removed during nitrogen starvation iv) T415
PMID:25590601	PBO:0023216	ii) removed during glucose starvation ii) observed during nitrogen starvation iv) S546
PMID:25590601	PBO:0023215	ii) removed during glucose starvation ii) observed during nitrogen starvation iv) S546
PMID:25590601	PBO:0023214	ii) removed during glucose starvation ii) observed during nitrogen starvation iv) S546
PMID:25619765	FYPO:0000227	cen2-lacO
PMID:25619765	FYPO:0000227	pNBg was used
PMID:25619998	PBO:0097964	(S2)
PMID:25619998	PBO:0097963	(S2)
PMID:25619998	GO:1990189	(S2)
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	PBO:0037529	causally upstream of ssp2
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:25639242	FYPO:0007434	figure 2a
PMID:25639242	PBO:0101663	causally upstream of ssp2
PMID:25639242	FYPO:0007434	figure 2a
PMID:25639242	PBO:0101653	2D & 4B
PMID:25639242	FYPO:0007434	figure 6E
PMID:25639242	PBO:0101660	fig 6A
PMID:25639242	FYPO:0002673	S3A
PMID:25639242	FYPO:0007434	Fig 3G
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	FYPO:0007434	fig 3B
PMID:25639242	FYPO:0007434	fig 3d
PMID:25639242	FYPO:0007434	Fig 3C
PMID:25639242	PBO:0101653	Fig 4C
PMID:25639242	PBO:0101653	Figure 4C
PMID:25639242	PBO:0101654	figure S2B
PMID:25639242	PBO:0101656	figure S2g
PMID:25639242	FYPO:0005206	FIG 3F
PMID:25639242	PBO:0101657	figure 5a
PMID:25639242	FYPO:0007434	FIG 3F DECOUPLED CELL GROWTH ASND DIVISION
PMID:25639242	PBO:0093770	figure 2b 9% longer
PMID:25639242	FYPO:0007434	figure 4D
PMID:25639242	FYPO:0007434	figure 6E
PMID:25639242	FYPO:0007434	figure 4E
PMID:25688133	FYPO:0004737	LifeAct-mCherry Sid4-GFP
PMID:25688133	PBO:0108656	residues 20â€-40 in synthetic peptide/ dissociation constant of 1.1 nM
PMID:25688133	FYPO:0004747	LifeAct-mCherry Sid4-GFP
PMID:25688133	FYPO:0004747	LifeAct-mCherry Sid4-GFP
PMID:25688133	PBO:0096493	smears as does not self associate, but localizes to medial cortex
PMID:25688133	GO:1990808	residues 20â€-40 in synthetic peptide/ dissociation constant of 1.1 nM
PMID:25688133	PBO:0095196	mCherry-cdc15,Rlc-GFP
PMID:25688133	PBO:0099724	mCherry-cdc15,Rlc-GFP
PMID:25688133	PBO:0095196	mCherry-cdc15,Rlc-GFP
PMID:25688133	PBO:0099724	mCherry-cdc15,Rlc-GFP
PMID:25688133	FYPO:0004737	LifeAct-mCherry Sid4-GFP
PMID:25688133	FYPO:0000729	Live-cell imaging of Rlc1-GFP Sid4-GFP 23% slower
PMID:25688133	FYPO:0000729	Live-cell imaging of Rlc1-GFP Sid4-GFP 26% slower
PMID:25688133	PBO:0101703	Cdc12-mNeonGreen, GFP-Adf1, Ain1-GFP
PMID:25688133	PBO:0101703	Cdc12-mNeonGreen, Ain1-GFP, GFP-Adf1
PMID:25724335	GO:0005739	Gene name : aco2
PMID:25724335	FYPO:0004530	Gene name : aco2
PMID:25724335	GO:0032543	Gene name : aco2
PMID:25724335	FYPO:0002061	Gene name : aco2
PMID:25724335	GO:0005634	Gene name : aco2
PMID:25724335	GO:0005737	Gene name : aco2
PMID:25736293	FYPO:0005988	3B?
PMID:25736293	PBO:0107637	microtubule cortical anchor (microtubule site clamp) add to other dynactin complex
PMID:25736293	PBO:0107637	microtubule cortical anchor (microtubule site clamp) add to other dynactin complex
PMID:25736293	PBO:0107637	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:0000903	Fig. 7F; supplementary material Table S1
PMID:25736293	FYPO:0000903	Fig. 7F; supplementary material Table S1
PMID:25736293	PBO:0107636	fig 7A
PMID:25736293	GO:0005938	accumulates on shrinking microtubules Fig. 2B,
PMID:25736293	GO:0035974	accumulates on shrinking microtubules Fig. 2B,
PMID:25736293	GO:1903754	accumulates on shrinking microtubules Fig. 2B,
PMID:25736293	PBO:0107635	Figure S2C
PMID:25736293	PBO:0107635	Figure S2C
PMID:25736293	GO:0005515	figure S2
PMID:25736293	PBO:0107634	(Fig. 1C; supplementary material Fig. S1C),
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	PBO:0107632	fig 7a
PMID:25736293	PBO:0107647	fig 7a
PMID:25736293	PBO:0107646	abnormal movement of dynein
PMID:25736293	PBO:0107645	abnormal movement of dynein
PMID:25736293	PBO:0107644	fig 6a
PMID:25736293	FYPO:0002177	figS1B
PMID:25736293	FYPO:0002177	figS1B
PMID:25736293	PBO:0107644	fig 6a
PMID:25736293	FYPO:0000927	fig 5 c
PMID:25736293	FYPO:0005988	fig 5 c
PMID:25736293	PBO:0107643	S4B
PMID:25736293	PBO:0107642	S4B
PMID:25736293	GO:1903754	(Fig. 5C
PMID:25736293	GO:0035974	(Fig. 5C
PMID:25736293	PBO:0107641	S4B
PMID:25736293	PBO:0107640	S4B
PMID:25736293	PBO:0107639	S4A
PMID:25736293	PBO:0107639	S4A
PMID:25736293	FYPO:0002177	figS1B
PMID:25736293	FYPO:0000964	figS1B
PMID:25736293	FYPO:0000964	figS1B
PMID:25736293	FYPO:0000964	figS1B
PMID:25736293	FYPO:0000964	figS1B
PMID:25736293	PBO:0107632	figS1B
PMID:25736293	PBO:0107638	S4A
PMID:25736293	PBO:0107632	figS1B
PMID:25736293	PBO:0107633	figS1B
PMID:25736293	PBO:0107633	figS1B
PMID:25736293	PBO:0107638	S4A
PMID:25736293	GO:0051285	fig 4 A
PMID:25736293	FYPO:0005990	fig 3 B , supp S 3 B) abolished microtubule cortical anchoring
PMID:25736293	PBO:0107637	microtubule cortical anchor (microtubule site clamp) add to other dynactin complex
PMID:25736293	PBO:0107636	fig 3 B , supp S 3 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: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:25771684	PBO:0098096	"The term ""Decreased protein binding to Sre1"" is ""decreased protein binding"" that is specific for decreased binding to the protein Sre1."
PMID:25771684	PBO:0097388	"Affecting Sre1 is ""abolished protein processing"" that is specific for defects in Sre1 protein processing."
PMID:25778919	PBO:0108460	Fig. 5 A
PMID:25778919	GO:0044820	Together, these experiments suggest that Aurora-dependent re- moval of Swi6/HP1 and consequently cohesin Rad21 from telo- meres in early mitosis contributes to telomere dispersion.
PMID:25778919	PBO:0108458	Fig 3D
PMID:25778919	PBO:0108462	fig6
PMID:25778919	PBO:0108461	fig 6
PMID:25778919	GO:0044820	Together, these experiments suggest that Aurora-dependent re- moval of Swi6/HP1 and consequently cohesin Rad21 from telo- meres in early mitosis contributes to telomere dispersion.
PMID:25778919	PBO:0108454	telomere disjunction
PMID:25778919	PBO:0108453	(Fig. 2 A, 0–3 min, arrows)
PMID:25778919	GO:0120110	(requested negative regulation of) synonym mitotic telomere dispersion during metaphase
PMID:25778919	PBO:0108455	Fig. S2 A, right
PMID:25778919	FYPO:0005442	Fig 2 CD
PMID:25778919	PBO:0108456	Fig 2 CD decreased telomere dispersion
PMID:25778919	FYPO:0005343	Fig 2 D
PMID:25778919	PBO:0108459	Fig 3
PMID:25778919	PBO:0108457	Fig 3
PMID:25778919	FYPO:0006267	Fig. 4 decreased telomere dispersion
PMID:25778919	FYPO:0004330	Fig. S4 A
PMID:25778919	FYPO:0006264	fig 4
PMID:25778919	FYPO:0006267	fig 4 decreased telomere dispersion
PMID:25778919	PBO:0108462	fig7
PMID:25793410	FYPO:0004752	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:0004751	100 ug/ml G418 for 4 h followed by recovery on YES
PMID:25793410	FYPO:0002344	Sensitivity was rescued by 0.6 M KCl, 10 ug/ml phleomycin for 4 h followed by recovery on YES
PMID:25793410	FYPO:0000633	10 ug/ml G418 for 4 h followed by recovery on YES
PMID:25793410	FYPO:0003559	Sensitivity was rescued by 0.6 M KCl, 40 ug/ml doxorubicin for 4 h followed by recovery on YES
PMID:25793410	FYPO:0002344	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	FYPO:0003559	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	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:0002344	Sensitivity was rescued less efficiently than for the wt by 150 - 600 mM KCl
PMID:25793410	FYPO:0001719	Sensitivity was rescued by 0.6 M KCl 4 mM lithium 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:0093581	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	PBO:0093618	spd1 deletion suppresses brc1delta ddb1delta sensitivity to DNA damage agents
PMID:25795664	PBO:0093631	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:0093614	spd1 deletion suppresses brc1delta csn1delta sensitivity to DNA damage agents
PMID:25795664	FYPO:0001234	A spd1 deletion partially suppresses the synthetic growth defect in a brc1 csn1 double mutant background
PMID:25795664	PBO:0093630	spd1 deletion suppresses brc1delta csn1delta sensitivity to DNA damage agents
PMID:25795664	PBO:0093614	spd1 deletion suppresses brc1delta ddb1delta sensitivity to DNA damage agents
PMID:25798942	GO:0006338	ATPase domain mutant phenotype fig 5 and S6
PMID:25803873	GO:0004175	no peptidase activity acting on azocoll substrate in isp6 null
PMID:25831549	FYPO:0004544	Fig. 3D
PMID:25831549	GO:0033696	Fig. 2
PMID:25831549	FYPO:0004544	Fig. 3D
PMID:25831549	FYPO:0004745	Fig. 7E
PMID:25831549	FYPO:0004544	Fig. 3B
PMID:25831549	FYPO:0004544	Fig. 3C
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:0000887	Fig. 7E
PMID:25831549	FYPO:0004745	Fig. 7D
PMID:25831549	FYPO:0004745	Fig. 7D
PMID:25831549	FYPO:0004745	Fig. 7D
PMID:25831549	FYPO:0004544	Fig. 2A
PMID:25831549	PBO:0098773	Fig. 7E
PMID:25831549	FYPO:0007479	Fig. 3E
PMID:25831549	FYPO:0007479	Fig. 2
PMID:25837586	PBO:0097265	Normal levels of Cdc42 and Cdc42-GTP (CRIB)
PMID:25837586	GO:0030427	Not affected by short-term actin cytoskeleton depolymerization by Latrunculin A
PMID:25837586	PBO:0103551	Increased levels of Cdc42 and Cdc42-GTP (CRIB)
PMID:25837586	PBO:0103556	more severe in presence of LatA
PMID:25837586	PBO:0099084	Decreased 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	PBO:0099084	Decreased levels of Cdc42 and Cdc42-GTP
PMID:25837586	FYPO:0000672	Internally tagged functional allele, allowing live-imaging of Cdc42
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:25838386	FYPO:0002335	Fig. S5
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:25847133	PBO:0107099	Cut14 accumulates at the mitotically-upregulated gene regions in mitosis. Cut14 enrichment requires a forkhead transcription factor Sep1.
PMID:25847133	FYPO:0000141	Abnormally streaked chromosomes in anaphase
PMID:25847133	PBO:0024930	GO:0000087 = mitosis
PMID:25847133	PBO:0107100	This mutant protein decreased chromatin binding at heat-shock genes, ssa1+ and hsp90+
PMID:25847133	PBO:0107098	Cut14 accumulates at the mitotically-upregulated gene regions in mitosis. Cut14 enrichment requires a forkhead transcription factor Sep1.
PMID:25869666	PBO:0098123	Fig. 4
PMID:25869666	GO:0008569	Single deletion slows down nuclear congression (minus-end diretcted), double deletion with dhc1 inhibits it.
PMID:25869666	GO:0008569	Single deletion slows down nuclear congression (minus-end diretcted), double deletion with klp2 inhibits it.
PMID:25869666	PBO:0098123	Fig. 1
PMID:25869666	PBO:0098127	Fig. 4
PMID:25869666	PBO:0098126	Fig. 1
PMID:25869666	PBO:0098125	Fig. 1
PMID:25869666	PBO:0098123	Fig. 4
PMID:25869666	FYPO:0007162	Fig. S1
PMID:25869666	PBO:0098124	Fig. 1
PMID:25869666	PBO:0098122	Fig. 1
PMID:25869666	PBO:0098123	Fig. 1
PMID:25869666	PBO:0098122	Fig. 1
PMID:25869666	PBO:0098121	Fig. S3A
PMID:25869666	PBO:0098120	Localization of GFP-tagged protein
PMID:25869666	PBO:0098119	Localization of GFP-tagged protein
PMID:25869666	GO:0000743	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:25891897	PBO:0033391	zygotic meiosis random spore analysis
PMID:25891897	PBO:0033390	zygotic meiosis random spore analysis,
PMID:25891897	PBO:0033389	zygotic meiosis random spore analysis,
PMID:25891897	PBO:0033404	zygotic
PMID:25891897	PBO:0033405	zygotic
PMID:25891897	PBO:0033402	zygotic 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:0033397	zygotic meiosis random spore analysis
PMID:25891897	PBO:0033396	zygotic
PMID:25891897	PBO:0033395	zygotic
PMID:25891897	PBO:0033392	This phenotype is not seen when cells undergo azygotic meiosis
PMID:25891897	PBO:0033408	zygotic
PMID:25891897	PBO:0033407	zygotic
PMID:25891897	PBO:0033406	zygotic
PMID:25891897	FYPO:0003378	azygotic meiotic cell cyle
PMID:25891897	FYPO:0003379	azygotic meiotic cell cycle/timing of pre-meiotic DNA replication is normal
PMID:25891897	PBO:0033403	zygotic meiosis/ Random spore analysis
PMID:25891897	FYPO:0003563	azygotic/ slight advance in the timing of MI and MII
PMID:25891897	PBO:0033400	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 meiosis, rem1 and crs1 do not have a major role in azygotic meiosis
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	PBO:0033398	zygotic
PMID:25891897	FYPO:0000478	azygotic
PMID:25891897	PBO:0033399	zygotic random spore analysis
PMID:25891897	FYPO:0000478	zygotic
PMID:25891897	PBO:0033332	zygotic
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: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	PBO:0098839	Mutations of the hydrophobic C2-C2 interface shifted Mid1 into monomeric state (Figure 6A),
PMID:25959226	GO:0005546	Interestingly, it binds to PI(4,5)P2 strongly, with a Kd up to 0.12 μM (Figure 3C and 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: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:25965521	PBO:0093618	same as brc1delta alone; brc1 epistatic
PMID:25965521	PBO:0093579	same as brc1delta alone; brc1 epistatic
PMID:25965521	FYPO:0002573	same as either single mutant
PMID:25965521	PBO:0093618	same as brc1delta alone; brc1 epistatic
PMID:25965521	PBO:0093631	same as brc1delta alone; brc1 epistatic
PMID:25965521	PBO:0093615	same as brc1delta alone; brc1 epistatic
PMID:25965521	FYPO:0000085	same as mus81delta alone; mus81 epistatic
PMID:25965521	FYPO:0000089	same as mus81delta alone; mus81 epistatic
PMID:25965521	FYPO:0000268	same as mus81delta alone; mus81 epistatic
PMID:25965521	FYPO:0000088	same as mus81delta alone; mus81 epistatic
PMID:25965521	FYPO:0000085	same as mus81delta alone; mus81 epistatic
PMID:25965521	FYPO:0000089	same as mus81delta alone; mus81 epistatic
PMID:25965521	FYPO:0000088	same as mus81delta alone; mus81 epistatic
PMID:25965521	FYPO:0000268	same as mus81delta alone; mus81 epistatic
PMID:25965521	FYPO:0000089	same as brc1delta alone; brc1 epistatic
PMID:25965521	FYPO:0000089	same as mus81delta alone; mus81 epistatic
PMID:25965521	FYPO:0000085	same as mus81delta alone; mus81 epistatic
PMID:25965521	FYPO:0000088	same as mus81delta alone; mus81 epistatic
PMID:25965521	FYPO:0000268	same as mus81delta alone; mus81 epistatic
PMID:25965521	FYPO:0000089	same as mus81delta alone; mus81 epistatic
PMID:25965521	FYPO:0000085	same as mus81delta alone; mus81 epistatic
PMID:25965521	FYPO:0000088	same as mus81delta alone; mus81 epistatic
PMID:25965521	PBO:0093631	same as brc1delta alone; brc1 epistatic
PMID:25965521	PBO:0093615	same as brc1delta alone; brc1 epistatic
PMID:25965521	PBO:0093579	same as brc1delta alone; brc1 epistatic
PMID:25965521	FYPO:0002573	same as either single mutant
PMID:25965521	FYPO:0000268	same as mus81delta alone; mus81 epistatic
PMID:25977474	FYPO:0000032	abnormal cleavage furrow disc formation fig 3
PMID:25977474	FYPO:0000032	abnormal cleavage furrow disc formation fig 3
PMID:25977474	FYPO:0000032	abnormal cleavage furrow disc formation fig 3
PMID:25977474	FYPO:0000032	abnormal cleavage furrow disc formation fig 3
PMID:25977474	FYPO:0000032	abnormal cleavage furrow disc formation fig 3
PMID:25987607	FYPO:0004396	I think the pkl rigor is spb tethered here?
PMID:25987607	FYPO:0003787	non additive
PMID:25987607	PBO:0018346	during mitotic M phase
PMID:25987607	PBO:0018346	during mitotic M phase
PMID:25987607	PBO:0108309	I want to represent the microtubule based-transporter function and cargo
PMID:25987607	FYPO:0002636	Fig. 5 B and Videos 1–4
PMID:25987607	FYPO:0006173	Fig. 5 B and Videos 1–4
PMID:25987607	PBO:0108310	Fig. 5 B and Videos 1–4
PMID:25987607	PBO:0018346	during mitotic M phase
PMID:25987607	PBO:0108312	Fig. 5 B and Videos 1–4
PMID:25987607	PBO:0108308	I want to represent the microtubule based-transporter function and cargo
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	exosome dependent
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	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	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	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	GO:0071039	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	PBO:0110921	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	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	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:25989903	FYPO:0002960	Deletion of iss10 or mmi1 only affects meiotic mRNAs
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:0008113	Similar to previous reports, we detected significantly increased intronic reads in the exosome mutant rrp6D strain (Fig. 4a,b).
PMID:25989903	GO:0071030	exosome dependent
PMID:25989903	GO:0071030	exosome dependent
PMID:25993311	GO:0090006	table 1
PMID:25993311	PBO:0101138	table 1
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:0101138	table 2
PMID:25993311	PBO:0106054	table2
PMID:25993311	PBO:0112555	table2
PMID:25993311	PBO:0099293	table2
PMID:25993311	FYPO:0005986	fig 3
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	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 2 a
PMID:25993311	PBO:0105331	fig2
PMID:25993311	PBO:0105331	fig2
PMID:25993311	PBO:0106060	fig 2 a
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	PBO:0106060	fig 2 a
PMID:25993311	PBO:0106061	table 3
PMID:25993311	FYPO:0000488	table 3
PMID:26031557	PBO:0098179	Fig. 1. I guess reporter gene assay is the right category, since they do this with the minichrosome bearing the ade6 gene from cerevisiae to rescue ade6-M210
PMID:26031557	PBO:0098180	Fig. 2
PMID:26031557	PBO:0098181	Fig. 2. I guess reporter gene assay is the right category, since they do this with the minichrosome bearing the ade6 gene from cerevisiae to rescue ade6-M210
PMID:26031557	PBO:0098182	Fig. 2. 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:0098187	Fig. S4
PMID:26031557	PBO:0098186	Fig. 4
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	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	FYPO:0000324	Fig. 3
PMID:26031557	FYPO:0005709	Fig. S2 Pkl1md-GFP localized primarily to the spindle poles
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	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	FYPO:0006464	increased length hererogeneity. taz1-4A cells still exhibited extremely heterogeneous telomeres similar to taz1Δ and taz1-4R cells (Figure 1E).
PMID:26088418	PBO:0107811	increased length hererogeneity
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	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	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: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:0107814	he L445R mutation caused a 10-fold decrease in DNA binding with a Kd of ~7 μM (Figure 1I), suggesting that Taz1 homodimerization is
PMID:26088418	PBO:0107811	increased length hererogeneity
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:0096672	large portion of the mutant forms cytoplasmic dots
PMID:26092938	PBO:0104502	decreased 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	PBO:0093560	figure 8a
PMID:26098872	FYPO:0001357	figure 8a
PMID:26098872	PBO:0093560	figure 8 b
PMID:26098872	PBO:0093559	figure 8a
PMID:26108447	FYPO:0002766	Figure 6
PMID:26108447	FYPO:0002640	Figure 6
PMID:26108447	FYPO:0003860	Figure 6
PMID:26108447	FYPO:0003860	Figure 6
PMID:26108447	FYPO:0003860	Figure 6
PMID:26108447	FYPO:0003860	Figure 6
PMID:26108447	FYPO:0003860	Figure 6
PMID:26108447	FYPO:0003358	Figure 6
PMID:26108447	FYPO:0002766	Figure 6
PMID:26108447	FYPO:0002766	Figure 6
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:26122634	FYPO:0004688	polysomal profiling
PMID:26122634	FYPO:0004688	polysomal profiling
PMID:26124291	FYPO:0004614	Fig 7 CD abnormal Q-MT bundle elongation upon G1 re-entry/interphase bundle reassembly
PMID:26124291	PBO:0035552	(Fig. 4 C)
PMID:26124291	PBO:0035552	(Fig. 4 C)
PMID:26124291	PBO:0035552	(Fig. 4 C)
PMID:26124291	PBO:0035552	(Fig. 4 C)
PMID:26124291	PBO:0035552	(Fig. 4 C)
PMID:26124291	PBO:0095574	Fig Fig. S5 E
PMID:26124291	PBO:0035555	Fig 7 E/F
PMID:26124291	FYPO:0005565	Fig 7 E
PMID:26124291	PBO:0095573	FFig. S5 E
PMID:26124291	GO:0099079	Fig 6 C
PMID:26124291	GO:0099079	Fig 6 C
PMID:26124291	PBO:0035552	(Fig. 4 C)
PMID:26124291	GO:0099079	Fig S5A C
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	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 present differ from wild type
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	GO:0072435	Chk1 binds to the unphosphorylated form of Cdc2 kinase
PMID:26132084	FYPO:0005873	figure 4B
PMID:26132084	PBO:0097173	P.P. Bgs4 and Ags1 abnormal localization in the septum membrane
PMID:26132084	FYPO:0003338	Fig 2A and B fragmented with RLC strands
PMID:26132084	FYPO:0003210	figure 1
PMID:26132084	PBO:0097178	Fig 2D and 2E
PMID:26132084	FYPO:0005289	figure 1c
PMID:26132084	PBO:0097179	figure 3
PMID:26132084	FYPO:0004495	fig 3C
PMID:26132084	FYPO:0003890	fig6 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:0005871	fig 4C
PMID:26132084	PBO:0097172	P.P. Bgs4 and Ags1 abnormal localization in the septum membrane
PMID:26132084	PBO:0097174	figure 1 A,B
PMID:26132084	PBO:0097175	fig 3C&D vw: changed to incomplete septum
PMID:26132084	PBO:0097177	fig 5 SH3 domain of Cdc15 is required for the proper concentration of Pxl1 at the CAR
PMID:26132084	FYPO:0000117	fig6
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	of cell tip
PMID:26152587	PBO:0020040	Gaf1-GFP is found in the nucleus following nitrogen starvation but not glucose starvation
PMID:26152587	PBO:0020038	Gaf1-GFP is found in the nucleus following nitrogen starvation but not glucose starvation
PMID:26152587	FYPO:0001357	fig1a
PMID:26152587	FYPO:0001357	fig1a
PMID:26152587	FYPO:0001357	fig1a
PMID:26152587	PBO:0100238	assayed by nuclear localization of Gaf1-GFP
PMID:26152587	FYPO:0001357	fig1a
PMID:26152587	FYPO:0001355	fig1a
PMID:26152587	PBO:0100226	1h in proline medium, a mild phenotype
PMID:26152587	FYPO:0001357	fig1a
PMID:26152587	PBO:0100230	1h in proline medium, a mild phenotype
PMID:26152587	PBO:0100230	1h in proline medium, a mild phenotype
PMID:26152587	PBO:0100228	assayed by nuclear localization of Gaf1-GFP
PMID:26152587	PBO:0100228	assayed by nuclear localization of Gaf1-GFP
PMID:26152587	PBO:0100232	fig1a
PMID:26152587	FYPO:0001357	fig1a
PMID:26152587	PBO:0100227	assayed by nuclear localization of Gaf1-GFP
PMID:26152587	PBO:0100226	1h in proline medium
PMID:26152587	PBO:0018647	Gaf1-GFP is found in the nucleus following nitrogen starvation but not glucose starvation
PMID:26152587	FYPO:0001357	fig1a
PMID:26152587	PBO:0100231	a mild phenotype
PMID:26152587	PBO:0100237	assayed by nuclear localization of Gaf1-GFP
PMID:26152587	PBO:0100231	a mild phenotype
PMID:26152587	PBO:0100239	assayed by nuclear localization of Gaf1-GFP
PMID:26152587	PBO:0100238	assayed by nuclear localization of Gaf1-GFP
PMID:26152587	PBO:0100239	assayed by nuclear localization of Gaf1-GFP
PMID:26160178	PBO:0096388	affecting binding to histone H2A (hta1)
PMID:26160178	PBO:0096385	affecting binding to Mdb1
PMID:26167880	PBO:0092728	Figure 2 SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
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: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	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	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	PBO:0113603	We conclude that phosphorylation of the Dsk1 substrate Bpb1 has a major effect on the genome-wide splicing pattern.
PMID:26167880	PBO:0113601	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:0113596	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:0113598	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	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	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:0092747	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:0113592	Figure 2 SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	PBO:0113593	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	PBO:0113595	Figure 2 SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26221037	PBO:0099739	higher than without nup132d
PMID:26221037	PBO:0099745	modification(s) not identified
PMID:26221037	PBO:0099745	modification(s) not identified
PMID:26221037	PBO:0099741	higher than without nup132d
PMID:26258632	PBO:0112052	fig2d
PMID:26258632	PBO:0093562	fig1a
PMID:26258632	PBO:0097990	fig1e
PMID:26258632	PBO:0093562	fig 3 b
PMID:26258632	FYPO:0005220	ABOLISHED tetermerization
PMID:26258632	FYPO:0004318	fig 3 a/b
PMID:26258632	PBO:0023853	fig2d GO:0000089= mitotic metaphase unattached kinetohore nda3-KM311 arrested cell
PMID:26258632	PBO:0018845	figure 2a (GO:0000090= mitotic anaphase)
PMID:26258632	PBO:0097991	figure 2a GO:0000236=mitotic prometaphase
PMID:26258632	PBO:0033342	fig1b
PMID:26258632	PBO:0096319	fig2a
PMID:26258632	PBO:0033342	fig1b
PMID:26258632	PBO:0093564	fig1a
PMID:26258632	PBO:0093564	fig1a
PMID:26258632	PBO:0093562	fig1a
PMID:26258632	PBO:0033341	fig1b
PMID:26258632	PBO:0097989	kinetochore localization of Cut7 is unaffected
PMID:26258632	FYPO:0005220	ABOLISHED tetermerization fig4f monomer
PMID:26258632	PBO:0097988	fig2a (diminished relocation from kinetochore)
PMID:26258632	PBO:0033340	fig 5 c
PMID:26258632	FYPO:0003762	Fig. 2b (mad1 locaizes to unattached kinetochores) and fig 3a
PMID:26258632	PBO:0097992	fig2a
PMID:26258632	FYPO:0004318	fig 3 a/b
PMID:26258632	FYPO:0004318	fig 3 a/b
PMID:26258632	PBO:0033345	fig 3c
PMID:26258632	PBO:0093562	fig1a
PMID:26258632	PBO:0093562	fig1a
PMID:26258632	PBO:0033343	fig1b
PMID:26258632	FYPO:0000030	"fig 5c ""gliding"" new GO term requested"
PMID:26258632	PBO:0097990	fig1e
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:0094771	Fig. 6
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:26264592	PBO:0094773	Fig. 4A
PMID:26264592	PBO:0094773	Fig. 4A
PMID:26264592	PBO:0094773	Fig. 4A
PMID:26264592	PBO:0094775	Fig. 4C
PMID:26264592	PBO:0094775	Fig. 4C
PMID:26264592	PBO:0094772	Fig. 4C
PMID:26264592	PBO:0094775	Fig. 4C
PMID:26264592	PBO:0094772	Fig. 4C
PMID:26264592	PBO:0094772	Fig. 4C
PMID:26264592	PBO:0111503	Fig. 3C
PMID:26264592	PBO:0111502	Fig. 3C
PMID:26264592	PBO:0111501	Fig. 3C
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:0094738	Fig.2
PMID:26264592	PBO:0094738	Fig.2
PMID:26264592	PBO:0094738	Fig.2
PMID:26264592	PBO:0094738	Fig.1
PMID:26264592	PBO:0094738	Fig.1
PMID:26264592	PBO:0101499	Fig. 1
PMID:26264592	PBO:0094771	Fig.1
PMID:26264592	PBO:0094771	Fig.1
PMID:26264592	PBO:0094771	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:0101499	Fig. 1
PMID:26264592	PBO:0111634	negative extracellular phosphate aquisition (S5P,P6?,S7P)
PMID:26264592	GO:0030643	negative extracellular phosphate aquisition
PMID:26264592	PBO:0111672	negative extracellular phosphate aquisition (S5P,P6?,S7P)
PMID:26264592	PBO:0111671	negative extracellular phosphate aquisition (S5P,P6?,S7P)
PMID:26264592	GO:0030643	negative regulation of extracellular phosphate aquisition
PMID:26264592	GO:0030643	negative regulation of extracellular phosphate aquisition
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: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: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:26275423	GO:0000775	Chromatin immunoprecipitation of this protein is highly enriched for centromeric sequences.
PMID:26365378	FYPO:0006294	macroautophagy? - selective autophagy is a child of macroautophagy
PMID:26365378	PBO:0098887	"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	s3
PMID:26365378	GO:0005515	s3
PMID:26365378	PBO:0110838	Indirect evidence, could be upstream
PMID:26365378	PBO:0098887	4h
PMID:26365378	PBO:0110838	Indirect evidence, could be upstream
PMID:26365378	PBO:0110838	Indirect evidence, could be upstream
PMID:26366556	PBO:0101181	low penetrance
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: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	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: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:0021323	determined by EMSA. Substrate: dsDNA oligonucleotide derived from promoters of cut6 and ptl1 genes (contain the CSL_response_element)
PMID:26366556	GO:0019216	ChIP-seq and microarray data indicate that Cbf11 regulates lipid metabolism genes.
PMID:26366556	FYPO:0006822	low penetrance
PMID:26366556	PBO:0018467	low penetrance
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: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	FYPO:0001122	large fractions of both abnormally long and abnormally short cells are present in the population
PMID:26368543	PBO:0096806	Chk1
PMID:26368543	PBO:0096807	Chk1
PMID:26401015	PBO:0094447	acetyltransferase normally processive in presence of K4-trimethylated H3 (bound by Sgf29)
PMID:26401015	PBO:0094447	acetyltransferase normally processive in presence of K4-trimethylated H3 (bound by Sgf29)
PMID:26401015	PBO:0094446	abolishes preference for K4-trimethylated H3
PMID:26401015	PBO:0094446	abolishes preference for K4-trimethylated H3
PMID:26412298	GO:0061578	Inferred from in vitro biochemical assay using K63-linked di-ubiquitinase (vw JAnel made this annotation , I transferred from process to MF)
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	GO:0016428	in response to queuosine incorporation into tRNA-Asp
PMID:26424849	PBO:0035522	waiting for go-ontology/issues/12536
PMID:26436826	PBO:0103249	alkaline DNA preparation
PMID:26436826	PBO:0103248	alkaline DNA preparation
PMID:26438724	PBO:0104236	fig5
PMID:26438724	GO:0033696	changed from: heterochromatin organization involved in chromatin silencing
PMID:26438724	FYPO:0000220	supp 1b
PMID:26438724	PBO:0104231	supp 1b
PMID:26438724	PBO:0104232	supp 1b
PMID:26438724	PBO:0104233	supp 1b
PMID:26438724	FYPO:0004137	EV3
PMID:26438724	FYPO:0002355	EV3
PMID:26438724	FYPO:0004743	EV3
PMID:26438724	FYPO:0003045	4a
PMID:26438724	FYPO:0005286	4a
PMID:26438724	FYPO:0004749	4a
PMID:26438724	PBO:0104234	EV3
PMID:26438724	FYPO:0004201	fig6
PMID:26438724	PBO:0098760	EV3
PMID:26438724	FYPO:0006362	fig6
PMID:26438724	PBO:0104235	EV3
PMID:26438724	PBO:0104237	fig5
PMID:26438724	PBO:0104236	fig5
PMID:26438724	PBO:0104237	fig5
PMID:26438724	PBO:0104236	fig5
PMID:26438724	PBO:0104237	fig5
PMID:26438724	PBO:0098773	EV3
PMID:26438724	GO:0031507	changed from: heterochromatin organization involved in chromatin silencing
PMID:26443059	FYPO:0005053	actually inferred from protein binding phenotypes
PMID:26443059	FYPO:0005053	actually inferred from protein binding phenotypes
PMID:26443240	PBO:0095330	Pom1 does not relocalize to cell sides
PMID:26443240	PBO:0095330	Pom1 relocalizes to cell sides
PMID:26443240	PBO:0095327	Tea4 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: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 relocalizes to cell sides
PMID:26443240	PBO:0095326	Pom1 does not relocalize to cell sides
PMID:26443240	GO:0005634	absent when glucose limited
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:0095326	Pom1 does not relocalize to cell sides
PMID:26443240	PBO:0095332	Pom1 relocalization to cell sides
PMID:26443240	GO:0031117	through negative regulation of Cls1
PMID:26483559	FYPO:0004093	Fig. 3, A and B; Fig. S5
PMID:26483559	PBO:0035153	Fig 2
PMID:26483559	PBO:0104216	(Fig. 8, B and C), increased or premature
PMID:26483559	PBO:0104215	(Fig. 6) increased or premature
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	FYPO:0005509	fig1b (vw moved down form) abnormal meiotic chromosome segregation
PMID:26483559	PBO:0104214	(Fig. 6) increased or premature
PMID:26483559	PBO:0104219	(Fig. 7 C)
PMID:26483559	FYPO:0005634	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	FYPO:0005634	fig 9A
PMID:26483559	FYPO:0005634	fig 9A
PMID:26483559	PBO:0104218	(Fig. 7, B and C)
PMID:26483559	FYPO:0005512	Fig S1. Assayed by assaying depletion of securin from spindle
PMID:26483559	PBO:0104217	(Fig. 1 D)
PMID:26483559	FYPO:0005383	(Fig. 1 D)
PMID:26483559	FYPO:0005574	Fig. S2
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. 1 B)
PMID:26483559	FYPO:0005384	(Fig. 1 B)
PMID:26483559	FYPO:0004667	(Fig. 4, C and D)
PMID:26483559	FYPO:0005634	fig 9A
PMID:26499799	GO:0030295	cerevisiae substrate
PMID:26518661	PBO:0095649	(Figure 7)
PMID:26518661	FYPO:0006985	(Figure 2)
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:0002336	(Figure 7)
PMID:26518661	FYPO:0006987	(Figure 4)
PMID:26518661	FYPO:0004138	(Figure 4)
PMID:26518661	FYPO:0000862	(Figure 4)
PMID:26518661	PBO:0095637	(Figure 4)
PMID:26518661	PBO:0095638	(Figure 4)
PMID:26518661	PBO:0095639	(Figure 4)
PMID:26518661	PBO:0095640	(Figure 4)
PMID:26518661	PBO:0095641	(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: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: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:26518661	PBO:0094679	(Figure 5) (VW: fixed from normal to decreased -compared to WT)
PMID:26518661	FYPO:0006995	(Figure 5)
PMID:26518661	FYPO:0006995	(Figure 5)
PMID:26518661	FYPO:0006995	(Figure 5)
PMID:26518661	FYPO:0006995	(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	FYPO:0003411	(Figure 5)
PMID:26518661	FYPO:0003094	(Figure 5)
PMID:26518661	FYPO:0006986	(Figure 2)
PMID:26518661	FYPO:0006986	(Figure 2)
PMID:26518661	PBO:0095645	ev4
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:0007002	(Figure 7)
PMID:26518661	PBO:0095650	(Figure 7)
PMID:26518661	PBO:0095652	(Figure 7)
PMID:26518661	FYPO:0007000	(Figure 7)
PMID:26518661	FYPO:0007001	(Figure 7)
PMID:26518661	FYPO:0007002	(Figure 7)
PMID:26518661	PBO:0095651	(Figure 7)
PMID:26518661	FYPO:0007003	(Figure 7)
PMID:26518661	PBO:0095647	(Figure 7)
PMID:26518661	PBO:0095648	(Figure 7)
PMID:26518661	FYPO:0004376	(Figure 7)
PMID:26518661	PBO:0095653	(Figure 7)
PMID:26518661	FYPO:0007000	(Figure 7)
PMID:26518661	FYPO:0007001	(Figure 7)
PMID:26518661	FYPO:0002336	ev4,ef
PMID:26518661	FYPO:0002336	(Figure 7)
PMID:26518661	FYPO:0006985	(Figure 1)
PMID:26518661	PBO:0095634	(Figure 1)
PMID:26518661	FYPO:0000024	(Figure 1)
PMID:26518661	FYPO:0001125	(Figure 1)
PMID:26518661	FYPO:0006985	(Figure 2)
PMID:26518661	FYPO:0006986	(Figure 2)
PMID:26518661	FYPO:0006986	(Figure 2)
PMID:26518661	FYPO:0001355	(Figure 2)
PMID:26527280	PBO:0102439	Fig. S6D
PMID:26527280	PBO:0102438	Fig. S3I,J
PMID:26527280	PBO:0101464	Fig. S3D
PMID:26527280	PBO:0101464	Fig. S3G,H
PMID:26527280	PBO:0102437	Fig. S3A,C
PMID:26527280	PBO:0102436	Fig. S3A,B (control for increased proteasome in nucleus)
PMID:26527280	PBO:0038176	(tetrad dioscection) Fig. 7C,E
PMID:26527280	PBO:0097773	Fig. 3A/B
PMID:26527280	PBO:0097772	Fig. 3E/F
PMID:26527280	PBO:0102434	Fig. 5C
PMID:26527280	PBO:0102434	Fig. 4D,E
PMID:26527280	PBO:0102435	Fig. 6G, S7F,G, TUBE pull-down
PMID:26527280	FYPO:0002151	Fig. 7D,E (tetrad dissection)
PMID:26527280	PBO:0038172	(tetrad disection) Fig. 7D,E
PMID:26527280	PBO:0102441	Fig. 4G,H
PMID:26527280	FYPO:0001357	Fig. 1J
PMID:26527280	PBO:0102443	(Figure S2F export of CDK1 from the nucleus, which depends on cyclin B degradation ,, was delayed
PMID:26527280	FYPO:0004705	(Figures 3B and 3D). sister chromatid separation (which depends on securin degradation, not on cyclin B degradation) was delayed as well
PMID:26527280	FYPO:0001357	Fig. 1I
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	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:0102442	In contrast, there was only a very slight delay in sister chromatid separation (Figures 2A and 2B).
PMID:26527280	PBO:0097773	Figure 2A Plo1 to SPBs persisted for more than 20 min
PMID:26527280	PBO:0097772	Fig. S2B
PMID:26527280	PBO:0102440	Fig. S6L,M
PMID:26536126	GO:0005783	grown in EMM or YES medium
PMID:26536126	FYPO:0000647	cell lysis on uracil depleted medium
PMID:26536126	FYPO:0005173	assayed_using(PomBase:fur4)
PMID:26536126	GO:0000324	nitrogen rich condition
PMID:26536126	GO:1905530	uracil uptake enhancement in pub1 deletion
PMID:26536126	FYPO:0001012	auxotrophic for cytosine, uridine and UMP
PMID:26536126	GO:0000139	nitrogen rich condition
PMID:26536126	PBO:0107662	inability to take up 14-C uracil in fur4 deletion mutant
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	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	2c
PMID:26582768	FYPO:0000089	Increased MMS sensitivity
PMID:26582768	PBO:0096037	SO:0000236 = ORF, SO:0001799=outer repeat, SO:0000186 = LTR retrotransposon
PMID:26582768	FYPO:0000089	Increased MMS sensitivity
PMID:26582768	PBO:0097889	SO:0000236 = ORF, SO:0001799=outer repeat, SO:0000186 = LTR retrotransposon
PMID:26582768	PBO:0098752	SO:0000236 = ORF, SO:0001799=outer repeat, SO:0000186 = LTR retrotransposon
PMID:26582768	PBO:0098561	SO:0000236 = ORF, SO:0001799=outer repeat, SO:0000186 = LTR retrotransposon
PMID:26652183	PBO:0097360	5 J/m2 UV; Delay is greater than rad51delta alone (see Fig. S7)
PMID:26652183	PBO:0035668	5 J/m2 UV; Fig 1A, Fig. S2
PMID:26652183	PBO:0097359	5 J/m2 UV; figure 1B, figure 3D, figure S6
PMID:26652183	PBO:0097363	2 or 5 J/m2 UV; Fig. 3F, Fig. S6
PMID:26652183	PBO:0097362	5 or 10 J/m2 UV; Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	PBO:0097363	5 J/m2 UV; Fig. 3E
PMID:26652183	PBO:0035673	5 J/m2 UV; Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	PBO:0035673	5 J/m2 UV; Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	PBO:0097363	5 J/m2 UV; Fig. 3C
PMID:26652183	PBO:0035673	5 J/m2 UV; Fig. 3B
PMID:26652183	PBO:0097364	5 J/m2 UV; Fig. 3C
PMID:26652183	PBO:0097365	2 or 5 J/m2 UV; Fig. 3F, Fig. S6
PMID:26652183	PBO:0097359	5 J/m2 UV; duration is similar to eso1-D147N alone (see Fig. 3H)
PMID:26652183	FYPO:0005625	5 or 10 J/m2 UV; Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	FYPO:0005625	5 or 10 J/m2 UV; Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	PBO:0097359	5 J/m2 UV; duration is similar to rad8delta or rhp18delta single mutants (see Fig. 3G)
PMID:26652183	PBO:0097363	5 J/m2 UV; Fig. 3D
PMID:26652183	PBO:0097360	25 J/m2 UV; delay is greater than rad51delta alone (Fig. 5A)
PMID:26652183	PBO:0097362	5 or 10 J/m2 UV; similar sensitivity to rev1delta and rev3delta single mutants (Fig. 3I, Fig. 4A, Fig. S6)
PMID:26652183	PBO:0097363	5 J/m2 UV; similar sensitivity to eso1-D147N single mutant (Fig. 3H)
PMID:26652183	PBO:0097363	5 J/m2 UV; sensitivity similar to rad8delta and rhp18delta single mutants (Fig. 3G)
PMID:26652183	PBO:0097363	5 J/m2 UV; Fig. S3
PMID:26652183	PBO:0093629	5 J/m2 UV; Sensitivity is greater than rad51delta or eso1-D147N single mutants (see Fig. S7)
PMID:26652183	PBO:0097362	5 or 10 J/m2 UV; Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	PBO:0097361	5 J/m2 UV; Fig. 1B, Fig. 3E
PMID:26652183	PBO:0097360	5 J/m2 UV; Fig. 1B
PMID:26670050	PBO:0111147	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111149	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111150	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111151	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111152	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111153	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111154	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111155	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0099655	gene locus affected: rps2202
PMID:26670050	PBO:0099656	increase > 50-fold
PMID:26670050	PBO:0099657	increase > 10-fold
PMID:26670050	PBO:0099658	increase > 10-fold
PMID:26670050	PBO:0099659	increase > 5-fold
PMID:26670050	PBO:0099660	increase > 5-fold
PMID:26670050	PBO:0099661	increase > 5-fold
PMID:26670050	PBO:0099662	increase > 5-fold
PMID:26670050	PBO:0099663	increase > 10-fold
PMID:26670050	PBO:0097114	increase > 10-fold
PMID:26670050	PBO:0099664	increase > 10-fold
PMID:26670050	PBO:0099665	increase > 10-fold
PMID:26670050	PBO:0099666	increase > 10-fold
PMID:26670050	PBO:0099667	increase > 10-fold
PMID:26670050	PBO:0099668	increase > 5-fold
PMID:26670050	PBO:0099669	increase > 5-fold
PMID:26670050	PBO:0099670	increase > 5-fold
PMID:26670050	PBO:0099671	increase > 5-fold
PMID:26670050	PBO:0099672	increase > 5-fold
PMID:26670050	PBO:0099673	increase > 5-fold
PMID:26670050	PBO:0099674	increase > 5-fold
PMID:26670050	PBO:0099675	increase > 5-fold
PMID:26670050	PBO:0099676	increase > 5-fold
PMID:26670050	PBO:0099677	increase > 5-fold
PMID:26670050	PBO:0099678	increase > 5-fold
PMID:26670050	PBO:0099679	increase > 5-fold
PMID:26670050	PBO:0099680	increase > 5-fold
PMID:26670050	PBO:0099681	increase > 5-fold
PMID:26670050	PBO:0099682	increase > 5-fold
PMID:26670050	PBO:0099683	increase > 5-fold
PMID:26670050	PBO:0099684	increase > 5-fold
PMID:26670050	PBO:0099685	increase > 5-fold
PMID:26670050	PBO:0099686	increase > 5-fold
PMID:26670050	PBO:0099687	increase > 5-fold
PMID:26670050	PBO:0099688	increase > 5-fold
PMID:26670050	PBO:0099689	increase > 5-fold
PMID:26670050	PBO:0099690	increase > 5-fold
PMID:26670050	PBO:0099691	increase > 5-fold
PMID:26670050	PBO:0111157	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111158	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111159	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111160	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111161	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111162	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111163	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111164	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111165	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111166	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111167	enrichment in CRAC > 10-fold
PMID:26670050	GO:0005515	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111169	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111170	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111143	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111142	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111141	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111140	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111139	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111138	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111137	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0099655	gene locus: rps2202
PMID:26670050	PBO:0099654	affects unspliced pre-mRNA
PMID:26670050	GO:0106222	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111135	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111134	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111171	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111172	SPCC1235.04c
PMID:26670050	PBO:0111173	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111174	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111175	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111176	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111177	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111178	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111179	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111180	enrichment in CRAC > 10-fold
PMID:26670050	GO:0106222	enrichment in CRAC > 10-fold; Mmi1 binds the 5' extended region of the overlapping regulatory lncRNA prt
PMID:26670050	PBO:0111181	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111182	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111183	SPBC1289.13c
PMID:26670050	PBO:0111184	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111185	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111186	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111187	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111188	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111189	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111190	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111191	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111192	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111193	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111194	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111195	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111196	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111197	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111198	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111199	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111200	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111201	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111202	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111203	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111204	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111360	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111361	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111207	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111208	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111209	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111210	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111211	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111212	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111213	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111214	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111215	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111216	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111217	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111218	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111219	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111220	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111221	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111222	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111223	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111224	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111225	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111226	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111227	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111228	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111229	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111230	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111055	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0099693	increase > 40-fold
PMID:26670050	PBO:0099694	increase > 10-fold
PMID:26670050	PBO:0099695	increase > 10-fold
PMID:26670050	PBO:0109063	increase > 5-fold
PMID:26670050	PBO:0099697	increase > 5-fold
PMID:26670050	PBO:0099698	increase > 5-fold
PMID:26670050	PBO:0099699	increase > 5-fold
PMID:26670050	PBO:0099700	increase > 5-fold
PMID:26670050	PBO:0099701	increase > 5-fold
PMID:26670050	PBO:0099702	increase > 5-fold
PMID:26670050	PBO:0099703	increase > 5-fold
PMID:26670050	PBO:0099704	increase > 5-fold
PMID:26670050	PBO:0099705	increase > 5-fold
PMID:26670050	PBO:0099706	increase > 5-fold
PMID:26670050	PBO:0099707	increase > 5-fold
PMID:26670050	PBO:0099708	increase > 5-fold
PMID:26670050	PBO:0099709	increase > 5-fold
PMID:26670050	PBO:0099710	increase > 5-fold
PMID:26670050	PBO:0099655	gene locus affected: dbp2
PMID:26670050	PBO:0099655	gene affected: rps2202
PMID:26670050	PBO:0099652	Fig. S4B
PMID:26670050	PBO:0099711	fig S5e
PMID:26670050	PBO:0099712	increase > 5-fold
PMID:26670050	PBO:0111326	enrichment in CRAC > 10-fold (vw changed dpp2->dbp2)
PMID:26670050	PBO:0111144	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111145	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111146	enrichment in CRAC > 10-fold
PMID:26670050	PBO:0111148	enrichment in CRAC > 10-fold
PMID:26687354	GO:0030892	(checked) Figure 1C
PMID:26687354	FYPO:0005557	(Figure 6C)
PMID:26687354	FYPO:0005556	(Figure 6A)
PMID:26687354	FYPO:0005555	(Figure 6A)
PMID:26687354	PBO:0104474	(Figure S4C)
PMID:26687354	PBO:0035230	figure 3B
PMID:26687354	FYPO:0005557	figure 3B
PMID:26687354	PBO:0034924	figure 3B
PMID:26687354	PBO:0034924	(checked) figure 3B
PMID:26687354	PBO:0034924	(checked) figure 3B
PMID:26687354	GO:0007064	(Figure 2B)
PMID:26687354	GO:0007064	(Checked) (Figure 2B) (dependent on pds5)
PMID:26687354	GO:0007064	(fig 2)
PMID:26687354	GO:0007064	(fig 2)
PMID:26687354	GO:0030892	(checked) Figure 1C
PMID:26697368	FYPO:0004490	link to GEO dataset- GSE71820
PMID:26697368	FYPO:0005301	link to GEO dataset- GSE71820
PMID:26702831	GO:0005886	2c in cos7
PMID:26730850	PBO:0109724	Figure 1D and 2D - examined via RT-PCR Figure 2A examined via RNA-Seq
PMID:26730850	FYPO:0000333	Figure 1C transient
PMID:26730850	PBO:0106551	Fig 4
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	regulation of efficiency at weak donor
PMID:26730850	FYPO:0000561	(S1 Fig)
PMID:26730850	PBO:0106553	Figure 1D
PMID:26730850	PBO:0106552	Figure 1D
PMID:26730850	PBO:0106551	Figure 4 efficiency of introns displaying weak splice sites
PMID:26730850	PBO:0106550	Figure 3+5 efficiency/ of introns displaying weak splice sites
PMID:26730850	FYPO:0000012	Figure 1A-1C transient growth arrest
PMID:26730850	PBO:0095406	Figure 1D efficiency/ of introns displaying weak splice sites
PMID:26730850	PBO:0106550	Figure 1D 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:0106550	Fig 5
PMID:26730850	PBO:0106555	Fig 5
PMID:26730850	PBO:0106551	Fig 4
PMID:26730850	PBO:0106551	Fig 4
PMID:26730850	PBO:0106551	Fig 4
PMID:26730850	PBO:0106550	Fig 3
PMID:26730850	PBO:0106550	Fig 3
PMID:26730850	PBO:0106554	Fig 3
PMID:26730850	PBO:0106554	Fig 3
PMID:26730850	PBO:0106554	Fig 3
PMID:26730850	PBO:0106554	Fig3
PMID:26730850	PBO:0106557	Fig 4
PMID:26730850	PBO:0106557	Fig 4
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:0094283	fig 3
PMID:26744419	PBO:0098769	s5a
PMID:26744419	PBO:0111257	3b
PMID:26744419	PBO:0111255	3b
PMID:26744419	PBO:0111255	3b
PMID:26744419	PBO:0111258	3b
PMID:26744419	PBO:0098772	fig 3c
PMID:26744419	PBO:0098773	fig 3c
PMID:26744419	FYPO:0006429	fig 3d
PMID:26744419	PBO:0098774	fig 4
PMID:26744419	PBO:0098775	fig 4
PMID:26744419	PBO:0098776	4e
PMID:26744419	PBO:0098776	4e
PMID:26744419	PBO:0098777	4e
PMID:26744419	GO:0005635	5
PMID:26744419	PBO:0098778	5
PMID:26744419	PBO:0098779	Fig 7b
PMID:26744419	PBO:0098780	Fig 7b
PMID:26744419	PBO:0098781	Fig 7b
PMID:26744419	PBO:0095834	fig S2
PMID:26744419	FYPO:0002360	S4
PMID:26744419	PBO:0098767	1d
PMID:26744419	PBO:0098767	1d
PMID:26744419	FYPO:0002360	1d
PMID:26744419	FYPO:0004742	1d
PMID:26744419	PBO:0097950	fig 6e
PMID:26744419	PBO:0097950	fig 6e
PMID:26744419	PBO:0095834	fig 6d
PMID:26744419	PBO:0095834	fig 6d
PMID:26744419	FYPO:0002360	fig 6d
PMID:26744419	FYPO:0003555	fig 6e
PMID:26744419	FYPO:0004924	fig 6c
PMID:26744419	PBO:0098759	fig 6c
PMID:26744419	PBO:0097950	fig 6e
PMID:26744419	PBO:0095834	fig 6d
PMID:26744419	PBO:0097950	fig 1c
PMID:26744419	PBO:0095652	fig 1c
PMID:26744419	PBO:0098758	Fig 1c SHOULD BRE ORGANIZATION
PMID:26744419	PBO:0098757	pericentric Fig 1c, In conclusion, while other tethering mechanisms in S. pombe could be functionally coupled to heterochroma- tin, the LEM-mediated centromere recruitment and the MSC-dependent silencing are independent mechanisms, although they are mediated by the same protein.
PMID:26744419	GO:0140698	Fig 1c,Fig 4e
PMID:26744419	GO:0072766	Fig 4 b & c
PMID:26744419	PBO:0098756	Fig 5c
PMID:26744419	PBO:0098755	fig 5c
PMID:26744419	PBO:0094679	fig 1c
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	7
PMID:26744419	PBO:0111257	7
PMID:26744419	PBO:0111257	7
PMID:26744419	PBO:0094681	fig 7
PMID:26744419	PBO:0093563	fig S1c
PMID:26744419	PBO:0095834	fig 1b
PMID:26744419	PBO:0093559	fig 1b
PMID:26744419	PBO:0113582	7
PMID:26744419	PBO:0094679	s10
PMID:26744419	PBO:0094679	s10
PMID:26744419	PBO:0094679	fig 1c
PMID:26744419	PBO:0094282	s10
PMID:26744419	PBO:0111257	fig 1c
PMID:26744419	PBO:0098783	Fig 5c. parent GO:0003682?
PMID:26744419	PBO:0098784	Fig 5c. parent GO:0003682?
PMID:26744419	PBO:0095834	fig S2
PMID:26744419	PBO:0095834	fig S2
PMID:26744419	FYPO:0004342	fig 1c
PMID:26744419	PBO:0098766	Fig 5b
PMID:26744419	PBO:0098766	Fig 5b
PMID:26744419	PBO:0098765	Fig 5b
PMID:26744419	PBO:0098765	Fig 5b
PMID:26744419	PBO:0098764	fig 5c
PMID:26744419	PBO:0098763	Fig 7b
PMID:26744419	PBO:0098762	Fig 7b
PMID:26744419	PBO:0098761	fig 6a (in combination with csi1∆; phenocopies lem2∆ csi1∆)
PMID:26744419	PBO:0098760	fig 3c
PMID:26744419	PBO:0096188	fig S2
PMID:26744419	PBO:0096189	fig S2
PMID:26744419	PBO:0111255	fig 1c
PMID:26744419	PBO:0111256	s2
PMID:26744419	PBO:0094679	s2
PMID:26744419	PBO:0094679	s2
PMID:26744419	PBO:0113582	fig 3
PMID:26746798	PBO:0093579	fig 1 A
PMID:26746798	PBO:0100920	fig 2 C
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 2 C
PMID:26746798	PBO:0100920	fig 2 C
PMID:26746798	PBO:0100919	fig 2 C
PMID:26746798	PBO:0100918	fig 2 C
PMID:26746798	PBO:0097986	fig 2 B
PMID:26746798	PBO:0097986	fig 2 B
PMID:26746798	PBO:0100313	fig 2 B
PMID:26746798	PBO:0093616	fig 2 A
PMID:26746798	PBO:0093618	fig 2 A
PMID:26746798	PBO:0093618	fig 2 A
PMID:26746798	PBO:0093581	fig 1 A
PMID:26746798	PBO:0093581	fig 1 A
PMID:26746798	PBO:0093579	fig 1 A
PMID:26746798	PBO:0093581	fig 1 A
PMID:26746798	PBO:0093579	fig 1 A
PMID:26746798	PBO:0093580	fig 1 A
PMID:26746798	PBO:0093580	fig 1 A
PMID:26746798	PBO:0093579	fig 1 A Defect in Checkpoint Signaling.
PMID:26749213	PBO:0035047	(Fig. 6D); evidence: filipin staining
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:0100969	moved down to new term from :protein mislocalized to cytoplasm during vegetative growth
PMID:26749213	PBO:0100970	moved down to new term from :protein mislocalized to cytoplasm during vegetative growth
PMID:26749213	PBO:0100971	figure 1a
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:0004247	fig. S2 A&B
PMID:26749213	PBO:0035060	FM4-64 uptake (I made Henars original annotation into a double mutant so the attribution has changed)
PMID:26749213	PBO:0035059	(Supporting Information Fig. S4A)
PMID:26749213	FYPO:0001235	fig 2 D
PMID:26749213	FYPO:0002061	fig 2 d
PMID:26749213	PBO:0100966	fig 7b
PMID:26749213	PBO:0098628	fig 1c
PMID:26749213	GO:0072583	moved down drom endocytosis. Delayed FM4-64 uptake when in combination with a clathrin mutationSlow dynamics of endocytic patch markers
PMID:26749213	PBO:0100976	Fig. S2C
PMID:26749213	PBO:0100968	moved down from abnormal protein localization to cell tip (new term)
PMID:26776736	PBO:0035246	important when growing on poor nitrogen sources
PMID:26776736	PBO:0095951	vw, changed to directly activates and added part_of 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. 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 sub- strates. Extracts from wild-type (ppk18+) and Myc-tagged (ppk18-13myc) Ppk18 cells, treated for 1 hr with rapamycin in or- der 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$B55 [8, 9, 27, 28, 35]. To test whether Igo1 is a direct target of Ppk18, we performed Ppk18 in vitro kinase assays using purified recombinant Igo1 and Igo1-S64A, as sub- strates. Extracts from wild-type (ppk18+) and Myc-tagged (ppk18-13myc) Ppk18 cells, treated for 1 hr with rapamycin in or- der to activate Ppk18, were immunoprecipitated with anti-c-Myc monoclonal antibodies. Ppk18-13myc immunoprecipitates were able to phosphorylate in vitro wild-type Igo1, but not Igo1-S64A Our genetic and physiological data is in agreement with published work in budding yeast, Drosophila, Xenopus, and mammalian cells indicating that greatwall phosphorylates endo- sulfine to inhibit PP2A$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 sub- strates. Extracts from wild-type (ppk18+) and Myc-tagged (ppk18-13myc) Ppk18 cells, treated for 1 hr with rapamycin in or- der 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.
PMID:26776736	GO:0035556	we need to give this a signal treansduction parentage positive regulation of G2/M transition of mitotic cell cycle involved in cellular response to nitrogen starvation
PMID:26776736	PBO:0095954	MOVE EXTENSION DOWN TO NITROGEN 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$Cyclin B (high in inter- phase and low in mitosis) [15]. To determine whether Ser64-phosphorylated Igo1 inhibits the PP2A$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, in- hibited 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:26804021	PBO:0101332	fig 3 B
PMID:26804021	PBO:0101332	fig 3 B
PMID:26804021	FYPO:0006260	fig 4
PMID:26804021	FYPO:0006260	fig 4c
PMID:26804021	FYPO:0005917	fig 5A
PMID:26804021	FYPO:0005917	fig 5 C
PMID:26804021	FYPO:0005917	fig 5A
PMID:26804021	FYPO:0005917	fig 5A
PMID:26804021	PBO:0101333	fig 5
PMID:26804021	PBO:0101333	fig 5
PMID:26804021	PBO:0101333	fig 5
PMID:26804021	PBO:0101334	fig 5
PMID:26804021	FYPO:0005758	Fig. 7a
PMID:26804021	FYPO:0006272	Fig. 7b increased occurance
PMID:26804021	PBO:0101334	fig 5
PMID:26804021	PBO:0101328	fig 4c
PMID:26804021	GO:0000775	fig 1a
PMID:26804021	PBO:0101330	fig 3 B
PMID:26804021	PBO:0101330	fig 3 D
PMID:26804021	PBO:0101331	fig S6 check allele????
PMID:26804021	PBO:0101334	fig 5
PMID:26804021	PBO:0101329	fig 1a. AND fig 4 (knob)
PMID:26804917	PBO:0102847	Serine 481 is phosphorylated by Cig2/Cdc2 during meiosis I. Phosphorylation decreases Fkh2 DNA binding affinity
PMID:26804917	PBO:0112058	EMSA fig4
PMID:26804917	PBO:0102857	EMSA fig4
PMID:2682257	PBO:0023760	Figs 1, 2, 3, 4,5 cells blocked in late G2 and in mid mitosis . I have used the term MOD00048 as I'm told that tyrosine phosphorylation is always 04' but in the paper they just show that the Y15 residue is phosphorylated
PMID:2682257	PBO:0094620	Fig6aC. Cells contain cdc2-F19 mutant on multi copy LEU2+ plasmid.
PMID:2682257	FYPO:0002085	Fig6bB. Cells contain cdc2-F19 mutant on multi copy LEU2+ plasmid.
PMID:2682257	PBO:0106437	Fig6a B. 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:0037729	Fig6b C-F. Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid.
PMID:2682257	PBO:0106436	Fig6b C-F. Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid.
PMID:2682257	PBO:0037727	Fig6b C-F. Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid.
PMID:2682257	PBO:0093712	Fig 6b C-F. Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid.
PMID:2682257	PBO:0106435	Figs 1, 2, 3, 4,5 cells blocked in late G2 and in mid mitosis . I have used the term MOD00048 as I'm told that tyrosine phosphorylation is always 04' but in the paper they just show that the Y15 residue is phosphorylated
PMID:26832414	PBO:0094283	Fig. 3B
PMID:26832414	PBO:0094283	Fig. 3B
PMID:26832414	FYPO:0006299	Fig. 4C
PMID:26832414	PBO:0112009	Fig. 4F
PMID:26832414	PBO:0112008	Fig. 4D
PMID:26832414	PBO:0108388	Fig. 4B
PMID:26832414	PBO:0104710	Fig. 4A
PMID:26869222	PBO:0037352	Cells grown at 29°C
PMID:26869222	PBO:0037351	cells grown at 29°C
PMID:26869222	PBO:0100991	cells grown at 29°C for 6 hours in 30µM Cutin-1
PMID:26869222	PBO:0037342	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:0100991	Growth was assayed in presence of 10µM Cutin-1.
PMID:26869222	PBO:0100991	assayed in presence of 30µM Cutin-1 for 6 hours 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	+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	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	cells grown at 29°C for 6 hours in 30µM Cutin-1
PMID:26869222	PBO:0100993	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	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	cells grown at 29°C for 6 hours in 30µM Cutin-1
PMID:26869222	PBO:0035594	cells grown at 29°C for 6 hours in 30µM Cutin-1
PMID:26869222	PBO:0100991	cells grown at 29°C for 6 hours in 30µM Cutin-1
PMID:26869222	PBO:0100995	Cells show partial resistance to 30µM Cutin-1 for 6 hours.
PMID:26869222	PBO:0037348	cells grown at 29°C for 6 hours in 30µM Cutin-1
PMID:26869222	PBO:0099529	cells grown at 29°C for 6 hours in 30µM Cutin-1
PMID:26877082	FYPO:0000419	Figures 1A, S1A, S1B, 1D, S1E medial ring assembly
PMID:26877082	FYPO:0002872	Figures 1A, S1A, S1B, 1D, S1E
PMID:26877082	PBO:0020891	Figures 2
PMID:26877082	PBO:0038073	Figure Figure S4C
PMID:26877082	PBO:0099935	Figure 2D (single clump!) condensation
PMID:26877082	FYPO:0000134	Figure 4A
PMID:26877082	PBO:0099935	Figure 2D (single clump!) condensation
PMID:26877082	PBO:0099936	Figure 2D abnormal cable clusering
PMID:26877082	PBO:0038070	Figures 2C
PMID:26882497	FYPO:0001687	S3
PMID:26882497	FYPO:0001687	S3
PMID:26882497	FYPO:0001687	S3
PMID:26882497	PBO:0095476	2bc,5
PMID:26882497	FYPO:0005781	2bc
PMID:26882497	FYPO:0003762	2b
PMID:26882497	FYPO:0004318	2b
PMID:26882497	PBO:0100104	text to fig2
PMID:26882497	PBO:0100105	text to fig2
PMID:26882497	GO:0007094	it looks like it is involved in MAINTAINING the checkpoint, fig S4A and 2C
PMID:26882497	GO:0007094	Fig S4A and 2C
PMID:26882497	GO:0007094	Fig S4A and 2C
PMID:26882497	PBO:0095476	2bc,5
PMID:26882497	PBO:0037610	2bc
PMID:26882497	PBO:0095474	2bc,5
PMID:26882497	PBO:0100110	4a
PMID:26882497	PBO:0100111	4a
PMID:26882497	PBO:0100111	5a
PMID:26882497	PBO:0100112	5a
PMID:26882497	PBO:0100113	5a
PMID:26882497	PBO:0100110	5a
PMID:26882497	FYPO:0005781	2bc,5
PMID:26882497	PBO:0100113	5a
PMID:26882497	PBO:0100094	1a - they don't really show that the modification is phosphorylation, but considering the rest of the data this annotation seems ok.
PMID:26882497	PBO:0109101	1b
PMID:26882497	MOD:00046	in text relevant to fig1
PMID:26882497	PBO:0100098	"they don't show the ""added during"" data so this is a bit anectdotal from the text"
PMID:26882497	PBO:0100098	"they don't show the ""added during"" data so this is a bit anectdotal from the text"
PMID:26882497	GO:1990757	3 E2s mixed in the same assay so can't specify a substrate
PMID:26882497	PBO:0100114	Fig6 they incubate with 3 different E2s so can't specify a substrate
PMID:26882497	MOD:00046	in text relevant to fig1
PMID:26882497	MOD:00046	in text relevant to fig1
PMID:26882497	PBO:0100097	"they don't show the ""added during"" data so this is a bit anectdotal from the text"
PMID:26882497	PBO:0100096	"they don't show the ""added during"" data so this is a bit anectdotal from the text"
PMID:26882497	PBO:0100096	"they don't show the ""added during"" data so this is a bit anectdotal from the text"
PMID:26882497	PBO:0100096	"they don't show the ""added during"" data so this is a bit anectdotal from the text"
PMID:26882497	PBO:0100096	"they don't show the ""added during"" data so this is a bit anectdotal from the text"
PMID:26882497	PBO:0100096	"they don't show the ""added during"" data so this is a bit anectdotal from the text"
PMID:26882497	MOD:00047	in text relevant to fig1
PMID:26882497	PBO:0100099	1b
PMID:26882497	PBO:0100100	1d
PMID:26882497	PBO:0100101	1d
PMID:26882497	PBO:0100102	1d
PMID:26882497	PBO:0100103	2a 20 mins after synchronized released into mitosis. I wouldn't want to guess exactly what stage of mitosis this is
PMID:26882497	FYPO:0000094	S3
PMID:26882497	PBO:0100112	5a
PMID:26890608	PBO:0021142	cellular response to HU = GO:0072711
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: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	"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. COUld also get 'upstream of/affects SAC"""
PMID:26912660	PBO:0097545	exists during veg growth & glucose starv & HU stress
PMID:26912660	PBO:0100552	exists during veg growth & glucose starv & HU stress
PMID:26912660	PBO:0100551	exists during veg growth & glucose starv & HU stress
PMID:26941334	GO:0110085	localization dependent on actin cytoskeleton
PMID:26942678	FYPO:0005857	some up some down
PMID:26942678	GO:1990251	Erh1 localizes with Mmi1 both during mitotic cell cycle and meiosis
PMID:26942678	FYPO:0005858	some up some down
PMID:26942678	FYPO:0000877	author statement
PMID:26960792	PBO:0108438	can't assess viability
PMID:26960792	PBO:0108232	RhoGAP, GTPase activating protein for Cdc42 and Rho2
PMID:26960792	PBO:0108437	hard to be more specific when cell shape is also abnormal (Rga6 normally goes to lateral cortex & non-growing tip)
PMID:26960792	PBO:0023536	can't assess viability
PMID:26960792	PBO:0108438	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	can't assess viability
PMID:26960792	PBO:0108438	can't assess viability
PMID:26960792	PBO:0108438	can't assess viability
PMID:26960792	PBO:0108438	can't assess viability
PMID:26990381	FYPO:0007342	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	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	FYPO:0002061	The same cells were not viable when grown in YPO (Figure S2B,C).
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: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: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	FYPO:0007342	analysis revealed that both strains had reduced whole-cell and lipid droplet TAG levels (Figure 3F,I).
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	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	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: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:0005585	analysis revealed that both strains had reduced whole-cell and lipid droplet TAG levels (Figure 3F,I).
PMID:27023709	GO:0002183	fig 2 H, cell free system
PMID:27023709	FYPO:0005387	fig. 2i
PMID:27023709	FYPO:0005387	fig. 2i
PMID:27023709	GO:0002183	fig 2 H, cell free system
PMID:27023709	GO:0002183	fig 2 H, cell free system
PMID:27023709	GO:0002183	fig 2 H, cell free system
PMID:27023709	GO:0002183	fig 2 H, cell free system
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:0032432	(Figure 3A and Supplemental Video 3).
PMID:27075176	GO:0051017	mixed orientations
PMID:27075176	PBO:0097845	(Figure 1, C and D).
PMID:27075176	PBO:0097848	6C
PMID:27075176	PBO:0097852	6C
PMID:27075176	PBO:0097850	6C
PMID:27075176	PBO:0097851	6C
PMID:27075176	PBO:0097847	6C
PMID:27075176	PBO:0097849	6C
PMID:27082518	PBO:0097577	Fig 7E
PMID:27082518	PBO:0097577	Fig 7E
PMID:27082518	PBO:0097576	Fig 7E
PMID:27082518	FYPO:0002086	fig 7D
PMID:27082518	FYPO:0002088	fig 7C/D
PMID:27082518	FYPO:0002087	fig 7C/D
PMID:27082518	FYPO:0002088	fig 7A
PMID:27082518	PBO:0097575	Fig S4F and S4G
PMID:27082518	PBO:0097581	Fig S6 C probably due to delayed fusion of TRAPP containing vesicles with PM
PMID:27082518	FYPO:0001364	fig 6 AB
PMID:27082518	PBO:0019716	fig 1 C-E
PMID:27082518	PBO:0019716	fig 1 C-E
PMID:27082518	PBO:0019716	fig 1 B
PMID:27082518	FYPO:0002088	fig 2H, 7A
PMID:27082518	PBO:0097572	Fig 3B
PMID:27082518	PBO:0097580	Fig S6 B probably due to delayed fusion of TRAPP containing vesicles with PM
PMID:27082518	FYPO:0003440	fig 6c
PMID:27082518	PBO:0097578	Fig S6A
PMID:27082518	PBO:0097574	Fig S4E
PMID:27082518	PBO:0035172	Fig 6E
PMID:27082518	PBO:0097573	Fig 3B
PMID:27082518	FYPO:0005543	Fig S 3 B
PMID:27082518	PBO:0022838	fig 5a
PMID:27082518	PBO:0035171	Fig 6E
PMID:27082518	FYPO:0002060	Fig 6E
PMID:27082518	FYPO:0002061	Figure S4D
PMID:27082518	FYPO:0001904	fig 6 AB
PMID:27082518	FYPO:0001368	fig 6 AB
PMID:27082518	FYPO:0003440	Fiig 6 AB
PMID:27082518	PBO:0097579	Fig S6A
PMID:27098497	PBO:0093617	same as rhp6delta alone
PMID:27098497	PBO:0098835	same as without exo1delta
PMID:27098497	FYPO:0002553	worse than without rqh1delta
PMID:27098497	PBO:0099553	distal to break point
PMID:27098497	PBO:0093617	same as rhp6delta alone
PMID:27098497	FYPO:0002553	same as without exo1delta
PMID:27098497	PBO:0098835	same as without exo1+ overexpression
PMID:27098497	FYPO:0002553	same as without csn1delta
PMID:27098497	PBO:0099568	same as without htb1-K119R
PMID:27098497	FYPO:0002553	same as without csn5delta
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 // I moved this to sequence specific DNA binding, appears to be author intent AL
PMID:27101289	PBO:0034987	binds with high affinity to diverged S. pombe telomeric repeats
PMID:27146110	FYPO:0006049	Figure 6
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	*****The definition of this term is not right Figure 2
PMID:27146110	FYPO:0004021	*****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: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	***DELAYED Figure 7
PMID:27146110	FYPO:0004705	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 (anaphase B)
PMID:27146110	FYPO:0003779	Figure 2
PMID:27151298	PBO:0105082	Delete K63-ubiquitin chains from 3 to 8 ubiquitins
PMID:27151298	PBO:0105079	K63-ubiquitin chain from 3 to 8 ubiquitin molecules
PMID:27151298	PBO:0108725	K63-diubiquitin chain
PMID:27151298	PBO:0105108	K63-ubiquitin chain from 3 to 8 ubiquitin molecules
PMID:27151298	PBO:0105109	K63-diubiquitin chain
PMID:27168121	FYPO:0000324	Figure 3E
PMID:27168121	GO:0005515	Fig 1 C
PMID:27168121	FYPO:0001492	Figure 3B
PMID:27168121	PBO:0018421	fig 1 b
PMID:27168121	PBO:0018576	fig 1b
PMID:27168121	FYPO:0001492	Figure 3B
PMID:27168121	FYPO:0000972	Figure 3C
PMID:27168121	FYPO:0001861	Figure 3D
PMID:27168121	FYPO:0001919	Figure 3C
PMID:27183912	PBO:0111256	can't distinguish tlh1 and tlh2 as identical sequences hence comma separated; assayed_using(PomBase:tlh1),assayed_using(PomBase:tlh2)
PMID:27183912	PBO:0113582	comma separated extension as can't distinguish transcipts (identical seq)
PMID:27188733	PBO:0099545	says increased proportion, which is a synonym
PMID:27191590	GO:0005737	Fig 1B
PMID:27191590	PBO:0108129	Fig 6B
PMID:27191590	FYPO:0005193	Fig 6C
PMID:27191590	FYPO:0005193	Fig 6C
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, Fig 4
PMID:27191590	FYPO:0001501	Fig 4E
PMID:27191590	FYPO:0001501	Fig 6C
PMID:27191590	FYPO:0005193	Fig 1C, Fig 6C, Fig 7C, Fig S5
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	FYPO:0000123	Fig 5A
PMID:27191590	FYPO:0001501	Fig 1C, Fig 4
PMID:27191590	FYPO:0001501	Fig 4D
PMID:27194449	FYPO:0003347	of human pyruvyltransferase activity for the LacNAc-pNP
PMID:27194449	FYPO:0003347	of human pyruvyltransferase activity for the LacNAc-pNP
PMID:27268234	FYPO:0003557	Fig. S6
PMID:27268234	FYPO:0007472	Fig. S6
PMID:27268234	FYPO:0008222	Fig. S5B
PMID:27268234	FYPO:0008222	Fig. S5B
PMID:27268234	PBO:0112813	Fig. 3B
PMID:27268234	FYPO:0008223	Fig. S5B
PMID:27268234	FYPO:0008224	Fig. S5B
PMID:27268234	FYPO:0003557	Fig. S6
PMID:27268234	FYPO:0007472	Fig. S6
PMID:27268234	PBO:0112814	Fig. 3A
PMID:27268234	PBO:0112815	Fig. 3B
PMID:27268234	FYPO:0008221	Fig. S5A
PMID:27268234	FYPO:0008221	Fig. S5A
PMID:27268234	PBO:0112812	Fig. 3A
PMID:27325741	FYPO:0002061	temperature permissive for ts cdc17-K42
PMID:27325741	FYPO:0002061	temperature permissive for ts cdc17-K42
PMID:27325741	FYPO:0002061	temperature permissive for ts cdc17-K42
PMID:27327046	PBO:0097059	Figures 2 and 3A, B
PMID:27327046	PBO:0097058	I changed the evidence from IDA to IMP /AL
PMID:27327046	FYPO:0001357	fig S2 & 3
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	FYPO:0001357	fig S2 & 3
PMID:27327046	FYPO:0002177	fig S2 & 3
PMID:27327046	GO:0140116	Expression of fex1 from a plasmid in fex1Del/fex2Del double deletion mutant rescues fluoride sensitivity.
PMID:27327046	PBO:0097058	I changed the evidence from IDA to IMP /AL
PMID:27327046	PBO:0097060	fig S2 & 3
PMID:27334362	PBO:0035015	fig 2a
PMID:27334362	PBO:0035014	fig 2D
PMID:27334362	PBO:0035014	(Fig. 2D) additive
PMID:27334362	FYPO:0005371	Fig. 2D
PMID:27334362	FYPO:0005371	Fig. 2D
PMID:27334362	FYPO:0002060	fig 9 D
PMID:27334362	FYPO:0002060	fig 9 D
PMID:27334362	FYPO:0001839	Fig 8B/tableB
PMID:27334362	PBO:0035021	Fig 8B/tableB
PMID:27334362	PBO:0037733	Fig 8B/tableB
PMID:27334362	FYPO:0002430	fig 9A
PMID:27334362	PBO:0105897	Fig3 D, added assayed genes, vw
PMID:27334362	FYPO:0005554	fig 3 c split into decreased at outer, abolished at inner (val)
PMID:27334362	PBO:0105898	Fig3 D, added assayed genes, vw
PMID:27334362	PBO:0105899	Fig3 D, added assayed genes, vw
PMID:27334362	FYPO:0005554	fig3 c
PMID:27334362	FYPO:0000888	fig 3 c
PMID:27334362	FYPO:0005554	fig 3 c
PMID:27334362	PBO:0037732	fig 3 c split into decreased at outer, abolished at inner (val)
PMID:27334362	FYPO:0000888	fig 3 c
PMID:27334362	FYPO:0004745	fig 3 c
PMID:27334362	FYPO:0001357	fig 6b
PMID:27334362	FYPO:0000887	fig 7 B
PMID:27334362	FYPO:0000887	fig 7 B
PMID:27334362	FYPO:0002061	fig 9D
PMID:27334362	FYPO:0002061	fig 9 D
PMID:27334362	FYPO:0000878	Fig. 3C (made this specific for inner and added decreased at outer)
PMID:27334362	GO:0061638	Fig. 3A,B changed from CENP-A containing nucleosome (val)
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:27350684	PBO:0105963	splicing of rad21, nda3 and mad2 is also affected
PMID:27350684	FYPO:0001387	conditional synthetic lethal with rna14-11
PMID:27350684	PBO:0098383	splicing of rad21, nda3 and mad2 is also affected
PMID:27350684	PBO:0105964	splicing of rad21, nda3 and mad2 is also affected
PMID:27350684	PBO:0105965	splicing of rad21, nda3 and mad2 is also affected
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: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:0110966	These results demon- strate that pFal1, Red5, and Red1 are required to generate spliced rec8+ mRNA during starvation-induced meiosis.
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:0110967	loss of mnh1 causes severe sporulation defects (Fig. 4F),
PMID:27365210	GO:0035145	We also observed interactions of pFal1-Myc with Rnps1-GFP and Y14-HA (Fig. 4B,D).
PMID:27365210	PBO:0110964	Diploid red5-2 cells show severe sporulation defects, with <1% of cells producing asci.
PMID:27365210	PBO:0110963	Diploid pfal1Δ−/− cells show a decreased sporulation efficien- cy 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: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: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	FYPO:0001355	While viable, pfal1Δ showed a strong growth defect at all three temperatures tested (Fig. 1A).
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 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	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	PBO:0110966	These results demon- strate that pFal1, Red5, and Red1 are required to generate spliced rec8+ mRNA during starvation-induced meiosis.
PMID:27365210	PBO:0110966	These results demon- strate that pFal1, Red5, and Red1 are required to generate spliced rec8+ mRNA during starvation-induced meiosis.
PMID:27365210	PBO:0110966	These results demon- strate that pFal1, Red5, and Red1 are required to generate spliced rec8+ mRNA during starvation-induced meiosis.
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:27365210	GO:0030874	S. pombe, pFal1 localizes to chromatin-contain- ing regions of the nucleus and is not restricted to the nucleolus.
PMID:27365210	GO:0000785	S. pombe, pFal1 localizes to chromatin-contain- ing 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:27385337	PBO:0096612	fig 3 C
PMID:27385337	PBO:0096603	table 1
PMID:27385337	PBO:0096605	table 1
PMID:27385337	PBO:0096603	table 1
PMID:27385337	PBO:0096603	table 1
PMID:27385337	PBO:0096604	table 1
PMID:27385337	PBO:0096603	table 1
PMID:27385337	PBO:0096604	table 1
PMID:27385337	PBO:0096603	table 1
PMID:27385337	PBO:0096602	table 1
PMID:27385337	PBO:0038155	figure 3 F
PMID:27385337	PBO:0038155	figure 3 F
PMID:27385337	PBO:0038154	figure 3 F
PMID:27385337	PBO:0038153	figure 3 F
PMID:27385337	PBO:0038152	figure 3 F
PMID:27385337	PBO:0038151	figure 3 F
PMID:27385337	PBO:0038150	Figure 3 F
PMID:27385337	PBO:0096601	fig 3 C
PMID:27385337	FYPO:0002023	figure 5 d/ figure 6
PMID:27385337	FYPO:0002023	figure 5 d/ figure 6
PMID:27385337	PBO:0096601	table 1, fig 3 C
PMID:27385337	PBO:0034985	Supplemental Figure S4F and Table 2
PMID:27385337	PBO:0096614	Supplemental Figure S4B
PMID:27385337	PBO:0096613	figure 4 G (localizes as a dot rather than a disk)
PMID:27385337	PBO:0096612	fig 3 C
PMID:27385337	PBO:0096611	figure 4 G
PMID:27385337	PBO:0096607	fig5a
PMID:27385337	PBO:0096603	Figure 4 F
PMID:27385337	PBO:0096607	fig 5 a
PMID:27385337	PBO:0096606	table 1
PMID:27385337	PBO:0095095	Figure 1F
PMID:27388936	PBO:0093560	fig 5 a
PMID:27388936	PBO:0093561	fig 5 a
PMID:27388936	PBO:0093560	fig 8a
PMID:27388936	FYPO:0005440	fig 5 b
PMID:27388936	PBO:0096314	fig 8c
PMID:27388936	PBO:0101262	fig 8c
PMID:27388936	PBO:0093561	fig 8a
PMID:27398807	PBO:0093560	30 degrees; semi-permissive for slx8-29
PMID:27398807	PBO:0093579	30 degrees; semi-permissive for slx8-29
PMID:27398807	PBO:0093580	30 degrees C
PMID:27398807	PBO:0093614	30 degrees C
PMID:27398807	PBO:0107296	30 degrees C
PMID:27398807	PBO:0099741	30 degrees C
PMID:27398807	FYPO:0001357	30 degrees; semi-permissive for slx8-29
PMID:27398807	PBO:0093561	30 degrees; semi-permissive for slx8-29
PMID:27398807	FYPO:0000963	30 degrees; semi-permissive for slx8-29
PMID:27398807	FYPO:0006822	30 degrees; semi-permissive for slx8-29
PMID:27398807	PBO:0093613	30 degrees; semi-permissive for slx8-29
PMID:27398807	FYPO:0000089	30 degrees; semi-permissive for slx8-29
PMID:27398807	FYPO:0000088	30 degrees; semi-permissive for slx8-29
PMID:27398807	FYPO:0000088	30 degrees; semi-permissive for slx8-29
PMID:27398807	FYPO:0000088	30 degrees; semi-permissive for slx8-29
PMID:27398807	PBO:0093559	30 degrees; semi-permissive for slx8-29
PMID:27398807	PBO:0093579	30 degrees; semi-permissive for slx8-29
PMID:27398807	FYPO:0001357	30 degrees; semi-permissive for slx8-29
PMID:27398807	FYPO:0000963	30 degrees; semi-permissive for slx8-29
PMID:27398807	FYPO:0001357	30 degrees; semi-permissive for slx8-29
PMID:27398807	PBO:0099747	30 degrees; semi-permissive for slx8-29
PMID:27401558	PBO:0101484	ChIP at rps2 gene
PMID:27401558	PBO:0101498	ChIP at rps2 gene
PMID:27401558	PBO:0101485	ChIP at rps2 gene
PMID:27401558	PBO:0101484	ChIP at rps2 gene
PMID:27401558	PBO:0101485	ChIP at rps2 gene
PMID:27401558	PBO:0101484	ChIP at rps2 gene
PMID:27444384	GO:0051536	through conserved cysteines
PMID:27451393	FYPO:0000877	fig 5A
PMID:27451393	PBO:0103720	DNS
PMID:27451393	FYPO:0003411	Fig. 1B, D, E
PMID:27451393	PBO:0103719	DNS
PMID:27451393	PBO:0103718	Fig. 4, A and B
PMID:27451393	FYPO:0000877	fig 5A
PMID:27451393	PBO:0112084	Fig. 5, C and D
PMID:27451393	FYPO:0004604	Fig. 3E
PMID:27451393	FYPO:0004604	Fig. 3E
PMID:27451393	GO:0099115	Fig. 3, A–D
PMID:27451393	GO:0033553	Fig. 3, A–D
PMID:27451393	GO:0061638	Fig. 2, B and C Fig. 2, D and E
PMID:27451393	GO:0061638	Fig. 2, F and G
PMID:27451393	PBO:0103721	Fig. 5, C and D
PMID:27451393	GO:0005515	Fig. 1A
PMID:27451393	GO:0005515	Fig. 1A
PMID:27451393	FYPO:0000091	Fig. G
PMID:27451393	FYPO:0000091	Fig. G
PMID:27451393	FYPO:0003411	Fig. 1B, D, E
PMID:27538348	PBO:0113957	Fig. 4D
PMID:27538348	PBO:0112527	Fig. 3C
PMID:27538348	PBO:0112528	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:0113946	Fig. 3C
PMID:27538348	PBO:0113947	Fig. 3C
PMID:27538348	PBO:0112521	Fig. 3C
PMID:27538348	PBO:0113948	Fig. 3C
PMID:27538348	PBO:0112530	Fig. 3C
PMID:27538348	PBO:0112526	Fig. 3C
PMID:27538348	PBO:0113949	Fig. 3C
PMID:27538348	PBO:0113950	Fig. 3C
PMID:27538348	PBO:0113942	Fig. 3C
PMID:27538348	PBO:0113951	Fig. 3C
PMID:27538348	PBO:0113952	Fig. 3C
PMID:27538348	PBO:0113940	Fig. 3C
PMID:27538348	PBO:0113939	Fig. 3C
PMID:27538348	PBO:0113938	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:0113945	Fig. 3C
PMID:27538348	PBO:0113953	Fig. 4B
PMID:27538348	PBO:0113954	Fig. 4B
PMID:27538348	PBO:0113955	Fig. 4B
PMID:27538348	PBO:0113931	Fig. 4C
PMID:27538348	PBO:0113929	Fig. 4C
PMID:27538348	PBO:0113930	Fig. 4C
PMID:27538348	PBO:0113956	Fig. 4C
PMID:27538348	PBO:0113955	Fig. 4D
PMID:27538348	PBO:0113958	Fig. 4D
PMID:27538348	PBO:0113953	Fig. 4D
PMID:27538348	PBO:0113954	Fig. 4D
PMID:27538348	PBO:0113955	Fig. 4D
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	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:0094691	Fig. 3A
PMID:27538348	FYPO:0004742	Fig. 2
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: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:27548313	FYPO:0000141	VW: I changed Ken-Ichi BP annotation to phenotype (Kenichi comment mitotic defects mitotic defects caused by eng1 deletion)
PMID:27548313	FYPO:0000141	VW: I changed Ken-Ichi BP annotation to phenotype (Kenichi comment mitotic defects mitotic defects caused by 343.20 deletion)
PMID:27548313	FYPO:0000141	VW: I changed Ken-Ichi BP annotation to phenotype (Kenichi comment mitotic defects mitotic defects caused by ace2 deletion)
PMID:27558664	PBO:0097286	affecting sua1 affecting cys11 affecting met14
PMID:27558664	PBO:0097287	affecting sua1 affecting cys11 affecting met14
PMID:27558664	PBO:0097286	affecting sua1 affecting cys11 affecting met14
PMID:27558664	PBO:0097285	affecting sua1 affecting cys11 affecting met14
PMID:27558664	PBO:0097287	affecting sua1 affecting cys11 affecting met14
PMID:27558664	PBO:0097285	affecting sua1 affecting cys11 affecting met14
PMID:27558664	PBO:0097285	affecting sua1 affecting cys11 affecting met14
PMID:27558664	PBO:0097286	affecting sua1 affecting cys11 affecting met14
PMID:27558664	PBO:0097287	affecting sua1 affecting cys11 affecting met14
PMID:27558664	PBO:0097288	affecting gst2
PMID:27558664	PBO:0097288	affecting gst2
PMID:27558664	PBO:0097288	affecting gst2
PMID:27558664	PBO:0113819	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	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:27587357	FYPO:0005760	Fig 3
PMID:27587357	FYPO:0003333	Fig 3
PMID:27587357	PBO:0105976	Fig 3
PMID:27587357	FYPO:0002196	Fig 3
PMID:27587357	FYPO:0002196	Fig 3
PMID:27587357	FYPO:0002196	Fig 3
PMID:27587357	FYPO:0002061	fig1
PMID:27587357	GO:0000139	deleted in error, added back
PMID:27587357	GO:0000139	deleted in error, added back
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	(vw: inferred from cell wall galactomannan defects)
PMID:27587357	FYPO:0003333	Fig 3
PMID:27587357	PBO:0105973	(vw: inferred from cell wall galactomannan defects)
PMID:27587357	FYPO:0005760	Fig 3
PMID:27587357	FYPO:0002061	Fig 3
PMID:27587357	FYPO:0003333	fig1d
PMID:27587357	FYPO:0002061	Fig 3
PMID:27587357	FYPO:0002196	Fig 3
PMID:27587357	FYPO:0006273	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	GO:0005789	deleted in error, added back
PMID:27587357	GO:0000139	deleted in error, added back
PMID:27587357	GO:0000139	deleted in error, added back
PMID:27587357	GO:0000139	deleted in error, added back
PMID:27587357	GO:0000139	deleted in error, added back
PMID:27587357	FYPO:0002482	fig1d
PMID:27611590	FYPO:0005768	assayed Cdc20 recruitment
PMID:27611590	FYPO:0005765	assayed Cdc20 recruitment
PMID:27611590	FYPO:0005766	assayed Cdc20 recruitment
PMID:27611590	FYPO:0005767	assayed Cdc20 recruitment
PMID:27613427	PBO:0093612	AA medium (Rose et al 1990 Methods in Yeast Genetics: A Laboratory Course Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.)
PMID:27613427	PBO:0094268	AA medium (Rose et al 1990 Methods in Yeast Genetics: A Laboratory Course Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.)
PMID:27618268	PBO:0104630	fig 1A
PMID:27618268	PBO:0095476	fig 1D
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	FYPO:0005781	fig 1B
PMID:27618268	FYPO:0005781	fig 1B
PMID:27618268	PBO:0104632	fig 1A
PMID:27618268	PBO:0104632	fig 1A
PMID:27618268	PBO:0104631	fig 1A
PMID:27618268	PBO:0104630	fig 1A
PMID:27618268	PBO:0104629	fig 1A
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: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:0104638	((Figure S4C)). non kinetochore bound
PMID:27618268	PBO:0101480	(Figures 4C and S4B). non kinetochore bound
PMID:27618268	PBO:0104641	(Figures 4C and S4B). non kinetochore bound
PMID:27618268	PBO:0104636	Figures 4B and S4A
PMID:27618268	PBO:0104640	Figures 4B and S4A
PMID:27618268	PBO:0101483	Figure S3E
PMID:27618268	PBO:0104640	Figure S3E
PMID:27618268	PBO:0104639	Figure S3E
PMID:27618268	PBO:0104638	fig 3C
PMID:27618268	PBO:0104637	fig 3C
PMID:27618268	PBO:0104636	fig 3C
PMID:27618268	FYPO:0000168	Figure 2D
PMID:27618268	FYPO:0000168	Figure 2E (how is this abnormal? i got confused here)
PMID:27618268	PBO:0104635	fig 2E
PMID:27618268	PBO:0095476	fig 2D
PMID:27618268	PBO:0104634	(Figure 2B)
PMID:27618268	PBO:0095476	fig 1D
PMID:27618268	PBO:0104633	(Figure 2A)
PMID:27618268	PBO:0101454	(Figure 2A)
PMID:27627185	PBO:0108748	(unphosphorylated form of tif211)
PMID:27627185	PBO:0095935	(unphosphorylated form of tif211) inhibited by stress-inducedphosphorylation of Ser51 in the a subunit of eIF2(tif211)
PMID:27630265	GO:0071341	(Figure 8A)
PMID:27630265	GO:0005085	Sec2 interacted with specifically with GTP- bound forms of Ypt3 (Figure 7, Supplemental Figure S8).
PMID:27630265	PBO:0097869	upplemental Figure S5A
PMID:27630265	PBO:0097868	Figure 6A and Supplemental Figure S3)
PMID:27630265	PBO:0097867	upplemental Figure S5A
PMID:27630265	PBO:0097866	Figure 6A and Supplemental Figure S3)
PMID:27630265	PBO:0097865	upplemental Figure S5A
PMID:27630265	PBO:0097864	Figure 5C, Supplemental Figure S4B
PMID:27630265	FYPO:0002061	Figure 1
PMID:27630265	FYPO:0002060	Figure 1
PMID:27630265	FYPO:0004609	Supplemental Figure S12
PMID:27630265	PBO:0037653	Figure 4, 5
PMID:27630265	PBO:0035494	Figure 4, 5, Supplemental Figure S4
PMID:27630265	PBO:0037651	initiation of forespore membrane delayed (Figure 3, Table 2)
PMID:27630265	PBO:0035494	Figure 8, Supplemental Figure S9
PMID:27630265	PBO:0097869	(Supplemental Figure S11B)
PMID:27630265	PBO:0097870	(Supplemental Figure S10A)
PMID:27630265	GO:0051285	(Figure 8A)
PMID:27630265	PBO:0097873	localizations at spindle poles during meiotic anaphase I (Figure 6, Supplemental Figure S6)
PMID:27630265	PBO:0097872	(Supplemental Figure S10A)
PMID:27630265	PBO:0097871	(Supplemental Figure S10A)
PMID:27630265	GO:0005628	(Figure 8A)
PMID:27630265	PBO:0037650	(Supplemental Figure S11)
PMID:27630265	PBO:0097863	Supplemental Figure S11
PMID:27630265	PBO:0037648	Supplemental Figure S11
PMID:27630265	PBO:0037641	Figure 6, Supplemental Figure S6
PMID:27630265	PBO:0097860	localizations at spindle poles during meiotic anaphase I (Figure 6, Supplemental Figure S6)
PMID:27630265	PBO:0097862	localizations at spindle poles during meiotic anaphase I (Figure 6, Supplemental Figure S3)
PMID:27630265	PBO:0097861	during meiosis (Figure 5, Supplemental Figure S4)
PMID:27630265	PBO:0097860	in sporulating cells (Figure 9, Supplemental Figure S9) (Supplemental Figure S10)
PMID:27630265	PBO:0097859	in vegetative cells (Supplemental Figure S10);
PMID:27630265	PBO:0037642	Figure 1, Supplemental Figure S1
PMID:27630265	FYPO:0002061	Figure 1
PMID:27630265	PBO:0037641	Figure 2
PMID:27630265	PBO:0025347	from metaphase II to postmeiosis (Figure 2)
PMID:27630265	GO:0032120	Figure 1 and Supplemental Figure S1
PMID:27630265	GO:0005515	Spo13 interacted with both GTP- and GDP-bound forms of Ypt3 (Figure 7, Supplemental Figure S8).
PMID:27630265	PBO:0097869	(Supplemental Figure S11B)
PMID:27630265	PBO:0097873	localizations at spindle poles during meiotic anaphase I (Figure 6, Supplemental Figure S6)
PMID:27648579	PBO:0103241	not increased (relative to wild type Hht3+/Clr4+) as with hht3-K9M alone
PMID:27648579	PBO:0103241	not increased (relative to wild type Hht3+/Clr4+) as with hht3-K9M alone
PMID:27648579	PBO:0103243	substrate: bulk histone octamers
PMID:27648579	PBO:0103234	substrate: recombinant mono-nucleosomes
PMID:27655872	PBO:0095816	Western blot analysis show Sre1 cleavage defect under low oxygen
PMID:27655872	GO:0000139	Fig 1E
PMID:27655872	PBO:0095816	"Fig 2B, lanes ""Sre1 cleavage defect under low oxygen"""
PMID:27655872	PBO:0095816	Fig 2C
PMID:27655872	PBO:0095816	Fig 2C
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 8C 8D Western blot analysis show Sre1 cleavage defect under low oxygen
PMID:27655872	FYPO:0001422	Fig 8C 8D Western blot analysis show decreased Sre1 cleavage activation under low oxygen
PMID:27655872	FYPO:0001245	Fig 2A
PMID:27655872	FYPO:0002061	Fig 2A
PMID:27655872	PBO:0094110	Fig 2A
PMID:27655872	PBO:0095816	"Fig 2B, lanes ""Sre1 cleavage defect under low oxygen"""
PMID:27655872	PBO:0103857	Fig 2B, lanes 5–13
PMID:27655872	PBO:0103858	Fig 2D, lane 3
PMID:27655872	PBO:0096888	Fig 2G, lanes 10– 12
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	PRECURSOR Figure 3 E
PMID:27655872	PBO:0110516	Fig 3E and Figure 3 D
PMID:27655872	PBO:0108957	Fig 3E and Figure 3 D
PMID:27655872	PBO:0103865	PRECURSOR Fig 5D and F (4.5 fold)
PMID:27655872	PBO:0103866	PRECURSOR Fig 5E and F
PMID:27655872	PBO:0103866	PRECURSOR Fig 5E and F
PMID:27655872	PBO:0103866	PRECURSOR Fig 5E and F
PMID:27655872	PBO:0103866	PRECURSOR Fig 5E and F
PMID:27655872	PBO:0103866	PRECURSOR Fig 5E and F
PMID:27655872	PBO:0103867	PRECURSOR Fig 5E and F
PMID:27655872	PBO:0103866	PRECURSOR Fig 5E and F
PMID:27655872	PBO:0103868	Fig 5E and F
PMID:27655872	PBO:0103869	fig 6 B
PMID:27655872	PBO:0103869	fig 6 B
PMID:27655872	PBO:0103870	fig 6 B
PMID:27655872	PBO:0103870	fig 6 B
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:27664110	FYPO:0002009	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 tempera- ture
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 tempera- ture
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 tempera- ture
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 tempera- ture
PMID:27664110	FYPO:0000256	3
PMID:27664110	FYPO:0000078	3
PMID:27664110	PBO:0100417	2
PMID:27664110	FYPO:0003810	2
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 tempera- ture
PMID:27664110	PBO:0093558	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 tempera- ture
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 tempera- ture
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 tempera- ture
PMID:27664110	FYPO:0000256	text
PMID:27664110	FYPO:0000256	text
PMID:27664110	FYPO:0000256	text
PMID:27664110	FYPO:0003004	3
PMID:27664222	PBO:0094985	Figure 3A
PMID:27664222	PBO:0094986	Figure 3A
PMID:27664222	PBO:0094987	Figure 3A
PMID:27664222	PBO:0094984	Figure 3A
PMID:27664222	PBO:0094988	Figure 3A
PMID:27664222	FYPO:0002693	Figure 2A
PMID:27664222	FYPO:0000763	Figure 2A
PMID:27664222	FYPO:0000962	Supplemen- tary Figure S3A
PMID:27664222	FYPO:0001037	Supplemen- tary Figure S3A NaCl or KCl)
PMID:27664222	FYPO:0000799	Supplementary Figure S1B
PMID:27664222	FYPO:0000096	Supplementary Figure S1B
PMID:27664222	GO:0034599	detoxification of thiol disulphide (in response to disulphide stress)
PMID:27664222	GO:0034599	detoxification of thiol disulphide (in response to disulphide stress)
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	PBO:0094995	Figure 3A
PMID:27664222	PBO:0094996	Figure 3A
PMID:27664222	PBO:0094997	Figure 3A
PMID:27664222	PBO:0094998	Figure 3A
PMID:27664222	PBO:0094999	diamide-induced promoters
PMID:27664222	GO:0005737	Figure 5A
PMID:27664222	PBO:0022693	Figure 5A
PMID:27664222	PBO:0095000	Figure 5A
PMID:27664222	GO:0006366	detoxification of thiol disulphide (in response to disulphide stress)
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	PBO:0094983	Figure 3A
PMID:27666591	PBO:0095880	Figure 5C
PMID:27666591	PBO:0093562	Figure 5C
PMID:27666591	PBO:0093564	Figure 5C
PMID:27666591	PBO:0095881	Figure 7B
PMID:27666591	PBO:0095882	7e
PMID:27666591	PBO:0095883	7F
PMID:27666591	FYPO:0000091	Figure 7C)
PMID:27666591	PBO:0095872	Figure 2A
PMID:27666591	PBO:0093564	Figures 2B and 2C
PMID:27666591	PBO:0095871	Figure 1B Figure S1F
PMID:27666591	PBO:0095877	Figure 4D
PMID:27666591	PBO:0095876	Figure S5B)
PMID:27666591	PBO:0095875	Figure 4C
PMID:27666591	FYPO:0005887	Figure 1B Figure S1F
PMID:27666591	FYPO:0002061	Figure 3A
PMID:27666591	PBO:0095874	Figures 2D and S3B
PMID:27666591	FYPO:0005887	Figure 2D
PMID:27666591	FYPO:0001234	Figures 1F and S2B
PMID:27666591	PBO:0095873	Figures S2A and S2B
PMID:27666591	FYPO:0001870	Figures S1A and S1B
PMID:27666591	PBO:0095871	Figure 1A. Figures S1C–S1E
PMID:27666591	GO:0140898	not sure if this is quite right
PMID:27666591	PBO:0095870	VW: added exists_during..
PMID:27666591	FYPO:0000228	Figure S1G
PMID:27666591	FYPO:0000091	Figure S1F
PMID:27666591	PBO:0095871	Fig- ure 7D
PMID:27666591	PBO:0095878	Figure 5A
PMID:27666591	PBO:0110819	Figure 5B
PMID:27666591	GO:0140898	Figure 5A
PMID:27687771	GO:0045944	target genes: cut6, vht1, bio2
PMID:27687866	FYPO:0000972	acetaldehyde absent
PMID:27687866	FYPO:0000972	acetaldehyde absent
PMID:27687866	FYPO:0000972	acetaldehyde absent
PMID:27697865	FYPO:0001513	Fig.
PMID:27697865	PBO:0098846	fig 6E
PMID:27697865	FYPO:0000228	6E
PMID:27697865	FYPO:0005976	fig5
PMID:27697865	FYPO:0000274	fig 5c
PMID:27697865	FYPO:0002638	(comment: vw: changed to increased activation, and D333A allele)
PMID:27697865	FYPO:0006476	Fig. S4
PMID:27697865	PBO:0098849	fig 6E
PMID:27697865	FYPO:0001355	fig6A
PMID:27697865	PBO:0098848	fig6 fig 7
PMID:27697865	FYPO:0000324	fig 5c
PMID:27697865	FYPO:0005342	fig4E
PMID:27697865	FYPO:0004438	fig4
PMID:27697865	FYPO:0004236	fig 1A
PMID:27729451	PBO:0106913	replced GO:1990601 (which acts on ss DNA)
PMID:27736299	PBO:0106440	Fig3. Nsp1 level reduced to ~45% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	PBO:0094266	Fig1. 18.92% longer than control mean
PMID:27736299	PBO:0106441	Fig3 Nup97 level reduced to ~55% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	PBO:0094266	Fig1. 16.78% longer than control mean
PMID:27736299	PBO:0094266	Fig1. 10.81% longer than control mean
PMID:27736299	PBO:0106445	Fig3. Cdr1 level reduced to ~55% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	PBO:0097393	Fig3. Ppa2 reduced to~45% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	PBO:0095712	Fig1. 9.10% shorter than control mean
PMID:27736299	PBO:0106451	Fig3. Nup189 level reduced to ~50% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	PBO:0093767	Fig1. 8.74% longer than control mean
PMID:27736299	PBO:0019143	Fig1. 31.94% longer than control mean
PMID:27736299	PBO:0094266	Fig1. 15.55% longer than control mean
PMID:27736299	PBO:0106443	Fig3. cdc25 level reduced to ~48% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	PBO:0094266	Fig1. 14.43% longer than control mean
PMID:27736299	PBO:0106444	Fig3. Cdc2 level reduced to about 48% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	PBO:0094266	Fig1. 11.63% longer than control mean
PMID:27736299	PBO:0106438	Fig3. Dea2 level reduced to 50%
PMID:27736299	PBO:0094266	Fig1. 23.46% longer than control mean
PMID:27736299	PBO:0093767	Fig1. 8.80% longer than control mean
PMID:27736299	PBO:0106439	Fig3. Nup184 level reduced to 30% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	PBO:0095711	Fig1. 16.50% shorter than control mean
PMID:27736299	PBO:0094967	Fig3 Wee1 level reduced to ~32% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	PBO:0095711	Fig1. 11.15% shorter than control mean
PMID:27736299	PBO:0106450	Fig3. Pom1 level reduced to ~55% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	PBO:0095711	Fig1. 10.86% shorter than control mean
PMID:27736299	PBO:0106449	Fig3. Suc1 level reduced to ~60% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	PBO:0094266	Fig1. 19.29% longer than control mean
PMID:27736299	PBO:0094266	Fig1. 15.82% longer than control mean
PMID:27736299	PBO:0097048	Fig3. cdc13 level reduced to ~44% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	PBO:0106448	Fig3. Cpc2 level reduced to about 55% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	PBO:0093767	Fig1. 8.78% longer than control mean
PMID:27736299	PBO:0106447	Fig3. nup45 level reduced to ~45% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	PBO:0106446	Fig3. Sal3 level reduced to ~48% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27736299	PBO:0106442	Fig3. Nup186 level reduced to ~45% decreased protein level in heterozygous diploid cell during vegetative growth
PMID:27737912	PBO:0104260	fig 6
PMID:27738016	PBO:0101388	S13; Tetrad dissection
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	PBO:0101386	G0 viability assay
PMID:27738016	PBO:0101386	G0 viability assay
PMID:27738016	FYPO:0006660	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: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; 15 ug/ml or 20 ug/ml thiabendazole
PMID:27738016	FYPO:0000069	Fig S6; 15 ug/ml or 20 ug/ml thiabendazole
PMID:27738016	FYPO:0000069	Fig S6; 15 ug/ml or 20 ug/ml thiabendazole
PMID:27738016	FYPO:0000069	Fig S6; 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:0007553	24h G0 cell microscopy
PMID:27738016	FYPO:0007553	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:0101389	S13; Tetrad dissection
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	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	G0-exit
PMID:27738016	PBO:0101396	Rad22-YFP, G0-exit
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	PBO:0098933	G0 viability assay
PMID:27738016	PBO:0098933	G0 viability assay
PMID:27738016	PBO:0098933	G0 viability assay
PMID:27738016	PBO:0098933	G0 viability assay
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	FYPO:0007553	24h G0 cell microscopy
PMID:27746023	PBO:0105074	Figures S1C and S1D
PMID:27746023	PBO:0105075	Figure 2C
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:27746023	PBO:0105075	Figure S1B
PMID:27746023	PBO:0105074	Figures 2A and S1A; Movie S1
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 S1C and S1D
PMID:27746023	FYPO:0000646	arrested
PMID:27746023	PBO:0105074	Movie S4. Sty1 activity is critical for maintaining a non-polarized Cdc42 module in N-starved quiescent cells.
PMID:27746023	PBO:0105076	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:0105074	Figure 2D
PMID:27746023	PBO:0105074	Figure 2C
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:27811944	PBO:0099388	deletion of Sre1 aa 877-900 also destabilized Sre1 and prevented proteolytic activation
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:0097767	GFP-LactC2 probe expressed from pREP3X
PMID:27852900	PBO:0019132	fig 8 a
PMID:27852900	PBO:0097762	fig 8 a
PMID:27852900	PBO:0097768	fig 4B. GFP-LactC2 probe expressed from pREP3X
PMID:27852900	PBO:0097769	GFP-LactC2 probe expressed from pREP3X
PMID:27852900	PBO:0097768	fig4 GFP-LactC2 probe expressed from pREP3X
PMID:27852900	FYPO:0004963	Figure 5D
PMID:27852900	PBO:0097763	Figure 8e
PMID:27852900	FYPO:0004964	fig8d
PMID:27852900	FYPO:0002297	fig 8d
PMID:27852900	PBO:0097771	fig 7
PMID:27852900	PBO:0097770	fig 7
PMID:27852900	FYPO:0006547	Figure 3, A and E
PMID:27852900	PBO:0097762	fig 8a
PMID:27852900	FYPO:0006547	Figure 3, A and E
PMID:27852900	PBO:0097767	fig 4 GFP-LactC2 probe expressed from pREP3X
PMID:27852900	PBO:0097769	GFP-LactC2 probe expressed from pREP3X
PMID:27852900	PBO:0097769	GFP-LactC2 probe expressed from pREP3X
PMID:27871365	GO:0006281	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	3H
PMID:27871365	GO:0003697	3H
PMID:27872152	PBO:0108496	adaptor for dis1-microtubule
PMID:27872152	FYPO:0002061	(Fig. 7B,C)
PMID:27872152	PBO:0093562	(Fig. 7D)
PMID:27872152	PBO:0093562	(Fig. 7D)
PMID:27872152	PBO:0108497	(Fig. 7E)
PMID:27872152	PBO:0108498	(comment: 2.0% versus <0.1%) (Fig. 7F)
PMID:27872152	PBO:0093562	(Fig. 7D)
PMID:27872152	GO:0005515	(Fig. 2A) (Fig. 2B; Fig. S2B).
PMID:27886462	PBO:0099519	Figure 4
PMID:27886462	PBO:0100375	Table 3
PMID:27886462	PBO:0100376	Table 3
PMID:27886462	PBO:0100377	Table 3
PMID:27886462	PBO:0100378	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:27886462	PBO:0094532	Table 2
PMID:27886462	PBO:0100379	Table 3
PMID:27886462	PBO:0100380	Table 3
PMID:27886462	PBO:0100381	Table 3
PMID:27886462	PBO:0100382	Table 3
PMID:27886462	PBO:0100383	Table 4
PMID:27886462	PBO:0100384	Table 4
PMID:27886462	PBO:0100385	Table 4
PMID:27886462	PBO:0100386	Table 4
PMID:27886462	PBO:0100387	Table 4
PMID:27886462	PBO:0094530	Table 2
PMID:27886462	PBO:0094523	Table 2
PMID:27886462	PBO:0094526	Table 2
PMID:27886462	PBO:0094527	Table 2
PMID:27886462	PBO:0094524	Table 2
PMID:27886462	FYPO:0003004	figure 3C
PMID:27886462	FYPO:0003004	figure 3C
PMID:27886462	PBO:0094194	figure 3C
PMID:27886462	FYPO:0003004	figure 3C
PMID:27886462	PBO:0109849	figure 3A
PMID:27886462	PBO:0109849	figure 3A
PMID:27886462	PBO:0109849	figure 3A
PMID:27886462	PBO:0109849	figure 3A
PMID:27886462	PBO:0100365	figure 2A
PMID:27886462	PBO:0100365	figure 2A
PMID:27886462	FYPO:0005760	Figure 1B
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:0000245	Figure 1A
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:0100373	Figure 4, Table 3
PMID:27886462	PBO:0100374	Figure 4, Table 3
PMID:27889481	FYPO:0002060	fig6
PMID:27889481	FYPO:0007486	Figure 1
PMID:27889481	FYPO:0004367	fig6
PMID:27889481	FYPO:0000737	abolished
PMID:27889481	FYPO:0004160	Figure 5C. spindle formation occurs normally at both MI and MII in sad1.2 meiosis
PMID:27889481	PBO:0098206	Figure 5B. centromeres are also released from LINC in bouquet-defective cells
PMID:27889481	PBO:0098205	fig 5.C
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:0098203	(Figure 4B)
PMID:27889481	PBO:0098202	(Figure 3DE)
PMID:27889481	PBO:0098201	fig 3DE
PMID:27889481	PBO:0098200	(Figure 3DE) At restrictive temperature, a population of sad1.2 cells emerges in which all three centromeres are clearly dissociated from the SPB
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:0098198	Figure S4B
PMID:27889481	PBO:0098197	Figure S4B
PMID:27889481	PBO:0098196	Figures 3B–C, S4A
PMID:27889481	PBO:0098195	Figures 3B–C, S4A
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: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	FYPO:0002061	fig2c
PMID:27889481	FYPO:0001234	fig2c
PMID:27889481	FYPO:0002061	fig2c
PMID:27889481	FYPO:0002060	fig2c
PMID:27889481	FYPO:0006363	Figure 1
PMID:27889481	FYPO:0005736	Figure I
PMID:27889481	FYPO:0007487	Figure 1C, I Figure 1F and 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	PBO:0098192	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	PBO:0098191	Figure 1 E 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:0098190	Figure 1 E 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:0035493	Figure 1D
PMID:27889481	PBO:0035494	Figure 1D
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:27898700	PBO:0096857	Fig 4
PMID:27898700	PBO:0096853	Fig S3B
PMID:27898700	PBO:0095928	Fig 4
PMID:27898700	PBO:0096852	Fig S3B
PMID:27898700	FYPO:0001035	Fig 2 A (3x WT)
PMID:27898700	FYPO:0005873	Fig 2 A (2x WT)
PMID:27898700	PBO:0096854	Fig 4
PMID:27898700	PBO:0096858	Fig 4
PMID:27898700	FYPO:0005872	Fig 2 A
PMID:27898700	FYPO:0005871	Fig 2 A
PMID:27898700	FYPO:0001369	fig 1FG slides along axis from midpoint
PMID:27898700	FYPO:0001365	fig 1FG
PMID:27898700	PBO:0037853	fig 1C
PMID:27898700	PBO:0037852	fig 1C
PMID:27898700	FYPO:0002423	fig 1B swollen multiseptate elongated
PMID:27898700	FYPO:0005469	fig 1A during cytokinesis
PMID:27898700	PBO:0037851	fig 1A
PMID:27898700	FYPO:0003205	Fig 2 A
PMID:27898700	PBO:0037854	fig 1C
PMID:27898700	FYPO:0001368	fig 1FG
PMID:27898700	FYPO:0004653	fig 1FG
PMID:27898700	PBO:0095928	Fig 4
PMID:27898700	PBO:0096856	Fig 4
PMID:27898700	PBO:0096854	Fig 4
PMID:27898700	PBO:0096855	Fig S4D S4E
PMID:27901072	PBO:0099059	asynchronous fig 3a
PMID:27901072	PBO:0099061	asynchronous fig 3a
PMID:27901072	PBO:0099063	asynchronous fig 3a
PMID:27901072	PBO:0099067	fig6
PMID:27901072	PBO:0099047	1d
PMID:27901072	PBO:0099048	asynchronous fig 3a
PMID:27901072	PBO:0099049	asynchronous fig 3a
PMID:27901072	PBO:0099050	asynchronous fig 3a
PMID:27901072	PBO:0099051	asynchronous fig 3a
PMID:27901072	PBO:0099052	asynchronous fig 3a
PMID:27901072	PBO:0099053	asynchronous fig 3a
PMID:27901072	PBO:0099054	asynchronous fig 3a
PMID:27901072	PBO:0099056	asynchronous fig 3a
PMID:27901072	PBO:0099057	asynchronous fig 3a
PMID:27901072	PBO:0099058	asynchronous fig 3a
PMID:27901072	PBO:0099060	asynchronous fig 3a
PMID:27901072	PBO:0099055	asynchronous fig 3a
PMID:27901072	PBO:0099056	asynchronous fig 3a
PMID:27901072	PBO:0099057	asynchronous fig 3a
PMID:27901072	PBO:0099058	asynchronous fig 3a
PMID:27901072	PBO:0099059	asynchronous fig 3a
PMID:27901072	PBO:0099060	asynchronous fig 3a
PMID:27901072	PBO:0099061	asynchronous fig 3a
PMID:27901072	PBO:0099062	asynchronous fig 3a
PMID:27901072	PBO:0099063	asynchronous fig 3a
PMID:27902423	FYPO:0002061	Promoter analysis
PMID:27902423	FYPO:0001407	Promoter analysis
PMID:27902423	FYPO:0002061	Promoter analysis
PMID:27966061	FYPO:0005886	indicates Hsf1 activation
PMID:27984744	PBO:0101377	Fig. 2E-F
PMID:27984744	FYPO:0007629	Fig. 1A
PMID:27984744	FYPO:0007629	Fig. 1B
PMID:27984744	FYPO:0007629	Fig. 1A
PMID:27984744	FYPO:0007629	Fig. 1B
PMID:27984744	FYPO:0006518	Fig. 1A
PMID:27984744	FYPO:0006518	Fig. 1A
PMID:27984744	FYPO:0006518	Fig. 1B
PMID:27984744	FYPO:0006518	Fig. 1A
PMID:27984744	FYPO:0006518	Fig. 1B
PMID:27984744	FYPO:0006518	Fig. 1B
PMID:27984744	FYPO:0006518	Fig. 1A
PMID:27984744	FYPO:0006518	Fig. 1B
PMID:27984744	FYPO:0006518	Fig. S2
PMID:27984744	PBO:0101377	Fig. 2E-F
PMID:27984744	PBO:0101377	Fig. 2E-F
PMID:27984744	PBO:0101377	Fig. 2A-B
PMID:27984744	FYPO:0004276	ChIP-seq; Fig. 1C-D
PMID:28011631	PBO:0105896	Fig. 4A,C)
PMID:28011631	FYPO:0006003	Fig. 3B normal lipid droplet localization to FSM leading edge
PMID:28011631	FYPO:0006053	Fig. 3B (also in lantrunculin treated sceels indicating actin dependeny)
PMID:28011631	FYPO:0004993	Fig. 4A
PMID:28011631	FYPO:0006054	Fig. 3B (also in lantrunculin treated sceels indicating actin dependeny)
PMID:28011631	GO:0140042	(Fig. 4B)
PMID:28011631	GO:0140042	(Fig. 4B)
PMID:28011631	FYPO:0004925	Fig. 4F Isp3-GFP was improperly assembled in the dga1Δplh1Δ mutant.
PMID:28011631	GO:0140043	Fig. 1F and Fig. 2C
PMID:28011631	GO:0140043	Fig. 1H and 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	PBO:0105893	figure S2
PMID:28011631	PBO:0105894	figure S2
PMID:28011631	FYPO:0006051	Figure S3 LP clustering at nucleus
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	GO:0019915	Fig. 4B The dga1Δplh1Δ mutant possessed few lipid droplets.
PMID:28011631	FYPO:0000808	2C
PMID:28011631	PBO:0105895	2C (also in lantrunculin treated sceels indicating actin dependeny)
PMID:28011631	FYPO:0006051	2C (also in lantrunculin treated sceels indicating actin dependeny)
PMID:28011631	FYPO:0006053	2C (also in lantrunculin treated sceels indicating actin dependeny)
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 bub3D 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:0094661	Fig. 5G, left panel
PMID:28031482	PBO:0094672	Fig 6 C
PMID:28031482	PBO:0094671	Fig 6 C
PMID:28031482	PBO:0094670	Fig 6 C
PMID:28031482	PBO:0094669	Fig 6 C
PMID:28031482	PBO:0094668	Fig 6 C
PMID:28031482	PBO:0094667	Fig 6 C
PMID:28031482	PBO:0094666	Fig 6 C
PMID:28031482	PBO:0094665	Fig 6 C
PMID:28031482	FYPO:0002061	figure 7A
PMID:28031482	PBO:0094664	Fig 6 D
PMID:28031482	PBO:0094664	Fig 6 D
PMID:28031482	PBO:0094664	Fig 6 D
PMID:28031482	PBO:0094664	Fig 6 D
PMID:28031482	PBO:0094664	Fig 6 D
PMID:28031482	PBO:0094663	Figure 6 c
PMID:28031482	PBO:0094663	Figure 6 c
PMID:28031482	PBO:0094662	Figure 6 A
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 Fig. 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 1 E
PMID:28031482	PBO:0094651	figure 1 D
PMID:28031482	PBO:0094650	figure 1 E
PMID:28031482	PBO:0094649	figure 1 E
PMID:28031482	FYPO:0001234	Fig 6 D
PMID:28031482	FYPO:0001234	Fig 6 D
PMID:28031482	FYPO:0001234	Fig 6 D
PMID:28031482	PBO:0094648	Fig 6 D
PMID:28031482	PBO:0094648	Fig 6 D
PMID:28031482	GO:0000290	pdc2 is required for mRNA decapping. Fig. 2A 2B
PMID:28031482	GO:0000932	Fig. 1D
PMID:28103117	PBO:0099452	fig3a Cdk1 consensus sites
PMID:28103117	PBO:0099453	changes in phosphorylation level Figs. 5A, B and S2)
PMID:28103117	PBO:0101618	fig 2a
PMID:28103117	PBO:0099449	fig 2a
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: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:0111515	fig 2a
PMID:28103117	PBO:0101618	fig 2a
PMID:28160081	FYPO:0000245	fig 5
PMID:28160081	FYPO:0000245	fig2A
PMID:28160081	FYPO:0000245	fig 2A
PMID:28160081	FYPO:0000245	fig 2A
PMID:28160081	FYPO:0000245	fig 2A
PMID:28160081	FYPO:0006331	fig2B
PMID:28160081	FYPO:0006331	fig2B
PMID:28160081	FYPO:0006331	fig2B
PMID:28160081	FYPO:0006333	fig2B
PMID:28160081	FYPO:0006331	fig2B
PMID:28160081	FYPO:0001309	fig 4c
PMID:28178520	PBO:0107454	(Figure 1D)
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:0107448	Figure 1B and S1B,C
PMID:28178520	PBO:0107447	Figure 1B and S1B,C
PMID:28178520	PBO:0105361	Figure 1B and S1B,C
PMID:28178520	PBO:0107446	Figure 1B and S1B,C
PMID:28178520	PBO:0022963	fig1
PMID:28178520	FYPO:0005343	FIg 3
PMID:28178520	GO:0000022	requires motor activity
PMID:28178520	PBO:0022963	Fig 1 requires Klp9, Clp1 activity
PMID:28178520	PBO:0022963	Fig 1 requires Clp1 activity
PMID:28178520	PBO:0025602	vw: moved down to nucleoplasm
PMID:28178520	PBO:0107475	(Figure S4C)
PMID:28178520	FYPO:0005684	Figure 4A
PMID:28178520	FYPO:0005684	Fig 4 A
PMID:28178520	FYPO:0005684	Fig 4 A
PMID:28178520	FYPO:0006257	Fig 4 A
PMID:28178520	FYPO:0006257	Fig 4 A
PMID:28178520	FYPO:0006257	Fig 4 A
PMID:28178520	FYPO:0005684	Fig 4 A
PMID:28178520	FYPO:0005683	Fig 4 A
PMID:28178520	FYPO:0005683	Fig 4 D
PMID:28178520	FYPO:0005683	Fig 4 D
PMID:28178520	FYPO:0006257	Fig 4 D
PMID:28178520	PBO:0107476	Figure 4E
PMID:28178520	FYPO:0004833	Fig 4 D
PMID:28178520	PBO:0107477	Figure 4E
PMID:28178520	FYPO:0005683	Fig 5
PMID:28178520	FYPO:0006475	(Figures S2B)
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:0107474	(Figure S4C)
PMID:28178520	PBO:0107469	Figure 2B
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:0107449	Figure 1B and S1B,C
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: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	FYPO:0006646	Fig 5
PMID:28178520	FYPO:0005684	Fig 5
PMID:28178520	FYPO:0006646	Fig 4 D
PMID:28178520	FYPO:0005684	Fig 4 D
PMID:28178520	FYPO:0005684	Fig 4 D
PMID:28178520	FYPO:0005684	Fig 4 A
PMID:28178520	FYPO:0006646	Fig 4 A
PMID:28178520	FYPO:0006646	Fig 4 A
PMID:28178520	FYPO:0006646	Fig 4 A
PMID:28178520	PBO:0107479	(Figure 5B)
PMID:28178520	PBO:0107478	(Figure 5B)
PMID:28178520	FYPO:0006257	Fig 5
PMID:28191457	PBO:0107139	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:28191457	PBO:0107140	Phenotype is inherited in non-Mendelian manner, via protein aggregates (prion-like).
PMID:28193844	GO:0140357	6a
PMID:28193844	FYPO:0006890	9
PMID:28193844	PBO:0094472	8b
PMID:28193844	GO:0000329	fig4
PMID:28193844	MOD:00171	they show it is GPI anchored, the specified residue is predicted
PMID:28193844	GO:0015886	6
PMID:28193844	GO:0000324	fig4
PMID:28202541	PBO:0106195	Ost1-mCherry, mCherry antibody
PMID:28202541	PBO:0106191	Scp1-13xMyc used for Scp1, pulled on Myc
PMID:28202541	FYPO:0002448	pulled on Dsc2
PMID:28202541	PBO:0106192	Anp1-GFP mislocalized from Golgi puncta to ER and vacuole
PMID:28202541	PBO:0106193	Ost1-mCherry increased signal in ER
PMID:28202541	PBO:0106194	Anp1-GFP degradation as assayed by appearance of free GFP
PMID:28202541	PBO:0106196	improved relative to WT Sre1
PMID:28218250	FYPO:0005952	ChIP-seq
PMID:28218250	PBO:0096563	ChIP-seq
PMID:28218250	PBO:0096564	ChIP-seq
PMID:28218250	FYPO:0005950	ChIP-seq
PMID:28218250	PBO:0096564	ChIP-seq; same severity as spt16-1 alone
PMID:28218250	FYPO:0005950	ChIP-seq
PMID:28218250	FYPO:0005951	ChIP-seq
PMID:28218250	PBO:0096565	ChIP-seq
PMID:28218250	PBO:0096563	ChIP-seq
PMID:28218250	PBO:0096565	ChIP-seq
PMID:28218250	FYPO:0005950	ChIP-seq
PMID:28218250	PBO:0096562	ChIP-seq
PMID:28218250	PBO:0096562	ChIP-seq
PMID:28218250	PBO:0096562	ChIP-seq
PMID:28218250	PBO:0096562	ChIP-seq
PMID:28218250	PBO:0096562	ChIP-seq
PMID:28218250	PBO:0096562	ChIP-seq
PMID:28218250	PBO:0096563	ChIP-seq
PMID:28242692	FYPO:0002085	Fig. 1B, supp table S1
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: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:0002085	Fig. 1B, supp table S1
PMID:28242692	FYPO:0001420	Fig. 1C
PMID:28242692	PBO:0097302	Fig 1C
PMID:28242692	PBO:0097302	Fig 1C
PMID:28242692	PBO:0097302	Fig 1C
PMID:28242692	PBO:0097024	Fig S1AB
PMID:28242692	PBO:0097300	Fig. 1 D–F
PMID:28242692	FYPO:0000772	severe leaking; Fig. 3B, arrow; Fig. 3 C and D, quantifi- cation, figure 4 B
PMID:28242692	FYPO:0001733	Fig. 2B)
PMID:28242692	PBO:0097301	Fig 1A
PMID:28242692	FYPO:0001513	rescue
PMID:28242692	PBO:0097303	Fig S1C
PMID:28242692	PBO:0097303	Fig S1C
PMID:28242692	FYPO:0006019	4B, arrowheads, and Fig. 5B
PMID:28242692	PBO:0097304	partial leaking; Fig. 3B, arrow; Fig. 3 C and D, quantifi- cation
PMID:28242692	PBO:0097304	partial leaking; Fig. 3B, arrow; Fig. 3 C and D, quantifi- cation
PMID:28242692	PBO:0097304	partial leaking; Fig. 3B, arrow; Fig. 3 C and D, quantifi- cation
PMID:28242692	PBO:0097305	cells with abnormal NE morphology at the beginning of the exper- iment, 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	FYPO:0003973	and the NPCs that were present were localized to re- gions that were largely free of karmellae and tubulo-vesicular structures (Fig. 4D).
PMID:28264193	PBO:0100360	Supp
PMID:28264193	PBO:0100361	Supp2
PMID:28264193	PBO:0100361	Supp2
PMID:28264193	PBO:0100361	Supp2
PMID:28264193	PBO:0100361	Supp2
PMID:28264193	PBO:0114477	fig5 fusion mutant not currently capturable
PMID:28264193	PBO:0100361	Supp2
PMID:2827111	FYPO:0001234	table 1
PMID:2827111	FYPO:0002061	table 1
PMID:2827111	GO:0003917	fig 7 B
PMID:2827111	FYPO:0002061	table1
PMID:2827111	FYPO:0002061	table1
PMID:28281664	PBO:0103670	figure 1c & d
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	FYPO:0001122	figure 1b divides longer than WT in the same conditions
PMID:28281664	PBO:0100665	figure 1D
PMID:28281664	PBO:0103667	Figure 2
PMID:28281664	PBO:0103667	Figure 2.
PMID:28281664	PBO:0103671	Figure 2
PMID:28281664	PBO:0093605	Figure 3.
PMID:28281664	PBO:0096662	Figure 3.
PMID:28281664	PBO:0097116	Figure 3.
PMID:28281664	PBO:0103672	Figure 3.
PMID:28281664	PBO:0103674	Figure 1
PMID:28281664	PBO:0095677	Figure 1D
PMID:28281664	PBO:0103675	Figure 2
PMID:28281664	PBO:0093606	Figure 2
PMID:28281664	PBO:0103675	Figure 2
PMID:28281664	PBO:0103676	Figure 2
PMID:28281664	PBO:0095677	Figure 3.
PMID:28281664	PBO:0093578	Figure 3.
PMID:28281664	FYPO:0001122	Figure 3.
PMID:28281664	PBO:0103678	Figure 3.
PMID:28282432	PBO:0114465	Fig. 4
PMID:28282432	FYPO:0006974	Fig. 4
PMID:28282432	FYPO:0006974	Fig. 4
PMID:28282432	FYPO:0006974	Fig. 4
PMID:28282432	FYPO:0004695	Fig. 5
PMID:28282432	FYPO:0004695	Fig. 5
PMID:28282432	FYPO:0008288	Fig. 5
PMID:28282432	FYPO:0005663	Fig. 2
PMID:28282432	FYPO:0005663	Fig. 2
PMID:28282432	FYPO:0008288	Fig. 5
PMID:28282432	PBO:0098222	Fig. 4
PMID:28282432	PBO:0114464	Fig. 4
PMID:28282432	PBO:0114465	Fig. 4
PMID:28292899	PBO:0100311	Fig. 4 D–F
PMID:28292899	GO:0005546	Fig 2 & Fig. 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:28292899	FYPO:0000927	Fig. 7
PMID:28292899	PBO:0100312	Fig. 6
PMID:28292899	FYPO:0003835	Fig. 5B
PMID:28292899	FYPO:0003835	Fig. 5B
PMID:28292899	FYPO:0002674	Fig. 5B A(ALSO FOR THE myo-1TH3 domain deletion(need genotype description)
PMID:28292899	PBO:0100311	Fig. 5B
PMID:28334955	PBO:0096226	Fig 1 A
PMID:28334955	PBO:0093796	Fig 1 A
PMID:28334955	PBO:0093793	Fig 1 A
PMID:28334955	FYPO:0003335	Supplementary Figure S3B (abolished by galactose addition)
PMID:28334955	FYPO:0002106	S3
PMID:28334955	PBO:0096234	Figure 8B,8C
PMID:28334955	PBO:0096233	Figure 8B,8C
PMID:28334955	PBO:0096232	Figure 8B,8C (barely detectable level )
PMID:28334955	PBO:0096244	figure 8 A
PMID:28334955	PBO:0096229	fig 1B inferred from
PMID:28334955	FYPO:0004153	Supplementary Figure S7
PMID:28334955	PBO:0093605	Fig 7 c
PMID:28334955	PBO:0096227	fig 7 B
PMID:28334955	PBO:0096226	Fig 7 A
PMID:28334955	FYPO:0002380	S3
PMID:28334955	PBO:0096231	S3
PMID:28334955	PBO:0096232	Figure 2B (barely detectable level )
PMID:28334955	PBO:0096233	Figure 2B
PMID:28334955	PBO:0096234	Figure 2B
PMID:28334955	PBO:0096235	Figure 2B, 8B,8C
PMID:28334955	FYPO:0002582	Figure 2C
PMID:28334955	GO:0005759	figure 6 c
PMID:28334955	GO:0005759	figure 6 c
PMID:28334955	PBO:0096238	figure 9 F
PMID:28334955	PBO:0096237	figure 9 F
PMID:28334955	PBO:0096240	figure 9 F
PMID:28334955	PBO:0096239	figure 9 F
PMID:28334955	PBO:0096238	figure 9 F
PMID:28334955	PBO:0096237	figure 9 F
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:0096248	figure 9 d
PMID:28334955	PBO:0096247	figure Supp S8
PMID:28334955	PBO:0096246	fig 9C
PMID:28334955	PBO:0096245	figure 9A
PMID:28334955	PBO:0096241	figure 8 D
PMID:28334955	PBO:0096240	figure 8 D
PMID:28334955	PBO:0096239	figure 8 D
PMID:28334955	PBO:0096238	figure 8 D
PMID:28334955	PBO:0096237	figure 8 D
PMID:28334955	PBO:0096236	figure 8 D
PMID:28334955	FYPO:0004153	Supplementary Figure S3B
PMID:28334955	PBO:0096239	figure 9 F
PMID:28334955	PBO:0096240	figure 9 F
PMID:28334955	GO:0005739	figure 6 a
PMID:28334955	GO:0005739	figure 6 a
PMID:28334955	PBO:0093796	Fig 7 A
PMID:28334955	PBO:0093605	Fig 1 E/F
PMID:28334955	PBO:0093793	Fig 1 C
PMID:28334955	PBO:0093796	Fig 1 C
PMID:28334955	PBO:0096229	fig 1B inferred from
PMID:28334955	PBO:0096228	fig 1B
PMID:28334955	PBO:0096227	fig 1B
PMID:28334955	PBO:0096227	fig 1B
PMID:28338873	GO:0051017	assayed in vitro
PMID:28338873	FYPO:0006026	assayed in vitro
PMID:28343969	PBO:0098608	figure 1 E
PMID:28343969	PBO:0109337	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	PBO:0093562	Fig 4f
PMID:28343969	PBO:0093557	Fig 4f
PMID:28343969	PBO:0098606	Fig 1B
PMID:28343969	PBO:0098605	Fig S2A, S2C
PMID:28343969	PBO:0098604	Fig 4F, 4H
PMID:28343969	PBO:0098612	"Fig 2C (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 2AB
PMID:28343969	PBO:0098611	Fig 2AB
PMID:28343969	PBO:0098610	Fig 2 B
PMID:28343969	PBO:0098610	Fig 2 B
PMID:28343969	PBO:0098609	Fig 2AB
PMID:28343969	PBO:0098616	fig S4B
PMID:28343969	PBO:0098615	Fig 2 F
PMID:28343969	FYPO:0006521	S4A
PMID:28343969	PBO:0098613	Fig 2F
PMID:28343969	PBO:0093558	Fig 4f
PMID:28343969	FYPO:0002061	Fig S4A
PMID:28343969	PBO:0095072	Fig 4G
PMID:28343969	PBO:0098603	Fig 2C, 2D, 2G
PMID:28343969	PBO:0095072	Fig 4G
PMID:28343969	PBO:0098612	"Fig 2C 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.)"" has_penetrance high , assayed_using ark1"
PMID:28343969	PBO:0098614	Fig 2E
PMID:28343969	PBO:0098614	Fig 2E
PMID:28343969	PBO:0093564	Fig 4f
PMID:28343969	PBO:0098613	Fig 2F
PMID:28343969	FYPO:0006521	S4A
PMID:28343969	PBO:0098617	fig 4b
PMID:28343969	PBO:0098617	fig 4b
PMID:28343969	FYPO:0002061	4C
PMID:28343969	FYPO:0002061	4C
PMID:28343969	PBO:0098618	Fig 4E
PMID:28343969	PBO:0098618	Fig 4E
PMID:28343969	PBO:0098604	Fig 4H
PMID:28343969	PBO:0098609	Fig 2AB
PMID:28343969	PBO:0098602	Fig 2C, 2D, 2G
PMID:28343969	PBO:0022253	(Figures S4D and S4E
PMID:28343969	PBO:0022253	(Figures S4D and S4E
PMID:28343969	PBO:0098619	Fig S4A
PMID:28343969	PBO:0098619	Fig S4A
PMID:28343969	PBO:0098620	(Figures S4D and S4E
PMID:28343969	PBO:0098620	(Figures S4D and S4E
PMID:28343969	PBO:0098619	Fig S4A
PMID:28343969	FYPO:0002060	Fig S4A
PMID:28345447	FYPO:0002865	restored by depletion of ammonium
PMID:28345447	FYPO:0002865	restored by depletion of ammonium
PMID:28345447	FYPO:0002865	restored by depletion of ammonium
PMID:28345447	FYPO:0002865	restored by depletion of ammonium
PMID:28345447	FYPO:0002865	restored by depletion of ammonium
PMID:28366743	PBO:0096933	Figure S3B
PMID:28366743	PBO:0096934	Figure S3B
PMID:28366743	PBO:0096935	Figure S3B
PMID:28366743	PBO:0095476	Fig. 2C/D, S2B,
PMID:28366743	PBO:0096922	figur 3A
PMID:28366743	PBO:0096929	Fig. 1C synchronous mitotic cells
PMID:28366743	PBO:0096928	synchronous mitotic cells fig 1c
PMID:28366743	FYPO:0004318	Fig 1B
PMID:28366743	FYPO:0003762	Fig. 2C/D, S2B,
PMID:28366743	FYPO:0004367	Fig. 4A
PMID:28366743	PBO:0095475	fig 4A
PMID:28366743	PBO:0096926	Fig. 4C
PMID:28366743	PBO:0096927	Fig. 4C
PMID:28366743	PBO:0096926	Fig. 4C
PMID:28366743	PBO:0096921	Fig 4D
PMID:28366743	PBO:0096925	Fig. 3B
PMID:28366743	PBO:0096924	Fig. 3B
PMID:28366743	PBO:0095476	Fig S1G
PMID:28366743	PBO:0095476	Fig 1B
PMID:28366743	PBO:0095475	Fig1b
PMID:28366743	PBO:0095474	Fig1B
PMID:28366743	PBO:0095474	Fig 1B
PMID:28366743	PBO:0095474	Fig 1B
PMID:28366743	PBO:0096925	Fig. 3 A/B present in interphase
PMID:28366743	PBO:0096924	Fig. 3 A/B present in interphase cells
PMID:28366743	PBO:0096923	fig 3a
PMID:28366743	PBO:0096922	fig 3.a
PMID:28366743	PBO:0096921	Figure 4D
PMID:28366743	PBO:0096920	Figure 4D
PMID:28366743	PBO:0095475	Figures 1FandS1H).
PMID:28366743	PBO:0096921	figure 4D. s
PMID:28366743	PBO:0096930	Figure S1e
PMID:28366743	PBO:0096931	Fig S3B
PMID:28366743	PBO:0096932	Figure S3B
PMID:28366743	PBO:0096932	Figure S3B
PMID:28366743	FYPO:0004318	(Figure 1F
PMID:28366743	FYPO:0004318	supp S1h
PMID:28366743	PBO:0096926	figure 4C. synchronous mitotic cells
PMID:28366743	PBO:0096923	figur 3A
PMID:28366743	PBO:0096933	Figure S3B
PMID:28366744	FYPO:0004318	Fig 1 A (checkpoint assay)
PMID:28366744	PBO:0105660	fig 2a
PMID:28366744	PBO:0095469	fig 2a
PMID:28366744	FYPO:0007173	fig 1 c
PMID:28366744	PBO:0105659	fig 2a
PMID:28366744	PBO:0105658	fig S1
PMID:28366744	FYPO:0005783	fig 1 c
PMID:28366744	FYPO:0005783	fig 1 c
PMID:28366744	FYPO:0004318	Fig 1 A (checkpoint assay)
PMID:28366744	FYPO:0004318	Fig 1 A (checkpoint assay)
PMID:28366744	PBO:0095469	fig 2a
PMID:28366744	FYPO:0004318	Fig 1 A (checkpoint assay)
PMID:28366744	FYPO:0004318	Fig 1 A (checkpoint assay)
PMID:28366744	PBO:0105657	"vw changed term from ""reduced ubiquitin ligase activity"""
PMID:28366744	FYPO:0005727	vw; I changed the genotype here
PMID:28366744	FYPO:0004318	vw I changed the genotype/ Fig 1 A (checkpoint assay)
PMID:28366744	GO:0031145	Required for mitotic checkpoint complex binding to the anaphase promoting complex.
PMID:28366744	GO:0031145	Deletion increases levels of mitotic checkpoint complex associated with the anaphase promoting complex in mitosis.
PMID:28366744	PBO:0105665	(Figure 3B).
PMID:28366744	PBO:0105663	(Figure 3A).
PMID:28366744	PBO:0105664	Figure 3A
PMID:28366744	PBO:0105663	(Figure 3A).
PMID:28366744	PBO:0105662	(Figure 3B).
PMID:28366744	PBO:0105661	Figures 3A and 3B
PMID:28366744	PBO:0095924	figure 2b
PMID:28367989	PBO:0111620	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	fig4
PMID:28377506	FYPO:0000726	fig4D
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	fig4
PMID:2837764	GO:0005786	assayed using mammalian proteins
PMID:28388826	FYPO:0006566	data not shown
PMID:28388826	FYPO:0006566	data not shown
PMID:28404620	FYPO:0006109	sequencing of Ago1-bound siRNA
PMID:28404620	PBO:0097039	also uses Pol ii-RNA immunoprecipitation
PMID:28404620	PBO:0111231	uses histone H3 RNA immunoprecipitation
PMID:28404620	FYPO:0006109	sequencing of Ago1-bound siRNA
PMID:28404620	FYPO:0006109	sequencing of Ago1-bound siRNA
PMID:28404620	FYPO:0006109	sequencing of Ago1-bound siRNA
PMID:28404620	FYPO:0002827	uses Pol ii-RNA immunoprecipitation
PMID:28404620	PBO:0097041	also uses Pol ii-RNA immunoprecipitation
PMID:28404620	PBO:0097042	uses Pol ii-RNA immunoprecipitation
PMID:28404620	FYPO:0006109	sequencing of Ago1-bound siRNA
PMID:28404620	FYPO:0006110	sequencing of Ago1-bound siRNA
PMID:28404620	FYPO:0006109	sequencing of Ago1-bound siRNA
PMID:28410370	PBO:0105712	wider localization at the shmoo tip
PMID:28410370	FYPO:0004806	Strong phenotype in crosses with fus1∆.
PMID:28410370	PBO:0102727	more severe phenotype when crossed to fus1delta
PMID:28410370	PBO:0102726	more severe phenotype when crossed to fus1∆
PMID:28410370	PBO:0102726	phenotype more severe when crossed to fus1∆
PMID:28410370	PBO:0105710	Wider localization at shmoo tip
PMID:28410370	PBO:0102726	stronger phenotype when crossed to fus1∆
PMID:28410370	FYPO:0006108	wider distribution along shmoo tip
PMID:28410370	PBO:0105710	wider localization
PMID:28410370	PBO:0105712	wider localization
PMID:28410370	PBO:0105713	wider localization
PMID:28410370	PBO:0105710	wider localization
PMID:28410370	PBO:0105710	wider localization
PMID:28432181	PBO:0100750	snRNA/ complementation of yeast pus1
PMID:28438891	PBO:0096226	Fig 1C
PMID:28438891	PBO:0099134	Fig 3C
PMID:28438891	PBO:0095073	Fig 3C
PMID:28438891	PBO:0095073	Fig 3C
PMID:28438891	PBO:0099135	Fig 3C
PMID:28438891	FYPO:0001357	fig 4
PMID:28438891	GO:0005515	fig 7
PMID:28438891	FYPO:0002061	Fig 1C
PMID:28438891	FYPO:0002061	Figure 5 B (exacerbates )
PMID:28438891	FYPO:0001357	Fig 1C
PMID:28438891	FYPO:0002060	Fig 4E
PMID:28438891	GO:0000785	Fig EV5
PMID:28438891	MOD:00046	Fig 3C
PMID:28438891	FYPO:0002061	Fig 1C
PMID:28438891	PBO:0096226	Fig 1C
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	PBO:0096226	Fig 1C
PMID:28438891	GO:0045875	type 2 cohesion (still bound) MITOTIC
PMID:28438891	FYPO:0002061	Fig 1C
PMID:28438891	PBO:0099133	type 2 cohesion (still bound)
PMID:28438891	PBO:0099132	required for Rad21 dephosphorylation
PMID:28438891	FYPO:0002060	Fig 5A
PMID:28438891	FYPO:0001357	Fig 1C
PMID:28438891	FYPO:0001357	Fig 1C
PMID:28438891	FYPO:0001357	Fig 1D
PMID:28438891	GO:0045875	MIOTOTIC
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. (I use 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. (I use txn rather than RNA level because we know it is transcription)
PMID:28469148	PBO:0102473	ade6 arg1
PMID:28469148	PBO:0102481	ura1 met5
PMID:28469148	PBO:0102480	lys3 ura1
PMID:28469148	PBO:0102481	ura1 met5
PMID:28469148	PBO:0102480	lys3 ura1
PMID:28469148	PBO:0102481	ura1 met5
PMID:28469148	PBO:0102480	lys3 ura1
PMID:28469148	PBO:0102481	ura1 met5
PMID:28469148	PBO:0102480	lys3 ura1
PMID:28469148	PBO:0102481	ura1 met5
PMID:28469148	PBO:0102479	lys3 ura1
PMID:28469148	PBO:0102480	lys3 ura1
PMID:28475874	FYPO:0004251	in response to a single blocked replisome
PMID:28475874	FYPO:0003589	in response to a single blocked replisome
PMID:28475874	FYPO:0006086	in response to a single blocked replisome
PMID:28475874	FYPO:0003589	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:28475874	FYPO:0005236	in response to a single blocked replisome
PMID:28475874	FYPO:0003589	in response to a single blocked replisome
PMID:28476936	FYPO:0007786	Fig 5 supplements added
PMID:28476936	PBO:0098323	Fig5 supplements added
PMID:28476936	FYPO:0007786	FigS5 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	FigS5 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	FigS5 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. no supplements added
PMID:28476936	PBO:0098322	Fig4D no supplements added
PMID:28476936	FYPO:0007787	Fig4A, C, E, F no supplements added
PMID:28476936	FYPO:0007786	Fig 2
PMID:28476936	FYPO:0007786	Fig 2
PMID:28476936	FYPO:0007786	Fig 2
PMID:28476936	FYPO:0007786	Fig 2
PMID:28476936	FYPO:0007786	Fig 2
PMID:28476936	FYPO:0007786	Fig 2
PMID:28476936	FYPO:0007786	Fig 2
PMID:28476936	FYPO:0007785	Fig S1A, Fig1B,C
PMID:28476936	FYPO:0007786	Fig 2, Fig3, Fig4B
PMID:28476936	FYPO:0007786	Fig 5 supplements added
PMID:28476936	FYPO:0007786	Fig 5 supplements added
PMID:28476936	FYPO:0007786	Fig 5 supplements added
PMID:28476936	FYPO:0007786	Fig 5 supplements added
PMID:28476936	FYPO:0007786	Fig 5 supplements added
PMID:28476936	FYPO:0007786	Fig 5 supplements added
PMID:28476936	FYPO:0007786	Fig 5 supplements added
PMID:28476936	FYPO:0007786	Fig 5 supplements added
PMID:28476936	PBO:0098321	Fig S1A, Fig1
PMID:28476936	FYPO:0007786	Fig 5 supplements added
PMID:28476936	FYPO:0007786	Fig 5 supplements added
PMID:28476936	FYPO:0007786	Fig 5 supplements added
PMID:28479325	PBO:0092427	mRNA quantitation was obtained by Nanostring experiments.
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:0001124	normal cell size. homeostasis
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:28479325	PBO:0097937	arelatively constant concentration during G2, as previously observed [2mRNA quantitation was obtained by Nanostring experiments.
PMID:28479325	PBO:0097937	mRNA quantitation was obtained by Nanostring experiments.
PMID:28479325	PBO:0092427	During G2, the concentration of Cdc25 increases about 2 fold (Figure 1A)
PMID:28481910	FYPO:0006031	BrdU incorporation
PMID:28481910	FYPO:0003923	BrdU incorporation
PMID:28481910	FYPO:0006031	BrdU incorporation
PMID:28481910	PBO:0093559	same as cdc20-M10 alone
PMID:28481910	FYPO:0005108	BrdU incorporation
PMID:28497540	GO:1990813	fig 1 B
PMID:28497540	PBO:0095110	mph1Δ cells (Fig. 2B)
PMID:28497540	PBO:0095111	mph1Δ cells (Fig. 2B)
PMID:28497540	PBO:0095112	S4
PMID:28497540	PBO:0095111	fig S2A
PMID:28497540	FYPO:0003606	(Fig. 2B)
PMID:28497540	FYPO:0003606	`s4
PMID:28497540	PBO:0112491	fig 5
PMID:28497540	PBO:0095120	4B
PMID:28497540	PBO:0095113	Fig 3C
PMID:28497540	PBO:0095113	Fig 3C
PMID:28497540	PBO:0095114	during interphase (not usually located then)
PMID:28497540	PBO:0112491	fig 1C
PMID:28497540	PBO:0095101	fig 4A
PMID:28497540	PBO:0095115	fig 4A
PMID:28497540	FYPO:0006423	fig 1B
PMID:28497540	PBO:0112490	fig 1B, 1D
PMID:28497540	PBO:0109670	fig 1B
PMID:28497540	PBO:0095101	fig 2b
PMID:28497540	PBO:0095100	Fig 2b
PMID:28497540	PBO:0109341	recruits
PMID:28497540	PBO:0109340	Fig. 3A,B
PMID:28497540	PBO:0109339	RECRUITS
PMID:28497540	PBO:0112490	fig 5
PMID:28497540	PBO:0109340	Fig. E
PMID:28497540	PBO:0095110	Fig. S5
PMID:28497540	PBO:0095117	Fig. S5
PMID:28497540	PBO:0112495	fig 5
PMID:28497540	PBO:0095118	Fig. 5C
PMID:28497540	PBO:0095119	Fig. 5C
PMID:28497540	PBO:0112491	fig 5C
PMID:28497540	PBO:0112492	fig 1D
PMID:28497540	PBO:0112493	fig 1E
PMID:28497540	FYPO:0006424	fig 1C
PMID:28497540	PBO:0112494	fig 1F
PMID:28497540	GO:1990813	fig 1 EF
PMID:28497540	PBO:0109676	fig 1B
PMID:28497540	PBO:0112495	fig 1F
PMID:28513584	FYPO:0000324	Fig. 2
PMID:28513584	PBO:0097932	Fig. 1
PMID:28513584	FYPO:0004085	Fig. 1
PMID:28513584	FYPO:0000276	Fig. S1
PMID:28513584	FYPO:0001574	Fig. S1 Not really abnormal, should be just bipolar
PMID:28513584	FYPO:0000049	Fig. 2
PMID:28513584	FYPO:0006174	Fig. 2
PMID:28513584	FYPO:0001053	Fig. 2 (main text)
PMID:28513584	FYPO:0004395	Fig. 2
PMID:28513584	FYPO:0005342	Fig. 2
PMID:28513584	FYPO:0000049	Main text (Figure S2 seems wrongly labelled)
PMID:28513584	FYPO:0004395	Fig. 2
PMID:28513584	FYPO:0000049	Fig. 3
PMID:28513584	PBO:0103044	Fig. 3
PMID:28513584	PBO:0103045	Fig. 3
PMID:28513584	PBO:0103046	Fig. 3
PMID:28513584	PBO:0103047	Fig. 3
PMID:28513584	FYPO:0005343	Fig. S4
PMID:28513584	FYPO:0002085	Fig. S4
PMID:28513584	FYPO:0000049	Fig. S3E
PMID:28513584	PBO:0103048	Fig. S3D and the fact that is required for bipolar spindle formation
PMID:28513584	GO:0061804	cut7D pkl1D ase1D lethal
PMID:28513584	GO:0061804	cut7D pkl1D cls1off lethal
PMID:28513584	GO:0061805	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:28515144	PBO:0096808	Reduced ssp2-T189 phosphorylation under osmotic stress
PMID:28515144	PBO:0096809	Abolished 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: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: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.
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	see comment on cid14
PMID:28545058	FYPO:0006926	Fig1D
PMID:28545058	FYPO:0006926	Fig1D
PMID:28545058	FYPO:0006926	Fig1D
PMID:28545058	FYPO:0006926	Fig1D
PMID:28545058	FYPO:0006926	Fig1D
PMID:28545058	FYPO:0001221	Fig1D
PMID:28545058	FYPO:0001221	Fig1D
PMID:28545058	FYPO:0001221	Fig1D
PMID:28545058	FYPO:0001221	Fig1D
PMID:28545058	FYPO:0001221	Fig1D
PMID:28545058	FYPO:0001221	Fig1 D
PMID:28545058	FYPO:0006926	Fig1A,B
PMID:28545058	FYPO:0006926	Fig1A,B
PMID:28545058	FYPO:0006926	Fig1A,B
PMID:28545058	FYPO:0006926	Fig1A,B
PMID:28545058	FYPO:0006926	Fig1A,B
PMID:28545058	FYPO:0006926	Fig1A,B
PMID:28545058	FYPO:0006926	Fig1A,B
PMID:28545058	FYPO:0006926	Fig1A,B
PMID:28545058	FYPO:0006926	Fig1A,B
PMID:28545058	FYPO:0006926	Fig1A,B
PMID:28545058	FYPO:0000836	Fig3B 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:0000836	Fig3A,B
PMID:28545058	PBO:0097188	Fig2A
PMID:28545058	PBO:0097190	FigS1C,D
PMID:28545058	PBO:0097189	Fig2 A,B
PMID:28545058	PBO:0097188	Fig2 A,B
PMID:28545058	FYPO:0000769	Fig1C
PMID:28545058	FYPO:0000769	Fig1C
PMID:28545058	FYPO:0001221	Fig2A, B
PMID:28545058	FYPO:0003286	Fig3A
PMID:28545058	FYPO:0000911	Table S5
PMID:28545058	PBO:0097188	Fig2A
PMID:28545058	PBO:0097188	Fig2A
PMID:28545058	FYPO:0001221	Fig 2A
PMID:28545058	FYPO:0001221	Fig4 A,B
PMID:28545058	FYPO:0001673	Fig4 A,B
PMID:28545058	FYPO:0006926	Fig1A,B
PMID:28545058	FYPO:0006926	Fig1A,B
PMID:28545058	FYPO:0006926	Fig1A,B
PMID:28545058	FYPO:0006926	Fig1A,B
PMID:28545058	FYPO:0001221	Fig 4A
PMID:28545058	PBO:0097188	Fig 4C,D
PMID:28545058	PBO:0097191	Fig 4c
PMID:28545058	PBO:0097191	Fig4C 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:0002061	data not shown
PMID:28545058	FYPO:0006926	Fig1D
PMID:28545058	FYPO:0006926	Fig1D
PMID:28545058	FYPO:0006926	Fig1D
PMID:28552615	FYPO:0002775	(Fig. S1C)
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	GO:0003918	Figure 3F and G
PMID:28552615	PBO:0098740	(Fig. S1C, 3A)
PMID:28552615	PBO:0098739	(Fig. 3a)
PMID:28552615	PBO:0098737	(Fig. 2i)
PMID:28552615	PBO:0098735	(Fig. 2h)
PMID:28552615	PBO:0098736	(Fig. 2h)
PMID:28552615	PBO:0098735	(Fig. 2h)
PMID:28552615	GO:0005515	Figure S2E
PMID:28552615	PBO:0098733	(Fig. S1E)
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:28552615	FYPO:0002775	(Fig. S1C)
PMID:28552615	FYPO:0002775	(Fig. S1C)
PMID:28552615	FYPO:0000969	(Fig. S1B)
PMID:28552615	FYPO:0000963	(Fig. S1B)
PMID:28552615	FYPO:0001690	(Fig. S1B)
PMID:28552615	FYPO:0000957	(Fig. S1B)
PMID:28572514	GO:0005628	fig 6
PMID:28572514	PBO:0019744	fig 6
PMID:28572514	PBO:0107770	Fig. 7
PMID:28572514	PBO:0107770	Fig. 7
PMID:28572514	PBO:0105204	Fig. 7
PMID:28572514	PBO:0107768	(comment: vw: changed to match previous session terms RNA ...from cuf1􏰀 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:0107769	Fig. 9
PMID:28572514	PBO:0107770	Fig. 7
PMID:28572514	GO:0005886	fig5
PMID:28572514	PBO:0107767	(comment: vw: changed to match previous session terms RNA ...from cuf1􏰀 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:0107766	(comment: vw: changed to match previous session terms RNA ...from cuf1􏰀 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 4C; decreased frequency of gene conversions at direct repeat recombination reporter
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:28586299	FYPO:0006920	Figure 4B; decreased frequency of deletions 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:28600551	FYPO:0004765	fig 4
PMID:28600551	FYPO:0006714	fig 5
PMID:28600551	FYPO:0006714	fig 5
PMID:28600551	FYPO:0006714	fig 5
PMID:28600551	FYPO:0003743	fig 1 - They say they use YES in methods and fig2
PMID:28600551	FYPO:0003743	fig 1 - They say they use YES in methods and fig2
PMID:28600551	PBO:0103776	fig 1 - They say they use YES in methods and fig2
PMID:28600551	PBO:0103790	fig 5
PMID:28600551	FYPO:0006713	fig 5
PMID:28600551	FYPO:0006713	fig 5
PMID:28600551	PBO:0103789	fig 5
PMID:28600551	FYPO:0000584	fig 5
PMID:28600551	FYPO:0000584	fig 5
PMID:28600551	FYPO:0000584	fig 5
PMID:28600551	FYPO:0006712	fig 5
PMID:28600551	FYPO:0006712	fig 5
PMID:28600551	PBO:0100647	fig 5
PMID:28600551	FYPO:0000303	fig 5
PMID:28600551	FYPO:0000303	fig 5
PMID:28600551	PBO:0103788	fig 5
PMID:28600551	PBO:0103787	fig 5
PMID:28600551	PBO:0101662	fig 5
PMID:28600551	PBO:0101662	fig 5
PMID:28600551	PBO:0103778	fig 4
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	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 - They say they use YES in methods and fig2
PMID:28600551	FYPO:0003743	fig 1 - 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	FYPO:0005968	fig 1
PMID:28600551	FYPO:0005968	fig 1
PMID:28600551	FYPO:0005968	I can never remember why e.g. sodium chloride isn't a child to salt stress
PMID:28600551	FYPO:0000852	fig 1 c
PMID:28600551	FYPO:0000852	fig 1 - They say they use YES in methods and fig2
PMID:28600551	FYPO:0000852	fig 1 - They say they use YES in methods and fig2
PMID:28600551	FYPO:0003743	fig 1 - They say they use YES in methods and fig2
PMID:28600551	FYPO:0003743	fig 1 - They say they use YES in methods and fig2
PMID:28600551	FYPO:0003743	fig 1 - They say they use YES in methods and fig2
PMID:28619713	PBO:0103586	fig 6 C
PMID:28619713	FYPO:0001791	fig 6 C
PMID:28619713	GO:0061496	Fig. S1 B
PMID:28619713	GO:0140480	rename 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 inser- tion before the cell even enters mitosis.fig6
PMID:28619713	GO:0061496	Fig. S1 B
PMID:28619713	GO:0140480	Our data suggest that Sad1 is present at the SPB early to set up structures that will trigger SPB inser- tion before the cell even enters mitosis.fig6
PMID:28631612	PBO:0092298	"""antidote"" product of longer alternative transcript; assayed by expressing S.k. ortholog in S.p."
PMID:28631612	GO:0072324	"""poison"" product of shorter alternative transcript;assayed by expressing S.k. ortholog in S.p."
PMID:28640807	FYPO:0003238	2 mM Glutathione restores aerobic growth.
PMID:28640807	PBO:0097692	2 mM Glutathione restores aerobic growth.
PMID:28640807	PBO:0093559	aerobic conditions
PMID:28640807	PBO:0093560	aerobic conditions
PMID:28640807	PBO:0093559	aerobic conditions
PMID:28640807	PBO:0093560	aerobic conditions
PMID:28640807	PBO:0093560	aerobic conditions
PMID:28640807	PBO:0093560	aerobic conditions
PMID:28640807	PBO:0093560	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: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	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	PBO:0105841	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	PBO:0097080	ditto
PMID:28652406	PBO:0097079	ditto
PMID:28652406	PBO:0105842	Atf1 is constitutively bound to srx1 and ctt1 in strain trr1....
PMID:28652406	PBO:0105838	....whereas it is never recruited to these promoters in cells expressing Pap1.C523D (Fig. 5D).
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:0105836	ditto
PMID:28652406	FYPO:0000087	ditto
PMID:28652406	PBO:0100901	ditto
PMID:28652406	PBO:0094384	ditto
PMID:28652406	PBO:0105837	Atf1.7M-HA are constitutively bound to the gpd1 and hsp9 promoters both before and after stress
PMID:28652406	PBO:0105837	ditto
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	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 pcr1 cells, with the only exception of srx1
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	FYPO:0000087	the HA-Atf1.1M mutant was fully able to suppress the sensitivity to peroxides of strain atf1, expression of the HA-Atf1.10M and 11M mutants did not alleviate this phenotype (supplemental Fig. S1C).
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:0000962	expression of HA-Atf1.10D fully suppressed all stress defects of cells lacking Sty1 (Fig. 2C).
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	FYPO:0000962	vw, I deleted Caludias annotation by mistake when comparing to the older partially completed session by Laura, so adding back !
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:0105834	whereas the expression of all stress genes in cells expressing HAAtf1.10D was not altered by sty1 deletion. Concomitantly
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	FYPO:0001485	the HA-Atf1.1M mutant was fully able to suppress the sensitivity to peroxides of strain atf1, expression of the HA-Atf1.10M and 11M mutants did not alleviate this phenotype (supplemental Fig. S1C).
PMID:28652406	FYPO:0000087	the HA-Atf1.1M mutant was fully able to suppress the sensitivity to peroxides of strain atf1, expression of the HA-Atf1.10M and 11M mutants did not alleviate this phenotype (supplemental Fig. S1C).
PMID:28652406	FYPO:0000087	atf1 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:0000962	Concomitantly, although expression of HA-Atf1.10M was not able to suppress the sensitivity to peroxides of strain atf1 (supplemental Fig. S1C and Fig. 1G), expression of HAAtf1.10D alleviated this phenotype (Fig. 1G).
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: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: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: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: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:0001357	figure 5 b
PMID:28656962	FYPO:0001357	figure 5 b
PMID:28656962	FYPO:0001357	figure 5 b
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	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	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: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	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:28659415	GO:0036286	Pil1p form filaments. Pil1 exchanges rapidly at the ends of these filaments in vivo.
PMID:28659415	GO:0070941	Pil1p form filaments. Pil1 exchanges rapidly at the ends of these filaments in vivo.
PMID:28667014	FYPO:0006131	LC-MS/MS
PMID:28667014	FYPO:0006131	idn1Δ loz1Δ – enhances gluconate accumulation when compared to idn1Δ cells LC-MS/MS and enzymatic assays were used to measure gluconate accumulation in wild-type, idn1Δ
PMID:28667014	FYPO:0006131	LC-MS/MS and enzymatic assays were used to measure gluconate accumulation in wild-type and idn1Δ
PMID:28674280	PBO:0103012	same as snf22delta alone
PMID:28674280	PBO:0103012	same as snf22delta alone
PMID:28674280	PBO:0103012	same as snf22delta alone
PMID:28765164	PBO:0099881	fig2e
PMID:28765280	PBO:0095311	Fig. 1EF
PMID:28765280	FYPO:0002060	figure 1D
PMID:28765280	PBO:0095316	Fig. 7A
PMID:28765280	PBO:0095316	Fig. 7A
PMID:28765280	FYPO:0002060	Fig 7A
PMID:28765280	FYPO:0002060	Fig 7A
PMID:28765280	PBO:0095314	(Fig. 6G).
PMID:28765280	PBO:0095315	6 ef
PMID:28765280	PBO:0095314	Fig 6C
PMID:28765280	FYPO:0000673	Fig 6C
PMID:28765280	FYPO:0002060	Fig 6A
PMID:28765280	PBO:0095313	3b
PMID:28765280	PBO:0095312	3b
PMID:28765280	FYPO:0000673	Fig 1B
PMID:28765280	FYPO:0002060	Fig 2A
PMID:28765280	FYPO:0002060	Fig 1B
PMID:28765280	FYPO:0002061	figure 1B
PMID:28765280	FYPO:0002060	Fig 1A
PMID:28765280	PBO:0038207	figure 2
PMID:28765280	PBO:0095310	we could probly go to increased degradation because of the bortezombin exp
PMID:28771613	PBO:0108424	unfortunately no direct binding data, but physical interactions have been shown in other organisms
PMID:28771613	PBO:0108419	1E
PMID:28771613	PBO:0108418	2B
PMID:28771613	PBO:0108417	1E
PMID:28771613	PBO:0108420	1E
PMID:28771613	PBO:0108423	The preRC- loading delay was abolished in the irradiated gcn1Δ cells (Fig 3C),
PMID:28771613	PBO:0108423	The preRC- loading delay was abolished in the irradiated gcn1Δ cells (Fig 3C),
PMID:28775153	FYPO:0000229	Fig4D. DAPI staining. 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	Fig4B. DAPI staining. 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	Fig4C. DAPI staining. 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	FYPO:0000339	Figure 1A
PMID:28784611	FYPO:0002061	Fig. S1, C and D)
PMID:28784611	PBO:0102560	Figure 1C
PMID:28784611	FYPO:0002061	Fig. S1, C and D)
PMID:28784611	FYPO:0006005	fig 5 B CR slid- ing events no longer occurred in myo51Δ efr3Δ
PMID:28784611	FYPO:0002253	fig S2C
PMID:28784611	FYPO:0002253	fig 5A
PMID:28784611	FYPO:0004293	fig 1 A&B
PMID:28784611	GO:0005886	Figure 1B
PMID:28784611	PBO:0098958	Figure 3E
PMID:28784611	PBO:0102556	Figure 3C
PMID:28784611	GO:0007009	phospholipid biosynthesis?
PMID:28784611	PBO:0102559	Figure 1C
PMID:28784611	PBO:0102562	Fig 2 A-C
PMID:28784611	PBO:0102561	Fig 2 A-C
PMID:28784611	PBO:0098955	Figure 3B
PMID:28784611	FYPO:0006005	fig 5 B CR slid- ing events no longer occurred in myo51Δ efr3Δ
PMID:28784611	FYPO:0002061	Fig. S2 D
PMID:28784611	PBO:0102564	Fig 2 A-C
PMID:28784611	FYPO:0002061	Figure S1C
PMID:28784611	PBO:0102558	Figure S2E
PMID:28784611	FYPO:0005020	Figure S2A-B
PMID:28784611	FYPO:0001489	Figure S1D
PMID:28784611	PBO:0102557	Figure 3D
PMID:28784611	FYPO:0005905	Figure S2A-B
PMID:28784611	GO:1903475	naintenence
PMID:28784611	PBO:0102565	Fig 3 A (in table, data not shown)
PMID:28784611	FYPO:0003278	"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:28806726	FYPO:0006242	replication forks stall with partial dependence on intra-S checkpoint (fig. 6)
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:0003923	untreated (table S1)
PMID:28806726	FYPO:0006240	replication forks slow independently of intra-S checkpoint (fig. 6)
PMID:28806726	FYPO:0006241	inhibition of origin firing requires intra-S checkpoint (fig. 5)
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:28811350	PBO:0096422	consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA
PMID:28811350	PBO:0096423	consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA
PMID:28811350	PBO:0096420	consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA
PMID:28811350	PBO:0096424	consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated by MMS mutagenesis
PMID:28821619	FYPO:0001245	generated from MMS mutagenesis
PMID:28825727	FYPO:0006248	hic and 3C pcr fig 2d increased mitotic intra centromere connection
PMID:28825727	FYPO:0000214	hi C????? Supplementary Figs. 1b,f and 4a–c
PMID:28825727	FYPO:0006302	fig 2b hi-C difference assay
PMID:28825727	FYPO:0006302	(vw made more specific) Hi-C Supplementary Figs. 1b,f and 4a–c
PMID:28825727	FYPO:0000214	Supplementary Figs. 1b,f and 4a–c Cnd3 depletion following promoter shut-off and auxin-induced degron activation
PMID:28825727	FYPO:0000214	Cnd3 depletion following promoter shut-off and auxin-induced degron activation
PMID:28825727	FYPO:0006302	Cnd3 depletion following promoter shut-off and auxin-induced degron activation
PMID:28825727	FYPO:0006302	fig 3 hi-C
PMID:28827290	FYPO:0002061	fig 3
PMID:28827290	FYPO:0002061	fig 3
PMID:28827290	PBO:0101837	fig 2D
PMID:28827290	PBO:0101836	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	FYPO:0002061	fig 3
PMID:28827290	FYPO:0002060	fig 4
PMID:28827290	FYPO:0002060	fig 4
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:0002061	fig 3
PMID:28827290	FYPO:0002061	fig 3
PMID:28827290	FYPO:0002061	fig 3
PMID:28827290	FYPO:0002061	fig 3
PMID:28827290	FYPO:0002060	fig 4
PMID:28827290	FYPO:0001355	fig 5
PMID:28827290	FYPO:0001355	fig 5
PMID:28827290	PBO:0094438	fig 5
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	FYPO:0001357	fig 6
PMID:28827290	PBO:0101838	fig 7
PMID:28827290	FYPO:0001357	fig 8
PMID:28841135	PBO:0108111	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	30 degrees
PMID:28904333	PBO:0100463	25 degrees
PMID:28904333	FYPO:0006843	especially at centromere; also at other regions where Ino80 complex normally binds
PMID:28914606	GO:0009898	Furthermore, the FRET signal of mCherry-Cdc15 with two other F-BAR domains (GFP-Imp2 and GFP-Rga7) indicates that all three cytokinesis F-BARs are packed in close proximity upon the membrane
PMID:28914606	GO:0009898	Furthermore, the FRET signal of mCherry-Cdc15 with two other F-BAR domains (GFP-Imp2 and GFP-Rga7) indicates that all three cytokinesis F-BARs are packed in close proximity upon the membrane
PMID:28914606	GO:0009898	A strong FRET signal between mCherry-Cdc15 and Acyl-GFP is consistent with the binding of Cdc15’s F-BAR to anionic phospholipids within the plasma membrane
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	Cdr2 does not exit nodes (unlike Cdr1) upon osmotic stress
PMID:28924043	PBO:0107341	Cdr1-K41A remains unphosphorylated; Cdr1+ not tagged
PMID:28934464	GO:0003714	5D a bit tenuous but we don't have this annotated..
PMID:28934464	GO:0140585	I replaced GO:0090579 dsDNA loop formation as per https://github.com/geneontology/go-annotation/issues/3610
PMID:28934464	PBO:0107974	fig 3D
PMID:28934464	PBO:0107975	fig 3E
PMID:28934464	PBO:0107976	fig 3E
PMID:28934464	GO:0003714	5D a bit tenuous but we don't have this annotated..
PMID:28934464	PBO:0107969	fig S2D
PMID:28934464	PBO:0107969	fig 3B
PMID:28934464	PBO:0107969	fig 3B
PMID:28934464	PBO:0107970	fig 3C
PMID:28934464	PBO:0107971	fig 3C
PMID:28934464	PBO:0107970	fig 3C
PMID:28934464	PBO:0107972	fig 3C
PMID:28934464	PBO:0107973	fig 3D
PMID:28944093	FYPO:0000271	can't disambiguate salt from specific calcium sensitivity in these experiments
PMID:28944093	FYPO:0000271	can't disambiguate salt from specific calcium sensitivity in these experiments
PMID:28944093	FYPO:0000098	can't disambiguate salt from specific calcium sensitivity in these experiments
PMID:28944093	FYPO:0000098	can't disambiguate salt from specific calcium sensitivity in these experiments
PMID:28947618	PBO:0106832	Fig 2A &B
PMID:28947618	FYPO:0003244	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:0045292	Intron-Specific pre-mRNA Splicing
PMID:28947618	PBO:0106840	Fig 8B in spliceosome
PMID:28947618	PBO:0106839	(Fig 7A)
PMID:28947618	PBO:0106838	(Fig 7A)
PMID:28947618	PBO:0106837	(Fig 7A)
PMID:28947618	GO:0005681	Fig 4A
PMID:28947618	PBO:0106836	Fig 3E LysSde2-C (pro-obo/term-requests/119/), is N-end rule substrate
PMID:28947618	PBO:0106835	Fig 3E (N-end rule pathway substrate) assayed_using(LysSde2-C)
PMID:28947618	PBO:0106834	Fig 2D
PMID:28947618	PBO:0106834	Fig 2D
PMID:28947618	PBO:0106833	Appendix Fig S2A
PMID:28947618	PBO:0106832	fig 1B
PMID:28947618	PBO:0106832	fig 1B
PMID:28947618	FYPO:0003244	assayed_using SPBC1778.02 | assayed_using SPAC227.16C | assayed_using SPBP16F5.02
PMID:28947618	PBO:0106831	(endo) mutant does not cleave Sde2 precursor
PMID:28947618	PBO:0106830	(endo) mutant does not cleave Sde2 precursor
PMID:28947618	PBO:0109713	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109712	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109711	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109710	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109709	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109708	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109707	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109706	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109705	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109704	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109703	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109702	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109701	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109700	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109699	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109698	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109697	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109696	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109695	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109694	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109693	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109692	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109691	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109690	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109689	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109688	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109687	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109686	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109685	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109684	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109683	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109682	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109681	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109680	Fig 5B; Appendix Fig S5A and B
PMID:28947618	PBO:0109679	Fig 5B; Appendix Fig S5A and B
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	FYPO:0001357	Fig EV2B normal processing, complements sde2Δ
PMID:28947618	FYPO:0001357	Fig EV2B normal processing, complements sde2Δ
PMID:28947618	FYPO:0001355	processing defective, does not complement sde2Δ
PMID:28947618	FYPO:0001355	reduced 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	normal processing, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, protein very stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, protein stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, protein unstable,complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, protein very stable, complements partially sde2Δ
PMID:28947618	FYPO:0001575	processing defective, does not complement sde2Δ
PMID:28947618	FYPO:0001355	normal processing, 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, protein very stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, protein stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, protein very stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, protein stable, complements partially 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 very stable, does not complement sde2Δ
PMID:28947618	FYPO:0001355	fig 1 D complements partially sde2Δ
PMID:28947618	FYPO:0001575	fig 1 D does not complement sde2Δ
PMID:28947618	FYPO:0001355	processing defective, does not complement sde2Δ
PMID:28947618	FYPO:0001355	normal processing, complements partially sde2Δ
PMID:28947618	FYPO:0001355	normal processing, protein very stable, complements partially sde2Δ
PMID:28947618	FYPO:0003244	does not complement sde2Δ, defective in telomeric silencing and genome stability
PMID:28947618	PBO:0109678	decreased cell population growth at high temperature
PMID:28947618	GO:0045292	Intron-Specific pre-mRNA Splicing
PMID:28947618	GO:0005634	column_17 Sde2UBL
PMID:28974540	PBO:0104458	fig 5 D-G nuclear envelope
PMID:28974540	PBO:0104459	fig 5 D-G 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	FYPO:0002061	fig 2E
PMID:28974540	FYPO:0002061	fig 2E
PMID:28974540	FYPO:0002061	fig 2E
PMID:28974540	FYPO:0002061	fig 2E
PMID:28974540	FYPO:0002061	fig 2E
PMID:28974540	FYPO:0002061	fig 2E
PMID:28974540	GO:0005635	5A
PMID:28974540	FYPO:0000227	fig1
PMID:28974540	FYPO:0000324	Fig. S2 B
PMID:28974540	PBO:0104441	fig 1b
PMID:28974540	FYPO:0002638	Fig. S3
PMID:28974540	PBO:0104442	added affected genes as extensions fig 3 A-C
PMID:28974540	PBO:0104443	added affected genes as extensions fig 3 A-C
PMID:28974540	PBO:0104444	added affected genes as extensions fig 3 A-C
PMID:28974540	PBO:0104445	added affected genes as extensions fig 3 A-C
PMID:28974540	PBO:0104446	added affected genes as extensions fig 3 A-C
PMID:28974540	PBO:0104447	added affected genes as extensions fig 3 A-C
PMID:28974540	PBO:0104448	added affected genes as extensions fig 3 A-C
PMID:28974540	PBO:0104449	added affected genes as extensions fig 3 A-C
PMID:28974540	PBO:0033477	Fig. S2 A & 1E
PMID:28974540	FYPO:0002649	vw: moved down to elongated (update fypo?) fig 1e
PMID:28974540	GO:0017056	fig 1a + others
PMID:28974540	FYPO:0000284	fig 1C
PMID:28974540	PBO:0104450	fig 1
PMID:28974540	PBO:0104451	fig S2
PMID:28974540	PBO:0104452	s3 C
PMID:28974540	PBO:0100719	s3 E
PMID:28974540	FYPO:0002061	fig 2E
PMID:28974540	PBO:0095380	Fig. S3, G and H
PMID:28974540	PBO:0104453	Fig. S3 I additive, do we know %?
PMID:28974540	PBO:0099862	added affected genes as extensions fig 3 E
PMID:28974540	PBO:0104454	added affected genes as extensions fig 3 E
PMID:28974540	FYPO:0003094	fig 3
PMID:28974540	FYPO:0006353	fig 3
PMID:28974540	FYPO:0004314	fig 3 G
PMID:28974540	PBO:0104446	fig 4a
PMID:28974540	PBO:0104455	fig 4c
PMID:28974540	PBO:0104446	fig 4e
PMID:28974540	MOD:01148	(Fig. 4 G and see the Ubiquitin pull-down section of Materials and methods).
PMID:28974540	GO:0005635	5A
PMID:28974540	PBO:0104456	fig 5b nuclear envelope
PMID:28974540	PBO:0104457	fig 5b
PMID:28976798	GO:0005515	fig1
PMID:28976798	GO:0005515	fig1
PMID:28976798	PBO:0099345	fig 1 D
PMID:28976798	GO:0005515	fig1
PMID:28976798	GO:0005515	fig1
PMID:28977643	GO:0045003	mhf1-L78R
PMID:28977649	PBO:0107497	Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU
PMID:28977649	PBO:0107498	Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU
PMID:28977649	PBO:0107499	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	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	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:0107495	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	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	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	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	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:0107504	tRNA-Ser GCU and tRNA-Ser AGA unaffected
PMID:28977649	PBO:0107505	tRNA-Ser GCU and tRNA-Ser AGA unaffected
PMID:28977649	PBO:0107506	tRNA-Ser GCU and tRNA-Ser AGA unaffected
PMID:28977649	PBO:0107509	tRNA-Ser GCU and tRNA-Ser AGA unaffected
PMID:28977649	PBO:0107508	tRNA-Ser GCU and tRNA-Ser AGA unaffected
PMID:28977649	PBO:0107507	tRNA-Ser GCU and tRNA-Ser AGA unaffected
PMID:28977649	PBO:0107495	Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU
PMID:28977649	PBO:0107496	Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU
PMID:28982178	FYPO:0000249	40 fold less
PMID:29021344	FYPO:0005343	Figure 2G
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 4B
PMID:29021344	FYPO:0002061	Figure 4A and Supplemental Figure S4
PMID:29021344	PBO:0095235	Figure S5D
PMID:29021344	PBO:0095235	Figure S5D
PMID:29021344	FYPO:0003241	fig3C
PMID:29021344	PBO:0095234	Figure 2E
PMID:29021344	FYPO:0002060	(Supplemental Figure S1A).
PMID:29021344	FYPO:0005343	Figure 1F
PMID:29032152	FYPO:0001357	fig 3b
PMID:29032152	PBO:0101316	Table 3
PMID:29032152	PBO:0101316	Table 3
PMID:29032152	PBO:0101316	Table 3
PMID:29032152	PBO:0101317	Table 3
PMID:29032152	PBO:0101316	Table 3
PMID:29032152	PBO:0101314	fig 4
PMID:29032152	PBO:0101314	fig 4
PMID:29032152	FYPO:0001689	fig 3e
PMID:29032152	FYPO:0000969	fig 3e
PMID:29032152	FYPO:0001689	fig 2
PMID:29032152	PBO:0101315	inferred from combined experiments
PMID:29032152	PBO:0101314	fig 4
PMID:29032152	PBO:0095685	fig 3b
PMID:29032152	PBO:0095685	fig 3b
PMID:29032152	GO:0005515	fig4
PMID:29032152	FYPO:0000957	fig 3e
PMID:29032152	FYPO:0001234	fig 1
PMID:29032152	FYPO:0002550	fig2
PMID:29032152	FYPO:0000089	fig2 b,c
PMID:29032152	FYPO:0001021	fig 2a
PMID:29032152	FYPO:0001926	fig 2
PMID:29032152	PBO:0094648	fig 1, 3b
PMID:29032152	PBO:0094648	fig 3b
PMID:29032152	PBO:0095685	fig 3b
PMID:29079657	PBO:0097752	fig2 and supp table
PMID:29079657	PBO:0097754	fig6
PMID:29079657	PBO:0097753	fig2 and supp table
PMID:29079657	PBO:0097752	fig2 and supp table
PMID:29079657	PBO:0097753	fig2 and supp table
PMID:29079657	PBO:0097752	fig2 and supp table
PMID:29079657	PBO:0097753	fig2 and supp table
PMID:29079657	PBO:0097752	fig2 and supp table
PMID:29079657	PBO:0097753	fig2 and supp table
PMID:29079657	PBO:0097752	fig2 and supp table
PMID:29079657	PBO:0097753	fig2 and supp table
PMID:29079657	PBO:0097752	fig2 and supp table
PMID:29079657	PBO:0097753	fig2 and supp table
PMID:29079657	PBO:0097752	fig2 and supp table
PMID:29079657	PBO:0097753	fig2 and supp table
PMID:29079657	PBO:0097753	fig2 and supp table
PMID:29079657	PBO:0097752	fig2 and supp table
PMID:29079657	PBO:0097753	fig2 and supp table
PMID:29079657	PBO:0097752	fig2 and supp table
PMID:29079657	PBO:0097753	fig2 and supp table
PMID:29079657	PBO:0097752	fig2 and supp table
PMID:29079657	PBO:0097753	fig2 and supp table
PMID:29079657	PBO:0097752	fig2 and supp table
PMID:29079657	PBO:0097753	fig2 and supp table
PMID:29079657	PBO:0097752	fig2 and supp table
PMID:29079657	PBO:0097753	fig2 and supp table
PMID:29079657	PBO:0097752	fig2 and supp table
PMID:29079657	PBO:0097753	fig2 and supp table
PMID:29079657	PBO:0097752	fig2 and supp table
PMID:29079657	PBO:0097753	fig2 and supp table
PMID:29079657	PBO:0097752	fig2 and supp table
PMID:29079657	PBO:0097753	fig2 and supp table
PMID:29079657	PBO:0097752	fig2 and supp table
PMID:29079657	PBO:0097753	fig2 and supp table
PMID:29079657	PBO:0097752	fig2 and supp table
PMID:29079657	PBO:0097753	fig2 and supp table
PMID:29079657	PBO:0097752	fig2 and supp table
PMID:29079657	PBO:0097753	fig2 and supp table
PMID:29079657	PBO:0097752	fig2 and supp table
PMID:29079657	GO:0010515	fig1
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:2908246	PBO:0099004	Fig 3
PMID:2908246	PBO:0099005	mild over expression of cdc13+ on multi copy plasmid pYep13 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:0038194	mild over expression of cdc2+ on multi copy plasmid rescues the cdc13-117 ts phenotype
PMID:2908246	PBO:0099003	Fig 3
PMID:29084823	PBO:0104949	Fig5E
PMID:29084823	PBO:0104945	Fig6A
PMID:29084823	PBO:0104945	Fig6A
PMID:29084823	PBO:0104950	Fig6A,B
PMID:29084823	PBO:0104935	Fig6 A,B
PMID:29084823	PBO:0104950	Fig6A,B
PMID:29084823	PBO:0104947	Fig6A,B
PMID:29084823	PBO:0104951	Fig6A,B
PMID:29084823	PBO:0099114	Fig7A shows that puc1delta shows increased mating efficiency at nitrogen levels which suppress mating in wild type cells
PMID:29084823	PBO:0104952	RNA
PMID:29084823	PBO:0104931	Figure 1A Sup Fig1
PMID:29084823	FYPO:0001890	"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:0104932	Figure 1C
PMID:29084823	PBO:0104933	Figure 1C
PMID:29084823	PBO:0104934	Fig 2B,C fig6a
PMID:29084823	PBO:0104935	Fig 2D, E, Sup Fig 2
PMID:29084823	PBO:0093825	Fig3A
PMID:29084823	FYPO:0001147	Fig3A deletion of puc1 increases mating efficiency of zfs1 delta to WT
PMID:29084823	PBO:0093825	Fig3B 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:0104946	Fig6A
PMID:29084823	PBO:0104946	Fig6A
PMID:29084823	PBO:0104945	Fig6A
PMID:29084823	PBO:0104944	Fig5E
PMID:29084823	PBO:0104943	Fig5E
PMID:29084823	PBO:0104942	Fig5C,D
PMID:29084823	PBO:0104942	Fig5C,D
PMID:29084823	PBO:0104941	Fig 5B, construct 3
PMID:29084823	PBO:0020460	Fig4A,B about 10%? of Zfs1 is phosphorylated during vegetative growth
PMID:29084823	PBO:0104940	Fig4D Sup Fig3 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	Fig4A,B Zfs is hyperphosphorylated in response to nitrogen depletion
PMID:29084823	PBO:0104938	Fig3C, Fig7A shows that zfs1delta shows high mating efficiency at nitrogen levels which suppress mating in wild type cells wild type cells
PMID:29084823	PBO:0104936	Fig3C
PMID:29084823	PBO:0104937	Fig3C
PMID:29084823	PBO:0104947	Fig6A,B
PMID:29084823	PBO:0093825	Fig3A deletion of cig1 does not rescue mating efficiency of zfs1 delta
PMID:29084823	PBO:0093825	Fig3A deletion of cig2 does not rescue mating efficiency zfs1delta
PMID:29084823	PBO:0104948	Fig5E
PMID:29109278	PBO:0094283	otr1R(SphI)::ura4+
PMID:29109278	PBO:0094283	otr1R(SphI)::ura4+
PMID:29109278	PBO:0094679	otr1R(SphI)::ura4+
PMID:29109278	PBO:0094679	otr1R(SphI)::ura4+
PMID:29109278	PBO:0094679	otr1R(SphI)::ura4+
PMID:29109278	FYPO:0002827	mat3M::ura4+
PMID:29109278	FYPO:0004604	tel2L::ura4+
PMID:29109278	FYPO:0003412	otr1R(SphI)::ura4+
PMID:29109278	FYPO:0004742	otr1R(SphI)::ura4+
PMID:29109278	PBO:0094282	otr1R(SphI)::ura4+
PMID:29109278	PBO:0105309	otr1R(SphI)::ura4+
PMID:29109278	PBO:0105308	otr1R(SphI)::ura4+
PMID:29123917	PBO:0102320	Later stage of meiotic prophase, observed by co-localisation with Taz1
PMID:29123917	FYPO:0006372	S10 E and F
PMID:29123917	PBO:0102323	fig6
PMID:29123917	PBO:0102320	Later stage of meiotic prophase, observed by co-localisation with Taz1
PMID:29134248	GO:0070867	Fusion domain
PMID:29134248	GO:0032220	plasma membrane fusion during conjugation
PMID:29134248	GO:0032220	plasma membrane fusion during conjugation
PMID:29136238	PBO:0107686	and observed a preferential association of Swi6 with Y41F over Y41p peptide, suggest- ing that phosphorylation of H3Y41 counteracts the interac- tion of Swi6 with histone H3 (Supplementary Figure S6A).
PMID:29136238	PBO:0107687	Fig4
PMID:29136238	PBO:0107688	Fig4/5
PMID:29136238	PBO:0097234	Fig4/5
PMID:29136238	PBO:0094681	Fig2
PMID:29136238	PBO:0094282	Fig2
PMID:29136238	PBO:0097950	Fig2
PMID:29136238	FYPO:0004743	Fig3
PMID:29136238	FYPO:0006429	Fig3
PMID:29136238	PBO:0094682	Fig4
PMID:29136238	PBO:0107685	and observed a preferential association of Swi6 with Y41F over Y41p peptide, suggest- ing that phosphorylation of H3Y41 counteracts the interac- tion of Swi6 with histone H3 (Supplementary Figure S6A).
PMID:29136238	PBO:0107684	and observed a preferential association of Swi6 with Y41F over Y41p peptide, suggest- ing that phosphorylation of H3Y41 counteracts the interac- tion of Swi6 with histone H3 (Supplementary Figure S6A).
PMID:29136238	FYPO:0006395	Fig3
PMID:29136238	FYPO:0000088	fig7
PMID:29136238	FYPO:0003575	Fig3
PMID:29136238	PBO:0101106	Fig1
PMID:29136238	PBO:0107682	Fig1
PMID:29136238	PBO:0107683	Fig2
PMID:29136238	PBO:0094283	Fig2
PMID:29149597	PBO:0095033	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: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:29160296	PBO:0114398	Fig. 3D
PMID:29160296	PBO:0114395	Fig. 2C
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:0114397	Fig. 3E
PMID:29160296	PBO:0114397	Fig. 3E
PMID:29160296	PBO:0114397	Fig. 3E
PMID:29160296	PBO:0114397	Fig. 3E
PMID:29160296	PBO:0114398	Fig. 3D
PMID:29160296	PBO:0114399	Fig. 3D
PMID:29160296	PBO:0114400	Fig. 3D
PMID:29160296	PBO:0114401	Fig. 3D
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:0114403	Fig. 4F
PMID:29160296	PBO:0114403	Fig. 4F
PMID:29160296	PBO:0114404	Fig. 4F
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:0093632	Fig. 5A
PMID:29160296	PBO:0093634	Fig. 5A
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:0114406	Fig. 5B
PMID:29160296	PBO:0114407	Fig. 5B
PMID:29160296	PBO:0114407	Fig. 5B
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:0114409	Fig. 5E
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:0093637	Fig. 5D
PMID:29167352	FYPO:0002060	(Fig. 1C
PMID:29167352	FYPO:0002060	(Fig. 1C 28 Celcius
PMID:29167352	GO:0072686	often in a punctate manner
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	PBO:0101442	~30% of the double mutant cells exhibited the monopolar spindle phenotype.
PMID:29167352	FYPO:0002060	(Fig. 1C
PMID:29167352	FYPO:0002060	(Fig. 1C
PMID:29167352	FYPO:0002060	(Fig. 1C
PMID:29167352	FYPO:0001489	28 celcius
PMID:29167352	FYPO:0002060	(Fig. 1C
PMID:29167439	FYPO:0006507	Require for subtelomeric DNA amplification in G0
PMID:29167439	FYPO:0006507	require for subtelomeric DNA amplification in G0
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:29180432	FYPO:0002638	fig 5f
PMID:29180432	PBO:0108192	figure 3
PMID:29180432	PBO:0108189	figure 3
PMID:29180432	PBO:0108188	fig3
PMID:29180432	PBO:0108187	fig 6
PMID:29180432	PBO:0108186	fig 2G
PMID:29180432	PBO:0108185	fig 2G
PMID:29180432	PBO:0108185	fig 2G
PMID:29180432	PBO:0108186	fig 4
PMID:29180432	PBO:0109271	fig 3
PMID:29180432	PBO:0098308	fig 5 (measured at 4 um spindle. WT has 6%)
PMID:29180432	FYPO:0006800	Fig. 5 B and D
PMID:29180432	PBO:0108191	increased duration of metaphase Fig. 5E
PMID:29180432	PBO:0108188	fig6
PMID:29194511	PBO:0102787	Figure 3C-D, Supplementary Figure 8A-B
PMID:29194511	GO:0005515	fig 5
PMID:29194511	FYPO:0006353	fig 4b
PMID:29194511	FYPO:0006353	fig 4b
PMID:29194511	FYPO:0003241	fig 4a
PMID:29194511	FYPO:0003241	fig 4a
PMID:29194511	PBO:0102796	fig 1b &C
PMID:29194511	PBO:0102793	fig 1b &C
PMID:29194511	PBO:0102795	fig 1b &C
PMID:29194511	PBO:0102794	fig 1b &C
PMID:29194511	PBO:0102793	fig 1b &C
PMID:29194511	PBO:0102792	fig 1b &C
PMID:29194511	PBO:0102791	fig 1b &C and 3H
PMID:29194511	PBO:0102790	fig 1b &C and 3H
PMID:29194511	PBO:0102789	fig 1b &C
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	FYPO:0003241	Figure S1A and B
PMID:29194511	PBO:0102788	Figure 2G, supplementary figure 4
PMID:29194511	PBO:0101834	Figure 2E-F, supplementary figure 5
PMID:29194511	FYPO:0001234	Figure 2A,B,C
PMID:29194511	PBO:0102787	Figure 3E-F, Supplementary figure 8 C-D
PMID:29214404	FYPO:0000873	at telomeres 1L, 2R
PMID:29214404	PBO:0094683	at telomeres 1L, 1R, 2L, 2R
PMID:29214404	PBO:0100489	greater decrease at telomeres 1R and 2L than at 1L and 2R
PMID:29214404	FYPO:0004137	at telomere 1R
PMID:29215009	FYPO:0006320	upstream reporter
PMID:29215009	FYPO:0003589	same as either single mutant
PMID:29215009	FYPO:0006318	same as exo1delta alone
PMID:29215009	FYPO:0006320	upstream reporter
PMID:29216371	PBO:0095218	IMP evidence for part_of extension
PMID:29216371	PBO:0095218	IMP evidence for part_of extension
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	FYPO:0000223	fig 2A
PMID:29249658	PBO:0103089	fig 2A
PMID:29249658	PBO:0103092	fig 2
PMID:29249658	PBO:0103093	figure 2
PMID:29249658	PBO:0103094	figure 2
PMID:29249658	PBO:0103095	figure 2
PMID:29249658	FYPO:0000224	fig 2A
PMID:29249658	PBO:0103096	fig 3A
PMID:29249658	PBO:0103096	fig 3B
PMID:29249658	PBO:0103097	fig 3c
PMID:29249658	PBO:0103097	fig S3A
PMID:29249658	PBO:0103098	fig 3D
PMID:29249658	PBO:0103099	fig 3
PMID:29249658	PBO:0103100	fig 3
PMID:29249658	PBO:0103101	Figure S-3F
PMID:29249658	PBO:0103102	Figure S-3F
PMID:29249658	PBO:0103102	Figure S-3F
PMID:29249658	PBO:0103101	Figure S-3F
PMID:29249658	PBO:0103103	Figure S-3F
PMID:29249658	PBO:0103103	Figure S-3F
PMID:29249658	PBO:0103102	Figure 3D
PMID:29249658	PBO:0103099	fig 3D
PMID:29249658	GO:0005515	fig 3h
PMID:29249658	PBO:0103104	Figure 3H
PMID:29249658	FYPO:0000013	Fig 4C D
PMID:29249658	FYPO:0000118	Fig 4C D
PMID:29249658	PBO:0103105	figure S4C
PMID:29249658	PBO:0103105	figure S4C
PMID:29249658	PBO:0103106	figure S4C
PMID:29249658	PBO:0103106	figure S4C
PMID:29249658	PBO:0103107	Fig 4F
PMID:29249658	PBO:0103108	Fig 4F (lasso)
PMID:29249658	PBO:0103089	fig 2A
PMID:29249658	PBO:0103088	CHeCK phenotypes
PMID:29249658	PBO:0103087	fig 1
PMID:29249658	PBO:0103086	fig 1
PMID:29249658	FYPO:0002021	fig 1
PMID:29249658	PBO:0099941	fig 1 `D,E ~55%
PMID:29249658	PBO:0103085	figure 1c
PMID:29249658	PBO:0103084	fig 1B
PMID:29249658	PBO:0103084	fig 1B
PMID:29259000	PBO:0102151	fig 7D,E,F
PMID:29259000	PBO:0102152	fig5
PMID:29259000	PBO:0102146	Figure S3C-E
PMID:29259000	FYPO:0000485	Figure 3F
PMID:29259000	PBO:0102148	Figure 4A and B: MI NDJ
PMID:29259000	PBO:0102145	fig 3D
PMID:29259000	PBO:0102144	fig 3D
PMID:29259000	FYPO:0000583	fig2 abolished asci formation
PMID:29259000	FYPO:0006314	fig2
PMID:29259000	FYPO:0006313	fig 2A abolished entry into meiosis (at pre meiosis?)
PMID:29259000	FYPO:0006313	fig 2A abolished entry into meiosis (at pre meiosis?)
PMID:29259000	FYPO:0000280	fig2A
PMID:29259000	PBO:0102147	Figure S3C-E
PMID:29259000	PBO:0102149	Figure 4A and B: 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:29290560	PBO:0108726	fig1 ER plasma membrane tethering ER-PM contact removal OR abnormal ER-PM contact formation
PMID:29290560	FYPO:0000539	Fig 3D
PMID:29290560	FYPO:0000537	Fig 3D
PMID:29290560	FYPO:0001945	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 *********lateral PM
PMID:29290560	FYPO:0006330	Figures 1C and S1C ER-PM contact removal
PMID:29290560	GO:0140268	fig1
PMID:29292846	PBO:0104334	fig2
PMID:29292846	PBO:0104333	fig2
PMID:29292846	GO:0019237	Deletion of LEM domain decreases the association of Lem2 at the centromere
PMID:29292846	PBO:0104332	fig5
PMID:29292846	GO:0003690	DNA binding site: 1-60 a.a.
PMID:29292846	PBO:0104333	fig2
PMID:29292846	PBO:0104337	fig5
PMID:29292846	PBO:0104339	fig 5
PMID:29292846	FYPO:0005612	fig5
PMID:29292846	FYPO:0002967	fig5
PMID:29292846	PBO:0104333	fig2
PMID:29292846	PBO:0104333	fig2
PMID:29292846	FYPO:0000655	fig3
PMID:29292846	FYPO:0000659	fig3
PMID:29292846	FYPO:0000655	fig3
PMID:29292846	GO:0005635	fig4
PMID:29292846	GO:0044732	fig4
PMID:29292846	GO:0005635	fig4
PMID:29292846	PBO:0104335	fig5
PMID:29292846	PBO:0104336	fig5
PMID:29292846	GO:0005515	fig 1a residues 200-307
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	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:29330317	GO:0006433	fig3
PMID:29330317	GO:0006421	fig3
PMID:29343550	FYPO:0002060	Figure 2C DAPI, methyl blue
PMID:29343550	PBO:0106952	Figure 1C
PMID:29343550	PBO:0106951	Figure 1A-B
PMID:29343550	FYPO:0004741	Figure 4A LifeAct-mcherry
PMID:29343550	FYPO:0001365	Figure 5
PMID:29343550	FYPO:0003339	Figure 5
PMID:29343550	FYPO:0005020	Figure 5
PMID:29343550	FYPO:0003339	Figure 5
PMID:29343550	FYPO:0004740	Figure 4A LifeAct-mcherry issues/3215
PMID:29343550	FYPO:0004741	Figure 4A LifeAct-mcherry
PMID:29343550	PBO:0106949	Figure 4E-F tagged with GFP
PMID:29343550	PBO:0099724	Figure 4C 4Cmcherry
PMID:29343550	PBO:0106492	Figure 3A allele tagged with mNeonGreen
PMID:29343550	FYPO:0004737	Figure 4A LifeAct-mcherry
PMID:29343550	FYPO:0002177	Figure 2C DAPI, methyl blue
PMID:29343550	PBO:0099724	Figure 4Cmcherry
PMID:29343550	PBO:0106948	Figure 4E tagged with GFP
PMID:29343550	PBO:0106492	Figure 3A allele tagged with mNeonGreen
PMID:29352077	FYPO:0001513	figure 2
PMID:29352077	FYPO:0002060	figure 3
PMID:29352077	FYPO:0002060	figure 3
PMID:29352077	FYPO:0002060	figure 4
PMID:29352077	FYPO:0002060	figure 4
PMID:29352077	FYPO:0002060	figure 3
PMID:29352077	FYPO:0002060	figure 3
PMID:29352077	FYPO:0002060	figure 3
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:0002060	figure 3
PMID:29352077	FYPO:0001513	figure 3
PMID:29352077	FYPO:0001513	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	FYPO:0002060	figure 4
PMID:29352077	FYPO:0002060	figure 4
PMID:29352077	PBO:0107889	figure 4F
PMID:29352077	FYPO:0002060	figure 2
PMID:29414789	PBO:0096175	Northern blot and primer extension analysis
PMID:29414789	PBO:0094613	Primer extension analysis
PMID:29414789	PBO:0097322	Northern blot and primer extension analysis
PMID:29414789	PBO:0096175	Primer extension analysis
PMID:29414789	PBO:0101896	Primer extension analysis
PMID:29414789	PBO:0094613	Primer extension analysis
PMID:29414789	PBO:0097322	Northern blot and primer extension analysis
PMID:29414789	PBO:0101896	Primer Extension Analysis
PMID:29414789	PBO:0096175	Northern blot and primer extension analysis
PMID:29414789	PBO:0097330	Northern blot and primer extension analysis
PMID:29414789	PBO:0096175	Primer extension analysis
PMID:29414789	PBO:0101897	Primer extension analysis
PMID:29414789	PBO:0101897	Primer extension analysis
PMID:29414789	PBO:0101897	Primer extension analysis
PMID:29414789	FYPO:0002243	8c
PMID:29414789	GO:0140256	GONEW: negative regulation of cellular response to phosphate starvation
PMID:29422501	PBO:0101695	fig1 c
PMID:29422501	PBO:0101696	fig 1c
PMID:29422501	PBO:0101702	fig 3a
PMID:29422501	PBO:0101696	fig 1c
PMID:29422501	PBO:0101688	fig2
PMID:29422501	PBO:0101688	fig2
PMID:29422501	PBO:0101688	fig2
PMID:29422501	PBO:0101688	fig 1 a
PMID:29422501	PBO:0101694	fig1 c
PMID:29422503	FYPO:0003106	figure 1 a
PMID:29422503	PBO:0095772	Supplementary Fig. 4
PMID:29422503	PBO:0095747	fig 5
PMID:29422503	GO:1904868	figs 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	figs 1-3
PMID:29422503	PBO:0095771	(created to replace WT phenotype annotation)
PMID:29422503	PBO:0095770	(created to replace WT phenotype)
PMID:29422503	GO:0003682	(created to replace WT phenotype)
PMID:29422503	PBO:0095769	(created to replace WT phenotype annotation) lsm3-myc chip
PMID:29422503	GO:0070034	(created to replace WT phenotype annotation)
PMID:29422503	PBO:0095768	(created to replace WT phenotype annotation) fig 3 b
PMID:29422503	PBO:0095769	(created to replace WT phenotype annotation) est1-myc chip
PMID:29422503	PBO:0095769	(created to replace WT phenotype annotation) trt1-myc chip
PMID:29422503	PBO:0095768	fig 3a (created to replace WT phenotype annotation)
PMID:29422503	PBO:0095767	fig 1 e
PMID:29422503	PBO:0095767	fig 1 e
PMID:29422503	PBO:0095767	fig 1 e
PMID:29422503	PBO:0095766	fig 1 c/d
PMID:29422503	PBO:0095765	fig 1 c/d
PMID:29422503	PBO:0095764	fig 1 c/d
PMID:29422503	GO:0140445	(created to replace WT phenotype annotation) 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 6 b
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: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: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 4 a 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 1 e 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 1 e 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 1 e 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 1 e 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 3 b
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 1 c/d Trt1-myc ChIP
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	fig1 Lose telomere signal, much like trt1∆ cells.
PMID:29424342	PBO:0102650	Fig. 6
PMID:29424342	PBO:0099879	Fig. 4B
PMID:29424342	PBO:0102644	Fig. 4
PMID:29424342	PBO:0102651	Fig. 6
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:0102642	Fig. 5
PMID:29424342	PBO:0102643	Fig. 5
PMID:29424342	PBO:0102649	Fig. 6
PMID:29424342	GO:0006406	Fig. 2
PMID:29432178	PBO:0100854	Fig. 3A
PMID:29432178	FYPO:0001357	Fig. 3A
PMID:29432178	FYPO:0006473	Fig. 3E
PMID:29432178	PBO:0100857	Fig. 3B during normal growth
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	Can we say somewhere - overexpresses genes involved by amino acid starvation, or something similar?
PMID:29453312	PBO:0096694	Active Ras1 is localized to cell poles during mitotic growth
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	GO:1990819	Ste6 co-localizes with the actin fusion focus during the process of cell-cell fusion
PMID:29453312	PBO:0092569	Ative Ras1 localizes to septa during mitotic growth
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: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	PBO:0096695	In the absence of efc25 Ras1 is not activated at the cell cortex
PMID:29458562	FYPO:0002060	Fig. 2
PMID:29458562	FYPO:0000562	fig2 (likey due to intron encoded maturase)
PMID:29458562	PBO:0096250	fig4
PMID:29458562	PBO:0096251	fig3 abolished
PMID:29458562	FYPO:0004085	Fig. 2
PMID:29458562	FYPO:0004085	Fig. 2
PMID:29458562	FYPO:0000245	Fig. 2
PMID:29458562	FYPO:0004153	DNS
PMID:29458562	PBO:0096252	fig3
PMID:29458562	PBO:0096258	fig4
PMID:29458562	PBO:0096257	fig4
PMID:29458562	PBO:0096256	fig4
PMID:29458562	PBO:0096255	fig4
PMID:29458562	PBO:0096254	fig3
PMID:29458562	PBO:0096253	fig3
PMID:29514920	PBO:0101337	fig 3A, fig 3B Fig. 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:0107825	figure 2B
PMID:29514920	PBO:0107824	figure 2B
PMID:29514920	PBO:0107825	figure 2B
PMID:29514920	PBO:0107824	fig2B
PMID:29514920	PBO:0023824	figure 2D Epistatic to cdr2delta
PMID:29514920	PBO:0107815	affecting Wee1
PMID:29514920	PBO:0107815	Affecting Wee1 vw Increased , term pending
PMID:29514920	PBO:0107816	fig 3D Affecting Wee1
PMID:29514920	PBO:0107823	Fig 1C
PMID:29514920	PBO:0107431	Fig 1B
PMID:29514920	PBO:0107823	Fig. 1A
PMID:29514920	PBO:0107822	Fig 1A
PMID:29514920	PBO:0107822	Fig 1A
PMID:29514920	PBO:0102684	affecting Cdr1 vw:ig. S2, F and G
PMID:29514920	PBO:0023824	figure 2D Epistatic to cdr2delta
PMID:29514920	PBO:0107817	Fig 2C 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:29529046	PBO:0102044	Fig 4 BE
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: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	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: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	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	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:0102040	"We made the term ""zinc ion import into organelle""in GO becuse it fits better witht the descendants"
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:0102051	Fig 8
PMID:29529046	PBO:0102051	Fig 8
PMID:29529046	PBO:0102050	Fig 8
PMID:29529046	PBO:0102049	Fig 8
PMID:29529046	PBO:0102048	Fig 8
PMID:29529046	PBO:0102047	Fig 8
PMID:29529046	PBO:0102046	Fig 8
PMID:29529046	PBO:0102045	Fig 8
PMID:29529046	PBO:0102039	fig6
PMID:29529046	PBO:0093561	Figure 1 (EDTA, zinc chelator)
PMID:29529046	PBO:0093559	Figure 1 (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:29549126	GO:0020037	fig6
PMID:29549126	GO:0016020	fig7
PMID:29549126	PBO:0106478	assayed using heme analog ZnMP
PMID:29549126	PBO:0106479	assayed using heme analog ZnMP
PMID:29549126	FYPO:0007397	assayed using heme analog ZnMP
PMID:29549126	GO:0020037	fig6
PMID:29549126	GO:0016020	fig7
PMID:29549126	GO:1904334	3B,C, We therefore concluded that Shu1 is required for hemin acquisition when hemin is present at very low concentrations (0.075 􏰄M), whereas its presence is dispens- able under conditions of high hemin concentrations
PMID:29549126	GO:0140420	3B,C,
PMID:29596413	PBO:0095605	fig 7C
PMID:29596413	PBO:0095607	fig 7C
PMID:29596413	PBO:0095609	fig 7C supression of trm7-delta
PMID:29596413	PBO:0095608	fig 7C supression of trm7-delta
PMID:29596413	PBO:0095606	fig 7C supression of trm7-delta
PMID:29596413	PBO:0095599	fig 7
PMID:29596413	PBO:0095600	fig 7
PMID:29596413	PBO:0095602	fig 7
PMID:29596413	PBO:0095601	fig 7
PMID:29596413	PBO:0095603	fig 7C
PMID:29596413	PBO:0095608	fig 7C supression of trm7-delta
PMID:29596413	PBO:0095610	fig 7C supression of trm7-delta
PMID:29596413	PBO:0095604	fig 7C
PMID:29596413	PBO:0095606	fig 7C supression of trm7-delta
PMID:29610759	FYPO:0005353	at MPS1
PMID:29610759	PBO:0105327	fig 5
PMID:29610759	PBO:0105325	fig 1
PMID:29610759	PBO:0105324	fig 2
PMID:29610759	PBO:0098985	enriched at mat1 right border and cenH left border; fig 1
PMID:29610759	PBO:0098985	figs 1 & 4
PMID:29610759	PBO:0098985	figs 1 & 4
PMID:29610759	PBO:0105326	fig 1
PMID:29618061	PBO:0108864	Interestingly, elevated pho1 levels were observed in prt-1, prt-2, and prt-3 (Figure 3B, lanes 1– 4) suggesting that element(s) responsible for pho1 silencing are located within the 5′ part of prt.
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 transcrip- tional level (Figure 5a).
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 rrp6 (Figure 5B and C).
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 rrp6 (Figure 5B and C).
PMID:29618061	PBO:0096778	. clr4, or the dou- ble mutant clr3clr4 (Supplementary Figure S3A, lane 4 and 5), also revealed no change in mRNA expression lev- els. These results indicate that unlike pho1, tgp1 repression
PMID:29618061	PBO:0096776	. clr4, or the dou- ble mutant clr3clr4 (Supplementary Figure S3A, lane 4 and 5), also revealed no change in mRNA expression lev- els. These results indicate that unlike pho1, tgp1 repression
PMID:29618061	PBO:0096778	. clr4, or the dou- ble mutant clr3clr4 (Supplementary Figure S3A, lane 4 and 5), also revealed no change in mRNA expression lev- els. These results indicate that unlike pho1, tgp1 repression
PMID:29618061	PBO:0096776	. clr4, or the dou- ble mutant clr3clr4 (Supplementary Figure S3A, lane 4 and 5), also revealed no change in mRNA expression lev- els. These results indicate that unlike pho1, tgp1 repression
PMID:29618061	PBO:0096778	No detectable increase in either tgp1 or nc-tgp1 was observed in sir2, 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 sir2, 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 sir2, 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 sir2, 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 ef- fect 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 per- formed 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 set1 strain (Figure 3E).
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 mu- tant clr3set1 with the respective single mutants (Figure 3D). We found that the double mutant did not lead to higher pho1 derepression as compared to single set1, indicating that both proteins do indeed function in the same pathway.
PMID:29618061	PBO:0110989	. Interest- ingly, 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 un- derlying pho1 silencing primarily relies on histone methy- lation by Set1
PMID:29618061	PBO:0110995	In the case of prt-3, this phenotype is likely a result of lost Mmi1 recruitment since this mu- tant 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:0110958	No change in pho1 ex- pression could be detected for either prt-4 or prt-5 (Fig- ure 3B, lanes 5 and 6).
PMID:29618061	PBO:0110958	No change in pho1 ex- pression could be detected for either prt-4 or prt-5 (Fig- ure 3B, lanes 5 and 6).
PMID:29618061	PBO:0108864	Interestingly, elevated pho1 levels were observed in prt-1, prt-2, and prt-3 (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-1, prt-2, and prt-3 (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	as expected, northern blot analysis revealed no obvious additive effect compared to the ncpro single mu- tant (Figure 2E).
PMID:29618061	PBO:0110992	H3K14ac levels were also increased in this strain (Figure 2D), similar to that seen in clr3 (Fig- ure 1E)
PMID:29618061	PBO:0110994	We found that, in the absence of non-coding transcription in a strain lacking the prt promoter (ncpro) (5), Clr3 recruitment to pho1 was re- duced (Figure 2C).
PMID:29618061	PBO:0110993	Re- markably, 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 sin- gle mutants, clr3 or clr4 (Figure 2B).
PMID:29618061	PBO:0110993	Re- markably, 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 sin- gle mutants, clr3 or clr4 (Figure 2B).
PMID:29618061	PBO:0110993	Re- markably, 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 sin- gle mutants, clr3 or clr4 (Figure 2B).
PMID:29618061	PBO:0110992	an increase in the lev- els of H3K14ac could be detected by ChIP-qPCR (Figure 1E);
PMID:29618061	PBO:0110991	(Figure 1D). We found that loss of Clr3 leads to in- creased Pol II levels upstream of the pho1 promoter and particularly across the gene body.
PMID:29618061	PBO:0110989	Northern blot (Supplementary Figure S1A). Compared to wild-type pho1 mRNA levels, a slight accumulation was de- tected for all strains. However, this is less pronounced than in clr3, 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 de- tected for all strains. However, this is less pronounced than in clr3, 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 de- tected for all strains. However, this is less pronounced than in clr3, indicating that Clr3 is unlikely to entirely depend on Clr2 or other components of SHREC for recruitment to pho1.
PMID:29618061	PBO:0110990	This revealed that Clr3 indeed local- izes to the gene, particularly at the non-coding region (Fig- ure 1C).
PMID:29618061	PBO:0110958	In contrast, deletion of TSA- insensitive sir2, which contributes to transcriptional silenc- ing at constitutive heterochromatin, had no effect on pho1 expression (Figure 1B, lane 5).
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:29632066	PBO:0104930	fig S1B
PMID:29632066	PBO:0104930	fig S1B
PMID:29632066	PBO:0104930	fig S1B
PMID:29641590	FYPO:0001135	fig3
PMID:29641590	FYPO:0007063	fig3
PMID:29641590	FYPO:0007065	fig3
PMID:29641590	FYPO:0007064	fig3
PMID:29641590	GO:0000472	A1 cleavage
PMID:29641590	GO:0000480	A0 cleavage
PMID:29641590	GO:0000447	A2 cleavage
PMID:29689193	GO:1903338	Promotes cell wall thickness hoemostasis
PMID:29689193	FYPO:0003889	fig 3C
PMID:29689193	FYPO:0006745	thicker and thinner, disrupted homeostasis
PMID:29689193	FYPO:0006745	thicker and thinner, disrupted homeostasis
PMID:29689193	FYPO:0006745	thicker and thinner, disrupted homeostasis
PMID:29689193	GO:1903338	Promotes cell wall thickness hoemostasis
PMID:29689193	FYPO:0001035	figure 3B
PMID:29689193	GO:1903338	Promotes cell wall thickness hoemostasis
PMID:29689193	FYPO:0006746	figure 2 F
PMID:29689193	FYPO:0001035	figure 3B
PMID:29699848	PBO:0102403	affect interaction with Tor1
PMID:29699848	PBO:0102404	abolished interaction with gad8
PMID:29735656	FYPO:0002060	figure 2 AB inactive separase, uncleavable kleisin
PMID:29735656	FYPO:0002061	figure 2 AB inactive separase, uncleavable kleisin
PMID:29735656	FYPO:0002060	figure 2 AB inactive separase, uncleavable kleisin
PMID:29735656	FYPO:0002060	figure 1A, supp S1A
PMID:29735656	FYPO:0002060	figure 1A, supp S1A
PMID:29735656	FYPO:0002060	figure 1 A
PMID:29735656	FYPO:0002060	figure 1 A
PMID:29735656	FYPO:0002060	figure 1 A
PMID:29735656	FYPO:0002060	figure 1 A
PMID:29735656	FYPO:0002060	figure 1 A
PMID:29735656	FYPO:0002060	figure 1 A
PMID:29735656	FYPO:0002060	figure 1 A
PMID:29735656	FYPO:0002060	figure 1 A
PMID:29735656	FYPO:0002060	figure 1 A
PMID:29735656	FYPO:0002060	figure 1 A
PMID:29735656	FYPO:0002060	fig 4b
PMID:29735656	FYPO:0002060	figure 1 A
PMID:29735656	FYPO:0002060	fig 4b
PMID:29735656	FYPO:0002060	fig 4b
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 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:0000268	figure 4d
PMID:29735656	PBO:0098320	fig 4e
PMID:29735656	PBO:0098320	figure 3c
PMID:29735656	FYPO:0000085	S4
PMID:29735656	FYPO:0000088	S4
PMID:29735656	FYPO:0002061	figure 2 AB inactive separase, uncleavable kleisin
PMID:29735745	PBO:0093733	Fig. 5 B
PMID:29735745	PBO:0105528	binds to the consensus sequence CCCCAY (Fig. 4)
PMID:29735745	PBO:0105528	binds to the consensus sequence CCCCAY (Fig. 4)
PMID:29735745	FYPO:0002061	Fig. 2 D
PMID:29735745	FYPO:0001357	Fig 2 B
PMID:29735745	FYPO:0001513	Fig 2 B
PMID:29735745	PBO:0105527	Fig. 3 D
PMID:29735745	PBO:0105527	Fig. 3 D
PMID:29735745	PBO:0105526	Fig. 3 D
PMID:29735745	PBO:0105526	Fig. 3 D
PMID:29735745	PBO:0105525	Fig. 3 D
PMID:29735745	PBO:0105525	Fig. 3 D
PMID:29735745	PBO:0105524	Fig. 3 D
PMID:29735745	PBO:0105524	Fig. 3 D
PMID:29735745	PBO:0105523	Fig. 3 D
PMID:29735745	PBO:0105523	Fig. 3 D
PMID:29735745	PBO:0105522	Fig. 3 D
PMID:29735745	PBO:0105522	Fig. 3 D
PMID:29735745	PBO:0105521	Fig. 3 D
PMID:29735745	PBO:0105521	Fig. 3 D
PMID:29735745	PBO:0105520	Fig. 3 D
PMID:29735745	PBO:0105520	Fig. 3 D
PMID:29735745	PBO:0105519	Fig. 3 D
PMID:29735745	PBO:0105519	Fig. 3 D
PMID:29735745	PBO:0105518	Fig. 3 D
PMID:29735745	PBO:0105518	Fig. 3 D
PMID:29735745	PBO:0105517	Fig. 5 A, B, C; Fig. 7 C
PMID:29735745	PBO:0105517	Fig. 5 A, B, C; Fig. 7 C
PMID:29735745	GO:0000977	binds to the consensus sequence CCCCAY (Fig. 4)
PMID:29735745	GO:0000977	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. 2 C
PMID:29735745	PBO:0018677	Fig. 2 C
PMID:29735745	FYPO:0000214	Fig. 5 H
PMID:29735745	FYPO:0004099	Fig. S2 D
PMID:29735745	FYPO:0004099	Fig. S2 D
PMID:29735745	FYPO:0004099	Fig. S2 D
PMID:29735745	FYPO:0004099	Fig. S2 D
PMID:29735745	FYPO:0004099	Fig. S2 D
PMID:29735745	FYPO:0004099	Fig S2 D
PMID:29735745	FYPO:0004099	Fig. S2 D
PMID:29735745	PBO:0105516	Fig 7 D
PMID:29735745	PBO:0105514	Fig. 7 C
PMID:29735745	FYPO:0001357	Fig. 7 B
PMID:29735745	PBO:0096226	Fig. 7 B
PMID:29735745	PBO:0105516	Fig. 7 C
PMID:29735745	PBO:0105516	Fig. 7 C
PMID:29735745	FYPO:0001357	Fig. 7 B
PMID:29735745	FYPO:0002151	Fig. 7 B
PMID:29735745	FYPO:0001234	Fig. 7 B
PMID:29735745	FYPO:0002061	Fig. 6 B
PMID:29735745	FYPO:0004099	Fig. 6 D
PMID:29735745	FYPO:0001420	Fig 6 B, C
PMID:29735745	FYPO:0001420	Fig. 6 B, C
PMID:29735745	FYPO:0001420	Fig. 6 B, C
PMID:29735745	FYPO:0001420	Fig. 6 B, C
PMID:29735745	FYPO:0001420	Fig. 6 B, C
PMID:29735745	FYPO:0001420	Fig. 6 B, C
PMID:29735745	FYPO:0001420	Fig. 6 B, C
PMID:29735745	FYPO:0001420	Fig. 6 B, C
PMID:29735745	FYPO:0001234	Fig. 6 B, C
PMID:29735745	FYPO:0001234	Fig. 6 B, C
PMID:29735745	PBO:0105516	Fig. 5 C
PMID:29735745	PBO:0105516	Fig. 5 C
PMID:29735745	PBO:0093732	Fig. 5 B
PMID:29735745	PBO:0093732	Fig. 5 B
PMID:29735745	PBO:0105355	Fig. 5 A
PMID:29735745	PBO:0105515	Fig. 5 A
PMID:29735745	PBO:0105354	Fig. 5 A
PMID:29735745	PBO:0105514	Fig. 5 A, 5 C
PMID:29735745	PBO:0105513	Fig. 3 D
PMID:29735745	PBO:0105512	Fig. 3 D
PMID:29735745	PBO:0105511	Fig. 3 D
PMID:29735745	PBO:0105510	Fig. 3 D
PMID:29735745	PBO:0105509	Fig. 3 D
PMID:29735745	PBO:0105508	Fig. 3 D
PMID:29735745	PBO:0105507	Fig. 3 D
PMID:29735745	PBO:0105506	Fig. 3 D
PMID:29735745	PBO:0105505	Fig. 3 D
PMID:29735745	PBO:0105504	Fig. 3 D
PMID:29735745	PBO:0105503	Fig. 3 D
PMID:29735745	PBO:0105502	Fig. 3 D
PMID:29735745	PBO:0105501	Fig. 2 D
PMID:29735745	FYPO:0002061	Fig. 2 D
PMID:29735745	FYPO:0001357	Fig. 2 D
PMID:29735745	PBO:0105500	Fig. 2 D
PMID:29735745	FYPO:0004481	Fig. 1 C
PMID:29735745	PBO:0033591	Fig. 1 E
PMID:29735745	FYPO:0000159	Fig. 1 D
PMID:29735745	PBO:0101242	Fig. 1 E
PMID:29735745	PBO:0032915	Fig. 1 E
PMID:29735745	FYPO:0004481	Fig. 1 C
PMID:29735745	FYPO:0004481	Fig. 1 C
PMID:29735745	FYPO:0000214	Fig. 1 D
PMID:29735745	FYPO:0004099	Fig. S2 D
PMID:29735745	FYPO:0004099	Fig. S2 D
PMID:29735745	FYPO:0004099	Fig. 7 D
PMID:29735745	FYPO:0001420	Fig. 5G
PMID:29735745	FYPO:0001420	Fig. 5 G
PMID:29742018	PBO:0106102	in vitro, casein substrate
PMID:29742018	PBO:0106095	in vitro, casein substrate
PMID:29742018	PBO:0106094	in vitro, casein substrate
PMID:29742018	PBO:0106096	in vitro, casein substrate
PMID:29742018	PBO:0106092	normal with and without spindle checkpoint activation
PMID:29742018	PBO:0106088	normal with and without spindle checkpoint activation
PMID:29742018	PBO:0106099	Hhp1 accumulates at SPB when spindle checkpoint activated
PMID:29742018	PBO:0106102	in vitro, casein substrate
PMID:29742018	PBO:0106103	in vitro, casein substrate
PMID:29742018	PBO:0106091	in vitro, casein substrate
PMID:29742018	PBO:0106102	in vitro, casein substrate
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	PBO:0112466	An acetyl-mimetic H2A-K119Q mutation slightly inhibited Bub1-mediated H2A phosphorylation (Fig. 4B)
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	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: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
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:29769606	FYPO:0005633	Consistently, sister chromatid non-disjunction at meiosis II was signifcantly increased in the K119D and K119E mutants
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: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: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	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: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	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	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:29774234	PBO:0093557	slightly better growth than stn1-226 alone
PMID:29774234	PBO:0097405	Exacerbated at high temperature
PMID:29774234	FYPO:0000266	Sensitive to HU, CPT and MMS
PMID:29774234	PBO:0093557	same as stn1-226 alone
PMID:29774234	FYPO:0000122	loss of telomeric and subtelomeric sequences at high temperature
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 and 6B).
PMID:29804820	FYPO:0001355	FIgure 4D
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:29804820	GO:0005515	A Homodimer of the Mis18 C-Terminal Domain Interacts with a Mis16-Eic1 Heterodimer
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: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:0003201	Fig 3
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: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 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: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: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 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	GO:1905757	Fig 4D & E
PMID:29813053	GO:1905758	Fig 5B, Table 1; also inferred from localization timing
PMID:29813053	GO:1905758	Fig 56A-D; also inferred from localization timing
PMID:29813053	GO:1905758	Fig 56E; also inferred from localization timing
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: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: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 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: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:29844133	FYPO:0001407	beware using old strains, phenotypic changes observed.
PMID:29844133	PBO:0094265	Beware using aged colonies, cell size recovery observed.
PMID:29851556	PBO:0100532	localization of mutated protein assayed
PMID:29851556	GO:0035861	in the presence or absence of Nbs1
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: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 S3
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	PBO:0113772	Fig. 3
PMID:29852001	PBO:0113772	Fig. 3
PMID:29852001	PBO:0113772	Fig. 3
PMID:29852001	PBO:0113773	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	FYPO:0003659	Fig. 3
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:29866182	PBO:0098371	FLAG-Ago1
PMID:29866182	PBO:0098375	FLAG-Ago1, Arb1-Myc
PMID:29866182	PBO:0098376	Tas3-Myc
PMID:29866182	PBO:0098375	FLAG-Ago1, Arb1-Myc
PMID:29866182	PBO:0098372	Myc-Ago1
PMID:29866182	PBO:0098372	Myc-Ago1
PMID:29866182	PBO:0098371	FLAG-Ago1
PMID:29898918	PBO:0093559	Epistatic genetic interaction (same as eme1delta alone)
PMID:29898918	PBO:0093559	Epistatic genetic interaction (same as mus81delta alone)
PMID:29898918	FYPO:0000085	Epistatic genetic interaction (same as mus81delta alone)
PMID:29898918	MOD:00085	Required for cellular resistance to MMS and CPT.
PMID:29898918	PBO:0111500	present in cycling cells and meiosis I cells. Required for cellular resistance to MMS and CPT.
PMID:29898918	PBO:0093617	Epistatic genetic interaction (same as mus81delta alone)
PMID:29898918	PBO:0093617	slightly worse than srs2delta alone
PMID:29898918	PBO:0093617	Epistatic genetic interaction (same as eme1delta alone)
PMID:29898918	PBO:0111499	present in cycling cells and meiosis I cells. Required for cellular resistance to MMS and CPT.
PMID:29898918	FYPO:0000085	Epistatic genetic interaction (same as mus81delta alone)
PMID:29898918	PBO:0093617	slightly worse than srs2delta alone
PMID:29899453	PBO:0107351	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 1c
PMID:29899453	FYPO:0000080	Fig 3e
PMID:29899453	PBO:0107350	fig 1b
PMID:29899453	PBO:0092258	Fig 1B vw: corrected back to dis2 not cdk9!
PMID:29899453	GO:1904595	Extended data figure 9
PMID:29899453	PBO:0107366	extended data figure 9 decreased RNA pol2 localization to chromatin (occurs at termination sites)
PMID:29899453	FYPO:0005260	FIgure 3d. Extended fig 8d (vw: some suppression?)
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:0107365	fig 6a.b
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 .(cdk9as, cdk9as ssu72C13S, ssu72C13S)
PMID:29899453	PBO:0107349	fig 1b
PMID:29899453	PBO:0107363	Fig. 2e, Extended Data Fig. 4c
PMID:29899453	PBO:0107365	fig 6a.b
PMID:29899453	PBO:0107361	Fig. 2d,
PMID:29899453	PBO:0094008	Fig S2, Extended Data Fig. 2d
PMID:29899453	PBO:0099622	Fig S2, Extended Data Fig. 2c
PMID:29899453	PBO:0107360	check this addition Fig. 2a, Extended Data Fig. 2a
PMID:29899453	PBO:0107359	Fig. 1d, Extended Data Fig. 1d)
PMID:29899453	PBO:0107359	Fig. 1d, Extended Data Fig. 1d)
PMID:29899453	PBO:0107369	Extended Data Fig 10
PMID:29899453	PBO:0107358	Fig 5c.
PMID:29899453	PBO:0107368	fig 1d
PMID:29899453	PBO:0107368	fig 1d
PMID:29899453	PBO:0107367	fig 1d
PMID:29899453	FYPO:0002061	figure 3 e
PMID:29899453	FYPO:0006614	figure 3 e Also increased termination index Fig. 4e
PMID:29899453	FYPO:0006613	Extended Data Fig 3a ig. 2c, Extended Data Fig. 3b–d)
PMID:29899453	PBO:0107350	Fig 1c, Extended Data Fig 2a
PMID:29899453	PBO:0099591	fig 1c
PMID:29899453	PBO:0107361	Extended Data Fig 2f
PMID:29899453	PBO:0099591	Fig 1b
PMID:29899453	PBO:0093559	Fig 3e
PMID:29899453	PBO:0107358	Extended Data Fig 5a 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:0107357	Extended Data Fig 5a vw: fixed allele and target
PMID:29899453	PBO:0107356	Extended Data Fig 5a vw: fixed allele and target
PMID:29899453	PBO:0107355	Extended Data Fig 4d (vw: fixed allele)
PMID:29899453	PBO:0107355	Extended Data Fig 4d Added Dis2 extension
PMID:29899453	PBO:0107361	Extended Data Fig 2f
PMID:29899453	PBO:0107362	Extended Data Fig 3a ig. 2c, Extended Data Fig. 3b–d)
PMID:29899453	PBO:0107363	Fig. 2e, Extended Data Fig. 4b
PMID:29899453	PBO:0107369	Extended Data Fig 10
PMID:29899453	PBO:0107369	Extended Data Fig 10
PMID:29914874	FYPO:0001234	Supplementary Fig. S3
PMID:29914874	FYPO:0001234	Supplementary Fig. S3
PMID:29914874	FYPO:0001234	Supplementary Fig. S3
PMID:29914874	FYPO:0004750	Supplementary Figure S3
PMID:29914874	FYPO:0000017	Supplementary Fig. S3
PMID:29914874	FYPO:0001234	Supplementary Fig. S3
PMID:29914874	FYPO:0000005	Supplementary Fig. S3
PMID:29914874	FYPO:0001234	Supplementary Table S3
PMID:29930085	GO:1902716	Figure 1
PMID:29930085	GO:0005938	Figure 1
PMID:29930085	PBO:0018345	Figure 1
PMID:29930085	PBO:0018345	Figure 1
PMID:29930085	GO:0110085	Figure 1
PMID:29930085	PBO:0020227	Figure 1
PMID:29930085	GO:0110085	Figure 1
PMID:29930085	GO:0005737	Figure 5, Figure S4, Movie 5
PMID:29930085	GO:0110085	Figure 5, Figure S4, Movie 5
PMID:29930085	FYPO:0005465	fig 2 interphase arrest
PMID:29930085	PBO:0103571	fig 1 interphase arrest
PMID:29930085	PBO:0103570	fig 1 interphase arrest
PMID:29930085	PBO:0097442	fig 1 interphase arrest (requested during interphase)
PMID:29930085	PBO:0103569	fig 1 interphase arrest (requested during interphase)
PMID:29930085	PBO:0094706	fig 1 interphase arrest (requested during interphase)
PMID:29930085	PBO:0096676	fig 1 interphase arrest (requested during interphase)
PMID:29930085	FYPO:0005465	fig 1 interphase arrest
PMID:29930085	PBO:0103572	PORTLI GROWTH Fig S6 https://github.com/pombase/fypo/issues/3339
PMID:29930085	PBO:0103575	PORTLI GROWTH Fig S6 https://github.com/pombase/fypo/issues/3339
PMID:29930085	PBO:0103576	(PORTLI GROWTH) fig 6 c https://github.com/pombase/fypo/issues/3339
PMID:29930085	PBO:0103577	PORTLI Growth Figure 6, Figure S6, Movie 7 https://github.com/pombase/fypo/issues/3339
PMID:29930085	PBO:0103572	Portli Figure 7, Movie 9 https://github.com/pombase/fypo/issues/3339
PMID:29930085	PBO:0103578	figure 7D
PMID:29930085	PBO:0093708	figure 7d
PMID:29930085	FYPO:0006639	fig 7c
PMID:29930085	FYPO:0005465	fig2 movie1
PMID:29930085	FYPO:0006617	S1
PMID:29930085	FYPO:0002104	Figure 7, Figure S8
PMID:29930085	PBO:0019141	Figure 7, Figure S8
PMID:29930085	PBO:0019153	Figure S6, Movie 8
PMID:29930085	PBO:0103568	Figure S6, Movie 8
PMID:29930085	FYPO:0002150	Figure S3
PMID:29930085	FYPO:0005465	Fig. 5B
PMID:29930085	FYPO:0002150	Figure S3
PMID:29930085	PBO:0103568	Figure 7, Movie 9
PMID:29930085	PBO:0103568	Figure 6, Figure S6, Movie 7
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	PBO:0103568	Figure 3, Movie 2
PMID:29930085	PBO:0103568	Figure 3, Figure 4, Figure S2, Movie 2, Movie 3, Movie 4
PMID:29930085	PBO:0103568	Figure 2
PMID:29930085	GO:0110085	Figure 1
PMID:29930085	PBO:0103573	fig 3
PMID:29930085	PBO:0103572	(PORTLI GROWTH) fig 2 interphase arrest https://github.com/pombase/fypo/issues/3339
PMID:29930085	PBO:0103572	PORTLI GROWTH (Figs 3B and 4B; Movie 2) https://github.com/pombase/fypo/issues/3339
PMID:29930085	PBO:0103572	PORTLI GROWTH (Figs 3B and 4B; Movie 2) https://github.com/pombase/fypo/issues/3339
PMID:29930085	FYPO:0003316	Figure 4,AB
PMID:29930085	PBO:0103574	Figure S3
PMID:29930085	FYPO:0002104	Figure 4, Movie 4
PMID:29930085	FYPO:0002060	Fig. 5B
PMID:29930085	PBO:0103573	fig 3
PMID:29975113	PBO:0096159	These data are consistent with auto-ubiquitination triggering Dma1 destruction.
PMID:29975113	PBO:0096158	Figure 2D
PMID:29975113	PBO:0096156	Figure S2A
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:0096154	Figure 2D in vivo
PMID:29975113	PBO:0096157	temporal localization pattern Figure S2B
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:0096158	Figure 2G
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	GO:0071341	Figure 1B and S1B
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	FYPO:0002060	Figure S2D
PMID:29975113	PBO:0096150	Figure 2B and C
PMID:29975113	PBO:0096151	Figure S2B
PMID:29975113	PBO:0096153	(Vw, because mutants are related to WT, I changed this to 'normal'), Dma1-I194A-mNeonGreen displays transient loss from SPB during anaphase, just like wildtype Dma1.
PMID:29975113	GO:0031030	[ 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:0098958	Fig. 4D; live cell imaging
PMID:29975157	PBO:0098957	Fig. 4C; live cell imaging
PMID:29975157	PBO:0098956	Fig. 4B; live cell imaging
PMID:29975157	PBO:0098955	Fig. 4A; live cell imaging
PMID:29975157	FYPO:0005289	Fig. 3; live cell imaging
PMID:29975157	FYPO:0002071	Fig. 2D; live cell imaging
PMID:29975157	FYPO:0001369	Fig. 2A-C; live cell imaging
PMID:29975157	FYPO:0001369	Fig. 2A-C; live cell imaging
PMID:29975157	FYPO:0000339	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	FYPO:0002253	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	FYPO:0002253	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	FYPO:0000339	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	FYPO:0002253	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	PBO:0098954	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	FYPO:0000339	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	FYPO:0002253	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	FYPO:0002253	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	FYPO:0002253	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	FYPO:0002253	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	FYPO:0002253	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	PBO:0098954	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	FYPO:0002253	Fig. 1B; DAPI and methyl blue staining
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:29975157	FYPO:0002253	Fig. 1B; DAPI and methyl blue staining
PMID:29975157	FYPO:0002253	Fig. S1F; DAPI and methyl blue staining
PMID:29975157	FYPO:0006628	Fig. 5A; Live cell imaging of PIP4 lipid sensor
PMID:29975157	FYPO:0006628	Fig. 5A; Live cell imaging of PIP4 lipid sensor
PMID:29975157	FYPO:0006628	Fig. 5A; Live cell imaging of PIP4 lipid sensor
PMID:29975157	FYPO:0006629	Fig. 5A; Live cell imaging of PIP4 lipid sensor
PMID:29975157	FYPO:0006628	Fig. 5A; Live cell imaging of PIP4 lipid sensor
PMID:29975157	FYPO:0006626	Fig. 5C; Live cell imaging of PIP2 lipid sensor
PMID:29975157	FYPO:0006625	Fig. 5C; Live cell imaging of PIP2 lipid sensor
PMID:29975157	FYPO:0006627	Fig. 5C; Live cell imaging of PIP2 lipid sensor
PMID:29975157	FYPO:0006625	Fig. 5C; Live cell imaging of PIP2 lipid sensor
PMID:29975157	FYPO:0006623	Fig. 5B; Live cell imaging of PIP3 sensor
PMID:29975157	FYPO:0006624	Fig. 5B; Live cell imaging of PIP3 sensor
PMID:29975157	FYPO:0006623	Fig. 5B; Live cell imaging of PIP3 sensor
PMID:29975157	FYPO:0006623	Fig. 5B; Live cell imaging of PIP3 sensor
PMID:29975157	FYPO:0006624	Fig. 5B; Live cell imaging of PIP3 sensor
PMID:29975157	FYPO:0000123	Fig. S2A
PMID:29975157	FYPO:0002253	Fig. S1F; DAPI and methyl blue staining
PMID:29975157	FYPO:0002253	Fig. S1F; DAPI and methyl blue staining
PMID:29975157	PBO:0098959	Fig. S1F; DAPI and methyl blue staining
PMID:30003614	FYPO:0002061	fig 5 = cerulenin
PMID:30003614	FYPO:0004695	fig 4
PMID:30003614	FYPO:0002227	fig 4
PMID:30003614	FYPO:0006632	fig 4 normal level of free fatty acid
PMID:30003614	FYPO:0000808	increased number of lipid droples/cell fig 3b/c
PMID:30003614	FYPO:0002236	fig 4
PMID:30044717	PBO:0107418	fig S2
PMID:30044717	GO:0032153	Fig 7E
PMID:30044717	GO:0035838	Fig 7E
PMID:30044717	GO:0090689	Figure 6E
PMID:30044717	FYPO:0001581	fig 5B
PMID:30044717	FYPO:0002061	fig 5B
PMID:30044717	FYPO:0004653	Fig 5
PMID:30044717	PBO:0108998	Figure 7
PMID:30044717	PBO:0107422	Fig. S6B
PMID:30044717	PBO:0108997	Fig5D and Movie 5
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: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:0035615	Fig S4C
PMID:30044717	PBO:0107404	Fig S4C
PMID:30044717	PBO:0107403	Fig S4C
PMID:30044717	PBO:0018421	fig1
PMID:30044717	PBO:0018576	Figure 1
PMID:30044717	PBO:0019669	Fig 2B
PMID:30044717	PBO:0107401	Fig2a (vw: average survival ~ 7 cell cycles)
PMID:30053106	GO:0070336	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	FYPO:0006779	Fig. 4C. Resistant to 1mM spermidine at 37C.
PMID:30072377	FYPO:0006779	Fig. 4C Resistant to 1 mM spermidine at 37C.
PMID:30072377	PBO:0103668	Fig. 4A,B
PMID:30072439	FYPO:0002327	Revealed by thin layer chromatography
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:30072439	FYPO:0004165	Normal glucose consumption, but cell division is sensitive to low glucose condition
PMID:30072439	PBO:0096874	Lack of lipid droplet formation
PMID:30072439	PBO:0096874	Lack of lipid droplet formation
PMID:30072439	PBO:0093560	Synthetic growth defect between cwh43-G753R mutant and dga1Δ plh1Δ double deletion mutant.
PMID:30072439	PBO:0093557	Partial suppression of growth defect in the presence of sorbitol
PMID:30072439	PBO:0093558	Synthetic growth defect between cwh43-G753R mutant and dga1Δ plh1Δ double deletion mutant.
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: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	FYPO:0006970	decreased cellular diphosphoglycerate level
PMID:30072439	PBO:0093556	Suppression of temperature sensitivity by 1.2M sorbitol
PMID:30072439	FYPO:0006951	increased cellular dimethyl-histidine level during vegetative growth
PMID:30072439	FYPO:0002227	Revealed by lipidomic analysis using mass spectrometry, thin layer chromatography, and lipid droplet staining
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:30076928	PBO:0106502	RT-PCR
PMID:30076928	PBO:0106504	transcription read through by PCR
PMID:30076928	PBO:0106503	RT-PCR
PMID:30076928	PBO:0106501	transcription read through by PCR
PMID:30076928	FYPO:0000227	mini-chromosome loss assay
PMID:30089114	MOD:01148	polyubiquitylated
PMID:30089114	GO:0034080	Heterochromatin structure protects native CENP-A from ubiquitin-mediated degradation.
PMID:30089908	PBO:0096717	*******to nucleus of opposite mating type cell******
PMID:30089908	GO:0062071	go-ontology/issues/16327
PMID:30089908	PBO:0096716	******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	PBO:0096715	Fig. 1a, type IIIb
PMID:30089908	PBO:0096714	Fig. 1g
PMID:30089908	PBO:0096713	Extended data figure 1 F dominant over shk2 downstream sporulation phenotypes
PMID:30089908	FYPO:0006673	Figure 1c
PMID:30089908	FYPO:0001147	Fig. 4a, Extended Data Fig. 4c, Supplementary Video 7b
PMID:30089908	FYPO:0000678	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	abolished karyogamy with transient cytogamy (this is a bit like twin haploid meiosis? should be siblings? also looks like karyogamy failure)
PMID:30089908	PBO:0096712	Fig. 1a, type IIIb
PMID:30089908	FYPO:0002052	Fig. 4a, Extended Data Fig. 4c, Supplementary Video 7b
PMID:30089908	FYPO:0006014	Fig. 2c never ending search for mating partner
PMID:30089908	FYPO:0006014	never ending search for mating partner by P cell
PMID:30089908	PBO:0112050	Regulation of asymmetric gene expression from parental genomes Factor that regulates differential gene expression of homologous parental gene copies
PMID:30089908	FYPO:0006669	(Fig. 1a, type IIIa
PMID:30089908	GO:0140538	GO:0140538 +name: negative regulation of conjugation with zygote https://github.com/geneontology/go-ontology/issues/16329
PMID:30089908	GO:0140538	GO:0140538 +name: negative regulation of conjugation with zygote https://github.com/geneontology/go-ontology/issues/16329
PMID:30089908	GO:0005634	Extended Data Fig. 3b, Supplementary Video 5a
PMID:30089908	GO:0005634	P-cells (rapid) M-cells (delayed)
PMID:30089908	GO:0005737	M-cells
PMID:30089908	PBO:0112050	Regulation of asymmetric gene expression from parental genomes Factor that regulates differential gene expression of homologous parental gene copies
PMID:30089908	FYPO:0000413	fig 1 II
PMID:30089908	GO:0032220	Homothalic pak2∆ partners exhibit fusion efficiency decrease of ~20% as compared to wildtype partner fusion. Homothalic pak2∆ cells undergo transient fusion with frequency of ~10%, which is absent in wildtype matings.
PMID:30089908	FYPO:0001886	in M-cell
PMID:30089908	PBO:0112056	Regulation of asymmetric gene expression from parental genomes
PMID:30089908	PBO:0112056	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	FYPO:0006014	Fig. 4a, Extended Data Fig. 4c, Supplementary Video 7b
PMID:30089908	PBO:0096719	Extended Data Fig. 5e, f, Supplementary Video 9; see also ref. 1
PMID:30089908	PBO:0096718	Fig. 3d, Supplementary Video 5b
PMID:30102332	FYPO:0004903	Figures 4 & 5.
PMID:30102332	FYPO:0000650	Figure 5.
PMID:30102332	FYPO:0004903	Figures 4 & 5.
PMID:30102332	GO:0006368	also inferred from orthology, interactions, and chromatin localization (ChIP)
PMID:30102332	FYPO:0004903	Figures 4 & 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:0000650	Figure 5.
PMID:30102332	FYPO:0000650	Figure 5.
PMID:30104346	PBO:0107547	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 directly
PMID:30104346	PBO:0107548	evidence is combination of ChIP in this paper plus data in other publications showing that Rad52 binds DNA directly
PMID:30104346	PBO:0107547	evidence is combination of ChIP in this paper plus data in other publications showing that Ctp1 binds DNA directly
PMID:30110338	PBO:0111555	H3 K9me3 https://github.com/geneontology/go-ontology/issues/16331
PMID:30110338	PBO:0103520	H3 K9me3
PMID:30110338	PBO:0111554	H3 K9me3 https://github.com/geneontology/go-ontology/issues/16331
PMID:30110338	PBO:0111553	H3 K9me3 https://github.com/geneontology/go-ontology/issues/16331
PMID:30116786	PBO:0107394	Fig 4E
PMID:30116786	PBO:0112759	Fig 4E
PMID:30116786	PBO:0107392	Fig 4E
PMID:30116786	PBO:0107377	fig 3B
PMID:30116786	PBO:0018802	fig 3B
PMID:30116786	PBO:0107391	Fig 4E
PMID:30116786	FYPO:0000238	Fig. 3F loss of mitotic competence
PMID:30116786	PBO:0107395	Fig 4E
PMID:30116786	PBO:0107390	Fig 4E
PMID:30116786	FYPO:0006667	fig 3C
PMID:30116786	PBO:0107389	Fig 4E
PMID:30116786	PBO:0107388	Fig 4E
PMID:30116786	PBO:0107387	Fig 4E
PMID:30116786	PBO:0107386	Fig 4E
PMID:30116786	PBO:0107385	Fig 4E
PMID:30116786	PBO:0107384	Fig 4E
PMID:30116786	PBO:0107383	Fig 4E
PMID:30116786	PBO:0107382	Fig 4E
PMID:30116786	FYPO:0006660	Fig. 3F loss of mitotic competence
PMID:30116786	PBO:0107378	Fig 3
PMID:30116786	PBO:0107378	Fig 3
PMID:30116786	FYPO:0002552	Fig 3
PMID:30116786	FYPO:0002552	Fig 3
PMID:30116786	PBO:0107379	Fig 4A,E
PMID:30116786	PBO:0107381	Fig 4C
PMID:30116786	PBO:0107380	Fig 4E
PMID:30116786	FYPO:0006662	Fig S3
PMID:30134042	PBO:0094697	assayed at cdc18 and cdc22
PMID:30134042	PBO:0094700	assayed at cdc18 and cdc22
PMID:30134042	PBO:0094700	assayed at cdc18 and cdc22
PMID:30134042	PBO:0094697	assayed at cdc18 and cdc22
PMID:30134042	PBO:0094696	assayed at cdc18 and cdc22
PMID:30134042	PBO:0094696	assayed at cdc18 and cdc22
PMID:30134042	PBO:0094697	assayed at cdc18 and cdc22
PMID:30134042	PBO:0094697	assayed at cdc18 and cdc22
PMID:30134042	PBO:0094697	assayed at cdc18 and cdc22
PMID:30134042	PBO:0094697	assayed at cdc18 and cdc22
PMID:30134042	PBO:0094697	assayed at cdc18 and cdc22
PMID:30134042	PBO:0094701	assayed at cdc18 and cdc22
PMID:30201262	FYPO:0001904	Temperature was shifted at anaphase B.
PMID:30201262	FYPO:0007201	fig6
PMID:30201262	PBO:0107957	fig6
PMID:30201262	PBO:0107958	fig6
PMID:30201262	FYPO:0000161	Temperature was shifted at prophase or metaphase.
PMID:30201262	FYPO:0007200	fig 1.
PMID:30201262	FYPO:0002061	SFig5
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: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:0101499	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:0104166	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:0094771	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	PBO:0094771	correlation with gel shift assays
PMID:30212894	FYPO:0006658	correlation with gel shift assays
PMID:30212894	PBO:0094771	correlation with gel shift assays
PMID:30217891	FYPO:0004602	S14
PMID:30217891	PBO:0103043	fig3
PMID:30217891	PBO:0103042	fig3
PMID:30279276	PBO:0100645	Cdc42-GTP assayed with CRIB; broad zones of activity
PMID:30280012	PBO:0093577	Fig 6
PMID:30280012	FYPO:0000082	Figure S5A, S5B,
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	PBO:0093577	Fig 6
PMID:30280012	FYPO:0002177	Fig S5C, S6
PMID:30282034	PBO:0100139	at transcription_termination_signal
PMID:30282034	PBO:0095888	at transcription_termination_signal
PMID:30282034	PBO:0100139	at transcription_termination_signal
PMID:30282034	PBO:0100141	at transcription_termination_signal
PMID:30332655	PBO:0107863	inferred from phenotypes and from direct assay using human calcineurin
PMID:30348841	PBO:0094938	Nse4 sumoylation reduced in brc1Δ
PMID:30348841	PBO:0094939	Nse4 sumoylation at wild type level
PMID:30348841	PBO:0094935	physical interaction between brc1-T672A and Smc5
PMID:30348841	PBO:0094936	deletion of Nse6 strongly reduced Nse4 residence at binding sites tested under normal and genotoxic stress
PMID:30348841	PBO:0094936	deletion of Nse5 strongly reduced Nse4 residence at binding sites tested under normal and genotoxic stress
PMID:30348841	PBO:0094936	deletion of Brc1 significantly reduced Nse4 residence at binding sites tested under normal and genotoxic stress
PMID:30348841	PBO:0094937	Nse4 sumoylation undetectable in nse6Δ
PMID:30348841	PBO:0094934	physical interaction between brc1-T672A and Nse6
PMID:30348841	PBO:0094933	Nse4 foci gone in nse6 mutant cells
PMID:30348841	PBO:0094945	MMS-induced Nse4 SUMOylation was also reduced in brc1􏰀 cells but was similar to wild-type in rhp18􏰀 cells, which support normal Nse4-GFP focus formation (Fig. 4B)
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: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 stimu- late de novo Smc5-Smc6 loading
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 stimu- late de novo Smc5-Smc6 loading
PMID:30348841	PBO:0093580	nse2-SA brc1􏰀 cells are more sensitive to genotoxins than either single mutant (Fig. 4C).
PMID:30348841	PBO:0094940	mutations in brc1 weaken interaction with nse6
PMID:30348841	PBO:0094932	fig 1 brc1 mutant cells expressing brc1-T672A are deficient in Nse4 foci formation
PMID:30348841	PBO:0094933	Nse4 foci gone in nse6 mutant cells
PMID:30348841	PBO:0094933	fig 1 a: brc1 mutant abolishes Nse4 nuclear foci in HU/MMS treated cells
PMID:30355493	PBO:0105005	2d
PMID:30355493	PBO:0105007	2d
PMID:30355493	PBO:0105006	2d
PMID:30355493	PBO:0105004	2d
PMID:30355493	PBO:0105008	2d
PMID:30355493	PBO:0105002	2d
PMID:30355493	PBO:0105003	2d
PMID:30355493	PBO:0105003	2d
PMID:30355493	PBO:0105009	3c
PMID:30355493	PBO:0105002	2d
PMID:30355493	PBO:0105005	fig4
PMID:30355493	PBO:0105001	S3C
PMID:30355770	FYPO:0001045	Fig. 7D
PMID:30355770	FYPO:0003267	Fig. 7D
PMID:30355770	FYPO:0002243	Fig. S5
PMID:30355770	PBO:0108848	Fig. S5
PMID:30355770	FYPO:0002243	Fig. 4B
PMID:30355770	PBO:0108849	Fig. 4B
PMID:30355770	PBO:0108849	Fig. 4B
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	PBO:0108846	Fig. 2B
PMID:30355770	PBO:0108845	Fig. 2B
PMID:30355770	PBO:0108844	Fig. 2B
PMID:30355770	PBO:0108843	Fig. 2B
PMID:30355770	FYPO:0002243	Fig. 2A
PMID:30355770	FYPO:0001045	Fig. 2A
PMID:30355770	FYPO:0001045	Fig. 2A
PMID:30355770	FYPO:0001045	Fig. 2A
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:0002061	Fig. S8
PMID:30355770	FYPO:0002061	Fig. S8
PMID:30355770	FYPO:0001045	Fig. 4B
PMID:30355770	FYPO:0002060	Fig. S8
PMID:30355770	FYPO:0003267	Fig. 7D
PMID:30355770	FYPO:0003267	Fig. 7D
PMID:30355770	FYPO:0003267	Fig. 7D
PMID:30355770	FYPO:0001045	Fig. 2A
PMID:30355770	FYPO:0001045	Fig. 2A
PMID:30355770	FYPO:0003267	Fig. 2A
PMID:30355770	FYPO:0001045	Fig. 7D
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	PBO:0108847	Fig. S6
PMID:30355770	PBO:0108847	Fig. S6
PMID:30355770	PBO:0108847	Fig. S6
PMID:30355770	FYPO:0001045	Fig. S5
PMID:30355770	FYPO:0003267	Fig. 2A
PMID:30389790	PBO:0093561	fig 2b
PMID:30389790	PBO:0093561	fig 5b
PMID:30389790	PBO:0095685	fig 5b
PMID:30389790	FYPO:0001910	figure 5c hypoglycosylation
PMID:30389790	PBO:0095685	fig 5b
PMID:30389790	FYPO:0001211	fig 6
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	PBO:0095685	fig 5b
PMID:30389790	PBO:0095634	fig 5b
PMID:30389790	FYPO:0001211	fig 6
PMID:30389790	FYPO:0007030	fig S4
PMID:30389790	FYPO:0006981	fig S4
PMID:30389790	FYPO:0000805	fig 10
PMID:30389790	FYPO:0001035	fig 10
PMID:30389790	FYPO:0006982	fig 10
PMID:30389790	FYPO:0002060	figure 5 and 11 (no loss of viability )
PMID:30389790	FYPO:0001357	figure 5b and S2
PMID:30389790	FYPO:0001124	figure 5c
PMID:30389790	FYPO:0000672	figure 5c
PMID:30389790	FYPO:0001211	fig 6
PMID:30389790	PBO:0093560	fig 2b
PMID:30393157	FYPO:0003004	fig 4
PMID:30393157	PBO:0094526	table2
PMID:30393157	PBO:0094525	table2
PMID:30393157	PBO:0094534	table2
PMID:30393157	PBO:0094533	table2
PMID:30393157	PBO:0094532	table2
PMID:30393157	PBO:0094531	table2
PMID:30393157	PBO:0094530	table2
PMID:30393157	PBO:0094529	table2
PMID:30393157	PBO:0094528	table2
PMID:30393157	PBO:0094524	table2
PMID:30393157	PBO:0094547	Fig. 5A
PMID:30393157	PBO:0094546	Fig. 5A
PMID:30393157	PBO:0094545	Fig. 5A
PMID:30393157	PBO:0094544	Fig. 5A
PMID:30393157	PBO:0094527	table2
PMID:30393157	PBO:0094543	Fig. 5A
PMID:30393157	PBO:0094542	Fig. 5A
PMID:30393157	PBO:0094541	Fig. 5A
PMID:30393157	PBO:0094540	table2
PMID:30393157	PBO:0094539	table2
PMID:30393157	PBO:0094538	table2
PMID:30393157	PBO:0094537	table2
PMID:30393157	PBO:0094536	table2
PMID:30393157	PBO:0094535	table2
PMID:30393157	PBO:0094523	table2
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	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	FYPO:0005823	Fig. 2C/D
PMID:30393157	FYPO:0005823	Fig. 2C/D
PMID:30393157	FYPO:0002061	Fig. 2B
PMID:30393157	FYPO:0002061	Fig. 2B
PMID:30393157	FYPO:0002061	Fig. 2B
PMID:30393157	FYPO:0002061	Fig. 2B
PMID:30393157	PBO:0094522	fig 1C/D
PMID:30393157	FYPO:0005823	fig 1A
PMID:3040264	FYPO:0003145	fig 2 b (uncondensed chromosomes)
PMID:3040264	FYPO:0000620	fig 2 a no spindle rod like chromsomes
PMID:3040264	FYPO:0002018	fig 2 a no spindle rod like chromsomes
PMID:3040264	FYPO:0001683	2b
PMID:3040264	GO:0007076	fig 2 B
PMID:3040264	PBO:0037113	fig 2 b (uncondensed chromosomes)
PMID:3040264	PBO:0037114	table1
PMID:3040264	PBO:0037115	table1
PMID:3040264	PBO:0037116	table1
PMID:3040264	FYPO:0002071	fig 2 a
PMID:3040264	FYPO:0001683	fig 2 a no spindle rod like chromsomes
PMID:30427751	PBO:0108000	figure 5A
PMID:30427751	FYPO:0005686	figure6AC
PMID:30427751	FYPO:0004511	figure6D
PMID:30427751	PBO:0108003	figure 5I
PMID:30427751	PBO:0108004	figure6AC
PMID:30427751	PBO:0108002	figure 5GH
PMID:30427751	PBO:0107999	Therefore, we concluded that Rsp1 is required to prevent excessive accumulation of Mto1
PMID:30427751	PBO:0107999	Therefore, we concluded that Rsp1 is required to prevent excessive accumulation of Mto1
PMID:30427751	PBO:0107998	figure 2 B
PMID:30427751	PBO:0107996	figure 2 A with increased loc to spb
PMID:30427751	PBO:0107995	figure 2 B
PMID:30427751	PBO:0107994	figure 2 A with increased loc to spb
PMID:30427751	FYPO:0000234	figure 1 G/H (from preexisting microtubules)
PMID:30427751	FYPO:0005558	figure 1
PMID:30427751	PBO:0107997	figure 2 B
PMID:30427751	GO:0005515	fig 5A (recruitment)
PMID:30427751	PBO:0108001	figure 5A
PMID:30451685	FYPO:0001245	Figures 2C, 2D, and Figure 2—figure supplement 2
PMID:30451685	FYPO:0006784	Figure 3—figure supplement 1B, 2B; assayed__using cpy1
PMID:30451685	PBO:0108008	Figure 3—figure supplement 1A, 2B
PMID:30451685	PBO:0108009	Figure 3—figure supplement 1A, 2B
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:0004247	Figure 4C,D
PMID:30451685	PBO:0108008	Figure 4B
PMID:30451685	PBO:0108016	Figure 4B
PMID:30451685	PBO:0108016	Figure 4B
PMID:30451685	PBO:0108010	Figure 4B
PMID:30451685	PBO:0108010	Figure 4B
PMID:30451685	PBO:0108010	Figure 4B
PMID:30451685	PBO:0108010	Figure 4B
PMID:30451685	PBO:0108015	Figure 4—figure supplement 1B; isothermal titration calorimetry (ITC)
PMID:30451685	PBO:0108015	Figure 4—figure supplement 1B; isothermal titration calorimetry (ITC)
PMID:30451685	PBO:0108015	Figure 4A; isothermal titration calorimetry (ITC)
PMID:30451685	PBO:0108015	Figure 4—figure supplement 1B; isothermal titration calorimetry (ITC)
PMID:30451685	PBO:0108015	Figure 4—figure supplement 1B; isothermal titration calorimetry (ITC)
PMID:30451685	PBO:0108014	Figure 4A; isothermal titration calorimetry (ITC)
PMID:30451685	PBO:0108013	Figure 4—figure supplement 1C; isothermal titration calorimetry (ITC)
PMID:30451685	PBO:0108013	Figure 4A; isothermal titration calorimetry (ITC)
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	FYPO:0006784	Figure 3—figure supplement 1B, 2B; assayed_using cpy1
PMID:30451685	FYPO:0006784	Figure 3—figure supplement 1B, 2B; assayed_using cpy1
PMID:30451685	FYPO:0006784	Figure 3—figure supplement 1B, 2B; assayed_using cpy1
PMID:30451685	FYPO:0006784	Figure 3—figure supplement 1B, 2B; assayed_using cpy1
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; isothermal titration calorimetry (ITC)
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	GO:0000329	Figure 1 (direct assay for vacuolar membrane) and Figure 1-figure supplement 1 (sequence feature evidence for transmembrane)
PMID:30451685	GO:0007033	Figure 2 and Figure 2-figure supplement 1
PMID:30451685	GO:0007033	Figure 2
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	PBO:0108005	Figures 2A and 2B; assayed_using cpy1
PMID:30451685	FYPO:0000116	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:0006579	Figures 2C, 2D, and Figure 2—figure supplement 2
PMID:30451685	PBO:0108006	Figures 2A and 2B; assayed_using cpy1
PMID:30451685	FYPO:0000116	Figures 2C, 2D, and Figure 2—figure supplement 2
PMID:30451685	PBO:0108009	Figure 3—figure supplement 1A, 2B
PMID:30451685	FYPO:0006579	Figures 2C, 2D, and Figure 2—figure supplement 2; same as either single mutant
PMID:30451685	FYPO:0001245	Figures 2C, 2D, and Figure 2—figure supplement 2; same as either single mutant
PMID:30451685	FYPO:0000116	Figures 2C, 2D, and Figure 2—figure supplement 2; 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:0006786	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	FYPO:0006786	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	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; assayed_using cpy1
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:30462301	FYPO:0006366	Figure 3B and Supplementary Figure S6
PMID:30462301	FYPO:0004791	Figure 3A
PMID:30462301	FYPO:0006515	Supple- mentary Figure S5B
PMID:30462301	PBO:0103847	Supple- mentary Figure S4A)
PMID:30462301	PBO:0103847	Supple- mentary Figure S4A)
PMID:30462301	PBO:0100089	Figure 2C, D, Supple- mentary Figure S3A and C
PMID:30462301	PBO:0100089	Figure 2C, D, Supple- mentary Figure S3A and C
PMID:30462301	PBO:0100089	(Fig- ure 2D, Supplementary Figure S3B and C
PMID:30462301	PBO:0100089	(Fig- ure 2D, Supplementary Figure S3B and C
PMID:30462301	PBO:0103846	Figure 2C, Supplementary Figure S3A and C
PMID:30462301	PBO:0100089	Figure 2C, Supplementary Figure S3A and C
PMID:30462301	PBO:0100089	Figure 2C, Supplementary Figure S3A and C
PMID:30462301	PBO:0100088	Supplementary Figure S1A-E
PMID:30462301	FYPO:0006515	Supple- mentary Figure S5B
PMID:30462301	PBO:0103856	Figure 6B and Supple- mentary Figure S8B
PMID:30462301	PBO:0103856	Figure 6B and Supplementary Figure S8C)
PMID:30462301	PBO:0103855	Figure 6B and Supplementary Fig- ure S8B
PMID:30462301	PBO:0103855	Figure 6B and Supplementary Fig- ure S8B
PMID:30462301	PBO:0103855	Figure 6B and Supplementary Fig- ure S8B
PMID:30462301	GO:0005515	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	FYPO:0004791	Figure 3A
PMID:30462301	PBO:0103853	Figure 4A
PMID:30462301	PBO:0103853	Supplementary Figure S7E
PMID:30462301	PBO:0103852	Figure 4A
PMID:30462301	FYPO:0004791	Figure 3A
PMID:30462301	PBO:0103852	Figure 4A
PMID:30462301	PBO:0103852	Figure 4A
PMID:30462301	GO:0005515	competatively with sad1
PMID:30462301	FYPO:0004791	Figure 3A
PMID:30462301	PBO:0100093	suggested by Junko
PMID:30462301	PBO:0100089	Figure 6B and Supplementary Figure S8C
PMID:30462301	PBO:0103851	Supplementary Figure S7A-D)
PMID:30462301	FYPO:0001894	Figure 3
PMID:30462301	PBO:0103856	Figure 6B and Supple- mentary Figure S8B
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:0006515	Supple- mentary Figure S5B
PMID:30462301	FYPO:0006515	Supple- mentary Figure S5B
PMID:30462301	FYPO:0006515	Supple- mentary Figure S5B
PMID:30462301	PBO:0103848	Supple- mentary Figure S4A)
PMID:30462301	PBO:0103848	Figure 2E and Supple- mentary Figure S4B
PMID:30462301	FYPO:0006366	Figure 3B and Supplementary Figure S6
PMID:30462301	FYPO:0000172	Figure 3B and Supplementary Figure S6
PMID:30462301	PBO:0103847	Supple- mentary Figure S4A)
PMID:30463883	PBO:0102980	figure 2 AB
PMID:30463883	PBO:0102980	figure 2 AB
PMID:30463883	FYPO:0002060	at 33 degrees Celsius
PMID:30463883	FYPO:0002060	at 33 degrees Celsius
PMID:30463883	FYPO:0002060	at 33 degrees Celsius
PMID:30463883	FYPO:0002060	at 36 degrees Celsius
PMID:30463883	FYPO:0002060	at 33 degrees Celsius
PMID:30463883	FYPO:0002060	at 36 degrees Celsius
PMID:30463883	FYPO:0002060	at 36 degrees Celsius
PMID:30463883	FYPO:0002060	at 36 degrees Celsius
PMID:30463883	FYPO:0002060	at 36 degrees Celsius
PMID:30463883	FYPO:0002060	at 36 degrees Celsius
PMID:30463883	PBO:0102980	figure 2 AB
PMID:30463883	PBO:0102980	figure 2 AB
PMID:30463883	FYPO:0006884	The mitotic spindle has two poles but is thicker than normal.
PMID:30463883	FYPO:0006884	The mitotic spindle has two poles but is thicker than normal.
PMID:30463883	PBO:0102981	figure 2 AB
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	PBO:0019133	when wtf13 antidote not present (homozygous, wtf13poison/wtf13+, or wtf13poison/wtf13Δ
PMID:30475921	FYPO:0006790	suppresses wtf13 drive
PMID:30475921	PBO:0092298	wtf18-2 allele assayed
PMID:30475921	FYPO:0006793	wtf13 driver, wtf18 suppressor
PMID:30475921	FYPO:0006793	wtf13 driver, wtf18 suppressor
PMID:30475921	FYPO:0006793	wtf13 driver, wtf18 suppressor
PMID:30475921	FYPO:0006793	wtf13 driver, wtf18 suppressor
PMID:30503780	FYPO:0000590	(transeferred from Junk's session PMID:30462301)
PMID:30503780	PBO:0100089	figure 2D
PMID:30503780	GO:0003677	figure3 (incompatible with rap1 binding)
PMID:30503780	FYPO:0000658	fig4
PMID:30503780	PBO:0100089	figure 2D
PMID:30503780	PBO:0100089	figure 2D
PMID:30503780	PBO:0100088	fig 2 D
PMID:30503780	FYPO:0004791	Figures 5A and 5B
PMID:30503780	FYPO:0000658	fig4
PMID:30503780	GO:0005515	incompatible with DNA binding
PMID:30503780	FYPO:0005612	fig S5B
PMID:30503780	FYPO:0005612	fig S5B
PMID:30503780	FYPO:0002687	fig S5B (southern blot)
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	(transeferred from Junk's session PMID:30462301)
PMID:30503780	PBO:0100092	(transeferred from Junk's session PMID:30462301)
PMID:30503780	PBO:0100093	(transeferred from Junk's session PMID:30462301)
PMID:30528393	GO:0005829	although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA
PMID:30528393	GO:0005739	although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA
PMID:30528393	GO:0005829	although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA
PMID:30528393	GO:0005739	although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA
PMID:30530492	GO:0140351	glucosylceramide, galactosylceramide
PMID:30530492	FYPO:0000464	glycosphingolipid transport
PMID:30573453	PBO:0096189	(Figure S7)
PMID:30573453	PBO:0096188	(Figure S7)
PMID:30573453	PBO:0096302	fig6
PMID:30573453	PBO:0096189	FIgure S7
PMID:30573453	FYPO:0000967	fig6
PMID:30573453	FYPO:0006814	fig6
PMID:30573453	FYPO:0000966	fig6
PMID:30573453	PBO:0095834	fig6
PMID:30573453	FYPO:0003411	fig6
PMID:30573453	FYPO:0003575	fig5
PMID:30573453	PBO:0094679	(Figure 2c)
PMID:30573453	PBO:0095652	(Figure 2c)
PMID:30573453	FYPO:0000833	2d
PMID:30573453	FYPO:0000703	2d
PMID:30573453	PBO:0096291	(Figure 2c)
PMID:30573453	PBO:0096297	fig6
PMID:30573453	PBO:0096296	fig6
PMID:30573453	FYPO:0003574	fig5
PMID:30573453	FYPO:0000966	fig5
PMID:30573453	PBO:0096295	fig5
PMID:30573453	FYPO:0003575	fig5
PMID:30573453	FYPO:0006814	fig5
PMID:30573453	PBO:0095652	(Figure 3a)
PMID:30573453	FYPO:0002336	(Figure 3a)
PMID:30573453	FYPO:0002336	(Figure 3a)
PMID:30573453	PBO:0096294	(Figure 4c)
PMID:30573453	PBO:0094679	(Figure 4d)
PMID:30573453	PBO:0096292	FIgure 4C
PMID:30573453	PBO:0094282	FIgure S4
PMID:30573453	PBO:0095834	fig6
PMID:30573453	PBO:0094679	(Figure 2c)
PMID:30573453	PBO:0096301	(figure S8)
PMID:30573453	PBO:0096300	(Figure S8)
PMID:30573453	PBO:0096299	FIgure S8
PMID:30573453	PBO:0096298	FIgure S8
PMID:30573453	FYPO:0006814	fig6
PMID:30601114	PBO:0101038	figure 2 B
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	GO:1905762	Figure 1–figure supplement 1A
PMID:30601114	GO:1905762	Figure 1–figure supplement 1A
PMID:30601114	PBO:0101033	Figure 1–figure supplement 1B/Figure 1–figure supplement 1C
PMID:30601114	GO:0062104	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 2 B
PMID:30601114	PBO:0101038	figure 2 B
PMID:30601114	PBO:0101039	figure 2 B
PMID:30601114	PBO:0101039	figure 2 B
PMID:30601114	PBO:0101038	figure 2
PMID:30601114	PBO:0101038	figure 2 B
PMID:30601114	FYPO:0006809	figure 2 B
PMID:30601114	FYPO:0006809	figure 2 B
PMID:30601114	FYPO:0006809	figure 2 B
PMID:30601114	PBO:0101038	figure 2 B
PMID:30602572	PBO:0096097	Figure 2C the mitochondria have a fission frequency that is almost double that of wild-type
PMID:30602572	FYPO:0000895	(Fig. S5B) Furthermore, in Klp4􏰀 cells, which typically contain sev- eral short mitochondria (Fig. 1A), absence of Dnm1 results in a single large, fused mitochondrion
PMID:30602572	FYPO:0003820	Fig 1C observed that Klp5􏰀/Klp6􏰀 contained only 2.3 􏰁 0.4 (mean 􏰁 S.E.).
PMID:30602572	FYPO:0003810	WT cells highly overex- pressing Dnm1 had 11.6 􏰁 0.2 mitochondria (mean 􏰁 S.E.), which is twice that of WT cells
PMID:30602572	PBO:0109849	We counted 23.3 􏰁 1.4 (mean 􏰁 S.E.) mitochondria in Klp5􏰀/Klp6􏰀 cells lacking Mmb1􏰀 (Fig. 6C), which was not significantly different from Mmb1􏰀 cells
PMID:30602572	PBO:0109848	Figure 6C-D Increased mitochondrial numbers and decreased mitochondrial sizes with overall mitochondrial volume same as what is observed in wild-type cells
PMID:30602572	FYPO:0007196	Klp5􏰀/Klp6􏰀 cells exhibited a fission frequency that was half that of WT
PMID:30602572	PBO:0096095	Figure 6B
PMID:30602572	PBO:0096096	Figure 1B the anti-parallel microtubule bundles are only about half the length of wild-type bundles
PMID:30602572	PBO:0109848	Figure 1C-D
PMID:30626735	PBO:0093620	200 Gy; Andres SN et al. (2019)
PMID:30626735	PBO:0101188	Andres SN et al. (2019)
PMID:30626735	PBO:0093630	75 J/m^2; Andres SN et al. (2019)
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 sig- nal (Figure 2A), suggesting an increase in Cnp1-GFP levels.
PMID:30635289	PomGeneEx:0000018	Cnp1-GFP protein increases ap- proximately twofold at 165-min postelutriation. This resulindicates that the mRNA increase in G1 results in augmenta- tion 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: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 chromo- somes, chromosome bridges, and also unequal nuclei segre- gation 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 sig- nal (Figure 2A), suggesting an increase in Cnp1-GFP levels.
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 sig- nal (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 chromo- somes, chromosome bridges, and also unequal nuclei segre- gation 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 sig- nal (Figure 2A), suggesting an increase in Cnp1-GFP levels.
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:0113858	ChIP analysis showed that Nrm1, Yox1, and Res2 bind to the cnp1 promoter (Figure 4B).
PMID:30635289	PBO:0113848	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromo- somes, chromosome bridges, and also unequal nuclei segre- gation during mitosis (Figure 2C and Figure S4).
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 chromo- somes, chromosome bridges, and also unequal nuclei segre- gation during mitosis (Figure 2C and Figure S4).
PMID:30635289	PBO:0113856	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromo- somes, chromosome bridges, and also unequal nuclei segre- gation during mitosis (Figure 2C and Figure S4).
PMID:30635289	PBO:0113855	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromo- somes, chromosome bridges, and also unequal nuclei segre- gation during mitosis (Figure 2C and Figure S4).
PMID:30635289	PBO:0113854	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromo- somes, chromosome bridges, and also unequal nuclei segre- gation during mitosis (Figure 2C and Figure S4).
PMID:30635289	PBO:0033884	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromo- somes, chromosome bridges, and also unequal nuclei segre- gation during mitosis (Figure 2C and Figure S4).
PMID:30635289	PBO:0113853	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromo- somes, chromosome bridges, and also unequal nuclei segre- gation during mitosis (Figure 2C and Figure S4).
PMID:30635289	PBO:0113852	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromo- somes, chromosome bridges, and also unequal nuclei segre- gation 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 sig- nal (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 sig- nal (Figure 2A), suggesting an increase in Cnp1-GFP levels.
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	FYPO:0000228	ICRF-193, a bisdioxopiperazine derivative [meso-4,4-(2,3-butanediyl)-bis (2,6-piperazinedione)], is 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:30635402	MOD:00046	Identified by mass spectrometry
PMID:30635402	MOD:00046	Identified by mass spectrometry
PMID:30635402	MOD:00047	Identified by mass spectrometry
PMID:30635402	MOD:00046	Identified by mass spectrometry
PMID:30635402	MOD:00046	Identified by mass spectrometry
PMID:30635402	MOD:00046	Identified by mass spectrometry
PMID:30635402	PBO:0106862	also assayed directly using human CKII
PMID:30639107	PBO:0096312	Fig. 1E
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:0096311	Fig. 1E
PMID:30639107	PBO:0114675	Fig. 1C
PMID:30639107	FYPO:0001392	Fig. 3
PMID:30639107	PBO:0114679	Fig. 1E
PMID:30639107	PBO:0114678	Fig. 1E
PMID:30639107	PBO:0114677	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:0098148	Fig. 1E
PMID:30640914	PBO:0103599	Cellular fractionation; affecting Rec25
PMID:30640914	PBO:0103591	Recombination assay; assayed region: leu1-his5 interval
PMID:30640914	PBO:0103592	mbs1 hotspot quantification
PMID:30640914	PBO:0103593	Recombination assay; assayed region: ade6 gene
PMID:30640914	PBO:0103594	Recombination assay; assayed region: leu1-his5 interval
PMID:30640914	PBO:0103592	mbs1 hotspot quantification
PMID:30640914	PBO:0103595	Recombination assay; assayed region: ade6 gene
PMID:30640914	PBO:0103596	Recombination assay; assayed region: leu1-his5 interval
PMID:30640914	PBO:0103597	mbs1 hotspot quantification
PMID:30640914	PBO:0103598	mbs1 hotspot quantification
PMID:30640914	PBO:0103593	Recombination assay; assayed region: ade6 gene
PMID:30640914	PBO:0102476	Recombination assay; assayed region: ade6 gene
PMID:30640914	PBO:0103593	Recombination assay; assayed region: ade6 gene
PMID:30640914	PBO:0103593	Recombination assay; assayed region: ade6 gene
PMID:30640914	FYPO:0004993	s1
PMID:30640914	FYPO:0006841	S2
PMID:30640914	FYPO:0005650	fig s4
PMID:30640914	FYPO:0004610	fig8
PMID:30640914	FYPO:0006838	Rec25 visualization
PMID:30640914	PBO:0102476	Recombination assay; assayed region: ade6 gene
PMID:30640914	PBO:0103595	Recombination assay; assayed region: ade6 gene
PMID:30640914	PBO:0103595	Recombination assay; assayed region: ade6 gene
PMID:30640914	PBO:0103595	Recombination assay; assayed region: ade6 gene
PMID:30640914	PBO:0103599	Cellular fractionation; affecting Rec25
PMID:30640914	PBO:0102476	Recombination assay; assayed region: ade6 gene
PMID:30640914	PBO:0103599	Cellular fractionation; affecting Rec25
PMID:30640914	PBO:0103592	mbs1 hotspot quantification
PMID:30640914	PBO:0103595	Recombination assay; assayed region: ade6 gene
PMID:30640914	PBO:0103596	Recombination assay; assayed region: leu1-his5 interval
PMID:30640914	PBO:0103598	mbs1 hotspot quantification
PMID:30640914	FYPO:0006838	Rec25 visualization
PMID:30640914	FYPO:0006838	Rec25 visualization
PMID:30640914	PBO:0102476	Recombination assay; assayed region: ade6 gene
PMID:30640914	FYPO:0005650	S4
PMID:30640914	FYPO:0004610	fig8
PMID:30640914	PBO:0103598	mbs1 hotspot quantification
PMID:30640914	FYPO:0005650	S2
PMID:30640914	FYPO:0004628	S2
PMID:30640914	FYPO:0004628	S2
PMID:30640914	FYPO:0000581	S1A
PMID:30640914	FYPO:0004993	S1A
PMID:30640914	FYPO:0004993	S1A
PMID:30640914	FYPO:0004993	S1A
PMID:30640914	PBO:0102476	Recombination assay; assayed region: ade6 gene
PMID:30640914	PBO:0102476	Recombination assay; assayed region: ade6 gene
PMID:30646830	PBO:0095187	abolished tRNA C34, C48 methylation (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:30646830	GO:0016428	trm402 (Trm4b) methylates C49 and C50 of tRNAs
PMID:30646830	PBO:0095187	Abolished tRNA cytosine-5 methylation of C49 and C50 (tRNA bisulphite sequencing)
PMID:30649994	PBO:0108066	3E
PMID:30649994	FYPO:0006896	3E
PMID:30649994	GO:1901612	Supplemental Figure S2
PMID:30649994	PBO:0018826	4b
PMID:30649994	FYPO:0006896	3E
PMID:30649994	GO:0070300	Supplemental Figure S2
PMID:30649994	PBO:0108065	S3
PMID:30649994	PBO:0108066	3E
PMID:30652128	PBO:0103455	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096838	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096838	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096838	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096838	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096839	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096838	Monitoring an extra-chromosome ChL
PMID:30652128	FYPO:0001740	rpd1-S7A increased the rate of gross chromosomal rearrangement in the otherwise wild-type background. Monitoring an extra-chromosome ChL
PMID:30652128	FYPO:0006811	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0094685	rpd1-S7A reduced centromere noncoding RNA in the clr4∆ strain. Northern blot assay
PMID:30652128	FYPO:0001742	Pulse-field gel electrophoresis (PFGE), Polymerase chain reaction (PCR), Monitoring an extra-chromosome ChL
PMID:30652128	FYPO:0001742	Pulse-field gel electrophoresis (PFGE), Polymerase chain reaction (PCR), Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0094685	tfs1∆ reduced centromere noncoding RNA in the clr4∆ strain. Northern blot assay
PMID:30652128	FYPO:0001742	Pulse-field gel electrophoresis (PFGE), Polymerase chain reaction (PCR), Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096842	Monitoring an extra-chromosome ChL
PMID:30652128	FYPO:0006810	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096842	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096842	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096838	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096842	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096839	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096839	Monitoring an extra-chromosome ChL
PMID:30652128	FYPO:0006811	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096838	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096838	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096842	Monitoring an extra-chromosome ChL
PMID:30652128	FYPO:0006811	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096838	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096842	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096839	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096839	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096839	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096842	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096838	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096839	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096838	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096842	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096842	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096842	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096839	Monitoring an extra-chromosome ChL
PMID:30652128	FYPO:0006811	Monitoring an extra-chromosome ChL
PMID:30652128	FYPO:0006811	Monitoring an extra-chromosome ChL
PMID:30652128	FYPO:0006811	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096839	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096842	Monitoring an extra-chromosome ChL
PMID:30652128	FYPO:0006811	Monitoring an extra-chromosome ChL
PMID:30652128	FYPO:0006811	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096842	Monitoring an extra-chromosome ChL
PMID:30652128	FYPO:0006811	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0096839	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0093563	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0103454	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0103454	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0103454	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0103455	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0103455	Monitoring an extra-chromosome ChL
PMID:30652128	PBO:0103456	Monitoring an extra-chromosome ChL
PMID:30658998	FYPO:0006034	supressed dna fragmentation
PMID:30658998	FYPO:0006911	fig 1B
PMID:30658998	FYPO:0006913	fig 1B
PMID:30658998	FYPO:0006914	fig 1B
PMID:30658998	FYPO:0003769	fig 1D supressed by hexestrol or clomifene
PMID:30658998	FYPO:0006034	supressed dna fragmentation
PMID:30658998	FYPO:0001355	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 supressed by hexestrol
PMID:30659798	GO:0008017	fig2
PMID:30659798	GO:0003777	fig 2f
PMID:30667359	FYPO:0007006	Figure 6C
PMID:30667359	FYPO:0006920	Figure 6B
PMID:30667359	FYPO:0007005	Figure 6C
PMID:30667359	FYPO:0007005	Figure 2B
PMID:30667359	FYPO:0007006	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:0007007	Figure 6C
PMID:30667359	FYPO:0007006	Figure 6C
PMID:30667359	FYPO:0007007	Figure 6c
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	PBO:0102223	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
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:0102221	No queuosine-mediated reduction of translational errors at GGC (Gly) and UGC (Tyr) codons
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:0102226	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
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	GO:1990145	... Q-modification in tRNAs is to improve translation ofC-ending codons relative to U-ending codons in S. pombe.
PMID:30726745	FYPO:0001903	Figure 7C, 7D
PMID:30726745	FYPO:0001903	Figure 7C, 7D
PMID:30726745	FYPO:0001045	Figure 7A
PMID:30726745	GO:1902716	Figure 6
PMID:30726745	PBO:0095261	Figure 1
PMID:30726745	PBO:0095262	Figure 2, Figure 3.
PMID:30726745	PBO:0095263	Figure S5
PMID:30726745	FYPO:0001045	Figure 7A
PMID:30726745	PBO:0095263	Figure 7C, 7D
PMID:30726745	PBO:0095262	Figure 2, Figure 3
PMID:30726745	FYPO:0001903	Figure 7C, 7D
PMID:30726745	FYPO:0001045	Figure 7A
PMID:30726745	FYPO:0003267	Figure 7A
PMID:30759079	FYPO:0006927	Fig6 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: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	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:0006927	Fig6 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:0002256	data not shown
PMID:30759079	FYPO:0006927	Fig6 The nuclear envelope is marked with Cut11-GFP
PMID:30759238	FYPO:0003353	Fig. 3C
PMID:30759238	FYPO:0003353	Fig. 3C
PMID:30759238	PBO:0093560	Fig. S6D
PMID:30759238	PBO:0093560	Fig. S6D
PMID:30759238	PBO:0112932	Fig. 6
PMID:30759238	PBO:0112933	Fig. 6
PMID:30759238	PBO:0112926	Fig. S9B
PMID:30759238	PBO:0112927	Fig. S9B
PMID:30759238	PBO:0112927	Fig. S9B
PMID:30759238	FYPO:0000472	Fig. S9B
PMID:30759238	FYPO:0003353	Fig. 3C
PMID:30759238	FYPO:0003353	Fig. 3C
PMID:30759238	PBO:0112926	Fig. 3B
PMID:30759238	PBO:0112926	Fig. 3B
PMID:30759238	PBO:0112927	Fig. 3B
PMID:30759238	PBO:0112928	Fig. 3B
PMID:30759238	PBO:0112929	Fig. 3B
PMID:30759238	PBO:0112929	Fig. 3B
PMID:30759238	PBO:0112929	Fig. S6B
PMID:30759238	PBO:0112929	Fig. S6B
PMID:30759238	PBO:0112929	Fig. S6B
PMID:30759238	PBO:0112929	Fig. S6B
PMID:30759238	PBO:0112926	Fig. S6B
PMID:30759238	PBO:0112931	Fig. 5
PMID:30759238	PBO:0112930	Fig. 4D
PMID:30759238	PBO:0112930	Fig. 4D
PMID:30759238	PBO:0112930	Fig. 4D
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:0112929	Fig. 4B
PMID:30759238	PBO:0112928	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	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. S6C
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	PBO:0112928	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. S6D
PMID:30759238	PBO:0093560	Fig. S6D
PMID:30759238	PBO:0093560	Fig. S6D
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	PBO:0112927	Fig. 4B
PMID:30759238	FYPO:0003353	Fig. 3C
PMID:30759238	FYPO:0003353	Fig. 3C
PMID:30773398	FYPO:0006858	Figure S2
PMID:30773398	GO:0005634	Fig 1a
PMID:30773398	GO:0005737	Fig 1a
PMID:30773398	PBO:0101841	Figs 1B, 1D, 1F, S1, S2
PMID:30773398	PBO:0101842	Figs 1B, 1D, 1F, S1, S2
PMID:30773398	PBO:0101843	Figs 1B, 1D, 1F, S1, S2
PMID:30773398	PBO:0033658	Fig 3
PMID:30773398	GO:0005515	homodimer
PMID:30773398	FYPO:0006858	Figure S2
PMID:30773398	FYPO:0006858	Figure S2
PMID:30773398	FYPO:0006858	Figure S2
PMID:30773398	FYPO:0006858	Figure S2
PMID:30773398	FYPO:0006858	Figure S2
PMID:30773398	FYPO:0006857	Figure 1E
PMID:30773398	FYPO:0006857	Figure 1E
PMID:30773398	FYPO:0002919	Figure 1E
PMID:30773398	FYPO:0002919	Figure 1E
PMID:30773398	GO:0046975	Figs 1C, S1
PMID:30796050	PBO:0093634	Fig EV3; restrictive temperature for cdc2-M68
PMID:30796050	PBO:0093632	Fig 1
PMID:30796050	PBO:0104035	Fig 1
PMID:30796050	PBO:0095229	Fig 1
PMID:30796050	PBO:0104036	Fig 2
PMID:30796050	FYPO:0005402	Fig 2, S2
PMID:30796050	PBO:0104037	Fig 3
PMID:30796050	FYPO:0006859	Fig 3; less intense Y arc in 2D gel
PMID:30796050	FYPO:0006860	Fig 3; less intense Y arc in 2D gel
PMID:30796050	PBO:0097407	Fig 4
PMID:30796050	PBO:0104038	Fig 4
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 S3
PMID:30796050	PBO:0093632	Fig S3
PMID:30796050	PBO:0104041	also inferred from orthology and various genetic interactions
PMID:30796050	PBO:0093632	Fig 1
PMID:30796050	PBO:0097410	Fig 3
PMID:30796050	PBO:0104037	Fig EV3
PMID:30796050	PBO:0104039	Fig EV3
PMID:30796050	PBO:0093632	Fig 4
PMID:30796050	PBO:0093632	Fig 4
PMID:30796050	PBO:0093632	Fig S3
PMID:30796050	PBO:0093632	Fig 2
PMID:30796050	PBO:0093632	Fig 2
PMID:30796050	PBO:0093632	Fig 3
PMID:30796050	PBO:0093634	Fig 4
PMID:30796050	PBO:0093636	Fig 1
PMID:30796050	PBO:0093636	Fig 2
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 S2
PMID:30796050	PBO:0093632	Fig S2
PMID:30796050	PBO:0102806	Fig EV2
PMID:30796050	PBO:0102806	Fig S2
PMID:30806623	FYPO:0000648	Fig. 1
PMID:30806623	FYPO:0004310	Fig. 1
PMID:30806623	FYPO:0005342	Fig. 6
PMID:30806623	FYPO:0005342	Fig. 6
PMID:30806623	FYPO:0001492	Fig. 1
PMID:30806623	FYPO:0004310	Fig. 1
PMID:30806623	FYPO:0003268	Fig. 1
PMID:30806623	FYPO:0007958	Fig. 5
PMID:30806623	PBO:0097932	Fig. 6
PMID:30806623	FYPO:0005342	Fig. 6
PMID:30806623	FYPO:0007958	Fig. 1
PMID:30806623	FYPO:0005706	Fig. 3
PMID:30806623	FYPO:0005343	Fig. 3
PMID:30806623	FYPO:0005343	Fig. 6
PMID:30810475	PBO:0103146	fig4
PMID:30810475	PBO:0103147	fig6
PMID:30810475	PBO:0103148	fig6
PMID:30810475	FYPO:0001917	fig7
PMID:30810475	FYPO:0000229	fig7
PMID:30810475	GO:0016887	In vitro RNA helicase activity using recombinant protein encoded by the helicase domain of Prp16
PMID:30810475	FYPO:0004742	fig7
PMID:30810475	FYPO:0003412	fig7
PMID:30810475	FYPO:0003412	fig7
PMID:30810475	PBO:0103152	fig7
PMID:30810475	PBO:0103151	fig7
PMID:30810475	PBO:0103152	figS6,7
PMID:30810475	PBO:0103151	figS6,7
PMID:30810475	PBO:0103150	figS6,7
PMID:30810475	PBO:0103149	figS6,7
PMID:30810475	FYPO:0000091	fig7
PMID:30810475	FYPO:0001919	fig7 they say fragmented nucleus but they stained chromosomes, not nuclear envelope
PMID:30810475	GO:0034458	In vitro RNA helicase activity using recombinant protein encoded by the helicase domain of Prp16
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	PBO:0103141	Required for splicing of introns with strong 5' splice site - U6 snRNA and branch site - U2 snRNA interactions
PMID:30810475	FYPO:0002141	fig1
PMID:30810475	FYPO:0001357	fig1
PMID:30810475	FYPO:0000674	fig1
PMID:30810475	FYPO:0000082	fig1
PMID:30810475	FYPO:0000082	fig1
PMID:30810475	PBO:0095406	fig1b
PMID:30810475	PBO:0100020	fig1b
PMID:30810475	PBO:0098392	fig1b
PMID:30810475	PBO:0103142	fig1b
PMID:30810475	PBO:0095406	fig1b - for dga1 normal splicing of intonr 3, abnormal intron 2, S4
PMID:30810475	PBO:0103143	fig1b - for dga1 normal splicing of intonr 3, abnormal intron 2, S4
PMID:30810475	PBO:0095902	fig1b - for dga1 normal splicing of intonr 3, abnormal intron 2, S4
PMID:30810475	PBO:0103144	fig1b - for dga1 normal splicing of intonr 3, abnormal intron 2, S4
PMID:30810475	PBO:0103145	fig1b - for dga1 normal splicing of intonr 3, abnormal intron 2, S4
PMID:30810475	FYPO:0002061	fig1
PMID:30810475	PBO:0093557	fig1
PMID:30810475	PBO:0093556	fig1
PMID:30810475	PBO:0100020	fig4
PMID:30810475	PBO:0100020	fig4
PMID:30810475	FYPO:0001355	fig4
PMID:30810475	PBO:0095406	fig4
PMID:30840879	PBO:0097520	fig 3 c
PMID:30840879	PBO:0097520	fig 3c
PMID:30840879	GO:0005546	MEMBRANE LIPID BINDING Rga7 F-BAR preferred membranes rich in PI(4)P and PI(4,5)P2 (Figure 3D)
PMID:30840879	PBO:0097517	fig 1B
PMID:30840879	PBO:0097521	fig 2b
PMID:30840879	PBO:0097536	1F
PMID:30840879	PBO:0097537	2b normal lpid binding
PMID:30840879	PBO:0097538	fig 2A Figure 2A
PMID:30840879	PBO:0097524	fig 4
PMID:30840879	PBO:0097536	1F 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:0097535	F-BAR/BAR domain adaptors Rng10(751–950) interacts directly with the Rga7 F-BAR domain
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	GO:0070273	MEMBRANE LIPID BINDING Rga7 F-BAR preferred membranes rich in PI(4)P and PI(4,5)P2 (Figure 3D)
PMID:30840879	PBO:0097519	fig 3 c
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:0097517	fig 3 e
PMID:30840879	PBO:0096613	fig 3e
PMID:30840879	PBO:0097518	Figure 2A
PMID:30840879	PBO:0097517	fig 1B
PMID:30840879	PBO:0096613	fig 2A Figure 2A
PMID:30840879	PBO:0097517	fig 3e
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	FYPO:0003210	Figure 4I (Live-cell time-lapse imaging)
PMID:30853434	FYPO:0003210	Figure 4G (live cell DIC)
PMID:30853434	FYPO:0006822	Figure S4F&H (live cell DIC)
PMID:30853434	FYPO:0003481	Figure S4F and G (vw move to FYPO:0006822 and requested parentage fix in FYPO) (live cell DIC)
PMID:30853434	FYPO:0003481	Figure S4F and G (vw move to FYPO:0006822 and requested parentage fix in FYPO) (live cell DIC)
PMID:30853434	FYPO:0003210	Figure 4G (live cell DIC)
PMID:30853434	FYPO:0001223	Figure 4G (live cell DIC)
PMID:30853434	FYPO:0003439	Figure 4G (live cell DIC)
PMID:30853434	FYPO:0003481	Figure 4H (vw moved down to FYPO:0003481) (live cell DIC)
PMID:30853434	FYPO:0003481	Figure S4G (vw moved down to FYPO:0003481) (live cell DIC)
PMID:30853434	FYPO:0006822	Figure S4F & H (vw move to FYPO:0006822 and requested parentage fix in FYPO) (live cell DIC)
PMID:30853434	PBO:0094431	Figure S4A (live cell imaging)
PMID:30853434	PBO:0094431	Figure S4A (live cell imaging)
PMID:30853434	PBO:0094432	Figure S3A (live cell imaging)
PMID:30853434	PBO:0094432	Figure S3C-D (live cell imaging)
PMID:30853434	PBO:0094431	Figure 1H-I (live cell imaging)
PMID:30853434	FYPO:0003210	Figure 3C-D (live cell DIC)
PMID:30853434	PBO:0018677	FIg 1 D
PMID:30853434	PBO:0024047	FIg 1 D
PMID:30853434	FYPO:0002873	Figure 3D (live cell DIC)
PMID:30853434	FYPO:0002873	Figure 3C-D
PMID:30853434	PBO:0094421	Figure 1H-I (live cell imaging)
PMID:30853434	PBO:0094422	Figure 1C
PMID:30853434	PBO:0094423	Figure S2A-B (vw changed from FYPO:0001677 to FYPO:0002874 to match rlc1) (live cell imaging)
PMID:30853434	PBO:0094419	Figure 2E-F (live cell imaging)
PMID:30853434	PBO:0094418	Figure 4A-B (live cell imaging)
PMID:30853434	FYPO:0005905	Figure 3A-B (Live-cell time-lapse imaging)
PMID:30853434	FYPO:0001365	Figure 3A-B (Live-cell time-lapse imaging)
PMID:30853434	PBO:0094417	Figure 2A-B (vw changed to cell division site during M-phase from septum) (live cell imaging)
PMID:30853434	PBO:0094416	Figure 1D-G (live cell imaging)
PMID:30853434	PBO:0094415	Figure 3A-B (Live-cell time-lapse imaging)
PMID:30853434	PBO:0094414	increased binding by about 2 fold from Figure 4C-D
PMID:30853434	FYPO:0007474	Figure 4E (moved from wee) (skewed towards small, low severity)
PMID:30853434	PBO:0094424	Figure S2A-B (vw changed from FYPO:0001677 to FYPO:0002874 to match rlc1) (live cell imaging)
PMID:30853434	PBO:0094425	Figure S2A-B (vw changed from FYPO:0001677 to FYPO:0002874 to match rlc1) (live cell imaging)
PMID:30853434	PBO:0094426	Figure S2A-B (live cell imaging)
PMID:30853434	PBO:0094427	Figure S2C (live cell imaging)
PMID:30853434	PBO:0094428	Figure S3A (live cell imaging)
PMID:30853434	PBO:0094429	Figure S3C-D (live cell imaging)
PMID:30853434	PBO:0094433	FIg 1 D
PMID:30853434	PBO:0094434	Fig 2 E-F
PMID:30853434	PBO:0094435	Figure S4A
PMID:30853434	PBO:0094420	Figure S4C-D
PMID:30862564	FYPO:0003125	converted from bp by cc
PMID:30862564	FYPO:0003125	converted from bp by cc
PMID:30967422	PBO:0104182	figure2b
PMID:30967422	PBO:0104186	figure2b
PMID:30967422	PBO:0104187	figure2b
PMID:30967422	PBO:0104185	figure2b
PMID:30973898	PBO:0093567	figure1 A
PMID:30973898	PBO:0093564	figure1 B
PMID:30973898	FYPO:0000964	figure1 A
PMID:30973898	FYPO:0001686	figure1 A
PMID:30973898	FYPO:0003809	figure1 A
PMID:30973898	FYPO:0005947	figure1 A
PMID:30973898	PBO:0093564	figure1 A
PMID:30973898	FYPO:0000107	figure1 A
PMID:30973898	FYPO:0001214	figure1 A
PMID:30973898	FYPO:0000229	figure 4 DAPI staining
PMID:30973898	PBO:0105556	figure 4 C mini-chromosome Ch16 loss assay
PMID:30973898	PBO:0093562	figure 5A
PMID:30973898	PBO:0105557	mini-chromosome Ch16 loss assay
PMID:30973898	FYPO:0000964	figure 1B
PMID:30973898	PBO:0093562	Fig 1D
PMID:30973898	PBO:0093562	Fig 1D
PMID:30973898	PBO:0095942	figure 3A
PMID:30973898	PBO:0105558	figure S2A
PMID:30973898	PBO:0105559	figure S2B
PMID:30973898	PBO:0105560	figure 2B (two hybrid)
PMID:30973898	PBO:0105561	figure 2B (two hybrid)
PMID:30973898	PBO:0105560	figure 2B (two hybrid)
PMID:30973898	PBO:0105560	figure 2B (two hybrid)
PMID:30973898	PBO:0095942	figure 2C
PMID:30973898	PBO:0095942	figure 2C
PMID:30973898	PBO:0093562	figure 2C
PMID:30973898	FYPO:0002061	figure 2C
PMID:30973898	PBO:0022298	Figure 2D
PMID:30973898	PBO:0105562	Figure 2D
PMID:30973898	PBO:0105563	figure 2D
PMID:30973898	PBO:0102086	figure 2D
PMID:30973898	PBO:0095942	figure 3A
PMID:30973898	PBO:0093562	figure 3A
PMID:30973898	FYPO:0002059	figure 3A
PMID:30973898	FYPO:0002061	figure 3A
PMID:30973898	PBO:0105564	figure 4C
PMID:30973898	PBO:0105564	figure 4C
PMID:30973898	PBO:0095942	figure 5A
PMID:30973898	PBO:0095942	figure 5A
PMID:30973898	PBO:0095942	figure 5A
PMID:30973898	PBO:0105558	figure S2A
PMID:30973898	PBO:0105559	figure S2B
PMID:30973898	PBO:0095942	figure 5A
PMID:30973898	PBO:0095942	figure 5A
PMID:30975915	FYPO:0001357	Figure 1
PMID:30975915	FYPO:0002061	Figure 1
PMID:30975915	FYPO:0002061	figure3
PMID:30975915	FYPO:0000088	Fig. 4B
PMID:30975915	FYPO:0001234	Fig. 4A
PMID:30975915	FYPO:0002061	Figure 3
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:30975915	FYPO:0002061	Figure 3
PMID:30975915	FYPO:0002061	Figure 1
PMID:30975915	FYPO:0002061	figure 1A
PMID:30975915	FYPO:0002061	Fig. 2B
PMID:30975915	FYPO:0002061	Figure 1
PMID:30992049	PBO:0093613	grows normally at 25 degrees but not at 30 degrees
PMID:30992049	PBO:0093615	same as nmt81-vid21 alone
PMID:30992049	FYPO:0000085	25 degrees; same as mst1-L344S alone
PMID:30992049	PBO:0093615	hhf2 and hhf3 are wild-type. Only hhf2 is mutated.
PMID:30992049	PBO:0093614	grows normally at 25 degrees but not at 30 degrees
PMID:30992049	PBO:0093617	same as swi1delta alone
PMID:30992049	FYPO:0001355	grows normally at 25 degrees but not at 30 degrees
PMID:30992049	FYPO:0000085	grows normally at 25 degrees but not at 30 degrees
PMID:30992049	FYPO:0000095	hhf1 and hhf3 are wild-type. Only hhf2 is mutated.
PMID:30992049	FYPO:0002550	hhf1 and hhf3 are wild-type. Only hhf2 is mutated.
PMID:30992049	PBO:0093617	hhf1 and hhf3 are wild-type. Only hhf2 is mutated.
PMID:30992049	PBO:0093615	hhf1 and hhf3 are wild-type. Only hhf2 is mutated.
PMID:30992049	PBO:0093615	hhf2 and hhf3 are wild-type. Only hhf2 is mutated.
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	PBO:0095634	Fig 2
PMID:30996236	PBO:0095634	Fig 2
PMID:30996236	FYPO:0001357	Fig 2
PMID:30996236	FYPO:0001357	Fig 2
PMID:30996236	PBO:0095685	Fig 2
PMID:30996236	PBO:0094648	Fig 2
PMID:30996236	PBO:0095685	Fig 2
PMID:30996236	PBO:0095634	Fig 2
PMID:30996236	PBO:0095634	Fig 2
PMID:30996236	FYPO:0001357	Fig 2
PMID:30996236	FYPO:0001234	Fig 2
PMID:30996236	PBO:0095634	Fig 2
PMID:30996236	PBO:0095634	Fig 2
PMID:30996236	PBO:0095634	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:0001357	Fig 2
PMID:30996236	FYPO:0002674	Fig 3
PMID:30996236	FYPO:0002674	Fig 3
PMID:31000521	FYPO:0001513	The swi6-sm1 allele disrupts silencing without lagging chro- mosomes (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	FYPO:0003412	fig 7 B
PMID:31000521	FYPO:0003412	fig 7 B
PMID:31000521	FYPO:0004310	) Rad21 locates to centromere in dfp1-3A mutants.
PMID:31000521	FYPO:0001007	(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	FYPO:0001513	(Figure 3B Chp1 fails to accumulate at noncentromeric location in the absence of Chp2 and Swi6.
PMID:31000521	PBO:0104282	(Figure 3B 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	PBO:0096842	Fig 7 using minichromosome
PMID:31000521	PBO:0096838	Fig 7 using minichromosome
PMID:31000521	FYPO:0006811	Fig 7 using minichromosome
PMID:31000521	FYPO:0003412	fig 7 B
PMID:31000521	FYPO:0004742	fig 7B
PMID:31000521	FYPO:0004742	Fig 7B
PMID:31000521	FYPO:0000634	5B abolish Swi6 protein localization to centromere during vegetative growth
PMID:31000521	FYPO:0004310	(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	PBO:0104283	Fig-2A Spindle pole-to-pole distance was measured based on the distance of duplicated SPBs revealed by Sad1-DsRed.
PMID:31000521	PBO:0104284	(vw 3B? changed from normal to lagging, added penetrance) dfp1-CFP-2CD rescues minichromosome loss in the absence of Swi6.
PMID:31000521	PBO:0104285	Fig-2A Spindle pole-to-pole distance was measured based on the distance of duplicated SPBs revealed by Sad1-DsRed.
PMID:31000521	PBO:0097773	Fig-2C
PMID:31000521	PBO:0104286	Fig-2C
PMID:31000521	PBO:0097772	Fig-2C
PMID:31000521	PBO:0104287	Figure 3B
PMID:31000521	PBO:0104288	fig 3B
PMID:31000521	PBO:0104289	Figure 3B
PMID:31000521	PBO:0104290	Figure 3B
PMID:31000521	PBO:0104291	Figure 3B
PMID:31000521	FYPO:0000091	SUPP S1
PMID:31000521	PBO:0104292	5B
PMID:31000521	PBO:0104292	5E
PMID:31000521	PBO:0104293	5C
PMID:31000521	PBO:0096838	Fig 7 using minichromosome
PMID:31000521	PBO:0104293	Rad21-GFP enrichment at the centromere is unaffected in swi6-sm1 (Figure S4C)
PMID:31015410	PBO:0107675	Fig3d, OE lem2 supresses the increased NC ratio of rae1-167
PMID:31015410	FYPO:0001221	Fig3a,b
PMID:31015410	PBO:0107677	Fig 3e
PMID:31015410	FYPO:0001221	Fig3d
PMID:31015410	FYPO:0001221	Fig1 and Fig1supp data
PMID:31015410	PBO:0107671	Fig3f
PMID:31015410	PBO:0107670	Fig3c,d, OE SUPRESSOR OF NEM1delta lem2 supresses the increased NC ratio of nem1 delta
PMID:31015410	PBO:0107671	Fig3f
PMID:31015410	PBO:0107673	Fig 4a,c
PMID:31015410	PBO:0097188	Fig 4,b,c ENHANCER OF N/C ratio of lem2/rae1
PMID:31015410	PBO:0107668	Fig2a,b,c
PMID:31015410	PBO:0107669	Fig2 d,e,f,g,h supp fig6b
PMID:31015410	PBO:0097191	Fig 1
PMID:31015410	FYPO:0001221	Fig4 a,c
PMID:31015410	PBO:0107673	Fig 4a,c
PMID:31015410	PBO:0107678	Fig 1 (normal compaction)
PMID:31015410	PBO:0097191	Fig 1a,b,c
PMID:31015410	PBO:0097191	Fig 3c
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:0097191	supp data Fig 1b,c
PMID:31015410	PBO:0097189	supp Fig 7 supression of lem2delta
PMID:31015410	FYPO:0001380	Fig 3c
PMID:31015410	PBO:0107674	Fig 3c
PMID:31015410	FYPO:0001221	Fig1 supp data
PMID:31015410	FYPO:0001221	Fig1 supp data
PMID:31015410	FYPO:0001221	Fig1 supp data
PMID:31015410	FYPO:0001221	Fig1 supp data
PMID:31015410	FYPO:0001221	Fig4 a,c
PMID:31015410	GO:0031965	Supp Fig6
PMID:31015410	FYPO:0001221	Fig1 supp data
PMID:31015410	PBO:0107672	supp Fig6a
PMID:31015410	FYPO:0001221	Fig1 supp data
PMID:31015410	PBO:0107676	Fig3e suppression of nem1delta
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:0105863	Fig7
PMID:31030285	PBO:0105862	Fig7
PMID:31030285	PBO:0105858	fig S1
PMID:31030285	PBO:0105859	fig S1
PMID:31030285	PBO:0105861	Fig7
PMID:31030285	PBO:0105863	Fig7
PMID:31030285	PBO:0105862	Fig7
PMID:31030285	FYPO:0006978	Fig6
PMID:31030285	PBO:0105860	Fig7
PMID:31030285	PBO:0105861	Fig7
PMID:31030285	PBO:0105855	Coq4 protein is decreased but Dlp1, Coq3, Coq5 and Coq8 are not
PMID:31030285	FYPO:0000442	cell growth is slower than wild type in glycerol and ethanol medium
PMID:31030285	PBO:0105858	fig S1
PMID:31030285	PBO:0105858	fig S1
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	PBO:0105857	fig S1
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:0105864	Fig7
PMID:31030285	PBO:0105865	not shown
PMID:31030285	FYPO:0001420	fig8
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:31041892	FYPO:0004646	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	FYPO:0005905	Figure 4; blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	PBO:0096768	Figure 5
PMID:31041892	PBO:0096767	Figure 3
PMID:31041892	PBO:0096764	Figure 2
PMID:31041892	PBO:0096764	Figure 2
PMID:31041892	PBO:0096766	Figure 3; blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	PBO:0096760	Figure 2; 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:31041892	PBO:0019202	fig1
PMID:31041892	PBO:0096767	Figure 3
PMID:31041892	PBO:0019202	fig1
PMID:31041892	PBO:0019202	fig1
PMID:31041892	PBO:0096760	Figure 2
PMID:31041892	PBO:0096760	Figure 2
PMID:31041892	PBO:0096761	Figure 3
PMID:31041892	PBO:0096761	Figure 3
PMID:31041892	PBO:0096762	Figure 5
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	FYPO:0005905	Figure 4; blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31053915	GO:1990748	detoxification
PMID:31053915	GO:1990748	detoxification
PMID:31053915	GO:0010340	catechol O-methyltransferase activity (Vw I kept this as o-methytransferase since no report of catachols in fission yeast)
PMID:31053915	GO:0008171	catechol O-methyltransferase activity
PMID:31072933	FYPO:0002060	figure 3F
PMID:31072933	FYPO:0002060	figure 4 AB
PMID:31072933	FYPO:0002060	figure 4 AB
PMID:31072933	FYPO:0002060	figure 4 AB
PMID:31072933	FYPO:0002060	figure 4 AB
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 5C
PMID:31072933	FYPO:0002061	Fig 5C
PMID:31072933	FYPO:0001355	figure 5C
PMID:31072933	FYPO:0002061	figure S8
PMID:31072933	FYPO:0002061	figure S8
PMID:31072933	FYPO:0002060	figure 3A
PMID:31072933	FYPO:0002060	figure 3A
PMID:31072933	FYPO:0002060	figure 3A
PMID:31072933	FYPO:0002060	figure 3A
PMID:31072933	FYPO:0001355	figure 1c
PMID:31072933	FYPO:0001355	fig 3 B
PMID:31072933	FYPO:0001355	fig 3 B
PMID:31072933	FYPO:0001355	fig 3 B
PMID:31072933	FYPO:0002060	figure S4
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 S3
PMID:31072933	FYPO:0002060	figure S3
PMID:31072933	FYPO:0002060	figure 2C
PMID:31072933	PBO:0100827	figure2
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:0002061	figure 1c
PMID:31072933	FYPO:0002061	figure 1c
PMID:31072933	PBO:0099134	(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	PBO:0100832	figure S7A
PMID:31072933	PBO:0100832	figure S7A
PMID:31072933	PBO:0100832	figure S7A
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:0098320	figure 6c
PMID:31072933	PBO:0100832	figure 6c
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	fig 2
PMID:31072933	PBO:0100825	figure 1G
PMID:31072933	PBO:0100825	figure 1G
PMID:31072933	PBO:0100825	Figure 1G/ figur2
PMID:31072933	FYPO:0002060	figure 3A
PMID:31072933	FYPO:0002060	figure 3A
PMID:31072933	FYPO:0002060	figure 3A
PMID:31072933	FYPO:0002060	figure 3A
PMID:31072933	FYPO:0002060	figure 4 AB
PMID:31089172	FYPO:0002061	Figure 4A
PMID:31089172	PBO:0101951	fig 4
PMID:31089172	PBO:0101949	fig 4
PMID:31089172	PBO:0097932	Figure 4AB
PMID:31089172	PBO:0097932	Figure 4AB
PMID:31089172	PBO:0097932	Figure 4AB
PMID:31089172	PBO:0097932	Figure 4AB
PMID:31089172	PBO:0097932	Figure 4AB
PMID:31089172	PBO:0101950	Figure 4AB
PMID:31089172	PBO:0101949	Figure 4AB
PMID:31089172	PBO:0101949	Figure 4AB
PMID:31089172	PBO:0101949	Figure 4AB
PMID:31089172	FYPO:0006918	Figure 4AB
PMID:31089172	FYPO:0004833	Figure 4AB
PMID:31089172	PBO:0024749	Fig. 4A
PMID:31089172	PBO:0021821	Fig. 4A
PMID:31089172	PBO:0033572	Fig. 4A
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	FYPO:0002061	Figure 4A
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:31089172	FYPO:0002061	Fig. 3
PMID:31089172	FYPO:0002061	Fig. 3
PMID:31089172	FYPO:0002061	Fig. 3A top
PMID:31089172	FYPO:0000324	fig 2 E
PMID:31089172	FYPO:0006917	fig 2 E
PMID:31089172	FYPO:0006917	fig 2 E
PMID:31089172	FYPO:0003268	fig 2 C/D
PMID:31089172	FYPO:0003268	fig 2 C/D
PMID:31089172	FYPO:0003268	fig 2 C/D
PMID:31089172	PBO:0101948	fig 2 A/B
PMID:31089172	PBO:0101948	fig 2 A/B
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:0101954	Figure 6C-E
PMID:31089172	PBO:0097932	Figure 6C-E
PMID:31089172	PBO:0097932	Figure 5E
PMID:31089172	PBO:0097932	Figure 5E
PMID:31089172	PBO:0097932	Figure 5E
PMID:31089172	PBO:0097932	Figure 5E
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:0101953	Fig. 5B,C)
PMID:31089172	PBO:0101953	Fig. 5B,C)
PMID:31089172	PBO:0095688	Fig. 5B,C)
PMID:31089172	PBO:0095688	Fig. 5B,C)
PMID:31089172	PBO:0101952	fig 4
PMID:31116668	FYPO:0006005	fig4
PMID:31116668	PBO:0098990	1e
PMID:31116668	GO:0009992	fig 5
PMID:31116668	FYPO:0006899	5c
PMID:31116668	GO:0031520	1d (vw: localized by the secretory pathway)
PMID:31131414	FYPO:0002019	Southern blot; same as rap1-7A single mutant
PMID:31149897	FYPO:0006923	Fig 3
PMID:31149897	FYPO:0000167	Fig 4
PMID:31149897	PBO:0097857	Fig 4
PMID:31149897	FYPO:0000167	Fig 4
PMID:31149897	FYPO:0000167	Fig 4; very small difference from fbh1delta alone
PMID:31149897	FYPO:0006921	Fig 6
PMID:31149897	FYPO:0006925	Fig 5
PMID:31149897	FYPO:0006920	elg1∆ exhibits reduced direct repeat recombination associated with replication fork collapse at the RTS1 replication fork barrier
PMID:31149897	FYPO:0000473	Figure 3A; increased spontaneous direct repeat recombination
PMID:31149897	FYPO:0006922	PCNA foci persist longer than normal, and form large bright patches before disappearing (Fig 2).
PMID:31149897	FYPO:0006924	Fig 5
PMID:31149897	FYPO:0006921	Fig 6
PMID:31178220	GO:1901612	SpTam41 interacts strongly with cardiolipin (CL)
PMID:31201205	FYPO:0002903	small viable
PMID:31201205	GO:0005635	Fig.3
PMID:31201205	GO:0005635	Fig.3
PMID:31201205	FYPO:0002061	Fig. 2BC
PMID:31201205	GO:0005886	Fig.3
PMID:31201205	FYPO:0002061	Fig. 2BC
PMID:31201205	PBO:0102634	Figure 4
PMID:31201205	PBO:0102633	Figure 4
PMID:31201205	PBO:0102633	Figure 4
PMID:31201205	PBO:0102633	Figure 4
PMID:31201205	FYPO:0002061	Fig. 2BC
PMID:31201205	GO:0005886	Fig.3
PMID:31201205	FYPO:0002061	Fig. 2BC
PMID:31201205	FYPO:0002061	Fig. 2BC
PMID:31201205	PBO:0102634	Figure 4
PMID:31201205	PBO:0096875	Figure 6
PMID:31201205	PBO:0102635	Figure 6
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:0002060	figure 7
PMID:31201205	FYPO:0002048	figure 7B small viable
PMID:31201205	FYPO:0006935	figure 7B small, viable
PMID:31201205	FYPO:0006660	figure 7B
PMID:31201205	FYPO:0006660	figure 7B
PMID:31201205	GO:0005783	Fig.3
PMID:31201205	GO:0005783	Fig.3
PMID:31201205	PBO:0102632	Figure 4
PMID:31201205	PBO:0102632	Figure 4
PMID:31201205	FYPO:0002251	Figure 5, (VW: I made this more specific- figure 1E (36) this phenotype in increased in the presence of magnesium
PMID:31201205	FYPO:0002903	Figure 5 (vw: changed to pear, descendent of spherical)
PMID:31201205	PBO:0096876	Figure 6
PMID:31206516	PBO:0110795	FLAG ChIP analysis revealed that H297A reduced appreciably Epe1 enrichment on centromeric dg repeats and IRC3 (Fig 4G), a centro- meric boundary sequence where Epe1 accumulates to a high level [12, 14
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: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: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 phe- notypes (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 phe- notypes (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 phe- notypes (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 his- tone deacetylases, are required for self-propagation of heterochromatin [30–34]. The introduc- tion 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 his- tone deacetylases, are required for self-propagation of heterochromatin [30–34]. The introduc- tion 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 his- tone deacetylases, are required for self-propagation of heterochromatin [30–34]. The introduc- tion 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 his- tone deacetylases, are required for self-propagation of heterochromatin [30–34]. The introduc- tion 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 his- tone deacetylases, are required for self-propagation of heterochromatin [30–34]. The introduc- tion 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 his- tone deacetylases, are required for self-propagation of heterochromatin [30–34]. The introduc- tion 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 his- tone deacetylases, are required for self-propagation of heterochromatin [30–34]. The introduc- tion 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 his- tone deacetylases, are required for self-propagation of heterochromatin [30–34]. The introduc- tion 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 ectopi- cally deposited H3K9me, which arrested red pigment formation.
PMID:31206516	PBO:0110797	(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. Con- sistent 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:31217286	PBO:0112013	Fig. S1C
PMID:31217286	PBO:0112013	Fig. S1C
PMID:31217286	PBO:0112012	Phenotype of Erg25 overexpression is suppressed by Erg11 inhibition. Fig. 1E
PMID:31217286	PBO:0112011	Fig. 1D
PMID:31217286	PBO:0112011	Fig. S6
PMID:31217286	FYPO:0008169	Fig. 6A and B
PMID:31217286	PBO:0112020	Fig. 4C
PMID:31217286	PBO:0112019	Fig. 4B
PMID:31217286	PBO:0112018	Fig. 4A
PMID:31217286	PBO:0112017	Fig. 3
PMID:31217286	PBO:0112024	Fig. 6D
PMID:31217286	FYPO:0007677	Fig. 1C
PMID:31217286	PBO:0112010	Fig. 1
PMID:31217286	PBO:0112012	Fig. 6D
PMID:31217286	PBO:0112023	Fig. 5A
PMID:31217286	PBO:0112016	Fig. 2
PMID:31217286	PBO:0112015	Fig. 2
PMID:31217286	PBO:0112014	Fig. S1E and F
PMID:31217286	GO:0005783	Fig. S1D
PMID:31217286	PBO:0112022	Fig. 6C
PMID:31217286	PBO:0112021	Fig. 6C
PMID:31239353	FYPO:0007044	10-100 micromolar
PMID:31239353	GO:0106219	(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:31239353	FYPO:0007041	figure 8
PMID:31239353	PBO:0095251	Figure 5D
PMID:31239353	PBO:0095250	Figure 5D
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	PBO:0095249	Figure 1B and 1C
PMID:31239353	PBO:0095248	abolished ?
PMID:31239353	PBO:0095248	fig1 abolished?
PMID:31239353	FYPO:0007045	fig1
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	PBO:0095246	Pho8 abundance is increased in high zinc in a loz1 deletion strain (Figure 2B and 2C)
PMID:31239353	PBO:0095245	consistent with Loz1 facilitating the repression of pho8 gene expression in high zinc (Figure 2A)
PMID:31239353	FYPO:0007044	fig1
PMID:31239353	FYPO:0007044	fig1
PMID:31239353	FYPO:0007048	figure 7
PMID:31239353	FYPO:0007048	figure 7
PMID:31239353	FYPO:0007044	reduced alkaline phosphatase activity and Pho8 dimerization (assayed via an EGS cross linking experiment - see Figures 6C and 6D)
PMID:31239353	FYPO:0007044	reduced alkaline phosphatase activity and Pho8 dimerization (assayed via an EGS cross linking experiment - see Figures 6C and 6D)
PMID:31239353	FYPO:0007047	figure 7
PMID:31239353	FYPO:0007042	reduced during conditions of zinc shock (Figure 8 and Figure 9). (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:0007043	Figure 5B
PMID:31239353	FYPO:0007043	figure 5B
PMID:31239353	PBO:0095244	Figure 2B
PMID:31239353	PBO:0095243	Figure 1B and 1C
PMID:31239353	PBO:0095242	pho8 transcript and protein levels are increased in high zinc BUT ZINC DEPENDENT CHAnges are independent of transcript levels
PMID:31239353	GO:0004035	Figure 1A Zinc-dependen
PMID:31239353	GO:0004035	Figure 1A
PMID:31257143	PBO:0101478	3b 80% 12 hours
PMID:31257143	PBO:0101478	Figure 2B demonstrates robust arres 3b 80% 12 hours
PMID:31257143	FYPO:0002638	Figures S3B and S3C
PMID:31257143	FYPO:0004318	figure 2D
PMID:31257143	FYPO:0004318	figure 2d
PMID:31257143	FYPO:0004318	figure 2d
PMID:31257143	FYPO:0002638	Figure 2B demonstrates robust arres
PMID:31257143	PBO:0101483	Figure S4
PMID:31257143	PBO:0101482	Figure S4
PMID:31257143	FYPO:0002638	Figures S3B and S3D
PMID:31260531	PBO:0103437	chromatin association at MCBs is part of positive regulation of G1/S transition of mitotic cell cycle
PMID:31260531	PBO:0103435	Rep2 locates SAGA complex at MBF-regulated promoters.
PMID:31269446	FYPO:0002664	18 °C
PMID:31269446	FYPO:0002173	18 °C
PMID:31269446	FYPO:0003049	18 °C
PMID:31269446	FYPO:0003049	18 °C
PMID:31269446	PBO:0111618	non-canonical termination sites
PMID:31269446	FYPO:0002664	18 °C
PMID:31269446	PBO:0111618	non-canonical termination sites
PMID:31269446	FYPO:0002173	18 °C
PMID:31269446	FYPO:0000080	18 °C
PMID:31269446	FYPO:0000080	18 °C
PMID:31269446	FYPO:0000080	18 °C
PMID:31269446	FYPO:0007213	18 °C
PMID:31269446	FYPO:0007213	18 °C
PMID:31269446	PBO:0111618	non-canonical termination sites
PMID:31269446	FYPO:0003049	18 °C
PMID:31269446	FYPO:0003049	18 °C
PMID:31269446	GO:0090052	si independent pericentric heterochromatin formation CPF and RNAi Act in Parallel to Assemble Centromeric Heterochromatin
PMID:31269446	GO:0090052	si independent pericentric heterochromatin formation CPF and RNAi Act in Parallel to Assemble Centromeric Heterochromatin
PMID:31269446	FYPO:0002664	18 °C
PMID:31269446	FYPO:0007213	18 °C
PMID:31276301	FYPO:0002060	Figure S1a
PMID:31276301	PBO:0106675	Fig 4b
PMID:31276301	FYPO:0003190	(Table 3)
PMID:31276301	FYPO:0003717	Figure S1a
PMID:31276301	FYPO:0004652	Figure S1a
PMID:31276301	FYPO:0004097	Figure S1a
PMID:31276301	FYPO:0002215	fig 6
PMID:31276301	FYPO:0004429	Furthermore, abnormally elon- gated cytoplasmic and spindle MTs were frequently observed in these cells (Figure 6).
PMID:31276301	PBO:0106674	fig. 4e
PMID:31276301	PBO:0106673	fig. 4e
PMID:31276301	PBO:0106672	fig 4d
PMID:31276301	PBO:0106677	Fig 4e
PMID:31276301	PBO:0106671	Fig 4a
PMID:31276301	FYPO:0000733	Furthermore, abnormally elon- gated 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	FYPO:0007182	Table 3
PMID:31276301	FYPO:0004622	Figure 7b
PMID:31276301	PBO:0106676	Fig 4a
PMID:31276301	FYPO:0003702	Figure S1a
PMID:31276588	PBO:0094772	Figure 1D
PMID:31276588	PBO:0111667	target genes repressing lncRNA
PMID:31276588	PBO:0111666	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 pyrophos- phatase with respect to phosphate homeostasis.
PMID:31276588	FYPO:0001357	reporter system
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	PBO:0094771	Figure 1F.
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:0098248	Figure 1C
PMID:31276588	FYPO:0000080	Figure 1B
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:31276588	FYPO:0000080	Figure 1B
PMID:31278118	FYPO:0002336	Figure 6B
PMID:31278118	PBO:0097429	cells revealed that H3K9me2 was notably decreased at cen- tromeres and telomeres in pds5D (Figure 3, A and B).
PMID:31278118	PBO:0097430	cells revealed that H3K9me2 was notably decreased at cen- tromeres and telomeres in pds5D (Figure 3, A and B).
PMID:31278118	FYPO:0007376	Figure 4A https://github.com/pombase/fypo/issues/3693
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: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 establish- ment, 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 hetero- chromatin-deficient cells (Figure 5E)
PMID:31278118	PBO:0097431	However, the localization of Pds5 to euchromatic locations was unaffected in hetero- chromatin-deficient cells (Figure 5E)
PMID:31278118	PBO:0097425	fig 1D/E
PMID:31278118	PBO:0097426	fig 1D/E
PMID:31278118	PBO:0097423	fig1 d
PMID:31278118	FYPO:0002336	Figure 6A)
PMID:31278118	PBO:0097422	Fig 5 B vw: moved pds5 to assayed target
PMID:31278118	PBO:0097420	fig 2B (Figure S1B and Table S2). This variegated staining pattern is a char- acteristic of mutants that are known to be defective in the main- tenance of heterochromatin and that show a reduction, but not loss, of H3K9me levels (Taneja et al. 2017). Indeed, ChIP anal- yses 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 establish- ment, 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:0097427	fig 1D/E
PMID:31278118	FYPO:0002336	fig7
PMID:31278118	FYPO:0002336	fig7
PMID:31278118	PBO:0097416	table 1
PMID:31278118	PBO:0097416	table1
PMID:31285271	GO:0001731	cytoplasmic translation is a parent to this term
PMID:31285271	PBO:0099585	3e
PMID:31285271	PBO:0099584	3e
PMID:31285271	PBO:0099583	3a
PMID:31285271	PBO:0099582	3a
PMID:31285271	PBO:0099581	2d
PMID:31285271	PBO:0037494	Fig5. Asc1 colocalized with stress granule proteins in response to heat shock.
PMID:31285271	PBO:0099586	6f
PMID:31285271	PBO:0099251	6
PMID:31285271	FYPO:0000046	fig4h
PMID:31285271	FYPO:0001234	fig4h
PMID:31285271	FYPO:0003125	fig4
PMID:31285271	GO:0016282	Fig.2 Asc1 associates with polysomes.
PMID:31285271	PBO:0099580	2d
PMID:31285271	PBO:0099579	2d
PMID:31285271	PBO:0099578	2d
PMID:31285271	PBO:0099577	2d
PMID:31285271	PBO:0099576	1e
PMID:31285271	PBO:0099575	1d
PMID:31289327	FYPO:0002019	S2
PMID:31289327	FYPO:0002019	S2
PMID:31289327	FYPO:0000012	5
PMID:31289327	FYPO:0000012	5
PMID:31289327	PBO:0100058	4a
PMID:31289327	FYPO:0002019	S2
PMID:31289327	FYPO:0002019	S2
PMID:31294478	FYPO:0007012	2b
PMID:31294478	PBO:0106267	3
PMID:31294478	PBO:0106268	3
PMID:31294478	PBO:0106269	4
PMID:31294478	PBO:0106270	4
PMID:31294478	PBO:0106271	4
PMID:31294478	PBO:0106272	4
PMID:31294478	PBO:0098170	coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472
PMID:31294478	PBO:0098170	coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472
PMID:31294478	PBO:0098170	coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472
PMID:31294478	PBO:0106252	AL fig 4. 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	coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472
PMID:31294478	FYPO:0007014	2b
PMID:31294478	FYPO:0007013	2b
PMID:31294478	FYPO:0001134	2b
PMID:31294478	PBO:0106254	AL fig 4. 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. 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	FYPO:0007013	2b
PMID:31294478	FYPO:0007012	2b
PMID:31294478	FYPO:0001134	2b
PMID:31294478	PBO:0106260	2c, 5d
PMID:31294478	PBO:0106259	2c, 5d
PMID:31294478	PBO:0106258	2c, 5d
PMID:31294478	PBO:0106257	2c, 5d
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:0106255	AL fig 4. and 5c 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 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 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 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 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 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:0106249	AL fig 4. and 5c 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:0098562	fig 1 A and F
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:0098170	COINCIDENT WITH 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472
PMID:31294478	FYPO:0002061	Figure 5B
PMID:31294478	FYPO:0007013	2b
PMID:31294800	GO:0035925	UAAU motif
PMID:31315658	FYPO:0007471	n 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	Additional file 1: Fig. S1b, c
PMID:31315658	FYPO:0006518	(Fig. 1c)
PMID:31315658	FYPO:0006518	Additional file 1: Fig. S1b, c
PMID:31332096	FYPO:0004372	reduced chk1 phosphorylation
PMID:31332096	PBO:0101079	elimination of Rad3-specific phosphorylation
PMID:31341193	PBO:0107621	fig 7 Syb1 co-localizes with late endosome markers
PMID:31341193	PBO:0107622	fig 7
PMID:31341193	FYPO:0001355	Reduced growth at 37ºC on YES agar plates
PMID:31341193	FYPO:0001355	Reduced growth on 0.6M KCl plates
PMID:31341193	PBO:0107629	fig1
PMID:31341193	PBO:0107631	this is in a mutant but I guess it occurs physiologicall?
PMID:31341193	GO:0005802	Fig1 (minor)
PMID:31341193	GO:0005770	Fig1 (major)
PMID:31341193	PBO:0107628	fig1
PMID:31341193	PBO:0107628	fig1
PMID:31341193	PBO:0107628	fig1
PMID:31341193	PBO:0107608	fig5
PMID:31341193	PBO:0107629	fig1
PMID:31341193	PBO:0107623	isp6 delta supresses the abnormal Vps10 processing detected in vps35 delta strain
PMID:31341193	GO:0000328	Microscopy
PMID:31341193	GO:0031906	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:0107606	Fig 1 a-c
PMID:31341193	PBO:0107623	isp6 delta supresses the abnormal Vps10 proessing detected in gga21 delta gga22 delta strain
PMID:31341193	GO:0032588	Microscopy
PMID:31341193	PBO:0107607	Fig 1 a-c
PMID:31341193	PBO:0107606	fig 1d
PMID:31341193	PBO:0107608	fig5
PMID:31341193	PBO:0107609	Dot-Blot assay
PMID:31341193	FYPO:0007055	Evaluated by measuring the size of Vps10-GFP foci
PMID:31341193	FYPO:0000674	37ºC
PMID:31341193	FYPO:0005947	28ºC
PMID:31341193	PBO:0107612	Reduced co-localyzation with the PI3P probe Cherry-FYVE
PMID:31341193	PBO:0107611	fig 1 Increased colocalization with Cfr1
PMID:31341193	GO:0005802	Co-localization with TGN marker
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:0107617	Increased co-localization with Cfr1
PMID:31341193	PBO:0107620	Dot-Blot test
PMID:31350787	GO:0005759	Fig. 3
PMID:31350787	FYPO:0007122	fig6
PMID:31350787	FYPO:0004529	fig5
PMID:31350787	FYPO:0002056	fig5
PMID:31350787	PBO:0095092	fig4B
PMID:31350787	GO:0005759	Fig. 3
PMID:31350787	PBO:0093578	"fig 1A """
PMID:31350787	PBO:0094264	"fig 1A """
PMID:31350787	PBO:0095091	"fig 1A """
PMID:31350787	FYPO:0007121	fig1
PMID:31350787	FYPO:0000962	fig1
PMID:31350787	FYPO:0001409	fig1
PMID:31350787	FYPO:0001409	fig1
PMID:31350787	FYPO:0001164	fig1
PMID:31350787	FYPO:0001164	fig1
PMID:31350787	PBO:0093576	fig1
PMID:31350787	FYPO:0005825	figb
PMID:31350787	FYPO:0001934	fig2A The Dmti2 mutant was not able to grow at all on medium containing glycerol at the restrictive temperature of 37 °C
PMID:31350787	PBO:0093797	"fig 1A 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:31366733	PBO:0103309	fig7
PMID:31366733	PBO:0103309	fig7
PMID:31366733	PBO:0103309	fig7
PMID:31366733	PBO:0103309	fig7
PMID:31366733	PBO:0103309	fig7
PMID:31371524	PBO:0107534	figure 2
PMID:31371524	PBO:0107533	figure 4
PMID:31371524	PBO:0107535	figure 6
PMID:31371524	PBO:0107536	figure 6
PMID:31371524	GO:0005515	inhinits hhf4 binding
PMID:31371524	PBO:0107533	figure 2
PMID:31371524	PBO:0107534	figure 2
PMID:31427431	PBO:0097933	7
PMID:31427431	PBO:0097933	7
PMID:31427431	PBO:0097932	7
PMID:31427431	FYPO:0005342	7
PMID:31427431	FYPO:0005342	7
PMID:31427431	FYPO:0001846	6
PMID:31427431	FYPO:0001846	6
PMID:31427431	FYPO:0001846	6
PMID:31427431	FYPO:0000228	6
PMID:31427431	PBO:0097931	6
PMID:31427431	FYPO:0000030	2
PMID:31427431	FYPO:0000324	2
PMID:31427431	FYPO:0000228	6
PMID:31427431	FYPO:0007071	6
PMID:31427431	FYPO:0007071	6
PMID:31427431	FYPO:0007071	6
PMID:31427431	FYPO:0000324	2
PMID:31427431	FYPO:0000228	2
PMID:31427431	FYPO:0000228	2
PMID:31427431	FYPO:0000069	2f
PMID:31427431	FYPO:0000069	2f
PMID:31427431	FYPO:0000069	2f
PMID:31427431	FYPO:0000069	2f
PMID:31427431	FYPO:0000733	s2
PMID:31427431	FYPO:0000733	s2
PMID:31427431	FYPO:0001943	4
PMID:31427431	FYPO:0000733	5
PMID:31427431	FYPO:0000324	5
PMID:31427431	FYPO:0000141	5
PMID:31427431	FYPO:0001357	1b
PMID:31427431	FYPO:0000674	1b
PMID:31427431	FYPO:0000030	2
PMID:31427431	FYPO:0002059	1
PMID:31427431	FYPO:0000069	1e
PMID:31427431	FYPO:0000069	1e
PMID:31427431	FYPO:0001357	S1
PMID:31427431	FYPO:0000082	1b
PMID:31427431	FYPO:0000080	1b
PMID:31427431	FYPO:0000674	1b
PMID:31427431	FYPO:0001357	1b
PMID:31427431	FYPO:0001357	1b
PMID:31427431	FYPO:0001357	1b
PMID:31427431	PBO:0019232	7, type II cells
PMID:31427431	PBO:0097933	7
PMID:31427431	FYPO:0000674	1b
PMID:31427431	FYPO:0002141	1b
PMID:31427431	FYPO:0002141	1b
PMID:31427431	FYPO:0000080	1b
PMID:31427431	PBO:0097927	1f
PMID:31468675	FYPO:0002827	measured by cell growth spot assay
PMID:31468675	PBO:0097202	spot assay
PMID:31468675	FYPO:0006993	measured by cell growth spot assay
PMID:31468675	FYPO:0002827	partial derepression of marker gene at silent mating-type cassette; measured by cell growth spot assay
PMID:31468675	GO:0000792	colocalizes with H3K9me2
PMID:31468675	GO:0000792	colocalizes with H3K9me2
PMID:31468675	GO:0000792	colocalizes with H3K9me2
PMID:31468675	FYPO:0002827	measured by cell growth spot assay
PMID:31477575	PBO:0101367	fig2b
PMID:31477575	PBO:0101370	S3B
PMID:31477575	PBO:0101352	S3B
PMID:31477575	PBO:0101352	S3B
PMID:31477575	GO:0005829	3c
PMID:31477575	GO:0005938	3c
PMID:31477575	PBO:0101352	S1
PMID:31477575	PBO:0101352	S1
PMID:31477575	PBO:0101352	S1
PMID:31477575	PBO:0101352	S1
PMID:31477575	PBO:0101352	S1
PMID:31477575	PBO:0101352	S1
PMID:31477575	PBO:0101352	S1
PMID:31477575	PBO:0101352	S1
PMID:31477575	PBO:0101352	S1
PMID:31477575	GO:0005515	fig1
PMID:31477575	PBO:0101369	fig2b
PMID:31477575	PBO:0101368	fig2b
PMID:31477575	PBO:0101366	fig2b
PMID:31477575	PBO:0101365	fig2b
PMID:31477575	PBO:0101363	fig1
PMID:31477575	PBO:0101363	fig1
PMID:31477575	PBO:0101363	fig1
PMID:31483748	FYPO:0000969	fig2
PMID:31483748	FYPO:0000963	fig2
PMID:31483748	FYPO:0000957	fig2
PMID:31483748	FYPO:0000957	fig2
PMID:31483748	FYPO:0000957	fig2
PMID:31483748	FYPO:0000957	fig2
PMID:31483748	PBO:0093616	Figure 2C
PMID:31483748	PBO:0093616	Figure 2C
PMID:31483748	FYPO:0007191	Figure 3, A and B
PMID:31483748	FYPO:0000089	Figure 2C No increase in severity to mto1 delete
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:0007209	issues/3588 Figure 5, A–E
PMID:31483748	FYPO:0000089	Figure 2A
PMID:31483748	FYPO:0000267	fig2
PMID:31483748	FYPO:0000085	fig2
PMID:31483748	FYPO:0000957	fig2
PMID:31483748	FYPO:0000089	Figure S1A
PMID:31483748	FYPO:0000089	Figure S1A
PMID:31483748	FYPO:0000972	Figure 3, A and B . number and intensity
PMID:31483748	FYPO:0006921	Recombination rates were decreased by 10-fold in mto1∆ strains in both recombination substrates (Figure 4B)
PMID:31483748	FYPO:0000185	Recombination rates were decreased by 10-fold in mto1∆ strains in both recombination substrates (Figure 4B)
PMID:31483748	PBO:0101859	Reduced Rad21 binding to chromosome arms
PMID:31483748	FYPO:0007209	issues/3588 decreased
PMID:31483748	FYPO:0007192	fig1 B–G
PMID:31495586	FYPO:0006108	Figure 3
PMID:31495586	PBO:0102739	Figure6
PMID:31495586	PBO:0102738	Figure6
PMID:31495586	PBO:0097695	Figure6
PMID:31495586	PBO:0097695	Figure6
PMID:31495586	PBO:0102737	Figure 4
PMID:31495586	PBO:0102733	Figure 3
PMID:31495586	FYPO:0007095	Figure2, Increased 1.5-fold, assayed using CHD
PMID:31495586	FYPO:0006081	FigureS5, assayed using LifeAct
PMID:31495586	FYPO:0006081	FigureS5, assayed using LifeAct
PMID:31495586	PBO:0102736	Figure S6
PMID:31495586	PBO:0102711	Figure S6
PMID:31495586	PBO:0102711	Figure S6
PMID:31495586	PBO:0102711	Figure S6
PMID:31495586	PBO:0102735	1.1 fold, Figure S2
PMID:31495586	PBO:0102723	Figure S3
PMID:31495586	PBO:0102719	Figure S3
PMID:31495586	PBO:0102722	Figure S3
PMID:31495586	PBO:0102733	Figure S3
PMID:31495586	FYPO:0007095	Figure S1, assayed using CHD
PMID:31495586	PBO:0102732	Figure3, S4, assayed using Myo52 and Fus1
PMID:31495586	PBO:0102734	Figure S5, assayed using LifeAct
PMID:31495586	PBO:0102723	FigureS3
PMID:31495586	PBO:0102719	FigureS3
PMID:31495586	PBO:0102722	FigureS3
PMID:31495586	PBO:0102733	FigureS3
PMID:31495586	FYPO:0007095	assayed using CHD, FigureS1
PMID:31495586	PBO:0102731	Figure 3, assayed using Myo52
PMID:31495586	PBO:0102716	Figure 5
PMID:31495586	PBO:0102732	Figure 5, assayed using Myo52
PMID:31495586	PBO:0102732	Figure 5, assayed using Myo52
PMID:31495586	PBO:0102731	Figure 5, assayed using Myo52
PMID:31495586	PBO:0102730	Figure 4 and 6
PMID:31495586	PBO:0102729	Figure5
PMID:31495586	PBO:0102729	Figure5
PMID:31495586	FYPO:0000413	Figure 2
PMID:31495586	FYPO:0000413	Figure 2
PMID:31495586	PBO:0102728	Figure 2
PMID:31495586	PBO:0102728	Figure 2
PMID:31495586	PBO:0102727	Figure 2
PMID:31495586	PBO:0102727	Figure 2
PMID:31495586	PBO:0102726	Figure 2
PMID:31495586	PBO:0102726	Figure 2
PMID:31495586	PBO:0102725	Figure 3, assayed using Myo52
PMID:31495586	PBO:0102724	Figure 3
PMID:31495586	PBO:0102723	Figure 3
PMID:31495586	PBO:0102722	Figure 3
PMID:31495586	PBO:0102717	Increased 4-fold, Figure2
PMID:31495586	PBO:0102717	Increased 4-fold, FigureS1
PMID:31495586	PBO:0102721	Figure 2
PMID:31495586	PBO:0102720	Figure 1
PMID:31495586	PBO:0102719	Figure 3
PMID:31495586	PBO:0102718	Figure 3
PMID:31495586	PBO:0102717	Increased 4-fold, Figure2
PMID:31495586	PBO:0102716	Figure1
PMID:31495586	PBO:0102716	Figure1
PMID:31495586	PBO:0102715	Figure 4 and 6
PMID:31495586	PBO:0102714	Figure 4 and 6
PMID:31495586	PBO:0102713	Figure 4 and 6
PMID:31495586	PBO:0102712	Figure 4
PMID:31495586	PBO:0102711	Figure 6
PMID:31495586	PBO:0102710	Figure6
PMID:31495586	FYPO:0002030	Figure 6
PMID:31495586	FYPO:0002021	Figure 6
PMID:31509478	PBO:0096673	fig6
PMID:31509478	FYPO:0002059	figure1
PMID:31509478	FYPO:0005543	Figure 3E)
PMID:31509478	FYPO:0002060	fig1
PMID:31509478	FYPO:0002059	fig2
PMID:31509478	FYPO:0002177	fig3
PMID:31509478	FYPO:0003343	fig3
PMID:31509478	FYPO:0000650	fig3
PMID:31509478	FYPO:0005840	3F
PMID:31509478	FYPO:0005543	Figure 3E)
PMID:31509478	PBO:0099934	figS3C
PMID:31509478	PBO:0099934	figS3C
PMID:31509478	PBO:0099934	figS3C
PMID:31509478	PBO:0099934	figS3C
PMID:31509478	FYPO:0001904	synonym =ring collapse fig3F
PMID:31509478	FYPO:0000650	fig3
PMID:31509478	FYPO:0002059	fig 1
PMID:31509478	PBO:0099932	Figure 6A
PMID:31509478	FYPO:0003343	fig3
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: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: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: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: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: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: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:0102516	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: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 (consistent with its role in gene repression in high zinc conditions
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: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: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: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: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:31532702	FYPO:0000732	Figure 5E
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:0000732	Figure S6
PMID:31532702	FYPO:0003566	Figure 5G (this term referes to initial
PMID:31532702	FYPO:0002060	Figure 5H
PMID:31532702	PBO:0105599	meiosis I inital Figure 3B, C
PMID:31532702	PBO:0105600	Figure 2A
PMID:31532702	FYPO:0007081	Figure S3B, C pentrance, frequently like quadruple
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	FYPO:0004159	figure 1B
PMID:31532702	PBO:0105592	figure 1B
PMID:31532702	PBO:0105593	single nucleus
PMID:31532702	PBO:0105595	Figure 1D, E . monopolar?
PMID:31532702	PBO:0105596	Figure figure 1B, D
PMID:31532702	PBO:0105597	Figure 2A
PMID:31532702	FYPO:0002060	I didn't check the supp, but probably can only make this annotation?
PMID:31532702	PBO:0105598	top, Figure 3B, C)
PMID:31532702	FYPO:0004668	Figure S5
PMID:31532702	PBO:0095634	Figure 5B
PMID:31532702	PBO:0105601	Figure 5C, D
PMID:31532702	PBO:0095634	Figure 5E
PMID:31532702	GO:0000073	The Nuf2-containing kinetochore complex serves as a physical fulcrum for microtubule-dependent SPB separation
PMID:31538680	FYPO:0000006	Mutant proliferates faster and with shorter lag than wildtype in sublethal concentrations of hydroxyurea, phleomycin or doxorubicin
PMID:31538680	FYPO:0000006	Mutant proliferates faster and with shorter lag than wildtype in sublethal concentrations of hydroxyurea, phleomycin or doxorubicin
PMID:31538680	PBO:0105152	Mutant proliferates faster and with shorter lag than wildtype in sublethal concentrations of hydroxyurea, phleomycin or doxorubicin
PMID:31562247	PBO:0097038	figure 4ab
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	PBO:0097036	figure 4c
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	FYPO:0000056	fig 3a
PMID:31562247	PBO:0097038	figure 4ab
PMID:31562247	FYPO:0007611	(with decreased total volume -. new term requested) Throughout the period of glucose starvation, mito- chondria 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: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: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	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	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	PBO:0110228	spExo5 showed activity on either substrate, with a preference for the 5’-ended substrate (Supplementary Fig. S2B).
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	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	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	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	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	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	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	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	PBO:0102116	Examination of the cell morphology revealed that the cells were elongated, indicative of checkpoint activation [17] (Fig. 4B
PMID:31563844	PBO:0110207	Examination of the cell morphology revealed that the cells were elongated, indicative of checkpoint activation [17] (Fig. 4B
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	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:0002060	S. pombe exo5Δ strains are viable, indicating that spExo5 is not essential for mitochondrial genome stability (Fig. 2B).
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	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	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	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:0093630	However, the exo5Δ mutant is more sensitive than isogenic wild-type to UV-irradiation and alkylating agents (Fig. 5A).
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: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: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: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:31575705	FYPO:0000957	Figure 1A
PMID:31575705	FYPO:0006686	fig1
PMID:31575705	FYPO:0006318	RTS1-RFB assay
PMID:31575705	FYPO:0000957	Figure 1A
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: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 re- sistance to replication stress.
PMID:31575705	FYPO:0006318	Fig 2 C RTS1-RFB assay
PMID:31575705	FYPO:0000089	Fig 1A growth inhibited by 0.005% MMS after 4 days
PMID:31575705	GO:0000785	constitutive
PMID:31582398	PBO:0104164	"tetrad dissection ""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 mitochondrial mixing during meiosis
PMID:31582398	PBO:0104162	Figure. 5C, D normal (increased mitochondrial segregation during meiosis)
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 mito- chondria continued to remain segregated (Fig. S2, C and D).
PMID:31582398	PBO:0104161	Figure. 3C, D, E, F and Video 5 mitochondrial mixing during meiosis
PMID:31584934	FYPO:0000957	fig. 6
PMID:31584934	PBO:0105875	"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:31584934	GO:0006335	fig. 3,4
PMID:31584934	FYPO:0007160	fig. 3
PMID:31584934	PBO:0105882	fig. 3c
PMID:31584934	PBO:0105883	coincident with replication fork barrier but dependent on JM formation - not sure if we can be more specific here than nuclear chromatin?
PMID:31584934	FYPO:0000957	fig. 6
PMID:31584934	FYPO:0003906	fig. 6
PMID:31584934	FYPO:0000095	fig. 6
PMID:31584934	FYPO:0000473	fig. 7
PMID:31584934	FYPO:0000089	fig. 6
PMID:31584934	FYPO:0003906	fig. 6
PMID:31584934	FYPO:0000085	fig. 6
PMID:31584934	FYPO:0001690	fig. 6
PMID:31584934	FYPO:0001690	fig. 6
PMID:31584934	FYPO:0000085	fig. 6
PMID:31584934	FYPO:0000085	fig. 6
PMID:31584934	FYPO:0000089	fig. 6
PMID:31615333	FYPO:0006613	Figure S3
PMID:31615333	PBO:0097134	Figure 2 and S3
PMID:31615333	FYPO:0006613	Figure S3
PMID:31615333	PBO:0097132	Figure 2 and 3
PMID:31615333	FYPO:0006613	Figure S3
PMID:31615333	PBO:0097133	Figure S1
PMID:31615333	PBO:0097133	Figure 2, detected by northern blot analysis
PMID:31615333	PBO:0097134	Figure 2 and S3
PMID:31615333	FYPO:0003165	Figure 1c
PMID:31615333	PBO:0097132	Figure 2 and 3
PMID:31615333	PBO:0097134	Figure 2 and S3
PMID:31615768	PBO:0094438	fig3a by cen2-GFP observation
PMID:31615768	FYPO:0002061	S1
PMID:31615768	FYPO:0002061	fig 3I
PMID:31615768	FYPO:0006174	1A
PMID:31615768	PBO:0094440	figureS4
PMID:31615768	PBO:0024749	S2A/4
PMID:31615768	PBO:0037411	S2A/4
PMID:31615768	PBO:0094442	fig 4
PMID:31615768	PBO:0094439	S2
PMID:31615768	PBO:0094444	1E unbundled microtubules seen in early mitosis
PMID:31615768	PBO:0094443	fig 4
PMID:31615768	FYPO:0003307	fig 3
PMID:31615768	GO:0000776	S2A
PMID:31615768	FYPO:0002638	fig 3
PMID:31615768	PBO:0094441	fig 3
PMID:31615768	FYPO:0007126	fig 1C
PMID:31615768	PBO:0094437	1E unbundled microtubules seen in early mitosis
PMID:31615768	FYPO:0005722	fig 1C
PMID:31618856	FYPO:0006475	fig 4
PMID:31618856	FYPO:0000131	fig 4
PMID:31618856	FYPO:0002061	fig1
PMID:31618856	FYPO:0005699	appears to retain normal microtubule nucleation activity
PMID:31618856	FYPO:0005681	defective in microtubule growth during both interphase and mitosis
PMID:31618856	FYPO:0005694	Figure 2D
PMID:31618856	FYPO:0004315	fig 3
PMID:31618856	PBO:0102760	fig 4
PMID:31641022	PBO:0097920	"chnaged from ""increased rate of sporulation"""
PMID:31641022	FYPO:0002060	fig2
PMID:31644361	PBO:0102681	Figure 1H (in vitro) Cdr1 directly phosphory- lated Wee1, but Cdr1(K41A) did not ().
PMID:31644361	PBO:0020446	Figure 3 B
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	Fig1B Cdr1 overexpression induced hyperphosphorylation of Wee1 and loss of Cdk1-pY15, indicating inhibition of Wee1 kinase activity,
PMID:31644361	PBO:0102677	Fig1B. In contrast, Cdr2 overexpression induced hyperphosphoryla- tion of Wee1 but no change in Cdk1-pY15
PMID:31644361	PBO:0102679	Fig1B Cdr1 overexpression induced hyperphosphorylation of Wee1 and loss of Cdk1-pY15, indicating inhibition of Wee1 kinase activity,
PMID:31644361	PBO:0093712	Fig 1C overexpression of Cdr1 but not of Cdr2 re- sulted in reduced cell size in cdr1∆cdr2∆ cells (Figure 1C
PMID:31644361	FYPO:0001124	Fig1 In contrast, Cdr2 overexpression induced hyperphosphoryla- tion of Wee1 but no change in Cdk1-pY15
PMID:31644361	PBO:0094002	Figure 1 D Phosphorylation of Wee1 in fission yeast cells was reduced in the catalytically inactive mutant cdr1(K41A)
PMID:31644361	PBO:0102680	Cdr1 directly phosphory- lated Wee1, but Cdr1(K41A) did not (Figure 1H).
PMID:31644361	PBO:0094002	Figure 3 A onsistent 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: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:0101181	Accordingly, the size of wee1(4A) cells was largely (but not entirely) insensitive to Cdr1 overexpression (Figure 3G).
PMID:31644361	PBO:0111082	(Figure 4A). We confirmed that S. pombe Cdk1- asM17 directly thiophosphorylates Wee1 and Wee1(K596L)
PMID:31644361	PBO:0102684	Figure 5B) We tested the effects of artificially recruiting mEGFP-cdr1(∆460-482) back to nodes using cdr2-GFP- binding peptide (GBP)-mCherry, which contains the GBP. In this system, mEGFP-cdr1(∆460-482) colocalized with cdr2-GBP-mCherry at nodes.
PMID:31644361	PBO:0099234	Along with enhanced Wee1 hyperphosphorylation, these cells di- vided 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:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	PBO:0109290	Fig. 3
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0001122	Fig. 4
PMID:31657618	FYPO:0001122	Fig. 4
PMID:31657618	FYPO:0001122	Fig. 4
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	PBO:0109290	Fig. 3
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31657618	FYPO:0009060	Table
PMID:31712578	FYPO:0003612	Table S3
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:0004993	Table S3
PMID:31712578	FYPO:0004993	Table S3
PMID:31712578	FYPO:0003612	Table S3; spore viability lower than wild type (~50% of wild-type viability)
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:0003612	Table S3; spore viability similar to wild type
PMID:31712578	FYPO:0003612	Table S3; spore viability similar to wild type
PMID:31719112	PBO:0103649	temperature permissive for mcm4/cdc21-M68
PMID:31719112	PBO:0103649	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	GO:0005198	Tra2 contributes to the scaffolding and stabilisation of the entire NuA4 complex.
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:0109851	. Similarly, we observed about a twofold reduction of Tra2 levels from NuA4 (Fig. 2b).
PMID:31748520	PBO:0109854	RNA-seq
PMID:31748520	PBO:0101995	RNA-seq
PMID:31748520	PBO:0101995	RNA-seq
PMID:31748520	PBO:0109861	(Fig.1e, f) spt7/tra1 pho84 and mei2 promoters. and spt7/tras ssa2 promoter
PMID:31748520	PBO:0109862	(Fig.1e, f) spt7/tra1 pho84 and mei2 promoters. and spt7/tras ssa2 promoter
PMID:31748520	PBO:0109863	(Fig.1e, f) spt7/tra1 pho84 and mei2 promoters. and spt7/tras ssa2 promoter
PMID:31748520	PBO:0109864	Decreased levels of Tra1 and Tra2 in SAGA and NuA4 complexes, respectively Figure 2
PMID:31748520	FYPO:0008117	See Figure 3a-b Describes the biogenesis of a multisubunit complex from nascent proteins. Could be linked to pombase ID of one or several components of the complex
PMID:31748520	FYPO:0008117	See Figure 3c-d
PMID:31748520	FYPO:0008121	See Figure 4
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:0109854	RNA-seq
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	FYPO:0008120	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	PBO:0109865	Abolished Tra1 interaction with SAGA complex
PMID:31748520	PBO:0109865	Decreased Tra1 interaction with SAGA complex
PMID:31748520	PBO:0093626	(Fig. 5d)
PMID:31748520	PBO:0109866	RNA-seq
PMID:31748520	PBO:0109867	RNA-seq
PMID:31748520	PBO:0109870	Decreased levels of Tra1 and Tra2 in SAGA and NuA4 complexes, respectively Figure 2
PMID:31748520	FYPO:0001216	Normal Tra1 interaction with SAGA complex
PMID:31748520	FYPO:0001855	RNA-seq
PMID:31748520	FYPO:0001522	whereas tra1-Sctra1 strains show no growth defects, as compared with wild-type cells (Fig. 5d).
PMID:31748520	FYPO:0000963	whereas tra1-Sctra1 strains show no growth defects, as compared with wild-type cells (Fig. 5d).
PMID:31748520	PBO:0109869	Impor- tantly, quantitative MS analyses show that both Tra1-SpTra2 and Tra1-ScTra1 hybrid mutant proteins efficiently copurify with Tti2 (Supplementary Fig. 9b).
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: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:31777937	GO:0140432	A novel 5′-hydroxyl dinucleotide hydrolase activity for the DXO/Rai1 family of enzymes
PMID:31811152	PBO:0105418	Figure 1b (live cell observation)
PMID:31811152	PBO:0105417	Figure 1b (live cell observation)
PMID:31811152	PBO:0105416	Figure 1b (live cell observation)
PMID:31811152	PBO:0105417	Figure 1b (live cell observation)
PMID:31811152	PBO:0105426	Figure 1c
PMID:31811152	PBO:0105427	fig2
PMID:31811152	PBO:0105416	Figure 1b, Figure 4b (live cell observation)
PMID:31811152	PBO:0105427	fig2
PMID:31811152	PBO:0105421	Figure 1b (live cell observation)
PMID:31811152	PBO:0105428	C24 locus. fig2
PMID:31811152	PBO:0105429	C24 locus. fig2
PMID:31811152	PBO:0105430	Figure 4b,
PMID:31811152	PBO:0105431	Figure 4b (live cell observation)
PMID:31811152	PBO:0105432	Figure 4b (live cell observation)
PMID:31811152	PBO:0105416	Figure 1b (live cell observation)
PMID:31811152	PBO:0105420	Figure 1b (live cell observation)
PMID:31811152	PBO:0105419	Figure 4a
PMID:31811152	PBO:0105426	Figure 1c
PMID:31811152	PBO:0105416	Figure 1b, (live cell observation)
PMID:31811152	PBO:0105422	Figure 4a. homologous pairing examined at C24 locus
PMID:31833215	FYPO:0000245	same as maf1delta alone
PMID:31837996	PBO:0104322	assayed using bulk histones
PMID:31837996	FYPO:0005917	RNA-seq
PMID:31837996	FYPO:0005917	RNA-seq
PMID:31837996	FYPO:0000854	similar to pob3delta alone
PMID:31837996	PBO:0104321	assayed using bulk histones
PMID:31837996	PBO:0104317	RNA-seq
PMID:31837996	PBO:0104318	similar to pob3delta alone
PMID:31837996	PBO:0104317	RNA-seq
PMID:31837996	PBO:0104317	RNA-seq
PMID:31848341	GO:0042393	binds H3-H4 dimer; assayed in vitro using Xenopus histones
PMID:31895039	PBO:0095068	Fig.6
PMID:31895039	PBO:0095069	Fig.7
PMID:31895039	PBO:0095054	Fig.7
PMID:31895039	PBO:0095069	Fig.4
PMID:31895039	PBO:0095054	Fig.4
PMID:31895039	PBO:0095070	Fig.7. Phenotype suppressed by the deletion of the pef1 gene
PMID:31895039	PBO:0095071	Fig.7. Phenotype suppressed by the deletion of the pef1 gene
PMID:31895039	FYPO:0002061	Fig.1b
PMID:31895039	PBO:0095072	Fig.2 supp1
PMID:31895039	PBO:0095073	"Figure 5Dm : ""In vitro Rad21 phosphorylation was abolished when Pef1 was purified from psl1 deleted cells"""
PMID:31895039	PBO:0095073	fig 5g
PMID:31895039	PBO:0114608	antagonises pef1
PMID:31895039	FYPO:0002060	Fig.8
PMID:31895039	FYPO:0002060	Fig.5
PMID:31895039	FYPO:0002060	34°C, Fig.7
PMID:31895039	PBO:0095073	(Figure 5E and Figure 5—figure supplement 1). Replacement of T262 by an alanine abolished in vitro Rad21 phosphorylation by Pef1-GFP
PMID:31895039	PBO:0095060	Fig.5
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	FYPO:0002060	36.5°C
PMID:31895039	FYPO:0002061	34°C, Fig.7
PMID:31895039	PBO:0095063	Fig.7. Phenotype suppressed by the deletion of pef1
PMID:31895039	FYPO:0002060	Fig.1 36.5°C
PMID:31895039	PBO:0095056	Fig. 2
PMID:31895039	FYPO:0002060	Fig. 1 36.5°C
PMID:31895039	PBO:0095057	fig1c
PMID:31895039	PBO:0095058	Fig.1
PMID:31895039	PBO:0095059	Fig.1
PMID:31895039	FYPO:0002060	Figure 1—figure supplement 1
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—figure supplement 1
PMID:31895039	PBO:0095062	Fig.7. Phenotype suppressed by the deletion of pef1
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	PBO:0095067	Fig.1
PMID:31895039	FYPO:0002060	Fig.8
PMID:31895039	FYPO:0000674	Fig.7
PMID:31895039	FYPO:0002060	Fig.7 34°C
PMID:31895039	FYPO:0000674	Fig.7
PMID:31895039	FYPO:0002060	Fig.8
PMID:31895039	FYPO:0002061	Fig.7
PMID:31895039	FYPO:0002060	Fig.8
PMID:31895039	FYPO:0002060	Fig.8
PMID:31895039	PBO:0095064	Fig.8
PMID:31895039	PBO:0095065	Fig.8
PMID:31895039	PBO:0095066	Fig.1
PMID:31895039	PBO:0033478	Fig.1
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 wak1􏰀, wis1􏰀 , atf1􏰀 , pyp1􏰀 , and pyp2􏰀 mRNAs in vitro (Fig. 5A)
PMID:31911490	PBO:0093712	fig 5e
PMID:31911490	PBO:0106157	Fig. 5B
PMID:31911490	PBO:0106176	Fig. 4B
PMID:31911490	PBO:0106167	Fig. 1B cell length at division either of pmk1􏰂 cells or in a mutant strain lacking the dual-specificity phos- phatase 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:0106179	I think these can be mopre specific decreased catabolism (ie increased stability in contract ti increased expression))
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 wak1􏰀, wis1􏰀 , atf1􏰀 , pyp1􏰀 , and pyp2􏰀 mRNAs in vitro (Fig. 5A)
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 wak1􏰀, wis1􏰀 , atf1􏰀 , pyp1􏰀 , and pyp2􏰀 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 wak1􏰀, wis1􏰀 , atf1􏰀 , pyp1􏰀 , and pyp2􏰀 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 wak1􏰀, wis1􏰀 , atf1􏰀 , pyp1􏰀 , and pyp2􏰀 mRNAs in vitro (Fig. 5A)
PMID:31911490	PBO:0106138	and enhanced expression of Wak1, Wis1, and Pyp1 proteins during unperturbed growth (Fig. 5C) a
PMID:31911490	PBO:0106170	fig 5C
PMID:31911490	PBO:0106164	fig 4h
PMID:31911490	FYPO:0006822	12.13 + 0.1
PMID:31911490	PBO:0106160	fig2C
PMID:31911490	FYPO:0001122	fig 1B
PMID:31911490	PBO:0106159	I think these can be mopre specific decreased catabolism (ie increased stability in contract ti increased expression))
PMID:31911490	PBO:0106158	I think these can be mopre specific decreased catabolism (ie increased stability in contract ti increased expression))
PMID:31911490	PBO:0106157	I think these can be mopre specific decreased catabolism (ie increased stability in contract ti increased expression))
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	PBO:0106146	FIg2
PMID:31911490	PBO:0101762	fig 3f
PMID:31911490	PBO:0106144	(Fig. 1D). In addition, basal Sty1 activity was significantly higher in exponentially growing rnc1􏰂 cells ex- pressing a genomic C-terminal hemagglutinin (HA)-tagged version of the MAP kinase, compared to wild-type cells or a pmk1􏰂 mutant
PMID:31911490	PBO:0106138	Fig 2B
PMID:31911490	PBO:0093712	Fig. 1B Fig. 1C (14.04􏰃0.25 versus 11.98􏰃0.29􏰋m, respectively)
PMID:31932483	FYPO:0000087	Fig 4B; 0.5 mM H2O2 in agar
PMID:31932483	FYPO:0000087	Fig 4B; 0.5 mM H2O2 in agar
PMID:31932483	PBO:0101318	Fig. 6E
PMID:31932483	FYPO:0005947	Fig 4B; 1 M KCl in agar
PMID:31932483	FYPO:0000962	Fig 4B; 0.5 mM H2O2 in agar
PMID:31932483	FYPO:0000962	Fig 4B; 0.5 mM H2O2 in agar
PMID:31932483	FYPO:0005947	Fig 4B; 1 M KCl in agar
PMID:31932483	FYPO:0005947	Fig 4B; 1 M KCl in agar
PMID:31932483	FYPO:0007332	Fig. 6F
PMID:31932483	FYPO:0000962	Fig 4B; 0.5 mM H2O2 in agar
PMID:31932483	MOD:00210	Fig. 3
PMID:31932483	PBO:0101320	Fig. 4A
PMID:31932483	PBO:0101319	Fig. 7E
PMID:31932483	FYPO:0000962	Fig 4B; 0.5 mM H2O2 in agar
PMID:31932483	FYPO:0001214	Fig 4B; 1 M KCl in agar
PMID:31932483	FYPO:0005947	Fig 4B; 1 M KCl in agar
PMID:31932483	PBO:0101321	Fig. 2
PMID:31932483	FYPO:0005947	Fig 4B; 1 M KCl in agar
PMID:31932483	FYPO:0005947	Fig 4B; 1 M KCl in agar
PMID:31932483	FYPO:0000087	Fig 4B; 0.5 mM H2O2 in agar
PMID:31941401	FYPO:0006295	Figure 1B
PMID:31941401	PBO:0108221	Figure 1G)
PMID:31941401	FYPO:0006266	Fig. S2
PMID:31941401	FYPO:0000674	Fig. S2)
PMID:31941401	PBO:0105271	Pho8Δ60 assay (Fig. S3A).
PMID:31941401	FYPO:0006295	Fig. S2)
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	PBO:0108220	Figure 3A,B
PMID:31941401	FYPO:0006295	Figure 2A Pho8Δ60 autophagy assay
PMID:31941401	PBO:0105271	Pho8Δ60 assay (Fig. S3A).
PMID:31941401	PBO:0108221	Figure 1E
PMID:31941401	PBO:0108221	Figure 1F
PMID:31941401	PBO:0108222	Figure 1G)
PMID:31941401	PBO:0108223	Figure 3A,B ut reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	PBO:0108221	Figure 1G)
PMID:31941401	PBO:0108221	Figure 1G)
PMID:31941401	PBO:0108224	Figure 3A,B ut 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:0108228	Figure 3A,B ut reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	PBO:0108227	Figure 3A,B ut reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	PBO:0108226	Figure 3A,B ut reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	PBO:0108225	Figure 3A,B ut reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
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 clus- terization did not reach WT level in ter1􏰀 cells after 3 days in G0.
PMID:31980821	PBO:0094923	When ter1+ gene was deleted in bqt4􏰀 cells, we observed that the combination of telomere erosion and NE dissociation provokes a massive accumula- tion of TERRA in Vg cells and this robust increase in tran- scription 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 ob- served that telomere erosion and STEEx formation in ter1􏰀 cells correlates with defects to exit properly from G0 (22)
PMID:31980821	PBO:0094925	Indeed, in bqt4􏰀 ter1􏰀 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 senes- cence
PMID:31980821	FYPO:0006516	5A. bqt4delta/ telomerase + cells exhibited wild-type telomeres that were stable in post-mitotic cells
PMID:31980821	PBO:0038206	In contrast to ter1􏰀 cells in which the loss of growth capacity was progressive, the growth of bqt4􏰀 ter1􏰀 cells was severely impaired (Figure 4A and Supplementary Fig- ure S2).
PMID:31980821	PBO:0094919	When ter1+ gene was deleted in bqt4􏰀 cells, we observed that the combination of telomere erosion and NE dissociation provokes a massive accumula- tion of TERRA in Vg cells and this robust increase in tran- scription is even stronger after 48H in quiescence
PMID:31980821	PBO:0094920	TERRA level was higher in bqt4􏰀 than WT in vegetative cells and this difference was substantially inten- sified after 48H in quiescence (Figure 6A),
PMID:31980821	FYPO:0007414	2B
PMID:31980821	FYPO:0007419	2D althouh also the percentage of cells that contain a unique telomeric cluster in G0 after streaks 3 and 4 (Fig- ure 2D). We found that telomere attrition observed in the absence of telomerase did not significantly impair telomere hyperclusterization in quiescence. However, telomere clus- terization did not reach WT level in ter1􏰀 cells after 3 days in G0.
PMID:31980821	FYPO:0007419	3D We confirmed that telomere foci moved from nuclear periphery to a more central area (zone 1 to zone 2 or 3) in bqt4􏰀 Vg cells
PMID:31980821	FYPO:0007419	zoning of telomere foci within the nuclear envelope was severely impaired in bqt4􏰀 ter1􏰀 for vegetative and qui- escent cells (Supplementary Figure S3D and E).
PMID:31980821	FYPO:0007419	zoning of telomere foci within the nuclear envelope was severely impaired in bqt4􏰀 ter1􏰀 for vegetative and qui- escent 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 bqt4􏰀 ter1􏰀 cells at early time points of quiescence (Figure 5A).
PMID:31980821	PBO:0094922	TERRA level was higher in bqt4􏰀 than WT in vegetative cells and this difference was substantially inten- sified after 48H in quiescence (Figure 6A),
PMID:32012158	PBO:0105690	figure 5A
PMID:32012158	PBO:0105681	figure S3A COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED
PMID:32012158	PBO:0105681	figure S3A COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED IN GENOME
PMID:32012158	PBO:0094866	figure S3A
PMID:32012158	PBO:0094605	figure S3A
PMID:32012158	PBO:0105689	figure 1 a
PMID:32012158	PBO:0105675	figure 1 a
PMID:32012158	PBO:0105688	figure 6 a
PMID:32012158	PBO:0105676	figure 1 a
PMID:32012158	PBO:0105677	figure 1 a
PMID:32012158	PBO:0105678	figure 1 a
PMID:32012158	PBO:0095145	figure 2
PMID:32012158	PBO:0105679	figure 1 a
PMID:32012158	PBO:0105680	figure 2
PMID:32012158	FYPO:0002085	figure S3A
PMID:32012158	FYPO:0006821	figure S3A
PMID:32012158	PBO:0094604	figure S3A
PMID:32012158	PBO:0094605	figure S3A
PMID:32012158	PBO:0094866	figure S3A
PMID:32012158	PBO:0094604	figure S3A
PMID:32012158	PBO:0095145	figure 5B
PMID:32012158	PBO:0105687	figure 5B
PMID:32012158	PBO:0105686	figure 5A
PMID:32012158	PBO:0105681	figure S3A COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED
PMID:32012158	PBO:0105684	figure 3A
PMID:32012158	PBO:0105682	figure S3A COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED
PMID:32012158	PBO:0105683	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:32023460	FYPO:0007273	fig2 the cortical tubular ER pattern changes faster than wild type
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:32023460	FYPO:0006330	(Figure 4 S4B).
PMID:32023460	FYPO:0007273	(Fig- ure S5G). the cortical tubular ER pattern changes faster than wild type
PMID:32023460	FYPO:0007268	(Figure 3A) 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) decreased cortical ER remodeling dynamics 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
PMID:32023460	FYPO:0007273	increased cortical ER remodeling dynamics
PMID:32023460	FYPO:0007273	increased cortical ER remodeling dynamics the cortical tubular ER pattern changes faster than wild type
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:0002872	(Figures 1A and 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 asso- ciation was abolished in scs2Dscs22D cells lacking ER-PM con- tacts.(the Exp says more but I don't know how to capture that)
PMID:32023460	FYPO:0007263	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	PBO:0103689	(Figure S1F). increased Pil1 phosphorylation was detected in these cells
PMID:32023460	FYPO:0007263	resulting in the formation of fewer punctate eisosomes (Figure S1B).
PMID:32023460	PBO:0103690	decreased Pil1 protein abundance Figure S1F
PMID:32023460	GO:0007029	cortical
PMID:32023460	PBO:0103691	Pil1 lacking the C terminus failed to interact with Scs2 (Figure S5F
PMID:32023460	PBO:0103693	(Figure 4 S4B).
PMID:32023460	FYPO:0007273	fig2 increased cortical ER remodeling dynamics
PMID:32023460	FYPO:0007273	fig2 increased cortical ER remodeling dynamics
PMID:32023460	FYPO:0007265	(Figure S1F). Pil1 mis-assembled into fewer and longer filaments
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:32032353	FYPO:0000590	Both wtf21 alleles were found at equal frequency in the viable spores.
PMID:32032353	PBO:0092298	S.p. wtf13 assayed; doesn't specify which isoform (or if it's both)
PMID:32032353	GO:0110134	inferred from crosses involving hemizygous diploids
PMID:32032353	GO:0110134	inferred from crosses involving hemizygous diploids
PMID:32032353	PBO:0092298	S.p. wtf13 assayed; doesn't specify which isoform (or if it's both)
PMID:32032353	GO:0005783	assayed by expressing S.k. ortholog in S.p.
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: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:32053662	PBO:0105870	6bc
PMID:32053662	PBO:0105866	figure5 a-c
PMID:32053662	PBO:0105867	figure5 a-c
PMID:32053662	PBO:0105868	6d
PMID:32053662	PBO:0105869	6d
PMID:32053662	PBO:0105866	figure5 a-c
PMID:32053662	PBO:0105870	6bc
PMID:32053662	PBO:0105870	6bc
PMID:32053662	PBO:0105866	figure5 a-c
PMID:32053662	PBO:0105867	figure5 a-c
PMID:32053662	PBO:0105866	figure5 a-c
PMID:32053662	PBO:0105869	6d
PMID:32053662	PBO:0105866	figure5 a-c
PMID:32053662	PBO:0105870	6bc
PMID:32053662	PBO:0105866	figure5 a-c
PMID:32053662	PBO:0105870	6bc
PMID:32062975	FYPO:0000091	fig 6B
PMID:32062975	FYPO:0003736	Figure 6A
PMID:32062975	FYPO:0001903	Figure 6A
PMID:32062975	FYPO:0000141	Figure 6A
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:0001896	Fig 6a
PMID:32071154	FYPO:0001896	Fig 6a
PMID:32071154	FYPO:0001896	Fig 6a
PMID:32071154	FYPO:0001896	Fig 6a
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	PBO:0106936	vw: changed from slow growth (6hr)
PMID:32071154	FYPO:0007317	polysome profile
PMID:32071154	PBO:0106937	fig 2B
PMID:32071154	FYPO:0007321	fig 4
PMID:32071154	FYPO:0007321	fig 4
PMID:32071154	FYPO:0007321	fig 4
PMID:32071154	FYPO:0007323	fig4
PMID:32071154	FYPO:0007323	fig 4
PMID:32071154	FYPO:0007319	fig 5C
PMID:32071154	FYPO:0007319	fig 5C
PMID:32071154	FYPO:0002350	figure 2C
PMID:32071154	FYPO:0007323	fig4
PMID:32071154	FYPO:0007319	fig 5C
PMID:32071154	FYPO:0001897	Figure 6E
PMID:32071154	FYPO:0002348	fig 5C
PMID:32071154	FYPO:0002061	polysome profile
PMID:32071154	FYPO:0001897	Figure 6E
PMID:32071154	FYPO:0007321	fig 4
PMID:32071154	FYPO:0002061	Fig 7B
PMID:32071154	FYPO:0002061	Fig 7B
PMID:32075773	FYPO:0007299	fig2B S2B-D
PMID:32075773	FYPO:0007300	fig2B S2B-D
PMID:32075773	FYPO:0007299	fig2B S2B-D
PMID:32075773	FYPO:0007299	fig2B S2B-D
PMID:32075773	FYPO:0007299	fig2B 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:32075773	FYPO:0007301	Fig S2
PMID:32075773	FYPO:0007301	Fig S2
PMID:32075773	FYPO:0007301	Fig S2
PMID:32075773	FYPO:0007301	Fig S2A
PMID:32075773	PBO:0100916	37 C 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	FYPO:0007299	fig2B S2B-D
PMID:32075773	FYPO:0007299	fig2B S2B-D
PMID:32075773	PBO:0108266	Figure 1B
PMID:32075773	PBO:0108267	Figure 1B.
PMID:32084401	PBO:0097952	FigS1-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:0097958	Fig2H 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:0097959	Fig3A 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	Fig2H cdc13HPM localisation to SPB in mitosis is dependent on plo1 activity
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: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:0018346	cdc13HPM mutant can localise to SPB in mitosis
PMID:32084401	FYPO:0002061	Fig2A cells expressing only cdc13HPM are unable to form colonies
PMID:32084401	PBO:0097954	Fig2A cells are unable to enter mitosis in absence of cdc13+ expression-no septated cells
PMID:32084401	PBO:0097953	Fig2B-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:0097951	Fig S1D cdc13+ and cdc13HPM are not differentially sensitive to rum1. S phase same in both strains in absence of rum1
PMID:32084401	FYPO:0001357	FigS1A,C 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	Fig1B cells blocked in G1 by nitrogen starvation and released in presence of nitrogen into S phase with cdc13+ switched off
PMID:32101481	PBO:0100707	Figure 6, A and B
PMID:32101481	PBO:0100706	Figure 6, A and B
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:32101481	FYPO:0007393	(Figure 2, C and
PMID:32101481	PBO:0100704	Figure 2D
PMID:32101481	PBO:0100695	Figure 1A and 1B
PMID:32101481	PBO:0100698	4B?
PMID:32101481	PBO:0100704	Figure 6E
PMID:32101481	PBO:0100702	Indeed, the percentage of tip septa was significantly reduced in mid1Δ pom1as1 cdc15-22D cells (Figure 4G).
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: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: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	PBO:0094604	fig 4g & S4. /Figure 5A)
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	PBO:0099437	3' mrna extension figure Figure 4C; Figure S3 Although the percentage of total reads was relatively small, the iss1-DC mutation caused a reproducible and statistically sig- nificant extension of the 30 end of transcripts by about 200 nt.
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:0099440	Figure S5 However, the truncation did not reduce Iss1 interaction with Rrp6
PMID:32101745	PBO:0099439	Figure 5F the iss1-DC truncation did disrupt its interaction with Mmi1.
PMID:32101745	PBO:0099438	Figure 5B the iss1-DC mutation significantly reduced H3K9me2 at both ssm4 and mei4).
PMID:32101745	FYPO:0004170	figure 3F
PMID:32101745	PBO:0094283	figure 3E
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen, spot assay
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen, spot assay
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007359	spot assay
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007359	spot assay
PMID:32142608	FYPO:0007359	spot assay
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007359	plate-based screen, spot assay
PMID:32142608	FYPO:0007358	spot assay
PMID:32142608	FYPO:0007358	plate-based screen, spot assay
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007359	spot assay
PMID:32142608	FYPO:0007358	plate-based screen, spot assay
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	MOD:00046	Phosphorylated during growth in media containing heavy water.
PMID:32142608	FYPO:0007359	spot assay
PMID:32142608	FYPO:0007359	spot assay
PMID:32142608	FYPO:0007359	spot assay
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	spot assay
PMID:32142608	FYPO:0007359	spot assay
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen, spot assay
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen, spot assay
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32142608	FYPO:0007358	plate-based screen
PMID:32168916	FYPO:0004085	fig3
PMID:32168916	FYPO:0002060	Figure S4
PMID:32168916	FYPO:0002060	Figure S4
PMID:32168916	FYPO:0002060	Figure S4
PMID:32168916	PBO:0101607	Figure 4 (ALSO TFIIH but not sure which sunbunit)
PMID:32168916	PBO:0101608	Figure 4 (ALSO TFIIH but not sure which sunbunit)
PMID:32168916	FYPO:0002060	Figure S4
PMID:32168916	PBO:0101610	Figure 3 & S4(ALSO TFIIH but not sure which sunbunit)
PMID:32168916	FYPO:0004085	fig3
PMID:32168916	PBO:0101609	Figure 4 SAP155K700E restopred splicing to prp10-1
PMID:32168916	PBO:0101609	Figure 3 & S4(ALSO TFIIH but not sure which sunbunit)
PMID:32204793	FYPO:0007346	Figure 7A,B; spot test and survival assay
PMID:32204793	FYPO:0007346	Figure 7A,B; spot test and survival assay
PMID:32204793	FYPO:0007346	Figure 7A,B; spot test and survival assay
PMID:32204793	PBO:0105172	in complex with Sfr1; Figure 6
PMID:32204793	PBO:0110075	actually inferred from combination of in vitro assay and phenotypes; Figures 1 & 5, including supplements
PMID:32204793	PBO:0105168	Figure 5B, Figure 5—figure supplement 1C
PMID:32204793	PBO:0105169	Figure 6—figure supplement 1
PMID:32204793	FYPO:0000265	Figure 1D, Figure 1—figure supplement 1; spot test and survival assay
PMID:32204793	FYPO:0000265	Figure 1D, Figure 1—figure supplement 1; spot test and survival assay
PMID:32204793	PBO:0105170	Figure 7C,D; spot test and survival assay
PMID:32204793	PBO:0110075	actually inferred from combination of in vitro assay and phenotypes; Figures 1 & 5, including supplements
PMID:32204793	PBO:0105171	Figure 7C,D; spot test and survival assay
PMID:32204793	PBO:0105171	Figure 7C,D; spot test and survival assay
PMID:32204793	PBO:0105170	Figure 7—figure supplement 1B; spot test
PMID:32204793	PBO:0105167	Figure 6—figure supplement 1
PMID:32204793	PBO:0105166	Figure 5B, Figure 5—figure supplement 1C
PMID:32204793	PBO:0105168	Figure 5B, Figure 5—figure supplement 1C
PMID:32204793	PBO:0105171	Figure 7—figure supplement 1B; spot test
PMID:32204793	PBO:0105171	Figure 7—figure supplement 1B; spot test
PMID:32204793	PBO:0105170	Figure 1—figure supplement 1A, Figure 7C,D, Figure 7—figure supplement 1A; spot test and survival assay
PMID:32204793	PBO:0105170	Figure 1—figure supplement 1A; spot test
PMID:32204793	PBO:0105170	Figure 1—figure supplement 1A; spot test
PMID:32204793	PBO:0105172	in complex with Swi5; Figure 6
PMID:32204793	PBO:0105169	Figure 5B, Figure 5—figure supplement 1C
PMID:32269268	FYPO:0007653	Fig 5
PMID:32269268	PBO:0107531	Fig 1
PMID:32269268	FYPO:0007226	Fig 5
PMID:32269268	PBO:0107528	Fig 1
PMID:32269268	PBO:0107526	Fig 1
PMID:32269268	PBO:0107527	Fig 1
PMID:32269268	PBO:0107524	"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	"25 degrees C; using ""low temperature"" to distinguish from 30 degrees C; Fig 1"
PMID:32269268	PBO:0033972	"25 degrees C; using ""low temperature"" to distinguish from 30 degrees C; Fig 1"
PMID:32269268	PBO:0107529	Fig 1
PMID:32269268	PBO:0107530	Fig 1
PMID:32269268	PBO:0107523	Fig 1
PMID:32269268	FYPO:0000220	Fig S2
PMID:32269268	FYPO:0004573	Fig 2, S1
PMID:32269268	PBO:0107525	"25 degrees C; using ""low temperature"" to distinguish from 30 degrees C; Fig 1"
PMID:32269268	GO:0140720	[vw added to cover missing EXP annotation based on localization phenotype below]
PMID:32269268	FYPO:0007654	Fig 5
PMID:32269268	FYPO:0007531	Fig 5
PMID:32269268	FYPO:0000220	Fig 4
PMID:32269268	FYPO:0004573	Fig 4
PMID:32269268	FYPO:0004137	Fig 2
PMID:32277274	PBO:0106053	fig2
PMID:32277274	FYPO:0007209	figb
PMID:32277274	FYPO:0000460	figa
PMID:32282918	PBO:0094805	Figure S7
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 and 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:0094856	Figure S2
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: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:0001355	Figure 5B
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:0000080	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:0000082	Figure 5A
PMID:32282918	FYPO:0000082	Figure 5A
PMID:32282918	FYPO:0001357	Figure 7A
PMID:32282918	FYPO:0000082	Figure 5A
PMID:32282918	PBO:0094776	Figure 3B
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:0094775	Figure 3B
PMID:32282918	PBO:0094774	Figure 3B
PMID:32282918	PBO:0094773	Figure 3B
PMID:32282918	PBO:0094772	Figure 3B
PMID:32282918	PBO:0094774	Figure 3B
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 and 9C
PMID:32282918	PBO:0094771	Figure 3A
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	FYPO:0002085	Figure 1
PMID:32282918	PBO:0094852	Figure S7
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:0094849	Figure S7
PMID:32282918	PBO:0094848	Figure S7
PMID:32282918	PBO:0094847	Figure S7
PMID:32282918	PBO:0094844	Figure S7
PMID:32282918	PBO:0094843	Figure S7
PMID:32282918	PBO:0094842	Figure S7
PMID:32282918	PBO:0094841	Figure S7
PMID:32282918	PBO:0094840	Figure S7
PMID:32282918	PBO:0094839	Figure S7
PMID:32282918	PBO:0094838	Figure S7
PMID:32282918	PBO:0094837	Figure S7
PMID:32282918	PBO:0094834	Figure S7
PMID:32282918	PBO:0094833	Figure S7
PMID:32282918	PBO:0094832	Figure S7
PMID:32282918	PBO:0094828	Figure S7
PMID:32282918	PBO:0094822	Figure S7
PMID:32282918	PBO:0094817	Figure S7
PMID:32282918	PBO:0094815	Figure S7
PMID:32282918	PBO:0094812	Figure S7
PMID:32282918	PBO:0094810	Figure S7
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:0094803	Figure S7
PMID:32282918	PBO:0094800	Figure S7
PMID:32282918	PBO:0094796	Figure S7
PMID:32282918	PBO:0094795	Figure S7
PMID:32282918	PBO:0094794	Figure S7
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: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:0094792	Figure S7
PMID:32282918	PBO:0094791	Figure S7
PMID:32282918	PBO:0094789	Figure S7
PMID:32282918	PBO:0094788	Figure S7
PMID:32282918	PBO:0094785	Figure S7
PMID:32282918	FYPO:0001355	Figure 2
PMID:32282918	FYPO:0001355	Figure 2
PMID:32282918	FYPO:0001357	Figure 7A
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:0001357	Figure 5C
PMID:32282918	FYPO:0001357	Figure S3
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	FYPO:0001357	Figure S3
PMID:32282918	FYPO:0001357	Figure 1
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	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: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	PBO:0094855	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: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	PBO:0094857	Figure S2
PMID:32295063	PBO:0102536	Loss of the HMG domain of Lsd2 (but not Lsd1) produces inviable cells (lethal).
PMID:32295063	PBO:0102522	KΔ::ade6+ monitored by qRT-PCR
PMID:32295063	GO:0031509	Fig. 4C
PMID:32295063	GO:0031509	Fig. 4C
PMID:32295063	PBO:0102552	KΔ::ade6+ monitored by qRT-PCR
PMID:32295063	FYPO:0003412	compared to Lsd1-ao single mutant
PMID:32295063	FYPO:0007339	compared to lsd1-ao single mutant
PMID:32295063	PBO:0102539	KΔ::ade6+ monitored by qRT-PCR
PMID:32319721	PBO:0100665	CFU counts
PMID:32320462	FYPO:0007678	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007440	Sterols accumulate in endosomes
PMID:32320462	FYPO:0007439	Eisosomes protruding towards cell interior
PMID:32320462	FYPO:0007676	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007678	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007440	Sterols do not accumulate in endosomes
PMID:32320462	FYPO:0007678	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007678	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007676	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007678	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007678	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007678	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007677	Evaluated with D4H sterol sensor; internal structures
PMID:32320462	FYPO:0007678	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007678	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007677	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007677	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0004963	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007676	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007678	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007678	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007678	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007677	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007676	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007678	Evaluated with D4H sterol sensor
PMID:32320462	FYPO:0007678	Evaluated with D4H sterol sensor
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:32327557	PBO:0097682	Fig. 3
PMID:32327557	PBO:0097681	Fig. 3
PMID:32327557	PBO:0097681	Fig. 3
PMID:32327557	PBO:0097690	Fig. 2
PMID:32327557	PBO:0097689	5ug/mL
PMID:32327557	PBO:0097688	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:0097673	Fig. 2
PMID:32327557	PBO:0112499	Fig. 2
PMID:32327557	PBO:0097675	Fig. 2
PMID:32327557	PBO:0097676	Fig. 2
PMID:32327557	FYPO:0007987	Fig. 2
PMID:32327557	PBO:0097677	Fig. 3
PMID:32327557	PBO:0097678	Fig. 3
PMID:32327557	PBO:0097679	Fig. 3
PMID:32327557	PBO:0097680	Fig. 3
PMID:32327557	PBO:0097681	Fig. 3
PMID:32327557	PBO:0097682	Fig. 3
PMID:32341083	FYPO:0001513	HU absent
PMID:32341083	PBO:0033067	HU absent
PMID:32341083	PBO:0104393	HU absent
PMID:32341083	PBO:0033071	HU absent
PMID:32355220	PBO:0095492	ade6B/ade6X at the ura4 locus
PMID:32355220	PBO:0095491	ade6B/ade6X at the ura4 locus
PMID:32355220	PBO:0095493	ade6B/ade6X at cen1
PMID:32355220	FYPO:0000185	ade6B/ade6X at the ura4 locus
PMID:32355220	FYPO:0006810	An extrachromosome ChLC
PMID:32355220	FYPO:0007425	ade6B/ade6X at the ura4 locus
PMID:32355220	FYPO:0006811	An extrachromosome ChLC
PMID:32355220	FYPO:0006811	An extrachromosome ChLC
PMID:32355220	FYPO:0007423	An extrachromosome ChLC
PMID:32355220	FYPO:0007423	An extrachromosome ChLC
PMID:32355220	FYPO:0007423	An extrachromosome ChLC
PMID:32355220	FYPO:0001742	PFGE; An extrachromosome ChLC
PMID:32355220	FYPO:0001742	PFGE; An extrachromosome ChLC
PMID:32355220	FYPO:0005788	ade6B/ade6X at cen1
PMID:32355220	PBO:0095493	ade6B/ade6X at cen1
PMID:32355220	PBO:0095493	ade6B/ade6X at cen1
PMID:32355220	PBO:0095493	ade6B/ade6X at cen1
PMID:32355220	PBO:0095493	ade6B/ade6X at cen1
PMID:32355220	PBO:0095494	ade6B/ade6X at cen1
PMID:32355220	PBO:0095494	ade6B/ade6X at cen1
PMID:32355220	PBO:0095494	ade6B/ade6X at cen1
PMID:32355220	FYPO:0006811	An extrachromosome ChLC
PMID:32355220	PBO:0095495	ade6B/ade6X at cen1
PMID:32355220	PBO:0095494	ade6B/ade6X at cen1
PMID:32355220	PBO:0095494	ade6B/ade6X at cen1
PMID:32355220	FYPO:0006811	An extrachromosome ChLC
PMID:32355220	FYPO:0001742	An extrachromosome ChLC
PMID:32355220	FYPO:0001859	An extrachromosome ChLC
PMID:32355220	FYPO:0007423	PFGE; An extrachromosome ChLC
PMID:32355220	FYPO:0000185	ade6B/ade6X at the ura4 locus
PMID:32355220	PBO:0095490	ade6B/ade6X at cen1
PMID:32355220	FYPO:0006810	An extrachromosome ChLC
PMID:32355220	FYPO:0006811	An extrachromosome ChLC
PMID:32355220	PBO:0095490	ade6B/ade6X at cen1
PMID:32355220	PBO:0095490	ade6B/ade6X at cen1
PMID:32355220	FYPO:0007423	An extrachromosome ChLC
PMID:32355220	FYPO:0006810	An extrachromosome ChLC
PMID:32355220	FYPO:0006810	An extrachromosome ChLC
PMID:32355220	PBO:0095491	ade6B/ade6X at the ura4 locus
PMID:32355220	FYPO:0006811	An extrachromosome ChLC
PMID:32355220	FYPO:0007424	PFGE; An extrachromosome ChLC
PMID:32355220	FYPO:0007425	ade6B/ade6X at the ura4 locus
PMID:32355220	FYPO:0007424	PFGE; An extrachromosome ChLC
PMID:32355220	FYPO:0006810	An extrachromosome ChLC
PMID:32355220	FYPO:0007423	An extrachromosome ChLC
PMID:32355220	FYPO:0007425	ade6B/ade6X at the ura4 locus
PMID:32361273	PBO:0104794	fig 2D length is 7.5 micron cf WT 6.2 in same conditions
PMID:32361273	PBO:0093823	fig1
PMID:32361273	FYPO:0003345	1D. The cells also presented a defect in the degradation of the cyclin Cdc13 and a delay in the dephosphorylation of Ste9
PMID:32361273	PBO:0096829	fig 7
PMID:32361273	PBO:0104802	protein phophatase substrate adaptor
PMID:32361273	PBO:0104801	(TAP-Par1F314Q), this interaction was reduced (Figure 6C)
PMID:32361273	PBO:0103204	Deletion of par1 also affected the survival of the wee1-50 mutant (Figure 4C), and this worsening of the phenotype corre- lated with the inability of the double wee1-50 par1D mutant to accumulate Rum1 (Figure 4D).
PMID:32361273	FYPO:0001387	Deletion of par1 also affected the survival of the wee1-50 mutant (Figure 4C), and this worsening of the phenotype corre- lated with the inability of the double wee1-50 par1D mutant to accumulate Rum1 (Figure 4D).
PMID:32361273	PBO:0104800	fig 4 Notably, loss of cig1 and cig2 utterly overrode these defects,
PMID:32361273	PBO:0104799	fig 2
PMID:32361273	PBO:0020550	Figure S4D
PMID:32361273	PBO:0101618	Figure S4D
PMID:32361273	PBO:0099448	Figure S4D
PMID:32361273	PBO:0023774	Figure S4D
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	FYPO:0001000	fig3
PMID:32361273	FYPO:0001043	fig3b
PMID:32361273	PBO:0104798	fig 2F
PMID:32361273	PBO:0104797	fig 3
PMID:32361273	FYPO:0001043	fig3
PMID:32361273	PBO:0104795	fig 2F
PMID:32361273	PBO:0104795	fig S2 B
PMID:32361273	PBO:0104795	fig 2E, S2A
PMID:32361273	PBO:0094966	fig 2D length is 10.299 micron cf WT 12.7 in same conditions
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:0104792	fig 2
PMID:32361273	PBO:0104791	fig 2
PMID:32361273	PBO:0104790	fig 1C (i.e normal TOR signalloing)
PMID:32361273	PBO:0104789	fig S1A
PMID:32361273	PBO:0096075	fig S1A
PMID:32361273	FYPO:0000708	fig1
PMID:32361273	FYPO:0001043	fig1
PMID:32361273	PBO:0097920	fig1
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	fig7A
PMID:32361273	FYPO:0007476	2G. the use of cdc10 mutant backgrounds is common for checking the ability of cells to arrest in G1
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	Surprisingly, pir2-1 showed a drastic upregulation of pho1 and byr2 genes as compared to wild- type (WT) (Fig. 1b),
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: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	GO:0031047	The requirement for Pir2 in mediating the repressive effects of lncRNAs is a highly significant finding.
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	PBO:0111097	However, the ago1Δ clr3Δ double mutant showed cumulative de-repression of pho1 (Fig. 5d).
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:0111092	(Fig. 1b), similar to the effect observed upon deletion of the lncRNA (Supplementary Fig. 1b)6,7,11.
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	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	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 immuno- precipitation 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:0111095	Interestingly, this interaction was impaired in the cwf10- 1 mutant, indicating that splicing factors are required for asso- ciation 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: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	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:0111091	(Fig. 1b), similar to the effect observed upon deletion of the lncRNA (Supplementary Fig. 1b)6,7,11.
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:0111090	as was also observed in mmi1Δ and rrp6Δ cells (Fig. 1a and Supplementary Fig. 1a)6
PMID:32415063	PBO:0111090	as was also observed in mmi1Δ and rrp6Δ cells (Fig. 1a and Supplementary Fig. 1a)6
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:0111089	as was also observed in mmi1Δ and rrp6Δ cells (Fig. 1a and Supplementary Fig. 1a)6
PMID:32415063	PBO:0111089	as was also observed in mmi1Δ and rrp6Δ cells (Fig. 1a and Supplementary Fig. 1a)6
PMID:32415063	PBO:0111089	The lncRNA-mediated repression of pho1 was impaired in cbc1-1 cells (Supplementary Fig. 1e), sug-
PMID:32496538	FYPO:0005518	Figure 6 and Supplementary Fig S8
PMID:32496538	FYPO:0002913	Strand-specific RT-qPCR; Figure 2
PMID:32496538	FYPO:0002913	Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5
PMID:32496538	FYPO:0002913	Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5
PMID:32496538	FYPO:0002913	Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5
PMID:32496538	FYPO:0006996	Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5
PMID:32496538	FYPO:0006996	Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5
PMID:32496538	FYPO:0006996	Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5
PMID:32496538	PBO:0095888	Figure 5; rbp1 also Figure 7
PMID:32496538	PBO:0101605	Supplementary Fig S7
PMID:32496538	PBO:0101605	Supplementary Fig S7
PMID:32496538	PBO:0101606	Supplementary Fig S7
PMID:32496538	FYPO:0005518	Supplementary Fig S8
PMID:32496538	FYPO:0005518	Supplementary Fig S8
PMID:32496538	FYPO:0007347	Supplementary Fig S7
PMID:32496538	FYPO:0007347	Supplementary Fig S7
PMID:32496538	FYPO:0007347	Supplementary Fig S7
PMID:32496538	FYPO:0004347	Figure 6 and Supplementary Fig S8
PMID:32496538	FYPO:0002913	Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5
PMID:32496538	FYPO:0002913	Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5
PMID:32496538	FYPO:0002913	Strand-specific RT-qPCR; 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	FYPO:0005518	Supplementary Fig S8
PMID:32496538	PBO:0101604	Figure 5; rbp1 also Figure 7
PMID:32496538	FYPO:0006996	Strand-specific RT-qPCR; Figure 2
PMID:32496538	FYPO:0002913	Strand-specific RT-qPCR; Figure 2
PMID:32496538	FYPO:0002913	Strand-specific RT-qPCR; Figure 2
PMID:32496538	FYPO:0002913	Strand-specific RT-qPCR; Figure 2
PMID:32496538	FYPO:0002913	Strand-specific RT-qPCR; Figure 2
PMID:32496538	FYPO:0002913	Strand-specific RNA-seq analysis, RT-PCR, Strand-specific RT-qPCR; Figure 1, 2 and 4; Supplementary Fig S1, S3 and S5
PMID:32496538	FYPO:0005516	Figure 6 and Supplementary Fig S8
PMID:32496538	FYPO:0002913	Strand-specific RNA-seq analysis, RT-PCR, Strand-specific RT-qPCR; Figure 1, 2 and 4; Supplementary Fig S1, S3 and S5
PMID:32496538	FYPO:0002913	Strand-specific RNA-seq analysis, RT-PCR, Strand-specific RT-qPCR; Figure 1, 2 and 4; Supplementary Fig S1, S3 and S5
PMID:32499400	PBO:0101148	EMM -U agar plates, supplemeted with 6AU concentration ranging from 3.6 to 150 ug/mL
PMID:32499400	PBO:0101147	100 ug/mL MPA
PMID:32499400	FYPO:0007411	at different lncRNA polyadenylation sites
PMID:32499400	PBO:0101157	also assayed genome-wide
PMID:32499400	PBO:0101157	also assayed genome-wide
PMID:32499400	PBO:0101156	at lncRNAs upstream of PHO regulon genes (nc-tgp1, nc-pho1, prt1)
PMID:32499400	PBO:0101155	at lncRNAs upstream of PHO regulon genes (nc-tgp1, nc-pho1, prt1)
PMID:32499400	PBO:0101151	at tgp1 promoter
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:0093562	Figure 2E
PMID:32499408	PBO:0098590	Figure 3
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: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: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:0094679	Figure 1B-E and supplementary Figure S1B
PMID:32499408	PBO:0094688	Figure 1B-E and supplementary Figure S1B
PMID:32499408	PBO:0098582	Figure 1B-E and supplementary Figure S1B
PMID:32499408	PBO:0095651	Figure 1B-E and supplementary Figure S1B
PMID:32499408	PBO:0094283	Figure 1B-E and supplementary Figure S1B
PMID:32499408	PBO:0098583	Figure 1B-E and supplementary Figure S1B
PMID:32499408	PBO:0094283	Figure 1B-E and supplementary Figure S1B
PMID:32499408	PBO:0098592	Figure 7A
PMID:32499408	PBO:0098591	fig 5e
PMID:32499408	PBO:0098584	Figure 3
PMID:32499408	PBO:0098586	(Figure 4B)
PMID:32502403	PBO:0106712	Apq12 localized in tubules con- nected 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: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	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: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: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), demon- strating 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:0022963	Figure 1A
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: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:0106711	Consistently, these cells showed a higher fre- quency of asymmetric NE divisions (Figure S2C)
PMID:32502403	GO:0140515	causally upstreasm of?
PMID:32502403	PBO:0106708	Apq12 localized in tubules con- nected 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 con- dition, 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 disas- semble by treating the cells with 30 mg/mL MBC, resulting in 35% (n = 34) of nuclear coalescence events.
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:32518066	GO:0008266	These data indicate that high affinity binding sites for the Lsm1–7 complex must be at the 3′ termini of RNA. On
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: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:0002085	Figure S1
PMID:32546512	FYPO:0006821	Figure 8
PMID:32546512	FYPO:0001357	Figure 8
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 5
PMID:32546512	PBO:0099750	Figure 5
PMID:32546512	PBO:0099750	Figure 5
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:0106694	Northern blotting and primer extension, Figure 6
PMID:32546512	PBO:0094775	Northern blotting, Figure 6
PMID:32546512	FYPO:0005369	Figure 2A
PMID:32546512	PBO:0094771	Figure 4
PMID:32546512	PBO:0094771	Figure 4
PMID:32546512	PBO:0094771	Figure 4
PMID:32546512	PBO:0094771	Figure 4
PMID:32546512	PBO:0094771	Figure 4
PMID:32546512	PBO:0094771	Figure 2B
PMID:32546512	PBO:0094738	Figure 5
PMID:32546512	PBO:0094738	Figure 2C
PMID:32546512	PBO:0094738	Figure 2B
PMID:32546512	PBO:0106693	Figure 2C
PMID:32546512	FYPO:0002061	Figure S1
PMID:32546512	FYPO:0002061	Figure S1
PMID:32546512	FYPO:0001234	Figure S1
PMID:32546512	FYPO:0001234	Figure S1
PMID:32546512	FYPO:0000082	Figure S1
PMID:32546512	FYPO:0004481	Figure S1
PMID:32546512	FYPO:0000082	Figure S1
PMID:32546512	FYPO:0000080	Figure S1
PMID:32546512	FYPO:0000080	Figure S1
PMID:32546512	FYPO:0001357	Figure 8
PMID:32546512	FYPO:0001357	Figure 8
PMID:32546512	GO:0043628	a scenario in which Erh1 acts as a brake on Mmi1’s ability to promote CPF-de- pendent termination during prt lncRNA synthesis.
PMID:32546512	GO:0043628	suggest ... Erh1 acts as a brake on Mmi1’s ability to promote CPF-de- pendent termination during prt lncRNA synthesis.
PMID:32546512	PBO:0094771	In addition, using the prt–pho1 reporter plas- mid 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	FYPO:0001357	Figure 8
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:0001045	Figure 4B
PMID:32546512	PBO:0094777	(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	(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 double- mutant was slow-growing on YES agar and cold-sensitive: he de-re- pression of Pho1 activity by erh1Δ was erased in the asp1-D333A back- ground
PMID:32546512	FYPO:0001234	Figure 2 We obtained viable erh1Figure 2A Δ asp1-D333A haploids after mating and sporulation; the double- mutant was slow-growing on YES agar and cold-sensitive: he de-re- pression of Pho1 activity by erh1Δ was erased in the asp1-D333A back- ground
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:0094777	Figure 2 vw changed from decreased to normal (compared to WT)
PMID:32546512	PBO:0094777	Figure 2 vw changed from decreased to normal (compared to WT)
PMID:32546512	PBO:0094771	Figure 4
PMID:32546512	FYPO:0000080	Figure 2A
PMID:32546512	FYPO:0000080	Figure 2A
PMID:32546512	FYPO:0000080	Figure 2
PMID:32546512	FYPO:0000080	Figure 2
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:32546830	PBO:0099069	Figure 2
PMID:32546830	GO:0005515	linker
PMID:32546830	FYPO:0002150	Figure 2E tetrad analysis
PMID:32571823	PBO:0096346	figure3D
PMID:32571823	FYPO:0005253	FIG 4 Ccr1 is a molecular target of TAM.
PMID:32571823	FYPO:0002060	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:32571823	PBO:0093642	figure 2d
PMID:32571823	PBO:0096345	figure3A (increased cacineurin signalling)
PMID:32571823	FYPO:0001198	figure3B
PMID:32571823	PBO:0096347	figure 2b
PMID:32571823	PBO:0093653	figure 1
PMID:32571823	PBO:0093653	figure 1
PMID:32571823	PBO:0096347	figure 2b
PMID:32571823	FYPO:0002716	fig5
PMID:32571823	FYPO:0000098	figure3C
PMID:32594847	FYPO:0001125	DNS
PMID:32594847	FYPO:0000047	DNS
PMID:32594847	FYPO:0001124	DNS
PMID:32650974	GO:0005515	split YFP and affinity capture
PMID:32650974	GO:0140497	M-Pol I complex
PMID:32650974	GO:0140497	M-Pol I complex
PMID:32650974	FYPO:0007436	swollen
PMID:32650974	GO:0018279	figures 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:0018279	figures 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: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	regulates pathway choice
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	PBO:0107263	Figure 5
PMID:32723864	PBO:0107264	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:0107265	Figure 5
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	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	FYPO:0001513	Figure 7
PMID:32723864	PBO:0107269	Figure 7
PMID:32723864	FYPO:0007756	Figure 7
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:32723864	PBO:0099173	Figure S1.
PMID:32723864	FYPO:0007746	Figure S1.
PMID:32723864	FYPO:0007746	Figure S1.
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	PBO:0107261	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: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:32735772	FYPO:0000843	Figure 6A
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:32735772	FYPO:0006294	Figure S1E nitrogen starvation-induced ER-phagy appeared to be normal in epr1D
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	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 bind- ing and contains the predicted FFAT motif, is sufficient for inter- acting with VAPs
PMID:32735772	PBO:0104089	Figure 3C The 42-amino-acid Epr1-C region (residues 339–380), which is capable of Atg8 bind- ing and contains the predicted FFAT motif, is sufficient for inter- acting with VAPs
PMID:32735772	PBO:0104091	Figure 3D ******check with DAN, is this an overexpression allele?
PMID:32735772	FYPO:0000843	Figure 6A
PMID:32735772	FYPO:0000843	Figure 6A
PMID:32735772	FYPO:0000843	Figure 6A
PMID:32735772	FYPO:0000843	Figure 6A
PMID:32735772	FYPO:0000843	Figure 6A
PMID:32735772	PBO:0093561	Fig. S1B
PMID:32735772	PBO:0104092	Figure 1C
PMID:32735772	PBO:0104090	Figure 1C
PMID:32735772	PBO:0104090	Figure 1C
PMID:32735772	GO:0000407	Figure 2a
PMID:32735772	GO:0044804	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	PBO:0104093	Figure 3C The 42-amino-acid Epr1-C region (residues 339–380), which is capable of Atg8 bind- ing and contains the predicted FFAT motif, is sufficient for inter- acting with VAPs
PMID:32735772	PBO:0104094	Figure 3C The 42-amino-acid Epr1-C region (residues 339–380), which is capable of Atg8 bind- ing and contains the predicted FFAT motif, is sufficient for inter- acting with VAPs
PMID:32735772	PBO:0104091	(Figure 3D) As expected, in cells lacking both Scs2 and Scs22, Epr1 became diffusely distributed in the cytoplasm
PMID:32735772	FYPO:0007449	figure 3D
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: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:0007444	Remarkably, Epr1-C, but not Epr1-N, could completely rescue the defects of epr1D in DTT-induced ER- phagy
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	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:0104095	The abilities of Epr1-C to bind Atg8 and VAPs using separate motifs suggest that one Epr1-C molecule may be able to interact with both an Atg8 molecule and a VAP molecule simultaneously and thereby bridge an Atg8-VAP association. To test this possi- bility, we performed an in vitro GST pull-down experiment using three proteins expressed in Escherichia coli: GST-tagged Scs2(1-126) corresponding to the FFAT-binding MSP domain, HA-tagged Atg8, and Smt3-tagged Epr1-C (Figure 4C). GST- Scs2(1-126) alone did not pull down Atg8. However, in the pres- ence of Epr1-C, GST-Scs2(1-126) efficiently pulled down both Epr1-C and Atg8, indicating that Epr1-C can bridge an indirect interaction between Scs2 and Atg8. Together, our results demonstrate that the main role of Epr1 in ER-phagy is to bridge an Atg8- VAP connection.
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:0007447	(Figure 5A) reduced in scs2D and abolished in scs2D scs22D
PMID:32735772	FYPO:0005264	fig 6b
PMID:32735772	FYPO:0000843	Figure 6A
PMID:32735772	FYPO:0005264	fig 6b
PMID:32735772	PBO:0104098	Figure 7E the ER-phagy defect of ire1D was largely rescued (Figure 7E).
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:0099298	viable spore yield assay
PMID:32790622	FYPO:0002052	viable spore yield assay
PMID:32790622	PBO:0099294	viable spore yield assay
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:0099293	viable spore yield assay
PMID:32817556	PBO:0097418	Phenotype is greatly enhanced by mutation of the IR-R boundary element
PMID:32841241	PBO:0102889	CCU codon/AGG anticodon tRNA
PMID:32841241	PBO:0102890	UAC codon/GUA anticodon tRNA
PMID:32841241	PBO:0102889	CCU codon/AGG anticodon tRNA
PMID:32841241	PBO:0102888	UAC codon/GUA anticodon tRNA
PMID:32841241	PBO:0102887	CCU codon/AGG anticodon tRNA
PMID:32841241	PBO:0102888	UAC codon/GUA anticodon tRNA
PMID:32841241	PBO:0102887	CCU codon/AGG anticodon tRNA
PMID:32841241	PBO:0102886	ACU codon/AGU anticodon tRNA
PMID:32841241	PBO:0102885	UAC codon/GUA anticodon tRNA
PMID:32841241	PBO:0102884	CCU codon/AGG anticodon tRNA
PMID:32841241	PBO:0102890	UAC codon/GUA anticodon tRNA
PMID:32841241	PBO:0102890	UAC codon/GUA anticodon tRNA
PMID:32841241	PBO:0102889	CCU codon/AGG anticodon tRNA
PMID:32848252	GO:0005637	Extended Data Figure 2 (nucleoplasmic side)
PMID:32848252	GO:0007084	lem2 (which encodes Lem2, the binding partner of Cmp7) is also SL with les1
PMID:32848252	GO:0007084	nstead, 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	PBO:0099376	causally upstream?
PMID:32848252	GO:0140512	fig 3b
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:0099373	fig 4/6
PMID:32848252	PBO:0099372	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	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:0099369	Les1 stalks functionally isolate daughter nuclei from the process of Imp1-dependent local NEB at the centre of the bridge prob- ably 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:32848252	PBO:0099364	extended fig4
PMID:32848252	PBO:0099362	Fig. 4, Extended Data Fig. 7
PMID:32878942	PBO:0099944	Fig S3F&G
PMID:32878942	PBO:0099946	Fig. S3A
PMID:32878942	PBO:0099942	Fig 4D,E&F
PMID:32878942	PBO:0099937	Figure 2D&E
PMID:32878942	FYPO:0003532	Fig S3B,C,&D
PMID:32878942	GO:0061245	Fig 3D
PMID:32878942	PBO:0099945	fig4
PMID:32878942	GO:2000099	Fig 3D
PMID:32878942	GO:2000099	Fig 3D
PMID:32878942	PBO:0099947	Fig. S3A
PMID:32878942	PBO:0099943	Fig 4H&I and S3F&G
PMID:32878942	PBO:0099943	Fig 4H&I and S3F&G
PMID:32878942	FYPO:0000674	Fig S3E
PMID:32878942	FYPO:0000674	Fig S3E
PMID:32878942	FYPO:0000674	Fig S3E
PMID:32878942	FYPO:0000674	Fig S3E
PMID:32878942	PBO:0099947	Fig. S3A
PMID:32878942	PBO:0099946	Fig. S3A
PMID:32878942	FYPO:0001396	Figure 2F-H
PMID:32878942	PBO:0099938	Figure 2I (vw changed tp FYPO:0002559)
PMID:32878942	FYPO:0003532	Fig S3B&C
PMID:32878942	FYPO:0003532	Fig S3B&C
PMID:32878942	PBO:0099943	Fig S3F
PMID:32896087	PBO:0092433	EMM media with arginine
PMID:32896087	PBO:0100493	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100492	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100492	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100492	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100492	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100492	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100493	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100493	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100492	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100493	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100492	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100493	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100494	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100494	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100494	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100494	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100494	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100495	Data from screening of prototroph deletion library
PMID:32896087	PBO:0100493	Liquid media growth assay. Mutant isolated from deletion collection.
PMID:32896087	PBO:0100493	Liquid media growth assay. Mutant isolated from deletion collection.
PMID:32896087	PBO:0092433	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	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:0100496	EMM media with arginine
PMID:32896087	PBO:0100496	EMM media with arginine
PMID:32896087	PBO:0100496	EMM media with arginine
PMID:32896087	PBO:0100496	EMM media with arginine
PMID:32896087	PBO:0100496	EMM media with arginine
PMID:32896087	PBO:0100496	EMM media with arginine
PMID:32896087	PBO:0100496	EMM media with arginine
PMID:32896087	PBO:0100496	EMM media with arginine
PMID:32896087	PBO:0100496	EMM media with arginine
PMID:32896087	PBO:0100496	EMM media with arginine
PMID:32896087	PBO:0100496	EMM media with arginine
PMID:32896087	PBO:0100496	EMM media with arginine
PMID:32896087	PBO:0100496	EMM media with arginine
PMID:32896087	PBO:0092433	EMM media with arginine
PMID:32896087	PBO:0100496	EMM media with arginine
PMID:32896087	GO:0005739	arg3-GFP fusion localisation in minimal media (EMM)
PMID:32896087	PBO:0100492	Liquid media growth assay. Mutant isolated from deletion collection.
PMID:32896087	PBO:0100492	solid media screen using prototroph deletion library.
PMID:32896087	PBO:0100493	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100494	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100494	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100493	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100492	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100494	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100492	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100492	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	PBO:0092433	EMM media with arginine
PMID:32896087	PBO:0100492	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100492	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100493	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100493	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100494	solid media screen using prototrophic deletion library
PMID:32896087	PBO:0100493	Liquid media growth assay. Mutant isolated from deletion collection.
PMID:32896087	PBO:0100493	Liquid media growth assay. Mutant isolated from deletion collection.
PMID:32896087	PBO:0100496	EMM media with arginine
PMID:32896087	PBO:0100496	EMM media with arginine
PMID:32896087	PBO:0100496	EMM media with arginine
PMID:32896087	PBO:0100496	EMM media with arginine
PMID:32896087	PBO:0092433	EMM media with arginine
PMID:32896087	PBO:0100496	EMM media with arginine
PMID:32908306	GO:0005739	Cup1-GFP immunofluorescence
PMID:32909946	FYPO:0006295	Fig 1a
PMID:32909946	FYPO:0006295	Fig 1 a
PMID:32909946	PBO:0096898	we found that in S. pombe, Atg1 from atg13D, atg17D, or atg101D mutant exhibited autophosphorylation activities simi- lar to that of Atg1 from wild type
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:32915139	PBO:0102270	Figure 1C
PMID:32915139	PBO:0102277	replaces wt annotation
PMID:32915139	PBO:0102277	replaces wt annotation
PMID:32915139	PBO:0093569	fig 3a
PMID:32915139	PBO:0102263	fig3b
PMID:32915139	FYPO:0004513	Overexpression under the control of B-estradiol promoter (vw: I added an allele synonym, later these will be searchable and visible)
PMID:32915139	PBO:0093569	fig1 SuppF
PMID:32915139	PBO:0093569	fi1 supp5
PMID:32915139	PBO:0102254	cells lacking Sty1 grew in these low LatA concentrations (Figure 1B).
PMID:32915139	FYPO:0004513	fig 1F
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:0102259	fig2-supp1
PMID:32915139	PBO:0102260	fig 5b
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:0102271	fig 4d
PMID:32915139	PBO:0102263	fig3c
PMID:32915139	PBO:0093569	fig 3a
PMID:32915139	PBO:0093570	fig1 SuppF
PMID:32915139	PBO:0093570	fig1 SuppF
PMID:32915139	PBO:0102270	Figure 1C
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	50%
PMID:32915139	PBO:0102260	fig 5b
PMID:32915139	PBO:0102262	25%
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: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:0007151	Figure 2A and C) check, has synonym increased stability (better than increased length?)
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: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:0102274	Figure 5—figure supplement 4
PMID:32915139	PBO:0102275	Figure 5—figure supplement 4
PMID:32915139	PBO:0102270	Figure 1C
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. 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. 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:0104048	Further analysis revealed that the levels of intron-retaining cox1 and cob1 tran- scripts were increased in 􏰀ppr10 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[􏰀i] and 􏰀ppr10[􏰀i] cells (Fig. 1E–G
PMID:33049028	FYPO:0001934	fig4
PMID:33049028	PBO:0100738	The results showed that in the intronless background, the cox1 and cob1 mRNAs were detected at similar levels in WT[􏰀i] and 􏰀ppr10[􏰀i] cells (Fig. 1E–G
PMID:33049028	PBO:0104049	Further analysis revealed that the levels of intron-retaining cox1 and cob1 tran- scripts were increased in 􏰀ppr10 cells in the intron-containing background (Fig. 1A–C)
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:0001355	Fig. 4B
PMID:33109728	FYPO:0002061	Fig. 4B
PMID:33109728	FYPO:0001357	Fig. 4B
PMID:33109728	FYPO:0001357	Fig. 4B
PMID:33109728	FYPO:0001357	Fig. 4B
PMID:33109728	FYPO:0001355	Fig. 4B
PMID:33109728	FYPO:0001357	Fig. 4B
PMID:33109728	FYPO:0001355	Fig. 4B
PMID:33109728	FYPO:0002061	Fig. 4B
PMID:33109728	FYPO:0002061	Fig. 4B
PMID:33125111	FYPO:0002401	(Fig. 1C).
PMID:33125111	FYPO:0000141	(Fig. 3).
PMID:33125111	FYPO:0000056	(Fig. 1A).
PMID:33125111	FYPO:0001234	(Fig. 1B). decreasing slows after 6 hours
PMID:33125111	FYPO:0000177	(Fig. 3).
PMID:33125111	FYPO:0007208	(Fig. 1C).
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	*****(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: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:33137119	PBO:0105953	Fig3A. affecting substrate Fkh2 in vitro
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:0105954	Fig3C. we found that Gad8-K263C is phosphorylated at T387 in Δtor1 cells under normal or low-glucose growth conditions.
PMID:33137119	PBO:0094345	Fig3C. 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	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	PBO:0093581	fig 6c L fig6D
PMID:33137119	PBO:0093581	fig 6c dominent negative effect
PMID:33137119	FYPO:0001021	pREP81-gad8-T260C. fig1a
PMID:33137119	FYPO:0000674	pREP81-gad8-T260C fig1a
PMID:33137119	PBO:0105948	affecting substrate Fkh2 in vitro
PMID:33137119	PBO:0105948	affecting substrate Fkh2 in vitro
PMID:33137119	PBO:0105947	affecting substrate Fkh2 in vitro
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:0105955	7B.
PMID:33137119	FYPO:0000674	fig1c
PMID:33137119	PBO:0093613	fig 6b
PMID:33137119	PBO:0093580	fig 6b
PMID:33137119	FYPO:0001021	fig1c
PMID:33137119	PBO:0105954	Fig3A. 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:0105956	Fig3A.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:0105949	Fig3A. affecting substrate Fkh2 in vitro
PMID:33137119	PBO:0105954	Fig3C. we found that Gad8-K263C is phosphorylated at T387 in Δtor1 cells under normal or low-glucose growth conditions.
PMID:33137119	PBO:0093823	pREP81-gad8-T260C fig 2B
PMID:33137119	PBO:0093612	figure 3d. I CHANGED THIS ONE< IS IT CORRECT?
PMID:33137119	PBO:0093558	fig 3b
PMID:33137119	FYPO:0005947	fig 3b
PMID:33137119	FYPO:0000674	fig 3B
PMID:33137119	PBO:0105952	Following release from campthotecin
PMID:33137119	PBO:0105950	affecting Gad8-S546 phosphorylation
PMID:33137119	PBO:0105950	affecting Gad8-S546 phosphorylation
PMID:33137119	PBO:0105950	affecting Gad8-S546 phosphorylation
PMID:33137119	PBO:0105948	affecting substrate Fkh2 in vitro
PMID:33137119	PBO:0105949	Fig3A. affecting substrate Fkh2 in vitro
PMID:33137119	FYPO:0001032	pREP81-gad8-Q298L
PMID:33137119	FYPO:0002578	pREP81-gad8-Q298L fig6D
PMID:33137119	PBO:0093824	pREP81-gad8-Q298L fig 5a
PMID:33137119	FYPO:0004765	fig2
PMID:33137119	PBO:0093824	pREP81-gad8-T260C fig 2B
PMID:33137119	PBO:0093824	pREP81-gad8-K263C
PMID:33137119	FYPO:0004765	pREP81-gad8-K263C
PMID:33137119	FYPO:0004765	pREP81-gad8-T260C fig2
PMID:33137119	FYPO:0001021	pREP81-gad8-K263C
PMID:33137119	FYPO:0000674	pREP81-gad8-K263C figure 2
PMID:33138913	FYPO:0007592	fig 3b
PMID:33138913	FYPO:0007448	fig1
PMID:33138913	FYPO:0007448	fig1
PMID:33138913	FYPO:0007596	fig1a
PMID:33138913	FYPO:0007596	Consistent with this, mitophagy was impaired in the mim1D and mim2D mutants (Figure 5D)
PMID:33138913	FYPO:0001355	Fig- ure 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	Fig- ure 5—figure supplement 1F
PMID:33138913	PBO:0092097	2A
PMID:33138913	FYPO:0007594	fig1D
PMID:33138913	FYPO:0007594	fig1
PMID:33138913	GO:0005741	figure 2F, 2G, 2H
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	PBO:0100128	We confirmed that Mim1 and Mim2 are required for stable localization of Tom70 on mitochondria in fis- sion 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	GO:0140595	MIM complex (requrested)
PMID:33138913	PBO:0100122	The interaction between full-length Atg43 and Mim2 was confirmed using reciprocal immunoprecipitation experi- ments (Figure 5A and Figure 5—figure supplement 1B).
PMID:33138913	PBO:0100123	figure 4G
PMID:33138913	PBO:0093560	fig 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	fig3 supp1b&c
PMID:33138913	FYPO:0007592	figure 4B
PMID:33138913	PBO:0100124	fig 4D
PMID:33138913	PBO:0100123	fig 4D
PMID:33138913	PBO:0100123	fig 3K
PMID:33138913	PBO:0093560	fig 3i
PMID:33138913	FYPO:0001357	figure 3I
PMID:33138913	FYPO:0007592	fig 3H
PMID:33138913	FYPO:0007592	fig 3H
PMID:33138913	FYPO:0007592	fig 3H
PMID:33138913	PBO:0100120	figure 3D
PMID:33138913	PBO:0100121	figure 3D
PMID:33138913	PBO:0100120	figure 3D
PMID:33138913	FYPO:0007594	check genotype. ***********figure 3c
PMID:33138913	FYPO:0007594	fig 3b/4b
PMID:33138913	PBO:0100119	fig 2.
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:0100133	figure 6B
PMID:33138913	PBO:0100134	figure 6B
PMID:33138913	PBO:0100133	figure 6B,D
PMID:33138913	PBO:0100132	This raises the possibility that the MIM complex assists Atg43 through facilitating its mitochondrial localization.
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:0100123	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: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 fis- sion yeast (Figure 5—figure supplement 1H
PMID:33153481	FYPO:0001352	Fig.2,3,S4; Hi-C, G2 arrested cells by cdc2-asM17
PMID:33153481	FYPO:0007517	Fig.4,S5; G2 arrested cells by cdc2-asM17
PMID:33153481	FYPO:0007519	Fig.6e; 3D quantification of DAPI stained DNA, G2 arrested cells by cdc2-asM17, + Thiolutin
PMID:33153481	FYPO:0000972	Fig. 6b-d; Rad52 foci quantification, G2 arrested cells by cdc2-asM17
PMID:33153481	FYPO:0007328	Fig. 6b-d; Rad52 foci quantification, G2 arrested cells by cdc2-asM17, + Thiolutin
PMID:33153481	FYPO:0007518	Fig. 6b-d; Rad52 foci quantification, G2 arrested cells by cdc2-asM17, + Thiolutin
PMID:33153481	FYPO:0007516	Fig.1a,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:0001221	Fig.S2; G2 arrested cells by cdc2-asM17
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: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	PBO:0100676	FISH; 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	GO:1990426	pmt3-D81R pmt3-KallR
PMID:33159083	FYPO:0007533	also assayed using ChIP to detect Rts1 binding to Npp106
PMID:33159083	PBO:0100676	FISH
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:33172987	PBO:0101371	(Fig. 1F-G
PMID:33172987	GO:0005546	Fig. 1D-E
PMID:33172987	PBO:0101372	Figure 3A
PMID:33172987	FYPO:0000339	Figure 4E-F
PMID:33172987	PBO:0101371	Figure S1
PMID:33172987	PBO:0101371	Figure S1
PMID:33172987	PBO:0101371	Figure S1
PMID:33172987	PBO:0101371	Figure S1
PMID:33172987	PBO:0101373	Figure S2
PMID:33172987	PBO:0101372	(Fig. S2B).
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	FYPO:0001357	Figure S2
PMID:33172987	PBO:0101374	Figure S3
PMID:33172987	FYPO:0001355	Figure S3
PMID:33172987	GO:0005543	Figure 3
PMID:33172987	GO:0005543	Opy1 PH1 (aa1-128) can directly bind phospholipids in vitro Figure 1
PMID:33172987	GO:1902635	I changed the function annotation to this process annotation because it precisely negates the SGD annotation
PMID:33172987	PBO:0101375	Figure1C (requested normal membrane lipid binding)
PMID:33172987	PBO:0101376	Figure 1C
PMID:33172987	GO:0005515	PH1 domain Fig. 2A, Table S2
PMID:33172987	PBO:0095685	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	FYPO:0001357	Figure S2
PMID:33172987	FYPO:0001355	Figure S3
PMID:33176147	FYPO:0007544	fig1E
PMID:33176147	FYPO:0007543	fig1F
PMID:33176147	FYPO:0007542	fig1F/figS2A
PMID:33176147	FYPO:0005018	fig1F
PMID:33176147	PBO:0094949	fig 2A
PMID:33176147	FYPO:0005555	figure 2c Figures 3B and S3B Figures 4C and 4D
PMID:33176147	FYPO:0005555	figure 2c Figures 3B and S3B Figures 4C and 4D
PMID:33176147	PBO:0100477	Figures 4E and 4F
PMID:33176147	PBO:0100478	Figures 4E and 4F
PMID:33176147	PBO:0100478	Figures 4E and 4F
PMID:33176147	FYPO:0005018	fig1F
PMID:33176147	FYPO:0007544	fig1E
PMID:33176147	FYPO:0007544	fig1E
PMID:33176147	FYPO:0007542	figS2A
PMID:33176147	PBO:0096647	fig 2A
PMID:33202882	PBO:0099385	intron 2
PMID:33225241	PBO:0093559	same as mas5delta alone
PMID:33225241	PBO:0093559	same as mas5delta alone
PMID:33357436	PBO:0106496	Figure 4F
PMID:33357436	PBO:0106491	fig 2B in vitro binding assay with Cdc15 F-BAR domain and Cdc12 peptide aa20-40
PMID:33357436	PBO:0106492	Figure 3A
PMID:33357436	FYPO:0004594	additional cewlll. poles
PMID:33357436	FYPO:0001365	Figures 3C and 3D
PMID:33357436	PBO:0106495	In vitro binding assay with Cdc15 F-BAR domain and full length Pxl1
PMID:33357436	FYPO:0005221	Figure S2B electron microscopy of purified Cdc15 F-BAR domain
PMID:33357436	PBO:0106497	Figure S2C
PMID:33357436	PBO:0106498	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:0099724	Figure S2E
PMID:33378674	GO:0006335	at pericentromeric regions
PMID:33378677	PBO:0107726	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:0107727	inferred from abolished interaction between Pof8 and Lsm subunits
PMID:33400299	FYPO:0006141	figure 4b
PMID:33400299	PBO:0103220	3a glucose starve
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:0007617	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	FYPO:0006141	figure 4b
PMID:33400299	FYPO:0006141	figure 4b
PMID:33400299	PBO:0103217	Figure 2n
PMID:33400299	FYPO:0006141	figure 4b
PMID:33400299	FYPO:0006141	figure 4b
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:0020037	3a glucose starve
PMID:33400299	PBO:0103219	3a glucose r excess
PMID:33400299	PBO:0103218	Figure 2n
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	PBO:0103212	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	PBO:0103212	Figure 1m
PMID:33400299	FYPO:0006141	figure 4b
PMID:33400299	PBO:0103214	Figure 1m
PMID:33400299	PBO:0103216	(Figure 2k–m).
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:0103217	Figure 2n
PMID:33400299	FYPO:0006141	figure 4b
PMID:33400299	FYPO:0006141	figure 4b
PMID:33410907	FYPO:0003004	(is thsi |+h2os, check) the intracellular level of ROS was elevated in pin1 and ssu72 mutants (Figure 6H),
PMID:33410907	FYPO:0006819	Figure 1
PMID:33410907	FYPO:0000087	Figure 1
PMID:33410907	FYPO:0005889	Figure 5e
PMID:33410907	FYPO:0000087	Figure 5
PMID:33410907	FYPO:0001103	Figure 5
PMID:33410907	PBO:0103163	Figure 4. Sty1 interacted and phosphorylated Rpb1-CTD at Ser5.
PMID:33410907	PBO:0096825	Figure 4. Sty1 interacted and phosphorylated Rpb1-CTD at Ser5.
PMID:33410907	PBO:0092468	Figure 1
PMID:33410907	PBO:0092468	Figure 1
PMID:33410907	PBO:0092468	Figure 1
PMID:33410907	PBO:0101320	fig2a
PMID:33410907	PBO:0103164	fig? (under calf alkaline phosphatase treated)
PMID:33410907	PBO:0097080	Figure 1C
PMID:33410907	PBO:0097079	Figure 1C
PMID:33410907	PBO:0103181	Figure 2c (this replaces the sty1 WT annotation Should this be normal? i.e. normal for the conditions? )
PMID:33410907	PBO:0103180	Figure 2c (this replaces the sty1 WT annotation Should this be normal? i.e. normal for the conditions? )
PMID:33410907	PBO:0094384	Figure 1C
PMID:33410907	PBO:0103165	2B
PMID:33410907	PBO:0103166	2B
PMID:33410907	PBO:0103167	2B
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: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: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: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:0103171	In line with theseresults, Ser2 phosphorylation of Rpb1-CTD, which facilitatedtranscription elongation, was reduced in pin1 mutantas a secondary effect derived from defect in transcription initiation to elongation (Figure 3A and B).
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: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: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:0114650	Figure 6c AND The anti-myc, anti-Rpb1 CTD (8WG16) and anti-pS5-Rpb1 CTD (H14) antibodies were used for immunoprecipitation.
PMID:33410907	PBO:0103178	Figure 4. Sty1 interacted and phosphorylated Rpb1-CTD at Ser5.
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	FYPO:0003004	(is this +H2o2, check) the intracellular level of ROS was elevated in pin1 and ssu72 mutants (Figure 6H),
PMID:33410907	PBO:0111318	( Figure 5D **I moved this from a WT phenotype)
PMID:33419777	FYPO:0007660	Fig 2, Table 2
PMID:33419777	FYPO:0007474	Fig 3I same in wild type background
PMID:33419777	FYPO:0007474	Fig3H same in wild type background
PMID:33419777	FYPO:0007660	Fig 3A-F same result in Wild type background
PMID:33419777	FYPO:0007660	Fig3A-F same result in wild type background
PMID:33419777	FYPO:0007660	Fig 2, Table 2
PMID:33419777	FYPO:0007474	Fig1B, C Table 1
PMID:33419777	FYPO:0007474	Fig1B, C Table 1
PMID:33419777	FYPO:0007474	Fig1B, C Table 1
PMID:33419777	PBO:0107435	increased cell size variability. 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	Fig5C 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	FYPO:0007474	Fig5C Table 3
PMID:33419777	PBO:0107437	Fig4A.
PMID:33419777	PBO:0104580	Fig5A
PMID:33419777	PBO:0107432	Fig1A
PMID:33419777	PBO:0107436	Fig5 E,F abnormal protein localisation in multinucleated cells
PMID:33419777	FYPO:0007474	Fig1B, C Table 1
PMID:33419777	FYPO:0007474	Fig1B, C Table 1
PMID:33419777	PBO:0107435	Fig5C 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	Fig5C 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:33419777	PBO:0102590	Fig5A
PMID:33419777	PBO:0102679	Fig5A
PMID:33419777	PBO:0107434	Fig4 B,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	FigS1. delayed septation, Cellular phenotype where cells initiate growth before septation has taken place, resulting in variable cell size at division.
PMID:33419777	PBO:0107433	Fig4A
PMID:33434270	PBO:0106086	Figure. 5A
PMID:33434270	PBO:0106087	Figure. 6A
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: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	PBO:0097069	figure 3a
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 though the expression levels of Mdm12 were comparable in WT and emr1Δ Cells
PMID:33483504	PBO:0097073	fig 5
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	GO:0120010	er to mitochondria
PMID:33483504	FYPO:0000895	fig1 (cox4-GFP to label Mt)
PMID:33483504	FYPO:0007611	fig. 1a
PMID:33483504	PBO:0097067	fig. 1b n=344
PMID:33483504	FYPO:0001234	fig. 1b n=344
PMID:33483504	PBO:0095634	fig 1c
PMID:33483504	GO:0032473	integral 2a,b,c,d
PMID:33496728	FYPO:0000161	Figure S1
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 (VW: changed severity from high to low as this seems to partially rescue mid1-delta?)
PMID:33496728	FYPO:0007832	Figure 5
PMID:33496728	PBO:0104822	Figure 1, Figure 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:0000161	Figure 6
PMID:33496728	FYPO:0003946	Figure S3
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	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:0000161	Figure 1A, B
PMID:33496728	PBO:0104824	Figure 1E, F. 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:33496728	FYPO:0003946	Figure S3
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 1
PMID:33496728	FYPO:0001364	Figure S1
PMID:33496728	FYPO:0000161	Figure S1
PMID:33496728	FYPO:0001368	Figure S1
PMID:33506191	PBO:0102842	fig4
PMID:33506191	PBO:0102837	fig1
PMID:33506191	PBO:0102837	fig1
PMID:33506191	PBO:0102837	fig1
PMID:33506191	PBO:0102837	fig1
PMID:33506191	PBO:0102837	fig1
PMID:33506191	PBO:0102837	fig1
PMID:33506191	PBO:0102837	fig1
PMID:33506191	PBO:0102838	fig1
PMID:33506191	PBO:0102838	fig1
PMID:33506191	PBO:0102838	fig1
PMID:33506191	PBO:0102838	fig1
PMID:33506191	PBO:0102838	fig1
PMID:33506191	PBO:0102838	fig1
PMID:33506191	PBO:0102839	fig2 live cell imaging
PMID:33506191	PBO:0102840	fig2 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	"fig4 If possible, please add the following comment - “The nucleus is retained in the center of the cell during mitosis."""
PMID:33506191	PBO:0102842	fig4
PMID:33506191	PBO:0102842	fig6
PMID:33506191	PBO:0102843	Fig7
PMID:33511417	FYPO:0004491	genome-wide average
PMID:33511417	FYPO:0007656	genome-wide average; slightly increased amplitudes of the -2, -1, +1 nucleosome peaks (relative to NDR)
PMID:33526714	PBO:0099413	figure2
PMID:33526714	PBO:0099413	figure2
PMID:33526714	PBO:0099410	figure 2
PMID:33526714	PBO:0099410	figure 2
PMID:33526714	PBO:0099410	figure2
PMID:33526714	PBO:0099412	figure2
PMID:33526714	PBO:0099411	figure2
PMID:33526714	PBO:0099410	figure2
PMID:33526714	PBO:0099410	figure2
PMID:33526714	PBO:0099410	figure2
PMID:33526714	PBO:0099413	figure2
PMID:33526714	PBO:0099413	figure2
PMID:33526714	PBO:0099413	figure2
PMID:33526714	PBO:0099413	figure2
PMID:33529549	PBO:0109808	Figure 1. Increased equational segregation in 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	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 signifi- cantly 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	GO:0031619	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:33534698	PBO:0100004	(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:33534698	PBO:0100006	5A). 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 medi- ated by the Gcn2-eIF2a-Fil1 pathway.
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	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:0001357	Figure 2a
PMID:33534698	FYPO:0001357	Figure 2a
PMID:33534698	FYPO:0001357	Figure 2a
PMID:33534698	FYPO:0001357	Figure 2a
PMID:33534698	PBO:0099988	fig4a
PMID:33534698	PBO:0099988	fig 4 a 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: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	GO:0010508	Autophagy in response to leucine starvation was abrogated by the gcn1D, but not gcn20D, mutation (Figure 4D),
PMID:33534698	FYPO:0001355	Figure 2a
PMID:33534698	PBO:0099986	Gcn2-dependent induction of autoph- agy 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: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	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: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 (Fig- ure 4—figure supplement 1H).
PMID:33534698	FYPO:0001355	Figure 2a
PMID:33534698	FYPO:0007803	Moreover, S. pombe cells lacking Gcn3 (Figure 4D) or Fil1 (Figure 4F) displayed autophagy defects during leucine starvation.
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 ala- nine (eIF2a-S52A).
PMID:33534698	PBO:0099984	vw I edited to make the response the extension to GCN2 mediated signalling, but I hope to improve these GO terms.
PMID:33534698	PBO:0093560	Figure 2b
PMID:33534698	FYPO:0001357	Figure 2b (any1 reescues)
PMID:33534698	FYPO:0001357	Figure 2b (any1 rescues)
PMID:33534698	FYPO:0001357	Figure 2e (sea3 rescued by gtr1 GDP-locked)
PMID:33534698	PBO:0099989	Figure 2f
PMID:33534698	FYPO:0001357	Figure 2e (sea3 rescued by gtr1 GDP-locked)
PMID:33534698	PBO:0099990	Figure 2g
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: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: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:0099993	Consis- tently, 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:0099994	Furthermore, consi tent with the essential role of Sea3 in the interaction between GATOR1 and the other GATOR2 sub- units, the vacuolar localization of Sea2, Sea4, and Seh1 ( was abrogated in the sea3D background (Figure 3—figure supplement 1C–E).
PMID:33534698	PBO:0099995	(Figure 3—figure supplement 1C–E).
PMID:33534698	PBO:0099996	(Figure 3—figure supplement 1C–E).
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:0099998	(Figure 3—figure supplement 2E,F and G),
PMID:33534698	PBO:0099999	(Figure 3—figure supplement 2E,F and G),
PMID:33534698	FYPO:0001357	Figure 2a
PMID:33534698	FYPO:0001357	Figure 2a
PMID:33534698	FYPO:0001357	Figure 2a
PMID:33534698	PBO:0100000	On the other hand, immuno- precipitation 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	FYPO:0001357	(Figure 3—figure supplement 3A), indicating that Arg854 of S. pombe Iml1 is not essential for the GATOR1 function.
PMID:33534698	PBO:0100001	(DIRECTLY INHIBITS) 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	PBO:0100002	(DIRECTLY INHIBITS) 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	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:33536395	GO:0006890	changed from protein retention in ER lumen
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	PBO:0095408	The gmn2∆ cells were highly sen- sitive to hygromycin B, being unable to grow on YES plates containing 25 μg/ml of the drug (Fig. 3A)
PMID:33536395	PBO:0106841	Fig. 3B
PMID:33536395	FYPO:0007288	Fig. 3C
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	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	FYPO:0007800	In contrast, gmn2∆ cells missorted and secreted a significant amount of BiP to the cell surface. These re- sults indicate that Gmn2p is required for normal retention of a luminal ER protein in S. pombe cells.
PMID:33536395	FYPO:0007800	In contrast, gmn2∆ cells missorted and secreted a significant amount of BiP to the cell surface. These re- sults indicate that Gmn2p is required for normal retention of a luminal ER protein in S. pombe cells.
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	GI Redundancy
PMID:33568651	FYPO:0004251	Polymerase usage sequencing
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:0005031	Polymerase usage sequencing
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:33568651	FYPO:0007679	Polymerase usage sequencing
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	GO:0080008	which?
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	FYPO:0007226	the deletion of ubi4, ddb1 or cul4 restored ade6-DSR silencing (Fig. 3g and Extended Data Fig. 3d).
PMID:33574613	GO:0080008	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	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:0105028	figure 1c
PMID:33574613	FYPO:0003235	Extended data Fig 1 b c (also at MTREC independent islands)
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: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: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: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 part- ner Pir1
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:0110910	he Tor2-containing TORC1 complex phosphorylated Pir1 in vitro and mutation of the 12 serine residues to alanine attenu- ated Pir1 phosphorylation (Extended Data Fig. 2a,c).
PMID:33574613	PBO:0105031	Fig 1 a
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:0105030	Fig 1 a
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	PBO:0105049	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:0105051	Compared with the WT, cells expressing Pir1-SD showed a marked decrease in recombination frequency (Fig. 6f).
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	FYPO:0004159	Defective chromosome segregation and reduced spore viability were also noted (Fig. 7a and Supplementary Videos 1–3)
PMID:33574613	FYPO:0000581	Defective chromosome segregation and reduced spore viability were also noted (Fig. 7a and Supplementary Videos 1–3)
PMID:33574613	FYPO:0003066	abnormal asci containing fewer than four, or no, spores were frequently generated (Fig. 7c).
PMID:33574613	MOD:01148	figure 1h
PMID:33574613	PBO:0105032	Fig. 1f,g
PMID:33574613	PBO:0105031	Fig 1 a
PMID:33574613	PBO:0105030	Fig 1 a
PMID:33574613	PBO:0105027	Fig 1 b (1.5x) (me2)
PMID:33574613	PBO:0105026	Fig 1 b (me2)
PMID:33574613	PBO:0105025	Fig 1 b (me2)
PMID:33574613	PBO:0105029	figure 1e
PMID:33574613	PBO:0105045	restores the MTREC and Rrp6 association with Mmi1 and Erh1 during meiosis (Fig. 5d).
PMID:33574613	PBO:0105044	restores the MTREC and Rrp6 association with Mmi1 and Erh1 during meiosis (Fig. 5d).
PMID:33574613	FYPO:0007686	Whereas Pir1-WT disappeared, Pir1-SD per- sisted during meiosis as multiple nuclear foci coinciding with Mmi1 and Erh1 foci (Fig. 5b,c).
PMID:33574613	PBO:0092302	Notably, Pir1 was depleted during early meiosis (Fig. 5a) but gradually recov- ered by middle meiosis.
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: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	We indeed observed that pir1∆ cells exhibited a growth defect on minimal medium
PMID:33574613	FYPO:0001355	We indeed observed that pir1∆ cells exhibited a growth defect on minimal medium
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	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: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: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: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: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: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:33579781	PBO:0094771	Fig. 5B
PMID:33579781	GO:0006369	Need to add modified version
PMID:33579781	FYPO:0002141	Fig. 2 However, S. pombe is viable when Pro3 or Pro6 is changed to alanine in every other heptad, includ- ing 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	FYPO:0000080	Fig. 2
PMID:33579781	PBO:0096584	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, includ- ing 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:0096575	Fig. 4A
PMID:33579781	PBO:0096576	Fig. 4A
PMID:33579781	PBO:0096577	Fig. 4A
PMID:33579781	PBO:0096578	Fig. 4A
PMID:33579781	PBO:0096579	Fig. 4A
PMID:33579781	PBO:0096576	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:0096583	Fig. 4A
PMID:33579781	PBO:0094773	Fig. 4A
PMID:33579781	PBO:0096585	Fig. 4A
PMID:33579781	FYPO:0001355	Fig. 5A
PMID:33579781	PBO:0094738	Fig. 5B
PMID:33579781	PBO:0094738	Fig. 5B
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:0094771	Fig. 5B
PMID:33579781	PBO:0094771	Fig. 5B
PMID:33579781	PBO:0094771	Fig. 5B
PMID:33658433	PBO:0103648	vw:added nucleosome assembly
PMID:33670267	FYPO:0007722	ATPase assay
PMID:33670267	FYPO:0004227	TAP co-purification, Western blot for histone H3
PMID:33670267	FYPO:0007722	ATPase assay
PMID:33670267	FYPO:0004227	TAP co-purification, Western blot for histone H3
PMID:33670267	FYPO:0007722	ATPase assay
PMID:33670267	FYPO:0007722	ATPase assay
PMID:33670267	FYPO:0004227	TAP co-purification, Western blot for histone H3
PMID:33670267	FYPO:0004227	TAP co-purification, Western blot for histone H3
PMID:33683349	FYPO:0002060	figure 6b
PMID:33683349	PBO:0094949	fig 5a
PMID:33683349	PBO:0107206	"fig1 &2 Nick suggested ""mitotic catastrophe""We would make this a related synonym?"
PMID:33683349	FYPO:0000082	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 addi- tion to, Cdc13/CDK activity.
PMID:33683349	PBO:0094949	figure 4
PMID:33683349	PBO:0094645	fig3
PMID:33683349	FYPO:0002516	fig 5
PMID:33683349	FYPO:0000400	QUESTION ig 5b (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:0037130	fig3
PMID:33683349	PBO:0037130	fig3
PMID:33683349	PBO:0019208	fig3 (i.e wee?)
PMID:33683349	PBO:0095165	fig2 (30 degrees) wee1-50ts mik1D cells divide at a smaller size than wee1-50ts mik1D cig2D cells
PMID:33711009	FYPO:0005369	20°
PMID:33711009	FYPO:0005369	20°
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	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:33711009	FYPO:0005369	20°
PMID:33711009	FYPO:0005369	20°
PMID:33711009	FYPO:0005369	20°
PMID:33723569	FYPO:0007711	live-cell imaging, 25ºC
PMID:33723569	FYPO:0007711	live-cell imaging, 25ºC
PMID:33723569	FYPO:0007710	live-cell imaging, 25ºC
PMID:33723569	FYPO:0007710	live-cell imaging, 25ºC
PMID:33723569	FYPO:0007710	live-cell imaging, 25ºC
PMID:33723569	FYPO:0007710	live-cell imaging, 25ºC
PMID:33723569	FYPO:0007711	live-cell imaging, 25ºC
PMID:33723569	PBO:0093585	25ºC
PMID:33723569	PBO:0093585	25ºC
PMID:33723569	PBO:0093585	25ºC
PMID:33723569	FYPO:0006686	live-cell imaging, 25ºC
PMID:33723569	FYPO:0006686	live-cell imaging, 25ºC
PMID:33723569	FYPO:0004516	live-cell imaging, 25ºC
PMID:33723569	FYPO:0007328	live-cell imaging, 25ºC
PMID:33723569	FYPO:0007328	live-cell imaging, 25ºC
PMID:33723569	FYPO:0007328	live-cell imaging, 25ºC
PMID:33723569	FYPO:0002573	live-cell imaging, 25ºC
PMID:33723569	FYPO:0002573	live-cell imaging, 25ºC
PMID:33723569	FYPO:0007710	live-cell imaging, 25ºC
PMID:33723569	FYPO:0000972	live-cell imaging, 25ºC
PMID:33723569	FYPO:0007328	live-cell imaging, 25ºC
PMID:33723569	FYPO:0002573	live-cell imaging, 25ºC
PMID:33723569	FYPO:0004466	live-cell imaging, 25ºC
PMID:33723569	FYPO:0000089	32ºC
PMID:33723569	FYPO:0000088	32ºC
PMID:33723569	FYPO:0000268	32ºC
PMID:33723569	FYPO:0001355	32ºC
PMID:33723569	PBO:0093616	32ºC
PMID:33723569	PBO:0093629	32ºC
PMID:33723569	FYPO:0000268	32ºC
PMID:33723569	FYPO:0000089	32ºC
PMID:33723569	FYPO:0004709	live-cell imaging, 25ºC
PMID:33723569	FYPO:0004516	live-cell imaging, 25ºC
PMID:33723569	FYPO:0004516	live-cell imaging, 25ºC
PMID:33723569	FYPO:0004516	live-cell imaging, 25ºC
PMID:33723569	FYPO:0000085	32ºC
PMID:33723569	PBO:0093773	25ºC
PMID:33723569	FYPO:0006686	live-cell imaging, 25ºC
PMID:33723569	PBO:0093585	25ºC
PMID:33723569	FYPO:0002601	25ºC
PMID:33723569	FYPO:0002573	live-cell imaging, 25ºC
PMID:33723569	FYPO:0000972	live-cell imaging, 25ºC
PMID:33723569	FYPO:0003906	25ºC
PMID:33723569	FYPO:0003503	25ºC, live-cell imaging, cell length at septation
PMID:33723569	FYPO:0003503	25ºC, live-cell imaging, cell length at septation
PMID:33723569	PBO:0093585	25ºC
PMID:33723569	FYPO:0002553	25ºC
PMID:33723569	FYPO:0006687	live-cell imaging, 25ºC
PMID:33723569	FYPO:0006686	live-cell imaging, 25ºC
PMID:33723569	FYPO:0004516	live-cell imaging, 25ºC
PMID:33723569	FYPO:0002573	live-cell imaging, 25ºC
PMID:33754639	FYPO:0002061	temperature sensitive 37°
PMID:33771877	PBO:0099491	Fig 2b
PMID:33771877	PBO:0099492	Fig 2
PMID:33771877	PBO:0099493	Fig 2
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	fig3.
PMID:33771877	PBO:0099494	fig 1
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:0099497	fig3.
PMID:33771877	PBO:0099498	fig3.
PMID:33771877	FYPO:0007738	fig 1
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: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:0099495	fig3.
PMID:33775921	FYPO:0001355	highest overexpression level
PMID:33788833	GO:0005802	co-localization with Cfr1
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:0095513	The mutant protein is observed faintly at the vacuolar surface of a low percentage of cells
PMID:33788833	PBO:0095512	The mutant protein is observed at the vacuolar surface
PMID:33788833	PBO:0095511	same as vps35delta alone
PMID:33788833	PBO:0095511	same as vps35delta alone
PMID:33788833	PBO:0095510	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:0095504	Affecting Vps10 and the PI(3) probe Cherry-FYVE
PMID:33788833	PBO:0095507	Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE
PMID:33788833	PBO:0095506	Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE
PMID:33788833	PBO:0095505	Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE
PMID:33788833	PBO:0095504	Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE
PMID:33788833	PBO:0095503	Affecting Cps1 carboxypeptidase
PMID:33788833	PBO:0095502	Affecting Cps1 carboxypeptidase
PMID:33788833	PBO:0093594	1.0 M KCl
PMID:33788833	PBO:0095501	80 mM MgCl2
PMID:33788833	PBO:0095509	The mutant protein is observed at the vacuolar surface
PMID:33788833	GO:0031902	co-localization with Vps35 and with Vps27
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	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:0095520	same as fsv1delta alone
PMID:33788833	PBO:0095526	Affecting Cps1 carboxypeptidase
PMID:33788833	PBO:0095503	Affecting Cps1 carboxypeptidase
PMID:33788833	PBO:0095529	Affecting Cps1 carboxypeptidase
PMID:33788833	PBO:0095530	Affecting Cps1 carboxypeptidase
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: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:0095510	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:33823663	PBO:0104294	figure9
PMID:33823663	FYPO:0007963	DNS
PMID:33823663	PBO:0104295	figure 9 modified form is activated for sexual differentiation
PMID:33823663	FYPO:0007963	DNS
PMID:33825974	FYPO:0004665	live cell imaging with 3D structured illumination microscopy (3D-SIM)
PMID:33825974	FYPO:0004665	live cell imaging with 3D structured illumination microscopy (3D-SIM)
PMID:33825974	FYPO:0004665	live cell imaging with 3D structured illumination microscopy (3D-SIM)
PMID:33825974	FYPO:0004602	Figure s2 (c); live cell imaging with 3D structured illumination microscopy (3D-SIM)
PMID:33825974	PBO:0104155	Figure 4d, 4e; Figure s3b; live cell imaging with 3D structured illumination microscopy (3D-SIM)
PMID:33825974	FYPO:0005914	live cell imaging with 3D structured illumination microscopy (3D-SIM)
PMID:33825974	FYPO:0004665	live cell imaging with 3D structured illumination microscopy (3D-SIM)
PMID:33836577	PBO:0093613	figure 3B
PMID:33836577	PBO:0093613	figure 3B
PMID:33836577	PBO:0093613	figure 3B
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: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:0019133	figure 3D
PMID:33836577	PBO:0019133	figure 3D
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	PBO:0100206	figure 2D
PMID:33836577	PBO:0100206	figure 2E
PMID:33836577	PBO:0100206	figure 2E
PMID:33836577	PBO:0019133	figure 3D
PMID:33836577	PBO:0019133	figure 3D
PMID:33836577	PBO:0019133	figure 3D
PMID:33836577	PBO:0100201	figure 2
PMID:33836577	PBO:0093613	figure 3C
PMID:33836577	PBO:0093613	figure 3C
PMID:33836577	PBO:0093613	figure 3C
PMID:33836577	GO:0005515	figure 2 requires phosphorylated T89, T154, T155 to bind Nbs1 FHA domain
PMID:33836577	GO:1990238	figure 2
PMID:33836577	PBO:0093613	figure 3B
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	FYPO:0006426	Figure 2A
PMID:33888556	FYPO:0002219	Figure 2F
PMID:33888556	FYPO:0002061	Figure 3D. phosphomimetic rec8
PMID:33888556	FYPO:0002060	Figure 3D.
PMID:33888556	FYPO:0002060	Figure 3D.
PMID:33888556	FYPO:0002061	Figure 3D. phosphomimetic rec8
PMID:33888556	PBO:0109332	To further examine this possibility, we reconstituted Rec8 dephosphorylation in vitro using immunoprecipitated Par1-containing PP2A complexes.
PMID:33888556	PBO:0109333	To further examine this possibility, we reconstituted Rec8 dephosphorylation in vitro using immunoprecipitated Par1-containing PP2A complexes.
PMID:33888556	PBO:0107033	figure 4 (no rescue by sgo3)
PMID:33888556	PBO:0107029	Figure (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:33888556	PBO:0107039	figure 4
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 cohesion protection defect
PMID:33909078	PBO:0105746	alpha-1,3-galactosylation of O-linked glycan
PMID:33909078	PBO:0105746	alpha-1,3-galactosylation of O-linked glycan
PMID:33909078	PBO:0097089	alpha-1,2-galactosylation of N-linked glycan
PMID:33909078	PBO:0097089	alpha-1,2-galactosylation of N-linked glycan
PMID:33909078	PBO:0097089	alpha-1,2-galactosylation of N-linked glycan
PMID:33909078	PBO:0097092	alpha-1,2-galactosylation of O-linked glycan
PMID:33909078	PBO:0105746	alpha-1,3-galactosylation of O-linked glycan
PMID:33909078	PBO:0097092	alpha-1,2-galactosylation of O-linked glycan
PMID:33925026	PBO:0097255	Assays were done in the MDR-sup (multi-drug resistance-suppressed) genetic background together with nda3-TB101
PMID:33925026	FYPO:0005682	same as klp6delta alone
PMID:33925026	FYPO:0001355	same as alp14delta alone
PMID:33925026	FYPO:0005681	same as alp14delta alone
PMID:33925026	FYPO:0005682	same as alp14delta alone
PMID:33925026	FYPO:0005703	same as alp14delta alone
PMID:33925026	FYPO:0000903	same as alp14delta alone
PMID:33925026	FYPO:0005681	same as klp6delta alone
PMID:33925026	PBO:0097257	reduced frequency of microtubule rescue
PMID:33925026	PBO:0097256	reduced frequency of microtubule catastrophe
PMID:33946513	PBO:0107001	Figure 2A,B
PMID:33946513	PBO:0107005	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	to pac
PMID:33946513	PBO:0107008	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	to pac
PMID:33946513	PBO:0107007	to pac
PMID:33946513	PBO:0107004	Figure 2D
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	FYPO:0002060	fig 1c dri1 supresses cut7
PMID:33946513	FYPO:0002060	fig1a
PMID:33946513	FYPO:0002060	fig1
PMID:33946513	PBO:0107001	Figure 2A,B
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:0107004	Figure 2D
PMID:33970532	FYPO:0007792	only amino acid auxotrophic cell
PMID:33970532	PBO:0094360	to capture target of ecl1
PMID:33970532	PBO:0094358	only amino acid auxotrophic cell
PMID:33970532	FYPO:0007792	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: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:34010645	FYPO:0007597	Figure 2.
PMID:34010645	FYPO:0007597	Figure 2
PMID:34010645	FYPO:0007597	Figure 2.
PMID:34019809	FYPO:0007841	fix catalytic activity
PMID:34019809	FYPO:0007841	fix catalytic activity
PMID:34019809	GO:0000822	structure, fig2
PMID:34028542	FYPO:0003743	Proliferation defect of gad8ts aly2 mutant in low glucose was similar to that of gad8ts mutant.
PMID:34028542	PBO:0114539	although not shown directly , genetic interactions are consistent with this activity
PMID:34028542	PBO:0099308	fig6 (phenocopies WT)
PMID:34028542	PBO:0099307	fig6
PMID:34028542	FYPO:0003743	Proliferation defect of gad8ts rod1 mutant in low glucose was similar to that of gad8ts mutant.
PMID:34028542	PBO:0099307	fig6
PMID:34028542	FYPO:0000047	Proliferation defect of gad8ts mutant in low glucose was restored by SPCC584.15c deletion.
PMID:34028542	PBO:0092254	fig 5
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:34028542	PBO:0099302	top panel, Fig. 6A; Fig. S3B,C).
PMID:34028542	PBO:0099303	Cytoplasmic Ght5-GFP was observed within the vacuolar membrane stained with FM4-64.
PMID:34028542	PBO:0099304	Fig1 aly3 rescues
PMID:34028542	FYPO:0003743	Proliferation defect of gad8ts aly1 mutant in low glucose was similar to that of gad8ts mutant.
PMID:34067465	PBO:0114709	(Fig. 4 and Fig. S2)
PMID:34067465	PBO:0114710	(Fig. 4 and Fig. S2)
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	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:34067465	PBO:0092385	(Fig. 1C)
PMID:34067465	PBO:0092176	(Fig. 1C)
PMID:34067465	FYPO:0002043	(Fig. 4 and Fig. S2)
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	PBO:0092319	(Fig. 1C)
PMID:34067465	FYPO:0008313	(Fig. 8)
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	FYPO:0005706	Fig. 4
PMID:34080538	FYPO:0007304	Fig. 4
PMID:34080538	PBO:0022963	Fig. 4
PMID:34080538	PBO:0109500	Fig. 4
PMID:34080538	PBO:0109501	Fig. 4
PMID:34080538	PBO:0109502	Fig. 5 - Dephosph form
PMID:34080538	PBO:0109503	Fig. 5 - Dephosph form
PMID:34080538	PBO:0097991	Fig. 5 -Phosph form (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:0109504	Fig. 4
PMID:34080538	FYPO:0005343	Fig. 4
PMID:34080538	FYPO:0005706	Fig. 4
PMID:34080538	FYPO:0007304	Fig. 4
PMID:34080538	PBO:0109507	Fig. 5 supp 3
PMID:34080538	PBO:0109508	Fig. 5 supp 3
PMID:34080538	PBO:0109499	Fig. 4
PMID:34080538	FYPO:0005343	Fig. 4
PMID:34080538	FYPO:0007304	Fig. 4
PMID:34080538	FYPO:0005343	Fig. 4
PMID:34080538	FYPO:0005706	Fig. 4
PMID:34086083	PBO:0108842	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	YES, YES (low-glucose)
PMID:34086083	GO:0005737	YES, YES (low-glucose)
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: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: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	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	PBO:0114831	The PPR motifs of Ppr10 are not involved in the association of Ppr10 with a subset of mitoribosomal proteins
PMID:34119521	PBO:0114830	The association of cob1 and cox1 mRNAs with assembled mitor- ibosomes was reduced by ppr10 deletion, whereas their asso- ciation with the mt-SSU was increased (Fig. 3).
PMID:34119521	PBO:0114829	The association of cob1 and cox1 mRNAs with assembled mitor- ibosomes was reduced by ppr10 deletion, whereas their asso- ciation with the mt-SSU was increased (Fig. 3).
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: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: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: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: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: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: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: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: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: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: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: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 mitor- ibosomes (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 mitor- ibosomes (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 mitor- ibosomes (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 mitor- ibosomes (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 mitor- ibosomes (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 mitor- ibosomes (Fig. 2, B–D).
PMID:34119521	PBO:0114793	deletion of PPR motifs in Ppr10 severely reduced the steady-state levels of Cob1 (subunit of the cyto- chrome bc 1 complex), the core subunits of cytochrome c oxidase (Cox1, Cox2, Cox3), and Atp6 (subunit of ATP syn- thase) (Fig. 1D).
PMID:34119521	PBO:0114792	deletion of PPR motifs in Ppr10 severely reduced the steady-state levels of Cob1 (subunit of the cyto- chrome bc 1 complex), the core subunits of cytochrome c oxidase (Cox1, Cox2, Cox3), and Atp6 (subunit of ATP syn- thase) (Fig. 1D).
PMID:34119521	PBO:0114791	deletion of PPR motifs in Ppr10 severely reduced the steady-state levels of Cob1 (subunit of the cyto- chrome bc 1 complex), the core subunits of cytochrome c oxidase (Cox1, Cox2, Cox3), and Atp6 (subunit of ATP syn- thase) (Fig. 1D).
PMID:34119521	PBO:0114794	deletion of PPR motifs in Ppr10 severely reduced the steady-state levels of Cob1 (subunit of the cyto- chrome bc 1 complex), the core subunits of cytochrome c oxidase (Cox1, Cox2, Cox3), and Atp6 (subunit of ATP syn- thase) (Fig. 1D).
PMID:34119521	PBO:0114789	deletion of PPR motifs in Ppr10 severely reduced the steady-state levels of Cob1 (subunit of the cyto- chrome bc 1 complex), the core subunits of cytochrome c oxidase (Cox1, Cox2, Cox3), and Atp6 (subunit of ATP syn- thase) (Fig. 1D).
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	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:34133210	PBO:0106246	although not IDA, there is experimental data to support this inference
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	FYPO:0007829	Figure 4, A and B
PMID:34133210	PBO:0092467	fig1
PMID:34133210	FYPO:0005543	Constriction took longer in pxl1(9A)
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: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	also assayed using Pil1 co-tethering with microscopy
PMID:34169534	PBO:0107986	also assayed using Pil1 co-tethering with microscopy
PMID:34198697	PBO:0113578	Figure 1a
PMID:34198697	FYPO:0005969	Figure 1B
PMID:34198697	FYPO:0007521	figure 1B This phenotype, known as “VIC” (viable in the presence of immunosup- pressant and chloride ion
PMID:34198697	FYPO:0000079	figure 1B
PMID:34198697	PBO:0113580	Cell wall damage induced with caspofungin
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:34209806	GO:0005681	Need to curate ref42 for earlier part of this story, but this can be. inferred here from the interactions
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	MOD:00047	i added as good to have multiple support.
PMID:34228709	FYPO:0001707	Chk1 is partially phosphorylated
PMID:34228709	FYPO:0003923	DNA combing
PMID:34228709	FYPO:0005032	equivalent substitution to cdc20-P287R
PMID:34228709	FYPO:0000173	Cds1 is partially phosphorylated
PMID:34228709	PBO:0095859	hypermutator
PMID:34250083	FYPO:0000245	Phenotype determined with robotics-based CFU assay.
PMID:34250083	FYPO:0000245	Phenotype determined with robotics-based CFU assay.
PMID:34250083	FYPO:0001309	Phenotype determined with robotics-based CFU assay.
PMID:34250083	FYPO:0001309	Phenotype determined with robotics-based CFU assay.
PMID:34250083	FYPO:0000245	Phenotype determined with robotics-based CFU assay.
PMID:34250083	FYPO:0000245	Phenotype determined with robotics-based CFU assay.
PMID:34250083	FYPO:0001309	Phenotype determined with robotics-based CFU assay.
PMID:3428262	FYPO:0003095	mitotic G2/M transition delay
PMID:34292936	PBO:0096842	worse than rad51delta alone
PMID:34292936	PBO:0096842	worse than rad51delta alone
PMID:34296454	PBO:0104158	Please refer to Fig. 5E&F 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 responsi- ble 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	in vitro (Figure 4A, Video 1).
PMID:34309513	GO:0140588	in vitro (Figure 4A, Video 1).
PMID:34309513	GO:0140588	in vitro (Figure 4A, Video 1).
PMID:34309513	GO:0140588	in vitro (Figure 4A, Video 1).
PMID:34309513	GO:0140588	in vitro (Figure 4A, Video 1).
PMID:34309513	GO:0140588	in vitro (Figure 4A, Video 1).
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:0007846	Figure 2F
PMID:34346498	PBO:0099596	Figure 7
PMID:34346498	PBO:0099595	Figure 7
PMID:34346498	FYPO:0003614	Figure 6B
PMID:34346498	FYPO:0007755	Figure 2F
PMID:34346498	PBO:0099600	figure7 C
PMID:34346498	PBO:0099601	decreased abnormal SPB-independent meiosis II
PMID:34346498	PBO:0022389	Figure 2
PMID:34346498	PBO:0099602	Figure 3A
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	PBO:0099607	Figure 1
PMID:34346498	PBO:0099608	Figure 1 (see above)
PMID:34346498	PBO:0099609	Figure 1 (see above)
PMID:34346498	PBO:0099610	Figure 2E
PMID:34346498	PBO:0099599	figure7 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: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:0099592	late spindle elongation (move down /when GO reflect stages of meiotic spindle elongation)
PMID:34346498	PBO:0099611	Figure 2E
PMID:34346498	FYPO:0007852	Figure 3
PMID:34346498	PBO:0099612	figure7 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: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	FYPO:0007849	Figure 2F
PMID:34346498	PBO:0099614	figure 7C
PMID:34346498	PBO:0099616	figure 7C
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 (Fig- ure 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 prema- ture termination.
PMID:34352089	GO:0000956	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 (Fig- ure 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 prema- ture termination.
PMID:34352089	PBO:0104074	5' extended precursors, C/C box (but not H/ACA box)
PMID:34352089	PBO:0093558	Supplementary Figure S5B
PMID:34352089	PBO:0104069	Figure 3A and Supplementary Fig- ure S5A
PMID:34352089	PBO:0104069	Figure 3A and Supplementary Fig- ure S5A
PMID:34352089	PBO:0104073	5' extended precursors, C/C box (but not H/ACA box)
PMID:34352089	GO:0030847	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) . Can this be added in the annotation extension ?
PMID:34352089	PBO:0104072	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 ac- cumulation 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:0104079	Pac1 strain (Pac1-AA) that allowed rapid rapamycin-dependent nuclear exclusion of Pac1 (Figure 1B).
PMID:34352089	PBO:0104078	MOVE DOWN
PMID:34352089	PBO:0104077	MOVE DOWN
PMID:34352089	GO:0000956	waiting for GO:NEW. We show this for only two mRNA: mfs2 and SPBC530.02. Can this be added in the annotation extension ?
PMID:34382912	PBO:0103457	figure 2
PMID:34382912	PBO:0103460	fig4
PMID:34382912	MOD:00046	fig 5
PMID:34382912	MOD:00046	fig 5
PMID:34382912	MOD:00046	fig 5
PMID:34382912	MOD:00046	fig 5
PMID:34382912	MOD:00046	fig 5
PMID:34382912	PBO:0103458	fig4
PMID:34382912	MOD:00046	fig 5
PMID:34382912	PBO:0103459	fig4
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	GO:1990819	figure5
PMID:34382996	GO:1990819	figure5
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:0000413	Stronger phenotype in h+ than 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:34382996	FYPO:0000413	Only when gpd1∆ is in h- cell
PMID:34382996	FYPO:0004804	no assembly of vesicles by electron microscopy (Because cell fu- sion completely fails when both partner cells lack fus1)
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:34389684	FYPO:0002061	Random spore analysis
PMID:34389684	FYPO:0001355	Figure 1c
PMID:34389684	PBO:0099762	NorthernBlotting
PMID:34389684	PBO:0099761	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	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:0099759	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	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:0099757	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	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	FYPO:0002061	Random spore analysis
PMID:34389684	FYPO:0002061	Random spore analysis
PMID:34389684	FYPO:0002061	Random spore analysis
PMID:34389684	FYPO:0002060	Figue 3A Notable findings were that seb1-G476S rescued the ts growth defect of rhn1Δ at 37 °C......
PMID:34389684	PBO:0099755	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	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	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	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	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 compared to WT
PMID:34389684	FYPO:0001489	Random spore analysis (DNS)
PMID:34389684	FYPO:0001489	Random spore analysis (DNS)
PMID:34389684	FYPO:0001489	Random spore analysis (DNS)
PMID:34389684	PBO:0099748	Figure 1A
PMID:34389684	FYPO:0000080	Figue 1C
PMID:34389684	PBO:0099749	Fig 7 compared to WT
PMID:34389684	FYPO:0001357	..... while rhn1Δ rescued the cs growth defect of seb1-G476S at 20 °C
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	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	FYPO:0002061	The seb1-G476S and aps1Δ alleles were synthetically lethal;
PMID:34389684	FYPO:0002061	Random spore analysis
PMID:34389684	PBO:0099765	this can be inferred from the experiments
PMID:34389684	PBO:0099749	compared to WT
PMID:34389684	PBO:0099750	compared to WT
PMID:34389684	PBO:0094738	compared to WT
PMID:34389684	FYPO:0002061	Random spore analysis
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	similar to wt
PMID:34389684	PBO:0099749	Figure 1A (vw changed to increased with low serverity as we compare to WT)
PMID:34389684	FYPO:0002061	Random spore analysis
PMID:34402513	PBO:0099820	Figure 3
PMID:34402513	FYPO:0007828	Figure 4
PMID:34402513	FYPO:0001368	Figure 4
PMID:34402513	FYPO:0002253	Figure S3B-C
PMID:34402513	FYPO:0001903	Figure S2A and C
PMID:34402513	PBO:0099818	Figure S2D and F
PMID:34402513	PBO:0099813	Figure S2D-E
PMID:34402513	FYPO:0002253	Figure S3B-C
PMID:34402513	PBO:0099819	Figure S2D-E
PMID:34402513	PBO:0099818	Figure S2D and F
PMID:34402513	FYPO:0001903	Figure SA and C
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:0004097	Figure 4
PMID:34402513	FYPO:0007828	Figure 4
PMID:34402513	FYPO:0001368	Figure 4
PMID:34402513	PBO:0099816	Figure 2D
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: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	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	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: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	FYPO:0001903	Figure S2A and C
PMID:34402513	FYPO:0001903	Figure S2A and C
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	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:0000316	Figure S4B
PMID:34402513	FYPO:0004085	Figure S4B
PMID:34402513	FYPO:0004085	Figure S4A
PMID:34402513	FYPO:0002062	Figure S4A
PMID:34402513	FYPO:0002062	Figure S4A
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:0000339	Figure S3B-C
PMID:34402513	FYPO:0001903	Figure S2A and C
PMID:34402513	PBO:0099811	Figure S2D-E
PMID:34402513	FYPO:0001368	Figure 4A-B
PMID:34402513	FYPO:0007828	Figure 4A-B
PMID:34402513	FYPO:0004097	Figure 4A-B
PMID:34402513	PBO:0099812	Figure 2G
PMID:34402513	PBO:0099813	Figure S2D-E
PMID:34402513	PBO:0099814	Figure S2F
PMID:34402513	FYPO:0001903	Figure S2C
PMID:34402513	FYPO:0002253	Figure S3B-C
PMID:34402513	FYPO:0001368	Figure 4
PMID:34402513	FYPO:0007828	Figure 4
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	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 wildtype (Fig. 3A, B, and C)
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:0099816	Figure 2G, H
PMID:34402513	FYPO:0002062	Figure S4A
PMID:34402513	FYPO:0000316	Figure S4B
PMID:34402513	PBO:0099821	Figure 2E
PMID:34402513	FYPO:0004097	Figure 4
PMID:34460892	PBO:0103880	Evidence was from RNA-seq data
PMID:34460892	PBO:0103878	Evidence was from RNA-seq data
PMID:34460892	PBO:0103878	Evidence was from RNA-seq data
PMID:34460892	PBO:0103880	Evidence was from RNA-seq data
PMID:34460892	PBO:0092140	Evidence was from RNA-seq data
PMID:34460892	PBO:0103880	Evidence was from RNA-seq data
PMID:34460892	PBO:0103878	Evidence was from RNA-seq data
PMID:34460892	PBO:0103880	Evidence was from RNA-seq data
PMID:34460892	PBO:0103880	Evidence was from RNA-seq data
PMID:34460892	PBO:0092337	Evidence was from RNA-seq data
PMID:34460892	PBO:0103880	Evidence was from RNA-seq data
PMID:34460892	PBO:0103880	Evidence was from RNA-seq data
PMID:34460892	PBO:0103878	Evidence was from RNA-seq data
PMID:34460892	PBO:0103878	Evidence was from RNA-seq data
PMID:34460892	PBO:0103878	Evidence was from RNA-seq data
PMID:34460892	PBO:0103878	Evidence was from RNA-seq data
PMID:34460892	PBO:0103878	Evidence was from RNA-seq data
PMID:34460892	PBO:0103878	Evidence was from RNA-seq data
PMID:34460892	PBO:0092337	Evidence was from RNA-seq data
PMID:34460892	PBO:0103878	Evidence was from RNA-seq data
PMID:34460892	PBO:0103878	Evidence was from RNA-seq data
PMID:34460892	PBO:0103880	Evidence was from RNA-seq data
PMID:34460892	PBO:0092337	Evidence from RNA-seq data
PMID:34460892	PBO:0103880	Evidence from RNA-seq data
PMID:34460892	PBO:0103878	Evidence form RNA-seq data
PMID:34460892	PBO:0103880	Evidence form RNA-seq data
PMID:34460892	PBO:0103878	Evidence form RNA-seq data
PMID:34460892	PBO:0103878	Evidence form RNA-seq data
PMID:34460892	PBO:0103878	Evidence form RNA-seq data
PMID:34460892	PBO:0103880	Evidence form RNA-seq data
PMID:34460892	PBO:0103879	Evidence code was RNA-seq
PMID:34460892	PBO:0103878	Evidence was from RNA-seq not from microarray
PMID:34460892	PBO:0092337	Evidence form RNA-seq data
PMID:34460892	PBO:0103880	Evidence form RNA-seq data
PMID:34460892	PBO:0103878	Evidence form RNA-seq data
PMID:34460892	PBO:0103878	Evidence form RNA-seq data
PMID:34460892	PBO:0092337	Evidence form RNA-seq data
PMID:34460892	PBO:0103880	Evidence form RNA-seq data
PMID:34460892	PBO:0103880	Evidence from RNA-seq data
PMID:34460892	PBO:0103878	Evidence from RNA-seq data
PMID:34460892	PBO:0103880	Evidence from RNA-seq data
PMID:34460892	PBO:0103880	Evidence from RNA-seq data
PMID:34460892	PBO:0103880	Evidence from RNA-seq data
PMID:34460892	PBO:0103880	Evidence from RNA-seq data
PMID:34460892	PBO:0103880	Evidence from RNA-seq data
PMID:34460892	PBO:0103878	Evidence from RNA-seq data
PMID:34460892	PBO:0103880	Evidence from RNA-seq data
PMID:34460892	PBO:0103880	Evidence from RNA-seq data
PMID:34460892	PBO:0092337	Evidence from RNA-seq data
PMID:34460892	PBO:0103880	Evidence from RNA-seq data
PMID:34460892	PBO:0103880	Evidence from RNA-seq data
PMID:34460892	PBO:0103878	Evidence from RNA-seq data
PMID:34460892	PBO:0103880	Evidence from RNA-seq data
PMID:34460892	PBO:0103878	Evidence was from RNA-seq data
PMID:34460892	PBO:0103878	Evidence was from RNA-seq data
PMID:34460892	PBO:0103880	Evidence was from RNA-seq data
PMID:34460892	PBO:0103878	Evidence was from RNA-seq data
PMID:34460892	PBO:0103878	Evidence from RNA-seq data
PMID:34464389	PBO:0105656	S7A Fig 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:0106084	during stationary phase. Figure 6C In fact, the protein levels of Scw1 markedly decreased in ageing cells.
PMID:34464389	FYPO:0007936	5B Notably, in aged cells the double mutant showed an ~3-fold increase in chro- mosomal junctions on average, albeit with large variation, but no increase in indels
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	PBO:0103668	Figure 5A Cells lacking Sir2 showed a subtle extension of chronological lifespan compared to wild-type, especially at later timepoints
PMID:34464389	PBO:0110916	Figure 4B Accordingly, our smFISH experiment showed that tlh2 was de-repressed in sir2 deletion cells
PMID:34464389	FYPO:0000245	Figure S7C Moreover, the tlh2 overexpression strain was substantially shorter-lived than wild-type cells
PMID:34464389	FYPO:0001309	Fig 5A Given the increased lifespan of rnh1Δ rnh201Δ cells
PMID:34464389	FYPO:0007936	Figure S7B The proportion of junctions down- stream 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	FYPO:0001357	Figure 3C
PMID:34499159	PBO:0105133	Figure 4b
PMID:34499159	FYPO:0001147	Figure S2B
PMID:34499159	PBO:0105133	Figure 4B
PMID:34499159	FYPO:0000111	Figure 3c
PMID:34499159	PBO:0105131	Figure 3d
PMID:34499159	PBO:0105132	Figure 4c
PMID:34499159	PBO:0105135	Figure 4B
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:0105139	Figure 5E
PMID:34499159	PBO:0105143	Figure 1
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:0105131	Figure 2
PMID:34499159	PBO:0105140	Figure 2
PMID:34499159	PBO:0105141	Figure 2
PMID:34499159	FYPO:0002672	Figure 5A
PMID:34499159	FYPO:0002672	Figure 5A
PMID:34524082	PBO:0111593	Figure 3F /fig1
PMID:34524082	PBO:0095977	Fig. 4D (Currently, we cannot explain why the dg transcripts in the 3FA mutant are only slightly elevated while completely losing H3K9me2/3.)
PMID:34524082	PBO:0095978	Fig. 4D
PMID:34524082	PBO:0095979	Fig. 4D
PMID:34524082	PBO:0111594	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:0111592	Figure 3F /fig1
PMID:34524082	PBO:0111591	Figure 3F / fig1 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: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:0095984	Fig. 4E
PMID:34524082	PBO:0095984	Fig. 4E
PMID:34524082	FYPO:0007334	Fig. 4A
PMID:34524082	PBO:0095983	Fig. 4E
PMID:34524082	PBO:0095983	Fig. 4E
PMID:34524082	PBO:0095982	Fig. 4D
PMID:34524082	FYPO:0007334	Fig. 4A
PMID:34524082	PBO:0095976	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:34524082	PBO:0095980	Fig. 4D
PMID:34524082	PBO:0095976	Fig. 4E REQUESTED ABOLISHED
PMID:34524082	PBO:0095981	Fig. 4D
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: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:34608864	PBO:0105486	presence or absence of HU
PMID:34608864	FYPO:0004240	presence or absence of MMS
PMID:34608864	PBO:0105485	presence or absence of HU
PMID:34608864	MOD:01148	in presence or absence of MMS
PMID:34608864	PBO:0105486	presence or absence of HU
PMID:34608864	PBO:0105485	presence or absence of HU
PMID:34608864	PBO:0105479	presence or absence of MMS
PMID:34608864	FYPO:0004240	presence or absence of MMS
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	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: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:0001365	WHY ISNNT THIS PART. OF ????FYPO:0000230 abnormal actomyosin contractile ring actin filament organization
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	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	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	PBO:0098926	Figure 2B
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	WHY ISNNT THIS PART. OF ????FYPO:0000230 abnormal actomyosin contractile ring actin filament organization
PMID:34666001	PBO:0101579	figure 5
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	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:0101580	In sharp contrast, Wsc1DSTR-GFP, Wsc1DWSC-GFP and Wsc1DSTRDWSC-GFP cells were completely devoid of any clustering phenotype, with an enrichment at con- tacts 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 con- tacts 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 con- tacts close to $2 (Figures 5D, 5E, and S2F–S2H).
PMID:34666001	PBO:0101579	Remarkably, the Wsc1DCC-GFP lacking a large fraction of the cytoplasmic C-ter- minal tail, and thus presumably defective in downstream signal transduction was dispensable for clustering. This finding rein- forces the notion that Wsc1 clustering occurs independently of downstream CWI signaling.
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	FYPO:0008003	figure 5
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	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: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	PBO:0101578	mechanoreceptor. Together, these results indicate that Wsc1 clustering may be triggered by local surface compression, independently of puta- tive ‘‘trans’’ homotypic interactions between extracellular sensors from neighbor cells or general cell-to-cell signaling.
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:0008012	(vw: 25% cell death)
PMID:34674264	PBO:0094520	Normal localization to medial cortical nodes, SPB, and division septum as wildtype
PMID:34674264	FYPO:0000776	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) chan- ged Dma1 phosphostatus as monitored by SDS/PAGE mobility suggesting that these kinases are not responsible for regulating Dma1 phosphostatus in cells.
PMID:34674264	PBO:0094517	Localization to SPBs at the same level as wildtype during spindle stress
PMID:34674264	PBO:0094518	Localization to SPBs at the same level as wildtype during spindle stress
PMID:34674264	FYPO:0003762	Fig 4a
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	PBO:0094517	Normal localization to medial cortical nodes, mitotic contractile ring, SPB, and septum as wildtype
PMID:34674264	PBO:0094517	Normal localization to medial cortical nodes, SPB, and division septum as wildtype
PMID:34674264	PBO:0094516	(Fig.3A–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: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:0094513	Fig. 2B). Almost abolished Dma1 auto-ubiquitination by in vitro assay
PMID:34674264	PBO:0094512	Decreased Dma1 auto-ubiquitination by in vitro assay
PMID:34674264	PBO:0094511	in vitro assay
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:0094507	in vitro kinase assay showed T18, S20, and S266 are phosphorylated by CK2
PMID:34674264	PBO:0094507	in vitro kinase assay showed T18, S20, and S266 are phosphorylated by CK2
PMID:34674264	PBO:0094506	in vitro kinase assay showed S251 is phosphorylated by Plo1
PMID:34674264	PBO:0093475	in vitro kinase assay showed S166 is phosphorylated by Cdk1
PMID:34674264	MOD:00047	in vivo phosphorylation site identified by mass spectrometry
PMID:34674264	PBO:0098166	in vitro kinase assay showed T18, S20, and S266 are phosphorylated by CK2
PMID:34674264	MOD:00046	in vivo phosphorylation sites identified by mass spectrometry
PMID:34686329	PBO:0102818	We used qRT-PCR to deter- mine 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	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 disso- ciates 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 disso- ciates ribosomes. Both treatments abolished Tti1 binding to tra1+ (Figure 2C).
PMID:34686329	PBO:0109908	Tti1 caused a strong decrease of Tti2 and Tel2 binding (Fig- ure 2J).
PMID:34686329	PBO:0109963	We conclude that Tti1, and to a lesser extent Tti2, re- cruits TTT to nascent Tra1 polypeptides
PMID:34686329	PBO:0109963	We conclude that Tti1, and to a lesser extent Tti2, re- cruits TTT to nascent Tra1 polypeptides
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 re- duces 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	FYPO:0001355	(Figures S1C and S1D).
PMID:34686329	PBO:0109874	We used qRT-PCR to deter- mine 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 ca- nonical TORC1 substrate, following Tel2, Tti1, and Tti2 depletion (Figure S1G)
PMID:34686329	PBO:0109876	Western blotting showed decreased phosphorylation of the ribosomal protein S6, a ca- nonical 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:0109878	(Figure 3D)
PMID:34686329	PBO:0109878	(Figure 3D)
PMID:34686329	PBO:0109880	(Figure 3C)
PMID:34686329	PBO:0109880	(Figure 3C)
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:0109882	(Figure 2H)
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 compensa- tory mechanisms boosting its synthesis.
PMID:34686329	PBO:0093580	(Figure 6B)
PMID:34686329	PBO:0109866	RNA-seq
PMID:34686329	PBO:0093580	(Figure 6B)
PMID:34686329	PBO:0100916	(Figure 6B)
PMID:34686329	PBO:0093576	(Figure 6B)
PMID:34686329	PBO:0093612	(Figure 6B)
PMID:34686329	PBO:0109890	Figure 2C) Abolished interaction between Tti2 protein and tra1 mRNA
PMID:34686329	PBO:0109897	(Figure 3E)
PMID:34686329	PBO:0109897	(Figure 3E)
PMID:34686329	PBO:0109893	(Figure 3E)
PMID:34686329	PBO:0109896	(Figure 3E)
PMID:34686329	PBO:0109896	(Figure 3E)
PMID:34686329	PBO:0093581	(Figure 6B)
PMID:34686329	PBO:0093580	(Figure 6B)
PMID:34686329	FYPO:0000847	(Figure 6J)
PMID:34686329	FYPO:0000847	RNA-seq
PMID:34686329	PBO:0109898	(Figure 6H)
PMID:34686329	PBO:0109898	(Figure 6H)
PMID:34686329	PBO:0109899	(figure 6F)
PMID:34686329	PBO:0109866	RNA-seq
PMID:34686329	FYPO:0002430	figure 6I
PMID:34686329	FYPO:0002430	figure 6I
PMID:34686329	PBO:0109869	(Figure 7A)
PMID:34686329	PBO:0109900	(Figure 7A)
PMID:34686329	FYPO:0000705	Abolished incorporation of Tra1 into SAGA complex
PMID:34686329	FYPO:0000705	Abolished incorporation of Tra1 into SAGA complex
PMID:34686329	FYPO:0000705	Abolished incorporation of Tra1 into SAGA complex
PMID:34686329	FYPO:0000705	Abolished incorporation of Tra1 into SAGA complex
PMID:34686329	FYPO:0000705	Abolished incorporation of Tra1 into SAGA complex
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	GO:0110078	(Figure 1A)
PMID:34686329	GO:0110078	(Figure 1A)
PMID:34686329	PBO:0109904	Finally, our published tran- scriptomic analysis of tti2-CKO mutants showed that PIKK mRNA levels remain unaffected following Tti2 depletion (Fig- ureS1H)
PMID:34686329	PBO:0109905	Finally, our published tran- scriptomic analysis of tti2-CKO mutants showed that PIKK mRNA levels remain unaffected following Tti2 depletion (Fig- ureS1H)
PMID:34686329	PBO:0109906	Finally, our published tran- scriptomic analysis of tti2-CKO mutants showed that PIKK mRNA levels remain unaffected following Tti2 depletion (Fig- ureS1H)
PMID:34686329	PBO:0109907	Finally, our published tran- scriptomic analysis of tti2-CKO mutants showed that PIKK mRNA levels remain unaffected following Tti2 depletion (Fig- ureS1H)
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	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 disso- ciates ribosomes. Both treatments abolished Tti1 binding to tra1+ (Figure 2C).
PMID:34731638	FYPO:0004577	ntriguingly, 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	Figure 4E
PMID:34731638	FYPO:0005917	we observed derepression of several subtelomeric genes (Figures 2E and S2G).
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:0007891	(Figure 2D) reduced heterochromatin spreading at mating-type and subtelomeric heterochromatin
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	PBO:0101113	(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:0101111	(Figures S4A–S4C) Histone H3 ChIP-seq revealed a small but reproducible reduction of H3 at subtelomeres in pob3Δ
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	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:0101108	Figures S2C–S2E in chromatin/euchromatin
PMID:34731638	PBO:0101107	Figures S2C–S2E in chromatin/euchromatin
PMID:34731638	GO:0000791	(Figure S1E)
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	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:0004604	Partial suppression of pob3∆ silencing phenotype.
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	PBO:0101106	(fig1G ) vw changed to increased (compared to WT)
PMID:34731638	FYPO:0006299	(fig1G) (fig1G ) vw changed to increased (compared to WT)
PMID:34731638	FYPO:0003555	(Figure 1 G)
PMID:34731638	FYPO:0002360	(Figure 1 G)
PMID:34731638	FYPO:0002360	vw changed from decreased to normal because look WT?
PMID:34731638	FYPO:0004542	(figure 1 f)
PMID:34731638	FYPO:0006299	(figure 1 f)
PMID:34731638	FYPO:0004604	Figure 4E
PMID:34731638	FYPO:0003412	Figure 4E
PMID:34731638	FYPO:0003412	synthetic defect in the silencing of dg and tlh1/2 transcripts (Figure 4C)
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	PBO:0093562	(Figure S7A),
PMID:34798057	PBO:0100613	V348A
PMID:34798057	FYPO:0000708	Figure S1 D
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 in- crease in the duration of metaphase was noted in both MI and MII (Figures 6D–6H).
PMID:34798057	FYPO:0002091	Figures 6I and 6J
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	(weird!) Intriguingly, the double nda2noD nda3noD mutant was less sensitive than the single ones. OK!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:34805795	PBO:0108098	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	PBO:0108097	Figure S1A
PMID:34805795	PBO:0108097	Figure S1A
PMID:34805795	PBO:0108097	Figure 5
PMID:34805795	PBO:0108097	Figure 5
PMID:34805795	PBO:0108106	during amino acid starvation
PMID:34805795	PBO:0108106	during amino acid starvation
PMID:34805795	PBO:0108104	BFC augments TORC1 activation in response to amino acid stimulation
PMID:34805795	PBO:0108103	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	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:0108102	(Figure S3) Bhd1 and Fnp1 localize to vacuoles in response to amino acid star- vation and that this localization is largely independent of the presence of the other protein.
PMID:34805795	PBO:0108101	(Figure S3) Bhd1 and Fnp1 localize to vacuoles in response to amino acid star- vation and that this localization is largely independent of the presence of the other protein.
PMID:34805795	FYPO:0006266	(Figure S1A)
PMID:34805795	FYPO:0006266	(Figure S1A)
PMID:34805795	PBO:0108099	(Figure 4F) (vw: ph9)
PMID:34805795	PBO:0108099	(Figure 4F) (vw: ph9)
PMID:34805795	FYPO:0001159	(figure 4d) (vw: assayed vacuolar pH as a surrogate for V-ATPase activity)
PMID:34805795	FYPO:0007909	(figure 4d) (vw: assayed vacuolar pH as a surrogate for V-ATPase activity)
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: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: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: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: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: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: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: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:0101628	(ndc80 receptor) 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	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:0101627	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	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: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: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: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: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: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: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:34849791	FYPO:0000964	Supplemental Figure S2B
PMID:34849791	FYPO:0000964	Supplemental Figure S1B
PMID:34849791	FYPO:0000674	Supplemental Figure S1B
PMID:34849791	PBO:0094562	Figure 4
PMID:34849791	FYPO:0000964	Supplemental Figure S1B
PMID:34849791	FYPO:0000674	Supplemental Figure S1B
PMID:34849791	PBO:0094563	Figure 4
PMID:34849791	FYPO:0000964	Supplemental Figure S1B
PMID:34849791	FYPO:0000674	Supplemental Figure S1B
PMID:34849791	PBO:0094564	Figure 4
PMID:34849791	FYPO:0000964	Supplemental Figure S1B
PMID:34849791	FYPO:0000674	Supplemental Figure S1B
PMID:34849791	PBO:0094565	Figure 4
PMID:34849791	PBO:0094555	Figure 4
PMID:34849791	FYPO:0000082	Figure 3A
PMID:34849791	FYPO:0000091	Figure 3B
PMID:34849791	PBO:0094554	Figure 4
PMID:34849791	FYPO:0000082	Figure 3A
PMID:34849791	FYPO:0000091	Figure 3B
PMID:34849791	FYPO:0000674	Figure 3A
PMID:34849791	FYPO:0000964	Figure 3B
PMID:34849791	FYPO:0001513	Figure 4
PMID:34849791	FYPO:0000964	Supplemental Figure S1B
PMID:34849791	FYPO:0000674	Supplemental Figure S1B
PMID:34849791	PBO:0094561	Figure 4
PMID:34849791	FYPO:0001513	Figure 4
PMID:34849791	FYPO:0000964	Supplemental Figure S1B
PMID:34849791	FYPO:0000674	Supplemental Figure S1B
PMID:34849791	FYPO:0000964	Supplemental Figure S6B
PMID:34849791	FYPO:0000674	Supplemental Figure S6B
PMID:34849791	PBO:0094559	Figure 4
PMID:34849791	FYPO:0000964	Supplemental Figure S6B
PMID:34849791	FYPO:0000674	Supplemental Figure S6B
PMID:34849791	PBO:0094559	Figure 4
PMID:34849791	FYPO:0000964	Supplemental Figure S6B
PMID:34849791	FYPO:0000674	Supplemental Figure S6B
PMID:34849791	PBO:0094564	Figure 4
PMID:34849791	FYPO:0000964	Supplemental Figure S6B
PMID:34849791	FYPO:0000674	Supplemental Figure S6B
PMID:34849791	PBO:0094560	Figure 4
PMID:34849791	FYPO:0000964	Supplemental Figure S6B
PMID:34849791	FYPO:0000674	Supplemental Figure S6B
PMID:34849791	PBO:0094565	Figure 4
PMID:34849791	FYPO:0001513	Figure 4
PMID:34849791	FYPO:0000964	Supplemental Figure S6B
PMID:34849791	FYPO:0000674	Supplemental Figure S6B
PMID:34849791	FYPO:0000082	Supplemental Figure S4B
PMID:34849791	FYPO:0000964	Supplemental Figure S4B
PMID:34849791	PBO:0094560	Figure 4
PMID:34849791	FYPO:0000082	Supplemental Figure S4B
PMID:34849791	FYPO:0000964	Supplemental Figure S4B
PMID:34849791	PBO:0094559	Figure 4
PMID:34849791	FYPO:0000082	Supplemental Figure S4B
PMID:34849791	FYPO:0000964	Supplemental Figure S4B
PMID:34849791	PBO:0094566	Figure 4
PMID:34849791	FYPO:0000674	Supplemental Figure S4B
PMID:34849791	FYPO:0000964	Supplemental Figure S4B
PMID:34849791	PBO:0094560	Figure 4
PMID:34849791	FYPO:0000674	Supplemental Figure S4B
PMID:34849791	FYPO:0000964	Supplemental Figure S4B
PMID:34849791	PBO:0094562	Figure 4
PMID:34849791	FYPO:0001513	Figure 4
PMID:34849791	FYPO:0000964	Supplemental Figure S4B
PMID:34849791	FYPO:0000674	Supplemental Figure S4B
PMID:34849791	FYPO:0000964	Figure 3B
PMID:34849791	FYPO:0000082	Figure 3A
PMID:34849791	PBO:0094567	Figure 4
PMID:34849791	FYPO:0000964	Figure 3B
PMID:34849791	FYPO:0000082	Figure 3A
PMID:34849791	PBO:0094567	Figure 4
PMID:34849791	FYPO:0000964	Figure 3B
PMID:34849791	FYPO:0000674	Figure 3A
PMID:34849791	PBO:0094560	Figure 4
PMID:34849791	FYPO:0000964	Figure 3B
PMID:34849791	FYPO:0000082	Figure 3A
PMID:34849791	PBO:0094563	Figure 4
PMID:34849791	FYPO:0000964	Figure 3B
PMID:34849791	FYPO:0000674	Supplemental Figure S5B
PMID:34849791	PBO:0094559	Figure 4
PMID:34849791	FYPO:0000964	Supplemental Figure S5B
PMID:34849791	FYPO:0000082	Supplemental Figure S5B
PMID:34849791	FYPO:0000082	Figure 3A
PMID:34849791	PBO:0094562	Figure 4
PMID:34849791	FYPO:0001513	Figure 4
PMID:34849791	FYPO:0000964	Figure 3B
PMID:34849791	FYPO:0000082	Figure 3A
PMID:34849791	FYPO:0000964	Supplemental Figure S5B
PMID:34849791	FYPO:0000674	Supplemental Figure S5B
PMID:34849791	PBO:0094566	Figure 4
PMID:34849791	FYPO:0000964	Supplemental Figure S5B
PMID:34849791	FYPO:0000082	Supplemental Figure S5B
PMID:34849791	PBO:0094563	Figure 4
PMID:34849791	FYPO:0000964	Supplemental Figure S5B
PMID:34849791	FYPO:0000082	Supplemental Figure S5B
PMID:34849791	PBO:0094562	Figure 4
PMID:34849791	PBO:0094561	Figure 4
PMID:34849791	FYPO:0000964	Supplemental Figure S5B
PMID:34849791	FYPO:0000082	Supplemental Figure S5B
PMID:34849791	PBO:0094559	Figure 4
PMID:34849791	FYPO:0000964	Supplemental Figure S5B
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	PBO:0094562	Figure 4
PMID:34849791	FYPO:0000964	Supplemental Figure S2B
PMID:34849791	FYPO:0000674	Supplemental Figure S2B
PMID:34849791	PBO:0094559	Figure 4
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:0000674	Supplemental Figure S3B
PMID:34849791	FYPO:0000964	Supplemental Figure S3B
PMID:34849791	FYPO:0000674	Supplemental Figure S3B
PMID:34849791	FYPO:0000964	Supplemental Figure S3B
PMID:34849791	PBO:0094560	Figure 4
PMID:34849791	PBO:0094560	Figure 4
PMID:34849791	PBO:0094559	Figure 4
PMID:34849791	FYPO:0000674	Supplemental Figure S3B
PMID:34849791	FYPO:0000964	Supplemental Figure S3B
PMID:34849791	FYPO:0001513	Figure 4
PMID:34849791	PBO:0094559	Figure 4
PMID:34849791	PBO:0094558	Figure 4
PMID:34849791	FYPO:0000082	Figure 3A
PMID:34849791	FYPO:0000091	Figure 3B
PMID:34849791	PBO:0094557	Figure 4
PMID:34849791	FYPO:0000082	Figure 3A
PMID:34849791	FYPO:0000091	Figure 3B
PMID:34849791	PBO:0094556	Figure 4
PMID:34849791	FYPO:0000082	Figure 3A
PMID:34849791	FYPO:0000091	Figure 3B
PMID:34849791	FYPO:0000964	Supplemental Figure S2B
PMID:34849791	FYPO:0000674	Supplemental Figure S2B
PMID:34849791	PBO:0094561	Figure 4
PMID:34849791	FYPO:0001513	Figure 4
PMID:34849791	FYPO:0000674	Supplemental Figure 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	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: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	FYPO:0005648	Non-separated signals were found to be significantly or nearly significantly wider than in wild-type cells (Fig. 3E,F;)
PMID:34910579	FYPO:0003890	We confirmed the defects in septa using electron microscopy. 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	Supplemental Figure S2, A–D
PMID:34910579	FYPO:0001188	Figure 2A
PMID:34910579	PBO:0102299	36 degrees
PMID:34910579	PBO:0102298	36 degrees
PMID:34910579	FYPO:0005840	see above
PMID:34910579	PBO:0102301	36 degrees
PMID:34910579	FYPO:0000650	38.5% cf WT 11.5% Figure 1F
PMID:34910579	PBO:0102297	recruits glucanases and glucan synthases to division site
PMID:34910579	PBO:0102309	recruits glucanases and glucan synthases to division site
PMID:34910579	PBO:0035615	Figure 1, C and D restrictive temperature mutant.
PMID:34910579	PBO:0102299	36 degrees
PMID:34910579	FYPO:0004292	Supplemental Figure S2, A–D
PMID:34910579	PBO:0102304	36 degrees
PMID:34910579	PBO:0102308	36 degrees
PMID:34910579	PBO:0102306	36 degrees
PMID:34910579	PBO:0102300	36 degrees
PMID:34910579	PBO:0102308	36 degrees
PMID:34910579	PBO:0102309	ogether, 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:34910579	PBO:0102302	36 degrees
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:34951983	GO:0007052	Not required for spindle repair following laser ablation
PMID:34951983	GO:0007052	required for spindle repair following laser ablation
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: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	(actually mid1-Nter)
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:0101343	We combined arf6Δ with the mid1(400–450Δ) mu- tant that cannot bind Cdr2. In the resulting cells, Cdr2 was ab- sent from the cell cortex and formed large cytoplasmic puncta (Figs. 4 A and S2 J).
PMID:34958661	PBO:0112444	Thus, Arf6 and Mid1 are partially over- lapping anchors for Cdr2 nodes.
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:0101338	A GDP-locked mutant arf6(T52N)-mNG lost node localization, (Fig. 2 F)
PMID:34958661	PBO:0101338	Arf6 node localization required Cdr2 but not other node proteins (Figs. 2 E and S2 B).
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	GO:0010971	Figure 1
PMID:34958661	GO:0010971	Figure 1
PMID:34958661	PBO:0096312	Fig S1A; 27 micron
PMID:34958661	PBO:0096312	Fig S1A; 26.6 micron
PMID:34958661	PBO:0096312	Fig S1A; 24.6 micron
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	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: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: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: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: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:0101339	but the GTP-locked allele arf6(Q75L)-mNG remained at nodes (Fig. 2 F)
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:0000417	Figure 3B and Figure 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 and Figure S2A 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 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:0000005	Figure 4A and Figure S2A Sublethal concentrations of caspofungin
PMID:34959732	FYPO:0001367	(Sub lethal and lethat doese) Figure 5 and Figure S3. Also in the Table 3.
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	(Sub lethal and lethat doese) Figure 5 and Figure S3. Also in the Table 3.
PMID:34959732	FYPO:0001367	Figure 3A and Figure S1A. Table 3. Suppression of the lytic phenotype at cytokinesis
PMID:34967420	PBO:0102813	RNA-Seq
PMID:34967420	PBO:0102811	RNA-Seq
PMID:34967420	PBO:0102810	Northern Blotting, RNA-Seq
PMID:34967420	PBO:0102817	RNA-Seq
PMID:34967420	PBO:0102818	RNA-Seq
PMID:34967420	PBO:0102819	RNA-Seq
PMID:34967420	PBO:0102820	RNA-Seq
PMID:34967420	PBO:0102821	RNA-Seq
PMID:34967420	PBO:0102822	RNA-Seq
PMID:34967420	PBO:0102823	RNA-Seq
PMID:34967420	PBO:0102824	RNA-Seq
PMID:34967420	PBO:0102825	RNA-Seq
PMID:34967420	PBO:0102826	RNA-Seq
PMID:34967420	PBO:0102827	RNA-Seq
PMID:34967420	PBO:0102828	RNA-Seq
PMID:34967420	PBO:0102815	RNA-Seq
PMID:34967420	PBO:0102816	RNA-Seq
PMID:34967420	PBO:0102814	RNA-Seq
PMID:34967420	PBO:0102812	RNA-Seq
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:0006133	fig 5 b. (thin-layer chromatography) We detected an accumulation of PHS and sphingoid bases-1-phosphate levels (PHS-1P or DHS-1P)
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	FYPO:0005593	(thin-layer chromatography) 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: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: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:0001357	These synthetic phenotypes were again suppressed by the nse1-C216S mutation (Figure S5).
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: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	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	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	FYPO:0001355	severe growth defects with smc6-X and nse6∆
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: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	GO:0061631	Figure 1A
PMID:35011726	PBO:0093618	(Figure 3A) ubiquitin ligase mutant
PMID:35011726	GO:0061631	Figure 1A
PMID:35011726	FYPO:0001913	(Figure 2D
PMID:35011726	PBO:0105578	Among the Nse1-bound factors, we repeatedly ob- served 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:35012333	PBO:0094771	Fig 10B
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	FYPO:0007820	Fig S6
PMID:35012333	PBO:0096728	Fig S6, new term suggested
PMID:35012333	FYPO:0008027	Fig 12B
PMID:35012333	FYPO:0008027	Fig 12B
PMID:35012333	FYPO:0008027	Fig 12B
PMID:35012333	FYPO:0001357	Fig S5A
PMID:35012333	FYPO:0001357	Fig S5A
PMID:35012333	PBO:0094777	Fig S5B
PMID:35012333	PBO:0094777	Fig S5B
PMID:35012333	FYPO:0001357	Fig S4
PMID:35012333	FYPO:0001357	Fig S4
PMID:35012333	FYPO:0000080	Fig S4
PMID:35012333	FYPO:0000080	Fig S4
PMID:35012333	FYPO:0000080	Fig S4
PMID:35012333	FYPO:0000080	Fig S4
PMID:35012333	FYPO:0001357	Fig S3
PMID:35012333	FYPO:0001357	Fig S3
PMID:35012333	FYPO:0001357	Fig S3
PMID:35012333	FYPO:0002085	Fig S3
PMID:35012333	FYPO:0001357	Fig S2
PMID:35012333	FYPO:0007820	Fig 13
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	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	Described in Garg et al. (NAR 2020) -PMID: 33010152
PMID:35012333	FYPO:0002061	Described in Garg et al. (NAR 2020) -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: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:0094738	Fig 10B
PMID:35012333	PBO:0094738	Fig 10B
PMID:35012333	PBO:0094738	Fig 10B
PMID:35012333	FYPO:0001357	Fig 4
PMID:35012333	PBO:0093553	Fig 8A
PMID:35012333	PBO:0093555	Fig 8A
PMID:35012333	PBO:0094738	Fig 8B
PMID:35012333	PBO:0094771	Fig 8B
PMID:35012333	PBO:0093557	Fig 7A
PMID:35012333	PBO:0093557	Fig 7A
PMID:35012333	PBO:0093555	Fig 7A
PMID:35012333	PBO:0093555	Fig 7A
PMID:35012333	PBO:0094777	Fig 7B
PMID:35012333	PBO:0094777	Fig 7B
PMID:35012333	PBO:0094777	Fig 7B
PMID:35012333	PBO:0094738	Fig 7B
PMID:35012333	PBO:0094738	Fig 7B
PMID:35012333	PBO:0094738	Fig 7B
PMID:35012333	PBO:0093553	Fig 7A
PMID:35012333	FYPO:0001357	Fig 7A
PMID:35012333	FYPO:0001357	Fig 7A
PMID:35012333	FYPO:0001357	Fig 6A
PMID:35012333	FYPO:0001357	Fig 6A
PMID:35012333	PBO:0094771	Fig 6B
PMID:35012333	PBO:0094771	Fig 6B
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: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:0093557	Fig 5A
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 5B
PMID:35012333	PBO:0094771	Fig 4B
PMID:35012333	PBO:0094777	Fig 4B
PMID:35012333	PBO:0094777	Fig 4B
PMID:35012333	PBO:0094777	Fig 4B
PMID:35012333	PBO:0094738	Fig 5B
PMID:35012333	PBO:0094738	Fig 5B
PMID:35012333	PBO:0094738	Fig 5B
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:0093558	Fig 4A
PMID:35012333	PBO:0093558	Fig 4A
PMID:35012333	PBO:0093558	Fig 4A
PMID:35012333	FYPO:0001357	Fig 2A
PMID:35012333	PBO:0094771	Fig 2B
PMID:35012333	PBO:0093553	Fig 2A
PMID:35012333	PBO:0093553	Fig 2A
PMID:35012333	PBO:0093553	Fig 2A
PMID:35012333	PBO:0094738	Fig 2B
PMID:35012333	PBO:0094738	Fig 2B
PMID:35012333	PBO:0094738	Fig 2B
PMID:35012333	PBO:0093553	Fig 1A
PMID:35012333	PBO:0093553	Fig 1A
PMID:35012333	PBO:0093561	Fig 1A
PMID:35012333	PBO:0093561	Fig 1A
PMID:35012333	PBO:0093561	Fig 1A
PMID:35012333	FYPO:0001357	Fig 1A
PMID:35012333	FYPO:0001357	Fig 1A
PMID:35012333	FYPO:0001357	Fig 1A
PMID:35012333	GO:0006799	from polyphosphate absent from cell
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	abolished figure 1E
PMID:35058438	PBO:0112402	abolished figure 1E
PMID:35058438	PBO:0112402	figure 1j
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	-v regulation, stationary phase
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. 3). We found that Fzo1 protein was not degraded at late time points in the ∆rsv2 mutant
PMID:35075549	PBO:0095252	****STATIONARY PhASE**** the protein level of Fzo1 is unstable during the stationary phase.
PMID:35075549	PBO:0095255	-ve regulation stat 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: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	PBO:0096832	(Figures 4A,B) we found that the protein level of Cdr2 in ksg1-208 cells was significantly lower than that in wild-type cells
PMID:35082773	FYPO:0002061	(Figure 2C) 33 degrees
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: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,B),
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: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:0096835	(Figure 5A) In addition, the Cdc25 protein level decreased in 􏰀ppk21 and 􏰀cdr2 cells as well, indicating the role of Ppk21 and Cdr2 on regulating Cdc25 protein level .
PMID:35082773	FYPO:0003503	(Figures 3A,B) overexpression of cdr2+ also reversed the defects in the cell length and the septation index of ksg1-208 cells
PMID:35082773	PBO:0096835	(Figure 5A). In addition, the Cdc25 protein level decreased in 􏰀ppk21 and 􏰀cdr2 cells as well, indicating the role of Ppk21 and Cdr2 on regulating Cdc25 protein level
PMID:35082773	PBO:0093561	Figure 1A
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: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	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:0096314	(Figures 2D,E) results showed that ksg1-208 􏰀ppk21 cells exhibited a longer cell length than either ksg1-208 or 􏰀ppk21 cells at both 27 and 33◦C
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	PBO:0104536	Pxl1-AxxA1-3 bound Cdc15C1(aa600-end) just as well as wild type Pxl1 (Figure S1A)
PMID:35108037	GO:0005515	Figure 1B, 1D-F, 2B-E, 3A-B, S1A-B
PMID:35108037	PBO:0104527	in vitro binding assay, Figure 3B
PMID:35108037	PBO:0104528	in vitro binding assay with purified Cdc15 F-BAR domain and purified Pxl1 (Fig 1E)
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 (19c)
PMID:35108037	FYPO:0000674	Figure S2D
PMID:35108037	FYPO:0001357	Figure S2D(25,29,32)
PMID:35108037	FYPO:0003809	Figure S2D
PMID:35108037	FYPO:0004675	Fig S2D
PMID:35108037	FYPO:0002141	Figure S2D
PMID:35108037	FYPO:0002141	Figure S2D
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: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	PBO:0104534	Figure 2B - Pxl1(AxxA1-6) reduced binding to Cdc15C(aa441-end) compared to wildtype Pxl1
PMID:35108037	PBO:0104528	Pxl1 (aa177-188 P181A, P184A) abolished binding to Cdc15 SH3 and Cdc15C1(aa600-end), Figure 2D
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+AxxA6 reduced binding to full-length Cdc15 compared to wild type Pxl1 (Figure 3A)
PMID:35108037	PBO:0104535	Pxl1-P18A reduced binding to full-length Cdc15 compared to wild-type Pxl1 (Figure 3A)
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 wildtype Pxl1 (Figure S1A)
PMID:35108037	FYPO:0006187	Figure S3A (25C)
PMID:35108037	FYPO:0006187	Figure S3A (25C)
PMID:35108037	FYPO:0006187	Figure S3A (25C)
PMID:35108037	FYPO:0007828	Figure S3A (25C)
PMID:35108037	FYPO:0007828	Figure S3A
PMID:35108037	FYPO:0007828	Figure S3A (25C)
PMID:35108037	FYPO:0004895	Figure S3A (25C)
PMID:35108037	FYPO:0001365	Figure S3A (25C)
PMID:35108037	FYPO:0001365	Figure S3A (25C)
PMID:35108037	PBO:0104537	Figure S3B (25C)
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:0002060	Figure S2E
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:0002060	Figure S2E
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:0002060	Figure S2E
PMID:35108037	FYPO:0002060	Figure S2E
PMID:35108037	FYPO:0002060	Figure S2E
PMID:35108037	FYPO:0002060	Figure S2E
PMID:35157728	FYPO:0003555	Figure2 A
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: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	GO:0000122	Tor1 inhibits the binding of Gcn5 at sub-telomeric genes and MBF promoters
PMID:35157728	FYPO:0003555	Figure2 A
PMID:35157728	FYPO:0003555	Figure2 A
PMID:35157728	FYPO:0006742	Figure2 A
PMID:35157728	FYPO:0006742	Figure2 A
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	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	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	FYPO:0003555	Figure2 A
PMID:35157728	PBO:0093824	24%
PMID:35157728	FYPO:0003555	Figure2 A
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	FYPO:0003555	Figure2 A
PMID:35157728	FYPO:0003555	Figure2 A
PMID:35157728	FYPO:0003555	Figure2 A
PMID:35157728	FYPO:0003555	Figure2 A
PMID:35157728	FYPO:0003555	Figure2 A
PMID:35157728	FYPO:0003555	Figure2 A
PMID:35157728	FYPO:0006742	Figure2 A
PMID:35157728	PBO:0110920	120 fold. Fig 2
PMID:35157728	PBO:0100683	The Δbdf2 muta- tion also suppresses the elevated levels of Gcn5 at the subtelomeric chromatin in Δtor1 cells (Fig 4E).
PMID:35157728	PBO:0110919	280 fold. Fig 2
PMID:35157728	PBO:0110918	30 fold. Fig 2
PMID:35157728	PBO:0100681	We detected a markedly higher level of Gcn5 binding at subte- lomeric genes in Δtor1 cells, compared with wild type cells (Fig 4A).
PMID:35157728	PBO:0093824	25%
PMID:35157728	FYPO:0003555	Figure2 A
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:3516412	GO:0004672	activated_by(CHEBI:18420)
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 silenc- ing defects of otr::ura4+ caused by Epe1 overexpression, as indicated by better growth on EMM medium containing 5-FOA (Fig 1D)
PMID:35171902	FYPO:0003574	H3K9me2 levels at dh repeats are restored close to wild-type levels in git3Δ nmt41-epe1+ cells (Fig 1E).
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:0104711	. Interestingly, although git3Δ nmt41-epe1+ cells form heterochromatin at pericentric repeats,
PMID:35171902	PBO:0104712	polysome profiling
PMID:35171902	PBO:0104712	polysome profiling
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: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: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: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: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 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	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:0113566	When treated with TAM, the vps54 heterozygous mutants showed more enlarged vesicles (yellow ar- rows in Fig. 3) ....., com- pared with the SP286 control.
PMID:35194019	PBO:0093562	TBZ 15ug/ml
PMID:35194019	FYPO:0001357	Fig S10 (tetrad analysis)
PMID:35194019	FYPO:0001357	Fig S10 (tetrad analysis)
PMID:35194019	FYPO:0001357	Fig S10 (tetrad analysis)
PMID:35194019	FYPO:0001357	Fig S10 (tetrad analysis)
PMID:35194019	FYPO:0002061	Fig S10 (tetrad analysis)
PMID:35194019	FYPO:0000964	TBZ 15ug/ml
PMID:35194019	FYPO:0002061	Fig S10 (tetrad analysis)
PMID:35194019	PBO:0032778	Figur 5D
PMID:35194019	PBO:0096785	Figur 5D
PMID:35194019	FYPO:0004742	Figure 5C forward strand RT-qPCR (dh repeat)
PMID:35194019	FYPO:0003412	Figur 5C forward strand RT-qPCR (dh repeat)
PMID:35194019	PBO:0093564	TBZ 15ug/ml
PMID:35194019	PBO:0093562	TBZ 15ug/ml
PMID:35194019	FYPO:0001357	Fig S10 (tetrad analysis)
PMID:35194019	FYPO:0004742	Figure 5C forward strand RT-qPCR (dh repeat)
PMID:35194019	FYPO:0004742	Figure 5C forward strand RT-qPCR (dh repeat)
PMID:35194019	FYPO:0004742	Figur 5C forward strand RT-qPCR (dh repeat)
PMID:35194019	FYPO:0003412	Figure 5C forward strand RT-qPCR (dh repeat)
PMID:35194019	PBO:0093562	TBZ 15ug/ml
PMID:35277511	FYPO:0002239	telomere southern (experiment)
PMID:35277511	FYPO:0002060	growth >48 hrs, growth to exponential phase
PMID:35277511	FYPO:0002239	telomere southern (experiment)
PMID:35286199	FYPO:0002058	Fig. 1
PMID:35286199	PBO:0093561	Fig. 1
PMID:35286199	FYPO:0002058	Fig. 1
PMID:35286199	FYPO:0002058	Fig. 1
PMID:35286199	PBO:0093559	Fig. 1
PMID:35286199	FYPO:0001357	Fig. 1
PMID:35286199	FYPO:0000339	Fig. 4
PMID:35286199	FYPO:0001357	Fig. 1
PMID:35286199	PBO:0101442	Fig. 3
PMID:35286199	PBO:0107133	Fig. 4
PMID:35286199	FYPO:0000069	Fig. 4
PMID:35286199	FYPO:0003227	Fig. 4
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	PBO:0093561	Fig. 1
PMID:35286199	FYPO:0002058	Fig. 1
PMID:35286199	FYPO:0002058	Fig. 1
PMID:35286199	PBO:0093559	Fig. 1
PMID:35286199	PBO:0093559	Fig. 1
PMID:35286199	FYPO:0001357	Fig. 1
PMID:35286199	PBO:0107132	Fig. 2
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:0000276	Fig. 2
PMID:35286199	FYPO:0002061	Fig. 1
PMID:35286199	FYPO:0002060	Fig. 1
PMID:35286199	FYPO:0002058	Fig. 1
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:0096311	Note: not sure about the term name and the child. Fig. 3 supp 1 A, C
PMID:35293864	PBO:0106718	Fig. 5 supp 3E
PMID:35293864	FYPO:0007972	mal3Δ cells exhibited lower microtubule growth speed throughout anaphase B Fig. 2G
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:0106719	Fig. 5E Ase1 is required for normal rescue distribution
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: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:0106716	Fig. 2 - Figure supplement 1 klp5Δklp6Δ cells exhibited slightly longer microtubule growth events
PMID:35293864	PBO:0106717	Fig. 2 - Figure supplement 2F
PMID:35293864	PBO:0106718	Fig. 2 - Figure supplement 2E
PMID:35300005	FYPO:0001029	100 ug/ml canavanine
PMID:35314193	PBO:0098306	Figures 1 and 3
PMID:35314193	PBO:0098307	Figure 8
PMID:35314193	PBO:0098307	Figure 8
PMID:35314193	PBO:0098307	Figure 8
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	GO:0016791	Cobalt/nickel-dependent inorganic pyrophosphatase activity, Figure 4
PMID:35314193	GO:0016791	Cobalt/nickel-dependent inorganic pyrophosphatase activity, Figure 1
PMID:35314193	FYPO:0002085	Figure 12
PMID:35314193	FYPO:0002085	Figure 12
PMID:35314193	PBO:0094738	Figure 12
PMID:35314193	PBO:0094777	Figure 12
PMID:35314193	PBO:0094738	Figure 12
PMID:35314193	PBO:0110566	Cobalt/nickel-dependent inorganic pyrophosphatase activity, Figure 3
PMID:35314193	PBO:0110566	Cobalt/nickel-dependent inorganic pyrophosphatase activity, Figure 4
PMID:35320724	PBO:0107705	Figure S5
PMID:35320724	PBO:0107692	Figure 1B, 5B
PMID:35320724	PBO:0107691	Figure 1B, 5B
PMID:35320724	PBO:0107693	Figure 4
PMID:35320724	PBO:0107690	Figure 1B, 2D, 5B, 6C, 7B, 7C
PMID:35320724	PBO:0107690	Figure S6B
PMID:35320724	PBO:0107690	Figure 3, S1
PMID:35320724	PBO:0107689	Figure S6G
PMID:35320724	FYPO:0001489	Figure 6
PMID:35320724	FYPO:0002061	Figure 6
PMID:35320724	FYPO:0001489	Figure 6
PMID:35320724	PBO:0107702	Figure 5
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: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 se- curin degradation was unaffected in the cdc48-353 mutant.
PMID:35320724	PBO:0107691	Figure 3, S1
PMID:35320724	FYPO:0001491	Figure 2C
PMID:35320724	FYPO:0001491	Figure 2C
PMID:35320724	PBO:0107692	Figure S1
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	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	FYPO:0002060	Figure 6
PMID:35320724	PBO:0107699	Figure 7
PMID:35320724	PBO:0107699	Figure 7
PMID:35320724	PBO:0107700	Figure 7
PMID:35320724	PBO:0107701	Figure 7
PMID:35320724	PBO:0107700	Figure 7
PMID:35320724	PBO:0107700	Figure 7
PMID:35320724	PBO:0107702	Figure 4
PMID:35320724	PBO:0107703	Figure 4
PMID:35320724	PBO:0107702	Figure S4
PMID:35320724	PBO:0107704	Figure S5
PMID:35320724	PBO:0096891	Figure 4
PMID:35320724	FYPO:0002061	Figure 5
PMID:35320724	FYPO:0002060	Figure 5
PMID:35320724	FYPO:0002061	Figure S6D
PMID:35320724	PBO:0107690	Figure 4
PMID:35320724	FYPO:0002060	Figure 4
PMID:35320724	FYPO:0002061	Figure 4
PMID:35320724	PBO:0107690	Figure S7
PMID:35320724	PBO:0107690	Figure 6
PMID:35320724	FYPO:0002060	Figure 4
PMID:35320724	FYPO:0001234	Figure 4
PMID:35325114	FYPO:0007990	TERM REQUESTED growth auxotrophic for isoleucine
PMID:35325114	FYPO:0007991	TERM REQUESTED growth auxotrophic for valine
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: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	FYPO:0002485	(Figure 7) rec8-F204S mutant is defective in LinE formation and recombination
PMID:35333350	FYPO:0003613	(Figure 5C) The rec8-F204S mutant maintained sister chromatid cohesion as assessed at the cut3 gene locus
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:0003179	(Figure 7)
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	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:0007945	Figure S4B
PMID:35333350	FYPO:0007942	figure 4c,e also supported by (Figure 4A), 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:0000197	Supplementary Figure S4B) wpl1Δ rarely showed torsional turning (Supplementary Figure S4C, Supplemen- tal 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: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: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: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:0003054	during horsetail/ prophase
PMID:35333350	FYPO:0001357	(Figure S5B)
PMID:35333350	FYPO:0001357	(Figure S5B)
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:35354597	FYPO:0003750	Fig. 2C
PMID:35354597	FYPO:0003750	Fig. 2C
PMID:35354597	FYPO:0003750	Fig. 2B
PMID:35354597	FYPO:0003750	Fig. 2B
PMID:35354597	FYPO:0003750	Fig. 2D
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	PBO:0112112	NPC clusters in nup132Δ nuclei coalesced into larger clusters that preferentially localized to the SPBs in mitosis. Fig. 3F
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	FYPO:0003750	Fig. 2C
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	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:35354597	GO:0044732	Fig. 5
PMID:35416247	PBO:0092325	in presence of tschimganine
PMID:35416247	PBO:0092325	in presence of tschimganine
PMID:35416247	PBO:0095654	in presence of tschimganine
PMID:35416247	PBO:0095654	in presence of tschimganine
PMID:35416247	PBO:0095654	in presence of tschimganine
PMID:35416247	PBO:0095654	in presence of tschimganine
PMID:35416247	PBO:0092325	in presence of tschimganine
PMID:35416247	PBO:0092325	in presence of tschimganine
PMID:35512546	GO:0008266	RRM3
PMID:35536002	PBO:0100393	Fig. 7
PMID:35536002	PBO:0100389	Fig. 8 and text
PMID:35536002	PBO:0100390	Fig. 7
PMID:35536002	PBO:0100390	Fig. 7
PMID:35536002	PBO:0100390	Fig. 7
PMID:35536002	PBO:0100390	Fig. 7
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: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: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: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:35609605	PBO:0099979	COMPACTION Figures 3A, 3B, and S3A (inhibiting exocytosis rescues defect of compaction)
PMID:35609605	PBO:0099978	(partial rescue) Incomplete ring compaction was still observed in myo2- E1pil1D, although such fraction was reduced as compared with myo2-E1 (Figure 3B I don't see the images - this is from the bar chart))
PMID:35609605	PBO:0099980	COMPACTION Figures 3A, 3B, and S3A
PMID:35609605	PBO:0099981	figure 4D
PMID:35609605	PBO:0099982	figure 4D
PMID:35609605	PBO:0099977	Figure 3 COMPACTION
PMID:35609605	FYPO:0001009	"Figures 3A, 3B, and S3A (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	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(aaG345R) 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:35622906	PBO:0113860	OLD SPB
PMID:35639710	PBO:0104696	Fig 1
PMID:35639710	PBO:0097854	Figure1
PMID:35639710	PBO:0104698	Increased protein ubiquitination.
PMID:35639710	PBO:0104696	Fig 1
PMID:35639710	PBO:0104695	Second, Any1R175C does not show an increase but rather a strong decrease in its ubiquiti- nation level.
PMID:35639710	PBO:0104699	Figure 2A
PMID:35639710	PBO:0097854	Figure3 confirms dominance of can1-1
PMID:35639710	FYPO:0001545	Figure 1 (same as WT)
PMID:35658118	PBO:0107530	Therefore, increased cell death rather than abnormal cell division was the conse- quence of the impaired cell proliferation caused by the absence of Acb1 (Fig. 3D).
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 conse- quence of the impaired cell proliferation caused by the absence of Acb1 (Fig. 3D).
PMID:35658118	FYPO:0008137	Intriguingly, the size of lipid droplets became lar- ger 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	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:0109726	he expression of Dnm1 was comparable in wild-type and acb1Δ cells (Fig. 2E).
PMID:35658118	PBO:0093797	(phenotypoe seems to be additive on glycerol) Consistently, the growth of acb1Δ and acb1Δdnm1Δ cells on nonfer- mentable 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 con- trast, 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 med- ium than acb1+ cells and much slower on nonfer- mentable medium.
PMID:35658118	PBO:0093559	Figure 1b and 3c
PMID:35658118	FYPO:0001357	figure 1b a nd 3C
PMID:35658118	PBO:0110548	We noticed that mito- chondrial 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 observa- tion showed that mitochondria were tubular in acb1+ cells but became fragmented in acb1Δ cells (Fig. 1A).
PMID:35673994	PBO:0102728	Fig. 5
PMID:35673994	FYPO:0006108	Fig. 6
PMID:35673994	PBO:0102726	Fig. 6
PMID:35673994	FYPO:0006108	Fig. 6
PMID:35673994	PBO:0108178	Fig. 6
PMID:35673994	PBO:0108178	Fig. 5
PMID:35673994	PBO:0108178	Fig. 2B
PMID:35673994	FYPO:0006108	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	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	PBO:0102716	Fig. 4E
PMID:35673994	PBO:0102716	Fig. 4E
PMID:35673994	PBO:0108173	Fig. 2B
PMID:35673994	PBO:0108173	Fig. 2B
PMID:35673994	PBO:0108172	Fig. 2B
PMID:35673994	FYPO:0005989	Fig. 2A
PMID:35673994	PBO:0108171	Fig. 2B
PMID:35673994	PBO:0102728	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. 6
PMID:35673994	PBO:0108170	Fig. 3
PMID:35673994	FYPO:0007683	Fig. 3
PMID:35673994	PBO:0102720	Fig. 2D
PMID:35673994	PBO:0102728	Fig. 6
PMID:35673994	PBO:0108175	Fig. 5
PMID:35673994	PBO:0108178	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	decreased
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:0093560	As anticipated, the resulting trm6Δ imt06Δ strain grew very poorly at 30 ̊C, and was temperature sensitive at higher tem- peratures, 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: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: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 quantifica- tion with the high background gave 2.0% for trm6Δ and 2.8% in trm61Δ).
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:0093558	S1
PMID:35901126	PBO:0093558	S1
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	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 tempera- ture, 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	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) lack- ing m1A58 in S. pombe.
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	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) lack- ing 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	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 tem- peratures, not growing at all at 37 ̊C,
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	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	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: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 quantifica- tion with the high background gave 2.0% for trm6Δ and 2.8% in trm61Δ).
PMID:35901126	PBO:0093558	As anticipated, the resulting trm6Δ imt06Δ strain grew very poorly at 30 ̊C, and was temperature sensitive at higher tem- peratures, not growing at all at 37 ̊C,
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:0093560	As anticipated, the resulting trm6Δ imt06Δ strain grew very poorly at 30 ̊C, and was temperature sensitive at higher tem- peratures, 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: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:35924983	FYPO:0001355	Supplemental Figure 4
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	PBO:0093560	Supplemental Figure 6
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	PBO:0109486	Fig. 6
PMID:35924983	PBO:0020040	Fig. 6
PMID:35924983	PBO:0093770	Figure 3
PMID:35924983	PBO:0109485	through nuclear exclusion
PMID:35924983	PBO:0109485	through nuclear exclusion
PMID:35924983	PBO:0109485	through degradation by ubiquitination
PMID:35924983	PBO:0109485	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:0109483	Figure 6
PMID:35924983	PBO:0109482	Figure 6
PMID:35924983	PBO:0109482	Figure 6
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	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: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:0093561	Supplemental Figure 4, Table 1
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: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	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: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 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:0093559	Supplemental Figure 4, Table 1
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	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: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	PBO:0093560	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093560	Supplemental Figure 4, Table 1
PMID:35924983	PBO:0093560	Supplemental Figure 4, Table 1
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	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:0093561	Supplemental Figure 4, Table 1
PMID:35940128	FYPO:0003480	Queuosine absent from tRNA when cells are supplied with queuosine nucleoside, but not when supplied with queuine nucleobase
PMID:35940128	PBO:0096360	term requested Queuosine nucleosidase activity
PMID:35970865	PBO:0095634	Fig. 2a
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).""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:0093558	Fig. 2a
PMID:35970865	PBO:0103733	decreased CENP-A maintenance
PMID:35970865	PBO:0105695	normal CENP-A maintenance
PMID:35970865	PBO:0105695	normal CENP-A maintenance
PMID:35970865	PBO:0105695	normal CENP-A maintenance
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: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: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 (during M-phase)
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: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	(during M-phase) Supplementary Fig. 9b). These results demonstrate that kinetochore mutants with the intact inner kinetochore architecture retained the ability to silence transcrip- tion at the central core region.
PMID:35970865	FYPO:0002360	(during M-phase) Supplementary Fig. 9b). These results demonstrate that kinetochore mutants with the intact inner kinetochore architecture retained the ability to silence transcrip- tion at the central core region.
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:35970865	PBO:0095634	Fig. 2a
PMID:35970865	PBO:0105693	figure4
PMID:35970865	PBO:0105694	figure4
PMID:35970865	PBO:0105695	normal CENP-A maintenance
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: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: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:0108631	However, no significant changes were observed for several meiotic mRNAs and PROMPTs/CUTs MTREC targets (Supplementary Fig. 8b, c)
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: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: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: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: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: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: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: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: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:0110945	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: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 simi- lar 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: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: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:0110942	Using these cells, reciprocal co-immunoprecipitation experiments showed that the Red1-L205R mutation also compro- mised Red1 association with Iss10 in S. pombe (Fig. 3a and Supple- mentary Fig. 3a).
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: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: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	FYPO:0005727	figure 1 D
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	FYPO:0005727	figure 1 D
PMID:36006032	FYPO:0005728	figure 1 D
PMID:36006032	FYPO:0005728	figure 1 D
PMID:36006032	FYPO:0005728	figure 1 D
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:0105586	figure 1 D
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	Pab1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest- and-release in the nda3-KM311 mutant background (Figure 2 and Figure S2).
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:0105581	Our in vitro dephosphor- ylation assay results demonstrated that individually overexpressing PP2A subunits indeed boosted the over- all phosphatase activity compared to expressing endog- enous subunits alone (Figure 3B).
PMID:36006032	FYPO:0005728	figure 1 D
PMID:36006032	PBO:0105585	Pab1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest- and-release in the nda3-KM311 mutant background (Figure 2 and Figure S2).
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	FYPO:0005728	figure 1 D
PMID:36006032	PBO:0105587	figure 1 D
PMID:36088506	GO:0005741	As observed, most of Mrz1 was localized in the mitochondrial fraction (Fig. 1B).
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	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:36088506	PBO:0110211	proteasome inhibitor MG132
PMID:36090151	PBO:0093664	1.6 mM
PMID:36090151	PBO:0093664	1.6 mM
PMID:36095128	GO:0045292	Figure S13. C
PMID:36095128	GO:0045292	Figure S13. C
PMID:36095128	GO:0045292	Figure S13. C
PMID:36095128	GO:0045292	Figure S13. C
PMID:36095128	PBO:0109788	figure 1 (rap1 intron2, ftp105 intron 3 and pyp3 intron 1)
PMID:36095128	PBO:0109793	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 lower- ing the temperature to 25◦C, splicing defects of these in- trons recovered in wt cells, but the recovery with whi5 and atg20 introns was slower in Δsde2.
PMID:36095128	GO:0045292	Figure S13. C
PMID:36095128	PBO:0109795	(Supplementary Figures S6 and S7A). rap1 intron 2
PMID:36095128	FYPO:0003619	figure 1 (rap1 intron2 branch site distance decreased)
PMID:36095128	PBO:0109797	Figure S12.B
PMID:36095128	PBO:0109798	Figure S12.B
PMID:36095128	PBO:0109799	Figure S12.B
PMID:36095128	PBO:0109790	figure 1 (rap1 intron2, ftp105 intron 3 and pyp3 intron 1)
PMID:36095128	GO:0045292	Figure S13. C
PMID:36095128	FYPO:0003619	figure 1 (rap1 intron2 branch site distance decreased)
PMID:36095128	FYPO:0008118	figure 1
PMID:36095128	FYPO:0008118	figure 1
PMID:36095128	PBO:0109800	Figure S12.B
PMID:36095128	PBO:0109797	Figure S12.B
PMID:36095128	PBO:0109800	Figure S12.B
PMID:36095128	PBO:0109798	Figure S12.B
PMID:36095128	PBO:0109799	Figure S12.B
PMID:36095128	FYPO:0008118	figure 1
PMID:36095128	PBO:0109800	Figure S12.B
PMID:36095128	PBO:0109791	A shorter form of the protein translated from intron-retained transcript
PMID:36095128	PBO:0109791	A shorter form of the protein translated from intron-retained transcript
PMID:36095128	PBO:0109791	A shorter form of the protein translated from intron-retained transcript
PMID:36095128	PBO:0109791	A shorter form of the protein translated from intron-retained transcript
PMID:36095128	PBO:0109791	A shorter form of the protein translated from intron-retained transcript
PMID:36095128	PBO:0109791	A shorter form of the protein translated from intron-retained transcript
PMID:36095128	PBO:0109791	A shorter form of the protein translated from intron-retained transcript
PMID:36095128	PBO:0109791	A shorter form of the protein translated from intron-retained transcript
PMID:36095128	PBO:0109791	A shorter form of the protein translated from intron-retained transcript
PMID:36095128	PBO:0109792	Semi quantitative RT-PCR followed by gel electrophoresis; Intron retention observed in absence of sde2, cay1 and tls1
PMID:36095128	PBO:0109791	A shorter form of the protein translated from intron-retained transcript
PMID:36095128	PBO:0109791	A shorter form of the protein translated from intron-retained transcript
PMID:36095128	PBO:0109791	A shorter form of the protein translated from intron-retained transcript
PMID:36095128	PBO:0109791	A shorter form of the protein translated from intron-retained transcript
PMID:36095128	PBO:0109791	Figure S13. C A shorter form of the protein translated from intron-retained transcript
PMID:36095128	PBO:0109791	Figure S13. C A shorter form of the protein translated from intron-retained transcript
PMID:36095128	PBO:0109793	Semi quantitative RT-PCR followed by gel electrophoresis; Intron retention observed in absence of sde2, cay1 and tls1
PMID:36095128	PBO:0109792	Semi quantitative RT-PCR followed by gel electrophoresis; Intron retention observed in absence of sde2, cay1 and tls1
PMID:36095128	FYPO:0008118	Among the mutants studied, Δcay1 and Δtls1 strains also showed splicing defects spe- cific for rap1 intron 2 (Supplementary Figure S10A).
PMID:36095128	FYPO:0008118	Among the mutants studied, Δcay1 and Δtls1 strains also showed splicing defects spe- cific for rap1 intron 2 (Supplementary Figure S10A).
PMID:36095128	GO:0045292	Figure S13. C
PMID:36095128	GO:0045292	Figure S13. C
PMID:36095128	GO:0045292	Figure S13. C
PMID:36095128	GO:0045292	Figure S13. C
PMID:36095128	PBO:0109798	Figure S12.B
PMID:36095128	GO:0045292	Figure S13. C
PMID:36095128	PBO:0109789	figure 1 (rap1 intron2, ftp105 intron 3 and pyp3 intron 1)
PMID:36095128	PBO:0109799	Figure S12.B
PMID:36095128	PBO:0109797	Figure S12.B
PMID:36108046	PBO:0093556	I changed to decreased. becasue the phenotype is compared to WT,
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	FYPO:0005706	but dnt1Δ cells stayed for extended length of time at ana- phase B (Fig 1D–1F)
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-segre- gation 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: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 pro- longed period compared to wild-type cells, almost to the same degree as previously identified SAC-inactivation defective mutant dis2Δ
PMID:36108046	PBO:0093556	I changed to decreased. becasue the phenotype is compared to WT,
PMID:36112198	PBO:0107566	low glucose MM
PMID:36112198	PBO:0107568	observed Pka1-GFP
PMID:36112198	PBO:0107568	observed Pka1-GFP
PMID:36112198	PBO:0107569	fig5
PMID:36112198	PBO:0107570	observed Pka1-GFP
PMID:36112198	PBO:0093594	fig1 (double mutant with cyr1 is more sensitive)
PMID:36112198	PBO:0093594	figure 2
PMID:36112198	PBO:0093594	figure 2
PMID:36112198	FYPO:0001020	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:0006717	Fig. S2
PMID:36112198	FYPO:0000961	Fig. S2
PMID:36112198	FYPO:0005947	figure 3
PMID:36112198	FYPO:0005947	fig4
PMID:36112198	PBO:0093595	figure 2
PMID:36112198	PBO:0093595	figure 2
PMID:36112198	FYPO:0000098	Fig. S2
PMID:36112198	FYPO:0006717	figure S2
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	FYPO:0001214	cgs1∆ partially rescues plb1∆ on KCl
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	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:0093593	Fig.1 Overexpression of Pka1 restores the KCl-sensitive pheno- type of the plb1∆ strain.
PMID:36112198	PBO:0093593	Fig.1 Overexpression of Pka1 restores the KCl-sensitive pheno- type of the plb1∆ strain.
PMID:36112198	PBO:0093595	Fig 1b
PMID:36112198	PBO:0093594	rst2∆ partially rescues pka1∆ plb1∆ on KCl
PMID:36112198	FYPO:0000961	rst2∆ rescues pka1∆ plb1∆ on KCl
PMID:36112198	PBO:0107561	glucose MM
PMID:36112198	PBO:0107562	glucose MM
PMID:36112198	PBO:0107567	observed Pka1-GFP
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	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: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	PBO:0020227	figure 1D.
PMID:36138017	PBO:0096644	Dma1 ubiquitinates Tip1
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 ubi- quitination (Fig. 4f), this is consistent with increased polar growth in dma1Δ cells (Fig. 4b).
PMID:36138017	PBO:0096651	(Fig. 2d)
PMID:36138017	FYPO:0002657	(Fig. 4)
PMID:36138017	FYPO:0001017	(Fig. 4)
PMID:36174923	FYPO:0000245	Fig 6
PMID:36174923	FYPO:0000245	Fig. 5.
PMID:36174923	FYPO:0002060	Fig. S5.
PMID:36174923	PBO:0093605	Fig. 5.
PMID:36174923	FYPO:0000245	Fig. 7b partial rescue - still loses viabiltiy at 48 hours
PMID:36174923	FYPO:0000245	Fig. 5.
PMID:36174923	FYPO:0001357	Fig. S5.
PMID:36174923	FYPO:0001357	Fig. S5.
PMID:36174923	PBO:0093605	Fig. 5.
PMID:36174923	PBO:0093605	Fig. 5.
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. 7b partial rescue - still loses viabiltiy at 48 hours
PMID:36174923	PBO:0093605	Fig. 5.
PMID:36174923	PBO:0095018	fig 4
PMID:36174923	PBO:0095017	fig S2
PMID:36174923	PBO:0095016	fig S2
PMID:36174923	PBO:0095015	fig S2
PMID:36174923	PBO:0095014	fig S2
PMID:36174923	PBO:0095013	fig S2
PMID:36174923	PBO:0095001	figure1
PMID:36200823	FYPO:0000047	However, deletion strains of two genes encod- ing SWI/SNF core components, snf5 and snf22, did not exhibit sensitivity to CENP-ACnp1 overexpression (Supple- mentary Figure S2A).
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: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: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:0094597	In sfh1-13 mutant cells, a small but signifi- cant increase in the localization of CENP-CCnp3 and CENP- IMis6 was observed at surrounding pericentromeric repeats (Figure 2B and C);
PMID:36200823	PBO:0094596	In sfh1-13 mutant cells, a small but signifi- cant increase in the localization of CENP-CCnp3 and CENP- IMis6 was observed at surrounding pericentromeric repeats (Figure 2B and C);
PMID:36200823	PBO:0094595	However, the sfh1-13 mutation had only a mild influence on H3K9me levels (Figure 1C), as we re- ported previously (12).
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: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	PBO:0094594	Importantly, no significant dif- ference in the level of Cnp1 protein or mRNA was seen in sfh1-13 cells (Figure 1E).
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:0000047	However, deletion strains of two genes encod- ing SWI/SNF core components, snf5 and snf22, did not exhibit sensitivity to CENP-ACnp1 overexpression (Supple- mentary Figure S2A).
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:0000141	In addition, a low concentra- tion of TBZ enhanced the chromosome segregation de- fects of the temperature-sensitive sfh1-13 mutant (Supple- mentary Figure S1A).
PMID:36200823	PBO:0093562	In addition, a low concentra- tion of TBZ enhanced the chromosome segregation de- fects of the temperature-sensitive sfh1-13 mutant (Supple- mentary Figure S1A).
PMID:36200823	FYPO:0008036	Importantly, MNase protection at sites i, iii, and v, which are located between CENP-ACnp1 and heterochro- matin 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), indicat- ing that Sfh1/RSC contributes to chromatin decompaction at the boundary.
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 sin- gle 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:36200871	GO:0005886	Supplemental Figure S5A). We concluded that the calcium-permeable Pkd2 primarily localizes to the plasma membrane.
PMID:36200871	PBO:0109062	Figure 2, E and F). We concluded that Pkd2 is calcium-permeable under the mechanical stimulus of membrane stretching.
PMID:36200871	FYPO:0008063	The peak amplitude of the cal- cium 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:36259651	FYPO:0003031	When cells were grown in media containing nitro- gen sources, some of the nc1669􏰄 cells underwent mating (followed by meiosis), whereas WT cells never initiated mat- ing (Figure 3B, C)
PMID:36259651	PBO:0094617	When cells were grown in media containing nitro- gen sources, some of the nc1669􏰄 cells underwent mating (followed by meiosis), whereas WT cells never initiated mat- ing (Figure 3B, C)
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: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:0001723	data not shown, related data in Figure 2A
PMID:36302945	FYPO:0002988	Figure 3, this phenotype was observed for cat1_delta leu1-32 double mutant.
PMID:36361590	PBO:0102894	figure3
PMID:36361590	PBO:0102895	figure3
PMID:36361590	GO:0005681	Gpl1-Gih35-Wdr83 complex
PMID:36361590	GO:0005681	Gpl1-Gih35-Wdr83 complex
PMID:36361590	PBO:0102894	figure3
PMID:36361590	PBO:0102895	figure3
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	GO:0005681	Gpl1-Gih35-Wdr83 complex
PMID:36361590	PBO:0102893	Figure 2
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	PBO:0100296	Figure 4 A (This obser- vation 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	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	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	PBO:0111081	Indeed, CDK1/Cyclin B phosphorylated recombinant Clr4 specifically at S458 (Fig 6E).
PMID:36408846	FYPO:0008048	This revealed reduced H3K9me2, but increased H3K9me3 levels upon 1-NM-PP1 addition in cdk1-as cells specifi- cally (Fig 6F),
PMID:36408846	FYPO:0008047	clr4F449Y/clr4F449Y cells displayed strongly ele- vated H3K9me2 levels when in mitosis, while H3K9me3 was absent (Figs 2A and EV3A).
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	FYPO:0008038	clr4F449Y/clr4F449Y cells displayed strongly ele- vated H3K9me2 levels when in mitosis, while H3K9me3 was absent (Figs 2A and EV3A).
PMID:36408846	FYPO:0008052	clr4F449Y/clr4F449Y cells displayed strongly ele- vated H3K9me2 levels when in mitosis, while H3K9me3 was absent (Figs 2A and EV3A).
PMID:36408846	FYPO:0008050	(Check tomorrow should this be tri methylation)
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	PBO:0112497	Consistent with earlier findings, we frequently observed spores with two GFP dots in a sin- gle 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 ana- lyzed (Fig 3E)
PMID:36408846	FYPO:0002150	figure 3F
PMID:36408846	PBO:0100295	figure 4a
PMID:36408846	PBO:0100295	figure 4a
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	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: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:0032040	We isolated nascent 40S (also known as small subunit processome) by pull- ing 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 pull- ing 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 pull- ing 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 pull- ing down fibrillarin (Nop1)-associated particles (Figure S4I; Table S3; Data S1)
PMID:36423630	PBO:0111365	Although the overall Fkbp39 protein levels are slightly reduced in fkbp41D total lysates (Fig- ure 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 accu- mulation 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 accu- mulation 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 de- tected Ytm1 on chromatin, primarily at the 30 end of the rDNA re- peats, specifically enriched at the 30 ETS and the non-tran- scribed 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 sepa- rates 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 pull- ing 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 pull- ing 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 pull- ing 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 pull- ing 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 pull- ing 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 pull- ing 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 pull- ing 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 pull- ing 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 pull- ing 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 pull- ing down fibrillarin (Nop1)-associated particles (Figure S4I; Table S3; Data S1)
PMID:36423630	GO:0000785	By contrast, Fkbp41 is found pri- marily in the insoluble chromatin fraction (Figure S1C).
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 nucle- ophosmins,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 nucle- ophosmins,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: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	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	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: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	GO:0030684	We identi- fied 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: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	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: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	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:36435910	PBO:0109110	Figure 2a
PMID:36435910	PBO:0109110	Figure 2a
PMID:36435910	PBO:0109107	Dis1 uses its TOG domains to induce microtubule catastrophe, in which polymerisation turns into depolymerisation
PMID:36435910	FYPO:0009057	Figure 2a
PMID:36435910	PBO:0114753	Evidence: in vitro biochemical assays using purified tubulin and recombinant Dis1 protein / New GO term requested: microtubule destabilization activity
PMID:36435910	PBO:0109109	Figure 2a
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: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: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	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: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: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: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: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: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	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:36537249	GO:0005515	binds to Mhf1
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	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:0108732	abolished Mhf1 localization
PMID:36537249	PBO:0108788	mitotic prophase
PMID:36537249	GO:0005515	binds to Mhf2
PMID:36574843	GO:0031569	dosage dependent (We conclude that increased levels of Cdr2 cause hyperphosphorylation of Wee1 leading to reduced cell size at division.)
PMID:36574843	PBO:0110794	HYPERPHOSPHORYLATED WEE1 (get identifier)
PMID:36574843	PBO:0110786	(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	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: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	PBO:0110789	figure3
PMID:36574843	PBO:0110788	figure3
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	FYPO:0003481	In contrast, Tet-based overexpression of cdr2(E177A) increased the size of dividing cells, consistent with dominant-negative effects for
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 wildtype 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:0107939	Fig. 1C, Fig. 1D and Fig. 1E
PMID:36633091	FYPO:0002071	Fig. 3B
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	PBO:0107936	Fig. S1D and S1E
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:36633091	PBO:0107936	Fig. 1C, ID and 1E
PMID:36633091	PBO:0107937	Fig. 2A and 2C
PMID:36633091	PBO:0107938	Fig. 2A and 2B
PMID:36633091	FYPO:0002029	Supplementary Fig. S1D and S1E
PMID:36650056	PBO:0102167	Lower levels in the akr1 mutant
PMID:36650056	FYPO:0002890	change to: twin horsetail nucleus
PMID:36650056	FYPO:0000510	Change to: Nuclear congression without nuclear fusion
PMID:36650056	PBO:0102161	akr1Δ affecting tht1
PMID:36650056	FYPO:0004795	Was annotated as normal meiosis
PMID:36650056	FYPO:0002890	change to: twin horsetail nucleus
PMID:36650056	FYPO:0000510	Change to: Nuclear congression without nuclear fusion
PMID:36650056	FYPO:0002890	change to: twin horsetail nucleus
PMID:36650056	FYPO:0000510	Change to: Nuclear congression without nuclear fusion
PMID:36650056	PBO:0102167	Lower levels in the akr1 mutant
PMID:36650056	PBO:0102168	palmitoylation of tht1D is reduced by akr1D
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:0103279	Very high levels of diploidization in minimal medium
PMID:36695178	PBO:0103280	Very prominent in minimal medium due to the lack of the Kennedy pathway precursors
PMID:36695178	FYPO:0000229	Very prominent in minimal medium due to the lack of the Kennedy pathway precursors
PMID:36695178	PBO:0019210	Very prominent in minimal medium due to the lack of the Kennedy pathway precursors
PMID:36695178	FYPO:0005584	LC-MS
PMID:36695178	FYPO:0005584	LC-MS
PMID:36695178	PBO:0103281	Sub-lethal phenotype, with only 10% of expected double mutants recovered.
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:0005584	LC-MS
PMID:36695178	FYPO:0005585	LC-MS
PMID:36695178	FYPO:0005585	LC-MS
PMID:36695178	FYPO:0005585	LC-MS
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:0109293	Figure 3 summarizes data
PMID:36705602	PBO:0109293	Figure 3 summarizes data
PMID:36705602	PBO:0100540	Figure 3 summarizes data
PMID:36749320	PBO:0109286	Figure 10 - Manu: transfer to FYPO:0008075
PMID:36749320	PBO:0109286	Figure 10 - 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: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: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: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: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:0109287	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:0109288	Figure 5A
PMID:36749320	PBO:0109288	Figure 5A
PMID:36749320	PBO:0109288	Figure 5A
PMID:36749320	PBO:0109286	Figure 5A
PMID:36749320	PBO:0109288	Figure 5A
PMID:36749320	PBO:0109287	Figure 5A
PMID:36749320	PBO:0109287	Figure 5A
PMID:36749320	PBO:0109287	Figure 5A
PMID:36749320	PBO:0109286	Figure 5A
PMID:36749320	PBO:0109288	Figure 5A
PMID:36749320	PBO:0109286	Figure 5A
PMID:36749320	PBO:0109287	Figure 5B
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:0093616	Fig. 3
PMID:36793083	PBO:0093581	Fig. 3
PMID:36793083	PBO:0093581	Fig. 3
PMID:36793083	PBO:0093581	Fig. 3
PMID:36793083	PBO:0100810	Fig. 4D
PMID:36793083	PBO:0100811	Fig. 4D
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:0093616	Fig. 3
PMID:36793083	PBO:0093616	Fig. 3
PMID:36793083	PBO:0100813	Fig. 4D
PMID:36793083	PBO:0100812	Fig. 4D
PMID:36793083	PBO:0100812	Fig. 4D
PMID:36793083	PBO:0093616	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:36794724	PBO:0092197	Figure 2
PMID:36794724	FYPO:0008119	Figure 5D ang G
PMID:36794724	FYPO:0008123	Figure 5B
PMID:36794724	PBO:0092197	Figure S4
PMID:36794724	PBO:0092197	Figure S4
PMID:36794724	PBO:0109736	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109737	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109738	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:0092197	Figure S4
PMID:36794724	PBO:0109751	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109750	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109749	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109748	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109747	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109746	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109745	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109744	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:0109762	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:0092197	Figure 2
PMID:36794724	PBO:0092197	Figure 2
PMID:36794724	PBO:0092197	Figure 2
PMID:36794724	FYPO:0008102	Figure 8
PMID:36794724	PBO:0092357	Figure S3
PMID:36794724	PBO:0092357	Figure S3
PMID:36794724	PBO:0092197	Figure 2
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 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: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:0109974	Figure 3A
PMID:36794724	PBO:0101499	Figure 1B
PMID:36794724	PBO:0109734	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109735	Figure 6, 7, 9 and 10
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:0109974	Figure 3C
PMID:36794724	PBO:0092197	Figure 2
PMID:36794724	PBO:0109739	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:0109731	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109732	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109733	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109974	Figure 3B
PMID:36794724	PBO:0109760	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109761	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109759	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109758	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109757	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109740	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:0109763	Figure 6
PMID:36794724	PBO:0109764	Figure 6
PMID:36794724	PBO:0109765	Figure 6
PMID:36794724	PBO:0109766	Figure 6
PMID:36794724	PBO:0109741	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109756	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109755	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109754	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109753	Figure 6, 7, 9 and 10
PMID:36794724	PBO:0109752	Figure 6, 7, 9 and 10
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:0109161	We performed an IP–WB experiment on the bqt4 background (‘bqt4’ 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.3D
PMID:36799444	PBO:0109163	We performed an IP–WB experiment on the bqt4 background (‘bqt4’ 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:0109162	We performed an IP–WB experiment on the bqt4 background (‘bqt4’ 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:0108829	Table 1
PMID:36820394	PBO:0108830	Table 1
PMID:36820394	PBO:0108800	Table 1
PMID:36820394	PBO:0108799	Table 1
PMID:36820394	PBO:0108831	Table 1
PMID:36820394	PBO:0108832	Table 1
PMID:36820394	PBO:0108819	Table 1
PMID:36820394	PBO:0108820	Table 1
PMID:36820394	PBO:0108812	Table 1
PMID:36820394	PBO:0108813	Table 1
PMID:36820394	PBO:0108802	Table 1
PMID:36820394	PBO:0108803	Table 1
PMID:36820394	PBO:0108804	Table 1
PMID:36820394	PBO:0108805	Table 1
PMID:36820394	PBO:0108806	Table 1
PMID:36820394	PBO:0108807	Table 1
PMID:36820394	PBO:0108808	Table 1
PMID:36820394	PBO:0108809	Table 1
PMID:36820394	PBO:0108810	Table 1
PMID:36820394	PBO:0108811	Table 1
PMID:36820394	PBO:0108814	Table 1
PMID:36820394	PBO:0108815	Table 1
PMID:36820394	PBO:0108816	Table 1
PMID:36820394	PBO:0108793	Fig.1
PMID:36820394	PBO:0108791	Table 1
PMID:36820394	PBO:0108795	Table 1
PMID:36820394	PBO:0108796	Table 1
PMID:36820394	PBO:0108798	Table 1
PMID:36820394	PBO:0108797	Table 1
PMID:36820394	PBO:0108793	Fig.1
PMID:36820394	PBO:0108792	Fig.1
PMID:36820394	PBO:0108792	Fig.1
PMID:36820394	PBO:0108827	Table 1
PMID:36820394	PBO:0108826	Table 1
PMID:36820394	PBO:0108825	Table 1
PMID:36820394	PBO:0108792	Fig.1
PMID:36820394	PBO:0108791	Fig.1
PMID:36820394	PBO:0108791	Fig.1
PMID:36820394	PBO:0108824	Table 1
PMID:36820394	PBO:0108823	Table 1
PMID:36820394	PBO:0108822	Table 1
PMID:36820394	PBO:0108792	Table 1
PMID:36820394	PBO:0108793	Table 1
PMID:36820394	PBO:0108794	Table 1
PMID:36820394	PBO:0108828	Table 1
PMID:36820394	PBO:0108817	Table 1
PMID:36820394	PBO:0108821	Table 1
PMID:36820394	PBO:0108818	Table 1
PMID:36820394	PBO:0108793	Fig.1
PMID:36820394	PBO:0108801	Table 1
PMID:36820394	PBO:0108791	Fig.1
PMID:36854376	FYPO:0001357	The mutant strain appears to grow normally (figure 2b). O
PMID:36854376	FYPO:0008215	). O1 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:0099749	Fig. 4
PMID:36882296	FYPO:0002085	Fig. 5A
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	PBO:0094777	Fig. 5B
PMID:36882296	FYPO:0002085	Fig. 6A
PMID:36882296	FYPO:0002085	Fig. 6A
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	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. 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:0094738	Fig. 7B, 10B, 12B
PMID:36882296	FYPO:0002085	Fig. 7A
PMID:36882296	FYPO:0002085	Fig. 7A
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:0000080	Fig. 9A
PMID:36882296	FYPO:0000080	Fig. 9A
PMID:36882296	FYPO:0000080	Fig. 9A
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:0094771	Fig. 1B
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: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	PBO:0108875	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	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:0000080	Fig. 1A
PMID:36882296	PBO:0094771	Fig. 1B
PMID:36882296	PBO:0094771	Fig. 1B
PMID:36882296	PBO:0094771	Fig. 1B
PMID:36882296	FYPO:0002085	Fig. 5A
PMID:36882296	FYPO:0002085	Fig. 5A
PMID:36882296	FYPO:0002061	Fig. 5A
PMID:36882296	FYPO:0002085	Fig. 6A
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:36951094	PBO:0112657	Fig. 5C
PMID:36951094	PBO:0112661	Fig. 3C
PMID:36951094	PBO:0112659	Fig. 2D
PMID:36951094	PBO:0112661	Fig. 3C
PMID:36951094	PBO:0112657	Fig. 6C
PMID:36951094	PBO:0112307	Fig. 6C
PMID:36951094	GO:0007534	we demonstrated that the Swi2-Swi5 complex promotes Rad51-driven strand invasion in vitro
PMID:36951094	PBO:0112662	Fig. 3C
PMID:36951094	PBO:0112665	the AT-hook motifs were required for the mat3-M donor choice.
PMID:36951094	GO:0007535	we demonstrated that the Swi2-Swi5 complex promotes Rad51-driven strand invasion in vitro
PMID:36951094	PBO:0112308	Fig. 5C
PMID:36951094	PBO:0112308	Fig. 5C
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	FYPO:0000468	Fig. 5B
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	PBO:0112663	Fig. 6A
PMID:36951094	PBO:0112663	Fig. 6A
PMID:36951094	GO:0007534	we demonstrated that the Swi2-Swi5 complex promotes Rad51-driven strand invasion in vitro
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	PBO:0112308	Fig. 5C
PMID:36951094	PBO:0112308	Fig. 6C
PMID:36951094	PBO:0112657	Fig. 5B and 5C
PMID:37039135	PBO:0114612	Fig. 4
PMID:37039135	PBO:0114611	Fig. 3
PMID:37039135	PBO:0114611	Fig. 4
PMID:37039135	PBO:0018611	we observed Cdc42 activation in early anaphase, at the time of ring assembly. Fig. 2
PMID:37039135	FYPO:0003250	Fig. 7
PMID:37039135	PBO:0114617	Fig. S4A
PMID:37039135	PBO:0114618	Fig. S4A
PMID:37039135	PBO:0114618	Fig. S4A
PMID:37039135	PBO:0114611	Fig. 6D
PMID:37039135	PBO:0114612	Fig. 6D
PMID:37039135	PBO:0114612	Fig. 6
PMID:37039135	PBO:0114616	Fig. 6
PMID:37039135	PBO:0114611	Fig. 5D
PMID:37039135	PBO:0114612	Fig. 5D
PMID:37039135	FYPO:0001357	Fig. 5A
PMID:37039135	PBO:0114617	Fig. S4A
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 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:0114612	Fig. S4
PMID:37039135	PBO:0114612	Fig. S4
PMID:37039135	PBO:0114613	Fig. S5
PMID:37039135	PBO:0114613	Fig. S5
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	PBO:0114614	Fig. S7D
PMID:37039135	PBO:0114612	Fig. 6D and Fig. S7F
PMID:37039135	PBO:0114611	Fig. 6D and Fig. S7F
PMID:37039135	PBO:0114612	Fig. 7
PMID:37039135	PBO:0114615	Fig. S7C
PMID:37039135	PBO:0093560	Fig. 5A
PMID:37039135	FYPO:0001357	Fig. 5A
PMID:37039135	FYPO:0001357	Fig. 5A
PMID:37039135	FYPO:0001357	Fig. 5A
PMID:37052630	PBO:0093570	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	Main text Table S1
PMID:37052630	PBO:0093564	Main text Table S1
PMID:37052630	PBO:0093564	Fig. 2b - control
PMID:37052630	PBO:0109067	Fig. 2b - control is the overexpressed pka1D with overexpressed wild-type (nmt81)
PMID:37052630	PBO:0109067	Fig. 2b - control is the overexpressed pka1D with overexpressed wild-type (nmt81)
PMID:37052630	PBO:0097264	Fig. 2b - control is the overexpressed pka1D with overexpressed wild-type (nmt81)
PMID:37052630	PBO:0097264	Fig. 2b - control is the overexpressed pka1D with overexpressed wild-type (nmt81)
PMID:37052630	PBO:0097264	Fig. 2b - control is the overexpressed pka1D with overexpressed wild-type (nmt81)
PMID:37052630	PBO:0097264	Fig. 2b - control is the overexpressed pka1D with overexpressed wild-type (nmt81)
PMID:37052630	PBO:0093564	Main text Table S1
PMID:37052630	PBO:0107560	Fig. S1
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: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:0032221	Figure 3.
PMID:37099380	FYPO:0006338	Closer to tip
PMID:37099380	FYPO:0009106	Closer to ring
PMID:37099380	FYPO:0006338	Closer to tip
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: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: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: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	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: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	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	GO:0140602	Localization depends on Cdc2 kinase activity but not on Clp1.
PMID:37128864	PBO:0102449	The phenotype can be seen at 32 degree.
PMID:37156397	FYPO:0002061	Figs. 2B, S1B
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	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	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	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	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	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	LC-MS analysis
PMID:37156397	GO:0006744	low CoQ10 level
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	FYPO:0002061	Figs. 2B, S1B
PMID:37156397	FYPO:0002061	Figs. 2B, S1B
PMID:37156397	FYPO:0002061	Figs. 2B, S1B
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:37158439	FYPO:0000674	Figure S2
PMID:37158439	FYPO:0000082	Figure 4D
PMID:37158439	FYPO:0000082	Figure 4D
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 S3
PMID:37158439	FYPO:0004481	Figure S3
PMID:37158439	FYPO:0000202	Figure 1E and G
PMID:37158439	FYPO:0007774	Figure 4C
PMID:37158439	FYPO:0000674	Figure 3C
PMID:37158439	FYPO:0004481	Figure 3C
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 S2
PMID:37158439	FYPO:0004481	Figure 3B
PMID:37158439	FYPO:0000202	Figure 1E and G
PMID:37158439	FYPO:0004481	Figure 3B
PMID:37158439	FYPO:0003532	Figure 4A
PMID:37158439	FYPO:0005905	Figure 1 E and G
PMID:37158439	FYPO:0005905	Figure 1E and G
PMID:37158439	FYPO:0008090	Figure 1
PMID:37158439	FYPO:0008090	Figure 1
PMID:37158439	FYPO:0008090	Figure 1
PMID:37158439	FYPO:0008090	Figure 2
PMID:37158439	FYPO:0006879	Figure 2
PMID:37158439	FYPO:0001760	Figure 2
PMID:37158439	PBO:0109256	Figure 2
PMID:37158439	FYPO:0000639	Figure 2 Fig. 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 Fig. 2. fic1-2A myo2-E1 cells can achieve membrane ingression and cell separation at myo2-E1’s restrictive temperature
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:0007774	Figure 4C
PMID:37158439	FYPO:0007774	Figure 4C
PMID:37158439	FYPO:0007774	Figure 4C
PMID:37158439	FYPO:0007774	Figure 4C
PMID:37158439	FYPO:0000674	Figure 4D
PMID:37158439	FYPO:0007774	Figure 4C
PMID:37158439	FYPO:0000674	Figure S2
PMID:37158439	FYPO:0000674	Figure S3
PMID:37158439	FYPO:0004481	Figure S2
PMID:37158439	FYPO:0003532	Figure 4A
PMID:37158439	FYPO:0000674	Figure S3
PMID:37158439	FYPO:0000674	Figure S3
PMID:37158439	FYPO:0004481	Figure S3
PMID:37158439	FYPO:0000082	Figure S1
PMID:37158439	FYPO:0000082	Figure S1
PMID:37158439	FYPO:0000674	Figure S1
PMID:37158439	FYPO:0000674	Figure S1
PMID:37158439	FYPO:0000674	Figure S1
PMID:37158439	FYPO:0000674	Figure S1
PMID:37158439	FYPO:0000080	Figure S1
PMID:37158439	FYPO:0000674	Figure S3
PMID:37158439	FYPO:0004481	Figure 3C
PMID:37158439	PBO:0109255	Figure 1B
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	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:0008090	Figure 1
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 1C
PMID:37158439	FYPO:0004481	Figure 1C
PMID:37160462	PBO:0109839	Phenotype complementation by human RAD23A
PMID:37162093	FYPO:0002058	Figure 4BD
PMID:37162093	FYPO:0002058	Figure 4BD
PMID:37162093	FYPO:0001420	Figure 4BD, Figure 6BDE
PMID:37162093	FYPO:0002058	Figure S2
PMID:37162093	FYPO:0002058	Figure S2
PMID:37162093	FYPO:0001420	Figure 6BDE, Figure S2
PMID:37162093	PBO:0093560	Figure 3AD, Figure 6ACE
PMID:37162093	FYPO:0002104	Figure 7
PMID:37162093	FYPO:0002104	Figure 7
PMID:37162093	FYPO:0002273	Figure 7
PMID:37162093	FYPO:0002058	Figure 5AB
PMID:37162093	FYPO:0002058	Figure 5AB
PMID:37162093	FYPO:0002058	Figure 4AC
PMID:37162093	PBO:0093561	Figure 3BE, Figure 6ACE
PMID:37162093	FYPO:0002105	Figure 7
PMID:37162093	PBO:0093559	Figure 3CF, Figure 6ACE
PMID:37162093	FYPO:0000017	Figure 7
PMID:37162093	FYPO:0002104	Figure 7
PMID:37162093	FYPO:0001420	Figure 5AB, Figure S3
PMID:37162093	PBO:0093561	Figure 4AC, Figure 6BDE
PMID:37162093	FYPO:0002058	Figure 4AC
PMID:37164017	PBO:0093559	Growth rate improved by addition of either glutamate, glutamine, or arginine
PMID:37164017	PBO:0093559	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 non- respiring 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 fuma- rate likely originates from the reductive TCA branch52,57–59 (Fig- ure 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 as- sessed 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 as- sessed 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 as- sessed 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 as- sessed 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 as- sessed 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 as- sessed 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 as- sessed 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 as- sessed 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	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 (Fig- ure 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	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 (Fig- ure 1A).
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	Growth rate improved by addition of either glutamate, glutamine, or arginine
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	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	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: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	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:0005783	Consistently, Hva22 was observed on the ER under both nitrogen-rich and starvation conditions (Figure 3C).
PMID:37191320	PBO:0104254	In hva22Δ cells, reticulophagy was abolished, similar to cells lacking the core autophagy protein Atg1 (Figure 1B).
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: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: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	FYPO:0007594	In atg44D cells, mitophagy was completely blocked similarly to cells lacking Atg1, a core autophagy protein (Figures 1A and S1B).
PMID:37192628	GO:0005758	Based on these results, we conclude that Atg44 localizes in the IMS and is not a transmembrane protein.
PMID:37192628	PBO:0109196	Unexpectedly, wenoticed 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: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	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 fragmentedand mitophagy was partially rescued (Figures 4A and S3F).
PMID:37192628	PBO:0109197	As expected, in S. pombe atg44D cellslacking Mgm1, some of the mitochondria became fragmentedand 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: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:0109424	Fig. 2
PMID:37200372	PBO:0109421	Fig. 6
PMID:37200372	PBO:0109421	Fig. 6
PMID:37200372	PBO:0109424	Fig. 2
PMID:37200372	PBO:0100985	Fig. S12
PMID:37200372	PBO:0109428	Fig. S12
PMID:37200372	PBO:0109429	Fig. S12
PMID:37200372	PBO:0109430	Fig. S12
PMID:37200372	PBO:0109430	Fig. S12
PMID:37200372	FYPO:0000268	Fig. 7
PMID:37200372	PBO:0093629	Fig. 7
PMID:37200372	FYPO:0000268	Fig. 7
PMID:37200372	FYPO:0000085	Fig. 7
PMID:37200372	FYPO:0000085	Fig. 7
PMID:37200372	PBO:0093613	Fig. 7
PMID:37200372	PBO:0093587	Fig. 7
PMID:37200372	PBO:0093587	Fig. 7
PMID:37200372	PBO:0093613	Fig. 7
PMID:37200372	PBO:0109424	Fig. 2
PMID:37200372	PBO:0109427	Fig. 6
PMID:37200372	PBO:0093587	Fig. 7
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: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:37200372	PBO:0109417	Fig. 1
PMID:37200372	FYPO:0002061	Fig. S2 and text
PMID:37200372	FYPO:0002061	Fig. S2 and text
PMID:37200372	FYPO:0002060	Fig. S2 and text
PMID:37200372	FYPO:0001355	Fig. S2 and text
PMID:37200372	FYPO:0000088	Fig. 6
PMID:37200372	FYPO:0000089	Fig. 6
PMID:37200372	PBO:0109425	Fig. 6B
PMID:37200372	FYPO:0000089	Fig. 6
PMID:37200372	PBO:0109412	Fig. 6B
PMID:37200372	FYPO:0000088	Fig. 6
PMID:37200372	PBO:0109414	Fig. 6
PMID:37200372	PBO:0109414	Fig. 6
PMID:37200372	PBO:0109418	Fig. 6
PMID:37200372	PBO:0109419	Fig. 6
PMID:37200372	PBO:0109426	Fig. 6
PMID:37200372	PBO:0109426	Fig. 6
PMID:37200372	PBO:0109427	Fig. 6
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	FYPO:0006437	Normal Chk1 phosphorylation and cell cycle arrest
PMID:37237082	PBO:0096838	srr1-W157R and rad52-R45K or pcn1-K107R additively reduce gross chromosomal rearrangement. srr1-W157R and pcn1-K107R also addi- tively 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 addi- tively reduced GCR rates in rad51Δ cells (Fig. 4a).
PMID:37237082	PBO:0093618	figure 3a
PMID:37237082	PBO:0093579	figure 3a
PMID:37237082	PBO:0093615	figure 3a
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:0093618	figure 5e
PMID:37237082	PBO:0093579	figure 5e
PMID:37237082	PBO:0093615	figure 5e
PMID:37237082	PBO:0093618	figure 5e
PMID:37237082	PBO:0093579	figure 5e
PMID:37237082	PBO:0093615	figure 5e
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:0096839	Fig. 6A
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:0096839	Fig. 6A
PMID:37237082	FYPO:0005371	(Fig. 3e).
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	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: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	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	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: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 3a
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	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	FYPO:0005371	(Fig. 3e).
PMID:37237082	PBO:0096839	Fig. 6A
PMID:37237082	PBO:0096839	Fig. 6A
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:0001690	figure 3a
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: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: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:0109208	Figure 2
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:37288768	PBO:0110058	Fig 2E
PMID:37288768	PBO:0110298	Fig 1B
PMID:37288768	FYPO:0000886	Fig 4A, S3
PMID:37288768	FYPO:0000891	Fig 4A, S2
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	PBO:0019232	Fig 3
PMID:37288768	PBO:0019232	Fig 3
PMID:37288768	PBO:0019031	Fig 3
PMID:37288768	PBO:0110055	Fig 1B
PMID:37288768	PBO:0019031	Fig 3
PMID:37288768	PBO:0110056	Fig 4C
PMID:37288768	PBO:0110057	Fig 2G
PMID:37288768	PBO:0019031	Fig 3
PMID:37288768	PBO:0110059	Fig 4D
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:37400983	PBO:0109932	The hinge and the N-terminal disor- dered regions of Chp2 (Chp2-H and Chp2-N) also bound DNA (Fig. 2H, J and M)
PMID:37400983	FYPO:0002336	mat3M::ura4+ reporter silencing
PMID:37400983	FYPO:0002336	mat3M::ura4+ reporter silencing
PMID:37400983	FYPO:0002827	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: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	mat3M::ura4+ reporter silencing
PMID:37400983	FYPO:0002827	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	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	Interest- ingly, 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	****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 disor- dered 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	Inter- estingly, 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	PBO:0109934	exhibited only a very weak DNA binding activity compared to wild- type Chp2-CD (Chp2-CSDWT ) (Fig. 3D and E, and Supple- mentary 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 Sup- plementary 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	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, Sup- plementary Figure S3).
PMID:37403782	FYPO:0008110	reproducible decrease in modification at several other sites, most notably A64 (Figure 1C, D, Sup- plementary Figure S3).
PMID:37403782	FYPO:0008110	reproducible decrease in modification at several other sites, most notably A64 (Figure 1C, D, Sup- plementary 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 in- crease 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, dis- played a statistically significant increase upon Bmc1 dele- tion at 32 ̊C in our RNA Seq dataset).
PMID:37403782	PBO:0112458	Bmc1 5 capping catalytic activity is not required for promoting 2 -O-methylation of U6
PMID:37403782	FYPO:0008113	Still, as mean intron retention values indeed showed an in- crease 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, dis- played a statistically significant increase upon Bmc1 dele- tion at 32 ̊C in our RNA Seq dataset).
PMID:37403782	PBO:0109669	Still, as mean intron retention values indeed showed an in- crease 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, dis- played a statistically significant increase upon Bmc1 dele- tion at 32 ̊C in our RNA Seq dataset).
PMID:37403782	GO:0016180	U6
PMID:37403782	GO:0016180	U6
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 neces- sary for an interaction with U6 (Figure 1A, Supplemen- tary Figure S1B).
PMID:37403782	GO:0005732	we found that all three proteins are neces- sary for an interaction with U6 (Figure 1A, Supplemen- tary 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 Fig- ure S1C).
PMID:37403782	PBO:0109446	Further support- ing 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	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 Fig- ure S1C).
PMID:37403782	GO:0005732	we found that all three proteins are neces- sary for an interaction with U6 (Figure 1A, Supplemen- tary Figure S1B).
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	GO:0016180	U6
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: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 com- plex (Figure 1A).
PMID:37403782	PBO:0109446	Further support- ing 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 support- ing 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: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
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PMID:37445861	PBO:0093786	Fig. 1
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PMID:37445861	PBO:0093786	Fig. 1
PMID:37445861	PBO:0093786	Fig. 1
PMID:37445861	PBO:0093786	Fig. 1
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PMID:37445861	PBO:0093785	Fig. 1
PMID:37445861	PBO:0093785	Fig. 1
PMID:37445861	FYPO:0001986	Fig. 1
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PMID:37445861	FYPO:0001986	Fig. 1
PMID:37445861	FYPO:0001986	Fig. 1
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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
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PMID:37445861	PBO:0093785	Fig. S2
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
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PMID:37445861	PBO:0093786	Fig. 2
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PMID:37445861	PBO:0093785	Fig. 3
PMID:37445861	PBO:0093785	Fig. 3
PMID:37445861	PBO:0093786	Fig. 3
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:0112316	Fig. 4
PMID:37445861	PBO:0112317	Fig. 5
PMID:37445861	PBO:0112317	Fig. 5
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	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
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PMID:37445861	PBO:0093785	Fig. 2
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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	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	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: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:0093786	Fig. 1
PMID:37445861	PBO:0093786	Fig. 1
PMID:37445861	PBO:0093786	Fig. 1
PMID:37445861	PBO:0093786	Fig. 1
PMID:37445861	PBO:0093564	Fig. S4
PMID:37445861	PBO:0093785	Fig. 1
PMID:37445861	PBO:0093786	Fig. 1
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PMID:37445861	PBO:0093564	Fig. S4
PMID:37445861	PBO:0093564	Fig. S4
PMID:37445861	PBO:0093564	Fig. S4
PMID:37445861	PBO:0093786	Fig. 1
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PMID:37445861	PBO:0093786	Fig. 1
PMID:37445861	FYPO:0001986	Fig. 1
PMID:37445861	PBO:0093564	Fig. S4
PMID:37445861	FYPO:0000964	Fig. S4
PMID:37445861	FYPO:0000964	Fig. S4
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
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PMID:37445861	FYPO:0000964	Fig. S3
PMID:37445861	FYPO:0000964	Fig. S3
PMID:37445861	PBO:0093786	Fig. 2
PMID:37445861	FYPO:0007035	Fig. 3
PMID:37445861	FYPO:0007035	Fig. 3
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:37459529	GO:0034739	assayed complex
PMID:37459529	GO:0180032	assayed complex
PMID:37459529	GO:0180033	assayed complex
PMID:37459529	GO:0140937	assayed complex
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:0032221	Alp13b is connected to the complex by both Cph1 and Cph2 (Figs. 2C and 3A)
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: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	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:37531259	GO:0061645	Figure 1C &F
PMID:37531259	PBO:0109530	Figure S1A
PMID:37531259	GO:0008289	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:0109539	Figure 1C
PMID:37531259	GO:0051285	Figure 1C
PMID:37531259	GO:0051285	Figure 1C
PMID:37531259	FYPO:0001357	Figure S1D (vw: same pathway)
PMID:37531259	FYPO:0004085	Figure S1D
PMID:37531259	FYPO:0004085	Figure S1D
PMID:37531259	FYPO:0004085	Figure S1D
PMID:37531259	FYPO:0004085	Figure S1D
PMID:37531259	PBO:0109538	Figure 1E
PMID:37531259	PBO:0109538	Figure 1E
PMID:37531259	PBO:0109537	Figure 3A
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	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:0109534	Figure 3C
PMID:37531259	PBO:0109524	Figure 3E
PMID:37531259	PBO:0109524	Figure 3E
PMID:37531259	PBO:0109533	Figure 3C
PMID:37531259	PBO:0109532	Fig. 1, Fig. 1B, Fig. 2D
PMID:37531259	PBO:0109531	Figure S1B
PMID:37531259	FYPO:0000744	Figure S1C
PMID:37531259	PBO:0109529	Figure S1C
PMID:37531259	FYPO:0001366	Figure 1C
PMID:37531259	PBO:0109528	Figure 1C
PMID:37531259	PBO:0109527	Figure 1C
PMID:37531259	PBO:0109526	Figure 1C
PMID:37531259	PBO:0109525	Figure 1C
PMID:37531259	PBO:0109524	Figure 1D
PMID:37531259	GO:0005737	Figure 1F
PMID:37540145	PBO:0109719	Figure 4F mitochondrial net-like morphology
PMID:37540145	PBO:0109593	Figure 4G
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: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:37540145	PBO:0109596	Figure 4G
PMID:37540145	PBO:0109720	Figure 4F mitochondrial net-like morphology
PMID:37550452	PBO:0109824	Extended Data Figure 9e
PMID:37550452	PBO:0108475	Figure 6
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:0112254	Fig. 1B and C
PMID:37553386	FYPO:0000355	Fig. S2D
PMID:37553386	FYPO:0001357	Fig. 1F
PMID:37553386	FYPO:0001357	Fig. 1F
PMID:37553386	FYPO:0007448	Fig. 1B and C
PMID:37553386	PBO:0112256	Fig. 1F
PMID:37553386	PBO:0112252	Fig. 6
PMID:37553386	FYPO:0001357	Fig. 1F
PMID:37553386	FYPO:0001030	Fig. 1F
PMID:37553386	PBO:0112265	Fig. 5B
PMID:37553386	PBO:0112264	Fig. 5B
PMID:37553386	FYPO:0001030	Fig. 1F
PMID:37553386	PBO:0112256	Fig. 1F
PMID:37553386	PBO:0112256	Fig. 1F
PMID:37553386	FYPO:0001357	Fig. 1F
PMID:37553386	PBO:0112263	Fig. 5B
PMID:37553386	PBO:0112263	Fig. 5B
PMID:37553386	FYPO:0001357	Fig. 1F
PMID:37553386	PBO:0112259	Fig. 2C
PMID:37553386	PBO:0112258	Fig. S2G and H
PMID:37553386	PBO:0112257	Fig. 1G
PMID:37553386	PBO:0112256	Fig. 5A
PMID:37553386	PBO:0112262	Fig. 5A
PMID:37553386	PBO:0112256	Fig. 5A
PMID:37553386	PBO:0102947	Fig. 5A
PMID:37553386	PBO:0102947	Fig. 5A
PMID:37553386	PBO:0112261	Fig. 3G
PMID:37553386	FYPO:0001030	Fig. 5A
PMID:37553386	FYPO:0001030	Fig. 5A
PMID:37553386	FYPO:0001030	Fig. 5A
PMID:37553386	PBO:0112258	Fig. S2G and H
PMID:37553386	PBO:0112260	Fig. 2C
PMID:37553386	PBO:0112248	Assayed using S. japonicus rop1 in vitro. Fig. 4
PMID:37553386	FYPO:0000381	Fig. 1D and E
PMID:37553386	PBO:0112250	Assayed using S. japonicus yop1 in vitro. Fig. 4
PMID:37553386	PBO:0112251	Fig. 1B
PMID:37553386	PBO:0112252	Fig. 6
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:0112255	Fig. 1B and C
PMID:37553386	PBO:0112257	Fig. 1G
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	FYPO:0000544	Sty1-Tpx1 disulfide formation abrogated (Figure S1C).
PMID:37572670	PBO:0111037	Crucially, both Sty1-Tpx1 fu- sions were expressed at similar levels to wild-type Sty1 and sup- ported 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 cys- teines in Sty1 are required for Sty1 function independently from forming disulfide-bonded complexes with Tpx1 (Figures 1B and S1F).39
PMID:37572670	PBO:0095350	Tpx1 is required for H2O2-induced activa- tion 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:0111043	We observed a small, but reproducible, stress-induced decrease in Wis1DD mobility in these cells, corroborating that Wis1 undergoes a stress- induced phosphorylation on different sites from those phosphor- ylated by the MAP3K (Figures 4A, S5A, S4A, S4B, and S4F).
PMID:37572670	PBO:0111044	Significantly, this stress-induced increase in Wis1DD phosphory- lation was mirrored by stress-induced increases in Sty1 phos- phorylation, strongly suggesting that it increases Wis1 activity (Figure 4A).
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 phosphory- lation 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 phosphory- lation 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:0005947	Sty15CS-expressing cells were able to adapt to os- motic stress but were less tolerant than wild-type cells to higher levels of H2O2 (Figure 1B).
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 (Fig- ure 2A)
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 ex- pressing 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: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: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 pro- mitotic function was compromised (Figures S1D and S1E).
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-ex- pressed. Indeed, analysis of colonies bearing markers of both al- leles revealed that surviving cells had completely eliminated Sty1-Tpx1 expression and activity (Figures 2J and 2K and not shown).
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-ex- pressed. Indeed, analysis of colonies bearing markers of both al- leles 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 mo- bile forms even in the absence of stress (Figures 3A and 3D).
PMID:37572670	FYPO:0001122	Indeed, our exam- ination indicated that ‘‘sty1-tpx1 wis1DD’’ strains, which genotyp- ically 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	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	PBO:0111038	By contrast, cells expressing Sty1-Tpx1C48S con- tained substantially increased levels of lower mobility and phos- phorylated 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	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 phos- phorylation in Dtrx1 mutant cells, where H2O2-induced Pyp1 disul- fides were not detected (Figures 2D and 2F).
PMID:37572670	PBO:0111041	By contrast, over- expression of Tpx1 increased H2O2-induced Sty1 phosphoryla- tion in wild-type cells and also restored some H2O2-inducibility to Sty1 phosphorylation in Dpyp2 cells (Figures 2A and S3E).
PMID:37572670	PBO:0111040	By contrast, over- expression of Tpx1 increased H2O2-induced Sty1 phosphoryla- tion in wild-type cells and also restored some H2O2-inducibility to Sty1 phosphorylation in Dpyp2 cells (Figures 2A and S3E).
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 ex- pressing either Sty1-Tpx1 or Sty1-Tpx1C48S (Figure 1D)
PMID:37572670	PBO:0093578	Sty15CS-expressing cells were able to adapt to os- motic stress but were less tolerant than wild-type cells to higher levels of H2O2 (Figure 1B).
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 mito- chondrial morphology.
PMID:37590302	FYPO:0000895	Yta4(EQ) impaired the for- mation 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: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	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:0003810	Figure 1
PMID:37590302	FYPO:0007194	Figure 1
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 activ- ity 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	PBO:0109729	Hence, these results show the character- istic property of Yta4 in reducing the affinity of Dnm1 for GTP and in inhibiting Dnm1 assembly.
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: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	PBO:0093617	Fig. 2-S1A
PMID:37615341	FYPO:0000963	Fig. 2-S1A
PMID:37615341	FYPO:0000963	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:0001357	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: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: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:0002061	Figure 1D
PMID:37637271	FYPO:0002061	Figure 1D
PMID:37637271	PBO:0093563	Figure 1H
PMID:37637271	FYPO:0000964	Figure 1H
PMID:37637271	PBO:0093563	Figure 1H
PMID:37637271	FYPO:0000964	Figure 1H
PMID:37637271	FYPO:0001235	Figure 1E
PMID:37637271	FYPO:0001235	Figure 1E
PMID:37694715	PBO:0110248	Fig5C and 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	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 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:0093554	Fig5B
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: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: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: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: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: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: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	GO:0016020	Bqt4 is an integral membrane protein
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: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	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: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	PBO:0110248	GFP–Bqt4 fluorescence in the nuclei of both bqt3+ and bqt3Δ cells was elevated (Fig. 1A)
PMID:37694715	PBO:0110248	Fig S1.
PMID:37694715	PBO:0110248	We confirmed it by microscopy as well. Fig 1C 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:37723847	FYPO:0002061	Interestingly, the internal transmem- brane region was sufficient to induce both CDRE activa- tion and growth inhibition (Figure 1a,d).
PMID:37723847	FYPO:0002061	Overexpression of either construct inhibited the growth like full length (Figure 1d), indicating that each of them is capa- ble 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 capa- ble of inducing cytotoxicity upon overexpression.
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	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:0002060	Figure 3b,tetrad analysis
PMID:37723847	FYPO:0002061	Figure 3b, tetrad analysis
PMID:37723847	GO:0031520	localized to the septum and the plasma membrane, especially enriched at cell tips (Figure 2d).
PMID:37723847	GO:0000935	localized to the septum and the plasma membrane, especially enriched at cell tips (Figure 2d).
PMID:37723847	PBO:0110118	Localizations of Pkd2ΔN170, Pkd2ΔC577, or Pkd2TM were identical to full length Pkd2 (Figures 2b and S2A).
PMID:37723847	FYPO:0002061	Although the CDRE signal is disap- peared (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	GO:0005783	full length of Pkd2 (GFP-Pkd2) colocalized with Pmr1, a marker for the ER (Nakazawa et al., 2019),
PMID:37723847	PBO:0110120	whereas C-terminus of Pkd2 (Pkd2C) displayed a uniform cytoplasmic pattern (Figures 2b and S2A).
PMID:37723847	PBO:0110119	N-terminus of Pkd2 (Pkd2N) localized to the cytoplasm and slightly to the ER,
PMID:37723847	FYPO:0002061	In accordance with previous observation, the colony did not form under the inducible condition of pkd2+ overexpres- sion (Figure 1b).
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:37746062	PBO:0110025	Figure1 G-H
PMID:37746062	PBO:0110026	Figure1 G-H
PMID:37746062	PBO:0110026	Figure1 G-H
PMID:37746062	PBO:0110026	Figure 1G-H
PMID:37772819	PBO:0108806	Table S3
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:37772819	FYPO:0000080	Fig. 9
PMID:37772819	FYPO:0000080	Fig. 8
PMID:37772819	FYPO:0001357	Fig. 8
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	PBO:0110078	Table S3
PMID:37772819	PBO:0110077	Table S3
PMID:37772819	FYPO:0008134	Fig. S1.
PMID:37772819	FYPO:0005485	Fig. 5
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	GO:0004309	Fig. 4
PMID:37772819	GO:0052843	Figs. 5 and 6
PMID:37772819	GO:0052845	Figs. 5 and 6
PMID:37772819	FYPO:0004303	Fig. 1B
PMID:37772819	FYPO:0004303	Fig. 1B
PMID:37772819	FYPO:0004469	para-nitrophenylphosphatase activity (Figs. 1B and 2B)
PMID:37772819	FYPO:0001357	Fig. 8
PMID:37772819	FYPO:0001357	Fig. 9
PMID:37772819	FYPO:0001357	Fig. 9
PMID:37772819	FYPO:0001357	Fig. 9
PMID:37772819	PBO:0108850	Table S3
PMID:37772819	PBO:0108804	Table S3
PMID:37772819	PBO:0108808	Table S3
PMID:37772819	PBO:0108810	Table S3
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. 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:0002061	Fig. 7
PMID:37772819	FYPO:0002061	Fig. 7
PMID:37772819	PBO:0110079	Table S3
PMID:37772819	PBO:0108800	Table S3
PMID:37783794	FYPO:0001355	Extended Data Fig. 4
PMID:37783794	PBO:0092114	25 ± 10 molecules at the spindle pole body | Fig. 2
PMID:37783794	PBO:0092114	77 ± 51 molecules at the spindle pole body | Fig. 2
PMID:37783794	PBO:0092114	30 ± 17 molecules at the spindle pole body | Fig. 2
PMID:37783794	PBO:0110098	25 ± 13 molecules at the spindle pole body | Fig. 2
PMID:37783794	PBO:0092114	69 ± 37 molecules at the spindle pole body | Fig. 2
PMID:37783794	PBO:0110098	75 ± 45 molecules at the spindle pole body | Fig. 2
PMID:37783794	PBO:0092114	15 ± 8 molecules at the spindle pole body | Fig. 2
PMID:37783794	PBO:0110098	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	Puncta | Likely endosomes/MVBs | Extended Data Fig. 1A,B
PMID:37783794	PBO:0110439	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	PBO:0110439	Fig. 1B–D
PMID:37783794	PBO:0110438	Fig. 1B–D
PMID:37783794	PBO:0110438	Fig. 1B–D
PMID:37783794	PBO:0110438	Fig. 1B–D
PMID:37783794	FYPO:0004429	mCherry-Atb2 | 1 h 5IAA | Extended Data Fig. 5H
PMID:37783794	FYPO:0004429	mCherry-Atb2 | 1 h 5IAA | Extended Data Fig. 5H
PMID:37783794	FYPO:0004429	mCherry-Atb2 | 1 h 5IAA | Extended Data Fig. 5G
PMID:37783794	FYPO:0004429	mCherry-Atb2 | 1 h 5IAA | Extended Data Fig. 5G
PMID:37783794	FYPO:0005695	mCherry-Atb2 | Extended Data Fig. 5H
PMID:37783794	PBO:0024258	mCherry-Atb2 | 3 h 5IAA | Extended Data Fig. 5I
PMID:37783794	FYPO:0005695	mCherry-Atb2 | 1 h 5IAA | Extended Data Fig. 5G
PMID:37783794	FYPO:0008126	MGM4 reporter | ±5IAA | Extended Data Fig. 5E,F
PMID:37783794	FYPO:0008126	MGM4 reporter | ±5IAA | Extended Data Fig. 5E,F
PMID:37783794	FYPO:0008126	MGM4 reporter | 1 h 5IAA | Extended Data Fig. 5E,F
PMID:37783794	PBO:0110093	MGM4 reporter | ±5IAA | Extended Data Fig. 5B,C
PMID:37783794	PBO:0110093	MGM4 reporter | ±5IAA | Extended Data Fig. 5B,C
PMID:37783794	FYPO:0008126	MGM4 reporter | 1 h 5IAA | Extended Data Fig. B,C
PMID:37783794	PBO:0110080	1 h 5IAA | Extended Data Fig. 3C
PMID:37783794	FYPO:0008127	Fig. 7G
PMID:37783794	FYPO:0008127	Fig. 7G
PMID:37783794	FYPO:0008126	MGM4 reporter | Fig. 7C–E
PMID:37783794	FYPO:0008126	MGM4 reporter | Fig. 7C–E
PMID:37783794	FYPO:0008126	MGM4 reporter | Fig. 7C,D
PMID:37783794	FYPO:0008126	MGM4 reporter | 1 h 5IAA | 2.5% 1,6-HD | Fig. 6B–I
PMID:37783794	FYPO:0008124	Fig. 4E–H
PMID:37783794	PBO:0110085	Fig. 3A,B
PMID:37783794	PBO:0110092	Fig. 3A,B
PMID:37783794	PBO:0110091	******** Fig. 3I decreased protein localization to spindle pole body during G1/S
PMID:37783794	PBO:0112754	Fig. 3I
PMID:37783794	PBO:0110089	Fig. 3H–J (vw: into G2)
PMID:37783794	PBO:0110090	*********** Fig. 3G decreased protein localization to spindle pole body during G1/S
PMID:37783794	PBO:0110089	Fig. 3F,G (vw: into G2)
PMID:37783794	PBO:0110088	Fig. 3D
PMID:37783794	PBO:0110087	Fig. 3D
PMID:37783794	PBO:0110086	Fig. 3D
PMID:37783794	PBO:0110085	Fig. 3D
PMID:37783794	PBO:0110084	Fig. 3E
PMID:37783794	PBO:0110083	Fig. 3C
PMID:37783794	PBO:0110082	Fig. 3C
PMID:37783794	PBO:0110081	Fig. 3C
PMID:37783794	PBO:0110080	Fig. 3C
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:0002141	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: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:0002061	Lethality determined by tetrad dissection
PMID:37783794	FYPO:0002061	Lethality determined by tetrad dissection
PMID:37787465	PBO:0112708	Fig. 4C and D
PMID:37787465	PBO:0112811	Fig. 5B
PMID:37787465	PBO:0112810	Fig. 5B
PMID:37787465	FYPO:0004166	Fig. 5A
PMID:37787465	PBO:0112709	Fig. 4F and G
PMID:37787465	FYPO:0002780	Fig. 5C and D
PMID:37787465	FYPO:0002780	Fig. 5C and D
PMID:37787465	FYPO:0008213	Fig. 2J
PMID:37787465	PBO:0112771	Fig. 1I and J
PMID:37787465	PBO:0112772	Fig. 1C and D
PMID:37787465	PBO:0112705	Fig. 5E and F
PMID:37787465	PBO:0112702	Table 1
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: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	PBO:0112707	Fig. 3C and D
PMID:37788281	GO:0005654	exclusion from nucleoplasm is delayed in rad24 deletion background
PMID:37788281	PBO:0099115	by expression of rad24-E185K
PMID:37788281	GO:0005654	in sam3 mutant
PMID:37788281	FYPO:0001864	dominat negative
PMID:37788281	PBO:0092097	in sam3 mutant
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:0005803	assayed using FRAP
PMID:37792890	FYPO:0000135	using GFP-D4H biosensor
PMID:37792890	FYPO:0000135	Using GFP-D4H biosensor
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:0001357	Indeed, we isolated a cold-sensitive mutant of cut6, cut6-1, as a strong suppressor of css1-3 (S3A Fig).
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	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 wildtype 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:37805140	PBO:0110226	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: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:0110215	These northern blots supported the expected subcellular targeting of the Trm1 isoforms: M24 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
PMID:37805140	PBO:0110215	These northern blots supported the expected subcellular targeting of the Trm1 isoforms: M24 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
PMID:37805140	PBO:0110222	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:0110223	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:0110224	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:0110225	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:0110299	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:0110227	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:0000257	normal stop codon readthrough
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	FYPO:0006627	GFP-2xPH(Plc) biosensor
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 wildtype 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	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	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 wildtype cells (Fig. 2E-F and S1E)
PMID:37815455	FYPO:0008040	GFP-P4C(SidC) biosensor
PMID:37815455	FYPO:0008133	GFP-P4C(SidC) biosensor
PMID:37815455	FYPO:0006628	GFP-P4C(SidC) biosensor
PMID:37815455	FYPO:0003736	Figure 1F
PMID:37815455	PBO:0110111	(Fig. S1D)
PMID:37815455	PBO:0110112	(Fig. S1D)
PMID:37815455	FYPO:0002060	pik1-11 cells grow similarly to wildtype at 25 ̊C and 29 ̊C but pik1-11 cells do not grow at 32 ̊C or 36 ̊C (Fig. 1C)
PMID:37815455	GO:0046854	**********phosphatidylinositol 4-phosphate biosynthetic process 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	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	FYPO:0001903	(Fig. 1D-E).
PMID:37815455	GO:0046854	**********phosphatidylinositol 4-phosphate biosynthetic process
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	PBO:0110110	(Fig. S1D)
PMID:37815455	FYPO:0002061	pik1-11 cells grow similarly to wildtype at 25 ̊C and 29 ̊C but pik1-11 cells do not grow at 32 ̊C or 36 ̊C (Fig. 1C)
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 wildtype 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	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	FYPO:0000994	GFP-P4C(SidC) biosensor
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. Three topologically closed dsDNA sub- strates—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: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.
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: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. Although an intact supercoiled plasmid remained stably bound to condensin in the bead fraction, linearized dsDNA was released into the su- pernatant. This experiment confirms that ATP-dependent con- densin loading results in a topological DNA interaction.
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:0003690	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: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	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: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	PBO:0113806	A gradient of force is detected along End4 molecule in wildtype 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: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	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:37913773	GO:0061188	We thus conclude that heterochromatinization of rDNA induced by glucose starvation is initiated by TORC1 inactivation (Figure 3F).
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 accumula- tion across the rDNA, predominantly in the 18S and 28S regions (Figures 1A and 1B).
PMID:37913773	GO:0060963	Taken together, the transcription of ribosome-associ- ated genes is regulated by TORC1.
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 accumula- tion 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 signif- icantly 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:0111446	Chromatin immunoprecipitation (ChIP) experiments targeting FLAG-tagged Tor2, Pop3/LST8, Tco89, and Mip1/Raptor, constituents of TORC1,31 exhibited significant TORC1 accumula- tion across the rDNA, predominantly in the 18S and 28S regions (Figures 1A and 1B).
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 accumula- tion across the rDNA, predominantly in the 18S and 28S regions (Figures 1A and 1B).
PMID:37913773	FYPO:0001134	Although the downstream S6K kinase Psk1 in the TORC1 pathway has been implicated in RP phosphorylation,39 our finding demon- strated that rRNA abundance was unaffected in the psk1D strain (Figure S3A)
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 (Fig- ure 3I).
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 (Fig- ure 3I).
PMID:37913773	PBO:0110885	nuc1-632 mutant strain, wherein RNA polymerase I function was impaired.33,34 As a result, we found a considerable reduc- tion 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	PBO:0110884	We per- formed 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: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 per- formed 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 per- formed 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:0110878	heterochromatin forma- tion 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 methyl- ation,40 in addition to the RNAi-dependent pathway.14 We there- fore 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 accu- mulated between rDNA repeats (Figures 3D and 3E).
PMID:37913773	FYPO:0006074	To investigate this, we performed ChIP-qPCR tar- geting H3K9 methylation, a marker of heterochromatin forma- tion, 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:0110885	We then examined their accumulation at rDNA using ChIP assays and found a decrease in the rDNA accu- mulation of FLAG-Tor2 lacking the HTH domain (Figure 2G).
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	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:37923140	PBO:0113736	Fig. 5
PMID:37923140	PBO:0113736	Fig. 5
PMID:37923140	PBO:0113736	Fig. 5
PMID:37923140	PBO:0113735	Fig. 5
PMID:37923140	PBO:0105380	Fig. 5
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:0113734	Fig. 3
PMID:37923140	PBO:0113733	Fig. 3
PMID:37923140	PBO:0113732	Fig. 3
PMID:37923140	GO:0008270	Metal and acid-labile sulfide analysis of anaerobically purified Fep1-DBD from three inde- pendent samples indicated 0.76 ± 0.12 Zn, 0.69 ± 0.08 Fe, and 0.85 ± 0.10 S2- bound per monomer.
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: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: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	FYPO:0008267	figure 1A
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: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	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	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:0001357	The Pi hyper-sensitivity of Δpqr1Δxpr1 was suppressed by the double gene deletion of Pho84 and Pho842 (Figs. 6A and S6).
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:0113629	figure 1A
PMID:37949217	PBO:0113629	figure 1A
PMID:37949217	PBO:0113628	figure 1a
PMID:37949217	PBO:0113627	figure 1a
PMID:37949217	FYPO:0002060	This time, we obtained Δpqr1Δxpr1Δvtc4 col- onies on PMG with 0.15 mM Pi, which did not grow on either normal PMG (15 mM Pi) or YES.
PMID:37949217	FYPO:0000646	Cells were severely deformed/swollen and many were collapsed and probably dying (Figs. 2D and S2).
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:0008227	figure 3
PMID:37949217	FYPO:0000364	figure 3
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	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:37970674	PBO:0112070	inhibits
PMID:37970674	PBO:0112060	However, in nup132Δ cells, whereas wild-type Pli1 was destabilised, Pli1K3R levels remained high (Fig. 1B).
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: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: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	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:0112061	However, in nup132Δ cells, whereas wild-type Pli1 was destabilised, Pli1K3R levels remained high (Fig. 1B).
PMID:37970674	FYPO:0006995	Figure 3D
PMID:37970674	GO:0072766	inhibits
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	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	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: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	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: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	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	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	PBO:0094433	As expected, Rng2 localized to the nodes and ring upon entry into mitosis (Figure 4B), w
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	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	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:38048463	GO:0140727	Our genetic assays revealed that Rex1BD acts in an RNAi- independent manner.
PMID:38048463	PBO:0111621	Fig. 1C
PMID:38048463	PBO:0112025	Fig. 1E
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:0112026	Fig. 1H
PMID:38048463	PBO:0112027	Fig. 2E
PMID:38048463	PBO:0112027	Fig. 2F
PMID:38048463	PBO:0111621	Fig. 3B
PMID:38048463	PBO:0112027	Fig. 3B
PMID:38048463	PBO:0112027	Fig. 3B
PMID:38048463	PBO:0111621	Fig. 3C
PMID:38048463	PBO:0111621	Fig. 4B
PMID:38048463	PBO:0112028	Fig. 4C
PMID:38048463	PBO:0112188	Fig. 4D
PMID:38048463	PBO:0112029	Fig. 4E
PMID:38048463	PBO:0112030	Fig. 4E
PMID:38048463	PBO:0112031	Fig. 5B and C
PMID:38048463	PBO:0112032	Fig. 5D
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:0112033	Fig. 5C
PMID:38048463	PBO:0112027	Fig. 5D
PMID:38048463	PBO:0112027	Fig. 5D
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: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:0031509	Fig. 1H
PMID:38048463	GO:0031509	Fig. 5D
PMID:38051102	PBO:0110687	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	GO:0003713	from
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: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	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	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: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 phos- phorylated 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 phos- phorylated form (Fig. 6B).
PMID:38051102	PBO:0110699	The Ifh1-Fhl1 associ- ation was detected both in the presence and absence of Sfp1, suggesting that Sfp1 is not required for their interaction (Fig. 4F).
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 inter- action depends on the forkhead-associated (FHA) domain of Fhl1.
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: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: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 indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110696	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110695	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110694	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110693	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110692	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110691	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110690	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110689	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110688	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110686	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110685	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110684	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110683	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110682	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110681	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110680	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110679	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110678	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110677	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110676	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110675	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110674	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110673	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110672	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110671	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110670	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110669	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110668	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110667	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110666	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110665	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110664	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110663	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110662	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110661	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110660	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110659	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110658	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110657	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110656	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110655	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110654	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110653	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110652	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110651	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110650	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110649	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110648	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110647	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110646	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110645	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110644	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110643	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110642	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110641	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110640	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110639	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110638	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110637	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110636	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110635	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110634	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110633	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110632	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110631	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110630	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110629	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110628	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110627	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110626	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110625	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110624	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110623	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110622	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110621	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110620	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110619	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110618	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110617	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110616	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110615	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110614	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110613	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110612	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110611	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110610	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110609	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110608	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110607	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110606	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110605	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110604	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110603	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110602	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110601	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110600	Our RNA-seq data indi- cated 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 pro- tein 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:0110599	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110598	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110597	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110596	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110595	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110594	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110593	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110592	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110591	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110590	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110589	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110588	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110587	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110586	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110585	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110584	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110583	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110582	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110581	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110580	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110579	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110578	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110577	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
PMID:38051102	PBO:0110576	Our RNA-seq data indi- cated 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 pro- tein synthesis linked to cell growth.
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: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:0110573	In the tor2-287 and tor2-13 mutants, the Sfp1 protein dra- matically 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 dra- matically decreased within 2h after shifting to the restrictive temperature (Fig. 2A),
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: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: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	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	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: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	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: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: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: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: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:38133430	FYPO:0001357	Fig. 5A
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:0004481	Fig. 4A
PMID:38133430	FYPO:0000080	Fig. 4A
PMID:38133430	FYPO:0001357	Fig. 4A
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:0094771	Fig. 5B
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:0004481	Fig. 5A
PMID:38133430	FYPO:0004481	Fig. 5A
PMID:38133430	PBO:0094771	Fig. 5B
PMID:38133430	FYPO:0001357	Fig. 5A
PMID:38133430	FYPO:0001357	Fig. 5A
PMID:38133430	FYPO:0000082	Fig. 4A
PMID:38133430	FYPO:0001357	Fig. 5A
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. 4C, Fig. S3B
PMID:38133430	PBO:0094738	Fig. 4C
PMID:38133430	PBO:0110727	Fig. 8B
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	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	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:0001357	Fig. 4A
PMID:38133430	FYPO:0001357	Fig. 4A
PMID:38133430	FYPO:0001357	Fig. 4A
PMID:38133430	FYPO:0000082	Fig. 4A, Fig. S3A
PMID:38133430	FYPO:0000082	Fig. 4A, Fig. S3A
PMID:38133430	FYPO:0002085	Fig. S3A
PMID:38133430	FYPO:0002085	Fig. S3A
PMID:38133430	PBO:0094738	Fig. S3B
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	PBO:0094738	Fig. 4C
PMID:38133430	PBO:0094738	Fig. 4C
PMID:38133430	PBO:0094777	Fig. 4C
PMID:38133430	PBO:0094777	Fig. 4C
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:0001355	Fig. 2, Fig. 4A, Fig. S3A
PMID:38133430	FYPO:0001355	Fig. 2, Fig. 4A, Fig. S3A
PMID:38133430	FYPO:0002141	Fig. 5A
PMID:38133430	FYPO:0002141	Fig. 5A
PMID:38133430	PBO:0094738	Fig. 4C, S3B
PMID:38133430	FYPO:0004481	Fig. 5A
PMID:38133430	FYPO:0004481	Fig. 5A
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: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:0094567	s shown in figure 5, the wee1 mutants with no functional spindle check- point indeed failed in accurate chromosome segregation and generated two sister cells with unequal nuclear size.
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 clus- tered 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 check- point 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 check- point 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 check- point indeed failed in accurate chromosome segregation and generated two sister cells with unequal nuclear size.
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: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: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:0112715	Notably, the localizations of Lsd1 and Lsd2 are diminished at the pro- moter 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 pro- moter 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	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: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	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	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	Loss of Ddb1 slightly enhances the Lsd1-FTP level, while having no significant effect on the Lsd2-FTP level (Fig 3E).
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: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	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: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: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: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: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: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: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:0112721	Lsd1 (Fig 4A) or Lsd2 (Fig 4B) was detected in the presence of a temperature-sensitive 26S pro- teasome 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:0112722	Lsd1 (Fig 4A) or Lsd2 (Fig 4B) was detected in the presence of a temperature-sensitive 26S pro- teasome 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:0112718	(Fig 5A)
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: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: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: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	figure 6
PMID:38181050	PBO:0112723	figure 6
PMID:38181050	PBO:0112724	figure 6
PMID:38181050	PBO:0112724	figure 6
PMID:38181050	PBO:0112725	figure 6
PMID:38181050	PBO:0112725	figure 6
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	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	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	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	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	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	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: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	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: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: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:0112731	However, the loss of Shg1 and Sdc1 seems to have little or no effect on Lsd1 protein levels.
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: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: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: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: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: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: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: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: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: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:0112740	Set1 signif- icantly at 37 ̊C compared to that at 30 ̊C, which is due to the temperature sensitive nature of cul4-1.
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:0095652	Fig. S1E
PMID:38181050	PBO:0095652	Fig. S1E
PMID:38181050	PBO:0095652	Fig. S1E
PMID:38188419	PBO:0093580	Fig. 1G
PMID:38188419	PBO:0114646	Fig. 1F
PMID:38188419	FYPO:0000957	Fig. 1D
PMID:38188419	PBO:0114645	Fig. 1D
PMID:38188419	FYPO:0000963	Fig. 1A
PMID:38188419	PBO:0093579	Fig. 1G
PMID:38188419	PBO:0093579	Fig. 1G
PMID:38188419	PBO:0093580	Fig. 1G
PMID:38188419	PBO:0093581	Fig. 1G
PMID:38188419	PBO:0093580	Fig. 1A
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:0093561	Figure 3
PMID:38269097	PBO:0112336	Figure 4
PMID:38269097	PBO:0112337	Figure 4
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: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. 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:0112363	Table S2
PMID:38269097	PBO:0112364	Table S2
PMID:38269097	PBO:0112365	Table S2
PMID:38269097	PBO:0112366	Table S2
PMID:38269097	PBO:0112367	Table S2
PMID:38269097	PBO:0112368	Table S2
PMID:38269097	PBO:0112369	Table S2
PMID:38269097	PBO:0112370	Table S2
PMID:38269097	PBO:0112371	Table S2
PMID:38269097	PBO:0112372	Table S2
PMID:38269097	PBO:0112373	Table S2
PMID:38269097	PBO:0112374	Table S2
PMID:38269097	PBO:0112375	Table S2
PMID:38269097	PBO:0112376	Table S2
PMID:38269097	PBO:0112377	Table S2
PMID:38269097	PBO:0112378	Table S2
PMID:38269097	PBO:0112379	Table S2
PMID:38269097	PBO:0112380	Table S2
PMID:38269097	PBO:0112381	Table S2
PMID:38269097	PBO:0112382	Table S2
PMID:38269097	PBO:0112383	Table S2
PMID:38269097	PBO:0112384	Table S2
PMID:38269097	PBO:0112385	Table S2
PMID:38269097	PBO:0112386	Table S2
PMID:38269097	PBO:0112387	Table S2
PMID:38269097	PBO:0112388	Table S2
PMID:38269097	PBO:0112389	Table S2
PMID:38269097	PBO:0112390	Table S2
PMID:38269097	PBO:0112391	Table S2
PMID:38269097	PBO:0112392	Table S2
PMID:38269097	PBO:0112393	Fig. 2C
PMID:38269097	PBO:0093556	Figure 2
PMID:38269097	FYPO:0001357	Figure 1
PMID:38269097	PBO:0112393	Fig. 2C
PMID:38269097	FYPO:0001357	Figure 1
PMID:38269097	FYPO:0001357	Figure 1
PMID:38269097	FYPO:0001357	Figure 1
PMID:38269097	PBO:0093561	Figure 3
PMID:38269097	PBO:0112394	Fig. 4C
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: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: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:0112362	Table S2
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: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:0112488	Table S3
PMID:38269097	PBO:0112488	Table S3
PMID:38269097	FYPO:0000674	Figure 1
PMID:38269097	FYPO:0001357	Figure 2 and 3
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
PMID:38269097	FYPO:0001357	Figure 2
PMID:38269097	FYPO:0001357	Figure 2
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 3
PMID:38269097	FYPO:0000674	Figure 3
PMID:38269097	FYPO:0001357	Figure 3
PMID:38269097	FYPO:0001357	Figure 3
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:0000674	Figure 4
PMID:38269097	FYPO:0001357	Figure 4
PMID:38269097	FYPO:0000674	Figure 4
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: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. 6D
PMID:38269097	FYPO:0000674	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	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	PBO:0112488	Table S3
PMID:38285941	PBO:0095651	Fig. S1. 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	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	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	FYPO:0003247	(Fig. 4 E and F).
PMID:38285941	FYPO:0008187	(Fig. 4 E and F).
PMID:38285941	PBO:0112227	Mcl1 localized to heterochromatic loci in S phase, like Mcm2 (Fig. 2B).
PMID:38285941	FYPO:0003246	(Fig. 2 D and E and SI Appendix, Figs. S2 A–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:0111391	(Fig. 4 E and F).
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: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:0095653	Fig. S1. Genetic screen for mutants defective in heterochromatin propagation.
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:0007159	(Fig. 4 E 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	PBO:0112226	Thus, although both mutants affect the retention of parental histones, Mcl1 plays a more critical role in the process.
PMID:38285941	PBO:0095652	Fig. S1. Genetic screen for mutants defective in heterochromatin propagation.
PMID:38285941	PBO:0095653	Fig. S1. Genetic screen for mutants defective in heterochromatin propagation.
PMID:38285941	PBO:0095651	Fig. S1. Genetic screen for mutants defective in heterochromatin propagation.
PMID:38285941	PBO:0095651	Fig. S1. Genetic screen for mutants defective in heterochromatin propagation.
PMID:38285941	PBO:0095653	Fig. S1. Genetic screen for mutants defective in heterochromatin propagation.
PMID:38289024	FYPO:0002336	Figure 6B; endogenous atf1+ was deleted
PMID:38289024	FYPO:0002336	Figure 6B; endogenous atf1 was deleted
PMID:38289024	PBO:0093558	Figure 6B, Figure 3-S1; endogenous atf1+ was deleted
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: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	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	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	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	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: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: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 mainte- nance of heterochromatin.
PMID:38289024	FYPO:0002336	Figure 3D; endogenous atf1+ was deleted
PMID:38289024	FYPO:0002336	Figure 3- S2A B
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:0004376	Figure 6B; endogenous atf1+ was deleted
PMID:38289024	FYPO:0002336	Figure 8A
PMID:38289024	FYPO:0002336	Figure 6B; endogenous atf1+ was deleted
PMID:38289024	FYPO:0002336	Figure 6B; endogenous atf1+ was deleted
PMID:38359013	FYPO:0002061	erratum corrected previous annotation
PMID:38360270	PBO:0112201	Fig. 4
PMID:38360270	PBO:0112200	Fig. 4
PMID:38360270	PBO:0112125	Fig. 4
PMID:38360270	PBO:0112199	Fig. 4
PMID:38360270	PBO:0112119	Fig. 2A
PMID:38360270	PBO:0112198	Fig. 4
PMID:38360270	PBO:0112124	Fig. 4
PMID:38360270	FYPO:0003118	Fig. 3
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	FYPO:0003118	Fig. 3
PMID:38360270	PBO:0112123	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	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: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:0112122	Fig. 2B
PMID:38360270	PBO:0093560	Fig. 2B
PMID:38360270	PBO:0112120	Fig. 2A
PMID:38360270	PBO:0112121	Fig. 2A
PMID:38360270	PBO:0093561	Fig. 2B
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: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. 5Cells 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 con- taining tunicamycin.
PMID:38360270	PBO:0112121	Fig. 2A
PMID:38360270	PBO:0112127	Fig. 4
PMID:38360270	PBO:0112203	Fig. 4
PMID:38360270	PBO:0112119	Fig. 2A
PMID:38360270	PBO:0112118	Fig. 2A
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	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 respi- ration was increased in erd2Δ cells.
PMID:38360270	PBO:0112117	Fig. 1 Intriguingly, we observed that the absence of erd2 caused mitochondrial fragmentation (Fig. 1, A and B)
PMID:38360270	PBO:0112202	Fig. 4
PMID:38376141	FYPO:0000278	Fig. 7D
PMID:38376141	PBO:0114141	Fig. 7B and C
PMID:38376141	FYPO:0007328	Fig. 7B and C
PMID:38376141	FYPO:0004742	Fig. 7A
PMID:38376141	PBO:0114152	Fig. 6C and D
PMID:38376141	PBO:0114151	Fig. 6
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 supple- ment 2G, Figure 3—figure supplement 3A–B).
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	FYPO:0002150	Fig. 7D
PMID:38376141	FYPO:0002150	Fig. 7D
PMID:38376141	FYPO:0000278	Fig. 7D
PMID:38376141	FYPO:0002150	Fig. 7D
PMID:38376141	FYPO:0002150	Fig. 7D
PMID:38376141	PBO:0112225	In contrast, when we comple- mented 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:38376141	PBO:0114145	Fig. 6C and D
PMID:38376141	PBO:0112225	In contrast, when we comple- mented 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:0114143	Fig. 6A
PMID:38376141	PBO:0114146	Fig. 7B and C
PMID:38376141	PBO:0114145	Fig. 6C and D
PMID:38376141	PBO:0094679	Fig. 7A
PMID:38376141	PBO:0114144	When we used the SpCAF-1-PIP* mutant, we did not detect super- coiling 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	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 comple- mented 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	FYPO:0007158	Fig. 2 supplement 1A
PMID:38376141	PBO:0114140	Fig. 6
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:0093589	Fig. 7A
PMID:38424265	PBO:0093588	Fig. 7A
PMID:38424265	FYPO:0001190	Fig. 7B
PMID:38424265	FYPO:0008237	Fig. 5
PMID:38424265	FYPO:0000245	Fig. 6A
PMID:38424265	PBO:0103077	Fig. 2C
PMID:38424265	PBO:0093595	Fig. 3B
PMID:38424265	FYPO:0005947	Fig. 3B
PMID:38424265	FYPO:0001357	Fig. 2C
PMID:38424265	FYPO:0001357	Fig. 1A
PMID:38424265	FYPO:0001043	Fig. 3A
PMID:38424265	PBO:0093577	Fig. 3C
PMID:38424265	PBO:0100665	Fig. 1A
PMID:38424265	PBO:0111039	Fig. 6B
PMID:38424265	FYPO:0001043	Fig. 3A
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:0111039	Fig. 6B
PMID:38424265	PBO:0093578	Fig. 3C
PMID:38442865	PBO:0112954	Fig. 4B
PMID:38442865	PBO:0112945	Fig. S1E and F
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	FYPO:0008233	Fig. S4
PMID:38442865	FYPO:0008233	Fig. S4
PMID:38442865	PBO:0112949	Fig. 3A and C
PMID:38442865	PBO:0112948	Fig. 3A and C
PMID:38442865	PBO:0093562	Fig. S1
PMID:38442865	PBO:0112947	Fig. 3A and C
PMID:38442865	FYPO:0008233	Fig. 2D, E and F
PMID:38442865	PBO:0093562	Fig. S1
PMID:38442865	PBO:0112950	Fig. 3B and C
PMID:38442865	PBO:0093562	Fig. S1
PMID:38442865	PBO:0093564	Fig. 1D
PMID:38442865	PBO:0112941	Fig. 1A and B
PMID:38442865	PBO:0112942	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	PBO:0112943	Fig. S1E and F
PMID:38442865	PBO:0112942	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	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:0112946	Fig. 2D, E and F
PMID:38442865	PBO:0112943	Fig. 2D, E and F
PMID:38442865	PBO:0112945	Fig. 2D, E and F
PMID:38442865	FYPO:0007114	Fig. 2A, B and C
PMID:38442865	FYPO:0007114	Fig. 2A, B and C
PMID:38442865	PBO:0112942	Fig. 2A, B and C
PMID:38442865	PBO:0112944	Fig. 1E
PMID:38442865	PBO:0093560	Fig. 1D
PMID:38442865	PBO:0093559	Fig. 1D
PMID:38442865	PBO:0093562	Fig. 1D
PMID:38442865	FYPO:0000177	Fig. 1C
PMID:38442865	PBO:0111723	Fig. 1E
PMID:38442865	PBO:0112951	Fig. 3B and C
PMID:38442865	PBO:0112952	Fig. 3B and C
PMID:38442865	PBO:0112953	Fig. 3D, E and F
PMID:38442865	PBO:0112946	Fig. 3D, E and F
PMID:38442865	FYPO:0008233	Fig. 3D, E and F
PMID:38442865	FYPO:0008233	Fig. 3D, E and F
PMID:38448160	PBO:0112141	Fig. 1B
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:0112154	Fig. 1B In moa1Δ cells, Rec8 cohesin localization increases at the core centromere although sister chromatid cohesion is abol- ished at this sit
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:0112153	Figure 4E
PMID:38448160	PBO:0109676	Figure 4E
PMID:38448160	PBO:0109676	Figure 4E
PMID:38448160	PBO:0112247	Figure 4E
PMID:38448160	PBO:0112137	Figure 4E
PMID:38448160	FYPO:0003176	Fig. 4D
PMID:38448160	FYPO:0003176	Fig. 4D
PMID:38448160	FYPO:0003176	Fig. 3D
PMID:38448160	PBO:0112151	Fig. 3F
PMID:38448160	PBO:0112150	Fig. 3E
PMID:38448160	PBO:0112246	Figure 2D
PMID:38448160	PBO:0112502	Fig. 2B
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	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	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:0112146	Fig. 3D
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	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:0112147	Figure 2D emarkably, introducing the rec8-15A mutation into rec12Δ rec8-2A cells increased equational segrega- tion 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:0112146	Figure 2D
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	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 centro- meres.
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 cen- tromeres.
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	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 cen- tromeres.....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	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	GO:0031619	In moa1Δ cells, a mi- nority 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: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: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:0112497	Unequal sister chromatid segregation in meiosis II after reductional segregation in meiosis I. Fig. 2B
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:0112138	Figure 4B
PMID:38448160	PBO:0112138	Figure 4E
PMID:38448160	PBO:0112142	Fig. 1B
PMID:38448160	PBO:0112143	Fig. 2B In moa1Δ cells, a mi- nority 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: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	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	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	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	Unequal sister chromatid segregation in meiosis II after reductional segregation in meiosis I. Fig. 3D
PMID:38448160	PBO:0112149	Fig. 3E
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	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	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	PBO:0112877	All subunits in the Arp2/3 complex, except for Arp2 and ARPC5, contact the mother filament directly.
PMID:38479839	PBO:0103247	Fig. 3F
PMID:38479839	PBO:0094679	Fig. 3
PMID:38479839	PBO:0096191	Fig. 1
PMID:38479839	PBO:0103245	Fig. 3D
PMID:38479839	GO:0006335	Deposits parental histone H3-H4 on both daughter strands during DNA replication
PMID:38479839	PBO:0103247	Fig. 3F
PMID:38479839	PBO:0112332	Fig. 3
PMID:38479839	PBO:0096191	Fig. 1
PMID:38479839	PBO:0103246	Fig. 3F
PMID:38479839	FYPO:0004742	Fig. 3
PMID:38479839	PBO:0096192	Fig. 1
PMID:38479839	PBO:0112330	Fig. 1E
PMID:38479839	PBO:0096191	Fig. 1
PMID:38479839	PBO:0112766	Fig. S2
PMID:38479839	PBO:0112330	Fig. 6A
PMID:38479839	PBO:0112766	Fig. S2
PMID:38479839	PBO:0096191	Fig. S2
PMID:38479839	PBO:0112329	Work with Dpb4 for parental histone H3-H4 transfer on the leading strand
PMID:38479839	PBO:0112329	Work with Dpb3 for parental histone H3-H4 transfer on the leading strand
PMID:38479839	PBO:0112334	Fig. 6A
PMID:38479839	PBO:0112333	Fig. 5D
PMID:38479839	PBO:0103247	Fig. 3F
PMID:38479839	PBO:0103247	Fig. 3F
PMID:38479839	PBO:0112329	Transfers parental histone H3-H4 on the lagging strand.
PMID:38479839	PBO:0112329	Deposits parental histone H3-H4 on both daughter strands during DNA replication.
PMID:38479839	PBO:0112766	Fig. 2
PMID:38479839	FYPO:0008186	Fig. 1E
PMID:38479839	FYPO:0008186	Fig. 1E
PMID:38479839	FYPO:0008186	Fig. 1E
PMID:38479839	PBO:0095977	Fig. 3E
PMID:38479839	PBO:0112331	Fig. 2
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:0112766	Fig. 2
PMID:38479839	PBO:0095977	Fig. 3E
PMID:38479839	PBO:0095977	Fig. 3E
PMID:38479839	PBO:0096191	Fig. S2
PMID:38479839	PBO:0112335	Fig. 5D
PMID:38479839	PBO:0112331	Fig. 6B, C and D
PMID:38479839	PBO:0112767	Fig. 6B, C and D
PMID:38479839	PBO:0096192	Fig. 6A
PMID:38479839	PBO:0096192	Fig. 6A
PMID:38479839	GO:0006335	Works with Dpb3 for parental histone H3-H4 transfer on the leading strand
PMID:38479839	GO:0006335	Transfers parental histone H3-H4 on the lagging strand.
PMID:38479839	PBO:0112331	Fig. S5
PMID:38479839	FYPO:0004742	Fig. S2
PMID:38479839	FYPO:0004742	Fig. S2
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:0114175	Fig. S2C
PMID:38482739	FYPO:0000957	Fig. 4D
PMID:38482739	PBO:0093564	Fig. S3
PMID:38482739	FYPO:0001357	Fig. S1
PMID:38482739	FYPO:0001355	Fig. S1
PMID:38482739	FYPO:0000957	Fig. 4D
PMID:38482739	PBO:0093615	Fig. 7G
PMID:38482739	PBO:0093615	Fig. 7G
PMID:38482739	PBO:0114174	Fig. S2C
PMID:38482739	FYPO:0000957	Fig. 4D
PMID:38482739	PBO:0093615	Fig. 4C
PMID:38482739	PBO:0093613	Fig. 4C
PMID:38482739	FYPO:0001690	Fig. 4B
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: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	PBO:0093615	Fig. 4
PMID:38482739	PBO:0093613	Fig. 4B
PMID:38482739	PBO:0114173	Fig. S2C
PMID:38482739	PBO:0114172	Fig. 1D and E
PMID:38482739	PBO:0093614	Fig. 4
PMID:38482739	PBO:0093563	Fig. 7G
PMID:38482739	PBO:0114171	Fig. 1D and E
PMID:38482739	PBO:0114168	Fig. 4D
PMID:38482739	PBO:0097220	Fig. 4D
PMID:38482739	FYPO:0000006	Fig. 4G and H
PMID:38482739	FYPO:0000010	Fig. 1B
PMID:38482739	FYPO:0000006	Fig. 6
PMID:38482739	FYPO:0001403	Fig. 1A
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: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: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:0001118	Fig. 2A
PMID:38482739	PBO:0114177	Fig. S2C
PMID:38482739	PBO:0114176	Fig. S2C
PMID:38499152	PBO:0114790	ABOLISHED ********These mutations also completely abolished Cox1 synthesis and decreased the syn- thesis of other mtDNA-encoded proteins (Fig. 5, B and C).
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:0114766	Similarly, deletion of ppr4 did not impair the inter- action among Mrh5-Myc, Sls1-FLAG, and Mtf2-HA (Fig. 2E).
PMID:38499152	PBO:0114765	Similarly, deletion of ppr4 did not impair the inter- action among Mrh5-Myc, Sls1-FLAG, and Mtf2-HA (Fig. 2E).
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: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: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: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: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:0114758	Deletion of sls1 resulted in a drastic reduction in the protein level of Mtf2 (Fig. 1B). A
PMID:38499152	PBO:0114757	(Fig. 1A)
PMID:38499152	PBO:0114756	Additionally, the Mtf2 protein level was moderately reduced in Δmrh5 cells (Fig. 1A).
PMID:38499152	PBO:0114774	Evidence: Sucrose sedimentation analysis | In contrast, Mrh5C subunits no longer co-sedimented with the mtSSU in Δmtf2 cells (Fig. 3D)
PMID:38499152	PBO:0114775	Evidence: Sucrose sedimentation analysis In contrast, Mrh5C subunits no longer co-sedimented with the mtSSU in Δmtf2 cells (Fig. 3D)
PMID:38499152	PBO:0114776	Evidence: Sucrose sedimentation analysis |In contrast, Mrh5C subunits no longer co-sedimented with the mtSSU in Δmtf2 cells (Fig. 3D)
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: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	[35S]-methionine/cysteine labeling
PMID:38499152	PBO:0114789	These mutations also completely abolished Cox1 synthesis and decreased the syn- thesis of other mtDNA-encoded proteins (Fig. 5, B and C).
PMID:38499152	PBO:0114791	These mutations also completely abolished Cox1 synthesis and decreased the syn- thesis of other mtDNA-encoded proteins (Fig. 5, B and C).
PMID:38499152	PBO:0114792	These mutations also completely abolished Cox1 synthesis and decreased the syn- thesis of other mtDNA-encoded proteins (Fig. 5, 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: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: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: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	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: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: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: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: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: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: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:0114764	Deletion of mrh5 did not impair the interaction among Prp4-CBP, Sls1-FLAG, and Mtf2-HA (Fig. 2D).
PMID:38499152	PBO:0114793	These mutations also completely abolished Cox1 synthesis and decreased the syn- thesis of other mtDNA-encoded proteins (Fig. 5, B and C).
PMID:38499152	PBO:0114789	These mutations also completely abolished Cox1 synthesis and decreased the syn- thesis of other mtDNA-encoded proteins (Fig. 5, B and C)
PMID:38499152	PBO:0114790	ABOLISHED **********These mutations also completely abolished Cox1 synthesis and decreased the syn- thesis of other mtDNA-encoded proteins (Fig. 5, B and C)
PMID:38499152	PBO:0114791	These mutations also completely abolished Cox1 synthesis and decreased the syn- thesis of other mtDNA-encoded proteins (Fig. 5, B and C)
PMID:38499152	PBO:0114792	These mutations also completely abolished Cox1 synthesis and decreased the syn- thesis of other mtDNA-encoded proteins (Fig. 5, B and C)
PMID:38499152	PBO:0114793	These mutations also completely abolished Cox1 synthesis and decreased the syn- thesis of other mtDNA-encoded proteins (Fig. 5, B and C)
PMID:38499152	FYPO:0002056	[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	evidence: sucrose sedimentation analysis | 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:0114768	evidence: sucrose sedimentation analysis | 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 abol- ished 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 abol- ished 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 abol- ished 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 abol- ished the association of the cox1 mRNA with the mtSSU (Fig. 8).
PMID:38499152	PBO:0114798	Immunoblot analysis of factions revealed that mutation of the DEAD-box of Mrh5 abol- ished 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 abol- ished 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 abol- ished the association of the cox1 mRNA with the mtSSU (Fig. 8).
PMID:38499152	PBO:0114798	Immunoblot analysis of factions revealed that mutation of the DEAD-box of Mrh5 abol- ished the association of the cox1 mRNA with the mtSSU (Fig. 8).
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	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	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	FYPO:0002056	[35S]-methionine/cysteine labeling
PMID:38499152	PBO:0114755	(Fig. 1A)
PMID:38499152	PBO:0114754	Deletion of mrh5 did not reduce the protein level of Ppr4 (Fig. 1A)
PMID:38598031	PBO:0107560	Figure 3c
PMID:38598031	PBO:0093594	Figure 2
PMID:38598031	PBO:0107560	Figure 2
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:0093595	Figure 3a
PMID:38598031	PBO:0093595	Figure 3a
PMID:38598031	PBO:0096587	Figure 3a
PMID:38598031	PBO:0096587	Figure 3a
PMID:38598031	PBO:0093594	Figure 3b
PMID:38598031	FYPO:0001020	Figure 3b
PMID:38598031	PBO:0093594	Figure 3b
PMID:38598031	PBO:0107560	Figure 3b
PMID:38598031	FYPO:0005947	Figure 3c
PMID:38598031	FYPO:0001020	Figure 3c
PMID:38598031	PBO:0093594	Figure 3c
PMID:38598031	PBO:0107560	Figure 1b
PMID:38598031	PBO:0093595	Figure 3c, rst2∆ partially rescues the pps1∆ pka1∆ strain on KCl
PMID:38598031	PBO:0107560	Figure 3c, rst2∆ partially rescues the pps1∆ pka1∆ strain on CaCl2
PMID:38598031	GO:0005783	Figure 4
PMID:38598031	PBO:0107562	Figure 4
PMID:38598031	GO:0005886	Figure 4
PMID:38598031	PBO:0112566	Figure 4
PMID:38598031	PBO:0112567	Figure 4a
PMID:38598031	GO:0005634	Figure 5
PMID:38598031	GO:0005737	Figure 5
PMID:38598031	PBO:0107565	Figure 5
PMID:38598031	PBO:0037579	Figure 5
PMID:38598031	PBO:0112568	Figure 5
PMID:38598031	PBO:0107568	Figure 5
PMID:38598031	PBO:0107568	Figure 5
PMID:38598031	PBO:0112569	Figure 5
PMID:38598031	PBO:0107570	Figure 6
PMID:38598031	PBO:0107569	Figure 6
PMID:38598031	PBO:0093594	Figure 1a
PMID:38598031	PBO:0112570	Figure 6
PMID:38598031	PBO:0112571	Figure 6
PMID:38598031	PBO:0107570	Figure 6
PMID:38598031	PBO:0112570	Figure 6
PMID:38598031	PBO:0112572	Figure 4a
PMID:38598031	PBO:0112569	Figure 5
PMID:38598031	PBO:0112568	Figure 5
PMID:38598031	PBO:0107568	Figure 5
PMID:38598031	PBO:0107568	Figure 5
PMID:38598031	PBO:0112573	Figure 6
PMID:38598031	PBO:0112573	Figure 6
PMID:38598031	PBO:0112574	Figure 6
PMID:38598031	PBO:0112574	Figure 6
PMID:38598031	PBO:0112574	Figure 6
PMID:38598031	PBO:0112574	Figure 6
PMID:38598031	PBO:0112570	Figure 6
PMID:38598031	PBO:0112571	Figure 6
PMID:38598031	PBO:0112570	Figure 6
PMID:38598031	FYPO:0005947	Figure 2
PMID:38598031	FYPO:0001020	Figure 2
PMID:38692277	GO:0042407	(comment: complex member)
PMID:38692277	GO:0042407	(comment: complex member)
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 lo- calizes to mitochondria (Figure 2B
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: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:0044284	. These data, in combination with previous immuno-EM-labeling experi- ments 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	******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	FYPO:0003393	disruption of cristae architecture through loss of the core MICOS subunit Mic60 caused a growth defect specifically on media that re- quires 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 re- quires respiration (Figure 1D).
PMID:38692277	GO:0044284	Both Mic60 and Mic26 appeared in a semi-punctate pattern distributed throughout the mitochondrial network (Fig- ure 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 (Fig- ure 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:0042407	(comment: complex member)
PMID:38692277	PBO:0112958	******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	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	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 re- quires 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	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	PBO:0112957	Approximately half of the Dmmc1 cells had abnormal mito- chondrial morphology, and many cells contained the lamellar and ring-shaped mitochondria characteristic of cells with MICOS sub- unit deletions (Figures 2H and 2I)
PMID:38692277	FYPO:0003393	disruption of cristae architecture through loss of the core MICOS subunit Mic60 caused a growth defect specifically on media that re- quires respiration (Figure 1D).
PMID:3870979	FYPO:0002043	at 33.5 degrees, which is restrictive for cdc10-129 but allows sporulation
PMID:3870979	FYPO:0002043	at 33.5 degrees, which is restrictive for cdc2-33 but allows sporulation
PMID:3870979	FYPO:0000681	at 33.5 degrees, which is restrictive for cdc2-33 but allows sporulation
PMID:3870979	FYPO:0000583	at 33.5 degrees, which is restrictive for cdc10129 but allows sporulation
PMID:3870979	FYPO:0001886	done in h- cells kinetics depend on medium composition (see fig 6B)
PMID:38780300	PBO:0114588	Fig. 3
PMID:38780300	PBO:0032852	Fig. 6A
PMID:38780300	PBO:0033073	Fig. 6C
PMID:38780300	PBO:0114551	Fig. 6A
PMID:38780300	PBO:0114550	Fig. 3
PMID:38780300	PBO:0114564	Fig. 3
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	PBO:0114564	Fig. 3
PMID:38780300	PBO:0114549	Fig. 3
PMID:38780300	PBO:0114548	Fig. 3
PMID:38780300	PBO:0114547	Fig. 3
PMID:38780300	PBO:0114546	Fig. 3
PMID:38780300	PBO:0114545	Fig. 3
PMID:38780300	PBO:0114544	Fig. 3
PMID:38780300	PBO:0114543	Fig. 3
PMID:38780300	PBO:0114542	Fig. 3
PMID:38780300	PBO:0114541	Fig. 3
PMID:38780300	PBO:0114588	Fig. 3
PMID:38780300	PBO:0114540	Fig. 1B
PMID:38780300	PBO:0114588	Fig. 3
PMID:38780300	PBO:0114544	Fig. 3
PMID:38780300	PBO:0114563	Fig. 3
PMID:38780300	PBO:0114543	Fig. 3
PMID:38780300	PBO:0114543	Fig. 3
PMID:38780300	PBO:0114543	Fig. 3
PMID:38780300	PBO:0114562	Fig. 3
PMID:38780300	PBO:0114562	Fig. 3
PMID:38780300	PBO:0114566	Fig. 3
PMID:38780300	PBO:0114566	Fig. 3
PMID:38780300	PBO:0114568	Fig. 3
PMID:38780300	PBO:0114550	Fig. 3
PMID:38780300	PBO:0114542	Fig. 3
PMID:38780300	PBO:0114561	Fig. 3
PMID:38780300	PBO:0114561	Fig. 3
PMID:38780300	PBO:0114561	Fig. 3
PMID:38780300	PBO:0114560	Fig. 3
PMID:38780300	PBO:0114559	Fig. 3
PMID:38780300	PBO:0114558	Fig. 3
PMID:38780300	PBO:0114557	Fig. 3
PMID:38780300	PBO:0114556	Fig. 3
PMID:38780300	PBO:0114555	Fig. 3
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:0114553	Fig. 1B
PMID:38780300	FYPO:0004646	Fig. 5
PMID:38780300	PBO:0114567	Fig. 3
PMID:38780300	PBO:0114548	Fig. 3
PMID:38780300	PBO:0114548	Fig. 3
PMID:38780300	PBO:0114547	Fig. 3
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: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	PBO:0114588	Fig. 3
PMID:38780300	PBO:0114587	Fig. 3
PMID:38780300	PBO:0114586	Fig. 3
PMID:38780300	PBO:0114585	Fig. 3
PMID:38780300	PBO:0114584	Fig. 3
PMID:38780300	PBO:0114583	Fig. 3
PMID:38780300	PBO:0114582	Fig. 3
PMID:38780300	PBO:0114581	Fig. 3
PMID:38780300	PBO:0114568	Fig. 3
PMID:38780300	PBO:0114579	Fig. 3
PMID:38780300	PBO:0114578	Fig. 3
PMID:38780300	PBO:0114580	Fig. 3
PMID:38780300	PBO:0114579	Fig. 3
PMID:38780300	PBO:0114567	Fig. 3
PMID:38780300	PBO:0114567	Fig. 3
PMID:38780300	PBO:0114578	Fig. 3
PMID:38780300	PBO:0114570	Fig. 3
PMID:38780300	PBO:0114570	Fig. 3
PMID:38780300	PBO:0114569	Fig. 3
PMID:38780300	PBO:0114569	Fig. 3
PMID:38780300	PBO:0114577	Fig. 3
PMID:38780300	PBO:0114576	Fig. 3
PMID:38780300	PBO:0114560	Fig. 3
PMID:38780300	PBO:0114547	Fig. 3
PMID:38780300	PBO:0114547	Fig. 3
PMID:38780300	PBO:0114566	Fig. 3
PMID:38780300	PBO:0114545	Fig. 3
PMID:38780300	PBO:0114560	Fig. 3
PMID:38780300	PBO:0114560	Fig. 3
PMID:38780300	PBO:0114575	Fig. 3
PMID:38780300	PBO:0114557	Fig. 3
PMID:38780300	PBO:0114557	Fig. 3
PMID:38780300	PBO:0114574	Fig. 3
PMID:38780300	PBO:0114574	Fig. 3
PMID:38780300	PBO:0114572	Fig. 3
PMID:38780300	PBO:0114545	Fig. 3
PMID:38780300	PBO:0114545	Fig. 3
PMID:38780300	PBO:0114572	Fig. 3
PMID:38780300	PBO:0114555	Fig. 3
PMID:38780300	PBO:0114555	Fig. 3
PMID:38780300	PBO:0114573	Fig. 3
PMID:38780300	PBO:0114572	Fig. 3
PMID:38780300	PBO:0114556	Fig. 3
PMID:38780300	PBO:0114571	Fig. 3
PMID:38780300	PBO:0114555	Fig. 3
PMID:38780300	PBO:0114558	Fig. 3
PMID:38780300	PBO:0114558	Fig. 3
PMID:38780300	PBO:0114570	Fig. 3
PMID:38780300	PBO:0114569	Fig. 3
PMID:38780300	PBO:0114565	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:0114588	Fig. 3
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	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	PBO:0113835	we did not detect Csc1-R31A-GFP on SPBs at any point in the cell cycle (Figure 1C).
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 wildtype 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 wildtype cells (Figure S1B).
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 wildtype cells (Figure S1B).
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	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	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: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	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: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 wildtype 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 wildtype cells (Figure 4B). This further demonstrates that ppa3-D82N is a loss of function allele.
PMID:38865179	PBO:0113841	In both wildtype 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 wildtype 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 wildtype anaphase cells (Figure 2, A and B).
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:0000582	(Fig. 2D)
PMID:38889144	PBO:0114681	(Fig. 2)
PMID:38889144	PBO:0114681	(Fig. 2)
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:38899862	FYPO:0000080	Fig. 3A
PMID:38899862	PBO:0094808	Fig. 7
PMID:38899862	PBO:0094808	Fig. 7
PMID:38899862	PBO:0113888	Fig. 7
PMID:38899862	PBO:0113889	Fig. 7
PMID:38899862	PBO:0113889	Fig. 7
PMID:38899862	PBO:0113890	Fig. 7
PMID:38899862	PBO:0113891	Fig. 7
PMID:38899862	PBO:0113891	Fig. 7
PMID:38899862	PBO:0113892	Fig. 7
PMID:38899862	PBO:0113892	Fig. 7
PMID:38899862	FYPO:0006658	Fig. 12
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	PBO:0113893	Fig. S1B
PMID:38899862	PBO:0093560	Fig. S2A
PMID:38899862	PBO:0093560	Fig. S2A
PMID:38899862	FYPO:0001357	Fig. S2B
PMID:38899862	FYPO:0001357	Fig. S2B
PMID:38899862	PBO:0113894	Fig. S3
PMID:38899862	PBO:0113894	Fig. S3
PMID:38899862	PBO:0113895	Fig. S3
PMID:38899862	PBO:0113896	Fig. S3
PMID:38899862	PBO:0113897	Fig. S3
PMID:38899862	PBO:0113898	Fig. S3
PMID:38899862	PBO:0113899	Fig. S3
PMID:38899862	PBO:0113900	Fig. S3
PMID:38899862	PBO:0113901	Fig. S3
PMID:38899862	PBO:0113902	Fig. S3
PMID:38899862	PBO:0094841	Fig. S3
PMID:38899862	PBO:0113895	Fig. S3
PMID:38899862	PBO:0113896	Fig. S3
PMID:38899862	PBO:0113897	Fig. S3
PMID:38899862	PBO:0113898	Fig. S3
PMID:38899862	PBO:0113899	Fig. S3
PMID:38899862	PBO:0113900	Fig. S3
PMID:38899862	PBO:0113901	Fig. S3
PMID:38899862	PBO:0113902	Fig. S3
PMID:38899862	PBO:0094841	Fig. S3
PMID:38899862	PBO:0113903	Fig. S3
PMID:38899862	PBO:0113903	Fig. S3
PMID:38899862	PBO:0094831	Fig. S3
PMID:38899862	PBO:0113904	Fig. S3
PMID:38899862	PBO:0113905	Fig. S3
PMID:38899862	PBO:0113906	Fig. S3
PMID:38899862	PBO:0113907	Fig. S3
PMID:38899862	PBO:0113906	Fig. S3
PMID:38899862	PBO:0113907	Fig. S3
PMID:38899862	PBO:0113908	Fig. S3
PMID:38899862	PBO:0113908	Fig. S3
PMID:38899862	PBO:0113909	Fig. S3
PMID:38899862	PBO:0113910	Fig. S3
PMID:38899862	PBO:0113910	Fig. S3
PMID:38899862	PBO:0113911	Fig. S3
PMID:38899862	PBO:0113911	Fig. S3
PMID:38899862	PBO:0094850	Fig. S3
PMID:38899862	PBO:0113912	Fig. S3
PMID:38899862	PBO:0113912	Fig. S3
PMID:38899862	PBO:0113913	Fig. S3
PMID:38899862	PBO:0113914	Fig. S3
PMID:38899862	PBO:0113915	Fig. S3
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	PBO:0113916	Fig. S3
PMID:38899862	PBO:0113917	Fig. S3
PMID:38899862	PBO:0113918	Fig. S3
PMID:38899862	PBO:0094844	Fig. S3
PMID:38899862	PBO:0094833	Fig. S3
PMID:38899862	FYPO:0001357	Fig. 6D
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, 6D (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:0113913	Fig. S3
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:0094774	Fig. 5
PMID:38899862	PBO:0094776	Fig. 5
PMID:38899862	FYPO:0001357	Fig. S4
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	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:0114449	Fig. 4
PMID:38913087	PBO:0114452	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:38913087	PBO:0114445	Fig. 5
PMID:38913087	PBO:0114453	Fig. 5
PMID:38913087	PBO:0114453	Fig. 5
PMID:38913087	PBO:0114453	Fig. 5
PMID:38913087	PBO:0114453	Fig. 5
PMID:38913087	PBO:0114453	Fig. 5
PMID:38913087	PBO:0114442	Table 2
PMID:38913087	PBO:0114444	Fig. 3
PMID:38913087	PBO:0114448	Fig. 3
PMID:38913087	PBO:0114444	Fig. 3
PMID:38913087	PBO:0114446	Fig. 2
PMID:38913087	PBO:0114447	Fig. 2
PMID:38913087	PBO:0114448	Fig. 4
PMID:38913087	PBO:0114448	Fig. 4
PMID:38913087	PBO:0114449	Fig. 4
PMID:38913087	PBO:0114449	Fig. 4
PMID:38913087	PBO:0114442	Fig. 6C
PMID:38913087	PBO:0114443	Fig. 6D
PMID:38913087	PBO:0114450	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:0114444	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:0114443	Fig. 6G
PMID:38913087	FYPO:0000280	Fig. 6H
PMID:38913087	FYPO:0000280	Fig. 6I
PMID:38913087	FYPO:0000280	Fig. 6J
PMID:38913087	PBO:0114442	Fig. 6F
PMID:38913087	PBO:0114444	Fig. 2
PMID:38913087	PBO:0114445	Fig. 2
PMID:38913087	PBO:0114446	Fig. 2
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:0114447	Fig. 2
PMID:38913087	PBO:0114454	Table 2
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:0114451	Fig. 4
PMID:38913087	PBO:0114445	Fig. 4
PMID:38913087	PBO:0114446	Fig. 5
PMID:38913087	PBO:0114447	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:0114442	Table 2
PMID:38913087	PBO:0114448	Fig. 5
PMID:38917328	PBO:0093618	Fig. S1A
PMID:38917328	PBO:0093617	Fig. S1A
PMID:38917328	PBO:0093580	Fig. S1A
PMID:38917328	PBO:0093579	Fig. S1A
PMID:38917328	PBO:0093580	Fig. S1A
PMID:38917328	PBO:0093580	Fig. S2A
PMID:38917328	PBO:0093581	Fig. S1A
PMID:38917328	PBO:0093613	Fig. S1A
PMID:38917328	PBO:0093614	Fig. S1A
PMID:38917328	FYPO:0007255	Fig. 1B and C
PMID:38917328	PBO:0114208	Fig. S6B
PMID:38917328	PBO:0114207	Fig. 4C
PMID:38917328	PBO:0114198	Fig. 3C
PMID:38917328	PBO:0093613	Fig. S2A
PMID:38917328	FYPO:0004003	Fig. S1B
PMID:38917328	PBO:0093586	Fig. S1A
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	PBO:0114211	Fig. 3A
PMID:38917328	PBO:0114211	Fig. 3A
PMID:38917328	PBO:0114210	Fig. 3A
PMID:38917328	PBO:0114198	Fig. 3C
PMID:38917328	PBO:0114201	Fig. 5D and E
PMID:38917328	PBO:0114199	Fig. 5A
PMID:38917328	PBO:0114200	Fig. 6A and D
PMID:38917328	FYPO:0006320	Fig. 2B
PMID:38917328	FYPO:0006320	Fig. 2B
PMID:38917328	PBO:0114199	Fig. 2B
PMID:38917328	PBO:0114199	Fig. 2B
PMID:38917328	PBO:0114209	Fig. 3A
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	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	FYPO:0006320	Fig. 5C
PMID:38917328	FYPO:0006320	Fig. 5C
PMID:38917328	PBO:0114206	Fig. 3A and B
PMID:38917328	PBO:0114205	Fig. 3B
PMID:38917328	PBO:0114205	Fig. 3B
PMID:38917328	PBO:0114204	Fig. S6D
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:0114200	Fig. 6A
PMID:38917328	PBO:0114200	Fig. 6D
PMID:38917328	PBO:0093587	Fig. S2A
PMID:38917328	PBO:0114199	Fig. 5E
PMID:38917328	PBO:0114202	Fig. 5D
PMID:38917328	PBO:0093616	Fig. S2A
PMID:38917328	FYPO:0006320	Fig. 5C
PMID:38917328	PBO:0114209	Fig. 3A
PMID:38917328	PBO:0093616	Fig. S1A
PMID:38917328	GO:0120292	Thus, Alm1 and Nup60 promote RDR in a pre- and post-anchoring manner, respectively.
PMID:38917328	FYPO:0004003	Fig. S1B
PMID:38917328	PBO:0114202	Fig. 5D
PMID:38940614	PBO:0093561	Fig. S1
PMID:38940614	PBO:0114197	Fig. 11
PMID:38940614	PBO:0114197	Fig. 11
PMID:38940614	PBO:0114196	Fig. 11
PMID:38940614	FYPO:0008286	Fig. 11
PMID:38940614	FYPO:0008285	Fig. 11
PMID:38940614	FYPO:0008285	Fig. 11
PMID:38940614	PBO:0114195	Fig. 11
PMID:38940614	PBO:0114195	Fig. 11
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	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: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	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: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: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:0001575	Fig. 10
PMID:38940614	FYPO:0001575	Fig. 10
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:0001357	Fig. 9
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:38985524	PBO:0114094	We found that mNG-Cam1 could not local- ize 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: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: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 nega- tive, 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:0114102	Similarly, we would expect overexpressed GFP-M+C to bind endoge- nous Pcp89 at the SPB to form larger SPBs and this was also observed (Supplemental Figure S1B).
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 overex- pressed, 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 ob- served 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:0114105	Additionally, while GFP-Pcp1(PACT) localized at the SPB, GFP-Pcp1(PACT-I1151A) was diffuse throughout the cy- tosol and nucleus (Figure 6D)
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:0114097	Pcp1 accumu- lated in enlarged Ppc89-containing structures upon overproduc- tion 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 ob- served 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:38989013	FYPO:0000082	All temperature-sensitive alleles grew less than wildtype at 36°C with the cdc16-C1 allele showing the greatest temperature-sensitivity (Figure 1I).
PMID:38989013	FYPO:0000082	All temperature-sensitive alleles grew less than wildtype at 36°C with the cdc16-C1 allele showing the greatest temperature-sensitivity (Figure 1I).
PMID:38989013	FYPO:0002002	(Figure 1H)
PMID:38989013	FYPO:0002049	(Figure 1E)
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 revealed that sid1-L2 had an intermediate restrictive temperature compared to sid1-125 and sid1-239 (Figure 1F).
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 wildtype at 36°C with the cdc16-C1 allele showing the greatest temperature-sensitivity (Figure 1I).
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:0000118	(figure 1H)
PMID:39010328	FYPO:0002672	Fig. 2A
PMID:39010328	PBO:0093561	Fig. 2B
PMID:39010328	PBO:0093561	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: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:0114118	Fig. 3C
PMID:39010328	PBO:0114120	Fig. 3C
PMID:39010328	PBO:0105134	Fig. 4B
PMID:39010328	PBO:0105134	Fig. 4B
PMID:39010328	PBO:0105134	Fig. 2C
PMID:39010328	FYPO:0001357	Fig. 4A
PMID:39010328	FYPO:0001357	Fig. 4A
PMID:39010328	PBO:0114119	Fig. 1C
PMID:39010328	PBO:0099989	Fig. 1B
PMID:39010328	PBO:0114118	Fig. 3D
PMID:39010328	FYPO:0001357	Fig. 2A and B
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:0114121	Fig. 4B
PMID:39010328	PBO:0114121	Fig. 4B
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	PBO:0093560	Fig. 4A
PMID:39010328	PBO:0105134	Fig. 4B
PMID:39010328	PBO:0093560	Fig. 4A
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:0093561	Fig. 2B
PMID:39010328	FYPO:0001357	Fig. 2A and B
PMID:39010328	FYPO:0002672	Fig. 2A
PMID:39010328	FYPO:0001357	Fig. 2B
PMID:39010328	FYPO:0001357	Fig. 2B
PMID:39010328	PBO:0105131	Fig. 2C
PMID:39010328	PBO:0093560	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:39012625	PBO:0114125	Fig. 1
PMID:39012625	PBO:0114123	Fig. 7G
PMID:39012625	PBO:0114133	Fig. 7A and B
PMID:39012625	FYPO:0000422	Fig. 9
PMID:39012625	PBO:0114132	The pak1-ts cells are characteristically mono- polar; 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	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	GO:0045807	Interestingly, we also find that Pak1 is required for normal endocytic patch dynamics. Fig. 9
PMID:39012625	PBO:0114124	Fig. 7C and D
PMID:39012625	PBO:0114131	Fig. 5A
PMID:39012625	PBO:0114130	Fig. 4A
PMID:39012625	PBO:0114129	Fig. 4A
PMID:39012625	PBO:0114128	Fig. 4A
PMID:39012625	PBO:0114127	Fig. S1C and D
PMID:39012625	PBO:0114126	Fig. S1A and B
PMID:39016088	PBO:0114649	Fig. 2 TBZ sensitivity testing for wild-type, 9A, and 9D
PMID:39016088	PBO:0114649	Fig. 2 TBZ sensitivity testing for wild-type, 9A, and 9D
PMID:39016088	PBO:0114620	The defect was observed in rec12-deletion rec8-2A mutant background. Fig 3C.
PMID:39016088	PBO:0114621	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:39105351	PBO:0114816	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: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	FYPO:0001355	he induction of sdr1+ expression, yeast cell growth was significantly suppressed (Figure 2d), indicating that excessive expression of sdr1+ plays an active role in sup- pressing yeast cell growth.
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: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: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	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: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: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	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: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 environ- ment (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 environ- ment (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 con- firms the occurrence of autophagy (Figure 2a).
PMID:39105351	PBO:0114814	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	FYPO:0008320	Although the morphological abnormalities of Δsdr1 cells under sulfur depletion were rectified by overexpres- sing sdr1+, those of Δecls cells were not (Figure 5).
PMID:39105351	PBO:0114815	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	FYPO:0007592	autophagy was triggered in ΔSPCC417.09c cells under nitrogen depletion but not under sulfur depletion.
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	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:0114820	Contrary to our predic- tion, the presence or absence of sdr1+ did not have signif- icant effect on atg1+ and atg20+ induction by sulfur starvation.
PMID:39105351	PBO:0114819	Contrary to our predic- tion, the presence or absence of sdr1+ did not have signif- icant effect on atg1+ and atg20+ induction by sulfur starvation.
PMID:39174851	FYPO:0000478	(Fig. 4A and Fig. S2)
PMID:39174851	PBO:0097898	(Fig. 7D)
PMID:39174851	PBO:0114697	(Fig. S3C)
PMID:39174851	PBO:0114691	(Fig. 5)
PMID:39174851	PBO:0114697	(Fig. S3C)
PMID:39174851	PBO:0114705	(Fig. 5)
PMID:39174851	PBO:0114697	(Fig. S3C)
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	PBO:0114703	(Fig. 1B and 2C)
PMID:39174851	PBO:0114693	(Fig. 7C)
PMID:39174851	PBO:0097905	(Fig. 7C)
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:0114702	(Fig. 1 and 5)
PMID:39174851	FYPO:0008305	(Fig. 6)
PMID:39174851	FYPO:0000478	(Fig. 4A and Fig. S2)
PMID:39174851	PBO:0095338	(Fig. 7D)
PMID:39174851	PBO:0114701	(Fig. 7A)
PMID:39174851	PBO:0114701	(Fig. 7A)
PMID:39174851	PBO:0095337	(Fig. 7D)
PMID:39174851	PBO:0095337	(Fig. 7D)
PMID:39174851	PBO:0097898	(Fig. 7D)
PMID:39174851	PBO:0097898	(Fig. 7D)
PMID:39174851	PBO:0114700	(Fig. 7A)
PMID:39174851	PBO:0114700	(Fig. 7A)
PMID:39174851	PBO:0114699	(Fig. 7A)
PMID:39174851	PBO:0114698	(Fig. 3A)
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:0114696	(Fig. S4C)
PMID:39174851	PBO:0106083	(Fig. 4 and Fig. EV2)
PMID:39174851	PBO:0114695	(Fig. S4B)
PMID:39174851	PBO:0101665	(Fig. S4A)
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:0114693	(Fig. 7C)
PMID:39174851	PBO:0114690	(Fig. EV4)
PMID:39174851	FYPO:0008303	(Fig. 4A and Fig. EV2)
PMID:39174851	PBO:0114692	(Fig. 3A and Fig. EV1A)
PMID:39174851	PBO:0114691	(Fig. 4A and Fig. EV2 and EV3)
PMID:39174851	FYPO:0004993	(Fig. 7D)
PMID:39174851	PBO:0105184	(Fig. 3B)
PMID:39174851	FYPO:0003891	(Fig. 3C)
PMID:39174851	PBO:0114690	(Fig. EV4)
PMID:39174851	PBO:0106083	(Fig. 4A and Fig. EV2)
PMID:39174851	PBO:0114689	(Fig. 3A and Fig. EV1A)
PMID:39174851	PBO:0114688	(Fig. 4A and Fig. EV2 and EV3)
PMID:39174851	FYPO:0004993	(Fig. 7D)
PMID:39174851	PBO:0095390	(Fig. 3C)
PMID:39174851	PBO:0095386	(Fig. 3B)
PMID:39174851	PBO:0097898	(Fig. 7D)
PMID:39174851	PBO:0097898	(Fig. 7D)
PMID:39174851	PBO:0114693	(Fig. 7C)
PMID:39174851	PBO:0114693	(Fig. 7C)
PMID:39174851	PBO:0114707	(Fig. 7A)
PMID:39174851	PBO:0114707	(Fig. 7A)
PMID:39174851	PBO:0114706	(Fig. 7A)
PMID:39174851	FYPO:0003176	Fig. 7A
PMID:39174851	FYPO:0003176	Fig. 7A
PMID:39174851	FYPO:0008305	(Fig. 6)
PMID:39174851	PBO:0114705	(Fig. 5)
PMID:39174851	FYPO:0000478	(Fig. 4A and Fig. S2)
PMID:39239853	PBO:0114516	Its3-mNG was increased at the septum in scs2Δ scs22Δ cells compared to wildtype cells by ~50% without a change in the lateral cortex levels (Fig. 7A-C).
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	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:0114519	There was no change in Its3-mNG septum intensity in duc1Δ cells compared to wildtype, as expected (Fig. S4E).
PMID:39239853	PBO:0114507	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 wildtype cells (Fig. S2A).
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 wildtype (Fig. 5A,B). These results are consistent with Duc1 requiring PM PI(4,5)P2 for its PM localization.
PMID:39239853	PBO:0114514	(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 wildtype (Fig. 5A,B).
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	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 wildtype (Fig. 6D-F).
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 wildtype cells (Fig 6G,H and Fig. S4C,D)
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	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 wildtype (Fig. 7D-F).
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	PBO:0114508	We also examined if Scs2 or Scs22 alone was responsible for preventing Duc1 division site localization but, as in wildtype 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 wildtype 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 wildtype 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 wildtype cells (Fig 6G,H and Fig. S4C,D)
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 wildtype cells (Fig. S2A).
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 wildtype 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 wildtype 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 wildtype cells (Fig. S2A).
PMID:39239853	PBO:0114510	In contrast to its exclusion from the division site in wildtype 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:0114510	Analysis of Duc1-mNG localization showed that, unlike in wildtype cells, Duc1- mNG localized at the septum in scs2-T39A,T40A scs22Δ cells (Fig. 4F).
PMID:39239853	PBO:0114511	(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	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	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	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	PBO:0114513	Live-cell imaging revealed that over-production of Duc1 indeed reduced Opy1-mNG at the PM by ~35% (Fig. 5C,D).
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: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: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: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: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	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	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	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: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	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	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: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	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: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: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: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	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	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	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	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:0114633	Our results showed that the expression of Cob1, Cox1, Cox2, Cox3, and Atp6 were greatly reduced in ∆shy1 cells (Fig. 5d).
PMID:39333500	PBO:0114720	(Fig. 2B)
PMID:39333500	PBO:0093559	(Fig. 2H)
PMID:39333500	PBO:0114716	(Fig. 2B)
PMID:39333500	PBO:0114718	(Fig. 2E and F)
PMID:39333500	PBO:0114719	(Fig. 2E and F)
PMID:39333500	PBO:0114717	(Fig. 2B)
PMID:39333500	PBO:0094949	(Fig. 2H)
PMID:39333500	PBO:0114715	(Fig. 2E)
PMID:39333500	FYPO:0002059	(Fig. 2G)
PMID:39333500	PBO:0098563	Fig. 4C
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: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	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	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 wildtype (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 wildtype (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 wildtype (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 wildtype (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 wildtype 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 wildtype 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	PBO:0114845	we also observed a reduction 3 in Mto2-mNG SPB signal at 36 ̊C in ppc89-3 and ppc89-4 compared to wildtype (Figure 4 S2D,E).
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	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	PBO:0114845	we also observed a reduction 3 in Mto2-mNG SPB signal at 36 ̊C in ppc89-3 and ppc89-4 compared to wildtype (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	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	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: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 wildtype (Figures 1E, F and 13 S1A).
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: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: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	PBO:0093556	ppc89(1-707)-mNG cells were 7 viable but temperature-sensitive (Figure 3C).
PMID:39471327	PBO:0093558	ppc89-2, ppc89-3 and ppc89-4 grow 19 similarly to wildtype 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 wildtype 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 wildtype at 25°C but do not form colonies at 36°C (Figure 1B
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: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	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: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	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	PBO:0114847	Pcp1 showed ~50% 9 reduction in pcp89-4 cells (Figure S3C)
PMID:4154968	GO:0004354	"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	activated by ATP
PMID:4698209	GO:0004794	inhibited_by CHEBI:17191
PMID:4698210	GO:0003984	inhibited_by CHEBI:27266
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: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:4821071	GO:0003984	activated_by FAD , inhibited_by L-valine
PMID:6094012	FYPO:0001972	parent child relationship with term above requested
PMID:6094012	FYPO:0000134	actually this only occurs in 30% of cells.. I don't know if it is viable or inviable
PMID:6526818	PBO:0114639	inhibited by methionine
PMID:6828164	FYPO:0000400	fig1A The transition point for cdc2 is 0.65 using cdc2.33
PMID:6828164	FYPO:0003449	fig1A 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	PBO:0095711	cell size at septation is 8.5µm
PMID:6828164	FYPO:0002516	TP. 0.33
PMID:6828164	PBO:0093767	cell size at separation is 16.7µm compared to 12.8µm for wild type
PMID:6828164	PBO:0094266	cell size at separation is 22.4µm compared to 12.8µm for wild type
PMID:6828164	PBO:0095711	cell size at septation is 9.6µm
PMID:6828164	PBO:0095711	cell size at septation is 10.3µm
PMID:6828164	PBO:0095711	cell size at septation is 8.4µm
PMID:6828164	PBO:0095711	cell size at septation is 8.9µm
PMID:6828164	FYPO:0000400	fig1A 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	FYPO:0000400	fig1A The transition point for cdc2 is 0.68 using cdc2.L7
PMID:6828164	FYPO:0000400	"fig1A 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 (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:0000400	fig1A The transition point for cdc2 (0.74) is not advanced using a cdc2.M35 wee1.6 mutant
PMID:6828164	FYPO:0000400	fig1A Table 1 cdc13 transition point (0.78) is not advanced in a cdc13-117 wee1.6 mutant
PMID:6828164	PBO:0095711	cell size at septation is 8.9µm
PMID:6828164	PBO:0095711	cell size at septation is 8.7µm
PMID:6828164	PBO:0095711	cell size at septation is 9.5µm in cdc2-1w (9.7µm in cdc2-2w)
PMID:6828164	FYPO:0000400	fig1A The transition point for cdc2 is 0.65 using cdc2.M26
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	The transition point for cdc2 is advanced from 0.65 to 0.53 using a cdc2.M26 wee1.6 mutant
PMID:6828164	FYPO:0003449	fig1A The transition point for cdc2 is advanced from 0.69 to 0.48 using a cdc2.33 wee1 [more...]
PMID:6828164	FYPO:0000400	fig1A The transition point for cdc2 is 0.65 using cdc2.M55
PMID:6828164	FYPO:0000400	fig1A The transition point for cdc2 is 0.66 using cdc2.M35
PMID:6828164	FYPO:0002516	???
PMID:6828164	FYPO:0000400	fig1A
PMID:6828164	FYPO:0000400	fig1A 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:0000400	fig1A Table 1 cdc13 transition point is 0.69 using a cdc13-117 mutant
PMID:6828164	FYPO:0000400	fig1A The transition point for cdc2 is 0.70 using cdc2.M63
PMID:6828164	FYPO:0000400	fig1A TTable 1 cdc27 transition point is 0.62 using a cdc27.K3 mutant
PMID:6828164	FYPO:0003449	fig1A 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	fig1A The transition point for cdc2 (0.68) is not advanced using a cdc2.M63 wee1.6 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:689088	FYPO:0006822	at division
PMID:6943408	FYPO:0003485	After release from HU block, cells can undergo one round of division without DNA replication
PMID:6943408	FYPO:0001248	abolished
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:0003738	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	After release from HU block, cells can undergo one round of division without DNA replication
PMID:6943408	FYPO:0000608	Cells able to undergo normal DNA replication and enter cell division, but fail to divide.
PMID:6943408	FYPO:0001982	Cells unable to divide, even after DNA replication is completed
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: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:0001982	Cells unable to divide, even after DNA replication is completed
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:0003485	After release from HU block, cells can undergo one round of division without DNA replication
PMID:6943408	FYPO:0003485	After release from HU block, cells can undergo one round of division without DNA replication
PMID:6943408	FYPO:0000608	Cells able to undergo normal DNA replication and enter cell division, but fail to divide.
PMID:6961452	GO:0004070	This was really IGI complemetnation of E-coli pyrB
PMID:7262540	PBO:0101531	cells septate at 58% of wild type diploid length
PMID:7262540	PBO:0101534	cells divide at 11% 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:7262540	PBO:0101535	cells divide at 7% longer than wild diploid cells at division
PMID:7262540	PBO:0101531	cells divide at 82% of wild diploid size at division
PMID:7262540	PBO:0101531	cells divide at 56% of the size at division of wild type diploids
PMID:7262540	PBO:0101531	Cells divide at 65% of wild type diploid cell length
PMID:7262540	PBO:0101533	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 10.2µm at 25°C
PMID:7262540	PBO:0101532	cells divide at 22.4µm at 25°C
PMID:7262540	PBO:0101531	cdc2-1w was previously called wee2-1
PMID:7262540	PBO:0101531	cells septate at 58% of wild type diploid length
PMID:7262540	PBO:0101531	cells septate at 56% of wild type diploid length
PMID:7262540	PBO:0101531	cells divide at 51% of control cell length at division
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 septate at 87% 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 85% of wild type diploid length
PMID:7262540	PBO:0101531	cells septate at 82% of wild type diploid length
PMID:7262540	PBO:0101531	cells septate at 81% of wild type diploid length
PMID:7262540	PBO:0101534	cells divide at 16.7µm at 25°C
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:0101536	cells divide at 8% 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: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 septate at 52% of wild type diploid length
PMID:7262540	PBO:0101531	cells septate at 54% of wild type diploid length
PMID:7498507	GO:0004725	activated_by(CHEBI:16356)
PMID:7501024	FYPO:0001490	non-ionic osmotic stress
PMID:7501024	FYPO:0001490	salt stress
PMID:7501024	FYPO:0001490	salt stress
PMID:7501454	GO:0003697	higher affinity during S phase than G2/M
PMID:7501454	MOD:00046	hyperphosphorylated in late S phase; phosphorylated on different sites in S versus G2/M
PMID:7501454	GO:0003887	constant throughout cell cycle
PMID:7559598	PBO:0097547	not shown
PMID:7559598	FYPO:0000280	not shown
PMID:7596817	FYPO:0003696	polysome profile
PMID:7596817	FYPO:0003695	polysome profile
PMID:7622618	FYPO:0000280	evidence is essentially IC, as I inferred sterility from the lack of shmoo formation (h- cells)
PMID:7626804	PBO:0099202	Fig 4A middle panel cells average size 11.6µm This strain is a gene replacement of cdc2+
PMID:7626804	PBO:0099200	Fig1A
PMID:7626804	MOD:00047	Fig1D peptide 3
PMID:7626804	PBO:0099201	Fig1D peptide 3 and peptide1
PMID:7626804	MOD:00047	Fig1D peptide 2
PMID:7626804	PBO:0094620	Fig3 chk1 1 is not required for T14 phosphorylation by wee1
PMID:7626804	FYPO:0000648	Table 2 cdc2-T14A is present on multicopy plasmid cells are viable but have a semi wee phenotype
PMID:7626804	FYPO:0002176	Table 2 cdc2-T14A is present on multicopy plasmid cells are viable and have a normal cell size phenotype
PMID:7626804	PBO:0093767	Fig 4A right panel cells average size 16.6µm This strain is a gene replacement of cdc2+
PMID:7626804	PBO:0099203	Fig 4B absence of peptide 3 This strain is a gene replacement of cdc2+
PMID:7626804	PBO:0099204	Fig 4B middle right panel presence of peptide 3 This strain is a gene replacement of cdc2+
PMID:7626804	PBO:0099205	Fig 4B absence of peptide 3 Overexpression of wee1 does not phosphorylate T14A residue. This strain is a gene replacement of cdc2+
PMID:7626804	PBO:0099206	Fig 4B increased peptide 3 compared to when wee1 is not overexpressed . This strain is a gene replacement of cdc2+
PMID:7626804	PBO:0099207	Fig5 B wee1 is necessary for T14 phosphorylation no peptide 3 is observed when wee1 is deleted
PMID:7626804	PBO:0099208	Fig7A,B At restrictive temperature T14 is not phosphorylated (no peptide when cells blocked at RT.)
PMID:7626804	PBO:0099209	Fig7A, B At shift to permissive temperature T14 becomes phosphorylated. Peptide 3 is only present at low stoichiometry
PMID:7626804	FYPO:0001706	Fig8
PMID:7626804	FYPO:0002102	Fig8
PMID:7626804	PBO:0099210	data not shown
PMID:7626804	PBO:0094619	Fig1B, C and D x = a small phospho peptide of T14Y15. T14 phosphorylation only occurs when wee1 is overexpressed
PMID:7651412	FYPO:0003735	switches specificity from direct repeats to inverted repeats
PMID:7651414	PBO:0105935	matmi and matpi
PMID:7651414	PBO:0105936	matmi and matpi
PMID:7651414	PBO:0105934	matmi and matpi
PMID:7651414	PBO:0105934	matmi and matpi
PMID:7651414	PBO:0105935	matmi and matpi
PMID:7657164	PBO:0094488	residue not determined, but probably Y173
PMID:7687541	GO:0005737	fig4
PMID:7706287	FYPO:0002522	assayed for bulk poly(A)+ RNA
PMID:7706287	FYPO:0000911	assayed for bulk poly(A)+ RNA
PMID:7706287	FYPO:0000400	arrest point determined by H1 kinase activity peak
PMID:7739540	FYPO:0001430	(Figure 3b)
PMID:7739540	FYPO:0001430	(Figure 3b)
PMID:7739540	FYPO:0001430	(Figure 3b)
PMID:7773104	FYPO:0005472	NADP-GDH-defective
PMID:7774573	PBO:0037522	pREP5-DL45 is integrated. cdc2+ is expressed from its own promoter on a multi copy plasmid
PMID:7774573	PBO:0037522	pREP5-DL41 is integrated. cdc2+ is expressed from its own promoter on a multi copy plasmid
PMID:7774573	PBO:0106643	pREP41cdc2-DL50 is integrated
PMID:7774573	PBO:0037520	pREP5cdc2+ is integrated. 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:0037519	pREP41cdc2-DL50 is integrated
PMID:7774573	PBO:0037506	pREP5cdc2-DL41 is integrated. cdc2-DL45 has same phenotype but it is not clear if it is under the same conditions
PMID:7774573	PBO:0037510	abnormal mitotic arrest with 4C DNA content Cells undergo an extra round of DNA replication without undergoing cytokinesis pREP5cdc2-DL41 is integrated. cdc2-DL45 has same phenotype but it is not clear if it is under the same conditions
PMID:7774573	PBO:0037507	pREP5cdc2-DL41 is integrated. cdc2-DL45 has same phenotype but it is not clear if it is under the same conditions
PMID:7774573	PBO:0106642	pREP5cdc2-DL41 is integrated.cdc2-DL45 has same phenotype but it is not clear if it is under the same conditions. Abnormal septum phenotype include misplace septum, multi septa and partially formed septa
PMID:7774573	PBO:0037511	child term of abnormal regulation of mitotic metaphase/anaphase transition. pREP5cdc2-DL41 is integrated. cdc2-DL45 has same phenotype but it is not clear if it is under the same conditions
PMID:7774573	PBO:0096052	pRIP45cdc2-DL41 is integrated
PMID:7774573	PBO:0037518	pREP41cdc2-DL50 is integrated
PMID:7774573	PBO:0093712	pREP41cdc2-DL50 is integrated
PMID:7774573	PBO:0095634	pIRT2suc1 multi copy plasmid partially rescues the pREP5cdc2-DL41 integrant mitotic arrest phenotype and allows formation of micro colonies. cdc2-DL45 is also partially rescued but it is not clear whether this is under the same conditions
PMID:7774573	PBO:0037516	pREP41cdc2-DL45 is a multi copy plasmid. No data shown
PMID:7774573	PBO:0037512	pREP5cdc2-DL41 is integrated. cdc2-DL45 has same phenotype but it is not clear if it is under the same conditions
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:0097954	pRIP45DL45 is integrated. cdc2-DL41 has same phenotype but it is not clear if it is under the same conditions. Figure 6B 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:0037515	pREP41cdc2-DL41 is a multi copy plasmid . No data shown
PMID:7774573	PBO:0037516	pREP41cdc2-DL41 is a multi copy plasmid . No data shown
PMID:7774573	PBO:0037509	pREP5cdc2-DL41 is integrated. cdc2-DL45 has same phenotype but it is not clear if it is under the same conditions
PMID:7774573	PBO:0037519	pREP41-DL50 is integrated
PMID:7774573	PBO:0096052	pRIP45cdc2-DL45 is integrated
PMID:7774573	PBO:0096053	pRIP45cdc2+ is integrated
PMID:7774573	PBO:0037515	pREP41cdc2-DL45 is a multi copy plasmid . No data shown
PMID:7796804	PBO:0104265	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:0023774	Figure 1, 4,5
PMID:7796804	PBO:0104261	Fig5A
PMID:7796804	PBO:0104268	Fig7B. 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:0104269	Fig7C
PMID:7796804	PBO:0097659	Fig 6 middle panels Fig7B panel 4 cells examined 7 hour after refeeding with nitrogen
PMID:7796804	PBO:0104270	Figure 1, 4,5
PMID:7796804	PBO:0097558	Fig 6 middle panels Fig7B panel 3 cells examined 7 hour after refeeding with nitrogen
PMID:7796804	PBO:0100985	Fig 6 top panels, Fig7B panel 1 cells examined 7 hour after refeeding with nitrogen
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:0102115	Fig7A panel 5
PMID:7796804	PBO:0104261	Fig7A 8,
PMID:7796804	PBO:0104264	Fig 5B cdc22-M45 blocks in G1/S
PMID:7796804	PBO:0104264	Fig 5B cdc22-M45 blocked in G1/S
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:7796804	PBO:0104262	Fig 5A
PMID:7796804	PBO:0104262	Fig 5A
PMID:7796804	PBO:0099448	Figure 1, 4,5
PMID:7796804	PBO:0099447	Figure 1, 4,5
PMID:7796804	PBO:0102115	Fig7A panel 3
PMID:7796804	PBO:0104265	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:0037896	Fig 7C
PMID:7796804	PBO:0097659	Fig 6, Fig7B panel 8,
PMID:7796804	PBO:0104266	Fig7A panel 1
PMID:7796804	PBO:0104261	Fig7A panel 2
PMID:7796804	PBO:0037896	Fig 7C
PMID:7796804	PBO:0104267	Fig5B cdc10-129 cells blocked in G1
PMID:7796804	PBO:0104261	Fig7A panel 6
PMID:7796804	PBO:0104261	Fig7A panel 4
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: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:7798319	FYPO:0002303	Consistently, the phenotype of cut9-T98 was indistinguishable from that of cut9-665
PMID:7813446	FYPO:0001355	not arrested like wee1+ overexp alone
PMID:7813446	FYPO:0001355	not arrested like wee1-50 overexp alone
PMID:7813446	FYPO:0001355	not arrested like wee1-50 overexp alone
PMID:7813446	PBO:0094967	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	endoglycosidase-H cleaves N-linked glycosylation
PMID:7883794	PBO:0106429	Fig1 B
PMID:7883794	PBO:0106431	Figure 2B
PMID:7883794	PBO:0102251	Table 1, Figure 1B appearance of IC peak at early timepoint
PMID:7883794	FYPO:0005773	Data not shown
PMID:7883794	PBO:0106430	Figure 1A
PMID:7883794	PBO:0106434	Figure 3B
PMID:7883794	PBO:0023560	Figure 3A
PMID:7883794	PBO:0106433	Table 1, Figure 2C
PMID:7883794	PBO:0106432	Figure 2C
PMID:7889932	GO:0000287	crystal structure
PMID:7903653	FYPO:0000249	ABOLISHED
PMID:7903653	FYPO:0000249	ABOLISHED
PMID:7903653	FYPO:0000249	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	3 kb transcript
PMID:7916653	FYPO:0001490	deletion with expressed plasmid, after plasmid loss
PMID:7916658	FYPO:0001355	constitutive cdc18+ expression
PMID:7916658	PBO:0105614	inferred from combination of phenotype shown in this paper with background knowledge
PMID:7916658	FYPO:0000012	constitutive cdc18+ expression
PMID:7916658	FYPO:0001492	constitutive cdc18+ expression
PMID:7923372	PBO:0103991	they interacted in the Y2H experiment, so inferring this relationship
PMID:7957097	PBO:0099590	inhibits
PMID:7957097	FYPO:0004922	no mitotic spindle
PMID:7957098	FYPO:0001933	same as rad4 cut5 allele alone
PMID:7957098	FYPO:0001933	same as rad4 cut5 allele alone
PMID:7957098	FYPO:0001933	same as rad4 cut5 allele alone
PMID:7957098	FYPO:0001933	same as rad4 cut5 allele alone
PMID:7957098	FYPO:0001933	same as rad4 cut5 allele alone
PMID:7957098	FYPO:0001933	same as rad4 cut5 allele alone
PMID:7957098	FYPO:0001933	same as rad4 cut5 allele alone
PMID:7957098	FYPO:0001916	same as cdc25-22 alone
PMID:7957098	FYPO:0001933	same as rad4 cut5 allele alone
PMID:7957098	FYPO:0001933	same as rad4 cut5 allele alone
PMID:7957098	FYPO:0001916	same as cdc13-117 alone
PMID:7957098	FYPO:0001916	same as cdc2-33 alone
PMID:7957098	PBO:0097701	same as cdc10-129 alone
PMID:7975894	PBO:0107866	increased transcriptional response to nitrogen starvation
PMID:7975894	PBO:0107866	increased transcriptional response to nitrogen starvation
PMID:7975894	PBO:0107869	increased transcription from TR box SO:0001858
PMID:7983142	FYPO:0000280	33 degrees (may be standard for them)
PMID:7983142	FYPO:0001357	33 degrees (may be standard for them)
PMID:7983142	FYPO:0001253	33 degrees (may be standard for them)
PMID:7983142	PBO:0026157	33 degrees (may be standard for them)
PMID:7983142	PBO:0104310	33 degrees (may be standard for them)
PMID:7983142	FYPO:0000021	33 degrees (may be standard for them); morphology same as ppe1delta alone
PMID:7983142	FYPO:0001253	33 degrees (may be standard for them)
PMID:8006074	FYPO:0000477	fig8
PMID:8006074	FYPO:0001043	fig8
PMID:8006074	FYPO:0000479	fig8
PMID:8006074	FYPO:0000477	fig8
PMID:8026462	FYPO:0001384	assayed using casein
PMID:8039497	FYPO:0002024	unstable plasmid loss experiment
PMID:8039497	GO:0140281	also some genetic interactions that cannot be described with biogrid
PMID:8039497	GO:0031028	also some genetic interactions that cannot be described with biogrid
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: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	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	cells are induced to increase their ploidy by a specific treatment e.g. heat shock or drug treatment
PMID:8087848	PBO:0037895	cells are induced to increase their ploidy by a specific treatment e.g. heat shock or drug treatment
PMID:8087848	PBO:0037893	cells are induced to increase their ploidy by a specific treatment e.g. heat shock or drug treatment
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	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:0037896	cdc13delete cells were kept alive by episomal pSM2 cdc13. Cell phenotype was observed after plasmid loss. Figure 2C
PMID:8121488	PBO:0112239	Table 1
PMID:8121488	PBO:0112237	in vitro assay data not shown
PMID:8121488	PBO:0112236	Table 1 increased cell size required for the G1/S transition.
PMID:8121488	PBO:0026408	Fig1A Overreplicating haploid cells become highly enlarged (Fig. la, left),
PMID:8121488	PBO:0112242	Fig3a
PMID:8121488	FYPO:0005097	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 progres- sion through GI into S phase. The appearance of a small popu- lation 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 progres- sion through GI into S phase. The appearance of a small popu- lation of IC cells at 16 h is consistent with this interpretation (Fig. lb).
PMID:8121488	PBO:0037896	(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	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: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:0001425	Fig1B they give a pulse of rum1
PMID:8121488	PBO:0112241	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 progres- sion through GI into S phase. The appearance of a small popu- lation of IC cells at 16 h is consistent with this interpretation (Fig. lb).
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: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	FYPO:0007476	data not shown cells become arrest in G2
PMID:8121488	PBO:0112238	Fig2B. prestart
PMID:8163505	GO:0004674	based on phenotype this annotation is possible
PMID:8187760	FYPO:0004105	grows in three dimensions instead of just at cell ends
PMID:8187760	FYPO:0001382	assayed in vitro using casein
PMID:8187760	FYPO:0000839	same as cdc25-22 alone
PMID:8187760	FYPO:0000839	same as cdc2-33 alone
PMID:8196631	GO:0043409	NEG REG OF PHEROMONE RESPONSE MAPK
PMID:8223442	FYPO:0007564	fig 1
PMID:8223442	FYPO:0007565	fig 1
PMID:8227198	FYPO:0001665	response curve differs from wt and other git mutants
PMID:8264625	GO:0043539	casein substrate (vw changed from GO:0004674 with contributes to)
PMID:8264625	GO:0004674	casein substrate
PMID:8292390	PBO:0096647	same as cps8-185 alone
PMID:8299169	FYPO:0002068	C868T (nt)
PMID:8319772	MOD:00046	present throughout cell cycle
PMID:8334988	FYPO:0002987	binucleate fypo/issues/#2400 fypo/issues/#2401
PMID:8346915	GO:0004019	inhibiyted by CHEBI:43040
PMID:8413241	PBO:0105255	tyrosine; residue not determined
PMID:8413241	PBO:0105255	tyrosine; residue not determined
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant expressed from multi copy plasmid pIRT2
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0107596	Table 1, Fig2 mutant gene expressed from multicopy plasmid pIRT2 partially suppresses the ts phenotype
PMID:8437586	PBO:0093712	Table 1 Fig 2 mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0107595	Fig 5 increased duration of G1 phase
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	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:0100985	Table 1 Fig 4 nmt1 ON
PMID:8437586	PBO:0097954	Fig 5 nmt1 promoter ON
PMID:8437586	PBO:0097954	Fig 5 nmt1 promoter ON
PMID:8437586	PBO:0097954	Fig 5 nmt1 promoter ON
PMID:8437586	FYPO:0002061	Table 1 nmt1 promoter ON
PMID:8437586	PBO:0019154	Table 1 nmt1 promoter ON
PMID:8437586	FYPO:0002061	Table 1 nmt1 promoter ON
PMID:8437586	PBO:0019154	Table 1 nmt1 promoter ON
PMID:8437586	FYPO:0002061	Table 1 nmt1 promoter ON
PMID:8437586	PBO:0019154	Table 1 nmt1 promoter ON
PMID:8437586	FYPO:0002061	Table 1 Fig 4 nmt1 promoter ON
PMID:8437586	PBO:0019154	Table 1 Fig 4 nmt1 promoter ON
PMID:8437586	FYPO:0002061	Fig 4 Table 1 nmt1 promoter ON
PMID:8437586	PBO:0019154	Fig 4 Table 1 nmt1 promoter ON
PMID:8437586	FYPO:0002061	Table 1 nmt1 promoter ON
PMID:8437586	PBO:0019154	Table 1 nmt1 promoter ON
PMID:8437586	FYPO:0002061	Fig 4 nmt1 promoter ON
PMID:8437586	PBO:0019154	Fig 4 nmt1 promoter ON
PMID:8437586	FYPO:0002061	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0001490	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0002085	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0001490	Table 1 mutant gene expressed from multicopy plasmid pIRT2 no suppression
PMID:8437586	FYPO:0002085	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0001490	Table 1 mutant gene expressed from multicopy plasmid pIRT2 no suppression
PMID:8437586	FYPO:0002085	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0001490	Table 1 mutant gene expressed from multicopy plasmid pIRT2 no suppression
PMID:8437586	FYPO:0002085	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0001490	Table 1 mutant gene expressed from multicopy plasmid pIRT2 no suppression
PMID:8437586	FYPO:0002085	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0002085	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0001490	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0001490	Table 1 mutant gene expressed from multicopy plasmid pIRT2 no suppression
PMID:8437586	FYPO:0002085	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0001490	Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	FYPO:0002061	mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0020446	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0002060	Table 1 mutant gene expressed from multicopy plasmid pIRT2 give partial suppression
PMID:8437586	FYPO:0000082	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	PBO:0019143	Table 1 mutant gene expressed from multicopy plasmid pIRT2 partially supresses the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0019154	mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0000082	Table 1 mutant gene expressed from multicopy plasmid pIRT2 partially supresses the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype
PMID:8437586	FYPO:0002061	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0093712	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0037209	Table 1 Fig 2 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0093712	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0001234	Table 1 mutant gene expressed from multicopy plasmid pIRT2 partially suppresses the ts phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	PBO:0019154	mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	FYPO:0002061	mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	PBO:0019154	mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	FYPO:0002061	mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	PBO:0019154	mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	PBO:0038194	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype
PMID:8437586	PBO:0038194	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0002061	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0093712	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0001234	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0099234	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2 surpresses the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0000082	Table 1 mutant gene expressed from multicopy plasmid pIRT2 partially supresses the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0002061	Table1 mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0093712	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype
PMID:8437586	PBO:0038194	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	FYPO:0002061	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype
PMID:8437586	FYPO:0002061	mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	FYPO:0002085	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0038194	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0000082	Table 1 mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	PBO:0020446	Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype
PMID:8437586	FYPO:0002061	mutant gene expressed from multicopy plasmid pIRT2
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	PBO:0019154	mutant expressed from multi copy plasmid has dominant negative phenotype Table 1
PMID:8437586	FYPO:0002061	mutant expressed from multi copy plasmid has dominant negative phenotype Table 1
PMID:8437586	PBO:0019154	Table 1 mutant expressed from multi copy plasmid has dominant negative phenotype Table 1
PMID:8437586	FYPO:0002061	Table 1 mutant expressed from multi copy plasmid has dominant negative phenotype Table 1
PMID:8437586	FYPO:0002061	Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype
PMID:8437586	PBO:0019154	mutant expressed from multi copy plasmid has dominant negative phenotype Table 1
PMID:8437586	FYPO:0002061	mutant expressed from multi copy plasmid has dominant negative phenotype Table 1
PMID:8437586	PBO:0019154	mutant expressed from multi copy plasmid has dominant negative phenotype Table 1
PMID:8437586	FYPO:0002061	mutant expressed from multi copy plasmid has dominant negative phenotype Table 1
PMID:8437586	PBO:0019154	Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype
PMID:8463273	GO:0004699	kinase assay, and hybridization with S. cerevisiae PKC
PMID:8485317	FYPO:0002060	like dis1-288 alone
PMID:8485317	FYPO:0002061	like dis1-288 alone
PMID:8496185	GO:0004017	inhibited by P(1),P(5)-bis(5'-adenosyl) pentaphosphate(5-)?
PMID:8497322	PBO:0093630	fig 2 c
PMID:8497322	FYPO:0006822	fig 3 fypo/issues/2818
PMID:8497322	PBO:0093629	fig 2 c
PMID:8497322	PBO:0093630	fig 2a
PMID:8497322	PBO:0093631	partial rescue of chk1, fig 2 b
PMID:8497322	PBO:0094949	fig 2 c
PMID:8497322	PBO:0094950	fig 2a DROPS TO ZERO
PMID:8497322	FYPO:0002060	fig 3 a
PMID:8497322	FYPO:0002061	fig 3
PMID:8497322	FYPO:0001046	fig 3 fypo/issues/2818
PMID:8497322	FYPO:0002061	data not shown
PMID:8497322	PBO:0094952	fig 2 c
PMID:8497322	PBO:0093581	fig 4
PMID:8497322	FYPO:0001971	fig 3 cells fail to separate and are clupmed together, multiple rounds of nuclear division
PMID:8515818	MOD:00046	Fig2b,
PMID:8515818	PBO:0097559	Fig2a lane1
PMID:8515818	PBO:0097560	Fig2a lane 3
PMID:8515818	MOD:00047	Fig2b
PMID:8515818	MOD:00047	Fig 2b
PMID:8515818	MOD:00046	Fig2b 2x serine phos to T phos
PMID:8515818	PBO:0097561	(directly inhibits) Fig4a,b together with data from fig 2,3
PMID:8515818	FYPO:0002060	Fig1b bottom R panel , bottom R K41A is predicted to be catalytically inactive. cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor
PMID:8515818	PBO:0097558	Fig1b bottom R panel , bottom R K41A is predicted to be catalytically inactive. cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor
PMID:8515818	FYPO:0002061	Fig1b bottom R panel, bottom L
PMID:8515818	PBO:0019218	Fig1b bottom R panel, bottom L
PMID:8515818	FYPO:0002061	Fig1b bottom R panel, top
PMID:8515818	FYPO:0002061	Fig1b top R panel, top cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor
PMID:8515818	FYPO:0002061	Fig1b top R panel bottom L cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor
PMID:8515818	PBO:0019218	Fig1b bottom R panel, top
PMID:8515818	FYPO:0002060	Fig1b top R panel bottom R. K41A is predicted to be catalytically inactive ref 18. cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor
PMID:8515818	PBO:0097558	Fig1b top R panel bottom R K41A is predicted to be catalytically inactive. cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor
PMID:8515818	PBO:0019218	Fig1b top R panel, top cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor
PMID:8515818	PBO:0019218	Fig1b top R panel bottom L cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor
PMID:8515818	FYPO:0006822	data not shown ref16
PMID:8521469	FYPO:0001425	same as cdc18+ oe alone
PMID:8521469	FYPO:0001425	same as cdc18+ oe alone
PMID:8521500	PBO:0101289	Fig3A
PMID:8521500	PBO:0101289	Fig3A
PMID:8521500	PBO:0101287	Fig3A
PMID:8521500	PBO:0101286	Fig2C rum1+ driven by nmt1 promoter in pREP6X is integrated
PMID:8521500	PBO:0101285	[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 Histone H1 used as substrate
PMID:8521500	PBO:0101284	Fig1 Histone H1 used as substrate
PMID:8521500	PBO:0101291	Fig3B
PMID:8521500	PBO:0101290	Fig3A
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	[ move to specific cyclin] Fig6 2.6nM rum1 inhibits cig2 associated cdc2 kinase activity by ~50%
PMID:8521500	PBO:0101299	Fig5B over expression abolishes cdc13 associated kinase activity even in absence of added rum1 protein
PMID:8521500	PBO:0101298	FigB over expression reduces cdc2 kinase activity even in absence of added rum1 protein
PMID:8521500	PBO:0101297	Fig5A
PMID:8521500	PBO:0101296	Fig5A
PMID:8521500	PBO:0101295	Fig 3C
PMID:8521500	PBO:0101294	Fig 3C
PMID:8521500	PBO:0101293	Fig4 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	Fig3B
PMID:8521500	PBO:0101288	Fig3A
PMID:8522609	FYPO:0002021	same as orb3-167 alone
PMID:8522609	FYPO:0000647	same as orb3-167 alone
PMID:8522609	FYPO:0001018	same as orb2-34 alone
PMID:8522609	FYPO:0000839	same as cdc2-33 alone
PMID:8522609	FYPO:0001018	same as orb2-34 alone
PMID:8522609	FYPO:0001418	same as orb3-167 alone
PMID:8552670	PBO:0104786	, activated_by(CHEBI:18420)
PMID:8557036	GO:0008353	assayed in S. cerevisiae cell extracts, with S.c. CTD substrate
PMID:8557036	GO:0004693	assayed in S. cerevisiae cell extracts, with S.c. CDK2 substrate
PMID:8557037	GO:0004693	activated_by(CHEBI:63041)
PMID:8569679	FYPO:0002061	fig2
PMID:8569679	FYPO:0002061	fig2
PMID:8569679	FYPO:0002061	fig2
PMID:8569679	FYPO:0002061	fig2
PMID:8569679	FYPO:0002061	fig2
PMID:8569679	FYPO:0002061	fig2
PMID:8569679	FYPO:0002061	fig2
PMID:8569679	FYPO:0002061	fig2
PMID:8590464	GO:0004043	inhibited_by L-lysine
PMID:8590465	GO:0004151	cryptic dihydroorotase domain
PMID:8590474	PBO:0095685	partial rescuie
PMID:8618924	GO:1902969	also inferred from orthology to all other Orc1s in the world
PMID:8621436	FYPO:0002303	transient phenotype, they then attempt to divide without segregation
PMID:8621436	FYPO:0000158	they show it is not abnormal regulation of rereplication in cdc25 double mutant expts
PMID:8621436	FYPO:0000620	transient phenotype, they then attempt to divide without segregation
PMID:8621436	FYPO:0000620	transient phenotype, they then attempt to divide without segregation
PMID:8621436	FYPO:0002303	transient phenotype, they then attempt to divide without segregation
PMID:8621436	FYPO:0000158	they show it is not abnormal regulation of rereplication in cdc25 double mutant expts
PMID:8649397	FYPO:0001122	Can't say if they are viable vegetative because it is in a pyp2+ background
PMID:8654750	PBO:0099148	PHEROMONE
PMID:8668131	GO:0006744	func comps S cer ABC1
PMID:8688826	GO:0034399	Val: changed from nuclear lumen to nuclear periphery
PMID:872890	FYPO:0006909	Table 1, DNA replication initiated at low protein content
PMID:872890	PBO:0102251	Table 1, Fig1
PMID:872890	PBO:0093712	Fig1, 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: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	PBO:0103505	Fig6, 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:0006909	Table 1
PMID:872890	FYPO:0006031	Table 1, Fig1
PMID:872890	PBO:0103506	Fig4, 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: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:8799335	PBO:0092041	present with ammonium, allantoin, or proline nitrogen source
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: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:0101514	Fig10
PMID:8811082	GO:0000703	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 super- coiled damaged DNA. None of the proteins caused breaks in undamaged DNA.
PMID:8824588	PBO:0105349	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 disor- ganized manner into the interior
PMID:8876193	PBO:0099353	Fig2
PMID:8876193	PBO:0099356	Fig3
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 in absence of septation, cells need to complete cell cycle to observe asymmetry
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 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	PBO:0099352	data not shown, cells blocked at G1/S, cells need to complete cell cycle to observe asymmetry
PMID:8876193	PBO:0099355	Fig3
PMID:8876193	PBO:0099354	Fig2 1% of cells still have a short mitotic spindle after 5h at restrictive temperature
PMID:8876193	PBO:0099351	data not shown
PMID:8876193	GO:0048311	Fig4
PMID:8879048	GO:0043409	NEG REG PHEROMONE MAPK
PMID:8918598	FYPO:0005112	ubiquitin conjugate
PMID:8918598	FYPO:0005112	ubiquitin conjugate
PMID:8918880	FYPO:0002060	fig 1
PMID:8918880	GO:0005680	fig 5
PMID:8918880	FYPO:0002060	fig 1
PMID:8918880	FYPO:0002060	fig 1
PMID:8918880	FYPO:0002061	fig 1
PMID:8943330	PBO:0095167	tyrosine; position(s) not determined
PMID:8943330	GO:0000196	not sure this annotation is 100% supported, can revise later if needed.
PMID:8946912	FYPO:0001007	fig 2a
PMID:8946912	FYPO:0003210	fig 2a
PMID:8946912	FYPO:0001234	fig 3
PMID:8946912	FYPO:0002070	fig 2a
PMID:8978670	FYPO:0001008	figure 1
PMID:8978670	FYPO:0002023	figure 1
PMID:8978670	FYPO:0000417	figure 1
PMID:8978670	FYPO:0002024	figure 1
PMID:8978687	FYPO:0002018	figure 5
PMID:8978687	FYPO:0001705	figure 5
PMID:8978687	FYPO:0005371	figure 6
PMID:8978687	FYPO:0004474	figure 5
PMID:8978687	FYPO:0002018	figure 5
PMID:8978687	FYPO:0002049	fig 7
PMID:8978687	FYPO:0005393	fig 7
PMID:8978687	FYPO:0003758	fig 6 a
PMID:8978687	FYPO:0000729	fig 6 a
PMID:8978687	FYPO:0004648	fig 6 a
PMID:8978687	FYPO:0002060	figure 2
PMID:8978687	FYPO:0001368	fig 4 b
PMID:8978687	FYPO:0002060	figure 1a
PMID:8978687	PBO:0104407	fig 6 c
PMID:9024682	PBO:0096483	severe when both cells are cpb1delta
PMID:9034337	PBO:0095685	Fig 3B
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:0108717	Fig 5, Fig6
PMID:9034337	PBO:0106846	Fig 4,
PMID:9034337	FYPO:0000444	Fig 2 D
PMID:9034337	FYPO:0002085	Data not shown chk1+ over expression phenotype is suppressed by over expressing cdc25+ independently of cdr1
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:0001575	Fig 2 A
PMID:9034337	PBO:0106845	Fig 2C
PMID:9034337	PBO:0096052	Fig 2B Histone H1 used as cdc2 substrate Chk2 expressed from nmt1 promoter
PMID:9034337	PBO:0108716	Fig1
PMID:9034337	FYPO:0005773	Fig 2 D
PMID:9042863	FYPO:0001046	temperature permissive for wee1-50; unirradiated
PMID:9042863	GO:0072435	Activity inhibited in response to mitotic G2 DNA damage checkpoint
PMID:9042863	FYPO:0007248	temperature restrictive for wee1-50
PMID:9042863	PBO:0108718	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	mei2 promotes g1 arrest, premeiotic dna replication and meiosis I
PMID:9078390	PBO:0037209	fig 3a
PMID:9078390	PBO:0037209	fig 3a
PMID:9078390	PBO:0096205	fig 2 C
PMID:9078390	FYPO:0002061	fig 3a
PMID:9078390	FYPO:0002061	fig 3a
PMID:9078390	PBO:0096205	fig 2 C
PMID:9078390	PBO:0096202	fig 2 C
PMID:9078390	PBO:0096204	fig 2 C
PMID:9078390	PBO:0096203	fig 2 C
PMID:9078390	PBO:0096202	fig 2 C
PMID:9078390	FYPO:0002061	fig 3a
PMID:9090050	PBO:0114483	inhibition by CCCP and DCCD
PMID:9092661	PBO:0110293	We found that the double mutant uvded rad2d was more resistant than a rad2d single mutant (Fig. 3).
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: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	Figure 2...The uvde gene disruption made cells only mildly sensitive to UV, even after high doses.
PMID:9092661	PBO:0109839	Cell survival assay
PMID:9092661	PBO:0110294	Figure 4
PMID:9092661	PBO:0109839	Cell survival assay
PMID:9092661	PBO:0106872	Cell survival assay
PMID:9092661	PBO:0106872	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	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	PBO:0110294	Figure 4
PMID:9105045	PBO:0105900	cdc12 froms a cortical spot
PMID:9111307	FYPO:0003241	not sure if this is the right term, sent a question
PMID:9125114	PBO:0096500	also increased (WT overexppression) normal (WT)
PMID:9135147	PBO:0095167	tyrosine; residue not determined
PMID:9135148	PBO:0094619	inferring that residue is Y15, though not shown experimentally
PMID:9136929	PBO:0094396	not annotated to other stresses as subsequent papers show it is critical for assembly of signaling MAPKKK-MAPKKmodule
PMID:9153313	PBO:0093629	same as rad26delta alone
PMID:9153313	PBO:0093629	same as crb2delta alone
PMID:9153313	PBO:0093629	same as rad3delta alone
PMID:9154834	FYPO:0004254	doesn't resume normally
PMID:9154834	PBO:0095824	residue not determined, but probably Y173
PMID:9154834	PBO:0105229	residue not determined, but probably Y173
PMID:9154838	PBO:0032853	has condensed chromosomes
PMID:9177184	PBO:0098824	as cyclin-CDK complex with Cdc13 or Cig2
PMID:9182664	FYPO:0002845	this might be dumbbell ask Jacky
PMID:9182664	FYPO:0003413	swollen
PMID:9182664	FYPO:0002462	swollen
PMID:9191273	PBO:0099148	PHEROMONE MAPK
PMID:9200612	PBO:0097441	Fig3A
PMID:9200612	PBO:0097442	Fig4 A
PMID:9200612	PBO:0097443	Fig4 A
PMID:9200612	PBO:0097440	Fig3A
PMID:9200612	PBO:0097443	Fig4 A
PMID:9200612	PBO:0097448	Fig1C ii
PMID:9200612	PBO:0097449	Fig1C iii
PMID:9200612	PBO:0097436	data not shown
PMID:9200612	PBO:0097442	Fig4 A
PMID:9200612	PBO:0037217	Fig5 shown using TBZ treatment and wash out and by cold shock and relocalization
PMID:9200612	FYPO:0001587	Fig 2D Protein localised to both cell tips during monopolar growth
PMID:9200612	FYPO:0001587	Fig 2C Protein localised to both cell tips during monopolar growth
PMID:9200612	FYPO:0001587	Fig 2C protein localised to both cell tips
PMID:9200612	FYPO:0002177	data not shown. tea1 on multi copy plasmid -R2 suppresses the cell shape defect of tea1 delta
PMID:9200612	PBO:0097439	Fig 2B,C
PMID:9200612	PBO:0097438	Fig2B C
PMID:9200612	PBO:0097444	Fig5C
PMID:9200612	PBO:0097445	Fig5C
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	PBO:0097446	Fig5C
PMID:9200612	PBO:0097445	Fig5C cells blocked in mitosis so have no interphase MTs
PMID:9200612	PBO:0097435	Fig1C iii
PMID:9200612	PBO:0097434	Fig1C iii
PMID:9200612	PBO:0097433	Fig1C ii
PMID:9200612	PBO:0097447	Fig 6D
PMID:9200612	PBO:0096501	Fig6D
PMID:9201720	PBO:0098805	physically interacts with and IMP evidence
PMID:9201720	PBO:0103195	not shown that it is ser/thr kinase activity, just that it is kinase activity
PMID:9201720	PBO:0103194	physically interacts with and IMP evidence
PMID:9202173	FYPO:0003265	Fig. 7
PMID:9202173	FYPO:0003458	Fig. 6
PMID:9202173	FYPO:0003458	Fig. 6
PMID:9202173	FYPO:0001682	Fig. 5
PMID:9202173	FYPO:0003265	Fig. 7
PMID:9211982	FYPO:0003698	truncated Gar2 accumulates in this dense body
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	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:0093637	Cells show progressive telomere shortening.
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: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	PBO:0037311	fig 2 b
PMID:9278510	FYPO:0004259	fig 1
PMID:9278510	PBO:0037311	fig 2 b
PMID:9285594	PBO:0101680	in vitro
PMID:9285594	GO:0000796	Fig 1
PMID:9285594	GO:0000796	Fig 1
PMID:9287302	GO:0036245	vw: I deleted accidintally , then readded
PMID:9287302	GO:0036245	vw: I deleted accidintally , then readded
PMID:9301023	FYPO:0002519	(Figure 2b)
PMID:9301023	PBO:0098600	(Figure 2a)
PMID:9301025	FYPO:0002060	just getting the allele in the database (they used it in the exp)
PMID:9303310	PBO:0096936	Fig 1 exponentially growing cells mainly in G2
PMID:9303310	FYPO:0000333	Fig7A
PMID:9303310	PBO:0096943	Fig7B
PMID:9303310	PBO:0096942	Fig 8 added by cig1 associated CDK1
PMID:9303310	PBO:0096941	Fig5 (vw, I edited the extensions)
PMID:9303310	PBO:0096940	Fig2, Fig3
PMID:9303310	PBO:0096938	Fig2
PMID:9303310	PBO:0096939	Fig2, Fig3
PMID:9303310	PBO:0096937	Fig2
PMID:9303310	PBO:0096936	Fig 1 cells blocked in G1 at the restrictive temp
PMID:9303312	PBO:0105913	Fig 4C Cdc18 transcript is low during G2
PMID:9303312	PBO:0105902	Fig 1A and C cdc18 transcription is not dependent on cdc2 function
PMID:9303312	PBO:0105903	Fig 1 B cdc2-M26 has no detectable kinase activity in G1 at restrictive temperature
PMID:9303312	PBO:0105904	Fig 1D cdc2-M26 does not enter S phase even though cdc18 transcription is presence
PMID:9303312	PBO:0037892	Fig2 B
PMID:9303312	PBO:0101286	Fig2 B
PMID:9303312	PBO:0101286	Fig2 B cells do not undergo re replication at restrictive temperature
PMID:9303312	PBO:0105905	Fig2A cells do not undergo re replication at restrictive temperature but cdc18 transcript increases
PMID:9303312	PBO:0105902	Fig2 B
PMID:9303312	PBO:0105906	Fig3A cdc18 transcript accumulates in absence of cig1, cig2 and cdc13
PMID:9303312	PBO:0105906	Fig3A cdc18 transcript accumulates in absence of cdc13
PMID:9303312	PBO:0105907	Fig3B cdc18 protein accumulates in absence of cig1, cig2 and cdc13
PMID:9303312	PBO:0105908	Fig3C no DNA replication in absence of all 3 cyclins
PMID:9303312	PBO:0105909	Fig3C DNA replication in presence of cig1 and cig2
PMID:9303312	PBO:0105910	Fig3C Abnormal DNA replication with cut DNA replication in absence cig1, cig2 and cdc13 promoter ON some cells have a cut phenotype. NOT sure the data warrants an annotation
PMID:9303312	PBO:0105911	Fig3C, D Absence of cdc2 kinase activity in absence cig1, cig2 and cdc13
PMID:9303312	PBO:0105912	Fig3C, 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: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	Fig5A, B decreased cdc18 transcript in HU block and on release
PMID:9303312	PBO:0098715	Fig5A decreased cdc18 transcript in HU block and on release
PMID:9303312	PBO:0098715	Fig5A, B decreased cdc18 transcript in HU block and on release
PMID:9303312	PBO:0105905	Fig5A, B level of cdc18 transcript does not decreased after release from HU block
PMID:9303312	FYPO:0004235	Fig 5C
PMID:9303312	PBO:0105905	Fig5C rep2delta has no effect on cdc18 transcript levels in the absence of res2
PMID:9303312	PBO:0105915	Fig6C
PMID:9303312	PBO:0098713	Fig6C
PMID:9303312	PBO:0098716	Fig6D
PMID:9303312	PBO:0105915	Fig6D
PMID:9303312	PBO:0098716	Fig6B
PMID:9303312	PBO:0105915	Fig6B
PMID:9303312	PBO:0105913	Data not shown
PMID:9303312	PBO:0105916	Fig7 res1 on multi copy pREP3X ON
PMID:9303312	PBO:0105915	Fig7 res1 on multi copy pREP3X ON
PMID:9303312	PBO:0098713	Fig7 res1 on multi copy pREP3X ON
PMID:9303312	PBO:0105917	Fig7
PMID:9303312	PBO:0105913	Fig7 res2 on multi copy pREP3X ON
PMID:9303312	PBO:0105913	Fig7 res2 on multi copy pREP3X ON
PMID:9303312	PBO:0105918	Fig8 DSC1 is now called MBF
PMID:9303312	PBO:0105918	Fig8B DSC1 is now called MBF
PMID:9303312	PBO:0105918	Fig8 DSC1 is now called MBF
PMID:9303312	PBO:0105918	Fig8B 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	Fig8 Presence of MBF is correlated with cdc10 dependent transcription repression during G2
PMID:9303312	PBO:0105921	Fig8 Presence of MBF is correlated with cdc10 dependent transcription repression during G2
PMID:9303312	PBO:0105921	Fig8 Presence of MBF is correlated with cdc10 dependent transcription repression during G2
PMID:9303312	PBO:0105921	Fig8 Presence of MBF is correlated with cdc10 dependent transcription repression during G2
PMID:9303312	PBO:0105922	Fig8 C
PMID:9303312	PBO:0105923	Fig2 B
PMID:9303312	PBO:0094078	Fig3C Abnormal DNA replication with cut DNA replication in absence cig1, cig2 and cdc13 promoter ON some cells have a cut phenotype. NOT sure the data warrants an annotation
PMID:9303312	PBO:0113868	Fig. 4B
PMID:9312055	FYPO:0002061	fig 3b
PMID:9312055	FYPO:0002060	fig 2 (synthetic rescue)
PMID:9312055	FYPO:0002060	fig 2 (synthetic rescue)
PMID:9312055	FYPO:0002061	fig 2
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:0003165	fig 1c
PMID:9312055	FYPO:0001946	fig 1c
PMID:9312055	FYPO:0002061	fig 1b
PMID:9312055	FYPO:0002061	fig 3b
PMID:9312055	FYPO:0002061	fig 3b
PMID:9312055	PBO:0095634	fig 1b
PMID:9312055	FYPO:0002060	fig 1b
PMID:9312055	FYPO:0002061	fig 1b
PMID:9312055	FYPO:0002061	fig 1b
PMID:9312055	PBO:0102753	fig9
PMID:9312055	PBO:0102752	fig9
PMID:9312055	MOD:01148	poly...
PMID:9312055	PBO:0020076	fig7
PMID:9312055	PBO:0096939	fig 6
PMID:9312055	PBO:0102751	fig 6
PMID:9312055	PBO:0102750	fig 4 b-d
PMID:9312055	PBO:0102749	fig 4a
PMID:9312055	PBO:0099779	fig 4
PMID:9312055	PBO:0102748	fig 4
PMID:9312055	FYPO:0002060	fig 3b (rescue)
PMID:9312055	FYPO:0002061	fig 3b (rescue)
PMID:9315645	GO:0062038	"This one comes in ""from the side"", see Ladds, Bond post 2010 publication summary"
PMID:9315645	PBO:0102572	fig7, sort of indirect - kinase dead mutant doesn't activate
PMID:9321395	PBO:0097481	(Figure 5)
PMID:9321395	FYPO:0000082	(Figure 4)
PMID:9321395	FYPO:0000271	(Figure 4)
PMID:9321395	FYPO:0001492	(Figure 4)
PMID:9321395	FYPO:0001492	(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	FYPO:0002177	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:9325108	GO:0008821	activated_by(CHEBI:18420)| activated_by(CHEBI:29035)
PMID:9325304	GO:0010498	via purification assay
PMID:9325304	FYPO:0006477	3B
PMID:9325304	FYPO:0000620	3B
PMID:9325304	GO:0010498	via purification assay
PMID:9325316	GO:0001055	author intent
PMID:9325316	GO:0001055	author intent
PMID:9325316	GO:0001055	author intent
PMID:9325316	GO:0003677	binds DNA on its own
PMID:9325316	GO:0003677	binds DNA in complex (2,3,11)
PMID:9325316	GO:0003677	binds DNA in complex (2,3,11)
PMID:9325316	GO:0003677	binds DNA in complex (2,3,11)
PMID:9325316	GO:0001055	author intent
PMID:9325316	GO:0006366	author intent
PMID:9325316	GO:0006366	author intent
PMID:9325316	GO:0006366	author intent
PMID:9325316	GO:0006366	author intent
PMID:9371883	PBO:0107553	two-hybrid assay
PMID:9371883	PBO:0107554	two-hybrid assay
PMID:9371883	PBO:0107554	two-hybrid assay
PMID:9371883	PBO:0107553	two-hybrid assay
PMID:9372936	FYPO:0001355	same as rae1-167 single mutant
PMID:9372936	FYPO:0001355	same as rae1-167 single mutant
PMID:9372936	FYPO:0000838	assayed using SV40 NLS-GFP-LacZ reporter protein
PMID:9372936	FYPO:0000838	assayed using SV40 NLS-GFP-LacZ reporter protein
PMID:9398669	PBO:0095554	nitrogen induced arrest
PMID:9398669	PBO:0033959	fig 5c switched from conjugtion freqeuncy to sterility as can only capture penetance on cell phenotypes
PMID:9398669	FYPO:0001425	fig 5a
PMID:9398669	FYPO:0000303	add penetrance?
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:9398669	PBO:0095555	G1 phase nitrogen induced arrest
PMID:9420333	PBO:0103702	(IN gthis paper we don't actually 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:0018634	Fig3A,C spg1-HA observed at SPB throughout the mitotic cell cycle
PMID:9420333	PBO:0103695	Fig2A loss of cdc16 function does not affect cdc7 kinase activity
PMID:9420333	PBO:0103694	"Fig 1 vw interpretation for ""active form"""
PMID:9420333	PBO:0103698	Fig5B
PMID:9420333	PBO:0103697	Fig5A
PMID:9420333	PBO:0113863	Fig 6A in late anaphase cdc7 is normally localized only one SPB
PMID:9420333	PBO:0103697	Fig5A
PMID:9420333	PBO:0023023	Fig3A,C spg1-HA observed at SPB throughout the mitotic cell cycle
PMID:9420333	PBO:0110202	(GTP bound)
PMID:9420333	PBO:0110201	(GTP bound)
PMID:9420333	PBO:0103703	(GTP bound)
PMID:9420333	PBO:0103695	Fig2A loss of spg1 function does not affect cdc7 kinase activity
PMID:9428701	GO:0004722	MBP substrate, activated_by(CHEBI:29035)
PMID:9430640	PBO:0092393	Fig1B
PMID:9430640	PBO:0096363	Fig2
PMID:9430640	MOD:01148	Fig2
PMID:9430640	PBO:0094205	Fig3, data not shown phenotype similar to rum+OP
PMID:9430640	PBO:0095634	Fig3B, similar to rum1+OP more severe than either single mutant. expressed from muliticopy plasmid. Colonies were integrants
PMID:9430640	PBO:0096365	Fig3C integrated copy
PMID:9430640	PBO:0096366	Fig 4B inhibitory for cdc2/cdc13 and cdc2/cig2 but not cdc2/cig1. Both Rum1+ and Rum1-A58A62 can inhibit cdk1 activity
PMID:9430640	MOD:00047	Fig3C
PMID:9430640	PBO:0096367	Fig5B
PMID:9430640	PBO:0096368	Fig6
PMID:9430640	PBO:0096369	Fig7, Fig8 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:0096370	Fig 10
PMID:9430640	PBO:0096371	Fig7B rum1 A58A62 mutant protein is unable to be phosphorylated by cdc2/cig1
PMID:9430640	PBO:0092211	Fig1B
PMID:9430640	PBO:0096372	Fig 4B inhibitory for cdc2/cdc13 and cdc2/cig2 but not cdc2/cig1. Both Rum1+ and Rum1-A58A62 can inhibit cdk1 activity
PMID:9430640	PBO:0096377	this isn't quite the right way to capture this target, still thinking
PMID:9430640	PBO:0096377	this isn't quite the right way to capture this target, still thinking
PMID:9430640	PBO:0096369	Fig7, Fig8 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:0096361	Fig5
PMID:9430640	PBO:0092114	Fig1B
PMID:9430640	PBO:0096362	Fig1C Peaks at the end of G2 40 min before peak of rum1 protein
PMID:9450991	FYPO:0003166	figure 1A
PMID:9450991	FYPO:0002061	fig 4A
PMID:9450991	FYPO:0001490	figure 4B
PMID:9450991	FYPO:0001418	30x figure 4B
PMID:9450991	PBO:0033643	figure 1A
PMID:9450991	PBO:0103183	figure 1A
PMID:9450991	FYPO:0000016	figure 1A
PMID:9450991	FYPO:0003166	figure 1A
PMID:9450991	FYPO:0004702	figure 2A/B
PMID:9459302	PBO:0035607	is this OK? its aseptate?
PMID:9468529	GO:0008444	inhibited_by CHEBI:29035
PMID:9488736	PBO:0096790	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:0105150	(Fig. 3)
PMID:9524127	PBO:0106212	(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:9524127	PBO:0106211	(Fig. 3a)
PMID:9524127	PBO:0106211	(Fig. 3a)
PMID:9524127	PBO:0105150	(Fig. 3a)
PMID:9531532	FYPO:0002061	over 25
PMID:9531532	FYPO:0000276	over 25
PMID:9531532	FYPO:0002060	over 25
PMID:9531532	FYPO:0002061	over 35
PMID:9531532	FYPO:0002061	over 25
PMID:9535817	FYPO:0005288	inferred from FYPO:0000825, FYPO:0001117, FYPO:0005743, FYPO:0007674 phenotypes (including conditions)
PMID:9552380	GO:0000307	cig2-cdc2
PMID:9560390	FYPO:0001122	osmotic stress
PMID:9560390	FYPO:0001122	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 main- tenance of the Cdc2 kinase in a pre-Start form, suggested by the fact that overexpression of Ste9 in- duced rereplication of the genome due to reduction of the mitotic kinase activity of the Cdc13/Cdc2 com- plex, and rereplication in the cdc2ts strain was pre- vented by the ste9 mutation.
PMID:9571240	FYPO:0000398	fig3
PMID:9571240	FYPO:0003012	4e
PMID:9571240	FYPO:0001054	4e
PMID:9572736	PBO:0112270	Fig. 2A
PMID:9572736	PBO:0112269	Fig. 1C
PMID:9572736	PBO:0112268	Fig. 1C
PMID:9572736	PBO:0112267	Fig. 1C
PMID:9572736	FYPO:0000963	Fig. 5B
PMID:9572736	PBO:0093580	Fig. 5B
PMID:9572736	PBO:0093580	Fig. 5B
PMID:9572736	PBO:0093581	Fig. 5B
PMID:9572736	FYPO:0005189	Fig. 5A
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:9572736	FYPO:0001492	Fig. 4
PMID:9572736	FYPO:0000088	Fig. 3D
PMID:9572736	PBO:0112273	Fig. 3C
PMID:9572736	PBO:0112273	Fig. 3C
PMID:9572736	PBO:0092345	Fig. 3C
PMID:9572736	PBO:0112272	Fig. 3B
PMID:9572736	PBO:0112271	Fig. 2B
PMID:9572736	PBO:0112270	Fig. 2A
PMID:9572736	PBO:0112270	Fig. 2A
PMID:9585506	FYPO:0001490	salt stress
PMID:9585506	GO:0005515	western but we know this happens and I wanted to capture the extension
PMID:9585506	FYPO:0001490	salt stress
PMID:9585506	GO:0005515	western but we know this happens and I wanted to capture the extension
PMID:9585506	FYPO:0001490	salt stress
PMID:9585506	FYPO:0001490	salt stress
PMID:9599405	PBO:0099148	PEHROMONE
PMID:9601094	PBO:0102017	fig 2D
PMID:9601094	FYPO:0001357	medium level of mph1 OEX (high is lethal)
PMID:9601094	PBO:0093562	Figure 4A
PMID:9601094	PBO:0102020	(Fig. 4D
PMID:9601094	PBO:0102019	fig 4B
PMID:9601094	FYPO:0003903	fig 4B
PMID:9601094	PBO:0102018	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:0001357	figure 6
PMID:9601094	FYPO:0000620	Fig 3C at metaphase/anaphase transiton
PMID:9601094	PBO:0102021	Fig 3C at metaphase/anaphase transiton
PMID:9606213	PBO:0107897	polarization, during conjugation, in shmoo fig1. We interpret the data as indicating that F-actin is first cor- rectly localized to the tip in all fus1 mutants, but is then re- distributed 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	polarization, in shmoo DNS
PMID:9606213	PBO:0107898	DNS actin distributed in cytoplasm
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:0107900	fig7
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: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	GO:0043332	By immunofluorescence, these antibod- ies 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	fig1
PMID:9606213	FYPO:0000573	fig1
PMID:9606213	FYPO:0000573	fig1
PMID:9614176	PBO:0099129	Fig6A transcript assayed was Mat1-Mm
PMID:9614176	GO:0031568	Fig2B 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	Fig4
PMID:9614176	PBO:0099121	Fig1 A
PMID:9614176	PBO:0099122	Fig3 A In absence of rum1 cdc2-cdc13 kinase activity remains high in presence of P factor
PMID:9614176	PBO:0099121	Fig3D loss of cig2 does not restore P factor induced G1 arrest
PMID:9614176	PBO:0099123	Fig4 - sows proteasome involvment as well
PMID:9614176	PBO:0099124	Fig5A
PMID:9614176	PBO:0099125	Fig5B
PMID:9614176	PBO:0099126	Fig5C
PMID:9614176	PBO:0099127	Fig5C
PMID:9614176	PBO:0099128	Fig5C
PMID:9614176	PBO:0099127	Fig5C
PMID:9614178	PBO:0100943	residue not determined experimentally, but probably Y173
PMID:9614178	PBO:0095827	residue not determined experimentally, but probably Y173
PMID:9614178	PBO:0103795	residue not determined experimentally, but probably Y173
PMID:9614178	PBO:0103795	residue not determined experimentally, but probably Y173
PMID:9614178	PBO:0106874	residue not determined experimentally, but probably Y173
PMID:9614178	PBO:0100943	residue not determined experimentally, but probably Y173
PMID:9622480	PBO:0097034	very mild as shown in xp
PMID:9635188	GO:0110085	dependent on F-actin (assayed using Latrunculin A)
PMID:9635188	FYPO:0002061	29 degrees; permissive for either single mutant
PMID:9635188	PBO:0018346	independent of F-actin (assayed using Latrunculin A)
PMID:9635188	PBO:0018634	independent of F-actin (assayed using Latrunculin A)
PMID:9635188	FYPO:0002060	24 degrees
PMID:9635188	PBO:0019716	independent of F-actin (assayed using Latrunculin A)
PMID:9635190	FYPO:0000783	fig 5 during mitotic M-phase
PMID:9635190	FYPO:0000783	fig 5 during mitosis
PMID:9635190	FYPO:0005000	fig 5 during interphase
PMID:9635190	FYPO:0001179	cytoplasm during interphase (with nuclear localization)
PMID:9635190	FYPO:0004754	fig 5 during mitotic M-phase
PMID:9635190	FYPO:0000783	fig 5 during mitotic M-phase
PMID:9635190	FYPO:0000783	fig 5 during mitotic M-phase
PMID:9635190	FYPO:0000783	fig 5 during mitotic M-phase
PMID:9635190	FYPO:0000783	fig 5 during mitotic M-phase
PMID:9635190	PBO:0033730	Figure 4b
PMID:9635190	FYPO:0001179	cytoplasm in interphase (Figure 4a, I)
PMID:9635190	PBO:0095293	Figure 2c
PMID:9635190	PBO:0095292	Figure 2b
PMID:9635190	PBO:0095291	(Fig 1i)
PMID:9635190	PBO:0095288	(Fig 1i)
PMID:9635190	PBO:0095290	Figure 2a
PMID:9636183	PBO:0095711	same severity as wee1-50 alone
PMID:9658208	FYPO:0002060	just to get the allele details of -P in the database
PMID:9660817	FYPO:0001147	data not shown
PMID:9660817	FYPO:0000708	data not shown
PMID:9660817	PBO:0093824	data not shown
PMID:9660818	PBO:0093825	when crossed with partner overexpressing shk1-deltaN; normal in cross with wild type
PMID:9660818	PBO:0093824	same severity when crossed with wild type or shk1delta
PMID:9660818	PBO:0093825	when crossed with shk1delta overexpressing shk2+ or wild type
PMID:9660818	GO:0004674	assayed using myelin basic protein
PMID:9660818	GO:0016020	including plasma membrane (GO:0005886)
PMID:9660818	PBO:0100579	assayed using myelin basic protein; interaction shown in separate experiment
PMID:9679144	PBO:0095940	Fig2C cells were pre NETO after temperature block about 5% cells are already branched at release
PMID:9679144	PBO:0095938	Fig2B cells were pre NETO after temperature block
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:0038218	Fig2C arrest released cells are pre NETO but only branch at low level.
PMID:9679144	PBO:0019143	Fig 3A-C pre NETO blocked cells do not branch if TBZ is added at shift down
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:0095939	Fig2B cells were pre NETO after temperature block
PMID:9679144	PBO:0095941	Fig 4 Short interphase microtubules located in the cell centre
PMID:9679144	PBO:0095942	Fig5 C,D
PMID:9679144	PBO:0095936	Fig1 F, H cells were pre NETO after temperature block
PMID:9679144	PBO:0095936	Fig2 B cells were pre NETO after temperature block
PMID:9679144	PBO:0095940	Fig2C cells were pre NETO after temperature block about 5% cells are already branched at release
PMID:9679144	PBO:0095937	Fig2A cdc25-22 arrest released cells ie post NETO do not branch
PMID:9679144	FYPO:0000672	Fig2C arrest released cells have NETO defect and do not branch.
PMID:9679144	PBO:0095946	Fig5 C,D Fig 12 Normal protein localisation in presence of TBZ
PMID:9679144	PBO:0095945	Fig 11 in the absence of microtubules and actin
PMID:9679144	PBO:0095945	Fig 11 absence of microtubules
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:9693363	FYPO:0003694	increased 25S/18S ration
PMID:9693384	PBO:0097481	probably Y173, but not determined experimentally
PMID:9693384	PBO:0095827	probably Y173, but not determined experimentally
PMID:9693384	PBO:0097481	probably Y173, but not determined experimentally
PMID:9718372	PBO:0100951	probably Y173, but not determined experimentally
PMID:9718372	PBO:0100943	probably Y173, but not determined experimentally
PMID:9718372	PBO:0095349	probably Y173, but not determined experimentally
PMID:9722643	GO:0005634	fig4
PMID:9722643	FYPO:0001840	table2
PMID:9722643	FYPO:0000091	fig5
PMID:9722643	FYPO:0000472	fig2
PMID:9722643	FYPO:0002060	fig1
PMID:9722643	PBO:0103534	fig3
PMID:9739083	PBO:0104507	Fig 3 not strictly a co-immunoprecitation experiment as they used suc1 beads to pull down cdc2 then a western blot
PMID:9739083	PBO:0104510	Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	PBO:0104511	Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	PBO:0099432	Fig 6 and cell phenotype data not shown. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	PBO:0104518	Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	PBO:0104512	Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	PBO:0104512	Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	PBO:0100985	Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	PBO:0104512	Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	PBO:0104517	Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	PBO:0104516	Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	PBO:0104509	Fig 6 cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal.
PMID:9739083	PBO:0104515	Fig 6 cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal.
PMID:9739083	PBO:0104514	Fig 6 cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal.
PMID:9739083	PBO:0104511	Fig 6 cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal.
PMID:9739083	PBO:0104509	Fig 6 cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal.
PMID:9739083	PBO:0104511	Fig 5 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 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 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 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 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 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 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 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:0104510	Fig 5 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 5 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	FYPO:0002995	Data not shown Cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	FYPO:0002519	Data not shown Cdc18 expressed from nmt1 promoter on multi copy plasmid
PMID:9739083	FYPO:0000402	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0000402	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0000402	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0000402	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0001052	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0005773	Fig 2A cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C
PMID:9739083	FYPO:0000402	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0000402	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0000402	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0000402	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0001052	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0001122	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0005773	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0005773	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0005773	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0005773	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0005773	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0005773	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0005773	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0005773	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0001122	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0001122	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0005773	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0005773	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0005773	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0005773	Fig 4 cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	PBO:0104508	Fig 3 not strictly a co-immunoprecitation experiment as they used suc1 beads to pull down cdc2 then a western blot
PMID:9739083	PBO:0104506	Fig 3 cdc18 expressed from pREP3X and assayed for 20 hours after removal of thiamine at 32°C
PMID:9739083	PBO:0096363	Fig 3 cdc18 expressed from pREP3X and assayed for 20 hours after removal of thiamine at 32°C
PMID:9739083	PBO:0096363	Fig 3 cdc18 expressed from pREP3X and assayed for 20 hours after removal of thiamine at 32°C
PMID:9739083	PBO:0096053	data not shown the kinase assay substrate used is Histone H1
PMID:9739083	PBO:0096053	Fig 3 the kinase assay substrate used is Histone H1
PMID:9739083	PBO:0096052	Fig 3 the kinase assay substrate used is Histone H1
PMID:9739083	PBO:0104505	Fig2B cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C
PMID:9739083	PBO:0102340	Fig 2B cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C
PMID:9739083	PBO:0097659	Fig 2A cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C
PMID:9739083	PBO:0097659	Fig 2A cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C
PMID:9739083	PBO:0097659	Fig 2A cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C
PMID:9739083	PBO:0097659	Fig 2A cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C
PMID:9739083	FYPO:0002061	cdc1-577 (NTP) when expressed on multi copy plasmid does not rescue cdc18-K46
PMID:9739083	FYPO:0002061	cdc18-150-577(T374A) when expressed on multi copy plasmid does not rescue cdc18-K46
PMID:9739083	FYPO:0002061	cdc18-150-577 when expressed on multi copy plasmid does not rescue cdc18-K46
PMID:9739083	FYPO:0002061	cdc18-1-141 when expressed on multi copy plasmid does not rescue cdc18-K46
PMID:9740803	GO:0008139	can't use IPI because we don't have identifiers for human importin alpha or the GST-NLS construct
PMID:9740803	GO:0061608	actually combination of in vitro assay, interactions, and sequence similarity
PMID:9740803	PBO:0103363	also assayed with GFP-NLS construct
PMID:9745017	PBO:0095902	inferred from decreased nda3 mRNA level
PMID:9745017	PBO:0095902	inferred from decreased nda3 mRNA level
PMID:9755169	PBO:0107542	Fig4C 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:0107542	Fig4C cd18 N term deletion can accumulate in a metaphase arrest
PMID:9755169	PBO:0107542	Fig5D
PMID:9755169	PBO:0107542	Fig5C
PMID:9755169	PBO:0096440	Fig5B
PMID:9755169	PBO:0107542	Fig4E cdc18 lacking cdc2 phosphorylation sites accumulates immediately as cells progress into mitosis
PMID:9755169	PBO:0107541	Fig3B
PMID:9755169	PBO:0107541	Fig3B cdc10 is a cdc18 transcriptional regulator see Fig2C
PMID:9755169	PBO:0107541	Fig3A cdc10 is a cdc18 transcriptional regulator see Fig2C
PMID:9755169	PBO:0107540	Fig 2C, cdc10 dependent transcription occurs during mitotic exit
PMID:9755169	PBO:0107539	Fig 2C, cdc10 dependent transcription occurs during mitotic exit
PMID:9755190	PBO:0096190	requested chromatin silencing term but advised to use this one
PMID:9755190	PBO:0096192	requested chromatin silencing term but advised to use this one
PMID:9755190	PBO:0096190	requested chromatin silencing term but advised to use this one
PMID:9755190	PBO:0096191	requested chromatin silencing term but advised to use this one
PMID:9755190	PBO:0096193	requested chromatin silencing term but advised to use this one
PMID:9771717	FYPO:0000678	not shown
PMID:9774107	PBO:0108165	data not shown
PMID:9774107	PBO:0108169	fig 4a
PMID:9774107	PBO:0108168	fig 4a
PMID:9774107	PBO:0108166	fig2
PMID:9774107	PBO:0108166	fig2
PMID:9774107	PBO:0095532	fig2
PMID:9774107	PBO:0095532	fig2
PMID:9774107	PBO:0094001	fig2e
PMID:9774107	PBO:0094001	fig2e
PMID:9774107	PBO:0108165	fig 2 e
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	FYPO:0006802	fig 2e
PMID:9786952	FYPO:0005870	fig 2b
PMID:9786952	FYPO:0001254	4a
PMID:9786952	PBO:0032815	4ab
PMID:9786952	FYPO:0001406	fig 2b
PMID:9786952	PBO:0102008	fig 2a
PMID:9786952	PBO:0102009	4de
PMID:9786952	PBO:0102010	fig6
PMID:9786952	FYPO:0003500	4a
PMID:9790887	GO:0004743	activated_by(CHEBI:18420), activated_by(CHEBI:29103)
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	PBO:0018346	(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 (Ha- gan and Yanagida, 1995)
PMID:9802907	FYPO:0002639	ADVANCED I hope I got this right?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:0018634	(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 (Ha- gan and Yanagida, 1995)
PMID:9808627	FYPO:0003241	G1 block
PMID:9808627	PBO:0033704	G2 block
PMID:9808627	PBO:0033703	(Fig. 2D)
PMID:9832516	PBO:0093579	severity estimated because wt (i.e. not overexpressing cdc25) not shown
PMID:9832516	PBO:0093579	severity estimated because wt (i.e. not overexpressing cdc25) not shown
PMID:9832516	PBO:0093579	severity estimated because wt (i.e. not overexpressing cdc25) not shown
PMID:9832516	PBO:0093579	severity estimated because wt (i.e. not overexpressing cdc25) not shown
PMID:9839953	PBO:0097089	at the second po- sition (Gal-Man-O)
PMID:9839953	PBO:0097089	low activity
PMID:9839953	PBO:0097092	at the second po- sition (Gal-Man-O)
PMID:9843572	PBO:0103076	Figure 9A
PMID:9843572	PBO:0103075	Figure 8
PMID:9843572	FYPO:0000711	figure 3 A&B
PMID:9843572	FYPO:0000712	figure 3 A&B
PMID:9843572	PBO:0098712	(Figure 1
PMID:9843572	FYPO:0003481	(Figure 3B)
PMID:9843572	FYPO:0003481	(Figure 3B)
PMID:9843572	FYPO:0003481	(Figure 3B)
PMID:9843572	PBO:0103075	Figure 8
PMID:9843572	PBO:0103074	figure 3 B (additive)
PMID:9843572	PBO:0094266	Figure 7A
PMID:9843572	FYPO:0001491	Figure 6B
PMID:9843572	FYPO:0001124	Figure 6A
PMID:9843572	FYPO:0003481	(Figure 3B)
PMID:9843577	FYPO:0007136	single micrograph, so can't tell if they're viable
PMID:9843577	FYPO:0007137	single micrograph, so can't tell if they're viable
PMID:9843966	PBO:0026234	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:0000403	biologically relevant? it can also cut these
PMID:9857040	GO:0070336	biologically relevant? it can also cut these
PMID:9862966	PBO:0101180	https://github.com/pombase/fypo/issues/3931
PMID:9862966	PBO:0101179	Fig3 CD
PMID:9864354	FYPO:0000229	Fig. 2 D
PMID:9864354	FYPO:0000620	indicated by high level of H1 kinase activity
PMID:9864354	FYPO:0007125	Fig. 2 E
PMID:9864354	FYPO:0007125	Fig. 2 E
PMID:9872416	PBO:0103889	figure 2.
PMID:9872416	PBO:0103890	figure 2.
PMID:9872416	PBO:0103891	figure 2.
PMID:9872416	PBO:0103892	figure 2.
PMID:9872416	PBO:0103888	figure 2.
PMID:9872416	PBO:0103893	figure 2.
PMID:9872416	PBO:0103887	figure 2.
PMID:9891039	FYPO:0001355	worse than cdc24-M38 alone (wt not shown)
PMID:9891039	FYPO:0001355	worse than cdc24-M38 alone (wt not shown)
PMID:9891039	FYPO:0001355	worse than cdc24-M38 alone (wt not shown)
PMID:9891039	FYPO:0001355	worse than cdc24-M38 alone (wt not shown)
PMID:9891047	PBO:0095859	temperature permissive for single mutant without rad2delta
PMID:9891047	PBO:0093560	temperature permissive for single mutant without rad26delta
PMID:9891047	PBO:0093560	temperature permissive for single mutant without rad26delta
PMID:9891047	FYPO:0002061	temperature permissive for single mutant without rad26delta
PMID:9891047	FYPO:0002061	temperature permissive for single mutant without rad26delta
PMID:9891047	PBO:0093561	temperature permissive for single mutant without cds1delta
PMID:9891047	PBO:0095859	temperature permissive for single mutant without rad2delta
PMID:9891047	PBO:0093560	temperature permissive for single mutant without cds1delta
PMID:9891047	PBO:0095859	temperature permissive for single mutant without rad2delta
PMID:9891047	FYPO:0002061	temperature permissive for single mutant without rad26delta
PMID:9891047	FYPO:0002061	temperature permissive for single mutant without rad26delta
PMID:9891047	FYPO:0002061	temperature permissive for single mutant without rad26delta
PMID:9891047	FYPO:0002061	temperature permissive for single mutant without rad26delta
PMID:9891047	PBO:0093560	temperature permissive for single mutant without rad26delta
PMID:9891047	FYPO:0002061	temperature permissive for single mutant without rad26delta
PMID:9891047	PBO:0095857	temperature permissive for single mutant without cds1delta
PMID:9891047	PBO:0093560	temperature permissive for single mutant without cds1delta
PMID:9891047	PBO:0095857	temperature permissive for single mutant without cds1delta
PMID:9891047	PBO:0093561	temperature permissive for single mutant without cds1delta
PMID:9891047	PBO:0095859	temperature permissive for single mutant without cds1delta
PMID:9891047	PBO:0093561	temperature permissive for single mutant without cds1delta
PMID:9891047	PBO:0095859	temperature permissive for single mutant without rad2delta
PMID:9891047	PBO:0095859	temperature permissive for single mutant without rad2delta
PMID:9891047	PBO:0095857	temperature permissive for single mutant without rad2delta
PMID:9891047	PBO:0095859	temperature permissive for single mutant without rad2delta
PMID:9891047	PBO:0095859	temperature permissive for single mutant without cds1delta
PMID:9891047	PBO:0093561	temperature permissive for single mutant without cds1delta
PMID:9891047	PBO:0095859	temperature permissive for single mutant without rad2delta
PMID:9891047	PBO:0095859	temperature permissive for single mutant without rad2delta
PMID:9891047	PBO:0095857	temperature permissive for single mutant without rad2delta
PMID:9891047	FYPO:0002061	temperature permissive for single mutant without cds1delta
PMID:9891047	PBO:0093560	temperature permissive for single mutant without cds1delta
PMID:9950674	FYPO:0002061	fig 9
PMID:9950674	FYPO:0003165	fig 9
PMID:9973368	FYPO:0001357	non-flocculating cells
PMID:9973368	GO:0036349	galactose specific flocculation should have cell-cell ahdesion parentage