pmid comment PMID:10022828 establishment, but not maintenance, of ring localization requires F-actin (assayed using latrunculin A) PMID:10022828 establishment, but not maintenance, of ring localization requires F-actin (assayed using latrunculin A) PMID:10022921 assayed using Tf1 transposon plasmid construct PMID:10022921 assayed using Tf1 transposon plasmid construct PMID:10022921 assayed using Tf1 transposon PMID:10022921 assayed using Tf1 transposon PMID:10022921 assayed using Tf1 transposon Gag and IN PMID:10087262 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 more than threefold over compared with wild-type cells (344%) PMID:10087262 translocation of actin from one end t the other (also fig7) PMID:10087262 Fig. 1 c PMID:10087262 pck2delta rescues ags1 ox defect PMID:10087262 . mok1-664pck2 was synthetically lethal at 30C, a temperature at which either single mutant could grew (Fig. 10b) PMID:10087262 . 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 . mok1-664pck2 was synthetically lethal at 30C, a temperature at which either single mutant could grew (Fig. 10b) PMID:10087262 combined localization and membrane fraction PMID:10087262 combined localization and membrane fraction PMID:10087262 data not shown PMID:10087262 Fig. 1 a, 'delocalized actin' PMID:10087262 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:10091325 activated_by CHEBI:29108 | activated_by CHEBI:18420 | inhibited_by CHEBI:16761 PMID:10207075 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 Csk1 activated both the monomeric and the Mcs2-bound forms of Mcs6. PMID:10226032 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 Surprisingly, Csk1 also activated Cdc2 in complexes with either Cdc13 or Cig2 cyclins. PMID:10364209 DNS PMID:10364209 Fig. 1B PMID:10364209 The same level of Myo2p co-immunoprecipitated with mutant Cdc4p as with wild-type Cdc4p (Fig. 5A). PMID:10364209 DNS PMID:10364209 Fig. 1B PMID:10365961 tyrosine, possibly Y188 (but not determined experimentally) PMID:10365961 tyrosine, possibly Y188 (but not determined experimentally) PMID:10365961 tyrosine, possibly Y188 (but not determined experimentally) PMID:10366596 astral PMID:10366596 The ~14-fold increase of the disomic spores indicated that chromosome missegregation increased during meiosis I PMID:10366596 in zygotic nucleus PMID:10366596 in zygotic nucleus PMID:10381387 it doesn't say old, but it is... PMID:10381387 it doesn't say old, but it is... PMID:10388806 cdc18delta::p[nmt*.cdc18+-LEU2] PMID:10388806 cdc18delta::p[nmt*.cdc18+-LEU2] PMID:10388806 Val: moved down from FYPO:0001429, its a fully penetrant inviable phenotype (anucleate) PMID:10392445 conditions under which pat1-114 alone induces meiosis & sporulation PMID:10398679 is response to heat a real process or should be resposne to denatured proteins or whatever? PMID:10398680 figure 3 (before phase 3 extension) PMID:10398680 Figure 1F & 7B (second mitosis) PMID:10398680 figure 8a PMID:10398680 Figure 1, A and B All of these required passage through G1 (second mitosis) PMID:10398680 figure 8a PMID:10398680 Figure 2 PMID:10398680 Figure 1, A and B All of these required passage through G1 (second mitosis) PMID:10398680 (Fig. 6D): Mis12 is thus required for maintaining the inner centromere structure. PMID:10398680 figure 8a PMID:10398680 figue 4 PMID:10398680 figure 3 PMID:10398680 figure3 PMID:10398680 fig 1a PMID:10398680 These results showed that Mis12 was localized at centromeres throughout the cell cycle PMID:10398680 figure 6 Hence, mis6–HA could interact with the centromere in the absence of functional Mis12. PMID:10398680 figure 6 Conversely, the mis6-302 strain integrated with the Mis12–HA gene was used. PMID:10398680 suggesting that sister centromeres were separated in the metaphase-arrested cells. PMID:10428959 Figure 5 PMID:10428959 (vw: sty1-atf1 pathway) PMID:10428959 figure 3b PMID:10428959 figure 3b PMID:10428959 table 2 PMID:10428959 figure 3 PMID:10428959 figure 3 PMID:10428959 Figure 3 (vw: severity 20.2 micron) PMID:10428959 Figure 3 (vw severity 23.4 micron) PMID:10428959 DNS PMID:10428959 figure 2C (vw: not by sty1) PMID:10428959 Figure 1/2 PMID:10428959 table 2 PMID:10428959 Figure1/2 PMID:10428959 figure 7 PMID:10428959 figure 7 PMID:10428959 Figure 6 PMID:10428959 Figure 5 PMID:10428959 (vw: sty1-atf1 pathway) PMID:10428959 figure 7 PMID:10428959 Figure 6B PMID:10430583 same as rad51delta alone PMID:10430583 same as rad51delta alone PMID:10459013 present throughout mitotic cell cycle PMID:10462529 4a PMID:10462529 fig1 PMID:10462529 fig1 PMID:10462529 fig2 PMID:10462529 fig2 PMID:10462529 Fig. 3 PMID:10462529 Fig. 3 PMID:10462529 fig5 PMID:10462529 fig5 PMID:10462529 fig5 PMID:10462529 fig 6 PMID:10462529 fig6 PMID:10462529 extension, of cdc25 7b PMID:10462529 fig 7 PMID:10462529 fig7 PMID:10462529 fig2 PMID:10462529 fig2 PMID:10462529 fig3 PMID:10462529 fig5 PMID:10462529 fig 6 PMID:10473641 broken PMID:10521402 Data not shown when rad1 is deleted checkpoint is not activated and cells attempt meiotic nuclear divisions see also Fig1, 2, 3B PMID:10521402 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 Fig 1A rad1 is required for meiotic DNA replication checkpoint PMID:10521402 Fig1B cds1 is required for meiotic DNA replication checkpoint PMID:10521402 Fig1B PMID:10521402 Fig1B PMID:10521402 Fig 1B double cds1delta chk1 delta has same phenotype as single cds1delta/cds1 delta PMID:10521402 Fig 2 A,B PMID:10521402 Fig 2 A,B PMID:10521402 Data not shown. kinetics same as pat1ts rad1delta diploid PMID:10521402 Data not shown. kinetics same as pat1ts rad1delta diploid PMID:10521402 Data not shown. kinetics same as pat1ts rad1delta diploid PMID:10521402 Data not shown prophase arrest with horsetail nuclear morphology see fig3A for pat1ts control PMID:10521402 Data not shown prophase arrest with horsetail nuclear morphology see fig3A for pat1ts control PMID:10521402 Fig3B data not shown PMID:10521402 Fig3B data not shown PMID:10521402 Fig3 B PMID:10521402 Fig3 B PMID:10521402 Fig3B PMID:10521402 Fig 4 PMID:10521402 Fig4 present during meiotic DNA replication checkpoint arrest PMID:10521402 Fig5A see control in Fig4A PMID:10521402 Fig5B see Fig4B for control PMID:10521402 Fig5A see control in Fig4A PMID:10521402 Fig 5A see Fig4A for control PMID:10521402 Fig 5A see Fig4A for control PMID:10521402 Fig6C PMID:10523629 Figure 1 a PMID:10523629 Fig 5 G PMID:10523629 Fig 5 C PMID:10523629 Fig 5 J PMID:10523629 fig 4 PMID:10523629 fig 4 PMID:10523629 fig 3 C PMID:10523629 fig 2a PMID:10523629 fig 2a PMID:10523629 Figure 1 a PMID:10523629 Figure 1 a PMID:10523629 Figure 1 a PMID:10523629 Figure 1 a PMID:10523629 Figure 1 a PMID:10523629 Figure 1 a PMID:10523629 Figure 1 a PMID:10523629 Figure 1 a PMID:10523629 Figure 1 a PMID:10523629 Figure 1 a PMID:10523629 Figure 1 a PMID:10523629 Figure 1 a PMID:10523629 Figure 1 a PMID:10526233 (it basically the same as cut except the nucleus is not bisected) PMID:10526233 (it basically the same as cut except the nucleus is not bisected) PMID:10545452 Figure 1, 0 hr PMID:10545452 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 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 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 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 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 Interestingly, unlike the drc1-191 mutant, drc1::ura4 underwent multiple nuclear division cycles causing arrested cells to accumulate up to 32 nuclei. PMID:10545452 capable of germination and establishing polarized growth, but were incapable of performing cytokinesis and did not maintain polarity (Figure 6B). PMID:10545452 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 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 Figure 1, 4 hr PMID:10545452 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 The drc1-191 rng2-D5 and drc1-191 cdc4-8 double mutants grew extremely poorly a PMID:10545452 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 capable of germination and establishing polarized growth, but were incapable of performing cytokinesis and did not maintain polarity (Figure 6B). PMID:10545452 capable of germination and establishing polarized growth, but were incapable of performing cytokinesis and did not maintain polarity (Figure 6B). PMID:10545452 At the drc1-191 arrest point all binucleate cells were found to have Cdc7p staining localized at one SPB. Merged images of chromosomal staining with DAPI and Cdc7p staining with HA antibodies is shown in Figure 4. The drc1-191 mutant, therefore, arrests at a point in the cell cycle where the septum-promoting Cdc7p is located on one SPB. PMID:10545452 i.e next round of replication PMID:10545452 i.e next round of replication PMID:10545452 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 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 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 The drc1-191 rng2-D5 and drc1-191 cdc4-8 double mutants grew extremely poorly a PMID:10545452 Figure 1, 8 hr PMID:10547441 this should be decreased thickness at old end during veg growth PMID:10567589 fig2d - number 7 and 8 PMID:10567589 3c PMID:10567589 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 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 fig2d - number 7 and 8 PMID:10574765 Figure 3 F actin is absent from non growing end PMID:10574765 Figure 3 normal at non-growing end PMID:10574765 "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 Figure 4 Ral3/cor-CGFP fusion is expressed from pMral3/cor-C PMID:10574765 Figure 4 Ral3/cor-CGFP fusion is expressed from pMral3/cor-C PMID:10574765 Figure 2a Boundary of non growing cell end maintained PMID:10574765 Figure 2b Boundary of non growing cell end maintained PMID:10574765 Figure 2c Boundary of the non growing cell end not maintained PMID:10574765 Figure 4 Ral3/cor-CGFP fusion is expressed from pMral3/cor-C PMID:10574765 Figure 3 normal at non-growing end PMID:10581266 fig6 PMID:10581266 fig4 PMID:10581266 fig6 PMID:10581266 fig9 PMID:10581266 fig6 PMID:10581266 fig9 high overexpression is lethal PMID:10588638 inferred from Chk1 phosphorylation phenotypes PMID:10588653 figure 1, after 5 hours PMID:10588653 Fig6 PMID:10588653 Fig6 PMID:10588653 figure 4 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 figure4 PMID:10588653 figure4 PMID:10588653 figure4 PMID:10588653 Fig3 synthetic rescue of cdc3 PMID:10588653 Fig3 PMID:10588653 Fig3 PMID:10588653 DNS In all tetrads, the viable colonies were Arp21 Ura2, indicating that arp21 is an essential gen PMID:10588653 figure 1c PMID:10588653 figure 1, after 8 hours, medial region of the cells continued to accumulate excess cell wall material PMID:10588653 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 DNS after 5 hours PMID:10588653 DNS PMID:10588653 DNS PMID:10588653 figure 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 Fig6 PMID:10588653 Fig6 PMID:10588653 figure (Figure 6) PMID:10588653 figure (Figure 6D) PMID:10588653 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 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 (Figure 8A). T12A protein was also labeled by the ATP analogue, but to a much lesser degree than wild-type Arp2p PMID:10588653 Fig6 PMID:10588653 (Figure 8A). Arp2-E316K mutant protein had a reduced affinity for ATP compared with wild type Arp2p PMID:10588653 8B & C These results clearly establish that the mutant Arp2-E316K protein turns over more rapidly than wild-type Arp2 protein PMID:10591634 IPI and IMP evidence PMID:10593886 only in vitro data evidence PMID:10641037 figure 3b PMID:10641037 figure 2 PMID:10641037 DNS PMID:10651902 normal volume? PMID:10651902 appeared thicker PMID:10651902 fig6 PMID:10651902 fig6 PMID:10651902 Rho1 appears to have a dual role in stabilizing and localizing Pck proteins PMID:10651902 Rho1 GTP bound form pck2 HR1 domain PMID:10683155 constant level throughout cell cycle PMID:10683155 cut if exposed to radiation during S phase, but not if exposed during G2 PMID:10698951 temperature restrictive for cdc27-P11 alone PMID:10698951 temperature restrictive for cdc27-P11 alone PMID:10712506 from materials and methods PMID:10712506 from materials and methods PMID:10712506 from materials and methods PMID:10712506 from materials and methods PMID:10718196 DNS PMID:10725227 Fig 1B G1 arrest of ded1-1D5 is dependent on rum1+ PMID:10725227 Fig4B PMID:10725227 Fig 5A 35S Methionine pulse measured incorporation PMID:10725227 Fig 5B 35S Methionine pulse, measured incorporation PMID:10725227 Fig 5B 35S Methionine pulse, measured incorporation PMID:10725227 Fig6 total protein translation not affect PMID:10725227 Fig6 total protein translation not affected PMID:10725227 Fig7C, D The protein and mRNA levels are compared to cDNA-I which is also expressed from medium strength nmt1 promoter ON PMID:10725227 Fig7 B over expression of cig2+ cDNAIII suppresses the rescue of cdc21-M68 by ded1-1D5 PMID:10725227 Fig7 B over expression of cig2+ cDNAII suppresses the rescue of cdc21-M68 by ded1-1D5 PMID:10725227 Fig7 B over expression of cig2+ cDNAI partially suppresses the rescue of cdc21-M68 by ded1-1D5 PMID:10725227 Fig8. The labelling looks wrong in this figure, not sure whether to annotate it or not PMID:10725227 Fig8. The labelling looks wrong in this figure, not sure whether to annotate it or not PMID:10725227 Fig9 PMID:10725227 Fig3B cdc13 protein presence in nuc2-663 alone PMID:10725227 Fig 1B there is a small G1 peak which get slightly bigger but they also cells arrested in G1 by -N, when refed and shifted to the restrictive temp cannot enter S phase but this is data not shown PMID:10725227 Fig9 PMID:10725227 Fig10B PMID:10725227 Fig2C ded1-61 is a cold sensitive mutant PMID:10725227 Fig2C ded1-78 is a cold sensitive mutant PMID:10725227 Fig2B PMID:10725227 Fig2B PMID:10725227 Fig2B PMID:10725227 Table 2 PMID:10725227 Table 2 PMID:10725227 Fig2B PMID:10725227 Fig2D the semi permissive temperature 34.5C for ded1-D5 allows it to suppress cdc19-P1 (mcm2) PMID:10725227 Fig3A PMID:10725227 Fig3A PMID:10725227 Table 2 PMID:10725227 Fig10A PMID:10725227 Fig 1B PMID:10725227 Fig3B cig2 protein presence in nuc2-663 alone PMID:10733588 Table2 PMID:10733588 Table2 PMID:10733588 Fig. 3D and data not shown PMID:10748059 inhibited_by(CHEBI:48828) PMID:10749926 Fig 6 PMID:10749926 Fig 6 PMID:10749926 figure 4 (spindle is still present, normally disaaembld by cytokinesis) PMID:10749926 figure 4 PMID:10749926 figure 1B PMID:10749926 figure 1B PMID:10757807 same as rqh1delta alone PMID:10757807 same as cds1delta alone PMID:10757807 same as cdc27-P11 alone PMID:10766248 severity correlates positively with overexpression level, and different isolates with same construct integrated show different Cdc18 levels PMID:10766248 severity correlates positively with overexpression level PMID:10766248 cdc18+ low level overexpression PMID:10769212 temperature restrictive for cdc4-8 alone PMID:10769212 inviable at 37 degrees; some growth at 34 degrees PMID:10769212 dependent on F-actin (assayed using Latrunculin A) PMID:10769212 temperature restrictive for cdc4-8 alone PMID:10769212 inviable at 37 degrees; some growth at 34 degrees PMID:10769212 inviable at 34 or 37 degrees PMID:10769212 temperature restrictive for cdc4-8 alone PMID:10769212 early mitosis; independent of F-actin (assayed using Latrunculin A) PMID:10769212 temperature restrictive for cdc4-8 alone PMID:10770926 activated by ATP PMID:10770926 activated by ATP PMID:10770926 activated by ATP PMID:10775265 Figure4;TableI;datanotshown PMID:10775265 Figure4;TableI;datanotshown PMID:10775265 I inferred new because it's asymmetric and we know sin is new PMID:10775265 fig 3c PMID:10775265 Figure4;TableI;datanotshown PMID:10775265 fig 3d PMID:10775265 Figure4;TableI;datanotshown PMID:10775265 Figure4;TableI;datanotshown PMID:10775265 dns PMID:10775265 I inferred new because it's asymmetric and we know sin is new PMID:10775265 Figure4;TableI;datanotshown PMID:10775265 I inferred new because it's asymmetric and we know sin is new PMID:10775265 Figure4;TableI;datanotshown PMID:10775265 Cdc7p cannot localize to the SPB(s) in cdc11 (Figure 4; Table I) PMID:10775265 Figure4;TableI;datanotshown PMID:10775265 Figure4;TableI;datanotshown PMID:10775265 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 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 Figure4;TableI;datanotshown PMID:10775265 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 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 Figure4;TableI;datanotshown PMID:10779336 1B PMID:10779336 1A increased size? PMID:10779336 3B PMID:10779336 3B PMID:10779336 3B PMID:10779336 2B PMID:10779336 2 PMID:10779336 3A PMID:10779336 5.6% PMID:10779336 3B PMID:10779336 2B PMID:10779336 2B PMID:10779336 4C PMID:10779336 2B PMID:10779336 1A PMID:10779336 fig8 PMID:10779336 3B PMID:10792724 residue=S200 PMID:10799520 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 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 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 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 is this the right term? PMID:10799520 Western analysis showed that this decrease was not due to reduced Byr4 amounts PMID:10799520 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 Figure 2E. These results show that Byr4 is re- quired to prevent septation in G1 cells. PMID:10799520 A corresponding decrease in the fraction of cells with Spg1 localized to SPBs occurred and reached 7% at 16 h (Fig. 3) PMID:10799520 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 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 combine, other binucleates should unde new term PMID:10799520 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 Cdc7-HA was not localized to SPBs during interphase (Fig. 1C, 1), PMID:10805744 not sown it is ser/thr kinase activity PMID:10805744 same as cdc2delta alone PMID:10805785 fig 1c PMID:10805785 fig 1c PMID:10805785 fig 1c PMID:10805785 fig2 PMID:10805785 fig 1c PMID:10805785 fig 1c PMID:10805785 fig 1c PMID:10805785 fig 1c PMID:10805785 fig 1c PMID:10850973 activated_by(CHEBI:18420)| activated_by(CHEBI:29103)| inhibited_by(CHEBI:48607)| inhibited_by(CHEBI:26710) PMID:10852821 fig8 myo2 clumped in nodes instead of ring PMID:10852821 fig8 myo2 clumped in nodes instead of ring PMID:10852821 fig8 PMID:10852821 fig9 PMID:10852821 fig 7A (depends on actin) PMID:10852821 fig9 PMID:10852821 fig 7A PMID:10852821 Fig 6 PMID:10852821 Fig 6 PMID:10852821 Fig 6 PMID:10852821 Fig. 3B PMID:10852821 Fig 6 PMID:10852821 Fig 6 PMID:10852821 fig8 PMID:10852821 fig8 PMID:10852821 fig8 PMID:10852821 Fig 6 PMID:10852821 fig9 maintenance PMID:10852821 Fig. 3B PMID:10852821 Fig. 3B PMID:10852821 Fig. 3B PMID:10864871 2nd division PMID:10871341 diploid; ran1 allele pat1-114 in background PMID:10871341 diploid; ran1 allele pat1-114 in background PMID:10871341 diploid; ran1 allele pat1-114 in background PMID:10871341 diploid; ran1 allele pat1-114 in background PMID:10879493 2M glucose = 36% w/v = A LOT, so it is osmolarity rather than glucose itself I guess PMID:10879493 2M glucose = 36% w/v = A LOT, so it is osmolarity rather than glucose itself I guess PMID:10886372 don't know veg or spore PMID:10905343 total alpha tubulin level reduced but not known whether from nda3 or atb2 or both PMID:10905343 total alpha tubulin level reduced but not known whether from nda2 or atb2 or both PMID:10921876 fig1a PMID:10921876 APC-SLP1 PMID:10921876 fig3 cdc25-22 block and release PMID:10921876 fig3 cdc25-22 block and release PMID:10921876 fig3 cdc25-22 block and release PMID:10921876 fig3 cdc25-22 block and release PMID:10921876 fig 3 cdc25-22 block and release PMID:10921876 fig 3 cdc25-22 block and release PMID:10921876 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 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 fig1a PMID:10921876 fig1 b PMID:10921878 during mitotic G2 arrest PMID:10930468 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 diffuse cytoplsmic throughout the cell cycle PMID:10930468 diffuse cytoplsmic throughout the cell cycle PMID:10930468 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 localized in an identical manner to wild-type mid1p (Figure 9A) and was fully functional (Figure 7 and Table 2). PMID:10930468 *******during interphase**********noNLS*-mid1p was detectable in the nucleus when expressedunder the control of mid1 promoter ( PMID:10930468 no NLS*-mid1p was detectable in the nucleus when expressed under the control of mid1 promoter ( PMID:10930468 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 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 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 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 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 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 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 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 and the generation time of the population was increased approximately two-fold (Figure 1C top). PMID:10950958 NOT PM PMID:10950958 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 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 In addition, its3-1 mutant had a septation index approximately twice that seen in wild-type cells at the permissive temperature. PMID:10950958 GFP-Its3 localized to the plasma membrane at all stages of the cell cycle (Fig. 9A). PMID:10950958 GFP-Its3 localized to the plasma membrane at all stages of the cell cycle (Fig. 9A). PMID:10950958 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 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 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 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 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 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 nterestingly, the level of PI(4)P was significantly higher than that of the wild-type cells. PMID:10950958 In wild-type cells, a shift from 27 to 33 °C caused a transient heat-induced disorganization of actin patches, PMID:10950958 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 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 PI(4)5K ac- tivity 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:10954610 steady-state labeling assay; stability increases in wt but not mutant upon UV exposure PMID:10954610 transcription run-on assay PMID:10954610 steady-state labeling assay; stability increases in wt but not sty1delta upon UV exposure PMID:10954610 transcription run-on assay PMID:10970777 decreased PMID:10970777 there is another unknown gene with this activity PMID:10978278 beta tubulin specific pathway PMID:11007487 """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 Fig 1 tip1 expressed from pREP3X PMID:11007487 Fig 1 tip1 expressed from pREP3X PMID:11007487 Fig 1 tip1 expressed from pREP3X PMID:11007487 Fig 3 H (methanol fixation) PMID:11007487 figure 4H in vitro PMID:11007487 Fig 4 PMID:11007487 Fig 6 (live cell imaging) GFP-tubulin expressed from nmt1 promoter on multi copy plasmid PMID:11007487 Fig 6 (live cell imaging) GFP-tubulin expressed from nmt1 promoter on multi copy plasmid PMID:11007487 (Figure 4I) PMID:11007487 (Figure 4I) I'm not sure if we knew it was the plus end then, but we do now ;) PMID:11007487 Fig 3 (methanol fixation) PMID:11007487 Fig 3 C PMID:11007487 Fig 4A & fig 3 G PMID:11007487 Fig 3I (Formaldehyde fixation) PMID:11007487 Fig3I PMID:11007487 Fig 1 B PMID:11007487 """These phenotypes establish that tip1p is required to properly position the growth zones at the antipodes of the cells.""" PMID:11007487 Fig 3 K (methanol fixation) PMID:11007487 Fig 3 K (methanol fixation) PMID:11007487 ( data for these cells not shown) PMID:11007487 Figures 4C and 4G PMID:11007487 Fig 3F (methanol fixation) PMID:11007487 Fig 3D PMID:11007487 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 Fig 3B PMID:11007487 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 data not shown PMID:11014802 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 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 structure PMID:11018050 Fig 5 PMID:11018050 growth assayed on agar plates at different temperature and media. PMID:11018050 growth assayed on agar plates at different temperature and media. PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 Fig 2B PMID:11018050 Fig 3 PMID:11018050 Fig 2D PMID:11018050 Data was not shown. PMID:11018050 Fig 4 PMID:11018050 Fig 2 PMID:11018050 forms microcolonies PMID:11018050 Fig 2G PMID:11018050 Fig 5 PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 Fig 6 cell tip localisation increased compared to exponentially growing cells PMID:11018050 Fig 8 and Fig 5 Tea2 is not completely delocalised but is has a more extended distribution along the microtubules PMID:11018050 Fig 8 (vw: I made this 'along micriotubule because we know its microtubule dept) PMID:11018050 Fig 6 PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media. PMID:11018050 fig 8 c PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11018050 growth assayed on agar plates at different temperature and media PMID:11027257 temp semi-permissive for spp2-8 alone PMID:11027257 temp semi-permissive for spp2-8 alone PMID:11027257 temp semi-permissive for spp2-9 alone PMID:11027257 temp semi-permissive for spp2-9 alone PMID:11027257 temp semi-permissive for spp2-9 alone PMID:11027257 higher temp, restrictive for spp2-9 alone PMID:11027257 higher temp, restrictive for spp2-9 alone PMID:11027257 higher temp, restrictive for spp2-9 alone PMID:11027257 temp semi-permissive for spp2-9 alone PMID:11027257 temp semi-permissive for spp2-9 alone PMID:11027257 temp semi-permissive for spp2-9 alone PMID:11027257 temp semi-permissive for spp2-9 alone PMID:11027257 temp semi-permissive for spp2-9 alone PMID:11027257 temp semi-permissive for spp2-8 alone PMID:11027257 temp semi-permissive for spp2-9 alone PMID:11027257 mixed population PMID:11027257 mixed population PMID:11027257 temp semi-permissive for spp2-8 alone PMID:11027257 temp semi-permissive for spp2-8 alone PMID:11027257 temp semi-permissive for spp2-8 alone PMID:11027257 higher temp, restrictive for spp2-8 alone PMID:11027257 higher temp, restrictive for spp2-8 alone PMID:11027257 higher temp, restrictive for spp2-8 alone PMID:11027257 temp semi-permissive for spp2-8 alone PMID:11027257 temp semi-permissive for spp2-8 alone PMID:11027257 temp semi-permissive for spp2-8 alone PMID:11027263 temp. restrictive for hsk1-1312 alone; fudged a bit because assayed at 32 PMID:11027263 same as hsk1-1312 alone PMID:11069657 they form parts that fail to mature PMID:11069779 **SYNTHETIC LETHAL PMID:11069779 toxic aa-analog PMID:11071923 global translation, not a specific gene PMID:11076964 dependent on F-actin (assayed using Latrunculin A) PMID:11080156 SAC- fypo/issues/2310 PMID:11080156 after passage through G1 PMID:11080156 with cut PMID:11080156 with cut at second division PMID:11084332 during G1 arrest fig4 C right hand panel PMID:11084332 total protein in proteasome mutant PMID:11084332 delayed during anaphase PMID:11084332 during anaphase PMID:11084332 total ubiquitinated PMID:11084332 total protein in proteasome mutant PMID:11084332 ubiquitinated PMID:11084332 ubiquitinated PMID:11084332 during G1 arrest fig4 C right hand panel PMID:11102508 WT 0.5% PMID:11134033 indicated by decreased polysome to monosome ratio PMID:11134033 Fig. 2 PMID:11134033 figure 1 b PMID:11134033 figure 1 b PMID:11134033 figure 1 b (I) PMID:11134033 figure 1 b (I) PMID:11134033 figure 1 C PMID:11134033 (data not shown) PMID:11134033 figure 1 a PMID:11160827 present throughout mitotic cell cycle PMID:11179424 residue not determined experimentally, but probably Y173 PMID:11226171 sequencing PMID:11226171 same sensitivity as rhp54delta alone PMID:11226171 same sensitivity as rhp54delta alone PMID:11226171 sequencing PMID:11231017 fig1 PMID:11231017 fig1 PMID:11231572 dependent on F-actin (assayed using Latrunculin A) PMID:11231572 dependent on F-actin (assayed using Latrunculin A) PMID:11238401 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 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:11250892 Fig 1 PMID:11250892 figure 3 PMID:11250892 fig 7 PMID:11250892 Figure 1 C PMID:11252721 facs and author comment about growth PMID:11260263 0.75 M PMID:11260263 Fig 2 B PMID:11260263 0.75 M PMID:11260263 Fig 2 B PMID:11279037 taf73 does not substitute for taf5 PMID:11290708 qualifier=predominantly PMID:11294895 localization requires F-actin (assayed using latrunculin A) PMID:11294895 localization requires F-actin (assayed using latrunculin A) PMID:11294895 localization requires F-actin (assayed using latrunculin A) PMID:11294907 dependent on actin cytoskeleton (assayed using Latrunculin A) PMID:11294907 dependent on actin cytoskeleton (assayed using Latrunculin A) PMID:11294907 dependent on actin cytoskeleton (assayed using Latrunculin A) PMID:11294907 dependent on actin cytoskeleton (assayed using Latrunculin A) PMID:11313455 chromatin fractionation assay PMID:11313455 chromatin fractionation assay PMID:11313455 chromatin fractionation assay; increased during response to DNA damage by MMS or ionizing radiation; dissociates during response to HU PMID:11313465 Rad3 phosphorylates T11 in response to hydroxyurea treatment PMID:11313465 cellular response to hydroxyurea PMID:11313465 phosphorylates Cds1 PMID:11331883 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 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 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 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 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 table1 PMID:11331883 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 Fig. 2c and Table 1), PMID:11350031 all taf1 introns affected PMID:11359920 30 degrees PMID:11359920 30 degrees PMID:11359920 30 degrees PMID:11359920 30 degrees PMID:11359920 30 degrees PMID:11359920 30 degrees PMID:11359920 30 degrees PMID:11359920 30 degrees PMID:11359920 30 degrees PMID:11359920 30 degrees PMID:11359928 fig 2 c PMID:11359928 Figure 4A PMID:11359928 fig 3a PMID:11359928 fig 2 c PMID:11359928 fig 8 PMID:11359928 Figure 4A PMID:11369198 fig 2B PMID:11369198 fig 2 B PMID:11369198 Figure 5b PMID:11369198 data not shown PMID:11369198 Figure 5b PMID:11369198 Figure 5b PMID:11369198 movie 1A PMID:11384993 a significant reduction in kinase activity (40% of Sid1) PMID:11384993 barely above background for vector alone and Sid1C (Fig. 2B) PMID:11387218 punctate in wild type, diffuse throughout nucleus in mutant PMID:11405625 high penetrance = large fraction of cells PMID:11432827 Figure 1 A PMID:11432827 dependent on mitotic spindle (GO:0072686) PMID:11432827 3f PMID:11432827 Figure 1 C PMID:11432827 Figure 1 A PMID:11432827 cut2 levels were reduced in alp14 mutant PMID:11432827 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 1A PMID:11432827 Figure 1 C PMID:11432827 figure 4A PMID:11432827 ind mad2 mutant loses viability PMID:11432827 2C PMID:11432827 2C PMID:11432827 1A PMID:11432827 figure 4B PMID:11432827 Figure 1 C PMID:11432827 Table 1 PMID:11432827 Figure 3A, rapid loss of viability PMID:11432827 Fig 3B PMID:11448769 (vw: sid2 phenotype indicates that Clp1 localization is independent of SIN) PMID:11493649 positive regulation of meiotic cell cycle exit PMID:11493649 negative regulation of meiotic exit PMID:11514435 (Figure 7b) heterologous complementation PMID:11514435 fig 6 PMID:11514435 from MF PMID:11514435 from MF PMID:11514435 (Figure 7D) assayed reaction products PMID:11514435 figure 1 & Figure 3B and Table 2 PMID:11514435 figure 1 PMID:11514435 figure 2a PMID:11514435 figure 2a PMID:11514435 figure 2a PMID:11514435 figure 1 Figure 3B and Table 2 PMID:11514435 Figure 4D, lane 3 PMID:11514435 fig 6 PMID:11514435 Figure 5 PMID:11514435 Figure 4D, lane 3 + figure 5 PMID:11514435 Figure 5D PMID:11514435 Figure 5 E PMID:11514435 Figure 5 E to membrane PMID:11514435 figure 7b PMID:11514435 figure 7b PMID:11514436 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 table 2, par1/2 does not supress sin phenotype PMID:11514436 table 2, par1/2 does not supress sin phenotype PMID:11514436 table 2, par1/2 does not supress sin phenotype PMID:11514436 table 2, par1/2 does not supress sin phenotype PMID:11514436 table 2, par1/2 does not supress sin phenotype PMID:11514436 table 2, par1/2 does not supress sin phenotype PMID:11514436 figure 4a PMID:11514436 table 2, par1/2 does not supress sin phenotype PMID:11514436 table 2, par1/2 does not supress sin phenotype PMID:11514436 table 2, par1/2 does not supress sin phenotype PMID:11514436 (Figure 1C, lane 8 PMID:11514436 (Figure 2A). PMID:11514436 SID PHENOTYPE (Figure 2B). PMID:11514436 figure 2b PMID:11514436 figure 3biv PMID:11514436 asymetric localization is normal PMID:11514436 dns PMID:11514436 table 2, par1/2 does not supress sin phenotype PMID:11514436 figure 3a PMID:11514436 figure 3a PMID:11514436 figure 3a PMID:11514436 figure 3biv PMID:11514436 figure 4a PMID:11514436 table 2, par1/2 does not supress sin phenotype PMID:11514436 table 2, par1/2 does not supress sin phenotype PMID:11532929 cdc25-22 background PMID:11532929 cdc25-22 background PMID:11532929 cdc25-22 background PMID:11553781 Rad3 phosphorylates S345 in response to DNA damage caused by ionizing radiation PMID:11553781 vw: changed from response to chemical to part of DNA damage checkpoint signalling PMID:11554922 evidence: immunoblot using antibody that recognizes thymine dimers PMID:11598020 fig 4a PMID:11598020 fig 4a PMID:11598020 fig 4a PMID:11598020 fig 4a PMID:11598020 fig 4a PMID:11600706 Figure 3B PMID:11600706 figure 1C PMID:11600706 figure 1C PMID:11600706 fig 2B PMID:11600706 fig 2B PMID:11600706 (vw: in vitro purification system) PMID:11600706 (vw: in vitro purification system) PMID:11600706 (vw: in vitro purification system) PMID:11606752 level of mutant cdc18deltaCDK1-5 protein PMID:1165770 Table 1, Figure 2 PMID:1165770 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 Table 1 PMID:1165770 Table 1 PMID:1165770 Table 1 PMID:1165770 Figure 3 PMID:11676915 fig 1 a PMID:11676915 figure 6 PMID:11676915 figure 6 PMID:11676915 figure 6 PMID:11676915 figure 6 PMID:11676915 figure 6 PMID:11676915 figure 6 PMID:11676915 dns PMID:11676915 fig 5c PMID:11676915 fig 5a PMID:11676915 fig 1 a PMID:11676915 fig 1 a PMID:11676915 figure 3 b PMID:11676915 figure 3 b PMID:11676915 scaffold, platform PMID:11676915 scaffold, platform PMID:11676915 scaffold, platform PMID:11676915 scaffold, platform PMID:11676915 figure 6 PMID:11676915 figure 6 PMID:11676924 colocalizes with this region and taz1, abnormal localization in taz1-delta, and physically associates with taz1 PMID:11676924 qualifier=same_pathway PMID:11683390 Figure 4A PMID:11683390 Fig 2C, pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF). PMID:11683390 Fig 2A, Fig3 Fig5D pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF). PMID:11683390 Fig 2A, Fig3 Fig5D pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF). PMID:11683390 Fig 2A, Fig 3, Fig5D pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF). PMID:11683390 Fig 2A, Fig 3, Fig5D pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF). PMID:11683390 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 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 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 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 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 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 Fig 2A b-c, Fig5 pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF). PMID:11683390 Fig 2A b-c, Fig5 pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF). PMID:11683390 Fig 2A b-c, Fig5 pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF). PMID:11683390 Fig 2A b-c, Fig5 pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF). PMID:11683390 Fig 2A b-c, Fig5D pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF). PMID:11683390 Fig 2A b-c, Fig5D pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF). PMID:11683390 Fig 2A b-c, Fig5D pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF). PMID:11683390 Fig2A pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF) PMID:11683390 Fig2A pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF) PMID:11683390 Fig2A pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF) PMID:11683390 Fig2A pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF) PMID:11683390 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 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 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 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 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 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 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 Fig 7 PMID:11683390 Fig 7 PMID:11683390 Fig 7 PMID:11683390 Fig 8 PMID:11683390 cdc2 is localised at the centromeres during horse tail movement. Fig 9 shows that cdc2YFP is associated with cen1GFP PMID:11683390 Fig 7 do not actually say it is associated with SPB just SPB region, i.e. telomere-SPB- centromere bouquet cluster PMID:11683390 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 Fig 6 Cdc13YFP and Cdc2YFP remain associated with spindle, SPB. Cdc13 is not recognised by defective APC PMID:11683390 Fig 6 Cdc2YFP and non-degradable Cdc13YFP remain associated with spindle, SPB.Cdc13 degradation is abolished rather than delayed PMID:11683390 Fig 6 PMID:11683390 Figure 4A. Cdc13YFP expressed from integrated pREP45. Decreased nuclear import of cdc2YFP compared to cdc13delta cig1delta mutant PMID:11683390 Figure 4B. Cdc13YFP expressed from integrated pREP45 PMID:11683390 Data not shown. Cdc2 does not go prematurely to the SPB in a cut12 mutant (this is the stf1-1 mutant) PMID:11683390 Figure 4A. Cdc13YFP expressed from integrated pREP45. PMID:11683390 Figure 4A. Cdc13YFP expressed from integrated pREP45 PMID:11685532 mitotic, in meiosis it is only n the kinetochore during meitoic division(metaphase/anaphase) not during prophase PMID:11694585 30 degrees C PMID:11694585 27 degrees C PMID:11694585 in vitro bundling, detected by microscopy; Figure 2 PMID:11694585 27 degrees C PMID:11694585 27 degrees C PMID:11694585 30 degrees C PMID:11694585 dependent on actin cytoskeleton (assayed using Latrunculin A) PMID:11694585 various abnormal shapes PMID:11694585 various abnormal shapes PMID:11694585 temperature restrictive for cdc4-8 PMID:11694585 temperature permissive for cdc4-8 PMID:11694585 dependent on actin cytoskeleton (assayed using Latrunculin A) PMID:11694585 assayed using purified rabbit skeletal muscle F-actin PMID:11696322 Figure 3fg PMID:11696322 data not shown PMID:11696322 figure 3 PMID:11696322 figure 3b-g PMID:11696322 Figure 4, table1 PMID:11696322 table1 PMID:11696322 figure 5bc PMID:11696322 table1 PMID:11696322 figure 5a PMID:11696322 figure 3b–g,i) PMID:11696322 igure 3b–g,i) PMID:11696322 Figure 3fg PMID:11696322 figure 5e PMID:11717425 filter binding assay PMID:11719193 magneisum activated_by(CHEBI:18420) PMID:11737264 population grows well, but very small cells look lysed PMID:11737264 population is viable but sick; can't tell which individual cells are viable PMID:11737264 population is viable but sick, and the elongated multiseptate cells are probably dead PMID:11737264 population is viable, but very small cells look lysed PMID:11737264 population is viable but sick; can't tell which individual cells are viable, but very small cells look lysed PMID:11737264 population is viable but sick; can't tell which individual cells are viable PMID:11739790 Figure 2 and Table 2 PMID:11739790 arrested PMID:11739790 arrested PMID:11739790 Figure 4, B&D PMID:11739790 Figure 4, B&D PMID:11739790 arrested PMID:11777938 figure 2 PMID:11777938 NORMAL LENGTH PMID:11781565 Fig1B PMID:11781565 Fig1B PMID:11781565 Fig1B PMID:11781565 Fig2B PMID:11781565 Fig2B PMID:11781565 Fig2B PMID:11781565 Fig2B PMID:11781565 Fig3A PMID:11781565 Fig3B PMID:11781565 Fig3B PMID:11781565 Fig1B PMID:11781565 Fig4D PMID:11781565 Fig4D PMID:11781565 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 Fig1C Shows 5 fold increase in presence of HU compared to no HU. res1 and lacZ fusion on episomal plasmids PMID:11781565 Data not shown 20 fold increase in response to res1 oe. res1 and lacZ fusion on episomal plasmids PMID:11781565 Fig2B PMID:11781565 Fig4D PMID:11781565 Fig2B PMID:11781565 Fig7B res1S130A prevents the normal down regulation of MBF dependent transcription by res1+ PMID:11781565 Fig7B res1S130A prevents the normal down regulation of MBF dependent transcription by res1+ PMID:11781565 Fig7B res1S130A prevents the normal down regulation of MBF dependent transcription by res1+ PMID:11781565 Fig6 PMID:11781565 Fig 5 res1-S130A can rescue the pat1-114 mutant at low levels of over expression PMID:11781565 Fig5 res1+ is unable to rescue the pat1-114 mutant at low levels of over expression PMID:11781565 FIg4E PMID:11781565 data not shown 8 fold increase in response to res1 oe. res1 and lacZ fusion on episomal plasmids PMID:11781565 Fig1C 5 fold increase in HU compared to no HU. res1 and lacZ fusion on episomal plasmids PMID:11781565 Fig1B PMID:11781565 Fig1B PMID:11781565 Fig1B PMID:11781565 Fig1B PMID:11792803 figure 2 a ( stretched chromaitn along elongating spindle at anaphase B) PMID:11792803 fig6 PMID:11792803 fig6 PMID:11792803 figure 2 b PMID:11792803 figure 2 b chromsome detached from spindle PMID:11792803 fig6 PMID:11792803 fig8 PMID:11792803 fig8 PMID:11792803 fig8 PMID:11792803 figure 2 b PMID:11792803 figure 2 b PMID:11818066 not really sure freq is normal, because wt not shown, but text suggests it's close PMID:11818066 does not undergo meiosis under conditions where pat1-114 single mutant does PMID:11818066 Rad24 sequesters phosphorylated Mei2, preventing Mei2 binding to meiRNA (sme2) PMID:11854402 during premeiotic DNA replication PMID:11854402 during premeiotic DNA replication PMID:11854402 during premeiotic DNA replication PMID:11854402 during premeiotic DNA replication PMID:11854402 during premeiotic DNA replication PMID:11854409 UPR PMID:11854409 UPR PMID:11854409 fig 2, 3 PMID:11854409 fig 1A inviable PMID:11854409 fig 2, 3 PMID:11854409 Figure 5A PMID:11854409 Figure 5B PMID:11854409 Figure 5C PMID:11854409 UPR PMID:11861551 fig 7a PMID:11861551 4 PMID:11861551 4 PMID:11861551 4 PMID:11861551 fig 7a PMID:11861551 fig 7 PMID:11861551 fig 1a PMID:11861551 fig 1 PMID:11861551 fig 1a PMID:11861551 fig 3 PMID:11861551 fig 3 PMID:11861551 4c PMID:11861551 igure 7 PMID:11861551 igure 7 PMID:11861765 fig 3B PMID:11861765 fig 8B PMID:11861765 fig 4B,C PMID:11861765 fig 3C PMID:11861765 fig 8A PMID:11861765 fig 8B PMID:11861765 fig 5B PMID:11861765 fig 3D PMID:11861765 fig 2 B PMID:11861765 fig 8C PMID:11861765 fig 8C PMID:11861765 fig 4A PMID:11861765 fig 4B PMID:11861765 fig 2 B PMID:11861765 fig 2 B PMID:11861765 fig 2 A PMID:11861765 fig 1 PMID:11861765 fig 4B,C PMID:11861765 fig 3A PMID:11861765 fig 4 D PMID:11861765 fig 2 PMID:11861765 fig 7B PMID:11861765 fig 3C PMID:11861765 fig 3C PMID:11861765 fig 5A PMID:11861765 fig 7C PMID:11861765 fig 3D PMID:11861765 fig 3C PMID:11861765 fig 4 D PMID:11861905 figure 1a PMID:11861905 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 figure 1a PMID:11870212 Fig. 3B PMID:11870212 movement in anap[hase A PMID:11870212 Fig. 3B PMID:11870212 Fig. 3B PMID:11870212 Fig. 3B PMID:11870212 Fig. 3B PMID:11870212 Fig. 3B PMID:11882285 fig 5a PMID:11882285 fig 2D PMID:11882285 figure 3 PMID:11882285 S1 PMID:11882285 S1 PMID:11882285 S1 PMID:11882285 S1 PMID:11882285 fig 5a ie wt like PMID:11882285 fig 1 PMID:11882285 fig 1 PMID:11882285 fig 1 PMID:11882285 fig 1 PMID:11882285 fig 1C PMID:11882285 fig 1 (3-4um normal metaphese lenght 2-2.5 um PMID:11882285 fig4 PMID:11882285 fig 2D PMID:11884512 same as rad17 single mutant, epistatic PMID:11884512 Figure 3 C PMID:11884512 data not shown PMID:11884512 data not shown PMID:11884512 3B PMID:11884512 NEM, which inhibit the Pmt3-processing activity of Ulp1, and the serine protease inhibitor PMSF, have no effect on Pmt3 deconjugating activity PMID:11884512 Of the inhibitors we tested, only iodoacetamide (10 mM) and NEM (10 mM) inhibited Ulp1 activity PMID:11884604 not much evidence of specificity for H3 vs. H4 or position PMID:11884604 broad specificity; actually inferred from combination of phenotype and sequence similarity PMID:11884604 broad specificity; actually inferred from combination of phenotype and sequence similarity PMID:11884604 broad specificity; actually inferred from combination of phenotype and sequence similarity PMID:11884604 not (coincident_with(SO:0001789) | coincident_with(SO:0001795)) PMID:11884604 actually inferred from combination of phenotype and sequence similarity PMID:11884604 actually inferred from combination of phenotype and sequence similarity PMID:11886869 storage PMID:11907273 using chromosome III PMID:11907273 2-hybrid PMID:11909965 figure 3a cell cycle arrest in mitotic ametaphase PMID:11909965 figure 3a cell cycle arrest in mitotic metaphase PMID:11909965 figure2C PMID:11909965 figure 5 PMID:11909965 figure 5A PMID:11909965 2B PMID:11909965 2B PMID:11909965 2B PMID:11909965 Fig 2A PMID:11909965 figure2C PMID:11909965 2B PMID:11909965 figure 3a DECREASDED cell cycle arrest in mitotic anaphase PMID:11927555 Figure 6 PMID:11927555 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 The double ®n1Dbub1D mutants were viable, though substantially retarded in colony formation and showed extensive chromosome segregation defects (Figure 7A). PMID:11927555 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 The double ®n1Dbub1D mutants were viable, though substantially retarded in colony formation and showed extensive chromosome segregation defects (Figure 7A). PMID:11927555 Figure 5 PMID:11927555 Figure 5 PMID:11927555 Figure 5 PMID:11927555 Figure 6 PMID:11927555 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 fig6 PMID:11927555 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 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 fig6 PMID:11927555 fig6 PMID:11927555 fig6 PMID:11927555 Figure 6 which was enhanced by the presence of the pim1-d1 mutation at 36°C to include all mitotic cells (arrowed PMID:11927555 Figure 6 PMID:11927555 (in. non mitotic cells) PMID:11927555 Double mutants between ®n1D and the temperature-sensitive allele rad21-K1 (Tatebayashi et al., 1998) were synthetically lethal at all temperatures PMID:11927555 suggesting the lethal synthetic interaction between ®n1D and cut11 might relate of the nuclear envelope rather than SPB anchoring during mitosis PMID:11950879 "indicated by ""majority of the Mad2-GFP was localized to the spindle""" PMID:11950879 "indicated by ""majority of the Mad2-GFP was localized to the spindle""" PMID:11950879 (vw: nda3 tubulin mutant does not assemble spindle and shows Mad2 is localized to unattached kinetochores) PMID:11950879 "indicated by ""majority of the Mad2-GFP was localized to the spindle""" PMID:11950884 Fig6C PMID:11950884 Fig6A PMID:11950884 Fig6A PMID:11950884 Fig 5, Table 3,4 PMID:11950884 Fig5 Table 3,4 PMID:11950884 Fig5 Table 4 PMID:11950884 Fig2A PMID:11950884 Fig2A PMID:11950884 Fig2A PMID:11950884 Fig1 PMID:11950884 Fig6B PMID:11950884 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 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 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 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 FIg 4 F location alkso exists during mating PMID:11950884 regulation of PMID:11950884 Fig6B PMID:11950884 Fig8D,E pom1 has a role in the relocalisation of actin to the shmooing cell tip PMID:11950884 Fig6C PMID:11950884 Fig6C PMID:11950884 location is abolished during mating Fig4Dc and Fig4Ec PMID:11950884 Fig6A PMID:11950927 Pic1– 765-924, which lacks the IN box, failed to bind Ark1p, PMID:11950927 Figure 6A) PMID:11950927 Figure 6A) PMID:11950927 dominent negative effect PMID:11950927 dominent negative effect PMID:11950927 dominent negative effect PMID:11950927 fig4 PMID:11950927 fig 3c PMID:11950927 fig 3c PMID:11950927 Figure2 PMID:11950927 Figure 1C PMID:11952833 premature SIN PMID:11952833 even though cdc13 is present PMID:11952833 even though cdc13 is present PMID:11955632 tRNA PMID:11967147 figure S1 PMID:11967147 figure S1 PMID:11967147 fig2a PMID:11967147 Fig 1D PMID:11967147 Fig 1D PMID:11967147 Figure 5B PMID:11967147 DNS PMID:11967147 DNs PMID:11967147 Fig 1C PMID:11967147 Fig 1A PMID:11967147 Fig 1A PMID:11967147 Fig 1A PMID:11967147 Fig 1A PMID:11967147 figure S1 (20% longer) PMID:11967147 figure S1 (20% longer) PMID:11967147 figure S1 PMID:11967147 fig2d PMID:11967147 fig2d PMID:11967147 figure S1 (20% longer) PMID:11967147 fig 5A PMID:11967147 fig 5A PMID:11967147 Figure 5D abolished pausing PMID:11967147 Figure 5D PMID:11967147 fig 5A PMID:11967147 fig2a PMID:11967147 fig2b PMID:11967147 fig2b PMID:11967147 Figure 5B PMID:11967147 Figure 5D PMID:11967147 Figure 5D PMID:11967147 Figure 5B PMID:11967147 Figure 5B PMID:11967147 Figure 5B PMID:11972332 Figure 1A PMID:11973289 "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 "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 "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 "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 "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 "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 "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 (vw: I added this as an inference, because the checkpoint is never satisfied) PMID:12000964 (vw: DNA checkpoint dept) PMID:12000964 (vw: delayed) PMID:12000964 (vw: I added this as an inference, because the checkpoint is never satisfied) PMID:12006645 tetrads only PMID:12006658 taking authors' word that ribosome profiling phenotype is specific enough to infer role in translation initiation PMID:12006658 assayed by incorporation of labeled methionine PMID:12006658 "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 polysome profiling PMID:12006658 assayed by incorporation of labeled methionine PMID:12007420 localisation of tea3 is a late event in septation PMID:12007420 Fig2D (jvh: no tea3GFP staining cell middle in nda3 block) PMID:12007420 Fig2D (jvh: tea3GFP staining cell middle after nda3 block and release) PMID:12007420 Fig3B PMID:12007420 Fig3B PMID:12007420 Fig3B PMID:12007420 Fig3B PMID:12007420 Fig4C PMID:12007420 Fig3C PMID:12007420 Fig 3D PMID:12007420 Fig3B PMID:12007420 Fig4B PMID:12007420 Fig4A PMID:12007420 Fig1D PMID:12007420 Fig1 C PMID:12007420 Fig3B PMID:12007420 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 Fig1 PMID:12007420 Fig1B PMID:12007420 Fig1 C PMID:12007420 Fig1D PMID:12007420 localises at both ends, slightly enriched at non growing end PMID:12007420 Fig2A PMID:12019258 assayed using 160-bp palindromic sequence inserted into ade6 locus PMID:12019258 assayed using 160-bp palindromic sequence inserted into ade6 locus PMID:12019258 assayed using 160-bp palindromic sequence inserted into ade6 locus PMID:12019258 assayed using 160-bp palindromic sequence inserted into ade6 locus PMID:12019258 assayed using 160-bp palindromic sequence inserted into ade6 locus PMID:12019258 assayed using 160-bp palindromic sequence inserted into ade6 locus PMID:12023299 (mah: same as rad51delta alone) PMID:12023299 (mah: sensitivity depends on how highly overexpressed top3+ is; more top3+ -> lower sensitivity) PMID:12023299 (mah: same as rqh1delta alone) PMID:12023299 (mah: same as rad51delta alone) PMID:12023299 (mah: same as rad51delta alone) PMID:12023299 (mah: localization to DSB sites also contributes to inference) PMID:12023299 (mah: assayed substrate: exogenous histone H1) PMID:12023299 (mah: same as rad51delta alone) PMID:12023299 (mah: residue=T215) PMID:12023299 (mah: slighly more severe than rad50delta alone) PMID:12023299 (mah: same as rad51delta alone) PMID:12023299 (mah: same as rad51delta alone) PMID:12023299 (mah: same as rad51delta alone) PMID:12023299 (mah: same as rad51delta alone) PMID:12034771 used endogenous tea2 gene tagged at C term with GFP. Fig1A PMID:12034771 Fig6 PMID:12034771 Fig6 PMID:12034771 Fig6 PMID:12034771 Fig5B PMID:12034771 Fig5B PMID:12034771 Fig5B PMID:12034771 Fig5A PMID:12034771 Fig5A PMID:12034771 Fig3C, Fig5A STILL TO ADD curved around cell end during mitotic interphase PMID:12034771 used endogenous tea1 gene tagged at C term with YFP and tubulin CFP for live cell imaging of tea1 on microtubules Fig1C PMID:12034771 used endogenous tea2 gene tagged at C term with GFP. Fig1A PMID:12034771 Figure 2A PMID:12034771 Fig2C OUTSTANDING Q IS IT ALONG OR ON? PMID:12034771 Fig3C PMID:12034771 Fig3C PMID:12034771 Fig4B PMID:12034771 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 Fig4A PMID:12034771 Fig3C PMID:12034771 Fig3C PMID:12034771 Fig3C PMID:12058079 activated_by(CHEBI:18420) PMID:12062100 longer transcript PMID:12062100 longer transcript PMID:12062100 longer transcript PMID:12065422 Figure 2B and C PMID:12065422 Figures 1C and 2C PMID:12065422 recessive, loss- of-function mutation PMID:12065422 Figure 2A; Table II PMID:12065422 recessive, loss- of-function mutation PMID:12065422 Table II PMID:12065422 25 degrees figure 7 PMID:12065422 25 degrees figure5d PMID:12065422 figure 5d PMID:12065422 DNS PMID:12065422 DNS PMID:12065422 25 degrees figure 7 PMID:12065422 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 Figure 1C PMID:12065422 Table II PMID:12065422 Figure 1A. We concluded that the severe phenotype of a ®n1.ts1 mutant is a transitory response to loss of Fin1 function. This implied that ®n1.D haploids adapted to loss of Fin1 after the ®rst division of a germinating spore. PMID:12065422 Figure 1B PMID:12065422 Figure 1C PMID:12074602 binds to 54-bp element at 1186-1239 PMID:12093738 Fig 3B no G1 peak is observed showing that S phase onset is not delayed PMID:12093738 Fig 3 data not shown cell viability is reduced at late time points PMID:12093738 Fig1C PMID:12093738 Fig1C PMID:12093738 Fig1C PMID:12093738 Fig1A PMID:12093738 Fig5A used forward scatter to measure cell size small peak of short cells PMID:12093738 Fig5A lower panel PMID:12093738 Fig5A lower panel used forward scatter to measure cell size PMID:12093738 Fig5B PMID:12093738 Fig 4A cells block normally with 1C DNA content even when cig2 is over expressed PMID:12093738 fypo/issues/3165 Fig5B in the absence of cig2 there is a delay in the appearance of cut cells PMID:12093738 Fig5C PMID:12093738 fypo/issues/3165 Fig5C PMID:12093738 Fig1D The protein cdc2 protein assayed is in complex with cig2 as there is no cdc2-cdc13 complex present PMID:12093738 Fig1D PMID:12093738 Fig 4B cig2 over expression also occurs when cells blocked with HU PMID:12093738 Fig 3A, D PMID:12093738 Fig 3C cig2 over expression from ~10hours after thiamine removal PMID:12093738 Fig5A small peak of less that 1C DNA content PMID:12093738 Fig2C the cdc2-cig2 and cdc2-cdc13 complexes have increased kinase activity PMID:12093738 Fig2C the cdc2-cig2 and cdc2-cdc13 complexe have no tyrosine 15 phosphorylation PMID:12112233 Figure 1 PMID:12112233 Figure 1 PMID:12112233 actually accumulation PMID:12181326 data not shown PMID:12181336 Fig 4 PMID:12181336 2 B PMID:12181336 2 B PMID:12181336 2B PMID:12181336 Fig 3 PMID:12181336 Fig 3 PMID:12181336 Fig 3 PMID:12181336 Fig 3 PMID:12181336 Fig 3 PMID:12181336 Fig 4 PMID:12181336 Fig 4 PMID:12181336 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 fig 5 PMID:12181336 fig 5 PMID:12181336 fig 5 PMID:12181336 small amount PMID:12181336 fig has 6 PMID:12181336 fig7 PMID:12181336 fig7 PMID:12185500 25 degrees C PMID:12185500 restrictive temp 36 PMID:12185500 25 degrees C PMID:12185500 27 degrees C PMID:12185500 29 degrees C PMID:12185500 25 degrees C PMID:12185500 27 degrees C PMID:12185500 29 degrees C PMID:12185500 restrictive temp 32 PMID:12185840 Figure 2C PMID:12185840 fig 2 C PMID:12186944 localization requires microtubules (assayed using thiabendazole or carbendazim) but not F-actin (assayed using latrunculin A) PMID:12186947 penetrance low if cells exposed to UV PMID:12196391 same as rad3delta alone PMID:12196391 same as either single mutant PMID:12196391 same as rad3delta alone PMID:12196391 same as rad3delta alone PMID:12196391 same as rad26delta alone PMID:12196391 same as either single mutant PMID:12196391 same as rad3delta alone PMID:12207036 Fig 6 PMID:12207036 Fig 6 PMID:12207036 Fig 6 PMID:12242222 fig 4 PMID:12242222 fig 4 PMID:12242222 fig 4 e PMID:12242294 data not shown PMID:12242294 fig8d PMID:12242294 fig8d PMID:12242294 fig 8b PMID:12242294 fig 8b PMID:12242294 figure 9 PMID:12242294 fig 1a PMID:12242294 fig 1a (maintenence of) PMID:12242294 data not shown PMID:12242294 fig 8a PMID:12242294 fig 8a PMID:12242294 data not shown PMID:12242294 data not shown PMID:12242294 fig 8a PMID:12242294 fig 8a PMID:12390246 penetrance is mentioned in EXP accompanying fig 6A PMID:12390246 fig 4a b PMID:12390246 penetrance is mentioned in EXP accompanying fig 6A PMID:12390246 Fig 6A PMID:12390246 penetrance is mentioned in EXP accompanying fig 6A PMID:12390246 penetrance is mentioned in EXP accompanying fig 6A PMID:12390246 penetrance is mentioned in EXP accompanying fig 6A PMID:12399381 figure 3 PMID:12399381 fig 5A PMID:12399381 fig 5A PMID:12399381 figure1 cdr phenotype PMID:12399381 table4 PMID:12399381 figure 6 b during x phase? PMID:12399381 semi wee PMID:12399381 figure 6A PMID:12399381 fig5 PMID:12399381 fig5 PMID:12399381 fig5 PMID:12399381 figure 4 cdr phenotype PMID:12399381 figure1 PMID:12399381 figure1 cdr phenotype PMID:12399381 figure1 PMID:12399381 figure1 PMID:12399381 fig 5A PMID:12399381 figure 4 cdr phenotype PMID:12399381 figure 4 cdr phenotype PMID:12399381 figure 4 cdr phenotype PMID:12399381 figure 4 cdr phenotype PMID:12399381 figure 4 cdr phenotype PMID:12399381 figure 4 cdr phenotype PMID:12399381 figure 4 cdr phenotype PMID:12399381 figure 5 CD PMID:12399381 fig 5 CD PMID:12399381 figure2a PMID:12399381 figure2a PMID:12399381 figure 2C/D PMID:12411492 same as plo1-ts35 alone PMID:12411492 same as plo1-ts35 alone PMID:12411492 same as plo1-ts35 alone PMID:12419251 actually ectopic expression, throughout cell cycle PMID:12419251 normal binding periodicity over cell cycle PMID:12419251 normal binding periodicity over cell cycle PMID:12419251 actually ectopic expression, throughout cell cycle PMID:12419251 normal binding periodicity over cell cycle PMID:12426374 (see rows 4±6 in Figure 1B) PMID:12426374 Figure 1A and C PMID:12426374 Figure 1B rows 4±6 PMID:12426374 figure 1 B PMID:12426374 (vw: assayed by increased mad2 at kinetochore - checkpoint active) PMID:12426374 (vw: assayed by increased mad2 at kinetochore - checkpoint active) PMID:12426374 Figure 1A and C PMID:12426374 (see rows 4±6 in Figure 1B) PMID:12427731 assayed using myelin basic protein; doesn't rule out tyrosine phosphorylation PMID:12427731 substrate myelin basic protein PMID:12427731 based just on this paper, candidate for involved_in_or_regulates qualifier PMID:12442907 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 (Figs. 3A and 3B). PMID:12442907 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 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 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 Table 1 PMID:12442907 (Figs. 3A and 3B). there were cells that initiated and completed the mitosis in a small portion (Table 1), which eventually led to cell proliferation until the stationary phase (Fig. 2A). PMID:12442907 As shown in Fig. 2A, the rate of cell proliferation was immediately reduced after the amount of Rrg1 was increased. PMID:12455694 32 degrees; mcl1-1 semi-permissive PMID:12455694 32 degrees; mcl1-1 semi-permissive PMID:12479804 Figure 2 PMID:12479804 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 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 fig 1B PMID:12479804 Figure 2A, panels 11 and 14 PMID:12479804 Figure 2A, panels 11 and 14 PMID:12479804 Figure 2D PMID:12479804 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 (faintly) Figure 3A, panel 2, arrowhead PMID:12479804 Figure 3A, panel 3 PMID:12479804 Figure 3A, panel 3 PMID:12479804 Figures 3E and 3F PMID:12479804 Figures 3E and 3F PMID:12479804 Figures 3E and 3F) PMID:12479804 Figures 3E and 3F) PMID:12479804 Figures 3E and 3F) PMID:12479804 Figures 3E and 3F) PMID:12479804 Figures 3E and 3F) PMID:12479804 Figures 3E and 3F) PMID:12479804 Figures 3E and 3F) PMID:12479804 Figure 4A 10% (2/20) of anaphase cells displayed Dma1p-GFP SPB signal PMID:12479804 Table1 PMID:12479804 Table1 PMID:12479804 Table1 PMID:12479804 Table1 PMID:12479804 Table1 PMID:12479804 Figure 4A PMID:12479804 Figure 4B) PMID:12479804 igure 4C, bottom PMID:12479804 igure 4C, bottom PMID:12479804 Fig4 PMID:12479804 Figure 5 PMID:12479804 Figure 5 PMID:12479804 fig 5 PMID:12479804 fig6 PMID:12479804 fig6 PMID:12482946 Fig. 2A PMID:12482946 Fig. 2B PMID:12482946 Fig. 2B PMID:12482946 Fig. 1D PMID:12482946 Fig. 2B PMID:12482946 Fig. 2B PMID:12526748 Figure S1 PMID:12526748 fig1 PMID:12526748 fig3 PMID:12526748 fig3 PMID:12526748 fig3 PMID:12526748 fig3 PMID:12526748 Figure S1 PMID:12526748 Figure S1 PMID:12526748 Pst1p colocalizes with the otr/imr region in a cell cycle-specific manner. PMID:12526748 fig1b PMID:12526748 fig3 PMID:12526748 D.N.S? PMID:12526748 D.N.S? PMID:12526748 D.N.S? PMID:12526748 figure1e PMID:12526748 figure1e PMID:12526748 figure1e PMID:12526748 figure1e PMID:12526748 Figure 1C PMID:12526748 Figure S1 PMID:12526748 fig1 PMID:12526748 fig1 PMID:12526748 fig3 PMID:12526748 figure1e PMID:12526748 fig3 PMID:12526748 fig3 PMID:12526748 fig1 PMID:12546793 (Figure 1B) n G2-arrested cdc2-17 cells overexpressing spg1p, cdc11p was predominantly in the hyperphosphorylated form PMID:12546793 (Figure 1A) In a mob1-R4 byr4::ura4 mutant, and also in cdc16-116 grown for 5 hr at 36C, cdc11p accumulated in the hyperphosphorylated (3) form PMID:12546793 (Figure 1A) In a mob1-R4 byr4::ura4 mutant, and also in cdc16-116 grown for 5 hr at 36C, 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 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 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 (Figure 1C, and data not shown) Immunofluorescence indicated that both byr4p and cdc7p showed a normal, asymmetric distribution during mitosis PMID:12546793 (Figure 1C, and data not shown) Immunofluorescence indicated that both byr4p and cdc7p showed a normal, asymmetric distribution during mitosis PMID:12546793 (see the Supplementary) Additional experiments indicated that neither mph1p nor fin1p regulate the phosphorylation of cdc11p PMID:12546793 (see the Supplementary) Additional experiments indicated that neither mph1p nor fin1p regulate the phosphorylation of cdc11p PMID:12546793 (see the Supplementary) Additional experiments indicated that neither mph1p nor fin1p regulate the phosphorylation of cdc11p PMID:12546793 (Figure 1D) The hyperphosphorylated form (3) of cdc11p was observed during mitosis in both sid2-250 and sid1- 239 mutants PMID:12546793 (Figure 1D) The hyperphosphorylated form (3) of cdc11p was observed during mitosis in both sid2-250 and sid1- 239 mutants PMID:12546793 (Figure 1D) The hyperphosphorylated form (3) of cdc11p was observed during mitosis in both sid2-250 and sid1- 239 mutants PMID:12546793 (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 (DNS) PMID:12546793 (Figure 1G) No significant hyperphosphorylation of cdc11p occurred at 36C. PMID:12546793 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 (Figure 1G) No significant hyperphosphorylation of cdc11p occurred at 36C . PMID:12546793 (Figure 2B). Immunofluorescence showed that byr4p was also present on the SPB in the arrested cells PMID:12546793 SIN signalling complex PMID:12546793 SIN signalling complex PMID:12546793 Less than 10% of these cells had cdc7p on the spindle pole body, consistent with previous studies [25]. PMID:12546793 (Figure 3B). However, at 36C, when cdc11p is no longer associated with the SPB [3, 4], most of the cdc11p was hypophosphory- lated (form 1) PMID:12565823 Fig 4a PMID:12565827 Fig. 2C PMID:12565827 Fig. 2C PMID:12589755 same as crb2delta alone PMID:12604790 assayed with other MCM subunits present PMID:12606573 figure 7A PMID:12606573 figure 7B PMID:12606573 figure 7B PMID:12606573 Figure 4E PMID:12606573 Figure 7A PMID:12606573 figure 7A PMID:12606573 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 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 decreased rate of spindle phase I elongation (70 mins. vs 40 wt) PMID:12606573 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 figure 7A PMID:12606573 in vitro assay for activity, phenotype for process PMID:12606573 Figure 3A during spindle checkpoint PMID:12606573 Figure 7Ca PMID:12646585 kinase activity increases in presence of salt PMID:12653962 fig 6B PMID:12653962 fig 6B PMID:12653962 fig 6B PMID:12653962 fig 6B PMID:12654901 not shown PMID:12654901 not shown PMID:12654901 fig2 PMID:12654901 Fig 6 PMID:12654901 fig 3 PMID:12654901 fig7a PMID:12654901 not shown PMID:12654901 fig 7 PMID:12654901 not shown PMID:12654901 not shown PMID:12654901 Fig 6 PMID:12654901 Fig 6 PMID:12654901 Fig. 4, B and C)I PMID:12654901 data not shown PMID:12654901 fig2 maximum 3 septa PMID:12654901 fig2 PMID:12654901 """exhibited well- defined, normal actin rings""" PMID:12654901 fig7c PMID:12654901 fig 8 PMID:12654901 fig 8 PMID:12654901 Fig 6 PMID:12654901 fig7b PMID:12654901 fig2 maximum 3 septa PMID:12668659 fig5 PMID:12668659 fig1 PMID:12668659 fig1 PMID:12668659 unpublished obsevation PMID:12668659 unpublished obsevation PMID:12668659 Fig8 PMID:12668659 Fig8 PMID:12668659 fig2a PMID:12668659 Fig. 3 A, lanes 1 and 7 PMID:12668659 Fig. 3 A, lanes 1 and 7 (control) PMID:12668659 Fig8 PMID:12668659 Fig3 PMID:12668659 Fig3 PMID:12668659 Fig3 PMID:12668659 Fig3 PMID:12668659 Fig. 3 C PMID:12668659 Fig. 3 C PMID:12668659 fig4 PMID:12668659 fig4 PMID:12668659 fig5 PMID:12668659 fig5 PMID:12668659 fig5 PMID:12668659 fig2a colocalizes with sep3 PMID:12668659 fig5 PMID:12668659 fig5 PMID:12668659 fig5 PMID:12668659 fig5 PMID:12668659 fig5 PMID:12668659 Fig. 7 D PMID:12668659 fig5 PMID:12668659 Fig8 PMID:12668659 Fig8 PMID:12668659 fig1 PMID:12676088 telomerase regulator PMID:12697806 after 100 generations PMID:12715160 salt stress PMID:12715160 salt stress PMID:12719471 at anaphase? PMID:12719471 abolished PMID:12719471 at anaphase? PMID:12759375 meiosis II PMID:12764130 Fig3B ii PMID:12764130 Fig 1B,C demonstrates in vitro kinase activity. 2A in vivo PMID:12764130 Fig1 GST tea1 directly phosphorylated by Shk1 in vitro Fig2A GST-tea1 is phosphorylated in vivo in a Shk1 dependent manner PMID:12764130 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 Fig3A tea1 delta is a temperature dependent suppressor of loss of skb15 PMID:12764130 Fig3Biii Cells shown a normal tea1 delta morphology PMID:12764130 Fig 4B PMID:12764130 Fig 4B PMID:12764130 Fig4C,D Cells shown a normal tea1 delta actin morphology PMID:12764130 Fig 4E PMID:12764130 Fig4F Cells have a similar defect to a tea1 delta cell wall defect PMID:12764130 Fig 5B PMID:12764130 Fig 5C,D PMID:12764130 Data not shown PMID:12764130 Fig5D PMID:12764130 Fig 6B,C PMID:12764130 Fig6D PMID:12764130 Fig 7A PMID:12764130 Fig 7B,C Penetrance refers to the penetrance of the NTR old-new end growth pattern PMID:12764130 Fig8. pREP3X tea1 is a multi copy plasmid and is over expressed from the nmt1 promoter PMID:12764130 Data not shown. pREP3X tea1 is a multi copy plasmid and is over expressed from the nmt1 promoter PMID:12773390 fig 4 a PMID:12773390 fig 4 a PMID:12773390 Figure 4A and B PMID:12773390 Figure 7A and B PMID:12773390 Figure 7A and B PMID:12773390 Figure 5B PMID:12773390 Figure 4A and B PMID:12773390 Fig 6 a PMID:12773390 Fig 6 a PMID:12773390 Figure 7A and B PMID:12773390 Fig 1 a PMID:12773390 Fig 1 a PMID:12773390 Fig 1 a PMID:12773390 figure 1 a PMID:12773390 figure 1 b (is described as a pair, but is cylindrical short and wide.... PMID:12773390 figure 1 a PMID:12773390 figure 1 a PMID:12773390 figure 1 E PMID:12773390 figure 1 E PMID:12773390 figure 1 E PMID:12773390 figure 1 E PMID:12773390 figure 1 F PMID:12773390 figure 1 F PMID:12773390 Fig 2 PMID:12773390 Fig 2 PMID:12773390 fig 3 a PMID:12773390 fig 3 a PMID:12773390 fig 3 a PMID:12773390 fig 3 a PMID:12773390 fig 3 a PMID:12773390 fig 3 a PMID:12773390 fig 3 b (WT 11%) PMID:12773390 fig 3 b (WT 11%) PMID:12773576 Figure 6C PMID:12773576 Figure 6C PMID:12773576 increased spatial extent of heterochromatin assembly (JUST, not at prpote4in coding gene!) PMID:12773576 outer repeats PMID:12773576 increased spatial extent of heterochromatin assembly (JUST) PMID:12773576 normal spatial extent of heterochromatin assembly (JUST) PMID:12773576 Figure 6A, 6B PMID:12773576 Figure 6C PMID:12773576 Figure 6C PMID:12789340 inferred from combination of FYPO:0005798 and FYPO:0005828 PMID:12791993 Fig 1B cell cycle arrest with post anaphase microtubule array PMID:12791993 Fig2 E,F PMID:12791993 Fig 3E PMID:12791993 Fig 3C PMID:12791993 Fig 3E PMID:12791993 Fig 3C PMID:12791993 Fig 3E, F. PMID:12791993 Fig 3C PMID:12791993 Fig 3C PMID:12791993 Fig1A PMID:12791993 Fig 3A PMID:12791993 data not shown PMID:12791993 Fig2 E,F PMID:12791993 data not shown PMID:12791993 data not shown PMID:12791993 Fig 1A PMID:12791993 Fig 1B, C Cells arrest with a stable actinomyosin ring and fail to undergo cytokinesis PMID:12791993 Fig 4D, E, F PMID:12791993 Fig 4D, E, F PMID:12791993 Fig 4D PMID:12791993 Fig 4C (displacemetn is supressed by inhibiting membrane trafficking PMID:12791993 data not shown PMID:12796476 figure 1D but lacked both actin con- tractile rings and polarized actin patches (Fig. 1 D) PMID:12796476 control, functional fragment PMID:12796476 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 figure 1D impressive enrichment of actin filaments in ab- errant thick cables and aster-like accumulations PMID:12796476 figure 1D impressive enrichment of actin filaments in ab- errant thick cables and aster-like accumulations PMID:12796476 figure 1D but lacked both actin con- tractile rings and polarized actin patches (Fig. 1 D) PMID:12796476 figure 1D arrested after 24 h (Fig. 1 E) PMID:12796476 abnormal (partial, broad, and misoriented) septa (Fig. 1 G) PMID:12796476 barbed end actin capping PMID:12796476 MF? PMID:12796476 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 actin binding inhibitor pointed end PMID:12805221 referred to in PMID:33137119 PMID:12808043 dependent on sme2 expression PMID:12810074 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 Fig. 2B PMID:12815070 Figs.1A,4C) PMID:12815070 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 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 Both plo1.ts2 and plo1.ts19 conferred temperature sensitivity for growth on minimal medium PMID:12815070 Both plo1.ts2 and plo1.ts19 conferred temperature sensitivity for growth on minimal medium PMID:12815070 ability to form colonies o nrich medium at 36°C was indistin- guishable from that of wild-typec ells PMID:12815070 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 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 ability to form colonies o nrich medium at 36°C was indistin- guishable from that of wild-typec ells PMID:12815070 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 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 triple cut12.s11 cdc25.22 plo1.ts19 cells were unable to grow (Fig. 9A). PMID:12815070 Fig. 2A; PMID:12815070 Fig. 2A; PMID:12815070 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 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 Unlike classic “cut” mutants (Hirano et al. 1986), septation did not always follow on from the mi- toticarrest. PMID:12815070 plo1.ts2 strains entered mitosis but did not form spindles PMID:12815070 plo1.ts2 strains entered mitosis but did not form spindles PMID:12815070 Fig. 2A; PMID:12815070 We concluded thatthePlo1-dependentkinaseactivityofbothplo1.ts2 andplo1.ts19wasgreatlyreduced. PMID:12815070 Western blot analysis showed that Plo1 levels in plo1.ts2cellswerenotradicallydifferentfromwildtype, PMID:12815070 We concluded thatthePlo1-dependentkinaseactivityofbothplo1.ts2 andplo1.ts19wasgreatlyreduced. PMID:12815070 full-lengthproteinappearedtobelargely absent from plo1.ts19 on either minimal or rich medium at either 25°C or 36°C (Fig. 7B) PMID:12815070 full-lengthproteinappearedtobelargely absent from plo1.ts19 on either minimal or rich medium at either 25°C or 36°C (Fig. 7B) PMID:12815070 Plo1.K65R,the“kinasedead”mutantprotein,onlyas- sociatedwithmitoticbutnotwithinterphaseSPBs(data not shown). PMID:12815070 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:12840005 assayed using RTS1 mut2 or mut8 on plasmid PMID:12840005 assayed using RTS1 mut2 or mut8 on plasmid PMID:12840005 assayed using RTS1 mut2 or mut8 on plasmid PMID:12840005 assayed using RTS1 mut2 or mut8 on plasmid PMID:12840005 assayed using RTS1 mut2 or mut8 on plasmid PMID:12840005 assayed using RTS1 mut2 or mut8 on plasmid PMID:12857865 data not shown PMID:12857865 Fig4 PMID:12857865 Fig4 PMID:12857865 Fig 2/3 PMID:12857865 Figure 6A PMID:12857865 Figure 6A PMID:12857865 Figure 7 (this protrusion is opposite side of nucleus to the SPB) PMID:12857865 Fig4 PMID:12857865 Figure 7 (this protrusion is opposite side of nucleus to the SPB) PMID:12857865 data not shown PMID:12857865 Figure 7 PMID:12861005 same as taz1d alone PMID:12861005 same as taz1d alone PMID:12861005 same as taz1d alone PMID:12861005 same as taz1d alone PMID:12861005 same as taz1d alone PMID:12861005 same as taz1d alone PMID:12861005 same as rad51d alone PMID:12861005 same as taz1d alone PMID:12868054 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 fig 6 PMID:12868054 fig 5 PMID:12868054 2b PMID:12868054 Fig3 PMID:12868054 n liquid YES medium at 27 ◦ C, the cells had a doubling time of ∼8 h, in contrast to 2 h 30 min for wild-type cells. PMID:12868054 fig 7 prevacuolar compartment membrane PMID:12868054 fig 7a PMID:12868054 strong sensitiv- ity to 100 mM CaCl2 (Figure 4A) PMID:12868054 at 5 μg/ml PMID:12868054 4 mM PMID:12871901 Northern blot PMID:12871901 homozygous diploid PMID:12871901 homozygous diploid PMID:12871901 permissive for cdc25-22; restrictive for cdt2-M1 PMID:12888492 IGI with cerevisiae PMID:12893961 fig5 PMID:12893961 fig3 PMID:12893961 fig4 PMID:12893961 fig4 PMID:12893961 fig4 PMID:12893961 fig4 PMID:12893961 fig3 PMID:12894167 """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 LOCALIZES OK, IS NOT RETAINED PMID:12925774 during mitotic DNA replication initiation PMID:12930956 assayed in pku80d haploid derived from pku80d pku+ heterozygous diploid PMID:12951601 fig 1a thinner discontinuous spindles fypo/issues/3208 PMID:12951601 Fig 1d PMID:12951601 Fig 1d PMID:12951601 Fig 1e PMID:12951601 Fig. 1c, cells 1 and 3 Furthermore, multiple Mad2 dots, which have never been seen in wild type cells PMID:12951601 Fig 1d PMID:12951601 Fig 1d PMID:12966087 epistasis with Rhp51 PMID:12966087 epistasis with Rhp51 PMID:12972434 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 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 e pyruvate kinase, thiazole biosynthetic enzyme, and ribosomal protein L25-A PMID:12972571 mcm4ts-td phenotype indicates that Cdc23 chromatin localization is independent of Mcm4 PMID:12972571 late anaphase PMID:12972571 late anaphase PMID:12972571 Promoter nmt1 PMID:1314171 inhibited by CCCP PMID:1316996 cdc2-A21 suppresses mitotic catastrophe at high temperature PMID:1316996 Hi used as substrate PMID:1316996 HI used as substrate PMID:1316996 Hi used as substrate PMID:1316996 cdc2-E9 suppresses mitotic catastrophe at high temperature PMID:1316996 cdc2-E8 suppresses mitotic catastrophe at high temperature PMID:1316996 HI used as substrate PMID:1316996 cells inviable at all temperatures in presence of wee1+ PMID:1316996 G2 arrest shown by FACS analysis. PMID:1316996 crosses with this mutant generate a high level of diploids. PMID:1316996 G2 arrest shown by FACS analysis. PMID:1324908 regulated by inositol PMID:1324908 regulated by inositol PMID:1324908 GO:0008444 CDP-DG synthase and GO:0003882 PS synthase PMID:1332977 phosphorylated and dephosphorylated forms both active; no PR col 17 because no evidence that dephosphorylated form is physiologically relevant (dephosphorylated in vitro) PMID:1332977 3 sites in N-terminus (1-75) and 7 in C-terminus (1221-1485), but positions not determined PMID:1372994 val: I used this to link to process term even though it isn't shown directly in this paper PMID:1372994 AL added as BP since Val had added it involved_in on MF PMID:1396704 activated_by(CHEBI:17234) PMID:1427071 hydroxyurea absent PMID:14519123 fig3 PMID:14519123 fig4 PMID:14519123 fig4 PMID:14519123 fig4 PMID:14519123 fig3 PMID:14528010 is not a resolvase - makes symmetric cuts on opposed strands across the junction but does not convert products to linear DNA molecules PMID:14528010 specific for dsDNA at ds/ssDNA junction PMID:14532136 there is good evidence for this, but not bullet proof PMID:14585996 in presence of hydroxyurea PMID:14585996 residue S604 PMID:14585996 phenotype indicates that mrc1/Phos:S604 has higher affinity for chromatin than Unphos:S604 PMID:14585996 residue S604 PMID:14585996 in presence of hydroxyurea PMID:14599746 rationale: increased transversion frequency indicates that 8-oxoG persists more in mutant, but normal indel frequency suggests not NER PMID:14599746 inferred from increased mutation rate upon UV exposure in mutant PMID:14602073 late interphase; independent of F-actin (assayed using Latrunculin A) PMID:14602073 late interphase; independent of F-actin (assayed using Latrunculin A) PMID:14602073 late interphase; independent of F-actin (assayed using Latrunculin A) PMID:14602073 late interphase; independent of F-actin (assayed using Latrunculin A) PMID:14602073 before late interphase PMID:14602073 late interphase; independent of F-actin (assayed using Latrunculin A) PMID:14602073 late interphase; independent of F-actin (assayed using Latrunculin A) PMID:14602073 late interphase; independent of F-actin (assayed using Latrunculin A) PMID:14602073 independent of F-actin (assayed using Latrunculin A) PMID:14602073 dependent on F-actin (assayed using Latrunculin A) PMID:14602073 dependent on F-actin (assayed using Latrunculin A) PMID:14602073 dependent on F-actin (assayed using Latrunculin A) PMID:14602073 dependent on F-actin (assayed using Latrunculin A) PMID:14602073 dependent on F-actin (assayed using Latruncilin A) PMID:14602073 dependent on F-actin (assayed using Latrunculin A) PMID:14602073 dependent on F-actin (assayed using Latrunculin A) PMID:14602073 late interphase; independent of F-actin (assayed using Latrunculin A) PMID:14602073 late interphase; independent of F-actin (assayed using Latrunculin A) PMID:14602073 late interphase; independent of F-actin (assayed using Latrunculin A) PMID:14612233 activated_by(CHEBI:29108)| activated_by(CHEBI:29035) PMID:14633985 Figure 4E). PMID:14633985 fig1 PMID:14633985 fig1 PMID:14633985 fig1c PMID:14633985 fig1c PMID:14633985 fig1c PMID:14633985 fig1c PMID:14633985 As shown in Figure 2C, H2O2 induced robust phosphorylation of Spc1 in csx1D cells..... Csx1 is not necessary for Spc1 activation. PMID:14633985 fig1 PMID:14633985 fig1 PMID:14633985 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 the large increase in atf1+ mRNA that is induced by H2O2 in wildtype cells was abolished in csx1D cells. PMID:14633985 This decrease correlated with a large drop in the amount of Atf1 protein (Figure 4C). PMID:14633985 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 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 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 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 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 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 (Figure 6B). decreased stability in response to oxidative stress PMID:14633985 from genetics and Sty1 consensus. Later papers say Activated Sty1 also phosphorylates Csx1 PMID:14633985 Figure 7A PMID:14633985 decreased stability in response to oxidative stress (Figure 6B) PMID:14633985 (Figure 6B) decreased stability in response to oxidative stress PMID:14633985 (Figure 6B) decreased stability in response to oxidative stress PMID:14648198 actually inferred from combination of phenotypes, prior knowledge about MBF proteins, and MCBs in promoters, but just using IMP is simpler PMID:14648198 actually inferred from combination of phenotypes, prior knowledge about MBF proteins, and MCBs in promoters, but just using IMP is simpler PMID:14648198 actually inferred from combination of phenotypes, prior knowledge about MBF proteins, and MCBs in promoters, but just using IMP is simpler PMID:14648198 actually inferred from combination of phenotypes, prior knowledge about MBF proteins, and MCBs in promoters, but just using IMP is simpler PMID:14648198 actually inferred from combination of phenotypes, prior knowledge about MBF proteins, and MCBs in promoters, but just using IMP is simpler PMID:14648198 actually inferred from combination of phenotypes, prior knowledge about MBF proteins, and MCBs in promoters, but just using IMP is simpler PMID:14648198 actually inferred from combination of phenotypes, prior knowledge about MBF proteins, and MCBs in promoters, but just using IMP is simpler PMID:14648198 actually inferred from combination of phenotypes, prior knowledge about MBF proteins, and MCBs in promoters, but just using IMP is simpler PMID:14648198 actually inferred from combination of phenotypes, prior knowledge about MBF proteins, and MCBs in promoters, but just using IMP is simpler PMID:14654689 also inferred from localization to telomere PMID:14654689 same as rad11-D223Y alone PMID:14654689 same as rad11-D223Y alone PMID:14654689 same as rad50delta alone PMID:14730319 Fig. 4d, e) PMID:14730319 Fig. 2c PMID:14730319 fig 2a PMID:14730319 Fig. 4c) PMID:14730319 Fig. 4d PMID:14730319 Fig. 2c PMID:14730319 Fig. 2c PMID:14730319 fig 2a PMID:14730319 fig 2 and 3d PMID:14730319 Fig. 4c) PMID:14730319 Fig. 4c) PMID:14730319 Fig. 4a) PMID:14730319 Fig. 4a) PMID:14739927 interaction increases during cellular response to UV PMID:14739927 proteins dissociate during cellular response to UV PMID:14742702 Figure 8E PMID:14742702 Figure 1A PMID:14742702 Figure 1A inferred from increased duration of mitosis PMID:14742702 Figure 1B PMID:14742702 Figure 1B PMID:14742702 Figure 1C PMID:14742702 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 Figure 1C PMID:14742702 Figure 1D PMID:14742702 Figure 1D PMID:14742702 Figure 2A PMID:14742702 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 Figure 2D PMID:14742702 Figure 1D PMID:14742702 Figure 2A PMID:14742702 Figure 3B PMID:14742702 Figure 3B PMID:14742702 Figure 4A PMID:14742702 Figure 3B PMID:14742702 Figure 3B PMID:14742702 Figure 4D PMID:14742702 Figure 4D PMID:14742702 Figure 4E PMID:14742702 Figure 4F PMID:14742702 Figure 5A, lane 4 PMID:14742702 Figure 5A, lane 4 PMID:14742702 Figure 6A PMID:14742702 Figure 6A PMID:14742702 Figure 6B PMID:14742702 8C PMID:14742702 Figure 8E PMID:14742702 Figure 8E PMID:14742702 Figure 8E PMID:14742702 Figure 8E PMID:1475195 other evidence = iodine staining PMID:14766746 filter binding assay PMID:14766746 filter binding assay PMID:14766746 filter binding assay PMID:14766746 filter binding assay PMID:14972679 Figures 1A and 2 PMID:14972679 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:14972679 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 Figures 1A and 2 PMID:14972679 Figures 1A and 2 PMID:14972679 Figures 1B PMID:14972679 Figures 1B PMID:14972679 Figures 1B PMID:14972679 Figures 1A and 2 PMID:15004232 Figure 5F PMID:15040954 qualifier=major PMID:15047861 fig1 PMID:15047861 DNS PMID:15047861 fig1 PMID:15047861 fig1 PMID:15047861 fig1 PMID:15047861 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 fig6 PMID:15047861 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 Figure 3B, a–c PMID:15047861 fig1 PMID:15047861 fig1 PMID:15047861 fig1 PMID:15047861 fig1 PMID:15047861 fig8c PMID:15047861 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:15052323 Mix of IMP evidence & a proxy assay for hydrolase function PMID:15062095 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 Fig. 7 PMID:15068790 Fig. 7 PMID:15068790 Fig. 7 PMID:15068790 Fig. 1 PMID:15068790 Fig. 1 PMID:15068790 Fig. 1 PMID:15068790 Fig. 1 PMID:15068790 Fig. 1 PMID:15068790 Fig. 1 PMID:15068790 Fig. 1 PMID:15068790 Fig. 1 PMID:15068790 Fig. 1 PMID:15068790 Fig. 2 PMID:15068790 Fig. 2 PMID:15068790 Fig. 2 PMID:15068790 Fig. 2 PMID:15068790 Fig. 6 PMID:15068790 Fig. 6 PMID:15068790 Fig. 7 PMID:15121844 three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site PMID:15121844 three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site PMID:15121844 three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site PMID:15121844 three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site PMID:15121844 three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site PMID:15132994 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 Fin1 failed to bind to the SPB when byr4+ was deleted (Table 1). PMID:15132994 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 fig 1 c PMID:15132994 Fin1 binds Byr4. (A) Fin1 failed to associate with SPBs when the SIN was either inactive or hyperactive. PMID:15132994 fig 1 c PMID:15132994 is this the correct term? PMID:15147872 fig 4 abnormally segregating nuclear membrane #2863 PENDING PMID:15147872 fig 3a PMID:15147872 fig 2 PMID:15147872 table1 PMID:15147872 table1 PMID:15147872 table1 PMID:15147872 fig 1 c. figure 2 PMID:15147872 fig 1 a b PMID:15147872 fig 1 a b PMID:15155581 Fig 4 PMID:15155581 Fig 4 PMID:15155581 Fig 1 PMID:15155581 Fig 1 PMID:15155581 Fig 3 PMID:15155581 Fig 5 PMID:15155581 Fig 5 PMID:15155581 Fig 4 PMID:15155581 Fig 4 PMID:15155581 Fig 1 PMID:15155581 Fig 1 PMID:15155581 Fig 1 PMID:15155581 Fig 1 PMID:15155581 Fig 1 PMID:15155581 Fig 1 PMID:15155581 Fig 1 PMID:15155581 Fig 1 PMID:15155581 Fig 3 PMID:15155581 Fig 1 PMID:15155581 Fig 3 PMID:15155581 Fig 3 PMID:15155581 Fig 4 PMID:15155581 Fig 3 PMID:15155581 Fig 3 PMID:15155581 Fig 3 PMID:15155581 Fig 3 PMID:15155581 Fig 2 PMID:15155581 Fig 2 PMID:15155581 Fig 2 PMID:15155581 Fig 2 PMID:15155581 Fig 2 PMID:15155581 Fig 3; same as either single mutant PMID:15155581 Fig 3 PMID:15155581 Fig 3 PMID:15155581 Fig 3 PMID:15155581 Fig 5 PMID:15155581 Fig 5 PMID:15155581 basal phosphorylation on T412 & S423 PMID:15155581 Fig 3 PMID:15155581 Fig 3 PMID:15155581 Fig 5 PMID:15155581 Fig 5 PMID:15155581 Fig 3 PMID:15161942 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 residue T11 PMID:15173168 residue T11 PMID:15173168 inferred from phenotypes of mrc1delta, rad3delta, Cds1-Rad26 fusion, other cds1 alleles, and combinations thereof PMID:15173168 residue T11 PMID:15173168 residue T11 PMID:15173168 residue T11 PMID:15173168 residue T11 PMID:15173168 residue T11 PMID:15173168 residue T11 PMID:15173168 residue T11 PMID:15173168 residue T11 PMID:15173168 residue T11 PMID:15173383 TEV protease present; Cdc6 truncated PMID:15173383 TEV protease present; Cdc6 truncated PMID:15175657 dns PMID:15177031 Fig6E PMID:15177031 colocalises with tip1 PMID:15177031 Fig 2 same phenotype as tea2delta and tip1delta single mutants PMID:15177031 Fig 4A,B PMID:15177031 Fig 4C Tip1YFP is expressed from endogenous tip1 gene tagged with YFP PMID:15177031 Fig 4C PMID:15177031 Fig 4E-H PMID:15177031 Fig 4I PMID:15177031 Fig 5C PMID:15177031 Fig 5A,B Endogenous tea2 tagged with GFP PMID:15177031 Fig 5A,B Endogenous tea2 tagged with GFP PMID:15177031 Fig 5A,B Endogenous tea2 tagged with GFP PMID:15177031 Fig 5E,F tea2-GFP is mildly overexpressed from the repressed integrated nmt1 promoter PMID:15177031 Fig 5E,F tea2-GFP is mildly overexpressed from the repressed integrated nmt1 promoter PMID:15177031 (plus end directed) PMID:15177031 Fig 6A,B GFPmal3 is mildly overexpressed from the repressed nmt1 promoter PMID:15177031 Fig 6C,D GFPmal3 is mildly overexpressed from the repressed nmt1 promoter PMID:15177031 Fig6 E PMID:15177031 Fig 2 same phenotype as tea2delta and tip1delta single mutants PMID:15177031 Fig 1 live imaging of Tip1YFP and CFP tubulin PMID:15177031 Fig 2 same phenotype as tea2delta and tip1delta single mutants PMID:15177031 Fig 2 same phenotype as tea2delta and tip1delta single mutants PMID:15177031 co-localises with tip1 PMID:15177031 data not shown PMID:15177031 data not shown PMID:15177031 Fig 4A,B PMID:15177031 Fig 4E-H Tip1YFP is expressed from endogenous tip1 gene tagged with YFP PMID:15184401 (G2) Fig. 6 B PMID:15184401 fig 4F PMID:15184401 fig 4F PMID:15184401 fig 4F PMID:15184401 Fig. 4 D PMID:15184401 Fig. 1 C PMID:15184401 Fig. 1 C PMID:15184401 Fig. 1 C PMID:15184401 Fig. 4 D PMID:15184401 Fig. 1 C PMID:15184401 Fig 1E PMID:15184401 Fig. 1 C/ Fig3 PMID:15184401 Fig 1E PMID:15184401 Fig. 1 C PMID:15184401 fig 6F PMID:15184401 Fig. 6 C . (G2) PMID:15184401 fig 6F PMID:15184401 fig 6F PMID:15184401 Fig. 6 B (G2) PMID:15184401 fig 4F PMID:15184402 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 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 figure2 PMID:15189983 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 git2 strains themselves were severely defective for growth on YEA medium containing 1 M KCl (Fig. 1). PMID:15189983 figure1 PMID:15189983 figure1 PMID:15189983 figure1 PMID:15189983 figure1 PMID:15189983 fig 7 PMID:15189983 fig 7 PMID:15189983 fig 7 PMID:15189983 fig 7 PMID:15189983 Fig. 7 (lanes 1 and 2), we observed that both cgs1 and pka1 are transcriptionally induced by glucose starvation. PMID:15189983 Fig. 7 (lanes 1 and 2), we observed that both cgs1 and pka1 are transcriptionally induced by glucose starvation. PMID:15189983 table 3 PMID:15189983 table 3 PMID:15189983 fig 6 PMID:15189983 fig 6 PMID:15189983 fig 6 PMID:15189983 fig 6 PMID:15189983 fig 6 PMID:15189983 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 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 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 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 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 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 figure2 PMID:15189983 figure2 PMID:15194812 Cdc45 reappears quickly after shift from restrictive to permissive temperature PMID:15194814 homozygous diploid PMID:15194814 homozygous diploid PMID:15219990 spectra looks the same as Adx PMID:15226378 homozygous diploid PMID:15226378 homozygous diploid PMID:15226405 frequency of different stages of LE development is different though, but morphology is normal PMID:15226405 frequency of different stages of LE development is different though, but morphology is normal PMID:15249580 (vw fixed from GO:0052812 to GO:0016308 based on e-mail from Pgaudet) The data are consistent with a model in which its3p, like its mammalian homologue, can convert PI(3)P to PI(3,4)P2 and PI(3,4,5)P3. PMID:15249580 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 fig 1c PMID:15249580 fig 1c PMID:15249580 mishapen PMID:15265986 in response to cytokinesis after mitosis checkpoint PMID:15265986 in response to cytokinesis after mitosis checkpoint PMID:15278909 during premeiotic DNA replication PMID:15297457 would it be better/safer to annotate to parent (generic intra-S checkpoint term)? PMID:15314153 25 degrees PMID:15314153 30 degrees PMID:15316017 activated_by(CHEBI:18420)| inhibited_by(CHEBI:29108) PMID:15329725 Fig. 1h PMID:15329725 Fig. 1d and Fig. 1h PMID:15329725 Fig. 1f) PMID:1533272 cdc13 expressed from own promoter on multi copy plasmid pUR18 PMID:1533272 Fig 5. Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid. Phosphorylation on threonine, but position(s) not determined. PMID:1533272 Fig 4 Histone H1 used as substrate. Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid. PMID:1533272 Fig 2. Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid. PMID:1533272 Fig 3. Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid. PMID:1533272 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:15367656 no hydroxyurea PMID:15369671 fig4 PMID:15369671 fig4 PMID:15369671 fig4 PMID:15371542 fig1 PMID:15371542 fig1 PMID:15371542 fig 1a PMID:15371542 fig 1a PMID:15385632 Figure 2A,Figure 2, D and E PMID:15385632 Figure 2A, Figure 2, D and E PMID:15385632 Figure 2A PMID:15385632 Figure 2A PMID:15385632 Figure 2A Figure 2, B and C) PMID:15385632 Figure 2A PMID:15385632 Figure 1H and Table 1 PMID:15385632 Figure 1I PMID:15385632 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 Figure 2, D and E PMID:15385632 Figure 5 C PMID:15385632 Figure 5 PMID:15385632 Figure 5 PMID:15385632 Figure 5 PMID:15385632 Figure 5 PMID:15385632 Figure 5 PMID:15385632 Figure 6, A, D, and E PMID:15385632 Figure 6, A, D, and E PMID:15385632 Figure 6, A, D, and E PMID:15385632 Figure 6, A, D, and E PMID:15385632 Figure 6, A, D, and E PMID:15385632 Figure 6, A, D, and E PMID:15385632 Figure 6, A, D, and E PMID:15385632 Figure 6, A, D, and E PMID:15385632 fig5 PMID:15385632 fig5 PMID:15385632 fig 6 PMID:15385632 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 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 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 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:1538784 throughout_cell_cycle PMID:15466421 homozygous diploid PMID:15466421 homozygous diploid PMID:15470240 fig2 PMID:15470240 fig2 PMID:15470240 fig2 PMID:15471884 lower affinity than for Y-form DNA PMID:15471884 low affinity PMID:15485922 same as taz1delta alone PMID:15485922 same as taz1delta alone PMID:15507118 inviable mononucleate aseptate vegetative cell with cell cycle arrest in mitotic G2 phase PMID:15509783 Fig. 7B PMID:15509783 Fig. 7D PMID:15509783 table2 PMID:15509783 checkpoint PMID:15509783 table2 PMID:15509783 table2 PMID:15509783 table2 PMID:15509783 Fig. 7D PMID:15509783 table2 PMID:15509783 figure 1B PMID:15509783 figure 1B PMID:15509783 Figure 2A PMID:15509783 Fig. 7B PMID:15509865 DURATION Fig. 2B,C PMID:15509865 (Table 3) assayed using pairing of his2 loci PMID:15509865 Fig. 3B PMID:15509865 (Table 2).leu1 and his2 loc, reduced 12 fold PMID:15509865 data not shown PMID:15509865 Fig. 3B PMID:15509865 Fig. 3C). PMID:15509865 data not shown , phenocopies ssm4 &dhc1 PMID:15509865 data not shown , phenocopies ssm4 &dhc1 PMID:15509865 (Fig. 6B,C). in meiotic cells, shmooing cells PMID:15509865 (Fig. 6B,C). in meiotic cells, shmooing cells PMID:15509865 (Fig. 6B,C). in meiotic cells, shmooing cells PMID:15509865 (Fig. 6B,C). in meiotic cells, shmooing cells PMID:15509865 (Fig. 6A-C), during meiotic prophase, shmooing PMID:15509865 Fig. 2B,C PMID:15509865 (Fig. 2A) PMID:15509865 (Fig. 2A) PMID:15509865 Table 3 PMID:15509865 Add? PMID:15509865 Table 3 PMID:15509865 Table 3 PMID:15509865 meiosis PMID:15525536 only required when there are problems , possibly involved in repair of monoorientation PMID:15537393 figure 2e PMID:15537393 figure 2e PMID:15537393 figure 2e PMID:15537393 figure 2e PMID:15537393 figure 2d PMID:15537393 figure 2d PMID:15537393 Figure 3d PMID:15537393 Figure 3d PMID:15537393 Figure 3b PMID:15537393 Figure 3c PMID:15537393 Figure 3b PMID:15537393 figure 2g PMID:15537393 figure 2f PMID:15537393 figure 2f PMID:15537393 figure 2f PMID:15537393 figure 2e PMID:15537393 Figure 3c PMID:15546915 (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 (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 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 Figure 5 These results indicate that Rgf3p acts as a specific Rho1p activator in S. pombe. PMID:15546915 Figure 4 GI Rho1 OEX rescues echinocandin sensitivity PMID:15546915 Figure 3 C shrunken cell PMID:15546915 (Fig. 1A PMID:15546915 Figure 3 C shrunken cell PMID:15546915 (Fig. 1A PMID:15546915 Figure 3B indicates a bypass of cytokinesis checkpoint PMID:15546915 Fig. 3A PMID:15546915 replace with cytokinetic phase PMID:15546915 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 figure4 PMID:15548596 three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site PMID:15601865 Fig. 3 PMID:15601865 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 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 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:15615784 assayed in vitro PMID:15615784 based just on this paper, candidate for involved_in_or_regulates qualifier PMID:15615784 based just on this paper, candidate for involved_in_or_regulates qualifier PMID:15615784 assayed in vitro PMID:15615848 (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 (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 (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 (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 (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 (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 (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 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 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 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 . 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 hypersensitive to TBZ, indicating that chromosome segregation is not robust in these mutant cells (Fig. 3A). PMID:15615848 (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 (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 (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 (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 Fig. 1B PMID:15615848 Fig. 1B PMID:15615848 Fig. 1B PMID:15615848 Fig. 1B PMID:15615848 Fig. 1B PMID:15615848 Fig. 1B PMID:15615848 Fig. 1A CenH PMID:15615848 Fig. 1A CenH PMID:15615848 Fig. 1A PMID:15625190 three-hybrid assay; also binds exogenous ESEs PMID:15632064 fig 1 The data sug- gest that the mutants are not deficient in termination effi- ciency. PMID:15632064 fig 1 The data sug- gest that the mutants are not deficient in termination effi- ciency. PMID:15632064 Mutated Rpc11p subunits associate with Pol III and impair its RNA 3 cleavage activity. PMID:15632064 fig 1 The data sug- gest that the mutants are not deficient in termination effi- ciency. PMID:15632064 trna chaperone PMID:15643072 assayed in strain with cdc10-129 to synchronize PMID:15647375 fig 4 PMID:15647375 GO:0051329 = mitotic interpase PMID:15647375 GO:0000093 = mitotic telophase PMID:15647375 fig4 PMID:15647375 fig 4 PMID:15654094 assayed using 160-bp palindromic sequence inserted into ade6 locus PMID:15654094 assayed using 160-bp palindromic sequence inserted into ade6 locus PMID:15654094 assayed using 160-bp palindromic sequence inserted into ade6 locus PMID:15654094 assayed using 160-bp palindromic sequence inserted into ade6 locus PMID:15665379 fig 2 PMID:15665379 fig 2 PMID:15665379 fig 2 PMID:15665379 fig 3b PMID:15671491 assayed using reporter based on S. cerevisiae MFA2 PMID:15671491 assayed using reporter based on S. cerevisiae MFA2 PMID:15671491 assayed using reporter based on S. cerevisiae MFA2 PMID:15671491 assayed using reporter based on S. cerevisiae MFA2 PMID:15671491 assayed using reporter based on S. cerevisiae MFA2 PMID:15689489 Fig. 1 PMID:15689489 Fig. 2 PMID:15689489 Fig. 2 PMID:15689489 Fig. 5 PMID:15689489 Fig. 6 PMID:15689489 Fig. 6 PMID:15689489 Fig. 6 PMID:15689489 Fig. 6 PMID:15689489 In metaphase the difference kinds of microtubules cannot be distinguished, but they can be distinguished during anaphase B PMID:15689489 Fig. 1 PMID:15689489 Fig. 1 PMID:15689489 Fig. 1 PMID:15710398 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 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 In Msp1p overexpressing cells, more than 85% of the cells had an aggregated filamentous mitochondrial network. PMID:15710398 MEMBRANE PMID:15710398 In the Dmsp1Ddnm1 strain, mtDNA depletion (Fig. 5F) and lethality (not shown) did not occur PMID:15710398 In the Dmsp1Ddnm1 strain, mtDNA depletion (Fig. 5F) and lethality (not shown) did not occur PMID:15710398 In the Dmsp1Ddnm1 strain, mtDNA depletion (Fig. 5F) and lethality (not shown) did not occur. PMID:15710398 In the Dmsp1Ddnm1 strain, mtDNA depletion (Fig. 5F) and lethality (not shown) did not occur. PMID:15710398 In the doubledisrupted Dmsp1Ddnm1 strain, the mitochondria formed elongated tubules which resembled those seen in wild-type cells, ...... (Fig. 5E). PMID:15710398 In the doubledisrupted Dmsp1Ddnm1 strain, the mitochondria formed elongated tubules which resembled those seen in wild-type cells, ...... (Fig. 5E). PMID:15710398 the mitochondrial network appeared as highly interconnected tubules forming net-like structures (Fig. 5A). PMID:15710398 Fig. 4B), PMID:15710398 Fig. 4B), PMID:15710398 (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 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 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 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 while cells that expressed cytosolic Msp1pDMIS or CAT died. PMID:15710398 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 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 while cells that expressed cytosolic Msp1pDMIS or CAT died. PMID:15710398 while cells that expressed cytosolic Msp1pDMIS or CAT died. PMID:15710398 while cells that expressed cytosolic Msp1pDMIS or CAT died. PMID:15710398 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:15716270 25S rRNA position 1723 PMID:15716270 25S rRNA position 1084 PMID:15716270 18S rRNA position 1307 PMID:15716270 25S rRNA positions 2216, 2220, 2351 PMID:15716270 25S rRNA position 3017 PMID:15716270 25S rRNA position 1074 PMID:15716270 18S rRNA position 1204 PMID:15716270 25S rRNA position 3069 PMID:15716270 25S rRNA positions 2298, 2401 PMID:15716270 18S rRNA positions 208, 2341 PMID:15728720 increased centromere spindle pole body detachment during meiotic prophase fission-yeast-phenotype/2055/ PMID:15731009 based just on this paper, candidate for involved_in_or_regulates qualifier PMID:15731009 same as orb3-167 alone PMID:15731009 same as orb3-167 alone PMID:15731009 dependent on F-actin (asayed using Latrunculin A); independent of microtubules (assayed using MBC) PMID:15731009 dependent on F-actin (asayed using Latrunculin A); independent of microtubules (assayed using MBC) PMID:15731009 assayed using casein; doesn't quite rule out tyrosine phosphorylation PMID:15731009 based just on this paper, candidate for involved_in_or_regulates qualifier PMID:15743909 homozygous cross PMID:15743909 homozygous cross PMID:15743909 homozygous cross PMID:15743909 dependent on F-actin (assayed using Latrunculin A) PMID:15743909 dependent on F-actin (assayed using Latrunculin A) PMID:15772152 normal length PMID:15797383 fig2 ln 11-12 PMID:15797383 fig2,3,4 PMID:15797383 fig2,5 PMID:15797383 fig2 PMID:15797383 fig1 PMID:15797383 fig1 PMID:15797925 assayed using NLS-LacI-GFP construct PMID:15797925 punctate, similar to nuclear pore components; localization not dependent on microtubules PMID:15800064 figure 3A PMID:15800064 figure 3A PMID:15800064 fig 2 a,c 2D PMID:15800064 fig 2 a 2D PMID:15800064 fig 2 a 2D PMID:15800064 fig 2 a,c 2D PMID:15800064 fig 1 C PMID:15800064 fig 6 c PMID:15800064 fig 6 B PMID:15800064 figure 3A c PMID:15800064 fig 5 a PMID:15800064 fig 5 a PMID:15800064 Figure 4 PMID:15800064 Figure 3 B fypo/issues/2830 PMID:15800064 Figure 3 fypo/issues/2830 PMID:15800064 Figure 3 fypo/issues/2830 PMID:15800064 Figure 3A PMID:15800064 figure 3A c PMID:15800064 fig 5 b PMID:15800064 figure 3A PMID:15809031 inferred from direct physical interactions between tea4,tea1 and tea4,for3, plus tea4delta phenotype PMID:15827087 Fig 4C PMID:15827087 Fig4B PMID:15827087 Fig2A and data not shown PMID:15827087 Fig1. They describe cells as swollen in their middle region PMID:15827087 data not shown PMID:15827087 Fig 4B PMID:15827087 Fig1 Table 2 PMID:15827087 Table 2 This distribution is only seen in cells with a rod shaped appearance PMID:15827087 Table 2 This distribution is only seen in cells with a rod shaped appearance PMID:15827087 Table 2 This distribution is only seen in cells with a rod shaped appearance PMID:15827087 Table 2 PMID:15827087 Fig1B This distribution is only seen in cells with a rod shaped appearance PMID:15827087 data not shown PMID:15827087 Fig2A,B PMID:15827087 Fig2A,B PMID:15827087 Fig2D PMID:15827087 Fig1 PMID:15827087 Fig1. They describe cells as swollen in their middle region PMID:15827087 Fig1 permissive temperature is 25°C PMID:15827087 data not shown, permissive temperature 25°C PMID:15827087 data not shown Non permissive temperature is 32°C and above PMID:15827087 data not shown PMID:15827087 Fig2A and data not shown PMID:15827087 Fig3A,B Deletion of the talin domain suppresses the premature activation of bipolar growth in a cdc10 mutant in latA PMID:15827087 Fig4D PMID:15827087 data for cdc25-22 block not shown but see also Fig4A PMID:15827087 Fig1C Table 2 PMID:15827087 data not shown, same as Fig 4C PMID:15837798 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 mto2 deletion strain, which yielded viable but slightly bent cells (Fig. 3 A) PMID:15837798 mto2 deletion strain, which yielded viable but slightly bent cells (Fig. 3 A) PMID:15857958 Fig. 2 PMID:15857958 Fig. 7 PMID:15857958 Fig. 7 PMID:15857958 Fig. 7 PMID:15857958 Fig. 7 PMID:15857958 Fig. 7 PMID:15857958 Fig. 7 PMID:15857958 Fig. 6 PMID:15857958 Fig. 6 PMID:15857958 Fig. 7 PMID:15857958 Fig. 5 PMID:15857958 Fig. 5 PMID:15857958 Fig. 5 PMID:15857958 Fig. 5 PMID:15857958 Fig. 5 PMID:15857958 Fig. 5 PMID:15857958 Fig. 5 PMID:15857958 Fig. 5 Synthetic phenotype PMID:15857958 Fig. 5 Synthetic phenotype PMID:15857958 Fig. 5 Synthetic phenotype PMID:15857958 Fig. 5 PMID:15857958 Fig. 5 PMID:15857958 Fig. 5 PMID:15857958 Fig. 5 PMID:15857958 Fig. 5 PMID:15857958 Fig. 5 PMID:15857958 Fig. 4 PMID:15857958 Fig. 4 PMID:15857958 Fig. 3 PMID:15857958 Fig. 3 rescue of FYPO:0000324 PMID:15857958 Fig. 3 - mad2 signal. background: cdc25-22 PMID:15857958 Fig. 3 - background: cdc25-22 PMID:15857958 Fig. 2 PMID:15857958 Fig. 2 and Fig. 3 (cdc13 signal) PMID:15857958 Fig. 2 PMID:1588914 multicopy pwis2 does not suppress wee1-50 ts phenotype PMID:1588914 Table 2 pwis4 does not suppress wee1-50 cdc25-22 mcs6-13 PMID:1588914 see Table 2 PMID:1588914 see Table 2 PMID:1588914 Table 2 pwis1 does not suppress wee1-50 cdc25-22 mcs6-13 PMID:1588914 Table 2 pwis1 does not suppress wee1-50 cdc25-22 mcs6-13 PMID:1588914 see Table 2 multi copy pwis4 does not suppress cdc25-22 wee1-50 mcs4-13 PMID:1588914 See Table 2 multi copy pwis4 does not suppress cdc25-22 wee1-50 mcs4-13 PMID:1588914 see Table 2 PMID:1588914 see Table 2 PMID:1588914 see Table 2 PMID:1588914 multicopy pwis4 does not suppress cdr2-69 phenotype PMID:1588914 multicopy pwis4 does not suppress cdr1-34 phenotype PMID:1588914 multicopy pwis4 does not suppress wee1-50 ts phenotype PMID:1588914 multicopy pwis4 does not suppress cdc2-3w phenotype PMID:1588914 multicopy pwis4 does not suppress cdc2-1w phenotype PMID:1588914 multicopy pwis4 does not suppress cdc13-117 ts phenotype PMID:1588914 multicopy pwis4 does not suppress cdc2-33 ts phenotype PMID:1588914 multicopy pwis2 does not suppress cdc2-3w phenotype PMID:1588914 multicopy pwis2 does not suppress cdc2-1w phenotype PMID:1588914 multicopy pwis2 does not suppress cdc13-117 ts phenotype PMID:1588914 multicopy pwis2 does not suppress cdc2-33 ts phenotype PMID:1588914 multicopy pwis1 does not suppress cdr2-69 phenotype PMID:1588914 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 the wis2 gene on a multi copy plasmid pwis2 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1 PMID:1588914 multicopy pwis3 does not suppress cdr2-69 phenotype PMID:1588914 the spo12 gene on a multi copy plasmid pwis3 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1 PMID:1588914 the wis4 gene on a multi copy plasmid pwis4 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1 PMID:1588914 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 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 multicopy pwis3 does not suppress cdr1-34 phenotype PMID:1588914 multicopy pwis3 does not suppress wee1-50 ts phenotype PMID:1588914 multicopy pwis3 does not suppress cdc2-3w phenotype PMID:1588914 multicopy pwis3 does not suppress cdc2-1w phenotype PMID:1588914 multicopy pwis3 does not suppress cdc13-117 ts phenotype PMID:1588914 multicopy pwis3 does not suppress cdc2-33 ts phenotype PMID:1588914 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 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 multicopy pwis1 does not suppress cdc2-33 ts phenotype PMID:1588914 multicopy pwis1 does not suppress cdc13-117 ts phenotype PMID:1588914 multicopy pwis1 does not suppress cdc2-1w phenotype PMID:1588914 multicopy pwis1 does not suppress cdc2-3w phenotype PMID:1588914 multicopy pwis1 does not suppress cdr1-34 phenotype PMID:1588914 multicopy pwis1 does not suppress wee1-50 ts phenotype PMID:1588914 multicopy pwis2 does not suppress cdr2-69 phenotype PMID:1588914 multicopy pwis2 does not suppress cdr1-34 phenotype PMID:1588914 see Table 2 PMID:1588914 see Table 2 PMID:1588914 see Table 2 PMID:1588914 see Table 2 PMID:1588914 data not shown PMID:1588914 Table 3 pwis4 surpresses the elongated cell phenotype of win1-1 PMID:1588914 Table 3 cells are 30-50% longer than wild type PMID:1588914 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 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 multicopy pwis4 does not suppress cdc13-117 ts phenotype PMID:1588914 multicopy pwis4 does not suppress cdc2-33 ts phenotype PMID:1588914 multicopy pwis3 does not suppress cdc13-117 ts phenotype PMID:1588914 multicopy pwis3 does not suppress cdc2-33 ts phenotype PMID:1588914 multicopy pwis2 does not suppress cdc13-117 ts phenotype PMID:1588914 multicopy pwis2 does not suppress cdc2-33 ts phenotype PMID:1588914 multicopy pwis1 does not suppress cdc13-117 ts phenotype PMID:1588914 multicopy pwis1 does not suppress cdc2-33 ts phenotype PMID:1588914 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 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 the wis4 gene on a multi copy plasmid pwis4 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1 PMID:1588914 the spo12 gene on a multi copy plasmid pwis3 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1 PMID:1588914 the wis2 gene on a multi copy plasmid pwis2 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1 PMID:1588914 the wis1 gene on a multi copy plasmid pwis1 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1 PMID:1588914 see Table 2 PMID:1588914 Table 2 pwis4 does not suppress wee1-50 cdc25-22 mcs6-13 PMID:15908586 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 Figure 3 There was a 4- fold reduction of Cnp1 at cnt2 in hrp1D cells, PMID:15908586 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 Figure 3 There was a 4- fold reduction of Cnp1 at cnt2 in hrp1D cells, PMID:15908586 Figure 3 PMID:15908586 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 Figure 3 PMID:15908586 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 Figure 2 PMID:15908586 Figure 2 PMID:15908586 Figure 2 PMID:15908586 Figure 2 PMID:15908586 Figure 2 PMID:15908586 Figure 2A However, growth of the double mutant cells was completely inhibited by TSA. PMID:15908586 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 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 Figure 2 PMID:15908586 Figure 2 In cultures without TSA, the hrp1D cells grew slightly faster than wt cells as reported previously (48). PMID:15908586 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 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 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 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 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 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 Figure 1 PMID:15908586 Figure 1 PMID:15908586 Figure 1 PMID:15908586 Figure 1 PMID:15915339 more sensitive than either single mutant PMID:15915339 more sensitive than either single mutant PMID:15915339 more sensitive than either single mutant PMID:15915339 more sensitive than either single mutant PMID:15920625 Proxy assay for hydrolase function used and IMP evidence for catalytic activity PMID:15925945 assayed using AlF4- to mimic GTP-bound Gpa2 PMID:15933715 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 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 However, in etd1-1 mutant cells, the medial ring marked with Cdc15p-GFP seems to fail constriction. To bette PMID:15933715 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 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 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 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 suggesting that Etd1p is somehow necessary to maintain Spg1p activity during anaphase until the completion of cytokinesis PMID:15933715 These results indicate that Etd1p is polyubiquitinated and degraded through the ubiquitin-dependent 26S-proteasome pathway. PMID:15933715 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 Figure 1A and B). PMID:15933715 Figure 1A and B). PMID:15933715 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 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 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 In interphase cells, Etd1p-GFP was located at the cell cortex and was more concentrated at the cell tips (Figure 2A, cell 1). PMID:15936270 Wsh3-GFP was abrogated by a mutation in β- tubulin, nda3-KM311 [39] even at its permissive temperature, 30oC (Figure 3B, left). PMID:15936270 Figure 2B). PMID:15936270 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 2c Δwsh3 cells were found to grow exclusively in a monopolar fashion. PMID:15936270 DNS PMID:15936270 (p;enetrance for m 6B) highly bent or branched morphology (Figure 2a) PMID:15936270 (p;enetrance for m 6B) highly bent or branched morphology (Figure 2a) PMID:15936270 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 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 highly bent or branched morphology (Figure 2a) PMID:15936270 DNS PMID:15936270 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 Cell polarity defects with bent and branched morphology were observed after shifting the Δspc1 mutant from 25oC to 36oC (Figure 6C). PMID:15936270 (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 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 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 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:15937127 fig 3C PMID:15937127 DNA at the tips, telophase delay PMID:15937127 Figure 3F-3 PMID:15937127 fig 5B PMID:15937127 fig 5B PMID:15937127 fig2 PMID:15937127 fig 4D PMID:15937127 fig 4D PMID:15937127 fig 4D PMID:15937127 fig 4D PMID:15937127 Figure 3F-3 PMID:15937127 Figure 3F-3 PMID:15937127 Figure 3F-3 PMID:15937127 fig2 PMID:15937127 fig2 PMID:15937127 fig2 PMID:15937127 fig2 PMID:15937127 fig3 PMID:15937127 fig3 PMID:15937127 fig3 B-2 (1.1% WT) PMID:15937127 fig3 B-2 (never seen in WT) PMID:15941470 Tev protease present; Cdc23 truncated; cells not synchronized PMID:15941470 Tev protease present; Cdc23 truncated; Cdc23 C-terminal fragment not retained in nucleus PMID:15941470 Tev protease present; Cdc23 truncated; Cdc23 C-terminal fragment not retained in nucleus PMID:15941470 Tev protease present; Cdc23 truncated PMID:15941470 Tev protease present; Cdc23 truncated; N starvation/recovery synchronizes cells PMID:15941470 Tev protease present; Cdc23 truncated PMID:15957215 from the catenated plasmid experiment (and failure to separate sisters) PMID:15992541 promoter repressed PMID:15992541 thiamine absent; expression level lower than with endogenous promoter but higher than when repressed PMID:16055437 figure 1a PMID:16079916 protein-coding genes and intergenic regions PMID:16079916 protein-coding genes and intergenic regions PMID:16079916 protein-coding genes and intergenic regions PMID:16079916 protein-coding genes and intergenic regions PMID:16079916 protein-coding genes and intergenic regions PMID:16079916 protein-coding genes and intergenic regions PMID:16079916 protein-coding genes and intergenic regions PMID:16079916 protein-coding genes and intergenic regions PMID:16079916 protein-coding genes and intergenic regions PMID:16079916 protein-coding genes and intergenic regions PMID:16079916 assayed in intergenic regions PMID:16079916 assayed in intergenic regions PMID:16079916 assayed in intergenic regions PMID:16079916 assayed in intergenic regions PMID:16079916 protein-coding genes and intergenic regions PMID:16079916 protein-coding genes and intergenic regions PMID:16085489 clp1 cytoplasmic localization not maintained during cytokinetic stress. cdc7 localization to SPB not maintained during cytokinetic stress PMID:16087707 also from timing of localization to patches PMID:16087707 also from timing of localization to patches PMID:16087707 also from synthetic lethality with myo1, timing of localization to patches, and vrp1 mutant phenotype PMID:16087707 dependent on F-actin (assayed using Latrunculin A) PMID:16087707 dependent on F-actin (assayed using Latrunculin A) PMID:16087707 specific Arp2/3 complex subunit(s) not identified; authors use Myo1 tail as representative of whole protein PMID:16087707 also from timing of localization to patches PMID:16087707 specific Arp2/3 complex subunit(s) not identified; authors use Myo1 tail as representative of whole protein PMID:16087707 dependent on F-actin (assayed using Latrunculin A) PMID:16096637 Pmo25 formed a complex with Nak1 and was required for both the localization and kinase activity of Nak1. PMID:16096637 both SPBs in early mitosis PMID:16111942 Fig 1A appeared at theSPB upon conjugation of haploid cells, persisted untilthe onset of meiosis I, and disappeared thereafter PMID:16111942 arious exp, and ectoptic mitotic exprression PMID:16111942 S1D PMID:16111942 arious exp, and ectoptic mitotic exprression PMID:16111942 Interestingly, however, azygotic asci arising from diploid hrs1D cells did not show an apparent defect in spore formation (Figure S1D PMID:16120966 can incorporate NTPs or dNTPs; changed from primase activity because not tested with unprimed template PMID:16120966 distributive; substrate preference: small gaps with a 5′-phosphate group PMID:16138082 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 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 Fig. 5A,B PMID:16141239 endocytosis restricted to cell end PMID:16141239 endocytosis restricted to cell end PMID:16141239 endocytosis restricted to cell end PMID:16141239 endocytosis restricted to cell end PMID:16141239 Fig. 5A,B PMID:16141239 Fig. 5A,B PMID:16169489 knocked out in diploid. Can't tell if it vegetative or spore? PMID:16169489 27% of spores produce viable colonies PMID:16169489 knocked out in diploid. Can't tell if it vegetative or spore? PMID:1617727 splicing of artificial construct with wt or mutated splice sites assayed in mutants PMID:16199877 Fig. 3C). PMID:16199877 Fig. S1C PMID:16199877 Fig. S1C PMID:16199877 S1B PMID:16199877 S1A PMID:16199877 Fig 5DE PMID:16199877 Fig. 3C). PMID:16199877 Figur 4B PMID:16199877 Figur 4B PMID:16199877 Figur 4B PMID:16199877 Figur 4B PMID:16199877 fig4 PMID:16199877 Fig 3C PMID:16199877 Fig 3C PMID:16199877 Fig. 3C). PMID:16199877 Fig. 3C). PMID:16199877 fig 3B PMID:16199877 fig 3B PMID:16199877 fig 3B PMID:16199877 fig 3A PMID:16199877 DNS PMID:16199877 DNS PMID:16199877 DNS PMID:16199877 Fig 1D PMID:16199877 Fig 1B PMID:16199877 DNS PMID:16199877 Fig 1E PMID:16199877 Fig 1D PMID:16199877 Fig 1A PMID:16251348 fig 2c PMID:16251348 fig3B PMID:16252005 (regulation ) can also infer (IC) from GO:0030674 PMID:16252005 same as pcu4delta alone PMID:16252005 same as cdt2delta alone PMID:16252005 same as csn1delta alone PMID:16252005 same as ddb1delta alone PMID:16252005 same as cdt2delta alone PMID:16252005 same as ddb1delta alone PMID:16252005 same as pcu4delta alone PMID:16262791 detectable in mutants that increase bound GTP:GDP ratio, implying that protein-protein interaction is GTP-dependent PMID:16291723 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 (Fig. 3C). PMID:16291723 Fig. 1A. PMID:16291723 Fig. 3C PMID:16291723 Fig. 1A. All cells lysed while undergoing division and the daughter cells remained attached to one another. PMID:16291723 (50 mM) PMID:16291723 Fig. 3C PMID:16291723 Fig. 3C PMID:16291723 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 (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 Fig. 3C. PMID:16291723 (Fig. 3C). PMID:16291723 Rgf3p appears necessary to stimulate Rho1p-mediated activation of a glucan synthase crucial after septation for proper new cell-end formation. PMID:16291723 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 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 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 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 `SYNTHETIC LETHAL PMID:16291723 fig 6 PMID:16291723 rgf3+ is essential PMID:16291723 rgf3+ is essential PMID:16291723 Figue 5C PMID:16291723 Figue 5C PMID:16291723 Rgf1p-GFP was also detected at cell ends (Fig. 4B). PMID:16291723 .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 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 Fig. 1A. All cells lysed while undergoing division and the daughter cells remained attached to one another. PMID:16291723 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:16317005 activated_by CHEBI:15422 | inhibited_by CHEBI:16284 PMID:16317005 activated_by CHEBI:15422 | inhibited_by CHEBI:16284 PMID:16325576 figure1 PMID:16325576 figure1 PMID:16325576 S1 PMID:16325576 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 S1 PMID:16325576 S1 PMID:16325576 (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 Figure 2C PMID:16325576 S1 PMID:16325576 figure2b PMID:16325576 figure2a PMID:16325576 figure2a PMID:16325576 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 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 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 induced PMID:16325576 figure1 PMID:16325576 figure1 PMID:16325576 fig 5A PMID:16325576 S2 PMID:16325576 S1 PMID:16325576 Figure 2C PMID:16325576 S1 PMID:16325576 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 Figure 2C PMID:16325576 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 figure1 PMID:16325576 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 Figure 2C/3b PMID:16394105 fig 3 PMID:16394105 both the growth and shrinkage rates were decreased down to 33 and 60%, respectively, PMID:16394105 Figure 9 PMID:16394105 both the growth and shrinkage rates were decreased down to 33 and 60%, respectively, PMID:16394105 fig 4 PMID:16394105 fig 4 PMID:16394105 fig 4 PMID:16394105 fig 4 PMID:16394105 fig 4 PMID:16394105 morphology PMID:16394105 Figure 1 B PMID:16394105 Figure 1 B PMID:16394105 supp data PMID:16394105 Figure 1 B PMID:16394105 Figure 1 B PMID:16394105 Figure 1 B PMID:16394105 fig 3 PMID:16394105 fig 4 PMID:16394105 fig 5 d PMID:16394105 fig 5 e PMID:16394105 table 4 PMID:16394105 table 4 PMID:16394105 table 4 PMID:16394105 table 4 PMID:16394105 table 4 PMID:16394105 Figur 6 B,C PMID:16394105 Figur 6 B,C PMID:16394105 fig 7 b PMID:16394105 fig 7 a PMID:16394105 fig 7 a PMID:16394105 Figure 8 AB PMID:16394105 Figure 8 C PMID:16394105 Figure 8 D PMID:16394105 Figure 8 D PMID:16394105 Figure 8 D PMID:16407242 higher protein level than in absence of HU, in both wild type and mutant PMID:16407242 higher protein level than in absence of HU, in both wild type and mutant PMID:16421249 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 (Figure 2A The resulting strain, rgf1, showed a slow growth pattern at 28°C PMID:16421249 (Figure 3B) 55% of cdc10-129 cells displayed bipolar growth, whereas only 4% of cdc10-129 rgf1 cells were bipolar PMID:16421249 positive regulation PMID:16421249 Figure 2B regardless of the growth temperature 30 –35% of the cells were lysed, PMID:16421249 positive regulation PMID:16421249 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 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 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 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 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 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 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 (Figure 2A The resulting strain, rgf1, showed a slow growth pattern at 28°C PMID:16421249 rga1 cells were severely impaired for growth, whereas rgf1rga1 exhibited a better growth pat- tern and resembled rgf1 cells. PMID:16421249 rescue of multiseptate, swollen PMID:16421249 increased gtp-bound gtpase (active) PMID:16421249 decreased gtp-bound gtpase (active) PMID:16421249 Figure 2B regardless of the growth temperature 30 –35% of the cells were lysed, PMID:16421249 (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 Figure 7A, only a moderate expres- sion of bgs4 restored growth of an rgf1 mutant in the presence of the antifungal agent PMID:16421249 Figure 7A, PMID:16421249 Figure 7A, PMID:16421249 Figure 7A, PMID:16421249 DNS PMID:16421249 positive regulation PMID:16421249 Figure 7C, PMID:16421249 Figure 8A PMID:16421249 Figure 8A PMID:16421249 Figure 2A PMID:16421249 Figure 2B regardless of the growth temperature 30 –35% of the cells were lysed, PMID:16421249 Figure 2B regardless of the growth temperature 30 –35% of the cells were lysed, PMID:16421249 Figure 2B regardless of the growth temperature 30 –35% of the cells were lysed, PMID:16421249 positive regulation PMID:16421249 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 Figure 8A PMID:16421249 Figure 8A PMID:16421249 Figure 3A at cell division site PMID:16453724 ABOLISHED SEPARATION PMID:16453724 ABOLISHED SEPARATION PMID:16453724 with re-replication PMID:16453733 when selfed produces 76% 2 spore asci at 25 compared to 5% in suc1+ background PMID:16453733 suppresses cdc2-33 temperature sensitive phenotype at 32 PMID:16453733 suppresses cdc2-L7 temperature sensitive phenotype at 32 and weakly at 35 PMID:16453733 suppresses cdc2-56 temperature sensitive phenotype at 35 PMID:16453733 23% 2 spore asci when selfed PMID:16453733 suppresses cdc2-56 temperature sensitive phenotype at 35 PMID:16453733 suppresses cdc2-M55 temperature sensitive phenotype at 32 PMID:16453733 suppresses temperature sensitive phenotype of cdc2-33 at 32 PMID:16453733 suppresses cdc2-M26 temperature sensitive phenotype at 32 PMID:16453733 suppresses cdc2-M55 temperature sensitive phenotype at 32 PMID:16453733 suppresses cdc2-L7 temperature sensitive phenotype at 32 PMID:16453733 increased expression gives increased % 2 spored asci PMID:16453733 suppresses cdc2-M26 temperature sensitive phenotype at 32 PMID:1645660 inhibited_by zinc(2+) activated_by magnesium(2+) PMID:16467379 localization dependent on F-actin (assayed using Latrunculin A) PMID:16481403 Fig1 D (actually 2 bundles) PMID:16481403 from both ends PMID:16481403 from both ends PMID:16481403 fig 1c PMID:16481403 fig1 PMID:16481403 igure 5B PMID:16481403 emtoc PMID:16483313 isn't really processing, cleavage PMID:16489217 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 genes specified in extensions assayed in low-throughput Northern blots; additional genes assayed in high-throughput microarrays not listed PMID:16537923 aerobic conditions PMID:16537923 genes specified in extensions assayed in low-throughput Northern blots; additional genes assayed in high-throughput microarrays not listed PMID:16537923 genes specified in extensions assayed in low-throughput Northern blots; additional genes assayed in high-throughput microarrays not listed PMID:16541024 Notably, we detected only a single combination of PP2A subunits associated with SpSgo1, namely SpPaa1A–SpPar1B′–SpPpa2C PMID:16541024 this is an inference, but almost certainly true based on the genetics PMID:16541024 Fig. 4 PMID:16541024 Supplementary Fig. S2a PMID:16541024 Fig. 2b PMID:16541024 Fig. 4b PMID:16541024 Fig. 4b PMID:16541024 Fig. 4b PMID:16541024 Fig. 4b PMID:16541024 Fig. 4 PMID:16541024 Fig. 4 PMID:16541024 fig.1 PMID:16541024 Fig. 2b PMID:16541024 Fig. 2b PMID:16541024 Fig. 2b PMID:16541024 fig.1 PMID:16541024 Fig. 2b PMID:16541024 Supplementary Fig. S2a PMID:16541024 Supplementary Fig. S2a PMID:16541024 Supplementary Fig. S2a PMID:16541024 Fig. 2b PMID:16541024 Fig. 2b PMID:16541024 Fig. 2b PMID:16541024 Fig. 2a PMID:16541024 Fig. 2a PMID:16541024 Fig. 2a PMID:16541024 Fig. 2a PMID:16541024 fig.1 PMID:16541024 Supplementary Fig. S2a PMID:16541025 Fig. 5a PMID:16541025 (Fig. 5b). PMID:16541025 dns PMID:16541025 (Supplementary Fig. 7) PMID:16541025 (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 We found that, like sgo1D cells, par1D cells mostly lost centromeric Rec8 localization at this stage (Fig. 5d) PMID:16541025 Fig. 5a PMID:16541025 Fig. 5b however, it colocalizes with Sgo1 at centromeres during meiosis I PMID:16541025 (Supplementary Fig. 7). PMID:16541025 (Supplementary Fig. 7) PMID:1655416 is delayed but the delay is reduced compared to the single mutant PMID:1655416 figure 10 C PMID:1655416 LENgth PMID:1655416 transient PMID:1655416 figure 10 C PMID:1655416 ADD MODIFIED FORMS PMID:1657594 fig 6 PMID:1657594 fig 6 PMID:16585273 Fig. 4 E PMID:16611237 indicates a G2 delay PMID:16618806 assayed substrate myelin basic protein PMID:16618806 assayed substrate myelin basic protein PMID:16618806 assayed substrate myelin basic protein PMID:16618806 assayed substrate myelin basic protein PMID:16618806 assayed substrate myelin basic protein PMID:16618806 abolished dimerization in kinase-dead cds1-D312E PMID:16618806 induced dimerization increases Cds1 autophosphorylation without prior phosphorylation on T11 PMID:16618806 effect of mutation in substrate Cds1 molecule PMID:16618806 effect of mutation in substrate Cds1 molecule PMID:16618806 assayed substrate myelin basic protein PMID:16618806 assayed substrate myelin basic protein PMID:16618806 assayed substrate myelin basic protein PMID:16618806 assayed substrate myelin basic protein PMID:16618806 assayed substrate myelin basic protein PMID:16618806 effect of mutation in substrate Cds1 molecule PMID:16618806 assayed substrate myelin basic protein PMID:16618806 residue T11 PMID:16618806 residue T11 PMID:16618806 residue T11 PMID:16618806 residue T11 PMID:16618806 has output PR:000037300 PMID:16618806 residue T11 PMID:16618806 residue T11 PMID:16618806 cells otherwise haploid PMID:16618806 cells otherwise haploid PMID:16618806 cells otherwise haploid PMID:16624923 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 membrane anchor PMID:16682348 (G1 arrested cells) PMID:16682348 G1 arrested cells PMID:16687577 fig 1 PMID:16687577 fig 1 PMID:16687577 fig 1 PMID:16687577 fig 2 PMID:16687577 different pathway PMID:16687577 different pathway PMID:16687577 fig4 PMID:16687577 fig 3 PMID:16687577 fig7 PMID:16687577 Figure 6 asymetric during cytokinesis delay PMID:16687577 Figure 5, D and E for maintenance of the actomyosin ring in response to cytokinesis delay upon PMID:16687577 Figure 5, D and E for maintenance of the actomyosin ring in response to cytokinesis delay upon PMID:16687577 fig 3 PMID:16687577 fig 5 (during ectopic SIN activation) PMID:16687577 fig 5 PMID:16687577 fig4 PMID:16687577 fig4 PMID:16687577 fig 5 PMID:16687577 fig 2 PMID:16738311 32 °C; better than without cid12delta PMID:16738311 32 °C PMID:16738311 nda3-KM311 allele also in genotype, but used as assay tool here PMID:16738311 centromere outer repeat transcripts PMID:16738311 homozygous diploid PMID:16738311 homozygous diploid PMID:16738311 homozygous diploid PMID:16738311 homozygous diploid PMID:16738311 homozygous diploid PMID:16738311 32 °C PMID:16738311 homozygous diploid PMID:16738311 32 °C PMID:16738311 32 °C; very slightly worse than without cid12delta PMID:16738311 32 °C PMID:16738311 32 °C PMID:16738311 32 °C; same as without cid12delta PMID:16738311 32 °C PMID:16738311 32 °C PMID:16738311 26 °C PMID:16738311 26 °C PMID:16775007 Figure 7A PMID:16775007 fig 5D PMID:16775007 Figure 5, A and B PMID:16775007 Figure 4C PMID:16775007 Fig2A PMID:16775007 Fig 2A PMID:16775007 Fig 1A PMID:16816948 pulse/chase PMID:16822282 fig3A PMID:16822282 fig3A PMID:16822282 fig3A PMID:16822282 caspase PMID:16822282 caspase PMID:16822282 caspase PMID:16822282 fig3A PMID:16822282 fig3A PMID:16822282 fig3A PMID:16822282 fig3A PMID:16823445 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05) PMID:16823445 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05) PMID:16823445 assayed in diploid PMID:16823445 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05) PMID:16823445 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05) PMID:16823445 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05) PMID:16823445 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05) PMID:16823445 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05) PMID:16823445 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05) PMID:16823445 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05) PMID:16823445 Abstract 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. PMID:16823445 assayed in diploid PMID:16823445 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05) PMID:16823445 assayed in diploid PMID:16823445 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPCP20C8.03) (mah 2014-08-05) PMID:16824200 requires intact mitotic spindle, as shown by cold-depolymerizing microtubules and nda3 mad2 double mutant phenotype PMID:16857197 might be abolished. Sometimes you see diploidization. PMID:16884933 PHEROMONE TERM PMID:16914721 microarray data shows 111 genes affected PMID:16914721 assayed using ade6-M26 PMID:16914721 microarray data shows 111 genes affected PMID:16914721 microarray data shows 111 genes affected PMID:16914721 microarray data shows 111 genes affected PMID:16920624 Figure 2B. PMID:16920624 Figure 2B. PMID:16920624 Figure 2B. The sensitivities of Dis1N3A and Dis1C3A were similar to that of the wild-type. PMID:16920624 Figure 2B. The sensitivities of Dis1N3A and Dis1C3A were similar to that of the wild-type. PMID:16920624 Figure 2C. The loss rate of CN2 minichromosome in Dis16A was much higher than that of the wild-type integrant... PMID:16920624 Figure 2C. .... whereas Dis1N3A and Dis1C3A had loss rates that were comparable to those of the wild- type Dis1 integrant. PMID:16920624 Figure 2C. .... whereas Dis1N3A and Dis1C3A had loss rates that were comparable to those of the wild- type Dis1 integrant. PMID:16920624 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 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 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:16920624 fig6 PMID:16920624 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 Figure 2A. PMID:16920624 figure 1B. PMID:16920624 Figure 1C PMID:16920624 Figure 2A. PMID:16920624 figure 1B. PMID:16920624 Figure 2B. PMID:16920624 UNPHOSPHORYLATED. In anaphase, Dis1WT-GFP signals abruptly increased along the spindle and at the SPBs despite being absent from the central zone. PMID:16920624 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 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 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 protein localized to spindle (also a child of mislocalized protein) PMID:16920624 PHOSPHORYLATED. Fig3A The Dis1WT-GFP signals are seen as the kinetochore dots in metaphase. AND 4b PMID:16920624 Figure 2D. However, the double mutant mis12 Dis16E could form colonies at 33C. PMID:16920624 Figure 2D. whereas mis12 Dis1N3A and mis12 Dis1C3A showed weak inhibition of colony formation PMID:16920624 Figure 2D. The double mutant mis12 Dis16A failed to produce colonies at 33 PMID:16920624 Figure 2D. whereas mis12 Dis1N3A and mis12 Dis1C3A showed weak inhibition of colony formation PMID:16921379 in complex with Swi5 PMID:16921379 sfr1 protein is not stable without swi5. swi5 alone does not bind rad51. PMID:16921379 sfr1 protein is not stable without swi5. swi5 alone does not bind rad51. PMID:16921379 in complex with Sfr1 PMID:16963626 using the cross-linking agent EGS, we found that the Php4 protein associates with the Php2/Php3/Php5 complex PMID:16963626 Consistently, mutations in the php3 - and php5 -encoded CCAAT-binding proteins were phenocopies of php2 PMID:16963626 Consistently, mutations in the php3 - and php5 -encoded CCAAT-binding proteins were phenocopies of php2 PMID:16963626 6b PMID:1699136 figure 1c PMID:1699136 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 figure2 PMID:1699136 figure 1c and Double staining using a combination of cdc13- and tubulin- specific antibodies showed that the dots corresponded exactly to the positions of the mitotic spindle poles (Fig. 3a, b) PMID:17004072 table 2 PMID:17004072 figure 2a PMID:17004072 figure 2a PMID:17004072 figure 5 b PMID:17005570 fig 1 PMID:17005570 Fig 1c lane 9 PMID:17005570 fig 1 PMID:17005570 fig 1 PMID:17005570 fig 5 A PMID:17005570 fig 5 C PMID:17005570 fig 1 PMID:17005570 fig 1 PMID:17005570 fig 6 A, lane 9 PMID:17005570 fig 6 B, lane 3 PMID:17005570 fig 1 PMID:17005570 fig 1 PMID:17005570 fig 7 A PMID:17005570 fig 1 b PMID:17005570 fig 7 A PMID:17005570 fig 6 B, lane 9 PMID:17005570 fig 1 b PMID:17005570 fig 1 c PMID:17005570 fig 1 d PMID:17005570 fig 1 F PMID:17005570 fig 1 f PMID:17005570 fig 1 f PMID:17005570 fig3 PMID:17005570 fig3 PMID:17005570 fig3 PMID:17005570 fig3 PMID:17005570 fig3 PMID:17005570 fig3 PMID:1703321 data not shown PMID:1703321 Figure 4D phospho amino acid analysis PMID:1703321 Figure 4 phospho amino acid analysis PMID:1703321 Figure 4D phospho amino acid analysis PMID:1703321 data not shown PMID:1703321 cdc25 over expressed from the constitutive ADH promoter. Data not shown PMID:1703321 cdc2-F15 gene is expressed from episomal pIRT2 PMID:1703321 cdc2-F15 gene is expressed from episomal pIRT2 PMID:1703321 I'm sure this has already been annotated. But previous annotations didn't come up, should they? PMID:1703321 cdc2-F15 gene is expressed from episomal pIRT2 PMID:1703321 cdc2-F15 gene is expressed from episomal pIRT2 PMID:1703321 Figure 4D phospho amino acid analysis PMID:1703321 Also think this is previously annotated PMID:17035632 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 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1) PMID:17035632 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3). PMID:17035632 whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3). PMID:17035632 whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3). PMID:17035632 whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3). PMID:17035632 whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3). PMID:17035632 whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3). PMID:17035632 whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3). PMID:17035632 whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3). PMID:17035632 whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, dur- ing meiotic prophase (Figure 3). PMID:17035632 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 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 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 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 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 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 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 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 fig1b PMID:17036054 figure 1a PMID:17036054 fig1b PMID:17036054 figure 1a PMID:17036054 figure 1a PMID:17036054 figure 1a PMID:17036054 figure 1a PMID:17036054 fig1b PMID:17036054 fig1b PMID:17036054 fig1b PMID:17036054 Supplement PMID:17036054 figure 1a PMID:17036054 figure 1a PMID:17036054 figure 1a PMID:17038309 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 binds both circular and linear DNA fragments PMID:17039252 especially during S and G2 phases PMID:17039252 especially during S and G2 phases PMID:17039252 especially during S and G2 phases PMID:17039252 especially during S and G2 phases PMID:17046992 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 cells stop growing at high temperature, but remain viable and resume growth and division when returned to standard temperature PMID:17046992 cells stop growing at high temperature, but remain viable and resume growth and division when returned to standard temperature PMID:17085965 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 25 degrees PMID:17112379 30 degrees PMID:17112379 25 degrees PMID:17112379 25 degrees PMID:17112379 30 degrees PMID:17121544 at 30 degrees// Tor1 becomes necessary for cell growth when Tor2 function is compromised. PMID:17121544 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 tor1∆tor2 -19 showed only the 2C peak, and no 1C peak appeared at 36 °C PMID:17121544 at 30 degrees PMID:17121544 70% of ts the tor2 -13 cells committed sexual development to ts form zygotes and spores (Fig. 3B,C) PMID:17121544 (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 (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 (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 (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 Figure 1B PMID:17121544 Figure 1B PMID:17130122 assayed using artificial reporter construct ura4 containing two introns and one exon from nda3 PMID:17130122 assayed using artificial reporter construct ura4 containing two introns and one exon from nda3 PMID:17130122 assayed using artificial reporter construct ura4 containing two introns and one exon from nda3 PMID:17130122 assayed using artificial reporter construct ura4 containing two introns and one exon from nda3 PMID:17178839 fig 4A PMID:17178839 fig 4A PMID:17178839 fig 4A PMID:17178839 fig 4B PMID:17178839 fig 4B PMID:17178839 fig 4C PMID:17178839 not sure if this is correct.... PMID:17178839 not sure if this is correct.... PMID:17178839 fig 2 a/b PMID:17178839 fig 2 a/b PMID:17178839 fig 1c/d PMID:17178839 fig 3A PMID:17178839 fig 3B PMID:17178839 fig 1B PMID:17178839 fig 3c PMID:17178839 fig 3C PMID:17178839 fig 4A PMID:17178839 fig 1B PMID:17178839 fig 1A PMID:17178839 fig 1A PMID:17178839 fig 1A PMID:17178839 fig 1B PMID:17178839 fig 1B PMID:17178839 Fig. 4D PMID:17178839 fig 2 a/b PMID:17178839 fig 1B PMID:17190600 H4K20me2 modified histone binding PMID:17190600 H4K20me2 modified histone binding PMID:17190600 H4K20me2 modified histone binding PMID:17192844 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 proteasomal PMID:17213188 binding by Pab2 PMID:17222800 25S rRNA positions 2304, 2497 PMID:17289569 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 6E PMID:17289569 6D PMID:17289569 6D PMID:17289569 by TGS PMID:17289569 by TGS PMID:17289569 by TGS PMID:17289569 by TGS PMID:17289569 6B PMID:17289569 6B PMID:17289569 (Figure 6B) PMID:17289569 6B PMID:17289569 (Figure 6A) both clr3D232N and mit1K587A mutant alleles alleviated silencing of a marker gene inserted at pericentromeric repeats PMID:17289569 (Figure 6A) both clr3D232N and mit1K587A mutant alleles alleviated silencing of a marker gene inserted at pericentromeric repeats PMID:17289569 (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 (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 (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 (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 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 (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 (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 (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 (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 (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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 (Figure 4C), Levels of Clr3 and Mit1 were dramati- cally reduced at subtelomeres in swi6 mutant strains PMID:17289569 part of tgs PMID:17289569 4B However, defect in RNAi pathway had no impact on Ccq1 localization PMID:17289569 4B We found that Clr3 localization at telomere ends was completely abolished in cells defective in both Taz1 and RNAi pathways. PMID:17289569 4B PMID:17289569 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 4B clr3 at telomeres were reduced to the same extent in mutant strains disrupted for either Ccq1 or Taz1, PMID:17289569 4B clr3 at telomeres were reduced to the same extent in mutant strains disrupted for either Ccq1 or Taz1, PMID:17289569 part of tgs PMID:17304223 foci disappear in HU; without HU foci appear but with abnormal dynamics PMID:17304223 foci disappear in HU; without HU foci appear but with abnormal dynamics PMID:17307401 same as mus81delta alone PMID:17307401 worse than either single mutant PMID:17307401 worse than either single mutant PMID:17307401 worse than either single mutant PMID:17307401 worse than either single mutant PMID:17307401 same as mus81delta alone PMID:17307401 same as mus81delta alone PMID:17307401 worse than either single mutant PMID:17307401 worse than either single mutant PMID:17307401 worse than either single mutant PMID:17307401 worse than either single mutant PMID:17307401 same as mus81delta alone PMID:17317928 assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25 PMID:17317928 assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25 PMID:17317928 assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25 PMID:17317928 assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25 PMID:17317928 assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25 PMID:17317928 assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25 PMID:17339332 same pathway PMID:17352737 anaphase, elongating beyond cell end resulting in long curved spindle, requested PMID:17363370 Fig. 4, A and B PMID:17363370 Fig 1D PMID:17363370 Fig. 4, A and B PMID:17363370 Fig. 4, A and B PMID:17363370 Fig. 4, A and B PMID:17363370 Interestingly, the H2B-K119R mutation sig- nificantly enhanced silencing of the otr1::ura4 (Fig. 5A), PMID:17363370 fig 5D PMID:17363370 fig 5D PMID:17363370 Fig. 1C PMID:17363370 Fig. 1C PMID:17363370 Fig. 1C PMID:17363370 Fig. 4, A and B PMID:17363370 Fig 1D PMID:17363370 Fig 1D PMID:17363370 Fig 1D PMID:17363370 Fig 1D PMID:17363370 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 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 figur 2b PMID:17363370 Fig. 1C PMID:17363370 figur 2b PMID:17363370 figur 2b PMID:17363370 figur 2b PMID:17363370 figur 2b PMID:17363370 figur 2d rhp6 resulted in enhanced silencing of the otr1::ura4, as shown by reduced growth on medium lacking uracil (Fig. 2D) PMID:17363370 figur 2d rhp6 resulted in enhanced silencing of the otr1::ura4, as shown by reduced growth on medium lacking uracil (Fig. 2D) PMID:17363370 figur 2d rhp6 resulted in enhanced silencing of the otr1::ura4, as shown by reduced growth on medium lacking uracil (Fig. 2D) PMID:17363370 figur 2d rhp6 resulted in enhanced silencing of the otr1::ura4, as shown by reduced growth on medium lacking uracil (Fig. 2D) PMID:17363370 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 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 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 (supplemental Fig. 2 PMID:17363370 Fig. 4, A and B PMID:17434129 data not shown PMID:17434129 also from localization and phenotypes PMID:17434129 TEL2L only PMID:17434129 TEL2L only PMID:17434129 TEL2L only PMID:17434129 data not shown PMID:17434129 also from localization and phenotypes PMID:17440621 they only show that this is part of a complex that demethylates H3K9 so there is a chance it is not active? PMID:17442892 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 sense strand PMID:17450151 bulk antisense transcripts PMID:17450151 bulk antisense transcripts PMID:17450151 sense strand PMID:17450151 bulk antisense transcripts PMID:17450151 bulk antisense transcripts PMID:17450151 bulk antisense transcripts PMID:17450151 bulk antisense transcripts PMID:17450151 bulk antisense transcripts PMID:17450151 bulk antisense transcripts PMID:17450151 bulk antisense transcripts PMID:17450151 bulk antisense transcripts PMID:17452352 5c PMID:17452352 "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 "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 fig7 PMID:17452352 fig7 PMID:17452352 fig7 PMID:17452352 fig7 PMID:17452352 fig7 PMID:17452352 fig7 PMID:17452352 fig7 PMID:17452352 fig7 PMID:17452352 fig7 PMID:17452352 fig7 PMID:17452352 fig7 PMID:17452352 fig7 PMID:17452352 5d PMID:17452352 5d PMID:17452352 5d PMID:17452352 5d PMID:17452352 5d PMID:17452352 5d PMID:17452352 5a PMID:17452352 5a PMID:17452352 bet this is a term Val hates :p PMID:17452352 5c PMID:17452352 5c PMID:17452352 5c PMID:17452352 5c PMID:17452352 5c PMID:17452352 fig6 PMID:17452352 fig6 PMID:17452352 fig6 PMID:17452352 fig6 PMID:17452625 regulates binding by myosin; assayed in vitro using rabbit actin and unspecified myosin motor domain PMID:17486116 assayed using bub1 PMID:17510629 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 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 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:17531813 Fig 6B PMID:17531813 Fig 6B PMID:17531813 Fig 6 B PMID:17531813 Fig 5B PMID:17531813 Fig 5B PMID:17531813 Fig5A cdc18 disappears at the end of S-phase in cig2+ strain and accumulates in the absence of cig2 PMID:17531813 Fig 4D In the absence of rad26, cdc18 is unable to stabilise rad3 on chromatin PMID:17531813 Fig 4A PMID:17531813 Fig 4 A PMID:17531813 Fig 4 A PMID:17531813 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 Figure 2D top of lower panel. PMID:17531813 Figure 2C lower panel. cds1 is no longer phosphorylated because rad3 is absent in absence of cdc18 PMID:17531813 Figure 2B upper right panel. In the cytosol rad3 is present in absence of cdc18 PMID:17531813 Figure 2B lower right panel. rad3 is not present in the chromatin fraction in the absence of cdc18 PMID:17531813 Fig 1C PMID:17531813 Fig 1C PMID:17531813 Fig 1C (vw data not shown, but assume are elongated) PMID:17531813 Fig 1C PMID:17531813 Fig 1B PMID:17531813 Fig 1B PMID:17531813 Fig 4A PMID:17531813 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 2A PMID:17531813 2A; during mitotic DNA replication checkpoint PMID:17531813 Fig 1C PMID:17531816 Tas3WG Cells Cannot Efficiently Establish De Novo Centromeric Heterochromatin PMID:17531816 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 centromeric siRNAs were present in the F276Aago1 and tas3WG single mutants but were undetectable in the double mutant (Figure 2F). PMID:17531816 centromeric siRNAs were present in the F276Aago1 and tas3WG single mutants but were undetectable in the double mutant (Figure 2F). PMID:17531816 the double mutant (tas3WG, F276Aago1) displayed markedly elevated levels of total centromeric transcripts (Figure 2E), similar to an ago1 null. PMID:17531816 F276A-ago1 (Figure S3B) caused a slight defect in silencing of the dg cen::ura4+ reporter (Figure S3C). PMID:17531816 ......as were Chp1 and the mutant Tas3WG protein (Figure 2C). PMID:17531816 ......as were Chp1 and the mutant Tas3WG protein (Figure 2C). PMID:17531816 Further, centromeric siRNAs were similarly abundant in tas3WG and tas3+ cells (Figure 2D). PMID:17531816 Chromatin immunoprecipitation (ChIP) analyses showed that Ago1 was indeed localized at centromeres in the tas3WG mutant, a PMID:17531816 Consistent with these findings, tas3WG mutant cells showed no defects in chromosome segregation (Table S2). PMID:17531816 (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 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 Tas3WG Cells Cannot Efficiently Establish De Novo Centromeric Heterochromatin PMID:17538026 fig1 B PMID:17538026 fig1a PMID:17538026 fig1 a PMID:17538026 fig1 2 PMID:17538026 fig 6 B PMID:17538026 fig 6 B PMID:17538026 fig 4 PMID:17538026 fig 4 PMID:17538026 fig 4 PMID:17538026 table 2 PMID:17538026 table 2 PMID:17538026 fig1 a PMID:17538026 figure 3, B and D PMID:17538026 igure 3, B and D PMID:17538026 fig 3a PMID:17538026 fig1 B PMID:17538026 fig1 2 PMID:17538026 fig1 a PMID:17556368 add note in curator feedback to get double mutant phenotypes PMID:17556368 add note in curator feedback to get double mutant phenotypes PMID:17556368 add note in curator feedback to get double mutant phenotypes PMID:17556368 add note in curator feedback to get double mutant phenotypes PMID:17561805 tested through observing no de;ay when checkpoin is inactivated PMID:17579515 Figure 6C (ablated Nuclear envelope) PMID:17579515 Figure 6C PMID:17579515 4G PMID:17579515 (Figure 1). PMID:17579515 Figure 3A and 3B, and Video S3) PMID:17579515 Figure 2 C check (also nuclear envelope protrusion? PMID:17579515 Figure S4) PMID:17579515 Figure S4 /Figure 3A and 3B, and Video S3) PMID:17579515 (APC) activation occurred and chromosome cohesion was lost (Figure 1A and 1B). PMID:17579515 (APC) activation occurred and chromosome cohesion was lost (Figure 1A and 1B). PMID:17579515 S1 PMID:17596513 E. coli ispA mutant used as assay system PMID:17632059 S3 PMID:17632059 table S3 PMID:17632059 fig1e twice their share of DNA and SPBs. PMID:17632059 table S3 PMID:17632059 fig1c PMID:17632059 fig1c PMID:17632059 fig1b PMID:17632059 table S3 PMID:17632059 table S3 PMID:17632059 S3 PMID:17632059 S3 PMID:17632059 S3 PMID:17632059 fig s4e movie S2 PMID:17632059 Matching synonym SPB detached from nucleuss fix syn PMID:17632059 table S3 PMID:17632059 fig3D PMID:17632059 fig3D (I) PMID:17632059 fig3 PMID:17632059 fig3 V-shaped patterns indicating multiple spindles PMID:17632059 fig3 PMID:17632059 fig3 PMID:17632059 fig3 PMID:17632059 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 Fig 1c PMID:17632059 Fig 1c PMID:17632059 Fig 1c PMID:17632059 fig1B PMID:17632059 fig1B PMID:17632059 fig1B PMID:17632059 fig1B PMID:17632059 fig1c PMID:17632059 fig1b PMID:17632059 fig1B PMID:17632059 fig1B PMID:17632059 fig1b PMID:17632059 fig1B PMID:17632059 fig1B PMID:17632059 fig1B PMID:17632059 fig1f PMID:17632059 S3 PMID:17632059 S3 PMID:17632059 S3 PMID:17677001 Figure 2B PMID:17677001 Figure 2B PMID:17677001 Figure 3A EXP says increased, but is normal compared to WT (i.e ura4 insertion derepresses) PMID:17677001 Figure 3B PMID:17677001 Figure 3C spreading is still within the central domain, to the flanking tRNAs PMID:17677001 Figure 4B PMID:17677001 Figure 4C PMID:17677001 Figure S8 PMID:17677001 Figure S1 PMID:17677001 Figure 2A PMID:17677001 Figure 2A PMID:17677001 Figure 2A PMID:17677001 Figure 2B PMID:17677001 Figure 2B PMID:17677001 Figure 2B PMID:17677001 Figure 2B PMID:17677001 Figure 2B PMID:17677001 Figure 2B PMID:17677001 Figure 2B PMID:17677001 Figure 2B PMID:17677001 Figure 2B PMID:17677001 Figure 2B PMID:17677001 Figure 2B PMID:17677001 Figure 2B PMID:17677001 Figure 2B PMID:17677001 Figure 2B PMID:17690116 Fig3 This is the mutant form of pREP4X cdc18 from the screen PMID:17690116 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 Fig9B, C reb1D reduces amount inappropriate recombination at DNA repeats leading to a reduction in cell elongation during checkpoint activation PMID:17690116 Fig9A PMID:17690116 Fig 8A, B PMID:17690116 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 Fig 6C shows Chromosome III smear is present throughout the cell cycle PMID:17690116 Fig3 and previous figs shows lack of re replication with moderate increase in cdc18 protein level PMID:17690116 Fig3 and previous figs shows lack of re replication with moderate increase in cdc18 protein level PMID:17690116 Fig 4C At 25°C rad3 is active but checkpoint cannot be activated in absence of hus1 PMID:17690116 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 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 Fig6A,B PMID:17690116 Fig5C PMID:17690116 Fig5C PMID:17690116 Fig 5B PMID:17690116 Fig 5A PMID:17690116 Fig4C at the permissive temperature rad3ts is active and the checkpoint is activated in absence of mrc1 PMID:17690116 Fig4C at 25°C rad3ts is active and the checkpoint is activated in absence of cds1 PMID:17690116 Fig4C At 25°C rad3 is active but checkpoint cannot be activated in absence of chk1 and cds1 PMID:17690116 Fig4C At 25°C rad3 is active but checkpoint cannot be activated in absence of crb2 PMID:17690116 Fig4C At 25°C rad3 is active but checkpoint cannot be activated in absence of rad26 PMID:17690116 Fig4C At 25°C rad3 is active but checkpoint cannot be activated in absence of rad1 PMID:17690116 Fig4C At 25°C rad3 is active but checkpoint cannot be activated in absence of rad17 PMID:17690116 Fig4C At 25°C rad3 is active but checkpoint cannot be activated in absence of rad9 PMID:17690116 Fig4C At the permissive temperature 25*C rad3 is active but checkpoint cannot be activated in absence of chk1 PMID:17690116 Fig4A PMID:17690116 Fig2D different to when pREP3X cdc18+ is over expressed in G2 block which show replicate intermediates and cells undergo re replication PMID:17690116 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 Fig2B cells arrested due to activation of the rad3 checkpoint gene do not rereplicate PMID:17690116 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 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 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 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 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 Fig9B, C rad52D reduces amount inappropriate recombination at DNA repeats leading to a reduction in cell elongation during checkpoint activation PMID:17690116 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 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 Fig6A,B PMID:17690116 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:17804800 emsa PMID:17868468 deleted existing genome maintence term, and annotated this instead, all things considered... PMID:17881496 Figure 3 A PMID:17881496 Figure 3 A PMID:17881496 ABOLISHED Figure 3 B PMID:17881496 Fig. 1A PMID:17881496 Fig. 1B PMID:17881496 Fig. 3A PMID:17881729 the evidence isn't great PMID:17936710 spores from mre11d/mre11d homozygous diploid PMID:17936710 actually inferred (IC) from combination of phenotype plus GO:0000014 MF PMID:17936710 spores from mre11d/mre11d rec12d/rec12d homozygous diploid PMID:17936710 spores from ctp1d/ctp1d rec12d/rec12d homozygous diploid PMID:17936710 assayed at ctp1 promoter PMID:17936710 spores from ctp1d/ctp1d homozygous diploid PMID:17936710 same as either single mutant PMID:17936710 spores from rec12d/rec12d homozygous diploid PMID:17936710 same as either single mutant PMID:17937917 (site B) PMID:17937917 (site B) PMID:17937917 (site A) PMID:18030666 spatial extent PMID:18030666 spatial extent PMID:18030666 spatial extent PMID:18030666 epigenetic variegation both 5-FOA-resistant and -sensitive colonies were found PMID:18030666 spatial extent PMID:18030666 spatial extent PMID:18030666 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 spatial extent PMID:18030666 "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 "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 spatial extent PMID:18042546 all microarray (table 1); arz1 also northern (fig 1) PMID:18042546 all microarray (table 1); arz1 also northern (fig 1) PMID:18042546 all microarray (table 1); arz1 also northern (fig 1) PMID:18042546 time course after transcription shutoff, so actually measuring degradation PMID:18042546 all microarray (table 1); arz1 also northern (fig 1) PMID:18042546 all microarray (table 1); arz1 also northern (fig 1) PMID:18042546 all microarray (table 1); arz1 also northern (fig 1) PMID:18042546 all microarray (table 1); arz1 also northern (fig 1) PMID:18042546 all microarray (table 1); arz1 also northern (fig 1) PMID:18042546 all microarray (table 1); arz1 also northern (fig 1) PMID:18042546 all microarray (table 1); arz1 also northern (fig 1) PMID:18042546 all microarray (table 1); arz1 also northern (fig 1) PMID:18042546 all microarray (table 1); arz1 also northern (fig 1) PMID:18059460 speckles in Fig. 4A PMID:18060866 localization independent of actin cytoskeleton (assayed using latrunculin A) and microtubule cytoskeleton (assayed using carbendazim) PMID:18061564 figure 6F PMID:18061564 fig6 PMID:18061564 bundle maintenence https://github.com/geneontology/go-ontology/issues/18215 PMID:18061564 in overlap zones PMID:18061564 activation PMID:18061564 FORMATION PMID:18061564 minus end PMID:18061564 figure 6F PMID:18079700 Figure 3 A (but not S phase) PMID:18079700 Rad21 PMID:18079700 Figure 3 A PMID:18079700 maintenence PMID:18079700 Supplementary Figure S2 PMID:18079700 Figure 3 A/B PMID:18079700 Figure 3C and E PMID:18079700 Figure 3 B PMID:18079700 Figure 3 B PMID:18079700 Figure 3 C/E PMID:18079700 Figure 3 C/E PMID:18079700 Figure 3 C/E during G1 PMID:18093330 Fig8 PMID:18093330 fig 1 PMID:18093330 Fig8 PMID:18157149 I guess this can be changed once we can do RNA mods PMID:18157152 this is a protein modification so should be changed once we can do RNA mods PMID:18160711 region between NdeI and XhoI sites deleted PMID:18160711 truncated at PacI site PMID:18160711 region between NsiI sites deleted PMID:18165685 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 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 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 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 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 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 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:18223116 fig2 PMID:18223116 fig2 PMID:18223116 fig2 PMID:18223116 fig2 PMID:18223116 fig6, it doesn't bind dna according to later studies PMID:18223116 fig2 PMID:18223116 fig2 PMID:18223116 fig2 PMID:18223116 fig2 PMID:18223116 fig2 PMID:18223116 fig2 PMID:18223116 fig2 PMID:18223116 fig2 PMID:18223116 fig2 PMID:18223116 fig2 PMID:18223116 fig2 PMID:18256284 figure 1A PMID:18256284 figure 1B (plus end) PMID:18256284 figure 1B (plus end) PMID:18256284 figure 1B (plus end) PMID:18256284 figure 1A PMID:18256284 figure 1B (plus end) PMID:18256290 increased more than pxl1delta alone PMID:18256290 increased more than pxl1delta alone PMID:18256290 less levere than pxl1 null PMID:18256290 increased more than pxl1delta alone PMID:18256290 increased more than pxl1delta alone PMID:18256290 increased more than pxl1delta alone PMID:18256290 less levere than pxl1 null PMID:18256290 localization dependent on filamentous actin (GO:0031941); tested using latrunculin A PMID:18262494 after chromosome segregation PMID:18262494 (Fig. 1B) PMID:18262494 with extreme sister chromtid oscillations PMID:18272786 data from table; nothing more specific shown PMID:18272786 dependent on F-actin (assayed using Latrunculin A) PMID:18272786 data from table; nothing more specific shown PMID:18272786 data from table; nothing more specific shown PMID:18272786 data from table; nothing more specific shown PMID:18272786 data from table; nothing more specific shown PMID:18276645 normal oxygen level PMID:18276645 normal oxygen level PMID:18328707 Fig 1 PMID:18328707 fig 1D PMID:18328707 GTP-bound Figure 4E, polarization localization to both cell ends PMID:18328707 Fig 1 PMID:18328707 Figure 3A PMID:18328707 Figure 3B PMID:18328707 Fig 1D (pom1 is catalytically active but not localized to cell ends) PMID:18328707 GTP bound PMID:18328707 GTP-bound Figure 4E PMID:18328707 Figure 4E PMID:18328707 GTP bound active form PMID:18328707 GTP bound fig 3C PMID:18328707 active GTP bound form PMID:18328707 *****OLD*****waiting for GO PMID:18328707 Fig 1D PMID:18328707 Fig 1D PMID:18328707 Fig 1 PMID:18328707 Fig 1 PMID:18328707 old end PMID:18328707 Fig1SE to cell cortex of (newnon growing) cell tip from medial cortex PMID:18328707 FigS1D PMID:18328707 Fig1SE to cell cortex of (new) cell tip from medial cortex PMID:18328707 Fig1SE to cell cortex of (new) cell tip from medial cortex PMID:18328707 Fig 2C PMID:18331722 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:18331722 in vitro assay PMID:18337696 at time 0. they don't look at nitrogen starvation for very long, only 60 mins PMID:18378696 same as nbs1delta alone PMID:18378696 same as nbs1delta alone PMID:18378696 same as either single mutant PMID:18378696 same as either single mutant PMID:18378696 same as nbs1delta alone PMID:18378696 same as nbs1delta alone PMID:18378696 same as rad51delta alone PMID:18378696 same as either single mutant PMID:18391219 "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:18399988 they show transfer to a heterologous cytochrome p450 enzyme, but pombe doesn't have any mitochondrial ones. PMID:18411246 Fig. 5B PMID:18411246 Fig. 2A PMID:18411246 (Fig. 3A) PMID:18411246 enclosure arrow in Figs 4Ci,ii) PMID:18411246 Fig. 2B PMID:18411246 (Fig. 3A) PMID:18414064 same with or without TBZ PMID:18414064 penetrance at 4 hours PMID:18414064 penetrance at 4 hours PMID:18414064 same with or without TBZ PMID:18414064 penetrance at 4 hours; increases upon longer time at restrictive temp PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 glycerol = derepressing for glucose repression also assayed using lacZ under fbp1 promoter (and maltose carbon source, also derepressing) PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 git2-1 is effectively null, even though it isn't a complete deletion of the coding sequence PMID:1849107 git2-1 is effectively null, even though it isn't a complete deletion of the coding sequence PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:1849107 also assayed using lacZ under fbp1 promoter PMID:18493607 present throughout mitotic cell cycle PMID:18493607 slighly more severe than sir2+ overexpression alone PMID:18493607 same as sir2+ overexpression alone PMID:18495844 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 Fig3B,C PMID:18495844 Fig3B PMID:18495844 Fig1B PMID:18495844 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 Fig1B and 2B,C normal MTs required to establish early orientation of mitotic spindle by aligning SPBs with long axis of cell PMID:18495844 Fig1B normal interphase MTs required to establish early orientation of mitotic spindle by aligning SPBs with long axis of cell PMID:18495844 Fig 2B PMID:18495844 Fig3B PMID:18514516 same as either single mutant PMID:18514516 same as either single mutant PMID:18514516 same as either single mutant PMID:18514516 same as either single mutant PMID:18514516 same as either single mutant PMID:18562692 Fig. 6C PMID:18562692 Fig. 6C PMID:18562692 Fig. 6C PMID:18562692 Fig. 5A PMID:18562692 Fig. 6C PMID:18562692 Fig. 6C PMID:18562692 Fig. 5A PMID:18562692 Fig. 6C PMID:18562692 Fig. 6C PMID:18562692 Fig. 6C PMID:18562692 Fig. 6C PMID:18562692 Fig. 6C PMID:18562692 Fig. 6C PMID:18562692 Fig. 5B PMID:18562692 Fig. 5B PMID:18562692 Fig. 5A PMID:18562692 Fig. 4 PMID:18562692 Fig. 3 PMID:18562692 Fig. 1 PMID:18562692 Fig. 1 PMID:18615848 same as swi7-H4 alone, i.e. it's dominant PMID:1863602 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 in vitro PMID:18653539 figure 2A PMID:18653539 figure 1A PMID:18653539 figure 1 C PMID:18653539 figure 1A, 8A PMID:18653539 Fig. 1D PMID:18653539 Fig. 1D, Fig. 1F PMID:18653539 figure 1B PMID:18653539 figure 2A PMID:18653539 figure 2A PMID:18653539 Fig 2 F during veg phase PMID:18653539 figure 8B PMID:18653539 figure 8B PMID:18653539 figure 8B PMID:18653539 figure 8B PMID:18662319 also L-gamma-glutamyl-L-cysteine PMID:18667531 synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81 (Figure 2, C and D). PMID:18667531 synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81 (Figure 2, C and D). PMID:18667531 synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81 (Figure 2, C and D). PMID:18667531 synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81 (Figure 2, C and D). PMID:18667531 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 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 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 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 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 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 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 The C219A mutant was not temperature sensitive (Figure 2A). PMID:18667531 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 nulcleolus inheritance PMID:18676809 Conversely, mutations disrupting dimerization did not disrupt -H2A.1 binding (Fig. 3C). PMID:18676809 Conversely, mutations disrupting dimerization did not disrupt -H2A.1 binding (Fig. 3C). PMID:18676809 Conversely, mutations disrupting dimerization did not disrupt -H2A.1 binding (Fig. 3C). PMID:18676809 fig 4 a PMID:18676809 fig 4 a PMID:18676809 fig 4 a PMID:18676809 fig 4 a PMID:18676809 fig 4 a PMID:18676809 fig 4 a PMID:18676809 fig 4 a PMID:18676809 fig 4 a PMID:18676809 fig 4 a PMID:18676809 fig 4 a PMID:18676809 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 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 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 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 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 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 the Ser666Arg and Cys663Arg mutants ran as monomeric species in gel filtration, indicative of disruption of their dimerization PMID:18676809 the Ser666Arg and Cys663Arg mutants ran as monomeric species in gel filtration, indicative of disruption of their dimerization PMID:18676809 Conversely, mutations disrupting dimerization did not disrupt -H2A.1 binding (Fig. 3C). PMID:18716626 (Supplementary Fig. 2a) , but not in another heterochromatin-defect- ive strain, clr4D, which lacks H3K9me (ref. 7) PMID:18716626 Fig. 1a PMID:18716626 Fig. 1a–d PMID:18716626 Fig. 1a–d PMID:18716626 Fig. 1a–d PMID:18716626 (Supplementary Fig. 2a) We confirmed that Psc3–2CD, as well as 2CD, itself localizesat discrete nuclear dots in swi6D cell PMID:18716626 (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 (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 (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 (Fig. 3f). The assay of chromosome segregation further revealed that sgo1-VE cells provoke nondisjunction in meiosis II, similarly to swi6D cells PMID:18716626 (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 (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 (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 (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 (Fig. 2f) Sgo1–CD did indeed localize at the centromere regardless of swi6D PMID:18716626 (Fig. 2e) Sgo1 localization is impaired in swi6D cells PMID:18716626 (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 (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 (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 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 figure 1g 30% cells? PMID:18716626 (Supplementary Fig. 3a). We confirmed that the expression of Psc3–2CD does not restore transcriptional silencing in swi6D cells PMID:18723894 no barrier activity with reversed polarity as in rtf1-S154L single mutant PMID:18723894 no barrier activity with reversed polarity as in rtf1-S154L single mutant PMID:18723894 "RTS1 inversion background abolishes DSB formation; ""decreased"" level in rtf1-W405G is relative to wild type and above the inverted-RTS1 background level" PMID:18769921 during vegetative growth because non-sporulating strains used PMID:18769921 during vegetative growth because non-sporulating strains used PMID:18769921 during vegetative growth because non-sporulating strains used PMID:18769921 slightly more sensitive at low temperature than standard PMID:18769921 during vegetative growth because non-sporulating strains used PMID:18769921 slightly worse than sfr1delta alone PMID:18769921 during vegetative growth because non-sporulating strains used PMID:18794373 arrest at Ter2 and Ter3 sites abolished PMID:18794373 arrest at Ter2 and Ter3 sites abolished PMID:18794373 binds at Ter3 site PMID:18794373 arrest at Ter2 and Ter3 sites abolished PMID:18794373 arrest at Ter2 and Ter3 sites abolished PMID:18794373 arrest at Ter2 and Ter3 sites abolished PMID:18794373 arrest at Ter2 and Ter3 sites abolished PMID:18849471 qualifier=major PMID:18854158 no extension because growth is decreased generally, making expressivity hard to judge PMID:18854158 no extension because growth is decreased generally, making expressivity hard to judge PMID:18854158 no extension because growth is decreased generally, making expressivity hard to judge PMID:18854158 no extension because growth is decreased generally, making expressivity hard to judge PMID:18854158 abolished interaction between wt and mutant; interaction partially restored if both copies are mutant PMID:18854158 abolished interaction between wt and mutant; interaction partially restored if both copies are mutant PMID:18854158 no extension because growth is decreased generally, making expressivity hard to judge PMID:18854158 no extension because growth is decreased generally, making expressivity hard to judge PMID:18854158 no extension because growth is decreased generally, making expressivity hard to judge PMID:18854158 no extension because growth is decreased generally, making expressivity hard to judge PMID:18854158 no extension because growth is decreased generally, making expressivity hard to judge PMID:18854158 no extension because growth is decreased generally, making expressivity hard to judge PMID:18854158 no extension because growth is decreased generally, making expressivity hard to judge PMID:18854158 no extension because growth is decreased generally, making expressivity hard to judge PMID:18951025 one or more of mutated serine residues PMID:18951025 one or more of mutated serine residues PMID:18957202 As shown in Figure 2E, lid2-j, like clr8Δ, is hypersensitive to TBZ PMID:18957202 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 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 Figure 1A PMID:18957202 Figure 2A PMID:18957202 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 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 drastic reduction of Swi6 binding (Figure 3D). PMID:18957202 In contrast, H3K4me3 methylation was increased significantly (Figure 3C) PMID:18957202 As shown in Figure 3B, H3K9 methylation at the centromere was completely abolished. PMID:18957202 mating-type region was likewise reduced (Figure 3A) PMID:18957202 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 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 Obvious reduction of H3K9 methylation was also observed in lid2-phd2 and lid2-phd3 mutants (Figure S9) PMID:18957202 Obvious reduction of H3K9 methylation was also observed in lid2-phd2 and lid2-phd3 mutants (Figure S9) PMID:18957202 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 RNAI dependent PMID:18957202 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 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 We further noted the striking similarity of the genome-wide transcription profiles of the lid2-j and lsd1Δ mutants (Figure 6C), suggest PMID:18957202 Figure 5F, the point mutation resulted in a significant loss of silencing at the centromere otr region. PMID:18957202 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 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 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 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 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:18957202 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 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 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 As shown in Figure 5C, siRNA is barely detectable. PMID:18957202 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 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 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 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 ChIP assays indicated that H3K9me2 methylation at the region was abolished, while H3K4me3 methylation was increased more than seven-fold (Figure S2) PMID:18957202 ChIP assays indicated that H3K9me2 methylation at the region was abolished, while H3K4me3 methylation was increased more than seven-fold (Figure S2) PMID:18957202 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 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 WT and frequently exhibited an aberrant elongated cell shape (Figure 2C) PMID:18957202 28% of the cells contained fragmented nuclear DNA (Figure 2D), indicating that the mutant nucleus is disorganized. PMID:18957202 overexpressing Lid2 enhances H3K9 methylation (Figures 5G and H) PMID:18957202 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 GFP-Lid2 is resistant to detergent extraction indicating Lid2 is a chromatin-binding protein (Figure 2A). PMID:1899284 also supported by complementation of S.c. deletion PMID:19001497 fig 1 C PMID:19001497 fig 4 F PMID:19001497 Fig4a PMID:19001497 fig3 PMID:19001497 supplementary material Fig. S1) PMID:19001497 Fig 1 E PMID:19001497 Fig4D PMID:19001497 Fig4D PMID:19001497 Fig4c PMID:19001497 fig 1 D, 1 E PMID:19001497 supplementary material Fig. S1) PMID:19001497 fig 4 F PMID:19001497 fig 1 D PMID:19001497 fig 1 D, 1 E PMID:19001497 fig3 PMID:19001497 fig3 PMID:19001497 Fig 2 D-F PMID:19001497 Fig 2 D-F PMID:19001497 Fig 2 D-F PMID:19001497 Fig 2 D-F PMID:19001497 Fig 2 D-F PMID:19001497 Fig 2 D-F PMID:19001497 Fig 2 D-F PMID:19001497 Fig 2 D-F PMID:19001497 Fig 2 D-F PMID:19001497 Fig 2 D-F PMID:19001497 fig 2 BC PMID:19001497 fig 2 BC PMID:19001497 fig 2 BC PMID:19001497 fig 2 a (this fig also has expression level for mutant alleles) PMID:19001497 supplementary material Movies 2-4). PMID:19001497 supplementary material Movies 2-4). PMID:19001497 supplementary material Movies 2-4). PMID:19001497 supplementary material Movies 2-4). PMID:19001497 Fig 1 E PMID:19001497 Fig 1 E PMID:19001497 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 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 fig 1 C PMID:19001497 fig 1 D PMID:19001497 fig 1 D, 1 E PMID:19001497 fig 1 D, 1 E PMID:19001497 fig 1 D, 1 E PMID:19001497 Fig 1 E PMID:19001497 fig 1 C PMID:19001497 fig 1 C PMID:19001497 Fig4c PMID:19023408 Southern blot PMID:19023408 Southern blot PMID:19023408 microarray PMID:19023408 Southern blot PMID:19023408 Southern blot PMID:19023408 ChIP PMID:19023408 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 Southern blot PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 Figure 4D PMID:19026779 *****ABOLISHED*****Figure 4D PMID:19033384 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 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 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 The checkpoint doesn't sense all types of dna damage eg that caused by gamma radiation or DNA adduct formation by PUVA PMID:19033384 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 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 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 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 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 Figure 4, A and B, and Supplemen- tal Movie S1 PMID:1905818 haploid, either mating type PMID:1905818 (changed to GTPase from signal transducer) PMID:19111658 binds centromeric transcripts PMID:19117951 gave dark staining with iodine,switch to the opposite state at a low rate PMID:19117951 mat1Msmto REIIdelta mat2::ura4 gave dark staining with iodine, metastable and switch to the opposite state at a low rate PMID:19117951 mat1Msmto REIIdelta mat2::ura4 PMID:19117951 mat1Msmto REIIdelta mat2::ura4 PMID:19117951 gave dark staining with iodine,switch to the opposite state at a low rate PMID:19117951 mat1Msmto REIIdelta mat2::ura4 PMID:19117951 mat1Msmto REIIdelta mat2::ura4 PMID:19117951 mat1Msmto REIIdelta mat2::ura4 PMID:19117951 heterochromatin PMID:19117951 mat1Msmto REIIdelta mat2::ura4 PMID:19117951 mat1Msmto REIIdelta mat2::ura4 PMID:19139265 Fig. S5 PMID:19139265 fig9 PMID:19139265 fig8 PMID:19139265 Fig. S5 PMID:19150433 covalent binding between topoisomerase and DNA PMID:19150433 covalent binding between topoisomerase and DNA PMID:19150433 covalent binding between topoisomerase and DNA PMID:19150433 covalent binding between topoisomerase and DNA PMID:19150433 covalent binding between topoisomerase and DNA PMID:19150433 covalent binding between topoisomerase and DNA PMID:19150433 covalent binding between topoisomerase and DNA PMID:19155267 Table S1, Supplementary Data PMID:19155267 Table S1, Supplementary Data PMID:19155267 Table S1, Supplementary Data PMID:19158664 "closest we can get to ""at stalled fork"" with available terms" PMID:19185548 qualifier=different_pathway PMID:19185548 qualifier=different_pathway PMID:19189958 Figure 2b PMID:19189958 Figure 2A PMID:19189958 Figure 2 PMID:19189958 Figure 2 PMID:19189958 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 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 Figure 1 PMID:19189958 Figure 1 PMID:19189958 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 10% of cells PMID:19189958 47% of cells PMID:19189958 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 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 Figue 5B How- ever, their growth was rescued in the presence of sorbitol PMID:19189958 Figue 5B As expected for the rgf31 shut-off, the cells died in the presence of thiamine (promoter off). PMID:19189958 Figue 5B How- ever, their growth was rescued in the presence of sorbitol PMID:19189958 Figue 5B As expected for the rgf31 shut-off, the cells died in the presence of thiamine (promoter off). PMID:19189958 Figure 5B viable and phenotypically in- distinguishable from the ehs2-1 mutant PMID:19189958 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 GS activity was threefold higher than that observed in the wild-type strain (Figure 4C) PMID:19189958 GS activity was threefold higher than that observed in the wild-type strain (Figure 4C) PMID:19189958 cells were larger than wild-type cells and displayed multiple abnormal septa. PMID:19189958 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 the amount of active Rho1p increased considerably in the strain over- expressing Rgf2p as compared with the wild-type strain (Figure 4B PMID:19189958 Figure 3B PMID:19189958 Figure 2A PMID:19189958 Figure 2A PMID:19189958 Figure 4c positive PMID:19189958 "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 Figure 3A PMID:19189958 Figure 2A PMID:19189958 Figure 2A PMID:19202278 absent beta 1,3 gal PMID:19202289 (Fig. 2B) PMID:19202289 (Fig. 2B) PMID:19202289 (data not shown). PMID:19202289 Fig. 1B PMID:19202289 Fig. 1B PMID:19202289 (Fig. 3B) PMID:19202289 Fig. 1A PMID:19202289 Fig. 1B PMID:19202289 (Fig. 3C) PMID:19202289 (Fig. 3A and B) PMID:19202289 (Fig. 3A and B) PMID:19202289 Fig. 1A PMID:19202289 (Fig. 2D) PMID:19202289 (Fig. 2D) PMID:19202289 (Fig. 3C) PMID:19202289 (Fig. 3B) PMID:19205745 temp semi-permissive for cdc6-23 alone PMID:19205745 temp semi-permissive for cdc20-M10 alone PMID:19205745 temp semi-permissive for pol1-1 alone PMID:19205745 temp semi-permissive for cdc6-23 alone PMID:19205745 temp semi-permissive for cdc6-23 alone PMID:19205745 temp semi-permissive for cdc6-23 alone PMID:19211838 spores from homozygous diploids PMID:19211838 spores from homozygous diploids PMID:19211838 spores from homozygous diploids PMID:19211838 spores from homozygous diploids PMID:19211838 spores from homozygous diploids PMID:19211838 spores from homozygous diploids PMID:19211838 spores from homozygous diploids PMID:19211838 spores from homozygous diploids PMID:19211838 spores from homozygous diploids PMID:19211838 spores from homozygous diploids PMID:19211838 spores from homozygous diploids PMID:19214192 DNA polymerases present in late S; epsilon (cdc20) earlier than alpha (pol1) or delta (cdc6) PMID:19214192 present in late S PMID:19214192 present throughout cell cycle but at higher level in S phase PMID:19214192 present throughout cell cycle but at higher level in late S phase PMID:19214192 present in late S PMID:19214192 present at roughly constant level throughout cell cycle PMID:19214192 present in late S PMID:19214192 present throughout cell cycle but at higher level in S phase PMID:19214192 DNA polymerases present in late S; epsilon (cdc20) earlier than alpha (pol1) or delta (cdc6) PMID:19214192 present throughout cell cycle but at lower level in S phase PMID:19214192 DNA polymerases present in late S; epsilon (cdc20) earlier than alpha (pol1) or delta (cdc6) PMID:19214192 present in late S, as late as pols alpha & delta PMID:19217404 abolished, fig1 d PMID:19217404 abolished, fig1 d PMID:19217404 abolished, fig1 d PMID:19217404 abolished, fig1 d PMID:19217404 fig S10 PMID:19217404 abolished, fig1 d PMID:19217404 abolished, fig1 d PMID:19250904 same as either single mutant PMID:19250904 assayed using purified HeLa histone octamers PMID:19250904 same as either single mutant PMID:19250904 same as either single mutant PMID:19250904 same as either single mutant PMID:19250904 same as either single mutant PMID:19250904 same as either single mutant PMID:19250904 same as either single mutant PMID:19250904 same as either single mutant PMID:19250904 same as either single mutant PMID:19250904 same as either single mutant PMID:19279143 fig 4F PMID:19279143 fig 4F PMID:19279143 """Thus, Nrd1 di- rectly binds with Cdc4 mRNA in vivo and in vitro""" PMID:19279143 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:19328067 serine2 PMID:19328067 (All at eng2 CDS) PMID:19328067 "Mcs6 ""primes"" Rpb1 for phosphorylation by cdk9" PMID:19328067 (All at eng2 CDS) PMID:19328067 (All at eng2 CDS) PMID:19328067 serine 2 PMID:19328067 serine 5/serine2 PMID:19328067 (All at eng2 CDS) PMID:19328067 (All at eng2 CDS) PMID:19330768 G2 temperature shift PMID:19330768 in arrested cells, indicating independent of cell cycle progression PMID:19330768 G1 temperature shift PMID:1934126 same as cdc25-22 single mutant PMID:1934126 same as cdc25-22 single mutant PMID:1934126 same as cdc25-22 single mutant PMID:1934126 same as cdc25-22 single mutant PMID:19357077 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:19363481 Figure 5 PMID:19363481 Figure 5 PMID:19363481 Figure 5 PMID:19363481 Figure 5 PMID:19363481 Figure 5 PMID:19363481 Figure 5 PMID:19363481 Figure 5 PMID:19363481 Figure 5 PMID:19363481 SLD1 PMID:19363481 Figure 5 PMID:19363481 Figure 5 PMID:19363481 Figure 5 PMID:19363481 Strikingly, a GST-Rad60 SLD2E380R construct did not detectably interact with Ubc9-TAP (Fig. 3a), PMID:19363481 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 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 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 Figure 5 PMID:19363481 Figure 5 PMID:19363481 Figure 5 PMID:19363481 Figure 5 PMID:19363481 Figure 5 PMID:19363481 Figure 5 PMID:19363481 Figure 5 PMID:19366728 fragmented PMID:19366728 fragmented PMID:19366728 fragmented PMID:19366728 fragmented PMID:19366728 fragmented PMID:19366728 fragmented PMID:19366728 fragmented PMID:19366728 fragmented PMID:19366728 fragmented PMID:19366728 fragmented PMID:19366728 fragmented PMID:19366728 fragmented PMID:19366728 fragmented PMID:19373772 "happens during mitotic M phase? term will be renames ""mitochondrial membrane fission""" PMID:19373772 "happens during mitotic M phase? term will be renames ""mitochondrial membrane fission""" PMID:19373772 during mitotic M phase? PMID:19373772 non fermentable carbon source PMID:19394293 Figure 3. PMID:19394293 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 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 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 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 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 (Figure 3C). PMID:19394293 (Figure 3C). PMID:19394293 (Figure 3C). PMID:19394293 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 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 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 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 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 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 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:19416828 "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 (Supplemental Table S1). PMID:19417105 figure 1 PMID:19417105 (Supplemental Table S1). PMID:19417105 (Supplemental Table S1). PMID:19417105 (Supplemental Table S1). PMID:19417105 Supplemental Table S1; Supplemental Fig. S3 PMID:19417105 Supplemental Table S1; Supplemental Fig. S3 PMID:19417105 Supplemental Table S1; Supplemental Fig. S3 PMID:19417105 figure 1 PMID:19417105 Supplemental Table S1; Supplemental Fig. S3 PMID:19417105 Supplemental Table S1; Supplemental Fig. S3 PMID:19417105 figure 5A PMID:19417105 figure 5A PMID:19417105 (Supplemental Table S1). PMID:19417105 (Fig. 5B) PMID:19417105 (Fig. 5B) PMID:19417105 figure 5A PMID:19417105 (Supplemental Table S1). PMID:19417105 (Fig. 5B) PMID:19417105 (Supplemental Table S1). PMID:19422421 actually 25 degrees, but calling it low to make distinction from inviable at 30 PMID:19422421 25 degrees, but calling it low to make distinction from inviable at 30 PMID:19422421 actually 25 degrees, but calling it low to make distinction from inviable at 30 PMID:19422421 actually 25 degrees, but calling it low to make distinction from inviable at 30 PMID:19422421 25 degrees (permissive for hsk1-89) PMID:19422421 25 degrees (permissive for hsk1-89) PMID:19422421 25 degrees (permissive for hsk1-89) PMID:19422421 25 degrees (permissive for hsk1-89) PMID:19422421 25 degrees (permissive for hsk1-89) PMID:19422421 25 degrees (permissive for hsk1-89) PMID:19422421 25 degrees (permissive for hsk1-89) PMID:19422421 increased chromatin association in presence of HU PMID:19422421 30 degrees PMID:19422421 25 degrees, but calling it low to make distinction from inviable at 30 PMID:19422421 25 degrees, but calling it low to make distinction from inviable at 30 PMID:19430462 urg1, gar2, act1, adh1, pof9 and hcn1 mRNAs were shown to be direct targets by cRACE sequence analysis. PMID:19430466 homodimer PMID:19430466 Fig. 2c PMID:19430466 Fig. 2d, lane 4 PMID:19430466 Fig. 2j PMID:19430466 Fig. 2j PMID:19430466 Fig. 1f ATP-dependent Supplementary Information, Movie 1) PMID:19431238 ocalization independent of actin cytoskeleton (assayed using latrunculin A) and microtubule cytoskeleton (assayed using carbendazim) PMID:19431238 ocalization independent of actin cytoskeleton (assayed using latrunculin A) and microtubule cytoskeleton (assayed using carbendazim) PMID:1943699 assay construct also has nt change G36C to distinguish from snu2+ transcript PMID:1943699 assay construct also has nt change G36C to distinguish from snu2+ transcript PMID:1943699 assay construct also has nt change G36C to distinguish from snu2+ transcript PMID:1943699 assay construct also has nt change G36C to distinguish from snu2+ transcript PMID:1943699 assay construct also has nt change G36C to distinguish from snu2+ transcript PMID:1944266 assayed substrate: rabbit muscle phosphorylase PMID:19454013 Rad21 PMID:19454013 Rad21 PMID:19474789 Fig 1 a,b PMID:19474789 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 Figure 4 d PMID:19474789 Supplementary Table 2 These experiments support the pom1 gradient model, pom1 is delocalized in tea1 delete PMID:19474789 Supplementary Table 2 These experiments support the pom1 gradient model, pom1 is delocalized in tea1 delete PMID:19474789 Supplementary Table 2 These experiments support the pom1 gradient model, pom1 is delocalized in tea1 delete PMID:19474789 Supplementary Table 2 PMID:19474789 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 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 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 Supplementary Fig. 10 PMID:19474789 fig3 PMID:19474789 fig3 PMID:19474789 fig3 PMID:19474789 fig3 PMID:19474789 fig3 PMID:19474789 fig3 PMID:19474789 fig3 PMID:19474789 fig3 PMID:19474789 fig3 PMID:19474789 fig3 PMID:19474789 fig3 PMID:19474789 fig3 PMID:19474789 fig3 PMID:19474789 Supplementary Figure S8 PMID:19474789 Supplementary Figure S8 PMID:19474789 Supplementary Figure S8 PMID:19474789 Supplementary Figure S8 PMID:19474789 Fig. 2a and Supplementary Fig. 3a PMID:19474789 Fig. 2a and Supplementary Fig. 3a PMID:19474789 Fig. 2a and Supplementary Fig. 3a PMID:19474789 Fig. 2a and Supplementary Fig. 3a PMID:19474789 Fig. 2a and Supplementary Fig. 3a PMID:19474789 Fig. 2a and Supplementary Fig. 3a PMID:19474789 Fig. 3a PMID:19474789 Supplementary Fig. 6 PMID:19474789 Supplementary Fig. 6 PMID:19474789 Fig. 2a and Supplementary Fig. 3a PMID:19474789 Fig. 2a and Supplementary Fig. 3a PMID:19474789 Fig. 2a and Supplementary Fig. 3a PMID:19474789 Fig. 2c,d,e PMID:19474789 Fig. 2c,d,e PMID:19474789 Fig. 2c,d,e PMID:19474789 Supplementary Table 1 PMID:19474789 Fig. 2a and Supplementary Fig. 3a PMID:19474789 Fig. 2a and Supplementary Fig. 3a PMID:19474789 Fig. 2a and Supplementary Fig. 3a PMID:19474789 Fig. 2a and Supplementary Fig. 3a PMID:19474789 Fig. 2a and Supplementary Fig. 3a PMID:19474789 Fig. 2a and Supplementary Fig. 3a PMID:19474789 Fig 1 a,b PMID:19474789 Fig 1 a,b PMID:19474789 Fig. 1c and Supplementary Fig. 2a PMID:19474792 Fig. 2a and data not shown PMID:19474792 Fig. 1e in vitro link from epistastis and delayed cdc2 phosphorylation PMID:19474792 (Fig. 3b). PMID:19474792 (Fig. 3b). PMID:19474792 (Fig. 3b). PMID:19474792 (Fig. 3b). PMID:19474792 (Fig. 3b). PMID:19474792 Table 1 and Fig. 2d PMID:19474792 Table 1 and Fig. 2d PMID:19474792 Table 1 and Fig. 2d PMID:19474792 or is this reduced with low exressivity? PMID:19474792 fig 1b PMID:19474792 table1 PMID:19474792 Table 1 PMID:19474792 Table 1 PMID:19474792 fig 1b PMID:19474792 Table 1 PMID:19474792 Table 1 PMID:19474792 Table 1 PMID:19474792 Table 1 PMID:19474792 table1 PMID:19474792 table1 PMID:19474792 table1 PMID:19474792 table1 PMID:19474792 Table 1 PMID:19474792 Table 1 PMID:19474792 Table 1 PMID:19474792 Table 1 PMID:19474792 Table 1 PMID:19474792 table1 PMID:19474792 table1 PMID:19474792 fig 1d ie not blocked in g2 PMID:19474792 Fig. 1e Fig. 1f) PMID:19474792 Fig. 1e in vitro link from epistastis and delayed cdc2 phosphorylation PMID:19474792 fig 1g PMID:19474792 Supplementary Fig. 2 PMID:19474792 Supplementary Fig. 2 PMID:19474792 fig 1b PMID:19474792 Supplementary Fig. 3 PMID:19474792 Supplementary Fig. 3 PMID:19474792 Supplementary Fig. 4 PMID:19474792 Fig. 2a and data not shown PMID:19474792 Fig. 2a and data not shown PMID:19474792 cortex PMID:19486165 Fig. 1A PMID:19486165 Fig. 1A PMID:19486165 Fig. 1A PMID:19486165 (data not shown). PMID:19486165 Fig. 1C PMID:19486165 Fig. 2A PMID:19486165 Fig. 2B PMID:19486165 (Fig. 4B) PMID:19486165 Figure 4 C PMID:19486165 Figure 4 C PMID:19486165 Figure 4 C PMID:19486165 Fig. 5A PMID:19486165 Fig. 5B PMID:19486165 Fig. 5C PMID:19486165 Fig. 5C PMID:19486165 Fig. 5C PMID:19486165 Fig. 6C PMID:19486165 figure 7 A PMID:19486165 (Fig. 7B) PMID:19486165 (Fig. 7B) PMID:19486165 (Fig. 7B) PMID:19486165 (Fig. 7B) PMID:19486165 (Fig. 7B) PMID:19486165 (Fig. 7B) PMID:19487457 (Fig. 4 C and Video 3) PMID:19487457 insertion PMID:19487457 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 monopolar PMID:19487457 gapped membrane distortions in the nuclear envelope of cut12.1 cells at 36°C (Fig. 3, A–D). 7D PMID:19487457 monopolar PMID:19487457 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 Surprisingly, in 50% (n = 79) of the cut12.1 cells that successfully completed mitosis, an efflux of the NLS-GFP–-Gal marker accompanied mitotic commitment (Fig. 7, C and D). PMID:19487457 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 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:19487461 Fig 1B PMID:19487461 Fig1A BrdU incorporation wee1-50 strain analysed at 32°C PMID:19487461 Fig1G amount of tos1-GFP in nucleus is dependent on cdc10 PMID:19487461 section titled MBF-dependent gene expression...these cells undergo G1 transcription, a seemingly normal Sphase (no region specific amplifications) and can only reinitiate replication once size per genome is minimal size. PMID:19487461 Fig5A PMID:19523829 increased dlocalization of mad2 to kinetochore PMID:19543678 (Fig. 3) PMID:19543678 from PM (Fig. 3c PMID:19543678 (Fig. 3) PMID:19546237 during recovery from stress PMID:19570908 myo2 PMID:19570908 myo2 PMID:19570908 request and use GO:new positive regulation of (MF) microfilament motor activity instead? depends on ancestry of motor activity branch PMID:19570908 25 degrees C, i.e. lower end of normal temp. range; penetrance higher at 29 degrees C PMID:19571115 Fig. 5B PMID:19571115 Fig. 5B PMID:19571115 fig1 PMID:19571115 fig1 PMID:19571115 Fig. 5a PMID:19571115 fig5D PMID:19592249 figure 1a PMID:19592249 figure 1a PMID:19592249 fig1 PMID:19592249 figure 1E apc complex binding PMID:19592249 figure 1E apc complex binding PMID:19592249 figure2 PMID:19592249 figure2 PMID:19592249 figure 2a abolished PMID:19592249 figure 2a abolished PMID:19592249 fig2 PMID:19605557 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 figure 6 PMID:19605557 figure 6 PMID:19605557 figure 6 PMID:19605557 GII Is Required for an Efficient In Vitro Glucose Trimming from G2M9 and G1M9 PMID:19605557 figure 6 PMID:19606211 See Fig. 1 PMID:19606211 Sequence LVIAMDQLNL mentioned in the text PMID:19624755 localized to large endosomal structures PMID:19624755 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 localized to large endosomal structures PMID:19624755 localized to large endosomal structures PMID:19624755 localized to large endosomal structures PMID:19624755 localized to large endosomal structures PMID:19624755 Fig. 6a, wt, arrowheads PMID:19624755 Fig. 6a, wt, arrowheads PMID:19624755 fig5 PMID:19624755 fig5 PMID:19624755 fig5 PMID:19624755 fig5 PMID:19624755 fig5 PMID:19624755 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 (Fig. 2b) whereas that of Dapl4 and Daps1 cells was partially inhibited PMID:19624755 (Fig. 2b) D-apl2 and D-apm1 cells was completely inhibited in the presence of FK506 PMID:19624755 (Fig. 2b) D-apl2 and D-apm1 cells was completely inhibited in the presence of FK506 PMID:19624755 fig5 PMID:19624755 fig5 PMID:19624755 fig5 PMID:19624755 Fig4. suggesting that the four adaptin subunits of the AP-1 complex are all localized to the Golgi ⁄ endosomes. PMID:19624755 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 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 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 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 localized to large endosomal structures PMID:19624755 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 localized to large endosomal structures PMID:19624755 localized to large endosomal structures PMID:19625445 fig8 PMID:19625445 Fig 1 16.5 +/- 0.78 PMID:19625445 Fig 1 IS THIS SMALL OR STUBBY? 11.6 +/- 0.45 PMID:19625445 Fig 1 PMID:19625445 Fig 1 PMID:19625445 Fig 1 PMID:19625445 Fig 1 PMID:19625445 Fig 1 PMID:19625445 Fig 1C PMID:19625445 Fig 1C PMID:19625445 Fig 1 C PMID:19625445 Fig 1C PMID:19625445 Fig 1C PMID:19625445 fig 1D PMID:19625445 fig 1D PMID:19625445 fig 1D PMID:19625445 fig 1D PMID:19625445 Fig 2A PMID:19625445 Fig 2A PMID:19625445 Fig 2A PMID:19625445 Fig 2B PMID:19625445 Fig 2A PMID:19625445 Fig 2B PMID:19625445 Fig 2A PMID:19625445 Fig 2B PMID:19625445 Fig 2B PMID:19625445 Fig 2A PMID:19625445 Fig 2A PMID:19625445 Fig 2D PMID:19625445 Fig 2D PMID:19625445 Figure 3D PMID:19625445 figure 4A PMID:19625445 figure 4A IS THIS NORMAL OR EVEN HIGHER THAN WT? PMID:19625445 figure 4A IS THIS NORMAL OR EVEN HIGHER THAN WT? (this is higher than wis1DD-cpc2delet so must be increased PMID:19625445 Figure 3D PMID:19625445 Figure 3D PMID:19625445 Figure 3D PMID:19625445 Figure 3D PMID:19625445 Figure 4B PMID:19625445 Figure 4B PMID:19625445 Figure 4B PMID:19625445 Figure 4B PMID:19625445 Figure 4B PMID:19625445 Figure 4c PMID:19625445 Figure 4c PMID:19625445 Fig 2A PMID:19625445 Fig 2A PMID:19625445 Figure 5A PMID:19625445 Figure 5A PMID:19625445 Figure 5B PMID:19625445 Figure 5B PMID:19625445 Figure 5B PMID:19625445 Figure 5B PMID:19625445 figure 5D PMID:19625445 figure 5D PMID:19625445 figure 6a PMID:19625445 figure 6a PMID:19625445 figure 6a PMID:19625445 figure 6a PMID:19625445 figure 6a PMID:19625445 figure 6a PMID:19625445 figure 6a PMID:19625445 figure 6a PMID:19625445 figure 6a PMID:19625445 figure 6a PMID:19625445 figure 6c,d PMID:19625445 Figure 7 PMID:19625445 Figure 7 PMID:19625445 Figure 7 PMID:19625445 fig8 PMID:19625445 fig9A PMID:19625445 Figure 9B PMID:19625445 Figure 9B PMID:19625445 Figure 9 PMID:19625445 Figure9 PMID:19627505 localization requires F-actin (assayed using latrunculin A) and membrane rafts (assayed using filipin) PMID:19636559 not shown, from text PMID:19636559 not shown, from text PMID:19636559 not shown, from text PMID:19643199 fig 1 d this term should really be trafficing PMID:19643199 fig 1 d PMID:19643199 fig 1 c PMID:19643199 fig 1 d PMID:19646873 2f PMID:19646873 2f PMID:19646873 2f PMID:19646873 S2 PMID:19646873 2f PMID:19680287 Fig. 3B/C. SEE ABOVE PMID:19680287 Fig. 1A PMID:19680287 Fig. 1A PMID:19680287 Fig. S6A/B PMID:19680287 Fig. S6C/D PMID:19680287 Fig. S6C/D PMID:19680287 Fig. S7 PMID:19680287 Fig. S10 PMID:19680287 (Fig 3C), showed a similar fraction of mono-oriented chromosomes as wild-type cells PMID:19680287 rarely showed a delay in bi-orienting chromosomes that had been pulled towards one SPB (Fig 3B,D; supplementary Fig S4F online). PMID:19680287 Fig. 1A PMID:19680287 Fig. 1A PMID:19680287 Fig. 1A PMID:19680287 Fig. 1B, S3 PMID:19680287 Fig. 1B, S3 PMID:19680287 Fig. 1B, S3 PMID:19680287 Fig. 1B, S3 PMID:19680287 Fig. 2A assayed with plo1 GFP PMID:19680287 Fig. S2B PMID:19680287 Fig. 2B PMID:19680287 Fig. S2B PMID:19680287 Fig. S2B PMID:19680287 Fig. S2A PMID:19680287 Fig. S2A PMID:19680287 Fig. S2A PMID:19680287 Fig. 3E, S9 PMID:19680287 Fig. 3E, S9 PMID:19680287 Fig. 2B PMID:19680287 Fig. 3B/C moved down from congresssion to abnormal mitotic sister chromatid biorientation ? PMID:19680287 Fig. 3E PMID:19680287 Fig. 3B/C PMID:19680287 Fig. 3E PMID:19680287 Fig. 3E PMID:19686686 fig 1e PMID:19686686 interphase, prophase, metaphase,anaphase A PMID:19686686 mitotic anaphase B PMID:19686686 fig 1e PMID:19686686 mitotic anaphase B, mitotic telophase PMID:19686686 mitotic anaphase B, mitotic telophase PMID:19686686 fig 4 a PMID:19686686 cdc2 dependent phophorylation (fig. 5B) PMID:19686686 fig 4 a PMID:19686686 Figure 3 D PMID:19686686 interphase, prophase, metaphase,anaphase A PMID:19686686 cdc2 dependent phophorylation (fig. 4B) PMID:19686686 fig 1e PMID:19686686 interacts with unmodified Klp9 PR:000027705 PMID:19686686 Figure 3 D PMID:19686686 interphase, prophase, metaphase,anaphase A PMID:19686686 interphase, prophase, metaphase,anaphase A PMID:19686686 interacts with unmodified Ase1 PR:000027520 PMID:19686686 fig 1e PMID:19686686 fig 1e PMID:19686686 fig 1e PMID:19686686 fig 1e PMID:19686686 Figure 3 D PMID:19686686 Figure 3 D PMID:19686686 Figure 3 D PMID:19686686 Fig. 5C PMID:19686686 Fig. 5C PMID:19686686 Fig. 5C PMID:19686686 Fig. 5C PMID:19686686 with monopolar spindle PMID:19696784 figure5 PMID:19696784 supplementary Fig S6 online PMID:19696784 fig 1 c PMID:19696784 fig 1 c PMID:19696784 (Fig 3B) PMID:19696784 (Fig 3B) PMID:19696784 (Fig 3B) PMID:19696784 Fig 2A,B PMID:19713940 temperature restrictive for cdc25-22 PMID:19713940 assayed using N-terminal Rng2-Ns fragment or calponin homology domain (CHD) fragment PMID:19713940 temperature restrictive for cdc25-22 PMID:19713940 temperature restrictive for cdc25-22 PMID:19713940 observed after short-duration overexpression PMID:19723888 figure 1B PMID:19723888 fig1C PMID:19723888 fig1C PMID:19723888 fig1A PMID:19723888 fig1A PMID:19723888 fig1A PMID:19723888 fig1C PMID:19723888 fig1C PMID:19723888 fig1C PMID:19723888 fig1D PMID:19723888 fig1D PMID:19723888 fig1D PMID:19723888 fig1C PMID:19723888 figure 1B PMID:19723888 fig1C PMID:19723888 Fig 2A III PMID:19723888 Fig 2A III PMID:19723888 Fig 2A III PMID:19723888 Fig 2A III PMID:19723888 figure 2B PMID:19723888 fig 2 PMID:19723888 fig 2 PMID:19723888 fig1A PMID:19723888 fig1A PMID:19723888 fig1A PMID:19723888 fig1A PMID:19723888 fig1A PMID:19723888 fig1A PMID:19723888 fig1A PMID:19723888 fig1A PMID:19723888 fig1A PMID:19723888 fig1A PMID:19723888 figure 1B PMID:19723888 figure 1B PMID:19723888 figure 1B PMID:19723888 figure 1B PMID:19723888 figure 1B PMID:19723888 figure 1B PMID:19723888 figure 1B PMID:19723888 fig1C PMID:19723888 fig1C PMID:19723888 fig1C,D PMID:19736319 Fig. 4 B and not depicted PMID:19736319 Fig. S1 B and not depicted PMID:19736319 2% fig 6a. to dauughter PMID:19736319 arrested normal size (multiple rounds of cytokinesis) in interphase PMID:19736319 Fig. 4 B and not depicted PMID:19736319 2% fig 6a PMID:19736319 Fig. S1 C, arrows PMID:19736319 add to def, septated in interphase. one compartment is anucleate PMID:19736319 fig 4d PMID:19758558 Fig. S3D PMID:19798055 decreased overall PMID:19804755 ctp-Phosphorylated PMID:19804755 residues include one or more of S77, T78, T79, S87, and T89, and other(s) PMID:19879140 MT spindown assay PMID:19879140 Biochemistry PMID:19879140 MT spindown assay. PMID:19942659 Like the gms1D mutant, neither the uge1D strain nor the uge1Dgal10D strain reacted with PNA (Fig. 2b PMID:19942659 minor PMID:19942659 major PMID:19942852 fig1 PMID:19942852 fig3 PMID:19942852 fig3 PMID:19942852 fig6a PMID:19942852 fig3 PMID:19942852 fig6a PMID:19942852 1D PMID:19942852 1D PMID:19942852 S2 &3 PMID:19942852 fig1 PMID:19942852 1D PMID:19942852 fig1 PMID:19942852 1D PMID:19942852 1D PMID:19942852 fig1 PMID:19942852 S2 &3 PMID:19942852 1D PMID:19942852 1D PMID:19942852 1D PMID:19948483 Fig. 3 PMID:19948483 Fig. 3 PMID:19948483 Fig. 3 PMID:19948483 Fig. 3 PMID:19948484 they say periphery in the text but it has TM domains PMID:19948484 this is an adaptor PMID:19948484 they say periphery in the text but it has TM domains PMID:19965387 S3, mes1delta background PMID:19965387 fusion experiments fig3 PMID:19965387 S3, mes1delta background PMID:19965387 S3, mes1delta background PMID:19965387 S3, mes1delta background PMID:19965387 fig S5 PMID:19965387 fig 3a PMID:19965387 fig 3a PMID:19965387 fig 3a PMID:19965387 fig 3a PMID:19965387 S6 PMID:19965387 S6 PMID:19965387 4c PMID:19965387 fig 3a PMID:19965387 fig 3a PMID:19965387 fig 3a PMID:19965387 fig2c, in psc3-1T background PMID:19965387 fig 2f PMID:19965387 fig 2f PMID:19965387 fig 2f PMID:19965387 fig 2f PMID:19965387 fig 2e PMID:19965387 fig 2e PMID:19965387 fig 2e PMID:19965387 fig 2e PMID:19965387 fusion experiments fig3 PMID:19965387 fusion experiments fig3 PMID:19965387 fusion experiments fig3 PMID:19965387 4g PMID:19965387 4g PMID:19965387 4g PMID:19965387 fig2c, in psc3-1T background PMID:19965387 4g PMID:19965387 fig 3a PMID:19965387 fig 3a PMID:19965387 4c PMID:19965387 fig2c, in psc3-1T background PMID:19965387 fig2c, in psc3-1T background PMID:19965387 fig 3a PMID:19965387 fig S3 PMID:19965387 fig S3 PMID:19965387 fig 3a PMID:19965387 S6 PMID:19965387 S6 PMID:19965387 S6 PMID:19965387 S6 PMID:19965387 S6 PMID:20062003 4 PMID:20062003 3 PMID:20062003 2D PMID:20062003 4 PMID:20062003 4 PMID:20062003 S1 PMID:20062003 S1 PMID:20062003 S1 PMID:20062003 4 PMID:20062003 4 PMID:20062003 4 PMID:20075862 3a left panel PMID:20089861 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 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 Forms gamma H2A dependent nuclear foci when over-expressed PMID:20110347 32 degrees PMID:20110347 32 degrees PMID:20110347 25 degrees PMID:20110347 25 degrees PMID:20110347 32 degrees PMID:20110347 25 degrees PMID:20110347 25 degrees PMID:20110347 32 degrees; semi-permissive for cdc8-27 alone PMID:20110347 25 or 32 degrees; latter semi-permissive for cdc8-27 alone PMID:20123974 increased unequal sister chromatid recombination PMID:20123974 increased unequal sister chromatid recombination PMID:20123974 also ctp1,rec12,rad22,rti1,rad51,dmc1 unequal sister chromatid recombination (USCR) PMID:20123974 increased unequal sister chromatid recombination PMID:20129053 snoRNAs with extended poly(A) tails accumulate in these foci PMID:20129053 snoRNAs with extended poly(A) tails accumulate in these foci PMID:20140190 same as nbs1-c60-delta alone PMID:20140190 same as nbs1-c60-delta alone PMID:20140190 full-length Rad3 or Rad3-kd-delta PMID:20140190 full-length Rad3 or Rad3-kd-delta PMID:20164182 unstressed cells PMID:20164182 unstressed cells PMID:20164182 unstressed cells PMID:20164182 unstressed cells PMID:20164182 unstressed cells PMID:20164182 unstressed cells PMID:20164182 unstressed cells PMID:20164182 unstressed cells PMID:20164182 unstressed cells PMID:20164182 unstressed cells PMID:20164182 unstressed cells PMID:20164182 unstressed cells PMID:20164182 unstressed cells PMID:20164182 unstressed cells PMID:20164182 unstressed cells PMID:20164182 unstressed cells PMID:20164182 unstressed cells PMID:20164182 unstressed cells PMID:20211136 not sure which clrc subunit it binds to? PMID:20211136 abolished at exogenous RNA polII transcribed gene PMID:20211136 endogenous ade6 PMID:20211136 this is the endogenous dg repeat PMID:20226666 Figure 1 PMID:20226666 Figure 1 PMID:20226666 Figure 1 in interphase PMID:20226666 Figure 1 in interphase PMID:20230746 involved in negative regulation of transcription via transcription factor catabolism PMID:20299449 IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT PMID:20299449 IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT PMID:20299449 IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT PMID:20299449 IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT PMID:20360683 assayed using ypt3 reporter with or without premature stop codons PMID:20360683 assayed using GFP reporter with or without premature stop codons PMID:20360683 assayed using ypt3 reporter with or without premature stop codons PMID:20360683 assayed using GFP reporter with or without premature stop codons PMID:2038306 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 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 Data not shown. pMNScdc2-DL5 is integrated PMID:2038306 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 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 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 CDC2HS complements cdc2delete phenotype Figure 4B PMID:2038306 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 pMNScdc2-DL5 is integrated PMID:2038306 Data not shown. pMNScdc2-DL5 is integrated PMID:2038306 pMNScdc2-DL5 is an episomal plasmid. PMID:2038306 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 pMNScdc2-DL5 fails to rescue cdc2-33 mutant at the restrictive temperature. Do not say how this was assayed PMID:2038306 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 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:20383139 fig3a par1, the regulatory subunit was used in the assay PMID:20383139 fig1b PMID:20383139 fig1b PMID:20383139 fig1b PMID:20383139 fig1b PMID:20383139 Fig 1d PMID:20383139 Fig 1e PMID:20383139 fig1e PMID:20383139 fig 1d PMID:20383139 Fig. S1a PMID:20383139 Fig. 2b PMID:20383139 Fig. 2b PMID:20383139 fig3a PMID:20383139 Fig. 2b PMID:20383139 Fig. 2b PMID:20383139 fig3a PMID:20383139 fig3a PMID:20383139 fig 3 c PMID:20383139 fig 3 c PMID:20383139 Fig. 5c PMID:20383139 Fig. 5b PMID:20383139 fig 5c PMID:20383139 fig 5B PMID:20383139 Fig. 5b PMID:20383139 Fig. 5b PMID:20383139 Fig. S5 PMID:20383139 Fig. S5 PMID:20383139 fig 4 c PMID:20383139 separation PMID:20434336 Figures2A and 2B PMID:20434336 Figures2A and 2B PMID:20434336 Figures2A and 2B PMID:20434336 Figures2A and 2B PMID:20434336 Fig 1 PMID:20434336 Fig 1 PMID:20434336 Fig 1 PMID:20434336 data not shown PMID:20434336 fig3 PMID:20434336 fig3 PMID:20434336 (Figure S3A) PMID:20434336 Fig3 C protein distributed in cortex PMID:20434336 Fig3 C PMID:20434336 Fig3 C PMID:20434336 Fig 4E PMID:20434336 Fig1 PMID:20434336 figure S1C PMID:20434336 fig3 PMID:20434336 Fig 1 PMID:20434336 figure S1B PMID:20434336 figure S1C PMID:20434336 Figures2A and 2B cortical/tubular PMID:20434336 Figures2A and 2B cortical/tubular PMID:20434336 Fig 2D tubular/cortical PMID:20434336 Figures2A and 2B PMID:20434336 Fig 1 PMID:20434336 Fig 1 PMID:20434336 Fig1 PMID:20434336 Fig1 PMID:20434336 Fig1 PMID:20434336 Fig 1 PMID:20434336 fig3 PMID:20434336 fig3 PMID:20434336 fig3 PMID:20434336 Figures2A and 2B PMID:20452294 assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all PMID:20452294 assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all PMID:20452294 assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all PMID:20452294 assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all PMID:20452294 assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all PMID:20452294 PCNA trimerization PMID:20452294 PCNA trimerization PMID:20452294 assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all PMID:20452294 assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all PMID:20452294 assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all PMID:20517925 Fig. 1B PMID:20517925 Fig. 1B oreover, actin cables often significantly overgrew in these cells while the actin ring formation seemed to be unaf- fected. PMID:20517925 Fig. 1B PMID:20517925 formation PMID:20517925 Fig. 3D PMID:20517925 Fig. 3D PMID:20517925 Fig. 1B PMID:20517925 Fig. S1 PMID:20547592 fig 2 e suggesting that Vgl1 might escort RNA from ER-associated polyribosomes to the cytosol under thermal stress. PMID:20547592 fig 5 e PMID:20547592 figure 4 PMID:20547592 Figure 5A PMID:20547592 fig 5 a PMID:20547592 fig 5 b PMID:20547592 Figure 5A PMID:20547592 fig 6 D PMID:20547592 fig 6 c PMID:20547592 Figure 6E) PMID:20547592 (Figure 7A) PMID:20547592 (Figure 7B) PMID:20547592 Figure 8A and B (fairly similar expression orofiles) PMID:20547592 fig 5 b PMID:20547592 figure 6 a PMID:20547592 fig 1 PMID:20547592 fig 1 PMID:20547592 fig 1 nuclear PMID:20547592 fig 1 c PMID:20605454 at ste11 PMID:20605454 at ste11 PMID:20605454 at ste11 PMID:20605454 at act1 & sam1 PMID:20605454 at ste11 PMID:20605454 at act1 & sam1 PMID:20605454 polII CTD; probably S5 but can't rule out effect on S7 PMID:20605454 pol II CTD; probably S2 but can't rule out effect on S7 PMID:20622008 at genes PMID:20622014 temperature restrictive for mmi1-ts3 PMID:20622014 temperature restrictive for mmi1-ts3 PMID:20622014 temperature restrictive for mmi1-ts3 PMID:20622014 pol II localization to sme2 locus PMID:20622014 temperature restrictive for mmi1-ts3 PMID:20622014 temperature restrictive for mmi1-ts3 PMID:20623139 low expressivity PMID:20623139 high expressivity PMID:20624975 depolymerization (cytoplasmic?) PMID:20624975 Fig. S5 B–E PMID:20624975 fig 5C PMID:2065367 incomplete penetrance due to translational frameshifting PMID:2065367 incomplete penetrance due to translational frameshifting PMID:2065367 incomplete penetrance due to translational frameshifting PMID:2065367 incomplete penetrance due to translational frameshifting PMID:2065367 severity is variable, and segregates over successive generations (but not 2:2) PMID:2065367 incomplete penetrance due to translational frameshifting PMID:2065367 incomplete penetrance due to translational frameshifting PMID:20661445 Phosphorylated at centromeres during S-phase, Rad3 dependent PMID:20661445 Rad3 dependent PMID:20661445 Rad3 dependent PMID:20661445 Rad3 dependent PMID:20661445 Rad3 dependent PMID:20661445 Rad3 dependent PMID:20661445 Rad3 dependent PMID:20661445 Rad3 dependent PMID:20661445 Rad3 dependent PMID:20661445 Rad3 dependent PMID:20661445 Rad3 dependent PMID:20661445 Phosphorylated at Tf2-type retrotransposons and wtf elements during S-phase, Rad3-dependent PMID:20661445 Phosphorylated at Tf2-type retrotransposons and wtf elements during S-phase PMID:20661445 ChIP PMID:20661445 Phosphorylated at mating type locus during S-phase, Rad3-dependent PMID:20661445 Phosphorylated at mating type locus during S-phase in Rad3 dependent manner PMID:20661445 Phosphorylated at centromeres during S-phase, Rad3 dependent PMID:20661445 Phosphorylated at centromeres during S-phase, Rad3 dependent PMID:20661445 Phosphorylated at centromeres during S-phase, Rad3 dependent PMID:20661445 Phosphorylated at Tf2-type retrotransposons and wtf elements during S-phase PMID:20679485 Crb2 binds phosphorylated histone H2A (Hta1 Serine-129 and Hta2 Serine-128) through its C-terminal BRCT domains PMID:20679485 Crb2 binds phosphorylated histone H2A (Hta1 Serine-129 and Hta2 Serine-128) through its C-terminal BRCT domains PMID:20705466 temperature semi-permissive for cdc8-27 PMID:20705466 temperature semi-permissive for cdc8-27 PMID:20705466 temperature semi-permissive for cdc8-27 PMID:20705466 temperature semi-permissive for cdc8-27 PMID:20705471 temperature permissive for cdc8-27 PMID:20736315 Fig4 PMID:20736315 Fig1B PMID:20736315 Fig1B PMID:20739936 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 figS6 PMID:20739936 figS6 PMID:20739936 fig2a PMID:20739936 fig2a PMID:20739936 fig2a,b. figS5 PMID:20739936 fig1S4/ figS5 PMID:20739936 fig1j PMID:20739936 fig1d,k PMID:20739936 fig1c PMID:20739936 The cdc13-M7 mutant is suppressed by bir1-8D PMID:20739936 fig 1k PMID:20739936 fig1 PMID:20739936 figb PMID:20739936 Supplementary Fig. 8a) PMID:20739936 fig2a,b. figS5 PMID:20739936 fig2a,b. figS5 PMID:20739936 fig 1b PMID:20739936 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 fig S1 PMID:20739936 Fig. 1e/Fig. 1f PMID:20739936 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 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 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 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 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 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 fig 1c PMID:20739936 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 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 Fig 1h PMID:20739936 Fig 1i PMID:20739936 fig1j PMID:20739936 Bir1-N-5A abolished the interaction with Sgo2, whereas Bir1-N-5D retained the interaction (Fig. 2h) PMID:20739936 Bir1-N-5A abolished the interaction with Sgo2, whereas Bir1-N-5D retained the interaction (Fig. 2h) PMID:20739936 Supplementary Fig. 8a) PMID:20799962 same as rid2-1 alone PMID:20799962 same as rid1-1 alone PMID:20805322 assayed substrate MBP PMID:20805322 assayed substrate MBP PMID:20805322 negative reg of polarization/remodelling PMID:20805322 assayed substrate casein PMID:20805322 assayed substrate MBP PMID:20805322 assayed substrate MBP PMID:20805322 assayed substrate MBP PMID:20805322 assayed substrate MBP PMID:20805322 assayed substrate MBP PMID:20805322 Fig. 1 A and Table I) PMID:20807799 GO:0051329= mitotic interphase PMID:20807799 acetylated Cdc82 so could use PR:000037081 PMID:20807799 PR:000037081= tropomyosin cdc8, acetylated form (fission yeast) PMID:20807799 "vw: I used ""added by naa20 which is the catalytic subunit for naa25""" PMID:20826461 fig 2A PMID:20826461 fig 6 PMID:20826461 fig 5 PMID:20826461 fig 6 PMID:20826461 fig 6 PMID:20826461 fig 6 PMID:20826461 fig 5 PMID:20826461 fig 5 PMID:20826461 fig 5 PMID:20826461 fig 4 PMID:20826461 fig 2C PMID:20826461 fig 2C PMID:20826461 fig 2C PMID:20826461 fig 2C PMID:20826461 fig 2B PMID:20826461 fig 2A PMID:20826461 fig 2A PMID:20826461 (Fig. 1F PMID:20826461 (Fig. 1F PMID:20826461 Fig. 1 PMID:20826461 Fig. 1 PMID:20826461 (Fig. 1C PMID:20826805 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 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 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 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 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 figure 2 a PMID:20829365 figure 5 PMID:20829365 figure 3 PMID:20829365 figure 2 a PMID:20829365 figure 3 PMID:20829365 figure 3 PMID:20829365 figure 3 PMID:20829365 figure 1 a PMID:20829365 figure 3 PMID:20829365 figure 1 a PMID:20833892 fig 3 B WT 10% PMID:20854854 fig 1b PMID:20854854 fig 1c PMID:20854854 fig 1c PMID:20854854 fig 1a PMID:20854854 fig 3 PMID:20854854 fig 3 PMID:20854854 I don't understand the chemistry well enough to know how the HPLC shows this but I think this is enough evidence? PMID:20854854 fig 1a PMID:20854854 fig 1b PMID:20854854 fig 1c PMID:20854854 fig 1a PMID:20885790 less sensitive than ssb3delta alone PMID:20890290 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 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 ternary complex normally forms with Swi1-Swi3 and Mrc1 on DNA PMID:20924116 regulates binding by Mrc1 PMID:20924116 regulates binding by Mrc1 PMID:20924116 ternary complex normally forms with Swi1-Swi3 and Mrc1 on DNA PMID:20924116 ternary complex normally forms with Swi1-Swi3 and Mrc1 on DNA PMID:20924116 ternary complex normally forms with Swi1-Swi3 and Mrc1 on DNA PMID:20929775 phosphorylated PMID:20929775 phosphorylated PMID:20929775 K9-mehtylated PMID:20929775 phosphorylated PMID:20929775 K9 methyl;ated PMID:20929775 K9-mehtylated PMID:20935472 during metaphase PMID:20935472 Thus, we conclude that Cdc2 activity prevents precocious localization of Mde4 to the metaphase spindle. PMID:20937798 in supp fig1 shows weak sensitivity at high cadmium concentrations PMID:20944394 https://github.com/geneontology/go-ontology/issues/15345 PMID:20967237 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 Fig6D,E in presence of LatA + MBC there is no SPB separation compared to + MBC only where SPBs can separate PMID:20967237 Fig2B in this case (high temp + MBC) cells can proceed through cell cycle and replicate their DNA PMID:20967237 Fig5A PMID:20967237 Fig4E PMID:20967237 Fig4C followed the presence of clp1 in the nucleolus to monitor cen3 PMID:20967237 data not shown PMID:20967237 Fig4B PMID:20967237 Fig4D PMID:20967237 Fig4A PMID:20967237 Fig3G suggests nuclear fission is independent of spindle checkpoint PMID:20967237 video S3 PMID:20967237 Fig3E PMID:20967237 Fig 3F PMID:20967237 Fig3 D PMID:20967237 Fig3C PMID:20967237 Fig3B just a short microtubule stub remains PMID:20967237 Fig2c in presence of MBC cells re-enter S phase earlier than in the absence of MBC PMID:20967237 Fig2c PMID:20967237 Fig2 A PMID:20967237 Fig1D; microtubules absent PMID:20967237 Fig1D PMID:20967237 Fig1D PMID:20967237 Fig1D PMID:20967237 Fig1E PMID:20967237 Fig1C PMID:20967237 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:20980623 figS1 PMID:20980623 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 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 Figure 4E PMID:20980623 Figure 4E PMID:20980623 upplemental Figure S3 PMID:20980623 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 fig2 PMID:20980623 Fig 2 B&C At anaphase II, however, many of the Dma1-GFP signals did not accumulate at SPBs PMID:20980623 upplemental Figure S3 PMID:20980623 figS1 PMID:20980623 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 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 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:21035342 "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 vw: bit 61 is importabt for torc2 regulation by ryh1 PMID:21035342 "(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 "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:21095590 phosphorylation of rad9 by DDK releases rad9 from damaged chromatin and allows repair factors to come in. fig6 PMID:21095590 fig 5b PMID:21095590 fig 5b PMID:21095590 phosphorylation of rad9 by DDK releases rad9 from damaged chromatin and allows repair factors to come in. fig6 PMID:21098122 no expressivity extension because of decreased growth when untreated PMID:21098122 no expressivity extension because of decreased growth when untreated PMID:21098122 no expressivity extension because of decreased growth when untreated PMID:21098122 no expressivity extension because of decreased growth when untreated PMID:21098122 no expressivity extension because of decreased growth when untreated PMID:21098122 nuclease-dead allele PMID:21098122 no expressivity extension because of decreased growth when untreated PMID:21098122 no expressivity extension because of decreased growth when untreated PMID:21098122 no expressivity extension because of decreased growth when untreated PMID:21098122 no expressivity extension because of decreased growth when untreated PMID:21098141 In SGs after hyperosmotic shock (1 M KCl) but not after glucose deprivation PMID:21099360 hsk1 phenotypes more informative than mrc1 itself PMID:21099360 30 degrees; same as hsk1-89 alone PMID:21099360 at ars2004 and oriChr2-1266, during early S phase PMID:21099360 30 degrees; same as hsk1-89 alone PMID:21099360 same as hsk1-89 alone PMID:21099360 same as hsk1-89 alone PMID:21099360 30 degrees PMID:21099360 25 degrees PMID:21099360 25 degrees, same as hsk1-89 alone PMID:21099360 same as hsk1-89 alone PMID:21099360 in SQ/TQ clusters . , activated_by(CHEBI:29035) PMID:21099360 25 degrees, same as hsk1-89 alone PMID:21099360 30 degrees; same as hsk1-89 alone PMID:21099360 MBP substrate PMID:21099360 25 degrees PMID:21099360 30 degrees PMID:21099360 30 degrees PMID:21099360 25 degrees, same as hsk1-89 alone PMID:21099360 25 degrees, same as hsk1-89 alone PMID:21099360 30 degrees; same as hsk1-89 alone PMID:21099360 30 degrees; restrictive for hsk1-89 alone PMID:21099360 not in SQ/TQ clusters PMID:21107719 localization independent of actin cytoskeleton (assayed using latrunculin A) and microtubule cytoskeleton (assayed using carbendazim) PMID:21113731 Microscopy co-localization PMID:21118717 Active against both cAMP and cGMP based on its ability to confer resistance to exogenous cyclic nucleotides. Fig. 1A, B PMID:21118717 Active against both cAMP and cGMP based on its ability to confer resistance to exogenous cyclic nucleotides. Fig. 1A, B PMID:21118717 Deletion of both cyr1/git2 and cgs2 produces cells that are hypersensitive to both exogenous cAMP and cGMP as these can activate PKA at low micromolar concentrations. Fig. 1A, B PMID:21131906 nda1- background to activate spindle checkpoint PMID:21131906 un- ubiquitinated PMID:21131906 nda1 background to activate spindle checkpoint PMID:21131906 nda1- background to activate splindle checkpoint PMID:21148300 Cdc42-GTP assayed with CRIB PMID:21148300 Cdc42-GTP assayed with CRIB PMID:21148300 Cdc42-GTP assayed with CRIB PMID:21148300 Cdc42-GTP assayed with CRIB PMID:21151114 independent of Clr4 PMID:21151114 independent of Clr4 PMID:21151114 independent of Clr4 PMID:21151114 SO:0000286 = LTR PMID:21151114 independent of Clr4 PMID:21151114 independent of Clr4 PMID:21151114 independent of Clr4 PMID:21151114 independent of Clr4 PMID:21151114 independent of Clr4 PMID:21151114 independent of Clr4 PMID:21151114 SO:0000286 = LTR PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21182284 i) unknown kinase ii) asynchronous cells iii) unknown PMID:21217703 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 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 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 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 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 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 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 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 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 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 binding site L405 ndc80 loop PMID:21256022 affecting dis1 PMID:21300781 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 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 fig7 PMID:21300781 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 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 supp fig 9A PMID:21317872 colocalization with Pcf11 PMID:21317872 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 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 presumably in homozygous diploid PMID:21357609 Mitochondrial dye showed diffuse staining. they think it is a loss of membrane potential so the dye is not drawn in properly PMID:21389117 fig 6C PMID:21389117 i changed this to +ve reg /AL PMID:21389117 I'm not completely sure if the Slp1-APC degrades mes1 or only ubiquitinates it, but this is most likely correct?... PMID:21389117 fig 1B: 4 nuclei appear later than normal. PMID:21389117 also fzr2 &3 PMID:21389117 fig 1B: 4 nuclei appear later than normal. PMID:21389117 fig 1c, no tetranucleates PMID:21389117 fig 1B: 4 nuclei appear later than normal. PMID:21389117 fig2A PMID:21389117 fig2A PMID:21389117 fig2B PMID:21389117 fig2B PMID:21389117 fig 6C PMID:21389117 fig 7A PMID:21389117 fig 7A PMID:21389117 fig 7A PMID:21389117 fig 7A PMID:21389117 also fzr3 PMID:21389117 fig2A PMID:21389117 fig2B PMID:21429938 cross between h+ and h- deletions, allowed to sporulate immediately PMID:21429938 cross between h+ and h- deletions, allowed to sporulate immediately PMID:21429938 cross between h+ and h- deletions, allowed to sporulate immediately PMID:21429938 cross between h+ and h- deletions, allowed to sporulate immediately PMID:21437270 ch16 PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21441914 no expressivity extension because of decreased growth when untreated PMID:21444751 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 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 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 Rpc2-T455I was clearly more active (white) in yJI1 than in yYH1, consistent with dT(6) readthrough as expected. PMID:21450810 C11-F32S was more active in yJI1 than in yYH1, while wild-type C11 had no effect (Sector 4). PMID:21518960 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 assayed at ars1 and ars2004 (early-firing origins) PMID:21518960 assayed elongation from ars1 and ars2004 (early-firing origins) PMID:21518960 comment assayed at ars1 and ars2004 PMID:21518960 comment assayed at ars1 and ars2004 PMID:21518960 assayed at ars1 and ars2004 (early-firing origins) PMID:21518960 comment assayed at ars1 and ars2004 PMID:21518960 assayed at ars1 and ori1-200 (early-firing origins); only affects origins normally bound by Mrc1 PMID:21518960 assayed elongation from ori1-200 PMID:21536008 "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 figure 7c, no rescue of cnd-2 PMID:21540296 fig 7a PMID:21540296 fig 5c PMID:21540296 fig 7a PMID:21540296 fig 7a PMID:21540296 figure 7c, no rescue of cnd-2 PMID:21540296 fig 1a PMID:21540296 fig 1a PMID:21540296 fig 1a PMID:21540296 t-shift on mitotic entry fig1d PMID:21540296 t-shift on mitotic entry fig1d PMID:21540296 t-shift on mitotic entry fig1c PMID:21540296 t-shift on mitotic entry fig1c PMID:21540296 t-shift on mitotic entry fig1c PMID:21540296 t-shift on mitotic entry fig1c PMID:21540296 t-shift on mitotic entry fig1c PMID:21540296 fig 4 PMID:21540296 fig 7a PMID:21540296 fig 7a PMID:21540296 figure 7e PMID:21540296 fig 7a PMID:21561865 present at basal level; increased in presence of hydroxyurea PMID:21561865 present at basal level; increased in presence of hydroxyurea PMID:21610214 sulphate PMID:21633354 decreased along arms PMID:21633354 condensin, which subunit assayed? PMID:21633354 all tested chromosome loci (Fig. 2g). PMID:21633354 all tested chromosome loci (Fig. 2g). PMID:21633354 H3-pS10 used to detect ark1 activity PMID:21633354 centromeric PMID:21652630 in fig s4b there is septal material hanging around one cell end PMID:21652630 see S5A PMID:21664573 (Figure 1D, Supplemental Figure 2A) PMID:21664573 (Figure 1D, Supplemental Figure 2A) PMID:21664573 (Figure 1D, Supplemental Figure 2A) PMID:21664573 (Figure 1D, Supplemental Figure 2A) PMID:21664573 (Supplemental Figure 2B) PMID:21664573 (Supplemental Figure 2B) PMID:21664573 (Supplemental Figure 2B) PMID:21664573 (Supplemental Figure 2B) PMID:21664573 (Supplemental Figure 2B) PMID:21664573 Figure 5B PMID:21664573 fig 2 b PMID:21664573 fig 2 b c PMID:21664573 ABOLISHED Fig 2 C PMID:21664573 Figure 5B PMID:21664573 Figure 5B PMID:21664573 Figure 5B PMID:21664573 Figure 5B PMID:21664573 (Figure 4E). PMID:21664573 Fig 4d NORMAL SILENCING PMID:21664573 Fig 4d NORMAL SILENCING PMID:21664573 Fig 4c NORMAL SILENCING PMID:21664573 fig 1A PMID:21664573 fig 1A PMID:21664573 fig 1A PMID:21664573 in vitro (Figure 1C & 2D) PMID:21664573 fig 3 b PMID:21664573 fig 3 b PMID:21664573 fig 3 b PMID:21664573 (Figure 4E). PMID:21664573 Figure 5B PMID:21664573 fig 3a. PMID:21664573 fig 3A. bub3 Δklp5 double mutants arrest as inviable micro-colonies of cells PMID:21676862 Fig 1 PMID:21693583 MF? myo1 PMID:21693583 Fig. 8B PMID:21693583 Fig. 8A PMID:21693583 Fig. 8B PMID:2170029 high temp is permissive PMID:2170029 std temp is restrictive PMID:2170029 high temp is permissive PMID:2170029 temperature restrictive for dis2cs alone PMID:2170029 high temp is permissive PMID:2170029 temperature restrictive for dis2cs alone PMID:2170029 temperature restrictive for dis2cs alone PMID:2170029 temperature permissive for dis2cs alone PMID:2170029 temperature restrictive for dis2cs alone PMID:2170029 temperature restrictive for dis2cs alone PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 Requires auto-phosphorylation to be restricted to cell tips (not restricted to cell tips for Pom1-6A and Pom1-KD allele)s PMID:21703453 Requires auto-phosphorylation to be restricted to cell tips (not restricted to cell tips for Pom1-6A and Pom1-KD allele)s PMID:21703453 not restricted to cell tips PMID:21703453 not restricted to cell tips PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 Requires auto-phosphorylation to be restricted to cell tips (not restricted to cell tips for Pom1-6A and Pom1-KD allele)s PMID:21703453 required for detachment from plasma membrane PMID:21703453 required for detachment from plasma membrane PMID:21703453 in tea4-RVXF* background PMID:21703453 This alleles recruits Pom1 to ectopic sites at the lateral plasma membrane PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:21703453 I guess some might be false positives but Sophie said it should be ok. PMID:2172964 both partners cyr1delta PMID:21775631 Figure S2B PMID:21775631 Figure S2A PMID:21775631 Figure S2A PMID:21775631 Figure S2B PMID:21775631 Figure S2B PMID:21775631 Figure S2A PMID:21775631 Figure 1A Figure 5D PMID:21811607 basal transcription is meaningless because emm contains calcium PMID:21813639 candidate for involved_in_or_involved_in_regulation_of qualifier PMID:21828039 homozygous diploid PMID:21832151 endosomal localization requires F-actin (assayed using latrunculin A) PMID:21847092 bound by the C-terminal dsrbd domain PMID:21849474 Fig6C PMID:21849474 Fig 1B PMID:21849474 Fig 1B PMID:21849474 Fig 1B PMID:21849474 Fig 1B PMID:21849474 Fig 1B PMID:21849474 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 Fig9 cdc42-CRIB-GFP localisation is actin dependent and sensitive to low levels (10mM) Lat A PMID:21849474 Fig 1B PMID:21849474 Table 1 not suppressed by sorbitol PMID:21849474 Fig 1A PMID:21849474 Fig4D PMID:21849474 Fig 1B PMID:21849474 Fig 1B PMID:21849474 Table 1 wide phenotype suppressed by sorbitol PMID:21849474 Table 1 not suppressed by sorbitol PMID:21849474 Table 1 not suppressed by sorbitol PMID:21849474 Table 1 not suppressed by sorbitol PMID:21849474 Table 1 not suppressed by sorbitol PMID:21849474 Fig 1A PMID:21849474 Fig 1A PMID:21849474 Fig 1A PMID:21849474 Table 1A PMID:21849474 Fig 1A PMID:21849474 Fig1A Fig2A PMID:21849474 Fig 1A PMID:21849474 Fig 1A Fig2A PMID:21849474 Fig 1A PMID:21849474 Fig 1A PMID:21849474 Fig2B PMID:21849474 Fig 2 C PMID:21849474 Fig 2 C PMID:21849474 Fig 3 increased cell width compared to single mutants PMID:21849474 Fig 3 increased cell width compared to single mutants PMID:21849474 Fig 3 cell width is wider than either of the single mutants PMID:21849474 Fig 3 no increase in cell width compared to single mutants PMID:21849474 Figure 4 A PMID:21849474 Figure 4 A PMID:21849474 Figure 4 A PMID:21849474 Fig4B PMID:21849474 Fig4B PMID:21849474 Fig4B, Fig8 localisation is actin dependent PMID:21849474 Fig4B, Fig8 localisation is actin dependent PMID:21849474 Fig4A PMID:21849474 Fig4C PMID:21849474 Fig4D PMID:21849474 Fig2B PMID:21849474 Fig5 PMID:21849474 Fig5 PMID:21849474 Fig5 PMID:21849474 Fig 6A fusion protein driven from nmt41 promoter PMID:21849474 Fig 6B fusion protein driven from nmt41 promoter PMID:21849474 Fig6C PMID:21849474 Fig 1B PMID:21849474 Fig 1B PMID:21849474 Fig 1B PMID:21849474 Fig7A, B PMID:21849474 Table 1 not suppressed by sorbitol PMID:21849474 Table 1 not suppressed by sorbitol PMID:21849474 Table 1 not suppressed by sorbitol PMID:21849474 Table 1 not suppressed by sorbitol PMID:21849474 Table 1 not suppressed by sorbitol PMID:21885283 Figures 3B PMID:21885283 Figures 1A, 1B and S1B - S1I; TableI PMID:21885283 Figures 1A, 1B and S1B - S1I; TableI PMID:21885283 Figures 1A, 1B and S1B - S1I; TableI PMID:21885283 Figures 1A, 1B and S1B - S1I; TableI PMID:21885283 Figures 1A, 1B and S1B - S1I; TableI PMID:21885283 Figures 1A, 1B and S1B - S1I; TableI PMID:21885283 Figures 1A, 1B and S1B - S1I; TableI PMID:21885283 Figures 1A, 1B and S1B - S1I; TableI PMID:21885283 Figure 3G PMID:21885283 Figures 1A, 1B and S1B - S1I; TableI PMID:21885283 Table I PMID:21885283 Table I PMID:21885283 Figures 1A, 1B and S1B - S1I; TableI PMID:21885283 Figures 1A, 1B and S1B - S1I; TableI PMID:21885283 Figures 1A, 1B and S1B - S1I; TableI PMID:21885283 Figures 1A, 1B and S1B - S1I; TableI PMID:21885283 Figure S1K PMID:21885283 Figure S1K PMID:21885283 Figures 2I – 2K and S3G – S3O) PMID:21885283 Figure 2A PMID:21885283 Table I PMID:21885283 Figures 1A, 1B and S1B - S1I; TableI PMID:21885283 Figure 2A PMID:21885283 Figure 2A PMID:21885283 Table I PMID:21885283 Table I PMID:21885283 Table I PMID:21885283 Figure 3D PMID:21885283 Figure 2A PMID:21885283 TAble II PMID:21885283 TAble II PMID:21885283 TAble II PMID:21885283 Figure 2A PMID:21885283 Figure 3B PMID:21885283 Figure 3B PMID:21885283 Figures 2L, S3P– S3R PMID:21885283 Figure 3C PMID:21885283 Figures 2L, S3P– S3R PMID:21885283 Figures 2I – 2K and S3G – S3O) PMID:21892183 microtubule sliding brake https://www.ebi.ac.uk/interpro/entry/InterPro/IPR007882/#PUB00070924 PMID:21920317 ( Figure 1B) PMID:21920317 Fig 6 PMID:21920317 fig 4B PMID:21920317 fig 4 PMID:21920317 >inc merotelic kinetochore attachment PMID:21920317 Fig 4 B PMID:21920317 Fig 4 A PMID:21920317 fig 1D PMID:21920317 ( Figure S3 A) PMID:21920317 ( Figure 1 A) phase II (metaphase) was substantially extended PMID:21920317 fig 1D PMID:21920317 fig 1D although sister kinetochore split, segregation ends up mostly normal PMID:21920317 fig 1D PMID:21920317 fig 1D PMID:21920317 fig 1D although sister kinetochore sometimes split, segregation ends up mostly normal PMID:21920317 fig 1D PMID:21920317 fig 1D PMID:21920317 fig 1D although sister kinetochore split, segregation ends up mostly normal PMID:21920317 fig 1D PMID:21920317 Figure 1C, 1D bipolar attachment of univalents PMID:21920317 ( 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 ( Figure 1 A) continuous rate of spindle elongation (I) PMID:21920317 prevents bipolar attachment PMID:21920317 prevents bipolar attachment PMID:21920317 prevents bipolar attachment (Ask Takeshi if this fits better rec role) PMID:21931816 Ser-2 of the heptad repeat PMID:21945095 during mitotic DNA replication initiation PMID:21945095 during replication fork processing PMID:21945095 during mitotic DNA replication initiation PMID:21945095 during mitotic DNA replication initiation PMID:21945095 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 during replication fork processing PMID:21945095 during replication fork processing PMID:21945095 during replication fork processing PMID:21945095 also inferred from interaction with Cdc23 and from timing of localization to chromatin at origins PMID:21949882 moved down from GO:0016706 30/8/2014 . activated_by(CHEBI:29033) PMID:21965289 dis2 is required for the retreival of unclustered kinetochores in nsk delete (additive chromosome segregation defects) PMID:21979813 4E decreased kinetochore mono orientation at meiosis I PMID:21979813 2C PMID:21979813 4E decreased kinetochore mono orientation at meiosis I PMID:21979813 4E decreased kinetochore mono orientation at meiosis I PMID:21979813 1B PMID:21979813 2B abolished mono orientation at meiosis I PMID:21979813 2B abolished kinetochore mono orientation at meiosis I PMID:21979813 2C PMID:21979813 2C PMID:21979813 2C PMID:21979813 Fig 4AB PMID:22017871 vw updated PMID:22017871 ubiquitin dependent due to need for rhp6 -AL PMID:22017871 ubiquitin dependent due to need for rhp6 -AL PMID:22017871 ubiquitin dependent due to need for rhp6 -AL PMID:22017871 fig 7c shows direct dna binding PMID:22024164 "30 degrees, ""high"" compared to 25 degrees" PMID:22024164 30 degrees PMID:22024164 actually 25 degrees, but calling it low to make distinction from inviable at 30 PMID:22024164 assayed using ars2004; not abolished as in hsk1delta alone (but single mutant not shown) PMID:22024164 at late-firing or dormant origins; genome-wide detection PMID:22024164 assayed using ars2004; not abolished as in hsk1delta alone (but single mutant not shown) PMID:22024164 30 degrees PMID:22024164 at late-firing or dormant origins; genome-wide detection PMID:22024164 early-firing origins; HU absent PMID:22024164 genome-wide detection PMID:22024164 genome-wide detection PMID:22024167 vw >50% activity PMID:22033972 structure PMID:2203537 Figure 3 A PMID:2203537 Figure 3 A PMID:2203537 Figure 3 A PMID:2203537 85% at 160 min PMID:2203537 30% at 120 min. (archery bow) PMID:22042620 Fig. S5 B PMID:22042620 Fig. 1, A and B; PMID:22042620 Fig. S2, B and C PMID:22042620 Fig. 3 and Fig. S3, for comparative images of an inserted pro-metaphase wild-type SPB, see Fig. S1 B PMID:22042620 not required after insertion PMID:22042620 Fig. S5 B PMID:22042620 fig7 PMID:22042620 Fig. S5 B PMID:22042620 Fig. S5 B PMID:22042620 Fig. S5 B PMID:22042620 Fig. S5 B PMID:22042620 Fig. S5 B PMID:22042620 fig7 PMID:22042620 fig7 PMID:22042620 Fig. 7 indicated by NDB cholesterol PMID:22064476 tested using several genes, and reporter construct to test mutations at or near splice sites PMID:22065639 GO:0000236= mitotic prometaphase PMID:22081013 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 3g PMID:22081013 3f PMID:22081013 3f In marked contrast, subtelomeric tlh transcripts (Figure 3a) accumulated in chp1ΔC strains (Figure 3b,e Supplementary Figure 9). PMID:22081013 In marked contrast, subtelomeric tlh transcripts (Figure 3a) accumulated in chp1ΔC strains (Figure 3b,e Supplementary Figure 9). PMID:22084197 FYPO:0007229 PMID:22085934 (Supplementary Figure S8C PMID:22085934 . 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 In summary, our data show that the Edc3 and Scd6 LSm domains compete for the same Dcp2- binding motifs and that both interactions are mutually exclusive PMID:22085934 (Figure 6A) PMID:22093869 The phenotype is assessed by the high-throughput sequencing. PMID:22093869 The phenotype is assessed by the high-throughput sequencing. PMID:22093869 The phenotype is assessed by the high-throughput sequencing. PMID:22093869 The phenotype is assessed by the high-throughput sequencing. PMID:22119525 fig 2A PMID:22132152 fig 6 PMID:22132152 fig 1, 7 PMID:22132152 fig 2 PMID:22132152 fig 2, 4 PMID:22132152 fig 5 PMID:22132152 fig 5 PMID:22132152 fig 6 PMID:22132152 fig 6 PMID:22132152 fig 8 increased calcinurin activity PMID:22132152 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:22134091 fig2AB PMID:22134091 fig2 PMID:22134091 Fig. S3A PMID:22134091 Fig. PMID:22134091 ig. S1B-j PMID:22134091 fig2B PMID:22134091 fig S2 PMID:22134091 fig 1c PMID:22134091 22.3% PMID:22134091 in vitro PMID:22134091 fig7F PMID:22134091 fig7F PMID:22134091 increased affinity PMID:22134091 in vitro PMID:22134091 in vitro PMID:22134091 fig3 PMID:22134091 fig3 PMID:22134091 in vitro PMID:22140232 same as ssp2delta alone PMID:22140232 (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 (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 ssp2 inferred from mutant phenotype PMID:22140232 same as ssp2delta alone PMID:22140232 same as ssp2delta alone PMID:22140232 same as ssp2delta alone PMID:22140232 same as ssp2delta alone PMID:22140232 same as ssp2delta alone PMID:22140232 same as ssp2delta alone PMID:22140232 same as ssp2delta alone PMID:22140232 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:22144463 during vegetative growth, near genes normally expressed in meiotic cell cycle PMID:22144463 during vegetative growth, near genes normally expressed in meiotic cell cycle PMID:22144463 during vegetative growth, near genes normally expressed in meiotic cell cycle PMID:22144909 (serine 2) PMID:22172946 fig 2 PMID:22172946 fig 1 a PMID:22172946 fig 2 PMID:22172946 fig 1 a PMID:22172946 fig3 PMID:22173095 fig 7 PMID:22173095 fig 7 sdj mutant is unstable PMID:22173095 fig 7 sdj mutant is unstable PMID:22173095 abolished homodimerization Fig. 6, PMID:22180499 floculation inhibited by galactose PMID:22184248 recruitment PMID:22184248 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 As shown in Fig. 3A, ex- pression of Mph1-Ndc80-GFP from pREP81 caused an arrest in the wild-type background. PMID:22184248 As shown in Fig. 3A, ex- pression of Mph1-Ndc80-GFP from pREP81 caused an arrest in the wild-type background. PMID:22184248 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 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 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 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 figure 1a PMID:22184248 figure 1a PMID:22184248 figure 1a PMID:22184248 figure 1a PMID:22184248 fig 1a PMID:22184248 fig 1a PMID:22184248 recruitment (is this the right way around?) PMID:22184248 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:22235339 also assayed using bulk histones from calf thymus PMID:22235339 also assayed using bulk histones from calf thymus PMID:22235339 also assayed using bulk histones from calf thymus PMID:22268381 GFP-Rdp1 was not detected in the nuclei of most cells (Figure 1B). PMID:22268381 GFP-Rdp1 was not detected in the nuclei of most cells (Figure 1B). PMID:22268381 fig 5 PMID:22268381 Moreover, expression of the Rdp1-SV40-NLS construct appeared to suppress centromeric transcript levels below that those found in wild type PMID:22268381 fig 4 PMID:22268381 fig 5 PMID:22268381 fig 5 PMID:22268381 fig 4 PMID:22268381 onsistent with the scenario in which Rdp1 is a cargo for Sal3, we were able to detect stable interaction between tagged Rdp1 and Sal3 by co-immunoprecipitation (Figure 2B). PMID:22268381 Pericentric transcript levels are increased in sal3 mutants PMID:22268381 localization of Dcr1-GFP and GFP-Ago1 was not affected by the loss of Sal3 activity (Figure S1). PMID:22268381 fig 5 PMID:22268381 ocalization of Dcr1-GFP and GFP-Ago1 was not affected by the loss of Sal3 activity (Figure S1). PMID:22279046 same as hsk1-89 alone PMID:22279046 same as hsk1-89 alone PMID:22279046 same as hsk1-89 alone PMID:22279046 same as hsk1-89 alone PMID:22279046 same as hsk1-89 alone PMID:22279046 same as hsk1-89 alone PMID:22279046 same as hsk1-89 alone PMID:22279046 same as hsk1-89 alone PMID:22279046 same as hsk1-89 alone PMID:22291963 mild expressivity PMID:22291963 in asf1-33 at higher temperature PMID:22292001 5 PMID:22292001 "strong contender for GO's ""acts upstream of or within"" (RO:0002264) gp-term relation" PMID:22292001 1d PMID:22292001 during meiosis I PMID:22292001 1a PMID:22292001 1d PMID:22292001 1d PMID:22292001 fig2 PMID:22292001 fig2 PMID:22292001 fig2 PMID:22292001 fig3d PMID:22292001 fig3e PMID:22292001 fig3e PMID:22292001 fig4 PMID:22292001 5 PMID:22292001 5 PMID:22292001 5 PMID:22292001 5c PMID:22292001 5c PMID:22292001 5c PMID:22292001 5c PMID:22292001 5d PMID:22292001 5d PMID:22292001 5d PMID:22292001 5 PMID:22292001 5 PMID:22292001 during meiosis I PMID:22292001 during meiosis I PMID:22292001 "strong contender for GO's ""acts upstream of or within"" (RO:0002264) gp-term relation" PMID:22328580 Figure 4, A and B, PMID:22328580 Figure 4, A and B, PMID:22328580 Figure 4, A and B, PMID:22328580 Figure Figures 5D, 6C PMID:22328580 Fig. 3B Figure 4, A and B, PMID:22328580 Fig. 3B Figure 4, A and B, PMID:22328580 Figure 2D PMID:22328580 fig 4 D PMID:22328580 Figure 4, A and B, PMID:22328580 Figure 4, A and B, PMID:22328580 fig 4 D PMID:22328580 fig 4 D PMID:22328580 Figure Figures 5D, 6C PMID:22328580 fig 1 PMID:22328580 Figure Figures 5D, 6C PMID:22328580 Fig 3A PMID:22328580 Fig 3A PMID:22344254 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 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 Fig. 1B and Fig. 1C, respectively Gtr2, and in particular Gtr1, inhibit sexual differentiation in rich medium. PMID:22344254 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 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 These results suggest that Vam6 functions upstream of Gtr1, possibly by acting as a GEF. PMID:22344254 ********nitrogen replete/with aa PMID:22344254 FM4-64 stained only small vesicles in the cytoplasm of vam6D cells, confirming a defect in vacuolar fusion in these cells. PMID:22344254 FM4-64 stained only small vesicles in the cytoplasm of vam6D cells, confirming a defect in vacuolar fusion in these cells. PMID:22344254 FM4-64 stained only small vesicles in the cytoplasm of vam6D cells, confirming a defect in vacuolar fusion in these cells. PMID:22344254 ***********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 *****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 fig6 PMID:22344254 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 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 Fig. 1B and Fig. 1C, respectively Gtr2, and in particular Gtr1, inhibit sexual differentiation in rich medium. PMID:22344254 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 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 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 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 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 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 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 fig 4a PMID:22344254 fig 4a PMID:22344254 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 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 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:22344694 not shown direct binding but want to capture the fact that it binds the oxidised form PMID:22344694 not shown direct binding but want to capture the fact that it binds the oxidised form PMID:22349564 Northern blots revealed no defect in the accumulation of mature messengers (Figure 5B) PMID:22349564 Figure 1A PMID:22349564 Northern blots revealed no defect in the accumulation of mature messengers (Figure 5B) PMID:22349564 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 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 5E PMID:22349564 Cytb, Cox1, 2 and 3 were clearly visible, although Cox2 was less strongly labeled in both mutants, especially Δmss51 (Figure 5A) PMID:22349564 Δmss51 cells showed normal cytochrome b and c1 peaks, but cytochromes aa3 were not detectable. PMID:22349564 Thus, in S. pombe, Mss51 appears to be required at a post-translational step of complex IV biogenesis PMID:22349564 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 (Figure 4B) A deletion mutants showed a clear growth defect on galactose medium PMID:22349564 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 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 absent respiratory complex III Figure 2D In both Δcbp6 and control Δcytb mitochondria, complex III was completely lacking (lanes 3 and 4) PMID:22349564 Figure 2D In both Δcbp6 and control Δcytb mitochondria, complex III was completely lacking (lanes 3 and 4) PMID:22349564 Figure 2C Thus, virtually all of the Cytb protein synthesized in the Δcbp6 mutant is degraded PMID:22349564 Figure 2A Both the cytb and cox2 mRNAs were present at normal levels in the Δcbp6 mutant PMID:22349564 Figure 2A Both the cytb and cox2 mRNAs were present at normal levels in the Δcbp6 mutant PMID:22349564 Figure 1C PMID:22349564 Figure 1C PMID:22349564 Figure 1C PMID:22349564 Figure S4A, B, C PMID:22349564 Figure 1C PMID:22349564 Figure 1C PMID:22349564 Figure 1C PMID:22349564 Figure 1B PMID:22349564 Figure 1B PMID:22349564 Figure 1A PMID:22349564 As expected, Δppr4 cells clearly lacked Cox1 PMID:22349564 Cytb, Cox1, 2 and 3 were clearly visible, although Cox2 was less strongly labeled in both mutants, especially Δmss51 (Figure 5A) PMID:22349564 Figure 1A PMID:22349564 Figure 1A PMID:22349564 Figure 1A PMID:22349564 Figure 1A PMID:22349564 Cytb, Cox1, 2 and 3 were clearly visible, although Cox2 was less strongly labeled in both mutants, especially Δmss51 (Figure 5A) PMID:22354040 Fig 7 A PMID:22354040 Fig 7 PMID:22354040 Fig 7B PMID:22354040 Fig 7 B PMID:22354040 figure 8 A PMID:22354040 fig 7 c PMID:22375066 ( positive). AMPK is required for proper advance entry into mitosis in nitrogen-starved cells and arrest in G1 before Start. PMID:22375066 ( positive). AMPK is required for proper advance entry into mitosis in nitrogen-starved cells and arrest in G1 before Start. PMID:22375066 ( positive). AMPK is required for proper advance entry into mitosis in nitrogen-starved cells and arrest in G1 before Start. PMID:22375066 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 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 positive PMID:22375066 positive PMID:22375066 ( positive). AMPK is required for proper advance entry into mitosis in nitrogen-starved cells and arrest in G1 before Start. PMID:22375066 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 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 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 "vw deleted ""+ve regulation of""" PMID:22426534 genes in extensions are assayed as represntative of highly transcribed genes PMID:22426534 genes in extensions are assayed as represntative of highly transcribed genes PMID:22426534 genes in extensions are assayed as represntative of highly transcribed genes PMID:22426534 genes in extensions are assayed as represntative of highly transcribed genes PMID:22426534 genes in extensions are assayed as represntative of highly transcribed genes PMID:22431512 localization independent of Ago1 PMID:22431512 SO:0001843 =ATF1/CRE; localization independent of Ago1 PMID:22431512 localization independent of Ago1 PMID:22431512 localization independent of Ago1 PMID:22438582 5 PMID:22438582 6A PMID:22438582 5 PMID:22438582 5A PMID:22438582 5A PMID:22438582 S6 PMID:22438582 S6 PMID:22438582 Figure 1 PMID:22438582 Figure 1 PMID:22438582 Figure 1 PMID:22438582 Figure 1 PMID:22438582 Figure 1 PMID:22438582 FIG 4B PMID:22438582 Figure 1 PMID:22438582 Figure 1 PMID:22438582 Figure 1 PMID:22438582 Figure 1 PMID:22438582 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 5F PMID:22438582 6A PMID:22438582 6A PMID:22438582 5A PMID:22438582 6A PMID:2245912 stf1-1/stf1-2 cells are not as elongated as stf1-1 heterozygous cells at restrictive temperature PMID:2245912 cells homozygous for stf1-1 form small colonies at restrictive temperature ~20-200 cells PMID:2245912 cells homozygous for stf1-1 are not as elongated as stf1-1 heterozygous cells at restrictive temperature PMID:2245912 cells heterozygous for stf1-1 form small colonies at restrictive temperature ~20-200 cells PMID:2245912 cells heterozygous for stf1-1 are more elongated that stf1-1 homozygous cells PMID:2245912 the restrictive temperature for a cdc25-22 diploid is 32°C PMID:2245912 Table 3 suppressor of cdc25-22 PMID:2245912 Table 4 suppressor of cdc25-22 PMID:2245912 Table 4 suppressor of cdc25-22 PMID:2245912 Table 5 This mutant is a revertant of cdc2-M35 PMID:2245912 Table 5 no genetic interaction with stf1-1 PMID:2245912 Table 5 no genetic interaction with stf1-1 PMID:2245912 Table 4 PMID:2245912 same phenotype as cells homozygous for stf1-1 PMID:2245912 same phenotype as cells homozygous for stf1-1 PMID:2245912 Table 4 suppressor of cdc25-22 PMID:2245912 Table 4 suppressor of cdc25-22 PMID:2245912 Table 4 stf1-1 is a suppressor of cdc25-M51 PMID:2245912 Table 4 suppressor of cdc25-disruption occasional cdc- cells observed PMID:2245912 Table 8 no genetic interaction with stf1-1 PMID:2245912 Table 8 no genetic interaction with stf1-1 PMID:2245912 Table 5 PMID:2245912 Table 5 cdc2-1w rescues cdc25-22 but cells are long PMID:2245912 Table 5 cdc2-1w and stf1-1 have additive effect on cdc25-22 cell size at restrictive temperature PMID:2245912 dis2+ over expression reverses the stf1-1 suppression cdc25-22 PMID:2245912 Table 7 Cells are slightly shorter at high temperature when stf1-1 present PMID:2245912 Table 7 Cells are slightly shorter at high temperature when stf1-1 present PMID:2245912 Table 6 PMID:2245912 Table 6 wee1-50 and stf1-1 have an additive effect to suppress cdc25-22 phenotype at the restrictive temperature PMID:2245912 Table 5 cdc2-3w and stf1-1 have additive effect on cdc25-22 cell size at restrictive temperature PMID:2245912 Table 5 no genetic interaction with stf1-1 PMID:2245912 Table 5 no genetic interaction with stf1-1 PMID:2245912 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 Table 5 This mutant is a revertant of cdc2-M35 PMID:2245912 Table 5 no genetic interaction with stf1-1. PMID:2245912 Table 5 no genetic interaction with stf1-1 PMID:2245912 Table 5 no genetic interaction with stf1-1 PMID:2245912 Table 5 no genetic interaction with stf1-1 PMID:2245912 Table 4 PMID:2245912 stf1-1/stf1-3 cells are not as elongated as stf1-1 heterozygous cells at restrictive temperature PMID:2245912 Table 4 suppressor of cdc25-disruption occasional cdc- cells observed PMID:2245912 Table 4 stf1-1 is a suppressor of cdc25-M51 PMID:2245912 stf1-1/stf1-3 cells form small colonies at restrictive temperature ~20-200 cells PMID:22484924 fig 2c PMID:22484924 fig4 (I moved this down from abnormal endocytisis, is that OK?) PMID:22484924 fig 4 PMID:22484924 vw, moved down to -decreased protein targeting to vacuole, with protein secreted PMID:22484924 fig 5c PMID:22484924 (protein) PMID:22484924 Fig. 2D PMID:22484924 fig 2d PMID:22496451 "allele tyep ""unknown"" because neither nt nor aa position 324 is A" PMID:22508988 fig 4 A/B PMID:22508988 fig 1a PMID:22508988 fig1 PMID:22508988 fig1 carboxy terminal region PMID:22508988 fig 1a PMID:22508988 fig 1a in vitro /in vivo PMID:22508988 fig1 carboxy terminal region PMID:22508988 fig 1a PMID:22508988 fig 1e in vitro PMID:22508988 (We also compared the activities of kinase complexes generated by translation in vitro toward Spt5. By this measurement also, Cdk9 and Cdk9C were stimulated to similar extents by Csk1 (Fig. 1F),(is this an physiological substrate?) PMID:22508988 fig 2b PMID:22508988 fig 2c PMID:22508988 fig 2c PMID:22508988 fig 2c PMID:22508988 fig 2c PMID:22508988 fig 2c PMID:22508988 fig 2c PMID:22508988 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 fig 2c PMID:22508988 fig 2c PMID:22508988 fig 2d Spt5-T1P (CTD repeat 1 residue) PMID:22508988 fig 2d Spt5-T1P (CTD repeat 1 residue) PMID:22508988 fig 3B PMID:22508988 fig 3B PMID:22508988 carboxy terminal region PMID:22508988 fig 4 A/B PMID:22558440 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 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 fig 2a PMID:22573890 figure 2 B/C PMID:22573890 fig 2a (WT 10% @36degrees) PMID:22573890 fig 3 A PMID:22573890 fig 3 A PMID:22573890 fig S2 PMID:22573890 fig 6 PMID:22573890 fig 6 PMID:22573890 fig 5 6 min late PMID:22573890 fig 5 PMID:22573890 fig 5 PMID:22573890 fig 5 PMID:22573890 fig 3 A PMID:22582262 "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 "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 TOR kinase activity was measured using immunoprecipitated proteins (Fig.2) PMID:22645648 """At 37C, the cell number increase of both mutants ceased.""" PMID:22645648 """At 37C, the cell number increase of both mutants ceased.""" PMID:22645648 Figure 6 PMID:22645648 Figure1a PMID:22645648 Figure4d PMID:22645648 Figure1a/6a . Rapamycin rescued cut1-21 and cut1-693 at 338C PMID:22645648 Figure1a PMID:22645648 Figure1a PMID:22645648 Figure 6 PMID:22645648 Figure6 PMID:22645648 Figure1a/6a . Rapamycin rescued cut1-21 and cut1-693 at 338C PMID:22645648 Dephosphorylation of Cdc2 Tyr15 PO4 is delayed in this mutant PMID:22645648 Figure4d PMID:22645648 Figure4ab PMID:22645648 Figure4e PMID:22645648 Mild sensitivity compared to tor2-S (L2048S) PMID:22645654 Fig1d PMID:22645654 Fig.1d, e, f PMID:22645654 Fig1d PMID:22645654 Fig1d PMID:22645654 Fig1h PMID:22645654 Fig1d PMID:22645654 Fig2e PMID:22645654 Fig2e PMID:22645654 Fig3a-g (evidence: immunpflouresence) PMID:22645654 Fig4 PMID:22645654 Fig5 PMID:22645654 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 Fig5 PMID:22645654 Fig7 PMID:22645654 fig 2b,c PMID:22645654 fig 2b,c PMID:22645654 Fig1g PMID:22645654 Fig1f (evidence:immunoblot using anti-thymine dimer anitbodies) PMID:22658721 bulky PMID:22658721 NMeed to check, its decreased duration of replication arrest? PMID:22658721 small PMID:22661707 more specific term required, during GO:0034599) PMID:22665807 1d PMID:22665807 Table S1 and Figure S1 PMID:22665807 Table S1 and Figure S1 PMID:22665807 Table S1 and Figure S1 PMID:22665807 Table S1 and Figure S1 PMID:22665807 Table S1 and Figure S1 PMID:22665807 Table S1 and Figure S1 PMID:22665807 Table S1 and Figure S1 PMID:22665807 Table S1 and Figure S1 PMID:22665807 Table S1 and Figure S1 PMID:22665807 Table S1 and Figure S1 PMID:22665807 Table S1 and Figure S1 PMID:22665807 1c PMID:22665807 1d PMID:22665807 2A PMID:22665807 figure 2A PMID:22665807 2A PMID:22665807 2A PMID:22665807 2A PMID:22665807 2A PMID:22665807 2A PMID:22665807 2A PMID:22665807 3a PMID:22665807 3b PMID:22665807 4b PMID:22665807 4b PMID:22665807 4b PMID:22665807 4b PMID:22665807 4b PMID:22665807 4b PMID:22665807 4b PMID:22665807 4b PMID:22665807 4b PMID:22665807 4b PMID:22682245 cleaves unpaired nascent DNA in replication forks (vw replaced GO:0045145) PMID:22682245 implies that dna2 E560A alone is inviable PMID:22682245 implies that dna2 K961T alone is viable PMID:22683269 assayed using bulk RNA PMID:22684255 Figure 2f lanes 1, 2 PMID:22684255 Figure 2f lanes 1, 2 PMID:22684255 Figure 3a PMID:22684255 Figure 3a PMID:22684255 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 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 Figure 2f lanes 1, 2 PMID:22684255 Figure 1g PMID:22684255 Figure 1g PMID:22684255 """mitotic commitment'" PMID:22684255 (Figure 4b) confirming that each kinase promotes mitotic commitment. PMID:22684255 fig 4d PMID:22684255 fig 4d PMID:22684255 Figure 1b PMID:22684255 Figure 1b PMID:22684255 fig 4d PMID:22684255 fig 4d PMID:22684255 fig 4d PMID:22684255 fig 4d PMID:22684255 fig 1a PMID:22684255 upstream of pom1 PMID:22684255 fig 4d PMID:22684255 fig 4d PMID:22684255 fig 4d PMID:22684255 fig 4d PMID:22684255 fig 4d PMID:22696680 Figure 2D Figure 2F PMID:22696680 Supplemental Figure S1, C–E PMID:22696680 Supplemental Figure S1, C–E PMID:22696680 Figure 3, Supplemental Table S2, and Supplemental Figure S4 PMID:22696680 Figure 2D Figure 2F PMID:22696680 Figure 2C PMID:22696680 Figure 2B PMID:22696680 Figure 2A PMID:22696680 Figure 2A PMID:22696680 Figure 1 PMID:22696680 Figure 1 PMID:22696680 Figure 1 PMID:22696680 Figure 1 PMID:22696680 (growing) fig 1A PMID:22696680 fig 1A PMID:22696680 fig 1A PMID:22696680 Supplemental Figure S1, C–E PMID:22705791 not sure if it is endo, exo, or both. It is def acting on DNA. More specific terms for DNA specify endo or exo. PMID:22705791 not sure if it is endo, exo or both? so went with more general term PMID:22711988 kinetochore localization requires MIND complex PMID:22711988 implies that MIND complex is required for Sos7 to localize to the kinetochore PMID:22718908 inferred from localization of proteins distal to origin PMID:22718908 BrdU incorporation PMID:22718908 BrdU incorporation PMID:22718908 BrdU incorporation PMID:22718908 inferred from localization of proteins distal to origin PMID:22718908 inferred from normal localization of CMG proteins at origin PMID:22718908 BrdU incorporation PMID:22718908 inferred from localization of proteins distal to origin PMID:22718908 inferred from localization of proteins distal to origin PMID:22723423 Fml1 catalyses the dissociation of displacement (D) loops PMID:22723423 Fml1 binds to the four-way junction at a displacement (D) loop. PMID:22727667 binds H3K9me PMID:22727667 binds H3K9me PMID:22727667 binds H3K9me PMID:22737087 Fig2. decreased aneuploid cell viability during vegetative growth PMID:22737087 Fig6 PMID:22737087 Fig6. PMID:22737087 Fig6. PMID:22737087 Table 2 This strain is disomic for Chromosome 3 PMID:22737087 All the genes affect by at least 1.5 fold (17) are reported in Table S2 PMID:22737087 All the genes affect by at least 1.5 fold (61) are reported in Table S2 PMID:22737087 All the genes affect by at least 1.5 fold (141) are reported in Table S2 PMID:22737087 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 Table 2 This strain is disomic for Chromosome 3 PMID:22737087 Fig 3B This strain is disomic for Chromosome 3 PMID:22737087 Fig 3A This strain is disomic for Chromosome 3 PMID:22737087 Fig 3B This strain is disomic for Chromosome 3 PMID:22737087 Fig 3A This strain is disomic for Chromosome 3 PMID:22737087 Table1 Fig1 affects C1 and C2 type colonies PMID:22737087 Fig2. reduced growth may not be specific to aneuploidy as it also interact with gtb1 though looks quite good to me PMID:22737087 Fig2. reduced growth may not be specific to aneuploidy as it also interacts with gtb1 PMID:22737087 Fig2 normal population growth in presence of aneuploid cells PMID:22737087 Fig2 normal population growth in presence of aneuploid cells PMID:22737087 data not shown PMID:22737087 data not shown PMID:22737087 data not shown PMID:22737087 data not shown PMID:22737087 Fig2. decreased aneuploid cell viability during vegetative growth PMID:22737087 Fig1, Table1 affects C1 and C2 type colonies PMID:22737087 Fig2. PMID:22737087 Fig2. PMID:22737087 Fig2. decreased aneuploid cell viability during vegetative growth PMID:22737087 Fig S1, decreased aneuploid cell viability during vegetative growth PMID:22737087 Fig S1, decreased aneuploid cell viability during vegetative growth PMID:22737087 data not shown decreased aneuploid cell viability during vegetative growth PMID:22737087 Fig S1 decreased aneuploid cell viability during vegetative growth PMID:22737087 Fig2. PMID:22737087 Fig1, Table1 affects C1 more than C2 type colonies PMID:22737087 Fig6 PMID:22737087 Fig6 PMID:22737087 Fig6. reduced growth may not be specific to aneuploidy as it also interacts with gtb1-93 PMID:22737087 Fig1, Table1 affects C1 and C2 type colonies PMID:22737087 Fig1, Table1 affects C1 type colonies PMID:22737087 Fig1, Table1 affects C1 type colonies PMID:22737087 Table 2 This strain is disomic for Chromosome 3 PMID:22737087 Table 2 This strain is disomic for Chromosome 3 PMID:22768388 fig 1 A PMID:22768388 fig 4C PMID:22768388 data not shown PMID:22768388 figure 1c PMID:22768388 Figur 1 c PMID:22768388 S1 E PMID:22768388 Figur 1 c PMID:22768388 figure 1c PMID:22768388 fig S4 PMID:22768388 fig 1 A PMID:22768388 fig 1 A PMID:22768388 figure 1c PMID:22768388 S1 E PMID:22768388 S1 E PMID:22768388 S1 E PMID:22768388 S1 E PMID:22768388 S1 E PMID:22768388 S1 E PMID:22768388 S1 E PMID:22768388 fig 1 A PMID:22768388 fig 1 A PMID:22768388 Figures S1C and S1D PMID:22768388 Figures S1C PMID:22768388 Figures 1B PMID:22768388 Figures 1B PMID:22768388 Figures 1B PMID:22768388 Figures 1B PMID:22768388 Figur 1 c PMID:22768388 data not shown PMID:22792081 This interaction depends on the phosphorylation of Crb2 on the T73 and S80 residues. PMID:22792081 cdc25-22 background PMID:22792081 cdc25-22 background PMID:22792081 This interaction depends on the phosphorylation of Crb2 on the T73 and S80 residues. PMID:22792081 cdc25-22 background PMID:22792081 This interaction depends on the phosphorylation of Crb2 on the T73 and S80 residues. PMID:22792081 cdc25-22 background PMID:22792081 cdc25-22 background PMID:22792081 cdc25-22 background PMID:22809626 "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 "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 "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 "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 35% cells (Fig. 1E,F). PMID:22825872 Fig. 4A and S8 PMID:22825872 Fig. 4A and S7 PMID:22825872 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 Fig. 4A and S8 PMID:22825872 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 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 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 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 Together this suggests that Ark1 is directly and continuously required to maintain Mph1 localization to kinetochores. PMID:22825872 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 (Fig. S9F) PMID:22825872 (Fig. 3C) (inhibiting Ark1 does not rescue the Mph1-kinetochore targeting, arguing that Ark1 is upstream) PMID:22825872 (Fig. 3C)increased mitotic index (Fig. S4A) PMID:22825872 (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 This is S4B and C PMID:22825872 This is S4B and C PMID:22825872 This is S4B and C PMID:22825872 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 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 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 Fig. 4C PMID:22825872 (Fig. 4B). PMID:22825872 Fig. S8 PMID:22825872 Fig. S7 PMID:22825872 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 Fig. S5 PMID:22825872 Fig. 4A and S9 PMID:22825872 Fig. 4A and S1 PMID:22825872 Fig. 4B Fig. S5 PMID:22825872 Mph1 localizes to unattached kinetochores in bub3D cells (Fig. 2A). PMID:22825872 Fig. 4A and S7 PMID:22825872 (Fig. 4C). PMID:22825872 The shorter truncation (Mph1-D1-150) maintained kinetochore localization and SAC signaling, PMID:22825872 The shorter truncation (Mph1-D1-150) maintained kinetochore localization and SAC signaling, PMID:22825872 ditto PMID:22825872 abolished both kinetochore localization and SAC signaling (Fig. 1C,D), suggesting that kinetochore localization is crucial for SAC activity. PMID:22891259 fig1 /figs1? PMID:22891259 fig1 /figs1? PMID:22891259 Localized at cell tips, actomyosin contractile ring and septum PMID:22891259 Explosive cell separation due to a weak primary septum. Absence of a secondary septum. PMID:22891673 decreased septum closure PMID:22891673 septation index constantly high PMID:22891673 septation index increased gradually over time PMID:22891673 Assayed by FM4-64 uptake PMID:22891673 At the end of ring constriction Filamentous projections from the unclosed ring toward the cytoplasm PMID:22891673 normal localization in several mutants indicates that Sec3 localization is independent of exocytosis and vesicle-mediated transport along microtubules PMID:22891673 decreased/delayed septum closure PMID:22891673 assayed at 32C, which is semi-permissive for sec3-913 PMID:22891673 Weak actin cables PMID:22905165 S1 PMID:22905165 S1 PMID:22905165 Cdc15-GFP PMID:22905165 Cdc15-GFP supplemental figure S3 PMID:22905165 S1 PMID:22905165 GFP-Bgs1 PMID:22905165 (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 GFP-Bgs1 PMID:22905165 figure S2, A protein distributed in cortex PMID:22905165 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 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 1B PMID:22905165 Cdc15-GFP However, we observed that a number of the Cdc15-GFP and the GFP-Cdc4 rings were asymmetric or broken. PMID:22905165 GFP-Cfh3 figure 1 A PMID:22905165 GFP-Cfh3 figure 1 A PMID:22905165 S1 PMID:22912768 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05) PMID:22912768 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05) PMID:22912768 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05) PMID:22912768 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05) PMID:22912768 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05) PMID:22912768 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05) PMID:22912768 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05) PMID:22918943 Figure 5, I, J, and L PMID:22918943 Figure 7 PMID:22918943 Figure 7 PMID:22918943 Figure 3A PMID:22918943 Figure 3A PMID:22918943 Figure 5, I, J, and L PMID:22918943 Figure 5, I, J, and L PMID:22918943 Figure 1A, 2A PMID:22918943 Figure 1A, 2A PMID:22918952 unspecfied RxxS site(s) PMID:22918952 unspecfied RxxS site(s) PMID:22918954 fig 3B PMID:22918954 Figure 4 PMID:22918954 Figure 4 PMID:22918954 Figure 4 PMID:22918954 Figure 4 PMID:22918954 Figure 4 PMID:22918954 Figure 4 PMID:22918954 Figure 4 PMID:22918954 fig 3B PMID:22918954 fig 3B PMID:22918954 fig 3B asymettrically localized septum PMID:22918954 fig 3B PMID:22918954 fig 3B PMID:22918954 fig 3B PMID:22918954 fig 3B PMID:22918954 fig 3B PMID:22918954 fig 3B PMID:22959349 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 at Ser/Thr-Pro site PMID:22959349 at Ser/Thr-Pro site PMID:22959349 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 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 at Ser/Thr-Pro site PMID:22959349 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 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 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 in vitro assay using rps602 so I am inferring rps601 PMID:22976295 in vitro assay using rps602 so I am inferring rps601 PMID:22976295 "I guess everything in the signaling cascade that isn't the ""final effector"" is part of the signaling cascade?" PMID:22976295 "I guess everything in the signaling cascade that isn't the ""final effector"" is part of the signaling cascade?" PMID:22976295 both rps proteins in extension because blot is for both of them PMID:22976295 both rps proteins in extension because blot is for both of them PMID:22976295 both rps proteins in extension because blot is for both of them PMID:22976295 both rps proteins in extension because blot is for both of them PMID:22976295 both rps proteins in extension because blot is for both of them PMID:22976295 both rps proteins in extension because blot is for both of them PMID:22976295 both rps proteins in extension because blot is for both of them PMID:22976295 both rps proteins in extension because blot is for both of them PMID:22976295 both rps proteins in extension because blot is for both of them PMID:22976295 both rps proteins in extension because blot is for both of them PMID:22976295 not shown PMID:22976295 in vitro assay using rps602 so I am inferring rps601 PMID:22976295 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 both rps proteins in extension because blot is for both of them PMID:22976295 both rps proteins in extension because blot is for both of them PMID:22976295 both rps proteins in extension because blot is for both of them PMID:22976295 both rps proteins in extension because blot is for both of them PMID:22976295 both rps proteins in extension because blot is for both of them PMID:22976295 blotted for rps601 & rps602 simultaneously PMID:22976295 blotted for rps601 & rps602 simultaneously PMID:22976295 blotted for rps601 & rps602 simultaneously PMID:22976295 blotted for rps601 & rps602 simultaneously PMID:22976295 blotted for rps601 & rps602 simultaneously PMID:22976295 blotted for rps601 & rps602 simultaneously PMID:22987637 "for evidence, ""BrdU incorporation assay evidence used in manual assertion"" (ECO:0001155) would be applicable." PMID:22987637 "for evidence, ""BrdU incorporation assay evidence used in manual assertion"" (ECO:0001155) would be applicable." PMID:22988247 This gene has been named as otg2 in the article. PMID:22988247 This gene has been named as otg3 in the article. PMID:22988247 This gene has been named as otg1 in the article. PMID:22990236 SO:0001899 = dh repeat PMID:23028377 move down to histone chaperone (H3-?) PMID:23032292 spacing is wrong as well as occupancy PMID:23051734 localization PMID:23051734 required for wildtype rates of actin cable retrograde flow in myo52∆ cells PMID:23066505 RIDD? - there is no RIDD term in GO, Val wants to wait with this PMID:23066505 ire1 breaks down mRNAs during ER stress, however bip1 is unusual in that ire1 cleavage stabilizes it PMID:23071723 throughout cell cycle, with peak at M/G1 PMID:23084836 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 (Figures S2A and S2B) PMID:23084836 (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 As previously shown, telomere tethering was significantly compromised in rap1Δ and bqt4Δ cells (Figure S2C; Chikashige et al., 2009). PMID:23084836 As previously shown, telomere tethering was significantly compromised in rap1Δ and bqt4Δ cells (Figure S2C; Chikashige et al., 2009). PMID:23084836 Interestingly, Tf clustering was impaired by pku70Δ and pku80Δ at a level similar to that observed in abp1Δ cells (Figure 2A). PMID:23084836 Interestingly, Tf clustering was impaired by pku70Δ and pku80Δ at a level similar to that observed in abp1Δ cells (Figure 2A). PMID:23084836 Interestingly, Tf clustering was impaired by pku70Δ and pku80Δ at a level similar to that observed in abp1Δ cells (Figure 2A). PMID:23084836 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 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 (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 (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 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 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 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 Figures 6A and 6B), see above PMID:23084836 Figures 6A and 6B) see above PMID:23084836 Figures 6A and 6B) see above PMID:23084836 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 Figure 6E). H3K56 acetylation antagonizes Tf clustering at centromeres. binding of Ku was reduced and enhanced in hst4Δ and rtt109Δ cells, respectively, PMID:23084836 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 Figure 6E). H3K56 acetylation antagonizes Tf clustering at centromeres. binding of Ku was reduced and enhanced in hst4Δ and rtt109Δ cells, respectively PMID:23084836 Figure 6E). H3K56 acetylation antagonizes Tf clustering at centromeres. binding of Ku was reduced and enhanced in hst4Δ and rtt109Δ cells, respectively PMID:23084836 We observed that Ku localization was diffuse after DNA damage, but this diffusion was inhibited by rtt109Δ (Figure 7D) PMID:23084836 Figures 6A and 6B) see above PMID:23084836 1A PMID:23084836 1A PMID:23084836 1A PMID:23084836 Figure S1C PMID:23084836 Figure S1C PMID:23087209 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 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 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 assayed in strain with RTS1 replication fork barrier inserted near ori3006/7 PMID:23093942 assayed in strain with RTS1 replication fork barrier inserted near ori3006/7 PMID:23093942 assayed by PCR in strain with RTS1 replication fork barrier inserted near ori3006/7 PMID:23093942 assayed by PCR in strain with RTS1 replication fork barrier inserted near ori3006/7 PMID:23093942 assayed by PCR in strain with RTS1 replication fork barrier inserted near ori3006/7 PMID:23093943 Cells lacking Fic1 or its interacting partners Cyk3 or Imp2 were significantly more invasive than wild-type cells (Figure 9A–9B). PMID:23093943 Figure S5B PMID:23093943 Figure S5B PMID:23093943 fig 1b PMID:23093943 fig 1b fig2 PMID:23093943 fiigure S1B–S1C PMID:23093943 fiigure S1B–S1C PMID:23093943 fiigure S1B–S1C PMID:23093943 Figure 1F–1G PMID:23093943 S1F PMID:23093943 S1F PMID:23093943 S1F PMID:23093943 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 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 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 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 fig S3F PMID:23093943 fig 4c PMID:23093943 fig 4c PMID:23093943 fig 4c PMID:23093943 Figure 4A–4C and Figure S3A–S3B PMID:23093943 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 Figure 4A–4C and Figure S3A–S3B PMID:23093943 Figure 3G PMID:23093943 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 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 fig 3c PMID:23093943 fig 3C PMID:23093943 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 fig 4c/ figure 6a PMID:23093943 Loss of Eng1 or its cooperating glucanase, Agn1 [34], resulted in high percentages of monopolar growth (Figure 6C–6D and Figure S5A) PMID:23093943 Loss of Eng1 or its cooperating glucanase, Agn1 [34], resulted in high percentages of monopolar growth (Figure 6C–6D and Figure S5A) PMID:23093943 fFigure 3D–3F PMID:23093943 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 Cells lacking Fic1 or its interacting partners Cyk3 or Imp2 were significantly more invasive than wild-type cells (Figure 9A–9B). PMID:23093943 Cells lacking Fic1 or its interacting partners Cyk3 or Imp2 were significantly more invasive than wild-type cells (Figure 9A–9B). PMID:23112169 binds O6-alkylguanine, 2-aminopurine and 2,6-diaminopurine PMID:23115244 evidence=mas spec, can I wang this into another evidence code or should we add it (or something similar?) PMID:23133674 Y2H fig 1 PMID:23133674 fig1 Y2H PMID:23133674 bqt1 is fused to the activation domain PMID:23133674 fig1 only bqt1 is fused to the activation domain (that's why I am not adding this function to bqt2) PMID:23133674 fig1 Y2H PMID:23166349 Coimmunoprecipitation, yeast-two-hybrid PMID:23166349 Further supported by PMID:25057016 PMID:23188080 affects intermolecular, but not intramolecular, end joining PMID:23188080 affects intermolecular, but not intramolecular, end joining PMID:23188080 affects intermolecular, but not intramolecular, end joining PMID:23188080 affects intermolecular, but not intramolecular, end joining PMID:23188080 affects intermolecular, but not intramolecular, end joining PMID:23188080 affects intermolecular, but not intramolecular, end joining PMID:23188080 affects intermolecular, but not intramolecular, end joining PMID:23200991 inferred from localization plus GTPase activity PMID:23200991 Observed with probe for active Cdc42 (CRIB) PMID:23200991 Observed with probe for active Cdc42 (CRIB) PMID:2320127 Fig1c Serine is the major phosphoamino acid PMID:2320127 Fig4a. Cells blocked in G2 PMID:2320127 Fig4a. Cells blocked in mitosis PMID:2320127 Fig1c threonine is the minor phosphoamino acid PMID:23209828 MBC resistance phenotype and pap1 ubiquitylation phenotype PMID:23209828 MBC sensitivity phenotype and ubiquitylation and degradation phenotype PMID:23209828 MBC resistance phenotype and pap1 ubiquitylation phenotype PMID:23209828 MBC sensitivity phenotype and ubiquitylation and degradation phenotype PMID:23209828 Pap1 is ubiquitylated by Rhp6 and Ubr1 PMID:23209828 Pap1 is ubiquitylated by Rhp6 and Ubr1 PMID:23211746 same as rad2delta alone PMID:23211746 same as rad2delta alone PMID:23211746 same as chk1delta alone PMID:23211746 same as chk1delta alone PMID:23211746 gel electrophoresis + southern blot PMID:23211746 same as exo1delta alone PMID:23211746 same as exo1delta alone PMID:23223230 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 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 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 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 Taken together, the Northern and array analyses indicate that adh1AS transcripts preferentially accumulate in zinc-limited cells, whereas adh1 mRNAs accumulate in zinc-replete cells. PMID:23223230 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 However, the larger band preferentially accumulated under zinc-replete conditions in wild-type cells and constitutively accumulated in SPCC13B11.02c cells. Thus, changes in adh1AS levels influence the levels of Adh1 protein, suggesting that this mechanism may exist to conserve zinc. PMID:23231582 at pho1+ and SPBC1271.09 PMID:23231582 represses Pho7-mediated transcription activationin phosphate-replete conditions; does not regulate Pho7 DNA binding PMID:23231582 also inferred from chromatin localization and reporter gene expression PMID:23236291 Figure 3 (PMID: 23236291) PMID:23236291 Figure 7A (PMID:23236291) PMID:23236291 Figure 7A (PMID:23236291) PMID:23236291 Figure 8D (PMID: 23236291) PMID:23236291 Figure 8D (PMID: 23236291) PMID:23236291 Requested new term from Sequence Ontology: CArG-box PMID:23236291 Figure 8D (PMID: 23236291) PMID:23236291 Figure 3 (PMID: 23236291) PMID:23236291 Figure 3 (PMID: 23236291) PMID:23236291 Figure 3 (PMID: 23236291) PMID:23236291 Figure 3 (PMID: 23236291) PMID:23236291 Figure 3 (PMID: 23236291) PMID:23236291 Figure 3 (PMID: 23236291) PMID:23236291 Figure 3 (PMID: 23236291) PMID:23236291 Figure 8D (PMID: 23236291) PMID:23236291 Figure 8D (PMID: 23236291) PMID:23236291 Figure 8D (PMID: 23236291) PMID:23236291 Figure 8D (PMID: 23236291) PMID:23236291 Figure 8B (PMID: 23236291) PMID:23236291 Figure 8A (PMID: 23236291) PMID:23236291 Figure 8B (PMID:23236291) PMID:23236291 Figure 8B (PMID:23236291) PMID:23236291 Figure 8E (PMID:23236291) PMID:23236291 Figure 8E (PMID:23236291) PMID:23236291 Figure 6A and 6C (PMID:23236291) PMID:23236291 Figure 1A and 1B (PMID: 23236291) PMID:23236291 Figure 1A (PMID: 23236291) PMID:23236291 Figure 1B (PMID: 23236291) PMID:23236291 Figure 6A (PMID:23236291) PMID:23245849 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 fig 1D PMID:23245849 fig 1D PMID:23245849 fig 1D PMID:23245849 multiple experiments PMID:23245849 Mag2 binds stronger to the abasic oligonucleotide than to non-damaged DNA (Figure 2), with a dissociation rate constant more than 15 times higher for non-damaged DNA (kd 26 × 10−3 s −1) as compared to DNA containing the AP site analogue tetrahydrofuran (THF) (kd 1.6 × 10−3 s−1). Mag2 injected on sensor chips coated with oligonucleotides containing a single ethenoadenine or 8-oxoguanine lesion showed the same resonance levels as non-damaged DNA (data not shown), demonstrating that Mag2 preferentially binds to AP sites in DNA. PMID:23245849 Figure 1C PMID:23245849 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:23254763 FIgure 2. +25 μg/ml Hyg.B PMID:23254763 complemented by S. cerevisiae GAL2 PMID:23254763 FIgure 2. +25 μg/ml Hyg.B PMID:23254763 FIgure 2 PMID:23254763 FIgure 2 PMID:23254763 FIgure 2 PMID:23254763 FIgure 2 PMID:23254763 FIgure 2 PMID:23254763 FIgure 2 PMID:23254763 FIgure 2 PMID:23254763 FIgure 2 PMID:23254763 FIgure 2. PMID:23254763 FIgure 2. PMID:23254763 FIgure 2. PMID:23254763 FIgure 2. PMID:23254763 FIgure 2. PMID:23254763 FIgure 2. PMID:23254763 FIgure 2. PMID:23254763 FIgure 2. PMID:23254763 FIgure 2. PMID:23254763 FIgure 2. +25 μg/ml Hyg.B PMID:23254763 FIgure 2. +25 μg/ml Hyg.B PMID:23254763 FIgure 2. +25 μg/ml Hyg.B PMID:23254763 FIgure 2. +25 μg/ml Hyg.B PMID:23254763 FIgure 2. +25 μg/ml Hyg.B PMID:23254763 FIgure 2. +25 μg/ml Hyg.B PMID:23254763 FIgure 2. +25 μg/ml Hyg.B PMID:23254763 FIgure 2. +25 μg/ml Hyg.B PMID:23254763 Fig 3. galactose-specific HRP-PNA staining was used to detect quantitative differences in the galactosyla- tion of cell-surface proteins PMID:23254763 Fig 3. galactose-specific HRP-PNA staining was used to detect quantitative differences in the galactosyla- tion of cell-surface proteins PMID:23254763 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 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 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:23260662 inferred directness from effects of different alleles and of mutations elsewhere (swi1delta, clr4delta, or mat1-SS2) PMID:23260662 same as lsd1-E918 single mutant PMID:23260662 same as lsd1-E918 single mutant PMID:23260662 same as lsd1-E918 single mutant PMID:23260662 same as lsd1-E918 single mutant PMID:23260662 inferred indirectness from author description and different effect of swi1delta PMID:23260662 inferred directness from effects of different alleles and of mutations elsewhere (swi1delta, clr4delta, or mat1-SS2) PMID:23273506 Figures 4B and 4C: Asp56Ser mutation endows Mag2 with the ability to excise εA at levels similar to Mag1. PMID:23297348 Sal3 is required for the nuclear import of Clp1 as shown by microscopy. PMID:23297348 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 S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 Phosphorylation site S265 was identified by mass spectrometry. PMID:23297348 S332, S700, and S732 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S332, S700, and S732 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S332, S700, and S732 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 T123 and S334 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 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 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 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 S267 was identified as phosphorylation sites by mass spectrometry. PMID:23297348 S321 was identified as phosphorylation sites by mass spectrometry. PMID:23297348 T297 and S364 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S303 was identified as phosphorylation sites by mass spectrometry. PMID:23297348 S57 and S206 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S57 and S206 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S183 and S372 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S183 and S372 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S674 was identified as phosphorylation sites by mass spectrometry. PMID:23297348 S502 was identified as phosphorylation sites by mass spectrometry. PMID:23297348 S196 and S252 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S196 and S252 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S345 was identified as phosphorylation sites by mass spectrometry. PMID:23297348 S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S411 was identified as phosphorylation sites by mass spectrometry. PMID:23297348 T554 was identified as phosphorylation sites by mass spectrometry. PMID:23297348 S372 was identified as phosphorylation sites by mass spectrometry. PMID:23297348 S436 was identified as phosphorylation sites by mass spectrometry. PMID:23297348 S220 was identified as phosphorylation sites by mass spectrometry. PMID:23297348 T106 was identified as phosphorylation sites by mass spectrometry. PMID:23297348 S148 was identified as phosphorylation sites by mass spectrometry. PMID:23297348 S65 was identified as phosphorylation sites by mass spectrometry. PMID:23297348 S216 and S298 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S216 and S298 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S301 and S499 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S301 and S499 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S558 was identified as phosphorylation sites by mass spectrometry. PMID:23297348 S74 and S95 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S74 and S95 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S370 was identified as phosphorylation sites by mass spectrometry. PMID:23297348 serine residues, presumably some or all of those mutated PMID:23297348 serine residues, presumably some or all of those mutated PMID:23297348 serine residues, presumably some or all of those mutated PMID:23297348 S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 T297 and S364 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 T123 and S334 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 T123 and S334 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry. PMID:23297348 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 non-flocculating cells PMID:23314747 Cnp1 localisation to centromere reduced in teb1-1 cells grown at 36C (based on immunofluorescence) PMID:23314747 AACCCT box, subtelomere PMID:23314747 AACCCT box, subtelomere PMID:23314747 AACCCT box, subtelomere PMID:23314747 Southern Blot of teb1-1 cells grown at permissive and restrictive temperatures shows no change in telomere length, compared to wild type cells PMID:23333317 Fig4A fin1 activation is dependent on sid1 PMID:23333317 Fig5B PMID:23333317 Fig5B plo1 increased specific activity PMID:23333317 Fig5B PMID:23333317 Fig5B PMID:23333317 Fig5B PMID:23333317 Fig5B plo1 decreased specific activity PMID:23333317 Fig 1. Rescue of cdc25-22 but not restored to full growth (partial rescue) PMID:23333317 Fig5B Dis2NGBP binds to cut12GFP and suppresses the cut12PDswap phenotype PMID:23333317 Fig5B plo1 increased specific activity PMID:23333317 Fig5B PMID:23333317 Fig5B PMID:23333317 Fig5B plo1 decreased specific activity PMID:23333317 Fig5B DELAYED PMID:23333317 Fig5B PMID:23333317 Fig5B plo1 decreased specific activity PMID:23333317 Fig5B DELAYED PMID:23333317 Fig5B PMID:23333317 Fig5B plo1 increased specific activity PMID:23333317 Fig5B PMID:23333317 Fig5B PMID:23333317 Fig 1. Rescue of cdc25-22 but not restored to full growth (partial rescue) PMID:23333317 Fig1. Rescue of cdc25-22 but not restored to full growth (partial rescue) PMID:23333317 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 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 Fig5B PMID:23333317 Fig5B PMID:23333317 Fig5B plo1 increased specific activity PMID:23333317 Fig5B PMID:23333317 Fig5B PMID:23333317 Fig5B PMID:23333317 Fig5B plo1 increased specific activity PMID:23333317 Fig5B PMID:23333317 Fig5B PMID:23333317 Fig5B plo1 decreased specific activity PMID:23333317 Fig5B DELAYED PMID:23333317 Fig5B PMID:23333317 Fig5B plo1 increased specific activity PMID:23333317 Fig5B PMID:23333317 Fig5B PMID:23333317 Fig5B plo1 increased specific activity PMID:23333317 Fig1. Rescue of cdc25-22 but not restored to full growth (partial rescue) PMID:23333317 Fig1. Rescue of cdc25-22 but not restored to full growth (partial rescue) PMID:23333317 Fig2E PMID:23333317 T75T78 PMID:23333317 T75 PMID:23333317 Fig 1b, F and G. (T75T78 UNPHOSPHORYLATED FORM) PMID:23333317 Fig 1b, F and G. (T75T78 PHOSPHORYLATED FORM) PMID:23333317 Fig1 C 2 hybrid PMID:23333317 Fig5B plo1 increased specific activity PMID:23333317 Fig5B PMID:23333317 Fig5B PMID:23333317 Fig5B plo1 increased specific activity PMID:23333317 Fig5B PMID:23333317 Fig1c 2-hybrid PMID:23333317 Fig1 C 2 hybrid PMID:23333317 Fig1C 2 hybrid PMID:23333317 Fig1C 2 hybrid PMID:23333317 Fig2H PMID:23333317 Fig2H (VWI added this and man=de the original 'abnormal cell size' small (variable size at division, mixed sized see #3800) PMID:23333317 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 Fig 2E phospho mimetic cdc12 mutant rescues cdc25 mutant PMID:23333317 Fig 2E phospho mimetic cdc12 mutant rescues cdc25 mutant PMID:23333317 Fig1c 2-hybrid PMID:23333317 Fig1D PMID:23333317 Fig1 D & E PMID:23333317 Fig1D PMID:23333317 Fig1D PMID:23333317 Fig1C increased interaction in 2 hybrid PMID:23333317 Fig1 E PMID:23333317 Fig1E PMID:23333317 Fig5B PMID:23333317 Fig5B PMID:23333317 Fig5B plo1 increased specific activity PMID:23333317 Fig5B PMID:23333317 Fig5B. premature recruitment of protein to the mitotic SPB PMID:23333317 Fig5B plo1 increased specific activity PMID:23333317 Fig5A plo1 localisation to SPB is dependent on fin1 activity PMID:23333317 Fig1E PMID:23333317 Fig1E PMID:23333317 Fig1 E PMID:23333317 "Fig1A, 2A. vw""Fig 1. Rescue of cdc25-22 but not restored to full growth (partial rescue)""" PMID:23333317 Fig2A PMID:23333317 Fig 2A,C Cut12.PD swap can no longer suppress cdc25-22 at 36°C because dis2.NGBP can bind to cut12.PDswap. When dis2 is deleted cdc25-22 suppression is restored PMID:23333317 Fig2G PMID:23333317 Fig2H PMID:23333317 Fig 2E phospho mimetic cdc12 mutant rescues cdc25 mutant PMID:23333317 Fig 2E unphosphorylatable cut12 mutants are unable to rescue cdc25 mutant (vw changed from decreased to abolished?) PMID:23333317 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 Fig2E single mutant T75D does not rescue cdc25-22 as well as double T75DT78D or singleT78D mutants. (vw: changed to decreased) PMID:23333317 Fig2I single mutant cut12. T75A binds dis2 PMID:23333317 Fig2I single mutant cut12.T78A binds Dis2 PMID:23333317 Fig5A plo1 localisation to SPB is dependent on fin1 activity PMID:23333317 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 Fig2I single mutant cut12. T75D reduces dis2 binding PMID:23333317 Fig5A No increase in recruitment of plo1 to SPB when fin1 is active if T75 T78 mutated to A PMID:23333317 Fig4F T75 T78 no longer phosphorylated and dis2 remains bound to cut12 PMID:23333317 Fig4F dis2 remains bound to cut12 PMID:23333317 Fig4E in absence of fin1 activity dis2 remains bound to cut 12 PMID:23333317 Fig4A an antibody that recognized Cut12 when phosphorylated on T75 [Figure S2C] alone established that MPF phosphorylates T75 in vitro [Figure 4D]). PMID:23333317 Fig2I single mutant cut12. T78D reduces dis2 binding PMID:23333317 Fig2I Fig3C double mutant cut12.T75A T78A binds dis2 PMID:23333317 Fig4A HU arrest Fig4E synchronous culture PMID:23348717 assayed using AspRec8c–FGFP construct PMID:23348717 assayed using cell growth with AspRec8c–FGFP–Mei2SATA construct (degradation frees Mei2SATA to arrest cell cycle) PMID:23348717 assayed using ArgDHFRts–HA–Mcm4ts construct or AspRec8c–FGFP construct PMID:23348717 also assayed using AspRec8c–FGFP construct, which persists longer than unmodified full-length Rec8 PMID:23348717 assayed using ArgDHFRts–HA–Mcm4ts construct or AspRec8c–FGFP construct PMID:23348717 assayed using AspRec8c–FGFP construct PMID:23349636 more specifically, response to mitotic DNA replication checkpoint signaling PMID:23349808 during cytokinesis PMID:23349808 during G2 phase of mitotic cell cycle PMID:23349808 during G2 phase of mitotic cell cycle PMID:23349808 during G2 phase of mitotic cell cycle PMID:23349808 during G2 phase of mitotic cell cycle PMID:23394829 also present in early anaphase; disappears by late anaphase PMID:23394829 also present in early anaphase; disappears by late anaphase PMID:23395004 mug20::GFP-kanMX6(C-terminal GFP tag) PMID:23395004 mug20::GFP-kanMX6(C-terminal GFP tag) PMID:23395004 ChIP-CHIP, rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag) PMID:23395004 ChIP-CHIP, rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag) PMID:23395004 ChIP-CHIP, rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag) PMID:23395004 ChIP-CHIP, rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag) PMID:23395004 ChIP-CHIP, rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag) PMID:23395004 ChIP-CHIP, rec27-205::GFP-kanMX6(C-terminal GFP tag) PMID:23395004 mug20::GFP-kanMX6(C-terminal GFP tag) PMID:23395004 rec27-205::GFP-kanMX6(C-terminal GFP tag) PMID:23395004 rec25-204::GFP-kanMX6(C-terminal GFP tag) PMID:23395004 mug20::GFP-kanMX6(C-terminal GFP tag) PMID:23395004 mug20::GFP-kanMX6(C-terminal GFP tag) PMID:23395004 mug20::GFP-kanMX6(C-terminal GFP tag) PMID:23395004 mug20::GFP-kanMX6(C-terminal GFP tag) PMID:23395004 mug20::GFP-kanMX6(C-terminal GFP tag) PMID:23395004 rec25-204::GFP-kanMX6(C-terminal GFP tag) PMID:23395004 ChIP-CHIP, rec27-205::GFP-kanMX6(C-terminal GFP tag) PMID:23427262 vw after attachment PMID:23427262 vw after attachment PMID:23442800 required for ubiquitination of Slp1 PMID:23462181 Fig. 2A and B PMID:23462181 Fig. 2A and B PMID:23462181 Fig. 2A and B PMID:23462181 Fig. 2A and B PMID:23462181 Fig. 2A and B PMID:23496905 Figure 1 PMID:23496905 Figure 3 PMID:23496905 fig 2 PMID:23496905 Figure 1 PMID:23496905 Figure 1 PMID:23496905 fig 2 PMID:23496905 fig 4 (40% act remaining) PMID:23496905 fig 2 PMID:23496905 Figure 3 PMID:23496905 Figure 3 PMID:23496905 Figure 3 PMID:23496905 Figure 1 PMID:23496905 fig 2 PMID:23496905 fig 2 PMID:23496905 Figure 1 PMID:23496905 Figure 2 PMID:23496905 fig 4 (60%) PMID:23503588 in vitro PMID:23551936 cellular response to rapamycin = GO:0072752 cellular response to caffeine =GO:0071313 PMID:23551936 cellular response to rapamycin = GO:0072752 cellular response to caffeine =GO:0071313 PMID:23555033 occurs_at CSL_response_element in vivo PMID:23555033 major region affecting localization between aa 395â465 PMID:23555033 overexpression PMID:23555033 to CSL_response_element PMID:23555033 to CSL_response_element PMID:23555033 occurs_at CSL_response_element, overexpression, in vitro PMID:23576550 anti-alpha-tubulin antibody used; included both pombe alpha-tubulin gene names in extension PMID:23576550 anti-alpha-tubulin antibody used; included both pombe alpha-tubulin gene names in extension PMID:23609449 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 figure 10 (check specificty) PMID:23609449 binds the non trimmed part of the N-glycan PMID:23615450 complements deletion Figure 6A PMID:23615450 complements deletion Figure 6A PMID:23615450 complements deletion PMID:23615450 complements deletion PMID:23615450 complements deletion PMID:23615450 complements deletion PMID:23615450 Figure 1D PMID:23615450 complements deletion PMID:23615450 complements deletion Figure 6A PMID:23615450 complements deletion PMID:23615450 Figure 1E and Supplemental Figure S1C PMID:23615450 Figure 4F PMID:23615450 Figure 4C PMID:23615450 Figure 4C PMID:23615450 complements deletion Figure 6A PMID:23615450 Kd ≈ 20 μM Supplemental Figure S5B PMID:23615450 complements deletion PMID:23615450 Figure 1E and Supplemental Figure S1C PMID:23615450 (Figure 3). PMID:23615450 Figure 1E and Supplemental Figure S1C PMID:23615450 Figure 1C and Supplemental Figure S1C PMID:23615450 in interphase PMID:23615450 (Figure 3). PMID:23615450 Figure 4F PMID:23615450 Supple- mental Figure S9C) PMID:23615450 (Figure 3). PMID:23615450 fig 5 PMID:23615450 Figure 4F inferred penetrance because growth not m,uch affected PMID:23615450 complements deletion PMID:23615450 complements deletion Figure 6A PMID:23628763 binds chromatin at promoter, and phenotypes suggest this PMID:23628763 fig3c PMID:23628763 fig3c PMID:23628763 fig2 PMID:23628763 boosts expression of the APC activator Fzr1/Mfr1 PMID:23658229 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05) PMID:23658229 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05) PMID:23658229 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05) PMID:23658229 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05) PMID:23658229 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05) PMID:23658229 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05) PMID:23658229 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05) PMID:23658229 deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05) PMID:23671279 RNA level increases upon amitrole exposure in wild type but not mutant PMID:23671279 RNA level increases upon amitrole exposure in wild type but not mutant PMID:23671279 vw edited PMID:23671279 RNA level increases upon amitrole exposure in wild type but not mutant PMID:23671279 RNA level increases upon amitrole exposure in wild type but not mutant PMID:23671279 same as either single mutant PMID:23671279 same as cpc2delta alone PMID:23671279 same as cpc2delta alone PMID:23671279 same as gcn2delta alone PMID:23671279 worse than cpc2delta alone PMID:23671279 RNA level increases upon amitrole exposure in wild type but not mutant PMID:23671279 RNA level increases upon amitrole exposure in wild type but not mutant PMID:23671279 RNA level increases upon amitrole exposure in wild type but not mutant PMID:23671279 RNA level increases upon amitrole exposure in wild type but not mutant PMID:23671279 RNA level increases upon amitrole exposure in wild type but not mutant PMID:23671279 RNA level increases upon amitrole exposure in wild type but not mutant PMID:23671279 RNA level increases upon amitrole exposure in wild type but not mutant PMID:23671279 RNA level increases upon amitrole exposure in wild type but not mutant PMID:23671279 RNA level increases upon amitrole exposure in wild type but not mutant PMID:23671279 RNA level increases upon amitrole exposure in wild type but not mutant PMID:23671279 RNA level increases upon amitrole exposure in wild type but not mutant PMID:23671279 RNA level increases upon amitrole exposure in wild type but not mutant PMID:23671279 RNA level increases upon amitrole exposure in wild type but not mutant PMID:23671279 RNA level increases upon amitrole exposure in wild type but not mutant PMID:23677513 same as rad9delta alone PMID:23677513 same as rad9delta alone PMID:23677513 same as hus1delta alone PMID:23677513 same as hus1delta alone PMID:23677513 same as hus1delta alone PMID:23677513 same as rad9delta alone PMID:23677513 same as rad9delta alone PMID:23677513 same as hus1delta alone PMID:23687372 homothallic h90 PMID:23687372 move down to G1, nitrogen induced PMID:23687372 occurs_during(G1 to Go transition) PMID:23687372 homothallic h90 PMID:23687372 occurs_during(G1 to G0 transition) PMID:23687372 occurs_during(G1 to G0 transition) PMID:23687372 occurs_during(G1 to G0 transition) PMID:23695302 they don't say whether the OEP populations continue to grow like normal (viable/inviable). Also data not shown. PMID:23754748 fig s1, can't tell after germination or before PMID:23770677 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 The Nuf2 complex interacts with the Alp7-Alp14 complex phosphorylated by the polo kinase Plo1 PMID:23770679 meiosis I PMID:23770679 figure 2a PMID:23770679 The Nuf2 complex interacts with the Alp7-Alp14 complex phosphorylated by the polo kinase Plo1 PMID:23770679 The Alp7-Alp14 complex localises to kinetochores prior to meiosis I independently of microtubules, which does not seem to occur in mitosis. PMID:23770679 fig 7c PMID:23770679 Fig 7 PMID:23770679 Fig 6c or abolished? PMID:23770679 Supp Fig S6 PMID:23770679 fig 2g PMID:23770679 Fig 2 b-d involved in kinetochore retrieval during meiotic prophase PMID:23770679 Fig 2 b-d nvolved in kinetochore retrieval during meiotic prophase PMID:23770679 fig 5b PMID:23770679 The Alp7-Alp14 complex localises to kinetochores prior to meiosis I independently of microtubules, which does not seem to occur in mitosis. PMID:23770679 The Alp7-Alp14 complex localises to kinetochores prior to meiosis I independently of microtubules, which does not seem to occur in mitosis. PMID:23770679 Fig 6a PMID:23770679 Figure 6 b/d (d used chromosome tethered polo mutants, I did not curate these phenotypes) PMID:23770679 Is this phase correct PMID:23770679 polo consensus fig 6b PMID:23770679 Supp Fig S6 PMID:23770679 fig 2G PMID:23770679 Fig 3b PMID:23770679 fig 3d PMID:23770679 fig 3d PMID:23770679 Is this phase correct PMID:23770679 Is this phase correct PMID:23770679 fig 4c PMID:23770679 fig 4c PMID:23770679 fig 4d PMID:23770679 fig 4d PMID:23770679 figure 4c PMID:23770679 figure 4 PMID:23770679 fig 5b PMID:23770679 Fig 5. d,e (unattached) PMID:23851719 results in retaining specifically modified histone H3 at the genes in question PMID:23874237 The SO ID's correspond to tRNA lys/gln/glu PMID:23874237 The SO ID's correspond to tRNA lys/gln/glu PMID:23874237 The SO ID's correspond to tRNA lys/gln/glu PMID:23885124 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 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 The mating rate was not affected in mtl2Dh+ 9 mtl2Dh or wsc1Dh+ 9 wsc1Dh homozygous crosses, PMID:23907979 Mtl2p-GFP showed an even membrane distribution with little intra- cellular signals. PMID:23907979 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 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 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 wsc1D and mtl2D cells did not exhibit any evident morphological changes (Fig. 1B) PMID:23907979 wsc1D and mtl2D cells did not exhibit any evident morphological changes (Fig. 1B) PMID:23907979 ~8% of the cells in the wsc1D mutant and 15% of the cells in mtl2D were lysed (Fig. 1B) PMID:23907979 ~8% of the cells in the wsc1D mutant and 15% of the cells in mtl2D were lysed (Fig. 1B) PMID:23907979 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 wsc1D cell growth was inhibited above 2 lg/mL of Csp (Fig. 1C) PMID:23907979 We found that GS activity was slightly reduced in mtl2D null cells (Fig. 1D) PMID:23907979 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 Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1). PMID:23907979 Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1). PMID:23907979 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 described as rounded , but more 'stubby' PMID:23907979 The wsc1Drgf2D double mutant was viable, but we failed to find any double- mutant spore wsc1Drgf1D. T PMID:23907979 . 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 . 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 . 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 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:23907979 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 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 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 (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 (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 (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 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 In tea4D cells, Wsc1p-GFP localized mainly to the growing tip that was stained with Cfw (Fig. 3C). PMID:23907979 Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1). PMID:23907979 Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1). PMID:23907979 Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1). PMID:23907979 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 Repres- sion of mtl2+ promoted cell lysis and the cells shrunk without the release of cytoplasmic material. PMID:23907979 The mating rate was not affected in mtl2Dh+ 9 mtl2Dh or wsc1Dh+ 9 wsc1Dh homozygous crosses, PMID:23907979 Repres- sion of mtl2+ promoted cell lysis and the cells shrunk without the release of cytoplasmic material. PMID:23936074 assayed using minichromosomes and internal telomeric repeat arrays PMID:23936074 increased staining of all chromatin PMID:23956092 was branched, elongated, multiseptate cell PMID:23962284 recombinant hal3 not a strong inhibitor in vitro PMID:23962284 we don't know if they germinate or not PMID:23966468 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 FYPO_EXT:0000001=high penetracne PMID:23977061 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:23977061 I changed this to exocytosis. This is required for cell wall organization, as it is causally upstream (val) PMID:23986474 (Table 1; Fig. 3A) PMID:23986474 (Table 1; Fig. 3A) PMID:23986474 fig 3c PMID:23986474 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 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 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 Fig. 2B orb5.as2 displayed moderate sensitivity to 30 mM of 3BrB-PP1, whereas orb5.as1 showed none PMID:23986474 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 fig 4c. PMID:23986474 dns PMID:23986474 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 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 Fig 1. PMID:23986474 Fig 1 PMID:23986474 DNS PMID:23986474 (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 Fig. 2B orb5.as2 displayed moderate sensitivity to 30 mM of 3BrB-PP1, whereas orb5.as1 showed none PMID:23986474 Fig. 2B orb5.as2 displayed moderate sensitivity to 30 mM of 3BrB-PP1, whereas orb5.as1 showed none PMID:23986474 Fig. 2B orb5.as2 displayed moderate sensitivity to 30 mM of 3BrB-PP1, whereas orb5.as1 showed none PMID:23986474 (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 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 The static FACS profiles established that replication was indeed inhibited in analogue-released cdc10.v50 wee1.as8 cdc25.22 cells after analogue addition (Fig. 7B, right panel). PMID:23986474 Fig 1. PMID:24003116 Grown in EMM + 200uM ZnSo4. Measurements made via ICP-MS. PMID:24003116 Grown in EMM + 200uM ZnSo4. Measurements made via ICP-MS. PMID:24003116 Grown in EMM + 200uM ZnSo4. Measurements made via ICP-MS. PMID:24003116 Visualized via Florescence using an integrated LOZ1::GFP construct grown in EMM +/- ZnSo4 PMID:24003116 directly regulates adh4 PMID:24003116 Via EMSA binds directly to adh4 promoter. PMID:24006256 wee1-50 epistatic to dnt1delta; shows that cell cycle regulation by Dnt1 depends on Wee1 PMID:24006256 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:24006488 fig4 PMID:24006488 Serine 720 and Serine 732 are phosphorylated by Chk1 Phosphorylation releases MBF from DNA and represses transcription of MBF-dependent genes. PMID:24006488 Serine 720 and Serine 732 are phosphorylated by Chk1 Phosphorylation releases MBF from DNA and represses transcription of MBF-dependent genes. PMID:24006488 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 fig4 PMID:24006488 fig4 PMID:24006488 fig4 PMID:24006488 fig4 PMID:24006488 fig4 PMID:24006488 localizes the MBF complex PMID:24013504 dependent_on(GO:0006312)| not_dependent_on(GO:0007004) PMID:24021628 heterologous complemetation of S. c HMO1 PMID:24039245 in vitro assay with purified proteins PMID:24047646 Fig3, Table 1 PMID:24047646 Fig1 PMID:24047646 Fig1 PMID:24047646 Fig1 PMID:24047646 Fig1 In early G2 nif1 localisation is monopolar and in late G2 it is bipolar PMID:24047646 Fig 6, shows pom1delta cells still have G2-M size control PMID:24047646 Fig 6, shows nif1delta cells still have G2-M size control PMID:24047646 Fig3, Table 1 PMID:24047646 Fig 6, shows wee1-50 cells at restrictive temperature have lost G2-M size control PMID:24047646 Fig3, Table 1 PMID:24047646 Fig1 PMID:24055157 Although Dma1-GFP still localized to SPBs in sid4(T275A) mutant cells (Figure S1F), PMID:24055157 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 Although Dma1-GFP still localized to SPBs in sid4(T275A) mutant cells (Figure S1F), PMID:24055157 Although mutating S278 to alanine abolished Sid4 ubiquitination (Figure 1D) PMID:24055157 assayed with human CK1 PMID:24055157 assayed with human CK1, process from phenotypes (dma1 dependent pathway) PMID:24055157 mutating S278 to a glutamate did not affect Sid4 ubiquitination (Figure 1D). PMID:24055157 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 Hhp1-GFP localization at SPBs is Sid4 independent (Figure S3E) PMID:24055157 Hhp1-GFP localization at SPBs is Sid4 independent (Figure S3E) PMID:24055157 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 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 In corroboration of these findings, sid4(T275A) mutants were refractory to dma1 overexpression lethality (Figure 2D). PMID:24055157 cells bypassed the arrest after 5 hrs (Figure 2C). PMID:24055157 cells bypassed the arrest after 5 hrs (Figure 2C). ......These data indicate that mutating T275 eliminates Dma1-dependent checkpoint signaling. PMID:24055157 Although Dma1-GFP still localized to SPBs in sid4(T275A) mutant cells (Figure S1F), PMID:2406029 same as cdc2-ww single mutant PMID:24074952 residue=T235 | residue=T187, annotation_extension=added_by(CDK COMPLEX, CDC2 AND CDC13) | residue=T215 PMID:24074952 residue=T235 | residue=T187, annotation_extension=added_by(CDK COMPLEX, CDC2 AND CDC13) | residue=T215 PMID:24074952 residue=T235 | residue=T187, annotation_extension=added_by(CDK COMPLEX, CDC2 AND CDC13) | residue=T215 PMID:24081329 evidence for all FYPO:0001908 = northern blot PMID:24095277 has substrates centromere outer repeat transcripts and polyA mRNA. Activated by mg2+ PMID:24095277 does it produce 5' monoesters? PMID:24095277 has substrates centromere outer repeat transcripts and polyA mRNA. Activated by mg2+ PMID:24095277 siRNA PMID:24115772 during(GO:0051329) PMID:24115772 dependent on septation initiation signaling (GO:0031028) PMID:24118096 Trx1's involvement in tis process is to recycle mxr1 for met-O conversion to met PMID:24127216 figs2a PMID:24127216 fig2a PMID:24127216 fig2a PMID:24127216 Truncation of Cdc12 at N-terminus leads to a requirement of For3 actin assembly for contractile ring assembly. PMID:24127216 fig3e PMID:24127216 fig 1d-g PMID:24127216 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 fig3e PMID:24127216 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 figS1a PMID:24127216 fig 1D-G PMID:24127216 fig1b PMID:24127216 fig 1d-g PMID:24127216 fig1b PMID:24127216 fig1a PMID:24127216 Truncation of Cdc12 at N-terminus leads to a requirement of For3 actin assembly for contractile ring assembly. AL -also see fig 2fgh PMID:24127216 fig 1h PMID:24146635 shorter duration of heat exposure (up to ~45 min) PMID:24146635 36 degrees (not brief heat shock) PMID:24146635 Global gene expression profile (RNAseq) of deletion similar to that of heat-stressed wild type. PMID:24146635 Global gene expression profile (RNAseq) of deletion similar to that of heat-stressed wild type. PMID:24146635 """Both Gef1-3YFP and Scd1-GFP exhibited bipolar localization in majority of late wild type cells""" PMID:24146635 """Both Gef1-3YFP and Scd1-GFP exhibited bipolar localization in majority of late wild type cells""" PMID:24146635 shorter duration of heat exposure (up to ~45 min) PMID:24146635 shorter duration of heat exposure (up to ~45 min) PMID:24146635 prolonged heat exposure (more than ~45 min) PMID:24146635 punctate; shorter duration of heat exposure (up to ~45 min) PMID:24146635 prolonged heat exposure (more than ~45 min) PMID:24146635 prolonged heat exposure (more than ~45 min) PMID:24146635 prolonged heat exposure (more than ~45 min) PMID:24146635 prolonged heat exposure (more than ~45 min) PMID:24146635 prolonged heat exposure (more than ~45 min) PMID:24147005 7c PMID:24147005 6A PMID:24155978 5X PMID:24155978 all independent of Sty1 (effects of H2O2 & NAC unchanged in sty1delta) PMID:24155978 5S PMID:24161933 5a. PMID:24161933 fig1 PMID:24161933 abundances of 40% or lower, cells lacked checkpoint activity. PMID:24161933 (Fig. 2d) PMID:24161933 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 In cells with 30% Mad1, the checkpoint was markedly impaired in minimal medium, although largely functional in rich medium PMID:24167631 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 supp fig7 PMID:24186976 supp fig7 PMID:24224056 in response to carbon source change from glucose to maltose regulates agl1 PMID:24224056 in response to carbon source change from glucose to maltose regulates agl1 PMID:24224056 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:24239120 Fig. 3 PMID:24239120 Fig. 1 PMID:24239120 Fig. 3 PMID:24239120 Fig. 3 PMID:24239120 Fig. 4 PMID:24239120 Fig. S1 (This is a rescue of FYPO:0000324) PMID:24239120 Fig. S1 (This is a rescue of FYPO:0000324) PMID:24239120 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 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 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 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 Fig. S1 PMID:24239120 Fig. S1 PMID:24239120 Fig. 1 PMID:24239120 Fig. 1 PMID:24239120 Fig. 2 (This is a rescue of FYPO:0004395) PMID:24239120 Fig. 2 (This is a rescue of FYPO:0004395) PMID:24239120 Fig. S1 (This is a partial rescue of FYPO:0004307) PMID:24239120 Fig. 3 PMID:24239120 Fig. 1 PMID:24239120 Fig. 1 PMID:24239120 Fig. 1 PMID:24239120 Fig. 1 PMID:24239120 Fig. 1 PMID:24239120 Fig. 1 PMID:24239120 Fig. 1 PMID:24239120 Fig. 3 PMID:24239120 Fig. 4 PMID:24239120 Fig. 2 (This is a rescue of FYPO:0000324) PMID:24239120 Fig. 1 PMID:24240238 Southern blot to detect telomeric sequence PMID:24240238 Rap1-GBD + low-level swi6+ overexpression allows assays using a reporter gene away from the telomere, to distinguish effects of taz1 and pot1 mutations. PMID:24240238 Southern blot to detect telomeric sequence PMID:24240238 Rap1-GBD + low-level swi6+ overexpression allows assays using a reporter gene away from the telomere, to distinguish effects of taz1 and pot1 mutations. PMID:24240238 Rap1-GBD + low-level swi6+ overexpression allows assays using a reporter gene away from the telomere, to distinguish effects of taz1 and pot1 mutations. PMID:24240238 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 silencing normal as long as heterochromatin assembly can take place normally PMID:24240238 Southern blot to detect telomeric sequence PMID:24240238 Southern blot to detect telomeric sequence PMID:24240238 Southern blot to detect telomeric sequence PMID:24240238 Southern blot to detect telomeric sequence PMID:24240238 Southern blot to detect telomeric sequence PMID:24244528 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 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:24244528 However, most filaments (99%) bound by -E1 were non-motile, while most filaments bound by wild-type Myo2p were motile (Movie S2). PMID:24244528 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:24247430 I think this is real i.e. downregulation of growth to allow differentiation PMID:24268782 vw: fixed extensions to link F-P and to delete GO:0051091 PMID:24268782 vw: fixed extensions to link F-P and to delete GO:0051091 vw: move up to from thioredoxin-disulfide reductase activity PMID:24291789 (Fig. 3b), suggesting that cohesin in principle achieves topological loading onto DNA independently of a cohesin loader, albeit inefficiently. PMID:24291789 fig 4 b part_of extension is 'positive regulation of mitotic cohesin loading' PMID:24291789 (Fig. 3b), suggesting that cohesin in principle achieves topological loading onto DNA independently of a cohesin loader, albeit inefficiently. PMID:24291789 (Fig. 3b), suggesting that cohesin in principle achieves topological loading onto DNA independently of a cohesin loader, albeit inefficiently. PMID:24291789 (Fig. 3b), suggesting that cohesin in principle achieves topological loading onto DNA independently of a cohesin loader, albeit inefficiently. PMID:24291789 (Fig. 2e) Fig. 2f) Fig. 3a,b). contributes to, mis4 is sufficient? PMID:24291789 Fig. 1c,d part_of extension is 'positive regulation of mitotic cohesin loading' PMID:24291789 (Fig. 2e) Fig. 2f) Fig. 3a,b). PMID:24291789 Fig. 2a,b and Extended Data Fig. 2a PMID:24291789 Fig. 2a,b and Extended Data Fig. 2a PMID:24291789 Fig. 2a,b and Extended Data Fig. 2a PMID:24291789 Fig. 2a,b and Extended Data Fig. 2a PMID:24291789 Fig. 2a,b and Extended Data Fig. 2a PMID:24291789 Fig. 2a,b and Extended Data Fig. 2a PMID:24291789 Fig. 2a,b and Extended Data Fig. 2a PMID:24291789 Fig. 2a,b and Extended Data Fig. 2a PMID:24291789 Fig. 1c,d (part_of extension is 'positive regulation of mitotic cohesin loading' PMID:24291789 Fig. 1a PMID:24291789 Fig. 1a PMID:24297439 it's a bit indirect, but they show this via consensus site mutations....I think it is borderline ok PMID:24297439 Two hybrid interaction using Gpa2K270E activated protein with Sck1. PMID:24297439 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 Two hybrid interaction using Gpa2K270E activated protein with Sck1. PMID:24313451 assayed using cell extract, overexpressed protien and synthetic UB conjugate PMID:24314397 inhibited by α-(hydroxymethyl)serine (CHEBI:28187) PMID:24316795 high concentration (1 uM) 3MB-PP1 PMID:24316795 same as cdr2-S755A-758A alone PMID:24316795 Pom1-as1 protein may preferentially localize to non-growing end. PMID:24316795 low concentration (<0.25 uM) 3MB-PP1 PMID:24316795 Negatively regulated by Pom1 via phosphorylation of C-ter PMID:24316795 Cdr2 phosphorylated by Pom1 at the CTD negatively regulates its activity PMID:24316795 Phosphorylates cdr2 at S755 in vitro PMID:24316795 high overexpression PMID:24316795 high overexpression PMID:24316795 high concentration (1 uM) 3MB-PP1 PMID:24316795 high concentration (1 uM) 3MB-PP1 PMID:24316795 same as cdr2-S755A-758A alone PMID:24316795 moderate overexpression PMID:24316795 low concentration (<0.25 uM) 3MB-PP1 PMID:24316795 high concentration (1 uM) 3MB-PP1 PMID:24316795 low concentration (<0.25 uM) 3MB-PP1 PMID:24316795 low concentration (<0.25 uM) 3MB-PP1 PMID:24327658 in vitro kinase assay using recombinant Sre1 aa 1-440 PMID:24327658 in vitro kinase assay using recombinant Sre1 aa 1-440 PMID:24327658 Binds specifically to active Sre1 transcription factor and not full-length precursor PMID:24327658 in vitro kinase assay using recombinant Sre1 aa 1-440 PMID:24327658 Ok as a single mutant despite sre1-N mutant? PMID:24327658 accelerates degradation of active Sre1 transcription factor PMID:24327658 hhp2 deletion increases steady-state ergosterol PMID:24344203 isp7+ overexpression decreases Gad8's kinase activity towards substrate Fkh2 PMID:24344203 same as isp7+ overexpression alone PMID:24344203 same as isp7+ overexpression alone PMID:24475199 Expression level up 3 times PMID:24475199 Expression level up 2 times PMID:24475199 Expression level up 2 times PMID:24475199 Expression level up 2 times PMID:24475199 Expression level up 25 times PMID:24475199 Expression level up 23 times PMID:24475199 Expression level up 35 times PMID:24475199 Expression level up 8 times. PMID:24475199 Expression level up 22 times PMID:24475199 Expression level up 38 times PMID:24475199 Expression level up 43 times PMID:24475199 Expression level up 31 times PMID:24475199 Expression level up 2.5 times PMID:24475199 Expression level up 2 times PMID:24477934 Fig S4A PMID:24477934 Fig 1I–L PMID:24477934 Fig1C/D PMID:24477934 Fig 1I–L PMID:24477934 Fig S1A and D PMID:24477934 Fig S2F PMID:24477934 Fig S2F PMID:24477934 Fig S2C,D,E PMID:24477934 Fig S2C,D,E PMID:24477934 Fig S2C,D,E PMID:24477934 Fig S1I PMID:24477934 Fig S1I PMID:24477934 Fig S1B PMID:24477934 Fig S1B PMID:24477934 Fig 3D PMID:24477934 Fig 3 D PMID:24477934 Fig3 B/C PMID:24477934 Fig3 B/C PMID:24477934 Fig 1I–L PMID:24477934 Fig S4a PMID:24477934 Fig S4a PMID:24477934 Fig S4a PMID:24477934 Fig S4a PMID:24477934 Fig 1A, C–E PMID:24477934 Fig 1A, C–D PMID:24477934 1H PMID:24477934 Fig 1H PMID:24477934 Fig 1H PMID:24477934 Fig 2B PMID:24477934 (Fig (Fig 2D and E). mad1 localized did not rescue, PMID:24477934 Fif 3F PMID:24477934 . 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 Fig S2C,D,E PMID:24477934 Fig S2F PMID:24477934 Fig S2F PMID:24477934 Fig S1I PMID:24477934 Fig S4a PMID:24477934 Fig S4a PMID:24477934 Fig S4a PMID:24477934 Fig S4a PMID:24477934 Fig S4a PMID:24477934 Fig S4a PMID:24477934 Fig S4a PMID:24477934 Fig S4a PMID:24477934 Fig S4a PMID:24477934 Fig S4a PMID:24477934 Fig S4a PMID:24477934 Fig S4a PMID:24477934 (Fig 1F PMID:24477934 fig1F PMID:24477934 Fig1F PMID:24477934 Fig1F PMID:24477934 Fig 1A, C–E PMID:24477934 Fig 1A, C–E PMID:24477934 Fig S4A PMID:24478458 phosphorylates rgf1 during HU response, part of maintenance of protien lcoation in nucleus PMID:24493644 fig5 PMID:24514900 low expressivity PMID:24514900 high penetrance PMID:24514900 Required for phosphatydil serine reorganization at the inner leaflet of plasma membrande during cell fusion PMID:24521463 mild phenotype PMID:24521463 decreased cell pop is not a child of this term PMID:24521463 mild expressivity PMID:24521463 high expressivity (strong phenotype) PMID:24521463 low expressivity PMID:24554432 sufficient to trigger cell shape change when targeted to cell sides by fusion with Cdr2 PMID:24554432 more specific term requested: involved in positive regulation of establishment of cell polarity regulating cell shape; similar pom1 deletion phenotype indicates that Tea4 is at least partly independent of Pom1 for Rga4 localization PMID:24554432 more specific term requested: involved in positive regulation of establishment of cell polarity regulating cell shape PMID:24554432 more specific term requested: involved in positive regulation of establishment of cell polarity regulating cell shape PMID:24554432 more specific term requested: involved in positive regulation of establishment of cell polarity regulating cell shape PMID:24554432 necessary to trigger cell shape change upon Tea4 targeting to cell sides by fusion with Cdr2 PMID:24554432 sufficient to trigger cell shape change when targeted to cell sides by fusion with Cdr2 PMID:24554432 necessary to trigger cell shape change upon Tea4 targeting to cell sides by fusion with Cdr2 PMID:24554432 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:24569997 figure 5B PMID:24569997 figur 5B PMID:24569997 changed from transcription because mrna measured fig2 (copper excess) PMID:24569997 changed from transcription because mrna measured fig2 PMID:24569997 changed from transcription because mrna measured (fig 1) PMID:24569997 changed from transcription because mrna measured (fig 1) PMID:24569997 changed from transcription because mrna measured (fig 1) PMID:24569997 *******during copper excess****** changed from transcription because mrna measured fig2 PMID:24569997 Observed at this location during spore maturation by indirect immunofluorescence PMID:24583014 Fig. 1A indicating that CDK1 activity remained high PMID:24583014 Fig. 1A PMID:24583014 Fig. 2B,C PMID:24583014 Fig. 1B, PMID:24583014 figure S1B PMID:24583014 Fig. S1B,C PMID:24583014 Fig. 3A,B,E, securin abnormally stabilized during anaphase PMID:24583014 Fig. 2B,C PMID:24583014 Fig. 1A PMID:24583014 Fig. 1A PMID:24583014 Fig. 1D,E PMID:24583014 Fig. 2A, , complex seen here in anaphase although it normally forms in prometaphase and disassembles before anaphase PMID:24586893 the extension means that the phenotype has low expressivity (i.e. weak sensitivity) PMID:24637836 sensitivity is weak. PMID:24637836 sensitivity is weak. PMID:24637836 sensitivity is weak. PMID:24637836 Fluorescence microscopy of Sec13 tagged with GFP at either its N-terminal or C-terminal end. PMID:24637836 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 weak sensitivity PMID:24637836 sensitivity is weak PMID:24652833 no MF possible PMID:24652833 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:24662054 binds both DNA and histone. Not sure if the H3 preference is an artefact of in vitro system PMID:24662054 binds both DNA and histone. Not sure if the H3 preference is an artefact of in vitro system PMID:24663817 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 1D, Fig. 2B PMID:24663817 1D,Fig. 2B PMID:24663817 1D,Fig. 2B PMID:24663817 1D PMID:24663817 1D PMID:24663817 C13Y and K56R mutations completely eliminated the phosphorylation of Chk1 in MMS-treated cells (Fig. 3A) PMID:24663817 C13Y and K56R mutations completely eliminated the phosphorylation of Chk1 in MMS-treated cells (Fig. 3A) PMID:24663817 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 C13Y and K56R mutations completely eliminated the phosphorylation of Chk1 in MMS-treated cells (Fig. 3A) PMID:24663817 3D PMID:24663817 3D PMID:24663817 3D PMID:24663817 3D PMID:24663817 f3 PMID:24663817 f3 PMID:24663817 The C13Y and K56R mutations abolished the scaffolding function of Rad4 required for the activation of Chk1 but not Rad3 PMID:24663817 C13Y-K56R mutation abolished the interaction with Crb2 (Fig. 5C), not Rad9 (Fig. 5A and B). PMID:24663817 E368K mutation abolished the binding to Rad9 as previously reported [47] (Fig. 5A and B) PMID:24663817 C13Y-K56R mutation abolished the interaction with Crb2 (Fig. 5C), not Rad9 (Fig. 5A and B). PMID:24663817 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 Fig. 5A and B PMID:24663817 3a/b PMID:24663817 3a/b. cds1-T11 PMID:24663817 3a/b PMID:24663817 affected by rad4 PMID:24663817 (phosphorylated rad9) PMID:24663817 1D, Fig. 2B PMID:24663817 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 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 1D PMID:24663817 1D,Fig. 2B PMID:24663817 1D, Fig. 2B PMID:24696293 supp fig PMID:24710126 convert to double mutant (cnp1 overexpression) PMID:24710126 central core PMID:24710126 central core PMID:24713849 mei4 ssm4 crs1 rec8 spo5 PMID:24713849 Observed in cells undergoing vegetative growth. PMID:24713849 mei4 ssm4 crs1 rec8 spo5 PMID:24713849 mei4 ssm4 crs1 rec8 spo5 PMID:24713849 mei4 ssm4 crs1 rec8 spo5 PMID:24713849 "[Term] id: FYPO_EXT:0000003 name: low def: ""small fraction of cells (penetrance) or weak phenotype (expressivity)"" [PomBase:curators]" PMID:24713849 mei4 ssm4 crs1 rec8 spo5 PMID:24713849 mei4 ssm4 crs1 rec8 spo5 PMID:24713849 mei4 ssm4 crs1 rec8 spo5 PMID:24713849 mei4 ssm4 crs1 rec8 spo5 PMID:24713849 Observed in cells undergoing vegetative growth. PMID:24713849 Observed in cells undergoing vegetative growth. PMID:24713849 Observed in cells undergoing vegetative growth. PMID:24713849 mei4 ssm4 crs1 rec8 spo5 PMID:24713849 mei4 ssm4 crs1 rec8 spo5 PMID:24713849 mei4 ssm4 crs1 rec8 spo5 PMID:24713849 Observed in cells undergoing vegetative growth. PMID:24713849 Observed in cells undergoing vegetative growth. PMID:24713849 mei4 ssm4 crs1 rec8 spo5 PMID:24713849 mei4 ssm4 crs1 rec8 spo5 PMID:24713849 mei4 ssm4 crs1 rec8 spo5 PMID:24713849 mei4 ssm4 crs1 rec8 spo5 PMID:24741065 phosphorylation of mei2 targets it for degradation via the proteasome PMID:24741065 tor2 phosphorylates mei2. Phosphorylated mei2 is ubiquitylated which targets it for degradation via the proteasome. PMID:24755092 SPAC12G12.09-mCherry localizes to stress granules PMID:24755092 Exo2-GFP localizes to stress granules PMID:24758716 qualifier=major PMID:24758716 qualifier=major PMID:24758716 qualifier=minor Hsp3106 (synonym: spDJ-1) has a lower in vitro glyoxalase III activity than Hsp3101 and Hsp3102 PMID:24768994 Figure 2B PMID:24768994 Figure 5 PMID:24768994 Figure 2C PMID:24768994 Figure 2B PMID:24768994 Figure 3 PMID:24768994 Figure 3 PMID:24768994 Figure 5 PMID:24768994 Figure 2A PMID:24768994 Figure 5 PMID:24774534 fig6 PMID:24774534 fig6 PMID:24774534 fig6 PMID:24774534 fig6 PMID:24774534 fig6 PMID:24774534 fig6 PMID:24774534 fig6 PMID:24774534 add other complex members PMID:24774534 fig6 PMID:24774534 fig6 PMID:24774534 fig6 PMID:24774534 fig6 PMID:24787148 ubiquitin monmomer inhibits sst2 PMID:24790093 Yeast two hybrid PMID:24790095 exists_during( metaphase? anaphase A????) PMID:24790095 mitotic interphase PMID:24790095 exists_during( metaphase? anaphase A????) PMID:24798735 "this annotation extension means ""small fraction of cells""" PMID:24798735 "this annotation extension means ""small fraction of cells""" PMID:24798735 "this annotation extension means ""small fraction of cells""" PMID:24798735 "this annotation extension means ""small fraction of cells""" PMID:24806815 This localisation requires phosphorylated histone H2A. PMID:24806815 Mdb1 binds to Hta1 phosphorylated on Ser-129. PR:000027566 = H2A phosphorylated on S129 PMID:24815688 "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 Figure 1 A PMID:24818994 figure 1 A PMID:24818994 Figure 1 A PMID:24818994 Figure 1 A PMID:24818994 Figures 3 and 6 PMID:24818994 figure 1D PMID:24818994 Figures 3 and 6 PMID:24818994 Figures 3 and 6 PMID:24818994 figure 1D PMID:24818994 Figure 5A, + PMID:24818994 minor PMID:24818994 figure 1D PMID:24818994 Figures 3 and 6 PMID:24831008 fig4 PMID:24831008 Fig 2 PMID:24831008 Fig 2 PMID:24831008 Fig 2 PMID:24831008 Fig 2 PMID:24831008 fig4 PMID:24831008 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 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 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 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 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 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 fig2 PMID:24831008 fig 4g PMID:24831008 fig1 PMID:24831008 fig1 PMID:24847916 The phenotype is assessed by the high-throughput sequencing. PMID:24876389 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 abolished internalization PMID:24876389 abolished internalization PMID:24876389 ubiquitinated probably at K263. PMID:24876389 abolished internalization PMID:24876389 have guessed at deleted residues PMID:24876389 internalization abolished PMID:24920274 figS1 PMID:24920274 figS1 PMID:24920274 figS1 PMID:24920274 figS1 PMID:24920274 figS1 PMID:24920274 figS1 PMID:24920274 figS1 PMID:24920274 figS1 PMID:24920274 figS1 PMID:24920274 figS1 PMID:24920274 figS1 PMID:24920274 figS1 PMID:24920274 figS1 PMID:24920274 figS1 PMID:24920274 abnormal RNA localization to chromatin PMID:24920274 fig3 PMID:24920274 fig3 PMID:24920274 fig3 PMID:24920274 fig3 PMID:24920274 "the def includes ""maintenance of lcoalization WITHIN nucleus"" so it fits the def, but maybe the term looks weird" PMID:24920274 "the def includes ""maintenance of lcoalization WITHIN nucleus"" so it fits the def, but maybe the term looks weird" PMID:24920274 at sme2 locus (one of several exosome foci in nucleus during vegetative growth) PMID:24920274 at sme2 locus (one of several exosome foci in nucleus during vegetative growth) PMID:24920823 S326, T429, S499: added by cyclin-dependent kinase (Cdk1) PMID:24920823 S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1) PMID:24920823 S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1) PMID:24920823 targets Byr4 at S248A, S326A, T412A, T429A, S499A, T502A, S533A, results in Byr4 removal from metaphase spindle pole bodies PMID:24920823 low penetrance PMID:24920823 Cdk1-dependent, Cdk1 non-phosphorylatable Byr4 localizes to one or both SPBs in >90% of metaphase cells PMID:24920823 S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1) PMID:24920823 medium penetrance PMID:24920823 S326, T429, S499: added by cyclin-dependent kinase (Cdk1) PMID:24920823 affecting Cdc7 PMID:24920823 Term name: supports establishment of SIN asymmetry Definition: characterized by asymmetric localization of the SIN initiator kinase Cdc7 in anaphase PMID:24920823 results from collapse of actomyosin contractile ring PMID:24920823 anaphase B PMID:24920823 S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1) PMID:24925530 starts with longer telomeres than wild type, which then shorten PMID:24928430 Fig. 3 PMID:24928430 Fig. 3 - minor rescue PMID:24928430 Fig. 3 - minor rescue PMID:24928430 Fig. 3 - minor rescue PMID:24928430 Fig. 4 - minor rescue PMID:24928430 Fig. 4 - minor rescue PMID:24928430 Fig. 1 PMID:24928430 Fig. 1 PMID:24928430 Fig. 2 PMID:24928430 Fig. 3 - minor rescue PMID:24928430 Fig. 3 PMID:24928510 Phosphorylation assayed in vitro PMID:24928510 Phosphorylation assayed in vitro PMID:24928510 Phosphorylation assayed in vitro PMID:24928510 Protein phosphorylation assayed in vitro PMID:24928510 protein phosphorylation assayed in vitro PMID:24928510 protein phosphorylation assayed in vitro PMID:24928510 protein phosphorylation assayed in vitro PMID:24928510 Protein phosphorylation assayed in vitro PMID:24928510 protein phosphorylation assayed in vitro PMID:24928510 protein phosphorylation assayed in vitro PMID:24928510 protein phosphorylation assayed in vitro PMID:24928510 Phosphorylation assayed in vitro PMID:24928510 protein phosphorylation assayed in vitro PMID:24928510 Phosphorylation assayed in vitro PMID:24928510 protein phosphorylation assayed in vitro PMID:24928510 protein phosphorylation assayed in vitro PMID:24928510 Phosphorylation assayed in vitro PMID:24936793 also inferrable (IC) from GO:0051787 PMID:24937146 affecting Pcp1 and Alp4 PMID:24937146 affecting Pcp1 and Alp4 PMID:24937146 affecting Alp7 PMID:24945319 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 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 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 Fig. 1B PMID:24947517 Fig 6 B. PMID:24947517 Fig 6 B. PMID:24947517 Fig 6 B. PMID:24947517 Fig 6 B. PMID:24947517 Fig. 6A PMID:24947517 Fig. 6A PMID:24947517 Fig 5 B PMID:24947517 Fig 5 A PMID:24947517 Fig. 5A PMID:24947517 Fig 4 C,D,E PMID:24947517 Fig. 4A PMID:24947517 Fig. 4A PMID:24947517 Fig 4 A PMID:24947517 Fig 4 A PMID:24947517 Fig 4 A PMID:24947517 Fig 4 A PMID:24947517 Data not shown PMID:24947517 Data not shown PMID:24947517 Fig. 3F PMID:24947517 Fig. 3F PMID:24947517 Fig. 3F PMID:24947517 Data not shown PMID:24947517 Data not shown PMID:24947517 Figure 3 C PMID:24947517 Figure 3 C PMID:24947517 fig 1 F PMID:24947517 Fig 1 F PMID:24947517 (Fig. 6D) PMID:24947517 Fig 1 F PMID:24947517 fig 1 F PMID:24947517 Fig 1 E PMID:24947517 Fig 1 E PMID:24947517 Fig 1 D PMID:24947517 Fig 1 D (decreased rate of cell separation) PMID:24947517 Fig. 1C PMID:24947517 Fig. 1B PMID:24947517 Fig. 1B PMID:24947517 Fig. 5A PMID:24947517 Fig. 3A PMID:24947517 Fig 6 D. PMID:24947517 Fig 6 C, D PMID:24947517 Fig 6 C. PMID:24947517 Fig 6 B. PMID:24947517 Fig 6 B. PMID:24954052 PR:000037081= ID for acetylated form of cdc8 PMID:24954052 GO:0051286 = cell tip PR:000037082 = ID for unacetylated form of cdc8 PMID:24954111 spindle defects caused by the loss of telomere clustering were rescued by stopping nuclear movement. PMID:24954111 fig1 In wild-type cells, monopolar or nonpolar spindles were not observed (Fig. 4C). PMID:24954111 fig1 PMID:24954111 fig1 PMID:24954111 never observed 54/54 PMID:24954111 bipolar spindle defects caused by the loss of telomere clustering were rescued by stopping nuclear movement. PMID:24954111 never observed 37/37 PMID:24954111 bipolar/spindle defects caused by the loss of telomere clustering were rescued by stopping nuclear movement. PMID:24954111 Fig 6 A,B even in the presence of the bipolar spindle PMID:24957674 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 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 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 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 should this move down to lobate? http://www.pombase.org/spombe/related/FYPO:0002005 PMID:24963130 GO:0000236 mitotic prometaphase PMID:24963130 (GO:0000279) = mitotic M-phase PMID:24963130 2 sub populations spindle elongation delayed during anaphase A spindle elongation delayed during anaphase B PMID:24963130 GO:0000087 mitotic M-phase PMID:24997422 ). 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 LTR and ncRNA PMID:25002536 occurs at LTR and ncRNA PMID:25002536 LTR and ncRNA PMID:25002536 occurs at LTR and ncRNA PMID:25002536 occurs at LTR and ncRNA PMID:25002536 occurs at LTR and ncRNA PMID:25009287 Skb1 and Slf1 (SPAC821.03C) mutually depend to form node-like structures on the plasma membrane. PMID:25009287 Skb1 and Slf1 (SPAC821.03C) mutually depend to form node-like structures on the plasma membrane. PMID:25015293 multinucleate inferred from DNA content PMID:25015293 same as spt20delta alone PMID:25015293 same as spt20delta alone PMID:25015293 same as spt20delta alone PMID:25015293 multinucleate inferred from DNA content PMID:25015293 multinucleate inferred from DNA content PMID:25015293 multinucleate inferred from DNA content PMID:25015293 multinucleate inferred from DNA content PMID:25015293 punctate PMID:25040903 Figure S1C PMID:25040903 Figure S1E PMID:25040903 Figure S1C PMID:25040903 Figure S1E PMID:25057016 Fig. 2 PMID:25057016 Fig. S1D PMID:25057016 Fig. 2 PMID:25057016 Fig. 1 PMID:25057016 Fig. 1 PMID:25057016 Fig. 1 PMID:25057016 Fig. 1 PMID:25057016 Thorough experiments throughout using both full deletions as well as phospho mutants. Direct physical interaction is confirmed by Y2H PMID:25057016 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 Fig. 3 PMID:25057016 Fig. 3 PMID:25057016 Fig. 3 PMID:25057016 Fig. 4 PMID:25057016 Fig. 4 PMID:25057016 Fig. 4 (BiFC) PMID:25057016 Fig. 4 PMID:25057016 Fig. 4 PMID:25057016 Fig. 4 PMID:25057016 Fig. 4 PMID:25057016 Fig. 4 (BiFC) PMID:25057016 Fig. 4 PMID:25057016 Fig. 4 PMID:25057016 Fig. 4 PMID:25057016 Fig. 4 PMID:25057016 Fig. 4 PMID:25057016 Fig. 4 PMID:25057016 Fig. S5D PMID:25057016 Fig. 6 PMID:25057016 Fig. 6 PMID:25057016 Fig. 6 PMID:25066056 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:25066056 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 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:25081204 prz1 is the pombe equivalent to NFAT (functional equivalent rather than orholog) PMID:25081204 the pop grows more slowly but I guess they are viable en large PMID:25081204 cmk1 seems to phosphorylate prz1 which makes prz1 cytoplasmic. During response to calcium, calcineurin dephosphorylates prz1 and it goes to the nucleus. PMID:25081204 prz1 is the pombe equivalent to NFAT (functional equivalent rather than orholog) PMID:25103238 Failure of NE fenestration during mitosis in the double tts1del cut1-6 mutant PMID:25103238 large fraction of cells = annotation_extension=has_penetrance(FYPO_EXT:0000001) PMID:25106870 RER should probably be a child of this PMID:25106870 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 Incision of ribonucleotides paired to 8oxoguanine in the DNA PMID:25106870 fig 1 PMID:25106870 fig5 PMID:25109267 Ricinoleic acid, RA moieties from phospholipids PMID:25122751 At stress response genes PMID:25195688 transmembrane import into Golgi lumen PMID:25195688 transmembrane import into Golgi lumen PMID:25203555 not sure PMID:25203555 regulator of structure-specific DNA nuclease PMID:25204792 defect in sexual development in response to zinc or iron limitation PMID:25204792 defect in sexual development in response to zinc or iron limitation PMID:25245948 cDNA; no introns PMID:25245948 cDNA; no introns PMID:25245948 cDNA; no introns PMID:25245948 cDNA; no introns PMID:25245948 cDNA; no introns PMID:25245948 cDNA; no introns PMID:25254656 Figure 4E PMID:25254656 igure 3B Figure 3C PMID:25254656 Figure S15 PMID:25254656 Figure S2A PMID:25254656 Figure 3A PMID:25254656 Figure 4E PMID:25254656 in vitro Figure S1A, right pane PMID:25254656 in vitro Figure S1A, right pane PMID:25254656 figure 3C PMID:25254656 figure 3C PMID:25254656 figure 3C the N erminal domain has a dominent -ve effect in in vitro assay (not expression should ne n/a) PMID:25254656 Figure 4A) PMID:25313826 the CAF-1 complex promotes Replication-coupled homologous recombination at blocked replication forks. PMID:25313826 the CAF-1 complex promotes Replication-coupled homologous recombination at blocked replication forks. PMID:25313826 the CAF-1 complex promotes Replication-coupled homologous recombination at blocked replication forks. PMID:25318672 permissive temperature for bbl1-9 PMID:25318672 Determined by thin layer chromatography (TLC) PMID:25318672 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 restrictive temperature for bbl1-9 PMID:25318672 The endoplasmic reticulum is wrapped around the abnormally large lipid droplets PMID:25318672 restrictive temperature for bbl1-9 PMID:25318672 restrictive temperature for bbl1-9 PMID:25318672 Determined by thin layer chromatography (TLC) PMID:25318672 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 Determined by thin layer chromatography (TLC) PMID:25318672 Mutant cells grow normally in liquid minimal medium supplemented with choline. PMID:25318672 Mutant cells grow normally in liquid minimal medium supplemented with ethanolamine. PMID:25318672 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 Mutant cells grow normally in liquid rich medium PMID:25318672 Determined by thin layer chromatography (TLC) PMID:25330395 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 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 Tpz1-L439R,L445R disrupts interaction with Ccq1 but retain interactions with Pot1 and Poz1 based on co-IP experiments. PMID:25330395 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:25348260 Fig. 3 PMID:25348260 Fig. 3 PMID:25348260 Fig. 3 PMID:25348260 Fig. 3 PMID:25348260 Fig. 3 PMID:25348260 Fig. 3 PMID:25348260 Fig. 3 PMID:25348260 Fig. 3 PMID:25348260 Fig. 3 PMID:25375240 Figure 4G PMID:25375240 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 indicated by increased mad2 on unattached kinetochores PMID:25375240 figure 5E PMID:25375240 Figure 7D PMID:25375240 Figure 7D PMID:25378562 Sensitive to 3 mM ZnCl2. Suppressed by overexpression of budding yeast VAM7. PMID:25378562 Vsl1p is a partner of Pep12p, and mainly functions on the prevacuolar and vacuolar membrane. PMID:25378562 Sensitive to 3 mM ZnCl2 PMID:25378562 mutants defective in vacuolar sorting do not deliver SpCPY to the 185 vacuole but rather to the outside of the cells. PMID:25378562 mutants defective in vacuolar sorting do not deliver SpCPY to the 185 vacuole but rather to the outside of the cells. PMID:25378562 Vsl1p is a partner of Pep12p, and mainly functions on the prevacuolar and vacuolar membrane. PMID:25392932 SO:0001272 = tRNA gene PMID:25392932 SO:0001272 = tRNA gene PMID:25392932 Our data only demonstrate that this true for RNA Polymerase III // MOVED UP TO 'REGULATION' FROM NEG REG BASED ON NEW PUBLICATION PMID:25402480 "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 "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 "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 "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 "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 Table 2 PMID:25404562 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 Table 2 PMID:25404562 Table 2 PMID:25404562 Table 2 PMID:25404562 Table 2 PMID:25404562 Table 2 PMID:25404562 Table 2 PMID:25404562 Table 2 PMID:25404562 Table 2 PMID:25404562 Table 2 PMID:25404562 Table 2 PMID:25404562 Table 2 PMID:25404562 Table 2 PMID:25404562 Table 2 PMID:25404562 specific term requested PMID:25404562 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 Fig. 2A (11 days for visible colonies) PMID:25404562 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 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 Fig. 3A PMID:25404562 specific term requested PMID:25404562 specific term requested PMID:25404562 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 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 Table 2 PMID:25404562 Table 2 PMID:25404562 Table 2 PMID:25404562 Table 2 PMID:25410910 yes it looks like pol II?! (val: changed to DNA binding term) PMID:25411334 check supp S2A is this increased septation index? PMID:25411334 check supp S2A PMID:25411334 check supp S2A PMID:25411334 A GEF of Rho4 PMID:25411334 check supp S2A PMID:25411334 changed from bud neck to medial cortex ring but the def will be updated so it does not refer to double ring https://sourceforge.net/p/geneontology/ontology-requests/11819/ || depends on septins to localize to the division site. PMID:25411338 strong phenotype = has_severity(FYPO_EXT:0000001) PMID:25411338 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 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 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 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 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 during cellular response to glucose starvation PMID:25411338 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 strong phenotype = has_severity(FYPO_EXT:0000001) PMID:25411338 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 during cellular response to glucose starvation PMID:25411338 during cellular response to glucose starvation PMID:25411338 during cellular response to glucose starvation PMID:25414342 50.7% of wild-type spore viability, synergistic relationship (Table S5) PMID:25414342 38.5% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Fig. 4B, Table S5) PMID:25414342 33.7% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 4A, Table S5) PMID:25414342 (Fig. 4C, Table S5) PMID:25414342 83.9% of wild-type spore viability (Fig. 4D, Table S5) PMID:25414342 (Table S2) PMID:25414342 (Table S2) PMID:25414342 117% of wild-type recombination assayed at various loci (Fig. 1, Table S2) PMID:25414342 78.4% of wild-type spore viability (Table S2) PMID:25414342 28.9% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Fig. 4B, Table S5) PMID:25414342 39.7% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 4A, Table S5) PMID:25414342 85.9% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 4C, Table S5) PMID:25414342 61.1% of wild-type spore viability (Fig. 4D, Table S5) PMID:25414342 61.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Fig. 3B, Table S4) PMID:25414342 42.4% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 3A, Table S4) PMID:25414342 82.9% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 4C, Table S5) PMID:25414342 95.2% of wild-type spore viability (Fig. 3D, Table S4) PMID:25414342 48.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Fig. 3B, Table S4) PMID:25414342 27.7% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 3A, Table S4) PMID:25414342 82.2% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 3C, Table S4) PMID:25414342 108.5% of wild-type spore viability (Fig. 3D, Table S4) PMID:25414342 49.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Fig. 3B, Table S4) PMID:25414342 49.2% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 3A, Table S4) PMID:25414342 90.5% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 3C, Table S4) PMID:25414342 133.5% of wild-type spore viability (Fig. 3D, Table S4) PMID:25414342 16.3% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Fig. 4B, Table S5) PMID:25414342 9.7% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 4A, Table S5) PMID:25414342 87.6% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 4C, Table S5) PMID:25414342 77.7% of wild-type spore viability (Fig. 4D, Table S5) PMID:25414342 31.4% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S6) PMID:25414342 8.0% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 6, Table S6) PMID:25414342 (Fig. 5, Table S6) PMID:25414342 43.6% of wild-type spore viability (Table S6) PMID:25414342 0.9% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S3) PMID:25414342 12.3% of wild-type recombination assayed between ade6-3083 and ade6-469 (Table S3) PMID:25414342 1.7% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 2B, Table S3) PMID:25414342 47% of wild-type spore viability (Fig. 2A, Table S3), 18.3-fold higher spore viability than mus81 single mutant PMID:25414342 19.1% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S3) PMID:25414342 2.2% of wild-type recombination assayed between ade6-3083 and ade6-469 (Table S3) PMID:25414342 10.5% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 2B, Table S3) PMID:25414342 42.9% of wild-type spore viability, 16.7-fold higher spore viability than mus81 single mutant (Fig. 2A, Table S3) PMID:25414342 26.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S3) PMID:25414342 30.1% of wild-type recombination assayed between ade6-3083 and ade6-469 (Table S3) PMID:25414342 9.9% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 2B, Table S3) PMID:25414342 21.2% of wild-type spore viability, 8.3-fold higher spore viability than mus81 single mutant (Fig. 2A, Table S3) PMID:25414342 6.4% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S3) PMID:25414342 57.9% of wild-type recombination assayed between ade6-3083 and ade6-469 (Table S3) PMID:25414342 7.8% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 2B, Table S3) PMID:25414342 28.9% of wild-type spore viability, 11.3-fold higher spore viability than mus81 single mutant (Fig. 2A, Table S3) PMID:25414342 58.1% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S3) PMID:25414342 36.3% of wild-type recombination assayed between ade6-3083 and ade6-469 (Table S3) PMID:25414342 6.9% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim (Fig. 2B, Table S3) PMID:25414342 44.7% of wild-type spore viability, 17.4-fold higher spore viability than mus81 single mutant (Fig. 2A, Table S3) PMID:25414342 48.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Fig.3B, Table S4) PMID:25414342 32.3% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig. 3A, Table S4) PMID:25414342 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 117.1% of wild-type spore viability (Fig. 3D, Table S4) PMID:25414342 55.5% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Fig. 3B, Table S4) PMID:25414342 44.4% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig. 3A, Table S4) PMID:25414342 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 104.8% of wild-type spore viability (Fig. 3D, Table S4) PMID:25414342 0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, synergistic relationship (Fig. 4B, Table S5) PMID:25414342 0.42% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship (Fig. 4A, Table S5) PMID:25414342 3.7% of wild-type spore viability, synergistic relationship (Fig. 4D, Table S5) PMID:25414342 4.5% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, synergistic relationship (Fig. 4B, Table S5) PMID:25414342 2.5% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship (Fig. 4A, Table S5) PMID:25414342 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 13.0% of wild-type spore viability, synergistic relationship (Fig. 4D, Table S5) PMID:25414342 33.5% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Fig. 4B, Table S5) PMID:25414342 14.2% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig. 4A, Table S5) PMID:25414342 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 93.8% of wild-type spore viability, epistatic relationship (Fig. 4D, Table S5) PMID:25414342 26.4% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Fig. 4B, Table S5) PMID:25414342 25.7% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig. 4A, Table S5) PMID:25414342 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 76.9% of wild-type spore viability, epistatic relationship (Fig. 4D, Table S5) PMID:25414342 0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, synergistic relationship (Fig. 4B, Table S5) PMID:25414342 2.1% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship (Fig. 4A, Table S5) PMID:25414342 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 9.9% of wild-type spore viability, synergistic relationship (Fig. 4D, Table S5) PMID:25414342 65.3% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Fig. 4B, Table S5) PMID:25414342 21.1% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig. 4A, Table S5) PMID:25414342 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 55.5% of wild-type spore viability, synergistic relationship (Fig. 4D, Table S5) PMID:25414342 54.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S5) PMID:25414342 31.1% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Table S5) PMID:25414342 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 15.4% of wild-type spore viability, synergistic relationship (Table S6) PMID:25414342 76.1% of wild-type recombination assayed between ade6-3083 and ade6-469 (Table S6) PMID:25414342 7.2% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship - similar to rqh1delta (Fig. 6, Table S6) PMID:25414342 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 60.64% of wild-type spore viability, epistatic relationship (Table S6) PMID:25414342 7.4% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6A, Table S6) PMID:25414342 24.3% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6) PMID:25414342 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 25.9% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6) PMID:25414342 2.55% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship (Fig.6A, Table S6) PMID:25414342 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 54.78% of wild-type spore viability, epistatic relationship (Table S6) PMID:25414342 28.85% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6) PMID:25414342 3.55% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig.6A, Table S6) PMID:25414342 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 55.62% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, partial rescue from rad55Δ levels (Table S6) PMID:25414342 35.42% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6B, Table S6) PMID:25414342 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 53.76% of wild-type spore viability, epistatic relationship (Table S6) PMID:25414342 15.19% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6) PMID:25414342 8.87% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6B, Table S6) PMID:25414342 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 3.68% of wild-type spore viability, synergistic relationship (Table S6) PMID:25414342 15.53% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6) PMID:25414342 12.19% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6B, Table S6) PMID:25414342 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 4.11% of wild-type spore viability (Table S6) PMID:25414342 69.41% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6) PMID:25414342 36.88% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6C, Table S6) PMID:25414342 101.33% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim; higher than rlp1ÃÂ-7, lower than fml1ÃÂ, skewed recombinant categories (Figs. 5C & 7A, Table S6) PMID:25414342 46.52% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6) PMID:25414342 52.08% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Table S6) PMID:25414342 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 73.46% of wild-type spore viability, epistatic relationship (Table S6) PMID:25414342 32.13% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6) PMID:25414342 8.33% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6C, Table S6) PMID:25414342 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 37.75% of wild-type spore viability, epistatic relationship (Table S6) PMID:25414342 59.57% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6) PMID:25414342 7.33% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6C, Table S6) PMID:25414342 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 21.45% of wild-type spore viability, synergistic relationship (Table S6) PMID:25414342 49.8% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6) PMID:25414342 27.08% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6D, Table S6) PMID:25414342 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 91.68% of wild-type spore viability, epistatic relationship (Table S6) PMID:25414342 38.89% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6) PMID:25414342 10.34% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6D, Table S6) PMID:25414342 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 21.46% of wild-type spore viability, synergistic relationship (Table S6) PMID:25414342 45.45% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6) PMID:25414342 15.59% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig.6D, Table S6) PMID:25414342 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 20.24% of wild-type spore viability (Table S6) PMID:25414342 55.49% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6) PMID:25414342 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 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 7.8% of wild-type spore viability, synergistic relationship (Table S6) PMID:25414342 30.92% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship (Table S6) PMID:25414342 9.88% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6E, Table S6) PMID:25414342 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 31.18% of wild-type spore viability (Table S6) PMID:25414342 20.15% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Table S6) PMID:25414342 6.87% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship (Fig.6E, Table S6) PMID:25414342 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 13.87% of wild-type spore viability (Table S6) PMID:25417108 occurs at rDNA, tRNA gene, protein coding gene PMID:25417108 affecting antisense transcription at rDNA PMID:25417108 affecting: highly transcribed genes antisense transcription of tDNA and rDNA PMID:25417108 Affecting Rad52 enrichment at rDNA PMID:25417108 occurs at rDNA, tRNA gene, protein coding gene PMID:25417108 occurs at rDNA, tRNA gene, protein coding gene PMID:25417108 Affecting Rad52 enrichment at rDNA PMID:25417108 occurs at tDNA PMID:25417108 affecting: highly transcribed genes antisense transcription of tDNA and rDNA PMID:25417108 affecting antisense transcription at tDNA PMID:25417108 Affecting Dcr1-terminated genes PMID:25417108 affecting: highly transcribed genes antisense transcription of tDNA and rDNA PMID:25428589 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 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 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 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 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 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 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 (repressed condition; Fig. 1c) PMID:25428589 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 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 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 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 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 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 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 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 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 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 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 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 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 mitotic interphase PMID:25451933 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:25451933 competatively with cofilin PMID:25451933 igs. 6B and C and Table 3 PMID:25451933 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 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 The fission yeast lacking Aip1 have normal appearing actin patches, cables, and contractile rings (Fig. 5B). PMID:25471935 assayed Cdc20 recruitment PMID:25472718 Fig 1A PMID:25472718 Fig. 1C; Fig. 3D PMID:25472718 fig 3C PMID:25472718 fig 3A PMID:25472718 Fig. 2C,D PMID:25472718 fig 2A PMID:25472718 fig 3A PMID:25472718 fig 3A PMID:25472718 fig 3A PMID:25472718 In any case, the results shown here imply that Klp5–Klp6 localises to the kinetochores through interaction with the Alp7–Alp14 complex. PMID:25472718 In any case, the results shown here imply that Klp5–Klp6 localises to the kinetochores through interaction with the Alp7–Alp14 complex. PMID:25472718 Overall, our data suggest that Klp5–Klp6 delivers PP1 to the attached kinetochores, thereby promoting SAC silencing. PMID:25472718 Overall, our data suggest that Klp5–Klp6 delivers PP1 to the attached kinetochores, thereby promoting SAC silencing. PMID:25472718 fig S2B PMID:25472718 fig S2B PMID:25472718 fig 2 A PMID:25472718 fig 2 A PMID:25472718 (supplementary material Fig. S1A PMID:25472718 Fig 1A PMID:25472718 (Fig. 1C–E; Type I PMID:25472718 (Fig. 1C–E; Type I PMID:25472718 (Fig. 1C–E; Type I PMID:25472718 fig 1A PMID:25472718 Fig. 4A,B PMID:25472718 fig 3 d PMID:25472718 Fig. 4E reduced by >70% PMID:25472718 Fig. 4C,D) PMID:25472718 Fig. 4A,B PMID:25472718 Fig. 1C; Fig. 3D PMID:25472718 Fig. 5D PMID:25472718 Fig. 5D PMID:25472718 Fig. 5A PMID:25472718 Fig. 5A PMID:25472718 Fig. 5A PMID:25472718 Fig. 4E reduced by >70% PMID:25473118 fig6 PMID:25473118 the ring seems to start off forming normally but maturation is delayed, this leads to delayed constriction. PMID:25473118 independent of actin PMID:25473118 fig6 PMID:25487150 unphosphorylated form PMID:25500221 secretion of acid phosphatase PMID:25500221 secretion of acid phosphatase PMID:25501814 fig1 PMID:25501814 fig1 PMID:25501814 fig1 PMID:25501814 fig1 PMID:25501814 fig1 PMID:25501814 fig1 PMID:25501814 fig1c PMID:25501814 (Fig. 3C). PMID:25501814 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 fig 2g PMID:25519804 suppresses ade6-M26 efficiently; suppresses ade6-M375 weakly PMID:25519804 efficient suppression of ade6-M26; very poor suppression of ade6-M375 PMID:25519804 high suppression of phenotype PMID:25519804 low suppression of phenotype PMID:25519804 high suppression of phenotype PMID:25520186 I only captured the OEX experiment PMID:25520186 Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro PMID:25520186 of condensin complex PMID:25520186 full-length Cut14 present; not sure how to interpret this, check PMID:25520186 Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro PMID:25520186 full-length Cut14 present; not sure how to interpret this, check PMID:25520186 of condensin complex PMID:25520186 Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro PMID:25520186 Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro PMID:25520186 Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro PMID:25520186 Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro PMID:25520186 Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro PMID:25520186 full-length Cut14 present; not sure how to interpret this, check PMID:25520186 Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro PMID:25520186 Auto-phosphorylation occurred in the presence of ATP in vitro PMID:25520186 Auto-phosphorylation occurred in the presence of ATP in vitro PMID:25520186 Auto-phosphorylation occurred in the presence of ATP in vitro PMID:25520186 Auto-phosphorylation occurred in the presence of ATP in vitro PMID:25520186 Auto-phosphorylation occurred in the presence of ATP in vitro PMID:25520186 I only captured the OEX Experiment PMID:25533340 leu1 PMID:25533340 phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining S192 PMID:25533340 phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining S192 PMID:25533340 phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining T180 PMID:25533340 phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining T180 PMID:25533340 increased end-joining activity in vegetative cells PMID:25533340 This looks like direct regulation because it phosphorylates xlf1 PMID:25533348 fig 3 A PMID:25533348 fig 3 A PMID:25533348 greater range of legths PMID:25533348 greater range of legths PMID:25533348 WT 3% PMID:25533348 WT 3% PMID:25533348 WT 3% PMID:25533348 WT 3% PMID:25533348 fig 3 A PMID:25533348 fig 3 A PMID:25533348 fig 3 A PMID:25533348 fig 3 A PMID:25533348 fig 3 A PMID:25533348 fig 3 A PMID:25533348 fig 3 A PMID:25533348 fig 3 A PMID:25533348 greater range of legths PMID:25533348 fig 3 A PMID:25533956 RECRUITS PMID:25533956 fig5 e PMID:25533956 fig5 e PMID:25543137 Diffuse cytoplasmic localisation at 37°C, no stress granules PMID:25543137 hsp104 refolds dicer and is required for robust centromeric silencing at 37°C PMID:25543137 Dcr1 represses hsp104 levels PMID:25543137 A prionogenic reporter (S. cerevisiae Sup35 prion domain) aggregates in cytoplasmic inclusions in dcr1Δ PMID:25543137 Dcr1 is not released from cytoplasmic inclusions at 37°C in hsp104Î PMID:25543137 Dcr1 localizes in electron-dense cytoplasmic inclusions at 37°C together with hsp104. Hsp104 is required for dissolution of these inclusions. PMID:25543137 Cytoplasmic localisation in electron-dense inclusions at 37°C PMID:25543137 Nuclear localization at 30°C PMID:25543137 Nuclear localization at 30°C PMID:25590601 iii) decreased during glucose starvation PMID:25590601 ii) in the presence of glucose PMID:25590601 ii) removed during glucose starvation ii) observed during nitrogen starvation iv) S546 PMID:25590601 ii) removed during nitrogen starvation iv) T415 PMID:25590601 ii) removed during glucose starvation ii) observed during nitrogen starvation iv) S546 PMID:25590601 ii) removed during glucose starvation ii) observed during nitrogen starvation iv) S546 PMID:25590601 strong phenotype = has_severity(FYPO_EXT:0000001) PMID:25619765 cen2-lacO PMID:25619765 pNBg was used PMID:25619998 (S2) PMID:25619998 (S2) PMID:25619998 (S2) PMID:25639242 figure 4D PMID:25639242 figure 2b 9% longer PMID:25639242 figure 2a PMID:25639242 figure 6E PMID:25639242 figure 6E PMID:25639242 fig 6A PMID:25639242 S3A PMID:25639242 Fig 3G PMID:25639242 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 figure 5a PMID:25639242 FIG 3F DECOUPLED CELL GROWTH ASND DIVISION PMID:25639242 FIG 3F PMID:25639242 figure S2g PMID:25639242 figure S2B PMID:25639242 Figure 4C PMID:25639242 Fig 4C PMID:25639242 Fig 3C PMID:25639242 fig 3d PMID:25639242 fig 3B PMID:25639242 2D & 4B PMID:25639242 figure 2a PMID:25639242 causally upstream of ssp2 PMID:25639242 Fig 6G PMID:25639242 fig s4c&d PMID:25639242 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 causally upstream of ssp2 PMID:25639242 An increase in AMPKaSsp2 Thr189 phosphorylation was also observed in the cbs2 .D AMPKg .D double mutant (Figure S2F). PMID:25639242 figure 4D PMID:25639242 figure 4E PMID:25688133 Cdc12-mNeonGreen, Ain1-GFP, GFP-Adf1 PMID:25688133 mCherry-cdc15,Rlc-GFP PMID:25688133 residues 20â-40 in synthetic peptide/ dissociation constant of 1.1 nM PMID:25688133 mCherry-cdc15,Rlc-GFP PMID:25688133 mCherry-cdc15,Rlc-GFP PMID:25688133 LifeAct-mCherry Sid4-GFP PMID:25688133 LifeAct-mCherry Sid4-GFP PMID:25688133 smears as does not self associate, but localizes to medial cortex PMID:25688133 Live-cell imaging of Rlc1-GFP Sid4-GFP 23% slower PMID:25688133 Live-cell imaging of Rlc1-GFP Sid4-GFP 26% slower PMID:25688133 LifeAct-mCherry Sid4-GFP PMID:25688133 Cdc12-mNeonGreen, GFP-Adf1, Ain1-GFP PMID:25688133 LifeAct-mCherry Sid4-GFP PMID:25688133 residues 20â-40 in synthetic peptide/ dissociation constant of 1.1 nM PMID:25688133 mCherry-cdc15,Rlc-GFP PMID:25724335 Gene name : aco2 PMID:25724335 Gene name : aco2 PMID:25724335 Gene name : aco2 PMID:25724335 Gene name : aco2 PMID:25724335 Gene name : aco2 PMID:25724335 Gene name : aco2 PMID:25736293 figS1B PMID:25736293 (Fig. 5C PMID:25736293 S4B PMID:25736293 S4B PMID:25736293 S4A PMID:25736293 S4A PMID:25736293 S4A PMID:25736293 S4A PMID:25736293 fig 4 A PMID:25736293 fig 3 B , supp S 3 B) abolished microtubule cortical anchoring PMID:25736293 microtubule cortical anchor (microtubule site clamp) add to other dynactin complex PMID:25736293 fig 3 B , supp S 3 B) PMID:25736293 accumulates on shrinking microtubules Fig. 2B, PMID:25736293 microtubule cortical anchor (microtubule site clamp) add to other dynactin complex PMID:25736293 3B? PMID:25736293 accumulates on shrinking microtubules Fig. 2B, PMID:25736293 accumulates on shrinking microtubules Fig. 2B, PMID:25736293 Figure S2C PMID:25736293 Figure S2C PMID:25736293 figure S2 PMID:25736293 figure S2 PMID:25736293 (Fig. 1C; supplementary material Fig. S1C), PMID:25736293 (Fig. 1C; supplementary material Fig. S1C), PMID:25736293 (Fig. 1C; supplementary material Fig. S1C), PMID:25736293 figS1B PMID:25736293 figS1B PMID:25736293 figS1B PMID:25736293 figS1B PMID:25736293 figS1B PMID:25736293 figS1B PMID:25736293 figS1B PMID:25736293 figS1B PMID:25736293 figS1B PMID:25736293 figS1B PMID:25736293 microtubule cortical anchor (microtubule site clamp) add to other dynactin complex PMID:25736293 microtubule cortical anchor (microtubule site clamp) add to other dynactin complex PMID:25736293 Fig. 7F; supplementary material Table S1 PMID:25736293 Fig. 7F; supplementary material Table S1 PMID:25736293 Fig. 7F; supplementary material Table S1 PMID:25736293 Fig. 7F; supplementary material Table S1 PMID:25736293 Fig. 7F; supplementary material Table S1 PMID:25736293 fig 7A PMID:25736293 fig 7a PMID:25736293 fig 7a PMID:25736293 abnormal movement of dynein PMID:25736293 abnormal movement of dynein PMID:25736293 fig 6a PMID:25736293 fig 6a PMID:25736293 fig 5 c PMID:25736293 fig 5 c PMID:25736293 S4B PMID:25736293 S4B PMID:25736293 (Fig. 5C PMID:25771684 "Affecting Sre1 is ""abolished protein processing"" that is specific for defects in Sre1 protein processing." PMID:25771684 "The term ""Decreased protein binding to Sre1"" is ""decreased protein binding"" that is specific for decreased binding to the protein Sre1." PMID:25778919 (requested negative regulation of) synonym mitotic telomere dispersion during metaphase PMID:25778919 Fig. S4 A PMID:25778919 fig 4 decreased telomere dispersion PMID:25778919 fig 4 PMID:25778919 Fig 2 D PMID:25778919 Fig 2 CD decreased telomere dispersion PMID:25778919 Fig 2 CD PMID:25778919 Fig. S2 A, right PMID:25778919 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 Fig 3 PMID:25778919 (Fig. 2 A, 0–3 min, arrows) PMID:25778919 Fig 3D PMID:25778919 telomere disjunction PMID:25778919 Fig. 5 A PMID:25778919 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 Fig 3 PMID:25778919 fig 6 PMID:25778919 fig6 PMID:25778919 fig7 PMID:25778919 Fig. 4 decreased telomere dispersion PMID:25793410 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 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 Sensitivity was rescued less efficiently than for the wt by 150 - 600 mM KCl PMID:25793410 10 ug/ml G418 for 4 h followed by recovery on YES PMID:25793410 Sensitivity was rescued by 0.6 M KCl, 10 ug/ml phleomycin for 4 h followed by recovery on YES PMID:25793410 100 ug/ml G418 for 4 h followed by recovery on YES PMID:25793410 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 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 Sensitivity was rescued by 0.6 M KCl, 40 ug/ml doxorubicin for 4 h followed by recovery on YES PMID:25793410 Sensitivity was rescued by 0.6 M KCl 4 mM lithium for 4 h followed by recovery on YES PMID:25793410 10 ug/ml phleomycin for 4 h followed by recovery on YES PMID:25795664 A spd1 deletion partially suppresses the synthetic growth defect in a brc1 ddb1 double mutant background PMID:25795664 spd1 deletion suppresses csn1delta sensitivity to DNA damage agents PMID:25795664 spd1 deletion suppresses csn1delta sensitivity to DNA damage agents PMID:25795664 spd1 deletion suppresses csn1delta sensitivity to DNA damage agents PMID:25795664 same as brc1delta alone PMID:25795664 same as brc1delta alone PMID:25795664 same as brc1delta alone PMID:25795664 spd1 deletion suppresses brc1delta ddb1delta sensitivity to DNA damage agents PMID:25795664 spd1 deletion suppresses brc1delta csn1delta sensitivity to DNA damage agents PMID:25795664 spd1 deletion suppresses brc1delta csn1delta sensitivity to DNA damage agents PMID:25795664 spd1 deletion suppresses brc1delta csn1delta sensitivity to DNA damage agents PMID:25795664 spd1 deletion suppresses brc1delta ddb1delta sensitivity to DNA damage agents PMID:25795664 spd1 deletion suppresses brc1delta ddb1delta sensitivity to DNA damage agents PMID:25795664 more than in csn1delta alone PMID:25795664 A spd1 deletion partially suppresses the synthetic growth defect in a brc1 csn1 double mutant background PMID:25795664 same as in csn1delta alone PMID:25795664 spd1 deletion suppresses brc1delta ddb1delta sensitivity to DNA damage agents PMID:25795664 spd1 deletion suppresses brc1delta csn1delta sensitivity to DNA damage agents PMID:25795664 spd1 deletion suppresses csn1delta sensitivity to DNA damage agents PMID:25798942 ATPase domain mutant phenotype fig 5 and S6 PMID:25803873 no peptidase activity acting on azocoll substrate in isp6 null PMID:25837586 more severe in presence of LatA PMID:25837586 Increased levels of Cdc42 and Cdc42-GTP (CRIB) PMID:25837586 Normal levels of Cdc42 and Cdc42-GTP (CRIB) PMID:25837586 Decreased levels of Cdc42 and Cdc42-GTP PMID:25837586 Decreased levels of Cdc42 and Cdc42-GTP (CRIB) PMID:25837586 Normal levels of Cdc42 and Cdc42-GTP (CRIB) PMID:25837586 Increased levels of Cdc42 and Cdc42-GTP (CRIB) PMID:25837586 Not affected by short-term actin cytoskeleton depolymerization by Latrunculin A PMID:25837586 Internally tagged functional allele, allowing live-imaging of Cdc42 PMID:25847133 GO:0000087 = mitosis PMID:25847133 This mutant protein decreased chromatin binding at heat-shock genes, ssa1+ and hsp90+ PMID:25847133 Cut14 accumulates at the mitotically-upregulated gene regions in mitosis. Cut14 enrichment requires a forkhead transcription factor Sep1. PMID:25847133 Abnormally streaked chromosomes in anaphase PMID:25847133 Cut14 accumulates at the mitotically-upregulated gene regions in mitosis. Cut14 enrichment requires a forkhead transcription factor Sep1. PMID:25869666 Fig. 4 PMID:25869666 Fig. 1 PMID:25869666 Localization of GFP-tagged protein PMID:25869666 Fig. 1 PMID:25869666 Localization of GFP-tagged protein PMID:25869666 Fig. S1 PMID:25869666 Fig. S3A PMID:25869666 Phenocopies dhc1 PMID:25869666 Delayed nuclear congresion in klp2D (Fig. 1) and double deletion dhc1D klp2D completely abolishes nuclear congression (Fig. 1)) PMID:25869666 Delayed nuclear congresion in dhc1D (Fig. 1) and double deletion dhc1D klp2D completely abolishes nuclear congression (Fig. 1)) PMID:25869666 Single deletion slows down nuclear congression (minus-end diretcted), double deletion with dhc1 inhibits it. PMID:25869666 Single deletion slows down nuclear congression (minus-end diretcted), double deletion with klp2 inhibits it. PMID:25869666 Fig. 1 PMID:25869666 Fig. 4 PMID:25869666 Fig. 1 PMID:25869666 Fig. 1 PMID:25869666 Fig. 1 PMID:25869666 Fig. 4 PMID:25869666 Fig. 1 PMID:25891897 zygotic PMID:25891897 azygotic PMID:25891897 zygotic meiosis PMID:25891897 zygotic meiosis/ Random spore analysis PMID:25891897 zygotic PMID:25891897 zygotic PMID:25891897 azygotic/ slight advance in the timing of MI and MII PMID:25891897 zygotic PMID:25891897 azygotic meiosis, rem1 and crs1 do not have a major role in azygotic meiosis PMID:25891897 zygotic PMID:25891897 zygotic random spore analysis PMID:25891897 zygotic meiosis random spore analysis PMID:25891897 zygotic PMID:25891897 zygotic PMID:25891897 zygotic meiosis random spore analysis PMID:25891897 presence of more than 2 SPBs dots after meiotic nuclear divisions 19.6% zygotes exhibit abnormal meiotic division during zygotic meiosis PMID:25891897 This phenotype is not seen when cells undergo azygotic meiosis PMID:25891897 zygotic meiosis random spore analysis PMID:25891897 zygotic PMID:25891897 zygotic PMID:25891897 zygotic PMID:25891897 zygotic PMID:25891897 zygotic meiosis random spore analysis, PMID:25891897 azygotic meiotic cell cycle/timing of pre-meiotic DNA replication is normal PMID:25891897 azygotic meiotic cell cyle PMID:25891897 zygotic meiosis random spore analysis, PMID:25891897 zygotic / >80% of asci have 4 spores PMID:25891897 zygotic/ random spore analysis PMID:25891897 azygotic/ slight advance in the timing of MI and MII PMID:25891897 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 azygotic// presence of 4x fusion protein restores the ability of cig1 cig2 puc1 rem1 quadruple deletion strain to undergo pre meiotic DNA replication PMID:25959226 In contrast, the monomeric Mid13A remained concentrated in the nucleus and its signals on the plasma membrane were more widespread, even reached the cell poles (Figure 6E PMID:25959226 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 Interestingly, it binds to PI(4,5)P2 strongly, with a Kd up to 0.12 μM (Figure 3C and 3D). PMID:25959226 Mutations of the hydrophobic C2-C2 interface shifted Mid1 into monomeric state (Figure 6A), PMID:25959226 which showed > 10-fold lower affinity to PI(4,5)P2 (Figure 3D). PMID:25959226 In contrast, monomerization only slightly reduced the affinity to PS. PMID:25959226 However, contractile ring assembly was significantly faster in mid13A than in mid1+ cells (Figure S6, C–F), PMID:25959226 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 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:25965521 same as brc1delta alone; brc1 epistatic PMID:25965521 same as brc1delta alone; brc1 epistatic PMID:25965521 same as brc1delta alone; brc1 epistatic PMID:25965521 same as brc1delta alone; brc1 epistatic PMID:25965521 same as mus81delta alone; mus81 epistatic PMID:25965521 same as mus81delta alone; mus81 epistatic PMID:25965521 same as mus81delta alone; mus81 epistatic PMID:25965521 same as mus81delta alone; mus81 epistatic PMID:25965521 same as brc1delta alone; brc1 epistatic PMID:25965521 same as mus81delta alone; mus81 epistatic PMID:25965521 same as mus81delta alone; mus81 epistatic PMID:25965521 same as mus81delta alone; mus81 epistatic PMID:25965521 same as mus81delta alone; mus81 epistatic PMID:25965521 same as mus81delta alone; mus81 epistatic PMID:25965521 same as mus81delta alone; mus81 epistatic PMID:25965521 same as mus81delta alone; mus81 epistatic PMID:25965521 same as mus81delta alone; mus81 epistatic PMID:25965521 same as mus81delta alone; mus81 epistatic PMID:25965521 same as brc1delta alone; brc1 epistatic PMID:25965521 same as mus81delta alone; mus81 epistatic PMID:25965521 same as either single mutant PMID:25965521 same as either single mutant PMID:25965521 same as brc1delta alone; brc1 epistatic PMID:25965521 same as brc1delta alone; brc1 epistatic PMID:25965521 same as brc1delta alone; brc1 epistatic PMID:25965521 same as mus81delta alone; mus81 epistatic PMID:25965521 same as mus81delta alone; mus81 epistatic PMID:25977474 abnormal cleavage furrow disc formation fig 3 PMID:25977474 abnormal cleavage furrow disc formation fig 3 PMID:25977474 abnormal cleavage furrow disc formation fig 3 PMID:25977474 abnormal cleavage furrow disc formation fig 3 PMID:25977474 abnormal cleavage furrow disc formation fig 3 PMID:25987607 non additive PMID:25987607 during mitotic M phase PMID:25987607 during mitotic M phase PMID:25987607 Fig. 5 B and Videos 1–4 PMID:25987607 Fig. 5 B and Videos 1–4 PMID:25987607 Fig. 5 B and Videos 1–4 PMID:25987607 Fig. 5 B and Videos 1–4 PMID:25987607 I want to represent the microtubule based-transporter function and cargo PMID:25987607 during mitotic M phase PMID:25987607 I want to represent the microtubule based-transporter function and cargo PMID:25987607 I think the pkl rigor is spb tethered here? PMID:25993311 table 2 PMID:25993311 fig 3 PMID:25993311 fig 3 PMID:25993311 fig 3 PMID:25993311 fig 3 PMID:25993311 table 3 PMID:25993311 table 3 PMID:25993311 table 3 PMID:25993311 fig 2 a PMID:25993311 fig 2 a PMID:25993311 fig2 PMID:25993311 fig2 PMID:25993311 fig 2 a PMID:25993311 Table S3 PMID:25993311 Table S3 PMID:25993311 Table S3 PMID:25993311 Table S3 PMID:25993311 table 2 PMID:25993311 table 1 PMID:25993311 table 1 PMID:25993311 table2 PMID:25993311 table2 PMID:25993311 table2 PMID:25993311 table2 PMID:25993311 table2 PMID:25993311 table2 PMID:25993311 table2 PMID:25993311 table 2 PMID:25993311 table 1 PMID:25993311 table 1 PMID:25993311 table 1 PMID:25993311 table 1 PMID:26007660 https://github.com/geneontology/go-ontology/issues/12379 I submitted an EC NTR PMID:26031557 Fig. 4 PMID:26031557 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 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 Fig. 3 PMID:26031557 Fig. S2 Pkl1md-GFP localized primarily to the spindle poles PMID:26031557 Fig. 2. It's only a bit worse (+3% chromosome loss). Not sure if worth including PMID:26031557 Fig. 2 PMID:26031557 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 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 Fig. S2 Pkl1md-GFP localized primarily to the spindle poles and almost completely rescued the protrusion phenotype PMID:26031557 Fig. S2 In contrast, in pkl1D msd1D cells, Pkl1md-GFP localized primarily to the spindle and only partially rescued the protrusion phenotype PMID:26031557 Fig. S4 PMID:26088418 Mutant proteins were expressed at a comparable level as wild-type Taz1 (data not shown). PMID:26088418 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 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 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 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 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 increased length hererogeneity PMID:26088418 increased length hererogeneity. taz1-4A cells still exhibited extremely heterogeneous telomeres similar to taz1Δ and taz1-4R cells (Figure 1E). PMID:26088418 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 increased length hererogeneity PMID:26088418 Mutant proteins were expressed at a comparable level as wild-type Taz1 (data not shown). PMID:26092938 decreased local concentration of the myosin-II PMID:26092938 large portion of the mutant forms cytoplasmic dots PMID:26092938 decreased local concentration of the myosin-II PMID:26092938 increased local concentration of the myosin-II PMID:26092938 localization of the myosin-II is abolished PMID:26098872 figure 8a PMID:26098872 figure 8c PMID:26098872 figure 8a PMID:26098872 figure 8 b PMID:26098872 figure 8a PMID:26108447 Figure 6 PMID:26108447 Figure 6 PMID:26108447 Figure 6 PMID:26108447 Figure 6 PMID:26108447 Figure 6 PMID:26108447 Figure 6 PMID:26108447 Figure 6 PMID:26108447 Figure 6 PMID:26108447 Figure 6 PMID:26108447 Figure 6 PMID:26108447 Figure 6 PMID:26108447 Figure 6 PMID:26108447 Figure 6 PMID:26108447 Figure 6 PMID:26108447 Figure 6 PMID:26122634 polysomal profiling PMID:26122634 polysomal profiling PMID:26124291 Fig S5A C PMID:26124291 (Fig. 4 C) PMID:26124291 Fig 7 E/F PMID:26124291 Fig 7 E PMID:26124291 (Fig. 4 C) PMID:26124291 (Fig. 4 C) PMID:26124291 Fig 6 C PMID:26124291 (Fig. 4 C) PMID:26124291 (Fig. 4 C) PMID:26124291 FFig. S5 E PMID:26124291 Fig Fig. S5 E PMID:26124291 (Fig. 4 C) PMID:26124291 Fig 6 C PMID:26124291 Fig 7 CD abnormal Q-MT bundle elongation upon G1 re-entry/interphase bundle reassembly PMID:26131711 Chk1 binds to the unphosphorylated form of Cdc2 kinase PMID:26131711 Chk1 binds to the unphosphorylated form of Cdc2 kinase PMID:26131711 modified forms of Cdc2 differ from both wild type and cdc2-1w alone PMID:26131711 Chk1 binds to the unphosphorylated form of Cdc2 kinase PMID:26131711 modified forms of Cdc2 present differ from wild type PMID:26131711 modified forms of Cdc2 present differ from wild type, but are same as in cdc2-1w alone PMID:26131711 modified forms of Cdc2 present differ from wild type, but are same as in cdc2-1w alone PMID:26131711 Chk1 binds to the unphosphorylated form of Cdc2 kinase PMID:26131711 Chk1 binds to the unphosphorylated form of Cdc2 kinase PMID:26131711 Chk1 binds to the unphosphorylated form of Cdc2 kinase PMID:26132084 figure 3 PMID:26132084 fig 3C&D vw: changed to incomplete septum PMID:26132084 figure 1 PMID:26132084 P.P. Bgs4 and Ags1 abnormal localization in the septum membrane PMID:26132084 figure 1 A,B PMID:26132084 fig 5 SH3 domain of Cdc15 is required for the proper concentration of Pxl1 at the CAR PMID:26132084 Fig 2D and 2E PMID:26132084 fig 4C PMID:26132084 Fig 2A and B fragmented with RLC strands PMID:26132084 P.P. Bgs4 and Ags1 abnormal localization in the septum membrane PMID:26132084 figure 4B PMID:26132084 fig 3C PMID:26132084 fig6 PMID:26132084 figure 1c PMID:26132084 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:26137436 table 1 PMID:26137436 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 of cell tip PMID:26152587 assayed by nuclear localization of Gaf1-GFP PMID:26152587 Gaf1-GFP is found in the nucleus following nitrogen starvation but not glucose starvation PMID:26152587 a mild phenotype PMID:26152587 assayed by nuclear localization of Gaf1-GFP PMID:26152587 assayed by nuclear localization of Gaf1-GFP PMID:26152587 assayed by nuclear localization of Gaf1-GFP PMID:26152587 Gaf1-GFP is found in the nucleus following nitrogen starvation but not glucose starvation PMID:26152587 fig1a PMID:26152587 fig1a PMID:26152587 assayed by nuclear localization of Gaf1-GFP PMID:26152587 fig1a PMID:26152587 fig1a PMID:26152587 assayed by nuclear localization of Gaf1-GFP PMID:26152587 fig1a PMID:26152587 fig1a PMID:26152587 Gaf1-GFP is found in the nucleus following nitrogen starvation but not glucose starvation PMID:26152587 fig1a PMID:26152587 fig1a PMID:26152587 fig1a PMID:26152587 a mild phenotype PMID:26152587 1h in proline medium, a mild phenotype PMID:26152587 1h in proline medium, a mild phenotype PMID:26152587 1h in proline medium, a mild phenotype PMID:26152587 assayed by nuclear localization of Gaf1-GFP PMID:26152587 assayed by nuclear localization of Gaf1-GFP PMID:26152587 1h in proline medium PMID:26160178 affecting binding to Mdb1 PMID:26160178 affecting binding to histone H2A (hta1) PMID:26221037 modification(s) not identified PMID:26221037 higher than without nup132d PMID:26221037 higher than without nup132d PMID:26221037 modification(s) not identified PMID:26258632 fig1a PMID:26258632 fig 3c PMID:26258632 fig 3 a/b PMID:26258632 fig 3 a/b PMID:26258632 fig2a PMID:26258632 fig2a PMID:26258632 figure 2a (GO:0000090= mitotic anaphase) PMID:26258632 figure 2a GO:0000236=mitotic prometaphase PMID:26258632 fig1e PMID:26258632 fig1a PMID:26258632 fig1a PMID:26258632 fig1a PMID:26258632 fig1a PMID:26258632 fig1a PMID:26258632 fig1b PMID:26258632 fig1b PMID:26258632 fig1b PMID:26258632 fig1b PMID:26258632 kinetochore localization of Cut7 is unaffected PMID:26258632 fig2a (diminished relocation from kinetochore) PMID:26258632 fig 5 c PMID:26258632 Fig. 2b (mad1 locaizes to unattached kinetochores) and fig 3a PMID:26258632 fig2d PMID:26258632 fig 3 b PMID:26258632 fig 3 a/b PMID:26258632 fig2d GO:0000089= mitotic metaphase unattached kinetohore nda3-KM311 arrested cell PMID:26258632 ABOLISHED tetermerization fig4f monomer PMID:26258632 "fig 5c ""gliding"" new GO term requested" PMID:26258632 fig1e PMID:26258632 ABOLISHED tetermerization PMID:26275423 Chromatin immunoprecipitation of this protein is highly enriched for centromeric sequences. PMID:26275423 Chromatin immunoprecipitation of this protein is highly enriched for centromeric sequences. PMID:26275423 Chromatin immunoprecipitation of this protein is highly enriched for centromeric sequences. PMID:26275423 Chromatin immunoprecipitation of this protein is highly enriched in centromeric DNA PMID:26275423 Chromatin immunoprecipitation of this protein is highly enriched for centromeric sequences. PMID:26275423 Chromatin immunoprecipitation of this protein is highly enriched in centromeric DNA PMID:26365378 s3 PMID:26365378 4h PMID:26365378 "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 Indirect evidence, could be upstream PMID:26365378 Indirect evidence, could be upstream PMID:26365378 Indirect evidence, could be upstream PMID:26365378 macroautophagy? - selective autophagy is a child of macroautophagy PMID:26365378 s3 PMID:26366556 determined by EMSA. Substrate: dsDNA oligonucleotide derived from promoters of cut6 and ptl1 genes (contain the CSL_response_element) PMID:26366556 low penetrance PMID:26366556 low penetrance PMID:26366556 large fractions of both abnormally long and abnormally short cells are present in the population PMID:26366556 determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c PMID:26366556 determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c PMID:26366556 determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c PMID:26366556 determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c PMID:26366556 determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c PMID:26366556 determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c PMID:26366556 ChIP-seq and microarray data indicate that Cbf11 regulates lipid metabolism genes. PMID:26366556 low penetrance PMID:26368543 Chk1 PMID:26368543 Chk1 PMID:26401015 acetyltransferase normally processive in presence of K4-trimethylated H3 (bound by Sgf29) PMID:26401015 abolishes preference for K4-trimethylated H3 PMID:26401015 acetyltransferase normally processive in presence of K4-trimethylated H3 (bound by Sgf29) PMID:26401015 abolishes preference for K4-trimethylated H3 PMID:26412298 Inferred from in vitro biochemical assay using K11 linked di-ubiquitin substrate PMID:26412298 Inferred from in vitro biochemical assay using K11 linked di-ubiquitin substrate PMID:26412298 Inferred from in vitro biochemical assay using K48-linked di-ubiquitin PMID:26412298 Inferred from in vitro biochemical assay using K63-linked di-ubiquitin PMID:26412298 Inferred from in vitro biochemical assay using K48-linked di-ubiquitin PMID:26412298 Inferred from in vitro biochemical assay using K63-linked di-ubiquitinase (vw JAnel made this annotation , I transferred from process to MF) PMID:26412298 Inferred from in vitro biochemical assay using K63-linked di-ubiquitin PMID:26412298 Inferred from in vitro biochemical assay using K11 linked di-ubiquitin substrate PMID:26412298 Inferred from in vitro biochemical assay using K11 linked di-ubiquitin substrate PMID:26412298 Inferred from in vitro biochemical assay using K11 linked di-ubiquitin substrate PMID:26422458 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 in response to queuosine incorporation into tRNA-Asp PMID:26424849 waiting for go-ontology/issues/12536 PMID:26436826 alkaline DNA preparation PMID:26436826 alkaline DNA preparation PMID:26438724 fig6 PMID:26438724 changed from: heterochromatin organization involved in chromatin silencing PMID:26438724 EV3 PMID:26438724 EV3 PMID:26438724 fig6 PMID:26438724 fig5 PMID:26438724 fig5 PMID:26438724 fig5 PMID:26438724 fig5 PMID:26438724 fig5 PMID:26438724 fig5 PMID:26438724 EV3 PMID:26438724 EV3 PMID:26438724 4a PMID:26438724 4a PMID:26438724 4a PMID:26438724 EV3 PMID:26438724 EV3 PMID:26438724 EV3 PMID:26438724 supp 1b PMID:26438724 supp 1b PMID:26438724 supp 1b PMID:26438724 supp 1b PMID:26438724 changed from: heterochromatin organization involved in chromatin silencing PMID:26443059 actually inferred from protein binding phenotypes PMID:26443059 actually inferred from protein binding phenotypes PMID:26443240 Pom1 does not relocalize to cell sides PMID:26443240 Pom1 relocalizes to cell sides PMID:26443240 Pom1 relocalizes to cell sides PMID:26443240 Pom1 relocalizes to cell sides PMID:26443240 through negative regulation of Cls1 PMID:26443240 Pom1 does not relocalize to cell sides PMID:26443240 Pom1 relocalizes to cell sides PMID:26443240 Pom1 relocalization to cell sides PMID:26443240 Tea4 does not relocalize to cell sides PMID:26443240 Pom1 relocalizes to cell sides PMID:26443240 Pom1 does not relocalize to cell sides PMID:26443240 absent when glucose limited PMID:26443240 Pom1 does not relocalize to cell sides PMID:26443240 Pom1 does not relocalize to cell sides PMID:26443240 Pom1 does not relocalize to cell sides PMID:26443240 Pom1 does not relocalize to cell sides PMID:26483559 fig 9A PMID:26483559 fig 9A PMID:26483559 fig 9A PMID:26483559 fig 9A PMID:26483559 fig 9A PMID:26483559 fig 9A PMID:26483559 (Fig. 1 D) PMID:26483559 fig 9A PMID:26483559 fig 9A PMID:26483559 (Fig. 1 B) PMID:26483559 (Fig. 4, C and D) PMID:26483559 Fig. 3, A and B; Fig. S5 PMID:26483559 Fig 2 PMID:26483559 (Fig. 8, B and C), increased or premature PMID:26483559 (Fig. 6) increased or premature PMID:26483559 fig1b (vw moved down form) abnormal meiotic chromosome segregation PMID:26483559 (Fig. 6) increased or premature PMID:26483559 fig 9A PMID:26483559 (Fig. 1 B) PMID:26483559 fig 9A PMID:26483559 fig 9A PMID:26483559 Fig. S2 PMID:26483559 (Fig. 1 D) PMID:26483559 fig 9A PMID:26483559 fig 9a, there other evidence elsewhere but we don't have this annotation on mad2 at present... PMID:26483559 fig 9A PMID:26483559 fig 9A PMID:26483559 Fig S1. Assayed by assaying depletion of securin from spindle PMID:26483559 (Fig. 7, B and C) PMID:26483559 (Fig. 7 C) PMID:26499799 cerevisiae substrate PMID:26518661 (Figure 7) PMID:26518661 (Figure 1) PMID:26518661 (Figure 2) PMID:26518661 (Figure 2) PMID:26518661 (Figure 2) PMID:26518661 (Figure 2) PMID:26518661 (Figure 2) PMID:26518661 (Figure 2) PMID:26518661 (Figure 2) PMID:26518661 (Figure 2) PMID:26518661 (Figure 2) PMID:26518661 (Figure 4) PMID:26518661 (Figure 4) PMID:26518661 (Figure 4) PMID:26518661 (Figure 7) PMID:26518661 (Figure 7) PMID:26518661 (Figure 7) PMID:26518661 (Figure 7) PMID:26518661 (Figure 7) PMID:26518661 (Figure 7) PMID:26518661 (Figure 7) PMID:26518661 (Figure 7) PMID:26518661 (Figure 7) PMID:26518661 (Figure 7) PMID:26518661 (Figure 7) PMID:26518661 (Figure 7) PMID:26518661 (Figure 7) PMID:26518661 (Figure 1) PMID:26518661 ev4 PMID:26518661 ev4 PMID:26518661 (Figure 2) PMID:26518661 (Figure 2) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) (VW: fixed from normal to decreased -compared to WT) PMID:26518661 (Figure 1) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 5) PMID:26518661 (Figure 4) PMID:26518661 (Figure 4) PMID:26518661 (Figure 4) PMID:26518661 (Figure 1) PMID:26518661 ev4,ef PMID:26518661 (Figure 4) PMID:26518661 (Figure 4) PMID:26518661 (Figure 4) PMID:26518661 (Figure 4) PMID:26518661 (Figure 4) PMID:26518661 (Figure 4) PMID:26518661 (Figure 4) PMID:26518661 (Figure 4) PMID:26518661 (Figure 4) PMID:26518661 (Figure 7) PMID:26518661 (Figure 7) PMID:26518661 (Figure 7) PMID:26518661 (Figure 7) PMID:26518661 (Figure 7) PMID:26518661 (Figure 7) PMID:26527280 Fig. 5C PMID:26527280 Fig. 6G, S7F,G, TUBE pull-down PMID:26527280 Fig. 7D,E (tetrad dissection) PMID:26527280 Fig. S3D PMID:26527280 Fig. S3G,H PMID:26527280 Fig. S3I,J PMID:26527280 Fig. S6D PMID:26527280 Fig. S6L,M PMID:26527280 Fig. 4G,H PMID:26527280 Fig. 1J PMID:26527280 Fig. 1I PMID:26527280 Figure 2A Plo1 to SPBs persisted for more than 20 min PMID:26527280 In contrast, there was only a very slight delay in sister chromatid separation (Figures 2A and 2B). PMID:26527280 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 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 (Figures 3B and 3D). sister chromatid separation (which depends on securin degradation, not on cyclin B degradation) was delayed as well PMID:26527280 (Figure S2F export of CDK1 from the nucleus, which depends on cyclin B degradation ,, was delayed PMID:26527280 Fig. 3A/B PMID:26527280 Fig. 3E/F PMID:26527280 Fig. 4D,E PMID:26527280 (tetrad dioscection) Fig. 7C,E PMID:26527280 (tetrad disection) Fig. 7D,E PMID:26527280 Fig. S2B PMID:26527280 Fig. S3A,B (control for increased proteasome in nucleus) PMID:26527280 Fig. S3A,C PMID:26536126 assayed_using(PomBase:fur4) PMID:26536126 nitrogen rich condition PMID:26536126 uracil uptake enhancement in pub1 deletion PMID:26536126 cell lysis on uracil depleted medium PMID:26536126 inability to take up 14-C uracil in fur4 deletion mutant PMID:26536126 grown in EMM or YES medium PMID:26536126 auxotrophic for cytosine, uridine and UMP PMID:26536126 nitrogen rich condition PMID:26545917 2c PMID:26545917 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 they don't actually use pombe isu1 because they couldn't purify it, but they try both C. thermophilum and S. cerevisiae Isu1 and get similar results & sequence conservation is good to pombe. PMID:26582768 Increased MMS sensitivity PMID:26582768 Increased MMS sensitivity PMID:26582768 SO:0000236 = ORF, SO:0001799=outer repeat, SO:0000186 = LTR retrotransposon PMID:26582768 SO:0000236 = ORF, SO:0001799=outer repeat, SO:0000186 = LTR retrotransposon PMID:26582768 SO:0000236 = ORF, SO:0001799=outer repeat, SO:0000186 = LTR retrotransposon PMID:26582768 SO:0000236 = ORF, SO:0001799=outer repeat, SO:0000186 = LTR retrotransposon PMID:26652183 5 J/m2 UV; duration is similar to rad8delta or rhp18delta single mutants (see Fig. 3G) PMID:26652183 5 J/m2 UV; figure 1B, figure 3D, figure S6 PMID:26652183 5 J/m2 UV; Fig 1A, Fig. S2 PMID:26652183 5 J/m2 UV; Fig. 1B PMID:26652183 5 J/m2 UV; Fig. 1B, Fig. 3E PMID:26652183 5 or 10 J/m2 UV; Fig. 3I, Fig. 4A, Fig. S6 PMID:26652183 5 or 10 J/m2 UV; Fig. 3I, Fig. 4A, Fig. S6 PMID:26652183 5 or 10 J/m2 UV; Fig. 3I, Fig. 4A, Fig. S6 PMID:26652183 5 J/m2 UV; Fig. 3C PMID:26652183 5 or 10 J/m2 UV; Fig. 3I, Fig. 4A, Fig. S6 PMID:26652183 2 or 5 J/m2 UV; Fig. 3F, Fig. S6 PMID:26652183 5 J/m2 UV; Fig. 3D PMID:26652183 5 J/m2 UV; Fig. 3E PMID:26652183 5 J/m2 UV; Fig. 3I, Fig. 4A, Fig. S6 PMID:26652183 5 J/m2 UV; Fig. 3I, Fig. 4A, Fig. S6 PMID:26652183 5 J/m2 UV; Fig. 3B PMID:26652183 5 J/m2 UV; Fig. 3C PMID:26652183 2 or 5 J/m2 UV; Fig. 3F, Fig. S6 PMID:26652183 5 J/m2 UV; duration is similar to eso1-D147N alone (see Fig. 3H) PMID:26652183 5 J/m2 UV; Delay is greater than rad51delta alone (see Fig. S7) PMID:26652183 25 J/m2 UV; delay is greater than rad51delta alone (Fig. 5A) PMID:26652183 5 or 10 J/m2 UV; similar sensitivity to rev1delta and rev3delta single mutants (Fig. 3I, Fig. 4A, Fig. S6) PMID:26652183 5 J/m2 UV; similar sensitivity to eso1-D147N single mutant (Fig. 3H) PMID:26652183 5 J/m2 UV; sensitivity similar to rad8delta and rhp18delta single mutants (Fig. 3G) PMID:26652183 5 J/m2 UV; Fig. S3 PMID:26652183 5 J/m2 UV; Sensitivity is greater than rad51delta or eso1-D147N single mutants (see Fig. S7) PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 increase > 10-fold PMID:26670050 increase > 10-fold PMID:26670050 increase > 40-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 increase > 5-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 gene locus affected: dbp2 PMID:26670050 gene affected: rps2202 PMID:26670050 Fig. S4B PMID:26670050 fig S5e PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 increase > 5-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 SPBC1289.13c PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 increase > 5-fold PMID:26670050 enrichment in CRAC > 10-fold; Mmi1 binds the 5' extended region of the overlapping regulatory lncRNA prt PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 SPCC1235.04c PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 affects unspliced pre-mRNA PMID:26670050 gene locus: rps2202 PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 gene locus affected: rps2202 PMID:26670050 increase > 50-fold PMID:26670050 increase > 10-fold PMID:26670050 increase > 10-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 enrichment in CRAC > 10-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 10-fold PMID:26670050 increase > 10-fold PMID:26670050 increase > 10-fold PMID:26670050 increase > 10-fold PMID:26670050 increase > 10-fold PMID:26670050 increase > 10-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26670050 increase > 5-fold PMID:26687354 (checked) Figure 1C PMID:26687354 (Figure 6C) PMID:26687354 (Figure 6B) acetylated form acts as a DNA sensor PMID:26687354 (Figure 6A) PMID:26687354 (Figure 6A) PMID:26687354 (Figure S4C) PMID:26687354 exit gate opening https://github.com/geneontology/go-ontology/issues/12608 (checked) (Figures 4B and S4A) current extension is part of mitotic cohesin unloading PMID:26687354 figure 3B PMID:26687354 figure 3B PMID:26687354 figure 3B PMID:26687354 (checked) figure 3B PMID:26687354 (checked) figure 3B PMID:26687354 (Figure 2B) PMID:26687354 (Checked) (Figure 2B) (dependent on pds5) PMID:26687354 (fig 2) PMID:26687354 (fig 2) PMID:26687354 (checked) Figure 1C PMID:26687354 (Figure 6C) acetylated form acts as a DNA sensor PMID:26697368 link to GEO dataset- GSE71820 PMID:26697368 link to GEO dataset- GSE71820 PMID:26702831 2c in cos7 PMID:26730850 Fig 3 PMID:26730850 Fig 4 PMID:26730850 Fig 4 PMID:26730850 Fig 4 PMID:26730850 Figure 1D and 2D - examined via RT-PCR Figure 2A examined via RNA-Seq PMID:26730850 Figure 1C transient PMID:26730850 Figure 1D efficiency/ of introns displaying weak splice sites PMID:26730850 Figure 1D efficiency/ of introns displaying weak splice sites PMID:26730850 Figure 1A-1C transient growth arrest PMID:26730850 Figure 3+5 efficiency/ of introns displaying weak splice sites PMID:26730850 Figure 4 efficiency of introns displaying weak splice sites PMID:26730850 Figure 1D PMID:26730850 Figure 1D PMID:26730850 (S1 Fig) PMID:26730850 regulation of efficiency at weak donor PMID:26730850 Fig 3 PMID:26730850 Fig 3 PMID:26730850 Fig 5 PMID:26730850 Fig 5 PMID:26730850 Fig 5 PMID:26730850 Fig 5 PMID:26730850 Fig 5 PMID:26730850 Fig 5 PMID:26730850 Fig 5 PMID:26730850 Fig 5 PMID:26730850 Fig 4 PMID:26730850 Fig 4 PMID:26730850 Fig 4 PMID:26730850 Fig 3 PMID:26730850 Fig 3 PMID:26730850 Fig 3 PMID:26730850 Fig 3 PMID:26730850 Fig 3 PMID:26730850 Fig3 PMID:26730850 Fig 4 PMID:26730850 Fig 3 PMID:26730850 Fig 3 PMID:26730850 Fig 4 PMID:26744419 fig 6e PMID:26744419 fig 6d PMID:26744419 s10 PMID:26744419 fig 1c PMID:26744419 s10 PMID:26744419 5 PMID:26744419 fig 1b PMID:26744419 fig 1b PMID:26744419 fig S1c PMID:26744419 fig 1c PMID:26744419 fig 5c PMID:26744419 Fig 5c PMID:26744419 Fig 4 b & c PMID:26744419 Fig 1c,Fig 4e PMID:26744419 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 Fig 1c SHOULD BRE ORGANIZATION PMID:26744419 fig 1c PMID:26744419 fig 1c PMID:26744419 s5a PMID:26744419 Fig 7b PMID:26744419 Fig 7b PMID:26744419 Fig 7b PMID:26744419 5 PMID:26744419 4e PMID:26744419 fig 3 PMID:26744419 fig 3 PMID:26744419 fig 3 PMID:26744419 fig 3 PMID:26744419 fig 3 PMID:26744419 fig 3 PMID:26744419 fig 3 PMID:26744419 s2 PMID:26744419 s2 PMID:26744419 s2 PMID:26744419 fig 1c PMID:26744419 fig 7 PMID:26744419 fig 7 PMID:26744419 fig S2 PMID:26744419 fig S2 PMID:26744419 fig S2 PMID:26744419 S4 PMID:26744419 4e PMID:26744419 fig 1c PMID:26744419 Fig 5c. parent GO:0003682? PMID:26744419 Fig 5c. parent GO:0003682? PMID:26744419 Fig 7b PMID:26744419 4e PMID:26744419 fig 4 PMID:26744419 fig 4 PMID:26744419 fig 3d PMID:26744419 fig 7 PMID:26744419 fig 3c PMID:26744419 fig 3c PMID:26744419 3b PMID:26744419 3b PMID:26744419 3b PMID:26744419 3b PMID:26744419 fig 7 PMID:26744419 7 PMID:26744419 7 PMID:26744419 7 PMID:26744419 fig 7 PMID:26744419 7 PMID:26744419 1d PMID:26744419 1d PMID:26744419 1d PMID:26744419 1d PMID:26744419 fig S2 PMID:26744419 fig S2 PMID:26744419 fig 1c PMID:26744419 Fig 5b PMID:26744419 Fig 5b PMID:26744419 Fig 5b PMID:26744419 Fig 5b PMID:26744419 fig 5c PMID:26744419 Fig 7b PMID:26744419 Fig 7b PMID:26744419 fig 6a (in combination with csi1∆; phenocopies lem2∆ csi1∆) PMID:26744419 fig 3c PMID:26744419 fig 6e PMID:26744419 s10 PMID:26744419 fig 6e PMID:26744419 fig 6d PMID:26744419 fig 6d PMID:26744419 fig 6d PMID:26744419 fig 6e PMID:26744419 fig 6c PMID:26744419 fig 6c PMID:26746798 fig 1 A PMID:26746798 fig 2 C PMID:26746798 Fig 7B PMID:26746798 Fig 7B PMID:26746798 Fig 7A PMID:26746798 fig 6 PMID:26746798 fig 6 PMID:26746798 fig 6 PMID:26746798 fig 6 PMID:26746798 fig 3C PMID:26746798 fig 3C PMID:26746798 fig 3C PMID:26746798 fig 3C PMID:26746798 fig 3B PMID:26746798 fig 3B PMID:26746798 fig 3B PMID:26746798 fig 3A PMID:26746798 fig 3A PMID:26746798 fig 3A PMID:26746798 fig 2 C PMID:26746798 fig 2 C PMID:26746798 fig 2 C PMID:26746798 fig 2 C PMID:26746798 fig 2 B PMID:26746798 fig 2 B PMID:26746798 fig 2 B PMID:26746798 fig 2 A PMID:26746798 fig 2 A PMID:26746798 fig 2 A PMID:26746798 fig 1 A PMID:26746798 fig 1 A PMID:26746798 fig 1 A PMID:26746798 fig 1 A PMID:26746798 fig 1 A Defect in Checkpoint Signaling. PMID:26746798 fig 1 A PMID:26746798 fig 1 A PMID:26746798 fig 1 A PMID:26749213 figure 1a PMID:26749213 (Fig. 6D); evidence: filipin staining PMID:26749213 moved down drom endocytosis. Delayed FM4-64 uptake when in combination with a clathrin mutationSlow dynamics of endocytic patch markers PMID:26749213 fig 1B PMID:26749213 fig 1B PMID:26749213 figure 1a PMID:26749213 moved down from abnormal protein localization to cell tip (new term) PMID:26749213 fig 1B PMID:26749213 figure 1a PMID:26749213 moved down to new term from :protein mislocalized to cytoplasm during vegetative growth PMID:26749213 moved down to new term from :protein mislocalized to cytoplasm during vegetative growth PMID:26749213 fig 2 d PMID:26749213 (Fig. 3B–D) (Fig. 4A and movies 3 and 4) slow dynamics of actin patch components: Sla1, wsc1, arc5, Crn1 PMID:26749213 fig 2 D PMID:26749213 (Supporting Information Fig. S4A) PMID:26749213 FM4-64 uptake (I made Henars original annotation into a double mutant so the attribution has changed) PMID:26749213 fig 7b PMID:26749213 fig 1c PMID:26749213 Fig. S2C PMID:26749213 fig 1B PMID:26749213 fig. S2 A&B PMID:26749213 fig 1B PMID:26749213 fig 1B PMID:26776736 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 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:26776736 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 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 important when growing on poor nitrogen sources PMID:26804021 fig 3 B PMID:26804021 fig 1a. AND fig 4 (knob) PMID:26804021 fig 5 PMID:26804021 fig 5 PMID:26804021 fig 5A PMID:26804021 fig 5A PMID:26804021 fig 5 PMID:26804021 fig 5 PMID:26804021 fig 5 C PMID:26804021 Fig. 7a PMID:26804021 Fig. 7b increased occurance PMID:26804021 fig 5 PMID:26804021 fig 5 PMID:26804021 fig 4c PMID:26804021 fig 3 D PMID:26804021 fig 1a PMID:26804021 fig 5A PMID:26804021 fig 4c PMID:26804021 fig 4 PMID:26804021 fig 3 B PMID:26804021 fig 3 B PMID:26804021 fig S6 check allele???? PMID:26804917 Serine 481 is phosphorylated by Cig2/Cdc2 during meiosis I. Phosphorylation decreases Fkh2 DNA binding affinity PMID:26804917 EMSA fig4 PMID:26804917 EMSA fig4 PMID:2682257 Fig6aC. Cells contain cdc2-F19 mutant on multi copy LEU2+ plasmid. PMID:2682257 Fig6b C-F. Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid. PMID:2682257 Fig6b C-F. Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid. PMID:2682257 Fig 6b C-F. Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid. PMID:2682257 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 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 Fig6bB. Cells contain cdc2-F19 mutant on multi copy LEU2+ plasmid. PMID:2682257 Fig6a B. Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid. PMID:2682257 Data not shown assayed by colony growth on plates PMID:2682257 Fig6b C-F. Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid. PMID:26869222 cells grown at 29°C for 6 hours in 30µM Cutin-1 PMID:26869222 cells grown at 29°C for 6 hours in 30µM Cutin-1 PMID:26869222 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 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 Growth was assayed in presence of 10µM Cutin-1. PMID:26869222 +10µM Cutin-1 PMID:26869222 cells grown at 29°C for 6 hours in 30µM Cutin-1 PMID:26869222 Cells show partial resistance to 30µM Cutin-1 for 6 hours. PMID:26869222 cells grown at 29°C PMID:26869222 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 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 cells grown at 29°C for 6 hours in 30µM Cutin-1 PMID:26869222 Cells grown at 29°C PMID:26869222 cells grown at 29°C for 6 hours in 30µM Cutin-1 PMID:26869222 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 Cells show increased mitotic chromosome segregation defects in presence of Cutin-1 PMID:26869222 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 cells grown at 29°C for 6 hours in 30µM Cutin-1 PMID:26869222 cells grown at 29°C for 6 hours in 30µM Cutin-1 PMID:26877082 Figures 1A, S1A, S1B, 1D, S1E medial ring assembly PMID:26877082 Figures 1A, S1A, S1B, 1D, S1E PMID:26877082 Figures 2 PMID:26877082 Figure Figure S4C PMID:26877082 Figure 4A PMID:26877082 Figure 2D abnormal cable clusering PMID:26877082 Figure 2D (single clump!) condensation PMID:26877082 Figures 2C PMID:26877082 Figure 2D (single clump!) condensation PMID:26882497 "they don't show the ""added during"" data so this is a bit anectdotal from the text" PMID:26882497 2b PMID:26882497 text to fig2 PMID:26882497 3 E2s mixed in the same assay so can't specify a substrate PMID:26882497 Fig6 they incubate with 3 different E2s so can't specify a substrate PMID:26882497 2bc,5 PMID:26882497 5a PMID:26882497 5a PMID:26882497 5a PMID:26882497 5a PMID:26882497 5a PMID:26882497 "they don't show the ""added during"" data so this is a bit anectdotal from the text" PMID:26882497 "they don't show the ""added during"" data so this is a bit anectdotal from the text" PMID:26882497 2a 20 mins after synchronized released into mitosis. I wouldn't want to guess exactly what stage of mitosis this is PMID:26882497 1d PMID:26882497 5a PMID:26882497 text to fig2 PMID:26882497 4a PMID:26882497 4a PMID:26882497 2bc,5 PMID:26882497 1d PMID:26882497 2bc PMID:26882497 2bc,5 PMID:26882497 Fig S4A and 2C PMID:26882497 Fig S4A and 2C PMID:26882497 it looks like it is involved in MAINTAINING the checkpoint, fig S4A and 2C PMID:26882497 1d PMID:26882497 2bc PMID:26882497 "they don't show the ""added during"" data so this is a bit anectdotal from the text" PMID:26882497 2bc,5 PMID:26882497 S3 PMID:26882497 S3 PMID:26882497 S3 PMID:26882497 S3 PMID:26882497 in text relevant to fig1 PMID:26882497 1b PMID:26882497 "they don't show the ""added during"" data so this is a bit anectdotal from the text" PMID:26882497 1b PMID:26882497 "they don't show the ""added during"" data so this is a bit anectdotal from the text" PMID:26882497 "they don't show the ""added during"" data so this is a bit anectdotal from the text" PMID:26882497 "they don't show the ""added during"" data so this is a bit anectdotal from the text" PMID:26882497 in text relevant to fig1 PMID:26882497 1a - they don't really show that the modification is phosphorylation, but considering the rest of the data this annotation seems ok. PMID:26882497 in text relevant to fig1 PMID:26882497 in text relevant to fig1 PMID:26882497 2b PMID:26890608 cellular response to HU = GO:0072711 PMID:26891792 Fig. 5 PMID:26891792 Fig. 4 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 4 PMID:26891792 Fig. 4 PMID:26891792 Fig. 5 PMID:26891792 Fig. 5 PMID:26891792 Fig. 5 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 1 PMID:26891792 Fig. 3 PMID:26891792 Fig. 4 PMID:26891792 Fig. 4 PMID:26891792 Fig. 5 PMID:26891792 Fig. 4 PMID:26891792 Fig. 1 PMID:26891792 Fig. 4 PMID:26891792 Fig. 4 PMID:26891792 Fig. 4 PMID:26900649 "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 exists during veg growth & glucose starv & HU stress PMID:26912660 exists during veg growth & glucose starv & HU stress PMID:26912660 exists during veg growth & glucose starv & HU stress PMID:26941334 localization dependent on actin cytoskeleton PMID:26942678 Erh1 localizes with Mmi1 both during mitotic cell cycle and meiosis PMID:26942678 some up some down PMID:26942678 some up some down PMID:26942678 author statement PMID:26960792 can't assess viability PMID:26960792 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 RhoGAP, GTPase activating protein for Cdc42 and Rho2 PMID:26960792 hard to be more specific when cell shape is also abnormal (Rga6 normally goes to lateral cortex & non-growing tip) PMID:26960792 can't assess viability PMID:26960792 can't assess viability PMID:26960792 can't assess viability PMID:26960792 can't assess viability PMID:26960792 can't assess viability PMID:26960792 can't assess viability PMID:26990381 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 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 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 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 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 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 As expected, these cells contained negligible amounts of TAG after lysis and TLC analysis (Figure 3K). PMID:26990381 mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B). PMID:26990381 mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B). PMID:26990381 mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B). PMID:26990381 mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B). PMID:26990381 mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B). PMID:26990381 analysis revealed that both strains had reduced whole-cell and lipid droplet TAG levels (Figure 3F,I). PMID:26990381 analysis revealed that both strains had reduced whole-cell and lipid droplet TAG levels (Figure 3F,I). PMID:26990381 analysis revealed that both strains had reduced whole-cell and lipid droplet TAG levels (Figure 3F,I). PMID:26990381 analysis revealed that both strains had reduced whole-cell and lipid droplet TAG levels (Figure 3F,I). PMID:26990381 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 The same cells were not viable when grown in YPO (Figure S2B,C). PMID:26990381 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:27023709 fig 2 H, cell free system PMID:27023709 fig. 2i PMID:27023709 fig 2 H, cell free system PMID:27023709 fig 2 H, cell free system PMID:27023709 fig 2 H, cell free system PMID:27023709 fig. 2i PMID:27023709 fig. 2i PMID:27023709 fig 2 H, cell free system PMID:27069798 Bundling activity inferred from pull-down experiments as well as from fluorescence microscopy PMID:27075176 (Figure 3A and Supplemental Video 3). PMID:27075176 6C PMID:27075176 6C PMID:27075176 6C PMID:27075176 (Figure 1, C and D). PMID:27075176 6C PMID:27075176 mixed orientations PMID:27075176 6C PMID:27075176 6C PMID:27082518 Fig 7E PMID:27082518 Fiig 6 AB PMID:27082518 fig 6c PMID:27082518 fig 6 AB PMID:27082518 fig 1 C-E PMID:27082518 fig 1 C-E PMID:27082518 fig 1 B PMID:27082518 fig 2H, 7A PMID:27082518 Fig 3B PMID:27082518 Fig 3B PMID:27082518 Fig S 3 B PMID:27082518 fig 5a PMID:27082518 fig 6 AB PMID:27082518 fig 6 AB PMID:27082518 Figure S4D PMID:27082518 Fig 6E PMID:27082518 Fig 6E PMID:27082518 Fig 6E PMID:27082518 Fig S4E PMID:27082518 Fig S4F and S4G PMID:27082518 fig 7A PMID:27082518 fig 7C/D PMID:27082518 fig 7C/D PMID:27082518 fig 7D PMID:27082518 Fig 7E PMID:27082518 Fig 7E PMID:27082518 Fig S6A PMID:27082518 Fig S6A PMID:27082518 Fig S6 B probably due to delayed fusion of TRAPP containing vesicles with PM PMID:27082518 Fig S6 C probably due to delayed fusion of TRAPP containing vesicles with PM PMID:27098497 same as rhp6delta alone PMID:27098497 worse than without rqh1delta PMID:27098497 same as without exo1delta PMID:27098497 distal to break point PMID:27098497 same as without exo1+ overexpression PMID:27098497 same as without htb1-K119R PMID:27098497 same as rhp6delta alone PMID:27098497 same as without exo1delta PMID:27098497 same as without csn1delta PMID:27098497 same as without csn5delta PMID:27101289 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 binds with high affinity to diverged S. pombe telomeric repeats PMID:27146110 Figure 7 &1 PMID:27146110 Figure 7 PMID:27146110 Figure 7 PMID:27146110 Figure 1, 2 PMID:27146110 Figure 7 PMID:27146110 ***DELAYED Figure 7 PMID:27146110 DELAYED Figure 7 PMID:27146110 Figure 2 PMID:27146110 Figure 2 PMID:27146110 Figure 3 PMID:27146110 Figure 3 PMID:27146110 Figure 4 PMID:27146110 Figure 4 PMID:27146110 Figure 2 PMID:27146110 Figure 2 PMID:27146110 Figure 8 (anaphase B) PMID:27146110 Figure 8 PMID:27146110 Figure 8 PMID:27146110 Figure 7 PMID:27146110 *****The definition of this term is not right Figure 2 PMID:27146110 *****The definition of this term is not right Figure 2 PMID:27146110 Figure 2 PMID:27146110 Figure 2 PMID:27146110 Figure 2 PMID:27146110 Figure 1, 2 PMID:27146110 Figure 1, 2 PMID:27146110 Figure 1, 2 PMID:27146110 ********Sensitive to cold shock Table 1 PMID:27146110 Figure 1, 2 PMID:27146110 ********Sensitive to cold shock Table 1 PMID:27146110 ********Sensitive to cold shock Table 1 PMID:27146110 ********Sensitive to cold shock Table 1 PMID:27146110 Figure 5 PMID:27146110 Figure 5 PMID:27146110 Figure 5 PMID:27146110 Figure 5 PMID:27146110 Figure 6 PMID:27146110 Figure 6 PMID:27146110 Figure 6 PMID:27146110 Figure 6 PMID:27151298 K63-ubiquitin chain from 3 to 8 ubiquitin molecules PMID:27151298 K63-diubiquitin chain PMID:27151298 K63-ubiquitin chain from 3 to 8 ubiquitin molecules PMID:27151298 Ubp2 is inhibited by hydrogen peroxide PMID:27151298 Delete K63-ubiquitin chains from 3 to 8 ubiquitins PMID:27151298 K63-diubiquitin chain PMID:27168121 Figure 3C PMID:27168121 Figure 3E PMID:27168121 Figure 3D PMID:27168121 Figure 3C PMID:27168121 Figure 3B PMID:27168121 Figure 3B PMID:27168121 fig 1b PMID:27168121 fig 1 b PMID:27168121 Fig 1 C PMID:27183912 can't distinguish tlh1 and tlh2 as identical sequences hence comma separated; assayed_using(PomBase:tlh1),assayed_using(PomBase:tlh2) PMID:27183912 comma separated extension as can't distinguish transcipts (identical seq) PMID:27188733 says increased proportion, which is a synonym PMID:27191590 Fig 7C PMID:27191590 Fig 7C PMID:27191590 Fig 1C, Fig 4 PMID:27191590 Fig 4D PMID:27191590 Fig 6E-G PMID:27191590 Fig 1B PMID:27191590 Fig 5A PMID:27191590 Fig 1C, Fig 6C, Fig 7C, Fig S5 PMID:27191590 Fig 4E PMID:27191590 Fig 6C PMID:27191590 Fig 6B PMID:27191590 Fig 6D PMID:27191590 Fig 1C, Fig 4 PMID:27191590 happens during cellular resposne to BFA Fig 3A, Fig 4A-B, Fig 5B, Fig S3 PMID:27191590 Fig 6C PMID:27191590 Fig 6C PMID:27191590 Fig 6B PMID:27191590 Fig 6C PMID:27194449 of human pyruvyltransferase activity for the LacNAc-pNP PMID:27194449 of human pyruvyltransferase activity for the LacNAc-pNP PMID:27325741 temperature permissive for ts cdc17-K42 PMID:27325741 temperature permissive for ts cdc17-K42 PMID:27325741 temperature permissive for ts cdc17-K42 PMID:27327046 I changed the evidence from IDA to IMP /AL PMID:27327046 fig S2 & 3 PMID:27327046 Figures 2 and 3A, B PMID:27327046 fig S2 & 3 PMID:27327046 fig S2 & 3 PMID:27327046 fig S2 & 3 PMID:27327046 Expression of fex1 from a plasmid in fex1Del/fex2Del double deletion mutant rescues fluoride sensitivity. PMID:27327046 I changed the evidence from IDA to IMP /AL PMID:27327046 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:27334362 fig 3 c PMID:27334362 (Fig. 2D) additive PMID:27334362 Fig. 2D PMID:27334362 fig 9A PMID:27334362 Fig 8B/tableB PMID:27334362 Fig 8B/tableB PMID:27334362 Fig 8B/tableB PMID:27334362 fig 9 D PMID:27334362 fig 9 D PMID:27334362 fig 9 D PMID:27334362 Fig. 2D PMID:27334362 fig 9D PMID:27334362 fig 7 B PMID:27334362 fig 7 B PMID:27334362 fig 6b PMID:27334362 fig 3 c PMID:27334362 fig 3 c split into decreased at outer, abolished at inner (val) PMID:27334362 fig 2D PMID:27334362 fig 2a PMID:27334362 Fig. 2B PMID:27334362 Fig. 2C) PMID:27334362 fig 1A PMID:27334362 fig 1a PMID:27334362 Fig. 3A,B changed from CENP-A containing nucleosome (val) PMID:27334362 Fig. 3C (made this specific for inner and added decreased at outer) PMID:27334362 Fig3 D, added assayed genes, vw PMID:27334362 fig 3 c split into decreased at outer, abolished at inner (val) PMID:27334362 Fig3 D, added assayed genes, vw PMID:27334362 Fig3 D, added assayed genes, vw PMID:27334362 fig3 c PMID:27334362 fig 3 c PMID:27334362 fig 3 c PMID:27350684 conditional synthetic lethal with rna14-11 PMID:27350684 splicing of rad21, nda3 and mad2 is also affected PMID:27350684 splicing of rad21, nda3 and mad2 is also affected PMID:27350684 splicing of rad21, nda3 and mad2 is also affected PMID:27350684 splicing of rad21, nda3 and mad2 is also affected PMID:27385337 table 1 PMID:27385337 table 1 PMID:27385337 table 1 PMID:27385337 table 1 PMID:27385337 table 1 PMID:27385337 table 1 PMID:27385337 table 1 PMID:27385337 table 1 PMID:27385337 figure 5 d/ figure 6 PMID:27385337 table 1, fig 3 C PMID:27385337 Supplemental Figure S4F and Table 2 PMID:27385337 Supplemental Figure S4B PMID:27385337 figure 4 G (localizes as a dot rather than a disk) PMID:27385337 fig 3 C PMID:27385337 fig 3 C PMID:27385337 Figure 1F PMID:27385337 figure 4 G PMID:27385337 fig5a PMID:27385337 figure 5 d/ figure 6 PMID:27385337 fig 3 C PMID:27385337 Figure 3 F PMID:27385337 figure 3 F PMID:27385337 figure 3 F PMID:27385337 figure 3 F PMID:27385337 Figure 4 F PMID:27385337 fig 5 a PMID:27385337 figure 3 F PMID:27385337 table 1 PMID:27385337 table 1 PMID:27385337 figure 3 F PMID:27385337 figure 3 F PMID:27388936 fig 5 b PMID:27388936 fig 8a PMID:27388936 fig 8a PMID:27388936 fig 8c PMID:27388936 fig 8c PMID:27388936 fig 5 a PMID:27388936 fig 5 a PMID:27398807 30 degrees; semi-permissive for slx8-29 PMID:27398807 30 degrees; semi-permissive for slx8-29 PMID:27398807 30 degrees; semi-permissive for slx8-29 PMID:27398807 30 degrees; semi-permissive for slx8-29 PMID:27398807 30 degrees C PMID:27398807 30 degrees C PMID:27398807 30 degrees C PMID:27398807 30 degrees C PMID:27398807 30 degrees; semi-permissive for slx8-29 PMID:27398807 30 degrees; semi-permissive for slx8-29 PMID:27398807 30 degrees; semi-permissive for slx8-29 PMID:27398807 30 degrees; semi-permissive for slx8-29 PMID:27398807 30 degrees; semi-permissive for slx8-29 PMID:27398807 30 degrees; semi-permissive for slx8-29 PMID:27398807 30 degrees; semi-permissive for slx8-29 PMID:27398807 30 degrees; semi-permissive for slx8-29 PMID:27398807 30 degrees; semi-permissive for slx8-29 PMID:27398807 30 degrees; semi-permissive for slx8-29 PMID:27398807 30 degrees; semi-permissive for slx8-29 PMID:27398807 30 degrees; semi-permissive for slx8-29 PMID:27398807 30 degrees; semi-permissive for slx8-29 PMID:27401558 ChIP at rps2 gene PMID:27401558 ChIP at rps2 gene PMID:27401558 ChIP at rps2 gene PMID:27401558 ChIP at rps2 gene PMID:27401558 ChIP at rps2 gene PMID:27401558 ChIP at rps2 gene PMID:27444384 through conserved cysteines PMID:27451393 Fig. 1A PMID:27451393 Fig. 1A PMID:27451393 DNS PMID:27451393 DNS PMID:27451393 Fig. 4, A and B PMID:27451393 Fig. G PMID:27451393 Fig. 1B, D, E PMID:27451393 Fig. 1B, D, E PMID:27451393 Fig. 3E PMID:27451393 fig 5A PMID:27451393 fig 5A PMID:27451393 Fig. 5, C and D PMID:27451393 Fig. 3E PMID:27451393 Fig. 5, C and D PMID:27451393 Fig. 3, A–D PMID:27451393 Fig. 3, A–D PMID:27451393 Fig. 2, B and C Fig. 2, D and E PMID:27451393 Fig. 2, F and G PMID:27451393 Fig. G PMID:27548313 VW: I changed Ken-Ichi BP annotation to phenotype (Kenichi comment mitotic defects mitotic defects caused by ace2 deletion) PMID:27548313 VW: I changed Ken-Ichi BP annotation to phenotype (Kenichi comment mitotic defects mitotic defects caused by eng1 deletion) PMID:27548313 VW: I changed Ken-Ichi BP annotation to phenotype (Kenichi comment mitotic defects mitotic defects caused by 343.20 deletion) PMID:27558664 affecting sua1 affecting cys11 affecting met14 PMID:27558664 affecting sua1 affecting cys11 affecting met14 PMID:27558664 affecting sua1 affecting cys11 affecting met14 PMID:27558664 affecting sua1 affecting cys11 affecting met14 PMID:27558664 affecting gst2 PMID:27558664 affecting gst2 PMID:27558664 affecting gst2 PMID:27558664 affecting sua1 affecting cys11 affecting met14 PMID:27558664 affecting sua1 affecting cys11 affecting met14 PMID:27558664 affecting sua1 affecting cys11 affecting met14 PMID:27558664 affecting sua1 affecting cys11 affecting met14 PMID:27558664 affecting sua1 affecting cys11 affecting met14 PMID:27587357 (vw: inferred from cell wall galactomannan defects) PMID:27587357 fig1 PMID:27587357 deleted in error, added back PMID:27587357 Fig 3 PMID:27587357 Fig 3 PMID:27587357 Fig 3 PMID:27587357 fig1d PMID:27587357 (vw: inferred from cell wall galactomannan defects) PMID:27587357 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 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 fig1d PMID:27587357 Fig 3 PMID:27587357 deleted in error, added back PMID:27587357 deleted in error, added back PMID:27587357 deleted in error, added back PMID:27587357 deleted in error, added back PMID:27587357 deleted in error, added back PMID:27587357 Fig 3 PMID:27587357 Fig 3 PMID:27587357 Fig 3 PMID:27587357 Fig 3 PMID:27587357 Fig 3 PMID:27587357 Fig 3 PMID:27587357 Fig 3 PMID:27587357 deleted in error, added back PMID:27611590 assayed Cdc20 recruitment PMID:27611590 assayed Cdc20 recruitment PMID:27611590 assayed Cdc20 recruitment PMID:27611590 assayed Cdc20 recruitment PMID:27613427 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 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 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 (Figure 2B) PMID:27618268 fig 2D PMID:27618268 (Figure 2A) PMID:27618268 (Figure 2A) PMID:27618268 fig 1D PMID:27618268 fig 1D PMID:27618268 fig 1B PMID:27618268 fig 1B PMID:27618268 fig 1B PMID:27618268 fig 1B PMID:27618268 fig 1B PMID:27618268 fig 1B PMID:27618268 fig 1A PMID:27618268 fig 1A PMID:27618268 fig 1A PMID:27618268 fig 1A PMID:27618268 fig 1A PMID:27618268 fig 1A PMID:27618268 fig 2E PMID:27618268 Figure 2E (how is this abnormal? i got confused here) PMID:27618268 Figure 2D PMID:27618268 fig 3C PMID:27618268 fig 3C PMID:27618268 fig 3C PMID:27618268 Figure S3E PMID:27618268 Figure S3E PMID:27618268 Figure S3E PMID:27618268 Figures 4B and S4A PMID:27618268 Figures 4B and S4A PMID:27618268 (Figures 4C and S4B). non kinetochore bound PMID:27618268 (Figures 4C and S4B). non kinetochore bound PMID:27618268 ((Figure S4C)). non kinetochore bound PMID:27618268 Together, these data indicate that Mph1 (Mps1) kinase and Dis2 (PP1) phosphatase antagonistically regulate the interaction of Mad1 and Mad2 with Bub1 in fission yeast, most likely through phosphorylation of the conserved central motif of Bub1. PMID:27627185 (unphosphorylated form of tif211) inhibited by stress-inducedphosphorylation of Ser51 in the a subunit of eIF2(tif211) PMID:27627185 (unphosphorylated form of tif211) PMID:27630265 (Figure 8A) PMID:27630265 (Supplemental Figure S10A) PMID:27630265 (Supplemental Figure S11B) PMID:27630265 (Supplemental Figure S11B) PMID:27630265 localizations at spindle poles during meiotic anaphase I (Figure 6, Supplemental Figure S6) PMID:27630265 Figure 6, Supplemental Figure S6 PMID:27630265 localizations at spindle poles during meiotic anaphase I (Figure 6, Supplemental Figure S6) PMID:27630265 Figure 1 PMID:27630265 Figure 1, Supplemental Figure S1 PMID:27630265 in vegetative cells (Supplemental Figure S10); PMID:27630265 (Supplemental Figure S10A) PMID:27630265 (Figure 8A) PMID:27630265 Figure 6A and Supplemental Figure S3) PMID:27630265 upplemental Figure S5A PMID:27630265 Sec2 interacted with specifically with GTP- bound forms of Ypt3 (Figure 7, Supplemental Figure S8). PMID:27630265 (Figure 8A) PMID:27630265 localizations at spindle poles during meiotic anaphase I (Figure 6, Supplemental Figure S6) PMID:27630265 in sporulating cells (Figure 9, Supplemental Figure S9) (Supplemental Figure S10) PMID:27630265 during meiosis (Figure 5, Supplemental Figure S4) PMID:27630265 localizations at spindle poles during meiotic anaphase I (Figure 6, Supplemental Figure S3) PMID:27630265 Figure 4, 5 PMID:27630265 Figure 4, 5, Supplemental Figure S4 PMID:27630265 initiation of forespore membrane delayed (Figure 3, Table 2) PMID:27630265 Figure 8, Supplemental Figure S9 PMID:27630265 Figure 2 PMID:27630265 from metaphase II to postmeiosis (Figure 2) PMID:27630265 Figure 1 and Supplemental Figure S1 PMID:27630265 Spo13 interacted with both GTP- and GDP-bound forms of Ypt3 (Figure 7, Supplemental Figure S8). PMID:27630265 upplemental Figure S5A PMID:27630265 Figure 6A and Supplemental Figure S3) PMID:27630265 upplemental Figure S5A PMID:27630265 Figure 5C, Supplemental Figure S4B PMID:27630265 Figure 1 PMID:27630265 Figure 1 PMID:27630265 Supplemental Figure S12 PMID:27630265 (Supplemental Figure S11) PMID:27630265 Supplemental Figure S11 PMID:27630265 Supplemental Figure S11 PMID:27630265 (Supplemental Figure S10A) PMID:27648579 substrate: bulk histone octamers PMID:27648579 substrate: recombinant mono-nucleosomes PMID:27648579 not increased (relative to wild type Hht3+/Clr4+) as with hht3-K9M alone PMID:27648579 not increased (relative to wild type Hht3+/Clr4+) as with hht3-K9M alone PMID:27655872 "Fig 2B, lanes ""Sre1 cleavage defect under low oxygen""" PMID:27655872 Fig 1E PMID:27655872 Fig 2C PMID:27655872 Fig 2C PMID:27655872 Western blot analysis show Sre1 cleavage defect under low oxygen PMID:27655872 Western blot analysis show Sre1 cleavage defect under low oxygen PMID:27655872 Western blot analysis show Sre1 cleavage defect under low oxygen PMID:27655872 Fig 8C 8D Western blot analysis show Sre1 cleavage defect under low oxygen PMID:27655872 Fig 8C 8D Western blot analysis show decreased Sre1 cleavage activation under low oxygen PMID:27655872 Fig 2A PMID:27655872 Fig 2A PMID:27655872 Fig 2A PMID:27655872 "Fig 2B, lanes ""Sre1 cleavage defect under low oxygen""" PMID:27655872 Fig 2B, lanes 5–13 PMID:27655872 Fig 2D, lane 3 PMID:27655872 Fig 2G, lanes 10– 12 PMID:27655872 Fig 2G, lanes 6–8 PMID:27655872 Fig 3A, lane 4 both cleavage products PMID:27655872 Fig 3A, lane 3 PMID:27655872 Fig 3A, lane 3 PMID:27655872 Fig 3D, compare lanes 3 and 4 PMID:27655872 Fig 3D, PMID:27655872 Fig 3D, PMID:27655872 Fig 3D, PMID:27655872 Fig 3D, compare lanes 3 and 4 PMID:27655872 Figure 3 D PMID:27655872 PRECURSOR Figure 3 E PMID:27655872 Fig 3E and Figure 3 D PMID:27655872 Fig 3E and Figure 3 D PMID:27655872 PRECURSOR Fig 5D and F (4.5 fold) PMID:27655872 PRECURSOR Fig 5E and F PMID:27655872 PRECURSOR Fig 5E and F PMID:27655872 PRECURSOR Fig 5E and F PMID:27655872 PRECURSOR Fig 5E and F PMID:27655872 PRECURSOR Fig 5E and F PMID:27655872 PRECURSOR Fig 5E and F PMID:27655872 PRECURSOR Fig 5E and F PMID:27655872 Fig 5E and F PMID:27655872 fig 6 B PMID:27655872 fig 6 B PMID:27655872 fig 6 B PMID:27655872 fig 6 B PMID:27655872 Fig 7A, lanes 4–6 PMID:27655872 Fig 7A, lanes 4–6 PMID:27655872 Fig 8A PMID:27655872 Fig 8 PMID:27655872 Fig 8A PMID:27655872 Fig 8 PMID:27655872 Fig 9A PMID:27655872 Fig 9A PMID:27655872 Fig 9A PMID:27655872 Fig 9A PMID:27655872 Fig 3A, lane 4 both cleavage products PMID:27664110 text PMID:27664110 text PMID:27664110 text PMID:27664110 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 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 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 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 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 3 PMID:27664110 3 PMID:27664110 3 PMID:27664110 2 PMID:27664110 2 PMID:27664110 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 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 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 1c PMID:27664222 Fig- ure 3A PMID:27664222 Fig- ure 3A PMID:27664222 Fig- ure 3A PMID:27664222 Fig- ure 3A PMID:27664222 detoxification of thiol disulphide (in response to disulphide stress) PMID:27664222 detoxification of thiol disulphide (in response to disulphide stress) PMID:27664222 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 Supplementary Figure S1B PMID:27664222 Supplementary Figure S1B PMID:27664222 Supplemen- tary Figure S3A NaCl or KCl) PMID:27664222 Supplemen- tary Figure S3A PMID:27664222 Figure 2A PMID:27664222 Figure 2A PMID:27664222 Fig- ure 3A PMID:27664222 Fig- ure 3A PMID:27664222 Fig- ure 3A PMID:27664222 Fig- ure 3A PMID:27664222 Fig- ure 3A PMID:27664222 diamide-induced promoters PMID:27664222 Figure 5A PMID:27664222 Figure 5A PMID:27664222 Figure 5A PMID:27664222 detoxification of thiol disulphide (in response to disulphide stress) PMID:27664222 Fig- ure 3A PMID:27664222 Fig- ure 3A PMID:27664222 Fig- ure 3A PMID:27664222 Fig- ure 3A PMID:27664222 Fig- ure 3A PMID:27664222 Fig- ure 3A PMID:27664222 Fig- ure 3A PMID:27664222 Fig- ure 3A PMID:27666591 7F PMID:27666591 Figure 3A PMID:27666591 Figures 2D and S3B PMID:27666591 Figure 2D PMID:27666591 Figures 1F and S2B PMID:27666591 Figures S2A and S2B PMID:27666591 Figures S1A and S1B PMID:27666591 Figure 1A. Figures S1C–S1E PMID:27666591 Fig- ure 7D PMID:27666591 Figure 7C) PMID:27666591 Figure 2A PMID:27666591 Figures 2B and 2C PMID:27666591 Figure 1B Figure S1F PMID:27666591 Figure 1B Figure S1F PMID:27666591 Figure S1F PMID:27666591 Figure S1G PMID:27666591 VW: added exists_during.. PMID:27666591 not sure if this is quite right PMID:27666591 Figure 5C PMID:27666591 Figure 5C PMID:27666591 Figure 7B PMID:27666591 7e PMID:27666591 Figure 4C PMID:27666591 Figure S5B) PMID:27666591 Figure 4D PMID:27666591 Figure 5A PMID:27666591 Figure 5B PMID:27666591 Figure 5C PMID:27666591 Figure 5A PMID:27687771 target genes: cut6, vht1, bio2 PMID:27687771 target genes: cut6, vht1, bio2 PMID:27687771 target genes: cut6, vht1, bio2 PMID:27687771 at cut6 gene promoter PMID:27687771 target genes: cut6, vht1, bio2 PMID:27687866 acetaldehyde absent PMID:27687866 acetaldehyde absent PMID:27687866 acetaldehyde absent PMID:27697865 fig 6E PMID:27697865 fig 1A PMID:27697865 vw: changed to increased activation, and D333A allele (as compared to WT) PMID:27697865 fig 5c PMID:27697865 fig5 PMID:27697865 6E PMID:27697865 fig 6E PMID:27697865 (anaphase) PMID:27697865 Fig. PMID:27697865 fig6A PMID:27697865 fig6 fig 7 PMID:27697865 Fig. PMID:27697865 fig 5c PMID:27697865 Fig. S4 PMID:27697865 fig4E PMID:27697865 fig4 PMID:27729451 replced GO:1990601 (which acts on ss DNA) PMID:27736299 Fig1. 11.63% longer than control mean PMID:27736299 Fig3. Nup189 level reduced to ~50% decreased protein level in heterozygous diploid cell during vegetative growth PMID:27736299 Fig3. Cdr1 level reduced to ~55% decreased protein level in heterozygous diploid cell during vegetative growth PMID:27736299 Fig1. 10.81% longer than control mean PMID:27736299 Fig3. Sal3 level reduced to ~48% decreased protein level in heterozygous diploid cell during vegetative growth PMID:27736299 Fig1. 8.80% longer than control mean PMID:27736299 Fig3. nup45 level reduced to ~45% decreased protein level in heterozygous diploid cell during vegetative growth PMID:27736299 Fig1. 8.78% longer than control mean PMID:27736299 Fig3. Cpc2 level reduced to about 55% decreased protein level in heterozygous diploid cell during vegetative growth PMID:27736299 Fig1. 8.74% longer than control mean PMID:27736299 Fig1. 9.10% shorter than control mean PMID:27736299 Fig3. Ppa2 reduced to~45% decreased protein level in heterozygous diploid cell during vegetative growth PMID:27736299 Fig3. Suc1 level reduced to ~60% decreased protein level in heterozygous diploid cell during vegetative growth PMID:27736299 Fig3. Pom1 level reduced to ~55% decreased protein level in heterozygous diploid cell during vegetative growth PMID:27736299 Fig1. 11.15% shorter than control mean PMID:27736299 Fig3 Wee1 level reduced to ~32% decreased protein level in heterozygous diploid cell during vegetative growth PMID:27736299 Fig1. 16.50% shorter than control mean PMID:27736299 Fig1. 10.86% shorter than control mean PMID:27736299 Fig1. 31.94% longer than control mean PMID:27736299 Fig3. Dea2 level reduced to 50% PMID:27736299 Fig1. 23.46% longer than control mean PMID:27736299 Fig3. Nup184 level reduced to 30% decreased protein level in heterozygous diploid cell during vegetative growth PMID:27736299 Fig1. 19.29% longer than control mean PMID:27736299 Fig3. Nsp1 level reduced to ~45% decreased protein level in heterozygous diploid cell during vegetative growth PMID:27736299 Fig1. 18.92% longer than control mean PMID:27736299 Fig3 Nup97 level reduced to ~55% decreased protein level in heterozygous diploid cell during vegetative growth PMID:27736299 Fig1. 16.78% longer than control mean PMID:27736299 Fig3. cdc13 level reduced to ~44% decreased protein level in heterozygous diploid cell during vegetative growth PMID:27736299 Fig1. 15.82% longer than control mean PMID:27736299 Fig3. Nup186 level reduced to ~45% decreased protein level in heterozygous diploid cell during vegetative growth PMID:27736299 Fig1. 15.55% longer than control mean PMID:27736299 Fig3. cdc25 level reduced to ~48% decreased protein level in heterozygous diploid cell during vegetative growth PMID:27736299 Fig1. 14.43% longer than control mean PMID:27736299 Fig3. Cdc2 level reduced to about 48% decreased protein level in heterozygous diploid cell during vegetative growth PMID:27737912 fig 6 PMID:27738016 Increase of stalled RNA polymerase I at rDNA during G0 phase; nuc1-FLAG PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 small-RNA-seq PMID:27738016 small-RNA-seq PMID:27738016 Rad22-YFP, G0-exit PMID:27738016 G0-exit PMID:27738016 Increased gH2AX/H2A ratio (marker of DNA damage) at rDNA during G0; 2 day G0 ChIP PMID:27738016 Increased gH2AX/H2A ratio (marker of DNA damage) at rDNA during G0; 2 day G0 ChIP PMID:27738016 Increased gH2AX/H2A ratio (marker of DNA damage) at rDNA during G0; 2 day G0 ChIP PMID:27738016 Increased gH2AX/H2A ratio (marker of DNA damage) at rDNA during G0; 2 day G0 ChIP PMID:27738016 Increased RNA polymerase II at rDNA during vegetative growth PMID:27738016 Increase of stalled RNA polymerase I at rDNA during G0 phase; nuc1-FLAG PMID:27738016 Increase of stalled RNA polymerase I at rDNA during G0 phase; nuc1-FLAG PMID:27738016 Increase of stalled RNA polymerase I at rDNA during G0 phase; nuc1-FLAG PMID:27738016 Decreased RNA polymerase I at rDNA during vegetative growth; nuc1-FLAG PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 15 ug/ml thiabendazole PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 S13; Tetrad dissection PMID:27738016 S13; Tetrad dissection PMID:27738016 S13; Tetrad dissection PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 2 day G0 ChIP PMID:27738016 2 day G0 ChIP PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 15 ug/ml thiabendazole PMID:27738016 15 ug/ml thiabendazole PMID:27738016 15 ug/ml thiabendazole PMID:27738016 15 ug/ml thiabendazole PMID:27738016 G0 viability assay PMID:27738016 24h G0 cell microscopy PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 24h G0 cell microscopy PMID:27738016 G0 viability assay PMID:27738016 24h G0 cell microscopy PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 24h G0 cell microscopy PMID:27738016 G0 viability assay PMID:27738016 24h G0 cell microscopy PMID:27738016 G0 viability assay PMID:27738016 24h G0 cell microscopy PMID:27738016 G0 viability assay PMID:27738016 24h G0 cell microscopy PMID:27738016 G0 viability assay PMID:27738016 24h G0 cell microscopy PMID:27738016 G0 viability assay PMID:27738016 24h G0 cell microscopy PMID:27738016 G0 viability assay PMID:27738016 24h G0 cell microscopy PMID:27738016 G0 viability assay PMID:27738016 24h G0 cell microscopy PMID:27738016 G0 viability assay PMID:27738016 24h G0 cell microscopy PMID:27738016 G0 viability assay PMID:27738016 24h G0 cell microscopy PMID:27738016 G0 viability assay PMID:27738016 24h G0 cell microscopy PMID:27738016 24h G0 cell microscopy PMID:27738016 G0 viability assay PMID:27738016 24h G0 cell microscopy PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 24h G0 cell microscopy PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 15 ug/ml thiabendazole PMID:27738016 15 ug/ml thiabendazole PMID:27738016 15 ug/ml thiabendazole PMID:27738016 15 ug/ml thiabendazole PMID:27738016 15 ug/ml thiabendazole PMID:27738016 15 ug/ml thiabendazole PMID:27738016 24h G0 cell microscopy PMID:27738016 G0 viability assay PMID:27738016 24h G0 cell microscopy PMID:27738016 G0 viability assay PMID:27738016 24h G0 cell microscopy PMID:27738016 G0 viability assay PMID:27738016 G0 viability assay PMID:27738016 24h G0 cell microscopy PMID:27738016 15 ug/ml thiabendazole PMID:27738016 mutant defective in maintenance of quiescence PMID:27738016 mutant defective in maintenance of quiescence PMID:27738016 Fig S6; 15 ug/ml or 20 ug/ml thiabendazole PMID:27738016 Fig S6; 15 ug/ml or 20 ug/ml thiabendazole PMID:27738016 Fig S6; 15 ug/ml or 20 ug/ml thiabendazole PMID:27738016 Fig S6; 15 ug/ml or 20 ug/ml thiabendazole PMID:27738016 24h G0 cell microscopy PMID:27738016 mutant defective in maintenance of quiescence PMID:27746023 Figure 2C PMID:27746023 Movie S4. Sty1 activity is critical for maintaining a non-polarized Cdc42 module in N-starved quiescent cells. PMID:27746023 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 Figures 2A and S1A; Movie S1 PMID:27746023 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 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 arrested PMID:27746023 Figure 2C PMID:27746023 Figure 2D PMID:27746023 Figure S1B PMID:27746023 Movie S4. Sty1 activity is critical for maintaining a non-polarized Cdc42 module in N-starved quiescent cells. PMID:27746023 Figures S1C and S1D PMID:27746023 Figures S1C and S1D PMID:27811944 mutation destabilized Sre1 precursor and prevented Sre1 proteolytic cleavage PMID:27811944 mutation destabilized Sre1 precursor and prevented Sre1 proteolytic cleavage PMID:27811944 deletion of Sre1 aa 877-900 also destabilized Sre1 and prevented proteolytic activation PMID:27851962 Figure 1 PMID:27851962 Figure 1 PMID:27851962 Figure 1 PMID:27851962 Figure 1 PMID:27851962 Figure 1 PMID:27851962 Figure 1 PMID:27851962 Figure 1 PMID:27852900 GFP-LactC2 probe expressed from pREP3X PMID:27852900 fig4 GFP-LactC2 probe expressed from pREP3X PMID:27852900 GFP-LactC2 probe expressed from pREP3X PMID:27852900 fig 4B. GFP-LactC2 probe expressed from pREP3X PMID:27852900 GFP-LactC2 probe expressed from pREP3X PMID:27852900 Figure 5D PMID:27852900 Figure 8e PMID:27852900 fig8d PMID:27852900 fig 7 PMID:27852900 fig 8d PMID:27852900 fig 8a PMID:27852900 fig 8 a PMID:27852900 fig 8 a PMID:27852900 fig 7 PMID:27852900 Figure 3, A and E PMID:27852900 Figure 3, A and E PMID:27852900 fig 4 GFP-LactC2 probe expressed from pREP3X PMID:27852900 GFP-LactC2 probe expressed from pREP3X PMID:27871365 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 3H PMID:27871365 3H PMID:27872152 Fig. 7D) PMID:27872152 adaptor for dis1-microtubule PMID:27872152 (Fig. 2A) (Fig. 2B; Fig. S2B). PMID:27872152 (Fig. 7B,C) PMID:27872152 Fig. 7E issues/2984 PMID:27872152 (2.0% versus <0.1%) (Fig. 7F) PMID:27872152 Fig. 7D) PMID:27872152 Fig. 7D) PMID:27886462 Table 3 PMID:27886462 figure 3A PMID:27886462 figure 3A PMID:27886462 Figure 1C PMID:27886462 Figure 1C PMID:27886462 Figure 1C PMID:27886462 Figure 1C PMID:27886462 Table 3 PMID:27886462 Table 3 PMID:27886462 Table 3 PMID:27886462 Figure 4, Table 3 PMID:27886462 Figure 4, Table 3 PMID:27886462 Figure 4, Table 3 PMID:27886462 Table 2 PMID:27886462 Figure 1B PMID:27886462 Figure 1B PMID:27886462 Figure 1C PMID:27886462 Figure 4 PMID:27886462 Table 4 PMID:27886462 Figure 4, Table 3 PMID:27886462 Table 4 PMID:27886462 Table 4 PMID:27886462 Table 4 PMID:27886462 figure 3A PMID:27886462 Figure 1A PMID:27886462 figure 3A PMID:27886462 figure 3C PMID:27886462 figure 3C PMID:27886462 figure 3C PMID:27886462 Figure 1C PMID:27886462 Figure 1C PMID:27886462 Table 2 PMID:27886462 Table 2 PMID:27886462 Table 2 PMID:27886462 Table 2 PMID:27886462 Figure 1C PMID:27886462 figure 2A PMID:27886462 figure 2A PMID:27886462 figure 2A PMID:27886462 figure 2A PMID:27886462 figure 3C PMID:27886462 Table 2 PMID:27886462 Table 3 PMID:27886462 Table 3 PMID:27886462 Figure 1A PMID:27886462 Figure 1A PMID:27886462 Figure 1A PMID:27886462 Figure 1A PMID:27886462 Table 2 PMID:27886462 Table 2 PMID:27886462 Table 2 PMID:27886462 Table 3 PMID:27886462 Table 3 PMID:27886462 Figure 1A PMID:27886462 Figure 4, Table 3 PMID:27886462 Figure 4, Table 3 PMID:27886462 Figure 4, Table 3 PMID:27886462 Figure 1A PMID:27886462 Figure 1A PMID:27886462 Figure 1A PMID:27886462 Figure 1B PMID:27886462 Figure 1B PMID:27886462 Table 4 PMID:27889481 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 Figure 1 PMID:27889481 Figure 1B PMID:27889481 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 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 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 Figure 1D PMID:27889481 fig6 PMID:27889481 fig6 PMID:27889481 abolished PMID:27889481 Figure 5C. spindle formation occurs normally at both MI and MII in sad1.2 meiosis PMID:27889481 Figure 5B. centromeres are also released from LINC in bouquet-defective cells PMID:27889481 fig 5.C PMID:27889481 (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 (Figure 4B) PMID:27889481 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 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 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 fig2c PMID:27889481 Figure I PMID:27889481 Figure 1 PMID:27889481 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 Figure 1D PMID:27889481 fig2c PMID:27889481 Figures 3B–C, S4A PMID:27889481 Figures 3B–C, S4A PMID:27889481 Figure S4B PMID:27889481 Figure S4B PMID:27889481 fig2c PMID:27889481 (Figure 3DE) PMID:27889481 fig 3DE PMID:27889481 (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 fig 3DE sad1.2 cells often show extra Mis6-GFP foci unassociated with the SPB, even at permissive temperature PMID:27889481 fig2c PMID:27889481 Figure 1B PMID:27898700 fig 1C PMID:27898700 Fig 2 A (3x WT) PMID:27898700 fig 1FG PMID:27898700 fig 1FG PMID:27898700 fig 1FG PMID:27898700 fig 1FG slides along axis from midpoint PMID:27898700 Fig 2 A PMID:27898700 Fig 4 PMID:27898700 Fig S4D S4E PMID:27898700 Fig 2 A (2x WT) PMID:27898700 Fig 2 A PMID:27898700 Fig 4 PMID:27898700 Fig 4 PMID:27898700 Fig 4 PMID:27898700 Fig 4 PMID:27898700 Fig 4 PMID:27898700 Fig S3B PMID:27898700 fig 1C PMID:27898700 fig 1C PMID:27898700 fig 1B swollen multiseptate elongated PMID:27898700 fig 1A during cytokinesis PMID:27898700 Fig 2 A PMID:27898700 fig 1A PMID:27898700 Fig 4 PMID:27898700 Fig S3B PMID:27901072 fig6 PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 1d PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27901072 asynchronous fig 3a PMID:27902423 Promoter analysis PMID:27902423 Promoter analysis PMID:27902423 Promoter analysis PMID:27966061 indicates Hsf1 activation PMID:27974503 Suquence homology, localization, co-immunoprecipitation PMID:27974503 Aberrant Golgi stacks PMID:27974503 Abnormal GFP-Syb1 distribution PMID:27974503 Cpy1 missorting in null mutant PMID:27974503 Cpy missorting in null mutant PMID:27974503 Cpy1 missorting in null mutant PMID:27974503 Cpy1 missorting in null mutant PMID:27974503 Slow growth. Reduced colony size PMID:27974503 Abnormal GFP-Syb1 localization PMID:27974503 Sequence similarityto ChAPs, protein localization, Co-immunoprecipitation PMID:27984744 Fig. 1B PMID:27984744 Fig. 1A PMID:27984744 Fig. 1B PMID:27984744 Fig. 1A PMID:27984744 Fig. 1A PMID:27984744 Fig. 1B PMID:27984744 Fig. 1A PMID:27984744 Fig. 1B PMID:27984744 Fig. 1A PMID:27984744 Fig. 1B PMID:27984744 Fig. 1B PMID:27984744 Fig. 1A PMID:27984744 Fig. S2 PMID:27984744 ChIP-seq; Fig. 1C-D PMID:27984744 Fig. 2A-B PMID:27984744 Fig. 2E-F PMID:27984744 Fig. 2E-F PMID:27984744 Fig. 2E-F PMID:28011631 Fig. 1H and Fig. 3B PMID:28011631 (Fig. 4B) PMID:28011631 Fig. 3B (also in lantrunculin treated sceels indicating actin dependeny) PMID:28011631 Fig. 4A PMID:28011631 Fig. 1F and Fig. 2C PMID:28011631 Fig. 4A,C) PMID:28011631 Figure S3 LP clustering at nucleus PMID:28011631 figure S2 PMID:28011631 figure S2 PMID:28011631 Fig. 4F Assembly of Isp3-GFP onto the spore surface was defective in the dga1Δplh1Δ mutant. PMID:28011631 Fig. 3B PMID:28011631 (Fig. 4B) PMID:28011631 Fig. 4B The dga1Δplh1Δ mutant possessed few lipid droplets. PMID:28011631 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 Fig. 4B The dga1Δplh1Δ mutant possessed few lipid droplets. PMID:28011631 Fig. 4F Isp3-GFP was improperly assembled in the dga1Δplh1Δ mutant. PMID:28011631 Fig. 3B (also in lantrunculin treated sceels indicating actin dependeny) PMID:28011631 Fig. 3B normal lipid droplet localization to FSM leading edge PMID:28011631 2C (also in lantrunculin treated sceels indicating actin dependeny) PMID:28011631 2C (also in lantrunculin treated sceels indicating actin dependeny) PMID:28011631 2C (also in lantrunculin treated sceels indicating actin dependeny) PMID:28011631 2C PMID:28017606 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 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 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 Spc7-wt arrested significantly faster than Spc7-9TE, with $60% mitotic arrest after 12 hr compared to 16 hr for Spc7-9TE. PMID:28017606 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 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 Fig 6 D PMID:28031482 Fig 6 D PMID:28031482 Fig 6 D PMID:28031482 Fig 6 D PMID:28031482 Fig 6 D PMID:28031482 figure 1 E PMID:28031482 figure 1 E PMID:28031482 figure 1 D PMID:28031482 figure 1 E PMID:28031482 figure 2B PMID:28031482 figure 2D PMID:28031482 figure 2D PMID:28031482 Fig. 2B PMID:28031482 Fig. 4B Fig. 4D PMID:28031482 Fig. 4D PMID:28031482 Fig. 4H, right panel PMID:28031482 Fig. 5A PMID:28031482 Fig. 5C PMID:28031482 Fig. 5B PMID:28031482 Fig. 5D PMID:28031482 Fig. 5G, left panel PMID:28031482 Fig. 5G, left panel PMID:28031482 Fig. 5G, left panel PMID:28031482 Figure 6 A PMID:28031482 Figure 6 c PMID:28031482 Figure 6 c PMID:28031482 Fig 6 D PMID:28031482 Fig 6 D PMID:28031482 Fig 6 D PMID:28031482 Fig 6 D PMID:28031482 figure 7A PMID:28031482 Fig 6 C PMID:28031482 Fig 6 C PMID:28031482 Fig 6 C PMID:28031482 Fig 6 C PMID:28031482 Fig 6 C PMID:28031482 Fig 6 C PMID:28031482 Fig 6 C PMID:28031482 Fig 6 C PMID:28031482 Fig. 1D PMID:28031482 pdc2 is required for mRNA decapping. Fig. 2A 2B PMID:28031482 Fig 6 D PMID:28103117 changes in phosphrylation level fig4 Wee1 to remain in the partially phosphorylated form throughout the cell cycle (Fig. S2) PMID:28103117 The cell cycle was 20 min longer in clp1D cells compared with wild type cells. PMID:28103117 changes in phosphorylation level Figs. 5A, B and S2) PMID:28103117 changes in phosphorylation level Figs. 5A, B and S2) PMID:28103117 fig 2a INCREASED PMID:28103117 fig 2a PMID:28103117 fig 2a INCREASED PMID:28103117 fig 2a INCREASED PMID:28103117 fig 2a INCREASED PMID:28103117 fig 2a INCREASED PMID:28103117 fig3a Cdk1 consensus sites PMID:28103117 changes in phosphrylation level fig4 Wee1 to remain in the partially phosphorylated form throughout the cell cycle (Fig. S2) PMID:28160081 fig 2A PMID:28160081 fig 2A PMID:28160081 fig 2A PMID:28160081 fig 5 PMID:28160081 fig 4c PMID:28160081 fig2A PMID:28160081 fig2B PMID:28160081 fig2B PMID:28160081 fig2B PMID:28160081 fig2B PMID:28160081 fig2B PMID:28178520 vw: moved down to nucleoplasm PMID:28178520 Fig 5 PMID:28178520 (Figure 5B) PMID:28178520 Figure 1B and S1B,C PMID:28178520 Figure 1B and S1B,C PMID:28178520 Figure 1B and S1B,C PMID:28178520 Fig 5 PMID:28178520 Fig 5 PMID:28178520 Fig 4 D PMID:28178520 Figure 1B and S1B,C PMID:28178520 Figure 1B and S1B,C PMID:28178520 Figure 1C PMID:28178520 (Figures S1D and S1E) PMID:28178520 (Figure 1D) PMID:28178520 (Figure 1D) PMID:28178520 Figure 1B and S1B,C PMID:28178520 Figure 1B and S1B,C PMID:28178520 fig1 PMID:28178520 Figure 1B and S1B,C PMID:28178520 Figure 1B and S1B,C PMID:28178520 Figure 1B and S1B,C PMID:28178520 Figure 1B and S1B,C PMID:28178520 Figure 1B and S1B,C PMID:28178520 Fig 4 D PMID:28178520 Fig 4 A PMID:28178520 Fig 4 A PMID:28178520 Fig 4 A PMID:28178520 Fig 4 A PMID:28178520 Fig 4 A PMID:28178520 Fig 4 A PMID:28178520 Fig 4 A PMID:28178520 Figure 4A PMID:28178520 (Figure S4C) PMID:28178520 (Figure S4C) PMID:28178520 (Figure S4C) PMID:28178520 (Figure S4C) PMID:28178520 Figure S3C/D PMID:28178520 Figure 2B PMID:28178520 Fig 4 D PMID:28178520 Figure 2B PMID:28178520 Figure S3B PMID:28178520 Figure S3B PMID:28178520 Figure 2A; Figure S3A PMID:28178520 Figure 2A; Figure S3A PMID:28178520 figure 2A PMID:28178520 (Figures S2B) PMID:28178520 (Figures S2B) PMID:28178520 (Figures S2A) PMID:28178520 (Figures S2A) PMID:28178520 (Figures 1J) PMID:28178520 (Figures 1J) PMID:28178520 (Figures 1J) PMID:28178520 (Figures 1J) PMID:28178520 (Figures 1J) PMID:28178520 Fig 4 D PMID:28178520 (Figures 1J) PMID:28178520 (Figures 1J) PMID:28178520 (Figures 1J) PMID:28178520 (Figures 1J) PMID:28178520 (Figures 1J) PMID:28178520 Figure 1I PMID:28178520 Figure 1I PMID:28178520 (Figures 1H) PMID:28178520 (Figures 1H) PMID:28178520 Figure 1E PMID:28178520 (Figures 1G and 1I; Figure S1F) PMID:28178520 (Figures 1G and 1I; Figure S1F) PMID:28178520 Figure 1H PMID:28178520 Figure 4E PMID:28178520 Fig 4 D PMID:28178520 Fig 4 A PMID:28178520 FIg 3 PMID:28178520 Fig 4 A PMID:28178520 requires motor activity PMID:28178520 Fig 1 requires Klp9, Clp1 activity PMID:28178520 Fig 1 requires Clp1 activity PMID:28178520 Fig 4 A PMID:28178520 Fig 4 A PMID:28178520 (Figure 5B) PMID:28178520 Figure 4E PMID:28178520 Fig 5 PMID:28178520 Fig 4 D PMID:28178520 Fig 4 D PMID:28191457 Phenotype is inherited in non-Mendelian manner, via protein aggregates (prion-like). PMID:28191457 SDS-PAGE followed by western blotting and proteinase K treatment. Dot plots with extracts for pellet, soluble and total cell fractions with and without pre-treatment with 2% SDS. SDD-AGE gels of samples treated at room temperature and at 95°C, both with and without curing with GdnHCl. PMID:28193844 8b PMID:28193844 they show it is GPI anchored, the specified residue is predicted PMID:28193844 fig4 PMID:28193844 6a PMID:28193844 6 PMID:28193844 fig4 PMID:28193844 9 PMID:28202541 Ost1-mCherry increased signal in ER PMID:28202541 Ost1-mCherry, mCherry antibody PMID:28202541 Anp1-GFP degradation as assayed by appearance of free GFP PMID:28202541 pulled on Dsc2 PMID:28202541 Scp1-13xMyc used for Scp1, pulled on Myc PMID:28202541 Anp1-GFP mislocalized from Golgi puncta to ER and vacuole PMID:28202541 improved relative to WT Sre1 PMID:28218250 ChIP-seq PMID:28218250 ChIP-seq PMID:28218250 ChIP-seq PMID:28218250 ChIP-seq PMID:28218250 ChIP-seq PMID:28218250 ChIP-seq PMID:28218250 ChIP-seq PMID:28218250 ChIP-seq; same severity as spt16-1 alone PMID:28218250 ChIP-seq PMID:28218250 ChIP-seq PMID:28218250 ChIP-seq PMID:28218250 ChIP-seq PMID:28218250 ChIP-seq PMID:28218250 ChIP-seq PMID:28218250 ChIP-seq PMID:28218250 ChIP-seq PMID:28218250 ChIP-seq PMID:28218250 ChIP-seq PMID:28242692 Fig. 1B, supp table S1 PMID:28242692 Fig 1A PMID:28242692 Fig. 2B) PMID:28242692 severe leaking; Fig. 3B, arrow; Fig. 3 C and D, quantifi- cation, figure 4 B PMID:28242692 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 Fig. 4B, asterisk PMID:28242692 and the NPCs that were present were localized to re- gions that were largely free of karmellae and tubulo-vesicular structures (Fig. 4D). PMID:28242692 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 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 Fig. 1B, supp table S1 PMID:28242692 4B, arrowheads, and Fig. 5B PMID:28242692 Fig S1C PMID:28242692 Fig S1C PMID:28242692 Fig. 1C PMID:28242692 Fig 1C PMID:28242692 partial leaking; Fig. 3B, arrow; Fig. 3 C and D, quantifi- cation PMID:28242692 partial leaking; Fig. 3B, arrow; Fig. 3 C and D, quantifi- cation PMID:28242692 rescue PMID:28242692 Fig 1C PMID:28242692 Fig 1C PMID:28242692 Fig S1AB PMID:28242692 Fig. 1 D–F PMID:28242692 partial leaking; Fig. 3B, arrow; Fig. 3 C and D, quantifi- cation PMID:28264193 fig5 fusion mutant not currently capturable PMID:28264193 Supp PMID:28264193 Supp2 PMID:28264193 Supp2 PMID:28264193 Supp2 PMID:28264193 Supp2 PMID:28264193 Supp2 PMID:2827111 table 1 PMID:2827111 table1 PMID:2827111 table1 PMID:2827111 fig 7 B PMID:2827111 table 1 PMID:28281664 Figure 3. PMID:28281664 Figure 3. PMID:28281664 Figure 2 PMID:28281664 Figure 2 PMID:28281664 Figure 3. PMID:28281664 figure 1D PMID:28281664 figure 1c & d PMID:28281664 figure 1d PMID:28281664 Figure 2 PMID:28281664 Figure 2 PMID:28281664 Figure 1B PMID:28281664 figure 1a PMID:28281664 Figure 2 PMID:28281664 Figure 3. PMID:28281664 Figure 2. PMID:28281664 Figure 2 PMID:28281664 Figure 1 PMID:28281664 Figure 1D PMID:28281664 Figure 2 PMID:28281664 Figure 2 PMID:28281664 Figure 3. PMID:28281664 Figure 3. PMID:28281664 figure 1b divides longer than WT in the same conditions PMID:28281664 Figure 3. PMID:28281664 Figure 3. PMID:28292899 Fig. 7 PMID:28292899 Fig. 6 PMID:28292899 Fig. 5B PMID:28292899 Fig. 7 PMID:28292899 Fig. 1A, Inset and Movie S1/ number of Mcp5 molecules per cluster 10 ± 2 ( Fig. 1D) PMID:28292899 Fig 2 & Fig. 3C PMID:28292899 Fig. 4 D–F PMID:28292899 Fig. 5B PMID:28292899 Fig. 5B A(ALSO FOR THE myo-1TH3 domain deletion(need genotype description) PMID:28292899 Fig. 5B PMID:28292918 decreased NHEJ repair of hairpin-capped chromosome breaks PMID:28292918 normal NHEJ repair of hairpin-capped chromosome breaks PMID:28292918 decreased NHEJ repair of hairpin-capped chromosome breaks PMID:28292918 decreased NHEJ repair of hairpin-capped chromosome breaks PMID:28292918 decreased NHEJ repair of hairpin-capped chromosome breaks PMID:28292918 normal NHEJ repair of hairpin-capped chromosome breaks PMID:28292918 normal NHEJ repair of hairpin-capped chromosome breaks PMID:28292918 normal NHEJ repair of hairpin-capped chromosome breaks PMID:28292918 decreased NHEJ repair of hairpin-capped chromosome breaks PMID:28292918 decreased NHEJ repair of hairpin-capped chromosome breaks PMID:28292918 decreased NHEJ repair of hairpin-capped chromosome breaks PMID:28292918 decreased NHEJ repair of hairpin-capped chromosome breaks PMID:28292918 normal NHEJ repair of hairpin-capped chromosome breaks PMID:28292918 decreased NHEJ repair of hairpin-capped chromosome breaks PMID:28334955 figure 9 F PMID:28334955 figure 9 F PMID:28334955 figure 9 F PMID:28334955 fig 1B PMID:28334955 Fig 1 A PMID:28334955 Fig 1 A PMID:28334955 Fig 1 A PMID:28334955 We named this gene mpa1 PMID:28334955 Fig 1 E/F PMID:28334955 Supplementary Figure S3B PMID:28334955 Supplementary Figure S3B (abolished by galactose addition) PMID:28334955 S3 PMID:28334955 S3 PMID:28334955 Fig 1 C PMID:28334955 S3 PMID:28334955 Figure 2B (barely detectable level ) PMID:28334955 Figure 2B PMID:28334955 Figure 2B PMID:28334955 Figure 2B, 8B,8C PMID:28334955 Figure 2C PMID:28334955 figure 6 c PMID:28334955 figure 6 c PMID:28334955 figure 6 a PMID:28334955 figure 6 a PMID:28334955 Fig 7 A PMID:28334955 Fig 7 A PMID:28334955 fig 7 B PMID:28334955 Fig 7 c PMID:28334955 Supplementary Figure S7 PMID:28334955 fig 1B inferred from PMID:28334955 fig 1B PMID:28334955 fig 1B inferred from PMID:28334955 Fig 1 C PMID:28334955 figure 8 A PMID:28334955 Figure 8B,8C (barely detectable level ) PMID:28334955 Figure 8B,8C PMID:28334955 Figure 8B,8C PMID:28334955 figure 8 D PMID:28334955 figure 8 D PMID:28334955 figure 8 D PMID:28334955 figure 8 D PMID:28334955 figure 8 D PMID:28334955 figure 8 D PMID:28334955 figure 9A PMID:28334955 fig 9C PMID:28334955 figure Supp S8 PMID:28334955 figure 9 d PMID:28334955 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 figure 9 F PMID:28334955 figure 9 F PMID:28334955 figure 9 F PMID:28334955 figure 9 F PMID:28334955 figure 9 F PMID:28334955 fig 1B PMID:28338873 assayed in vitro PMID:28338873 assayed in vitro PMID:28343969 Fig 4f PMID:28343969 Fig 2C, 2D, 2G PMID:28343969 18degC Fig 2C, 2D, 2G This phenotype is largely suppressed by tethering Hrk1 to centromeres. (bw, I made an annotation to represent this suppression below) PMID:28343969 Fig 4H (cut9-665 move to background for this one) PMID:28343969 Fig 4F, 4H (cut9-665 move to background for this one) PMID:28343969 Fig S2A, S2C PMID:28343969 Fig 1B PMID:28343969 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 figure 1 E PMID:28343969 Fig 2AB PMID:28343969 Fig 2AB PMID:28343969 Fig 2 B PMID:28343969 Fig 2 B PMID:28343969 Fig 2AB PMID:28343969 Fig 2AB PMID:28343969 "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 "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 Fig 2F WT is about the same? PMID:28343969 Fig 2F WT is about the same? PMID:28343969 Fig 2E PMID:28343969 Fig 2E PMID:28343969 Fig 2 F PMID:28343969 fig S4B PMID:28343969 S4A PMID:28343969 S4A PMID:28343969 fig 4b PMID:28343969 fig 4b PMID:28343969 4C PMID:28343969 4C PMID:28343969 Fig 4E PMID:28343969 Fig 4E PMID:28343969 Fig 4f PMID:28343969 Fig 4f PMID:28343969 Fig 4f PMID:28343969 Fig 4G PMID:28343969 Fig 4G PMID:28343969 Fig S4A PMID:28343969 Fig S4A PMID:28343969 Fig S4A PMID:28343969 (Figures S4D and S4E PMID:28343969 (Figures S4D and S4E PMID:28343969 Fig S4A PMID:28343969 Fig S4A PMID:28343969 (Figures S4D and S4E PMID:28343969 (Figures S4D and S4E PMID:28345447 restored by depletion of ammonium PMID:28345447 restored by depletion of ammonium PMID:28345447 restored by depletion of ammonium PMID:28345447 restored by depletion of ammonium PMID:28345447 restored by depletion of ammonium PMID:28366743 Fig. 2C/D, S2B, PMID:28366743 Figure S3B PMID:28366743 Figure S3B PMID:28366743 Figure S3B PMID:28366743 Figure S3B PMID:28366743 Figure S3B PMID:28366743 Figure S3B PMID:28366743 Fig S3B PMID:28366743 Figure S1e PMID:28366743 figure 4D. s PMID:28366743 Figures 1FandS1H). PMID:28366743 (Figure 1F PMID:28366743 supp S1h PMID:28366743 figure 4C. synchronous mitotic cells PMID:28366743 figur 3A PMID:28366743 figur 3A PMID:28366743 Fig. 1C synchronous mitotic cells PMID:28366743 synchronous mitotic cells fig 1c PMID:28366743 Fig 1B PMID:28366743 fig 4A PMID:28366743 Fig. 4C PMID:28366743 Fig. 4C PMID:28366743 Fig. 4C PMID:28366743 Fig 4D PMID:28366743 Fig. 3B PMID:28366743 Figure 4D PMID:28366743 fig 3a PMID:28366743 Fig. 3 A/B present in interphase cells PMID:28366743 Fig. 3 A/B present in interphase PMID:28366743 Fig 1B PMID:28366743 Fig 1B PMID:28366743 Fig1B PMID:28366743 Fig1b PMID:28366743 Fig 1B PMID:28366743 Fig. 3B PMID:28366743 Fig S1G PMID:28366743 fig 3.a PMID:28366743 Figure 4D PMID:28366743 Fig. 4A PMID:28366743 Fig. 2C/D, S2B, PMID:28366744 Figure 3A PMID:28366744 vw; I changed the genotype here PMID:28366744 "vw changed term from ""reduced ubiquitin ligase activity""" PMID:28366744 Fig 1 A (checkpoint assay) PMID:28366744 Fig 1 A (checkpoint assay) PMID:28366744 Fig 1 A (checkpoint assay) PMID:28366744 (Figure 3B). PMID:28366744 Fig 1 A (checkpoint assay) PMID:28366744 Fig 1 A (checkpoint assay) PMID:28366744 fig 1 c PMID:28366744 fig 1 c PMID:28366744 fig S1 PMID:28366744 fig 2a PMID:28366744 fig 1 c PMID:28366744 fig 2a PMID:28366744 fig 2a PMID:28366744 fig 2a PMID:28366744 figure 2b PMID:28366744 Figures 3A and 3B PMID:28366744 (Figure 3B). PMID:28366744 (Figure 3A). PMID:28366744 (Figure 3A). PMID:28366744 Deletion increases levels of mitotic checkpoint complex associated with the anaphase promoting complex in mitosis. PMID:28366744 Required for mitotic checkpoint complex binding to the anaphase promoting complex. PMID:28366744 vw I changed the genotype/ Fig 1 A (checkpoint assay) PMID:28367989 S2P form PMID:28377506 fig4 PMID:28377506 fig4 PMID:28377506 fig4D PMID:28377506 "fig 7: ""unlike the hem13-1 mutant, the hem12 and hem14 null mutants of the heme biosynthesis pathway are insensitive to HU""" PMID:28377506 "fig 7: ""unlike the hem13-1 mutant, the hem12 and hem14 null mutants of the heme biosynthesis pathway are insensitive to HU""" PMID:2837764 assayed using mammalian proteins PMID:28388826 data not shown PMID:28388826 data not shown PMID:28404620 sequencing of Ago1-bound siRNA PMID:28404620 sequencing of Ago1-bound siRNA PMID:28404620 also uses Pol ii-RNA immunoprecipitation PMID:28404620 sequencing of Ago1-bound siRNA PMID:28404620 uses Pol ii-RNA immunoprecipitation PMID:28404620 uses histone H3 RNA immunoprecipitation PMID:28404620 sequencing of Ago1-bound siRNA PMID:28404620 also uses Pol ii-RNA immunoprecipitation PMID:28404620 uses Pol ii-RNA immunoprecipitation PMID:28404620 sequencing of Ago1-bound siRNA PMID:28404620 sequencing of Ago1-bound siRNA PMID:28404620 sequencing of Ago1-bound siRNA PMID:28410370 wider localization at the shmoo tip PMID:28410370 wider localization PMID:28410370 wider localization PMID:28410370 wider localization PMID:28410370 wider localization PMID:28410370 wider localization PMID:28410370 wider distribution along shmoo tip PMID:28410370 stronger phenotype when crossed to fus1∆ PMID:28410370 Wider localization at shmoo tip PMID:28410370 phenotype more severe when crossed to fus1∆ PMID:28410370 more severe phenotype when crossed to fus1∆ PMID:28410370 more severe phenotype when crossed to fus1delta PMID:28410370 Strong phenotype in crosses with fus1∆. PMID:28432181 snRNA/ complementation of yeast pus1 PMID:28438891 Fig 1C PMID:28438891 Fig 1C PMID:28438891 Fig 1C PMID:28438891 Fig 1C PMID:28438891 Fig 1C PMID:28438891 Fig 1C PMID:28438891 Fig 1C PMID:28438891 Fig 1D PMID:28438891 Fig 1D PMID:28438891 Fig 1C PMID:28438891 Fig 1C PMID:28438891 fig 7 PMID:28438891 Fig EV5 PMID:28438891 Fig 3C PMID:28438891 MIOTOTIC PMID:28438891 type 2 cohesion (still bound) MITOTIC PMID:28438891 Fig 1C PMID:28438891 Fig 3C PMID:28438891 Fig 3C PMID:28438891 Fig 3C PMID:28438891 Fig 3C PMID:28438891 fig 4 PMID:28438891 Fig 1C PMID:28438891 required for Rad21 dephosphorylation PMID:28438891 Fig 5A PMID:28438891 Figure 5 B (exacerbates ) PMID:28438891 Fig 4E PMID:28438891 type 2 cohesion (still bound) PMID:28438891 Fig 1C PMID:28467824 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 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 ura1 met5 PMID:28469148 ade6 arg1 PMID:28469148 lys3 ura1 PMID:28469148 ura1 met5 PMID:28469148 lys3 ura1 PMID:28469148 lys3 ura1 PMID:28469148 lys3 ura1 PMID:28469148 ura1 met5 PMID:28469148 lys3 ura1 PMID:28469148 ura1 met5 PMID:28469148 lys3 ura1 PMID:28469148 ura1 met5 PMID:28475874 In the absence of Rad52, newly replicated strands are extensively resected at dysfunctional replication forks thus generating mitotic sister chromatid bridging. PMID:28475874 in response to a single blocked replisome PMID:28475874 in response to a single blocked replisome PMID:28475874 in response to a single blocked replisome PMID:28475874 In the absence of Rad51, newly replicated strands are extensively resected at dysfunctional replication forks thus generating mitotic sister chromatid bridging PMID:28475874 in response to a single blocked replisome PMID:28475874 in response to a single blocked replisome PMID:28475874 in response to a single blocked replisome PMID:28476936 Fig 2, Fig3, Fig4B PMID:28476936 Fig 5 supplements added PMID:28476936 Fig 5 supplements added PMID:28476936 Fig 5 supplements added PMID:28476936 Fig 5 supplements added PMID:28476936 Fig 5 supplements added PMID:28476936 Fig 5 supplements added PMID:28476936 Fig 5 supplements added PMID:28476936 Fig 5 supplements added PMID:28476936 Fig 5 supplements added PMID:28476936 Fig 5 supplements added PMID:28476936 Fig 5 supplements added PMID:28476936 Fig 5 supplements added PMID:28476936 Fig5 supplements added PMID:28476936 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 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 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 Fig S4A cell growth at G2/M1 arrest is dependent on transcription. no supplements added PMID:28476936 Fig4D no supplements added PMID:28476936 Fig4A, C, E, F no supplements added PMID:28476936 Fig 2 PMID:28476936 Fig 2 PMID:28476936 Fig 2 PMID:28476936 Fig 2 PMID:28476936 Fig 2 PMID:28476936 Fig 2 PMID:28476936 Fig 2 PMID:28476936 Fig S1A, Fig1B,C PMID:28476936 Fig S1A, Fig1 PMID:28479325 mRNA quantitation was obtained by Nanostring experiments. PMID:28479325 During G2, the concentration of Cdc25 increases about 2 fold (Figure 1A) PMID:28479325 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 normal cell size. homeostasis PMID:28479325 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 arelatively constant concentration during G2, as previously observed [2mRNA quantitation was obtained by Nanostring experiments. PMID:28479325 mRNA quantitation was obtained by Nanostring experiments. PMID:28481910 BrdU incorporation PMID:28481910 BrdU incorporation PMID:28481910 same as cdc20-M10 alone PMID:28481910 BrdU incorporation PMID:28481910 BrdU incorporation PMID:28497540 fig S2A PMID:28497540 S4 PMID:28497540 mph1Δ cells (Fig. 2B) PMID:28497540 mph1Δ cells (Fig. 2B) PMID:28497540 fig 1 B PMID:28497540 fig 1F PMID:28497540 fig 5 PMID:28497540 Fig. S5 PMID:28497540 Fig. S5 PMID:28497540 Fig. E PMID:28497540 fig 5 PMID:28497540 fig 4A PMID:28497540 fig 4A PMID:28497540 during interphase (not usually located then) PMID:28497540 Fig. 5C PMID:28497540 4B PMID:28497540 fig 5 PMID:28497540 fig 5C PMID:28497540 fig 1B PMID:28497540 fig 1 EF PMID:28497540 fig 1F PMID:28497540 fig 1E PMID:28497540 RECRUITS PMID:28497540 Fig. 3A,B PMID:28497540 recruits PMID:28497540 fig 1D PMID:28497540 Fig 2b PMID:28497540 fig 1C PMID:28497540 fig 1C PMID:28497540 fig 1B PMID:28497540 fig 1B, 1D PMID:28497540 fig 1B PMID:28497540 fig 2b PMID:28497540 Fig. 5C PMID:28497540 Fig 3C PMID:28497540 Fig 3C PMID:28497540 `s4 PMID:28497540 (Fig. 2B) PMID:28513584 Fig. 3 PMID:28513584 Fig. 1 PMID:28513584 Fig. 2 PMID:28513584 Fig. S1 Not really abnormal, should be just bipolar PMID:28513584 Fig. S1 PMID:28513584 Fig. 1 PMID:28513584 Fig. 2 (main text) PMID:28513584 Fig. 2 PMID:28513584 Fig. 2 PMID:28513584 Main text (Figure S2 seems wrongly labelled) PMID:28513584 Fig. 2 PMID:28513584 Fig. 2 PMID:28513584 Fig. 3 PMID:28513584 Fig. 3 PMID:28513584 Fig. 3 PMID:28513584 Fig. 3 PMID:28513584 Fig. S4 PMID:28513584 Fig. S4 PMID:28513584 cut7D pkl1D klp9off does not elongate during anaphase B, cut7D pkl1D klp9D lethal, deleting all other kinesins except klp9 did not affect elongation after removing cut7 PMID:28513584 cut7D pkl1D cls1off lethal PMID:28513584 cut7D pkl1D ase1D lethal PMID:28513584 Fig. S3D and the fact that is required for bipolar spindle formation PMID:28513584 Fig. S3E PMID:28513584 Fig. 2 PMID:28515144 Increased duration of ssp2-T189 phosphorylation under osmotic stress PMID:28515144 Increased duration of ssp2-T189 phosphorylation under osmotic stress PMID:28515144 Increased duration of ssp2-T189 phosphorylation under osmotic stress PMID:28515144 Reduced ssp2-T189 phosphorylation under osmotic stress PMID:28515144 Reduced ssp2-T189 phosphorylation under osmotic stress PMID:28515144 Increased duration of ssp2-T189 phosphorylation under osmotic stress PMID:28515144 Abolished ssp2-T189 phosphorylation under osmotic stress PMID:28533364 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 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 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 see comment on cid14 PMID:28545058 Fig1A,B PMID:28545058 Fig1A,B PMID:28545058 Fig1A,B PMID:28545058 Fig1A,B PMID:28545058 Fig1A,B PMID:28545058 Fig1A,B PMID:28545058 Fig1A,B PMID:28545058 Fig1A,B In the paper this strain is called dss1 PMID:28545058 Fig1 D PMID:28545058 Fig1D PMID:28545058 Fig1D PMID:28545058 Fig1D PMID:28545058 Fig1D PMID:28545058 Fig1D PMID:28545058 Fig1D PMID:28545058 Fig1D PMID:28545058 Fig1D PMID:28545058 Fig1D PMID:28545058 Fig1D PMID:28545058 Fig1D PMID:28545058 Fig1D PMID:28545058 Fig1D PMID:28545058 data not shown PMID:28545058 Fig1C PMID:28545058 Fig1C rpn15 is called dss1 in this paper PMID:28545058 Fig2 A,B PMID:28545058 Fig2 A,B PMID:28545058 FigS1C,D PMID:28545058 Fig2A PMID:28545058 Fig3A,B PMID:28545058 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 Fig2A, B PMID:28545058 Fig3A PMID:28545058 nuclear accumulation of mRNA ************S5 Table microarrays used PMID:28545058 Fig2A PMID:28545058 Fig2A PMID:28545058 Fig 2A PMID:28545058 Fig4 A,B PMID:28545058 Fig4 A,B PMID:28545058 Fig 4C,D PMID:28545058 Fig 4A PMID:28545058 Fig 4c PMID:28545058 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 Fig 4D PMID:28545058 Fig 4D PMID:28545058 Fig1A,B PMID:28545058 Fig1A,B PMID:28545058 Fig1A,B PMID:28545058 Fig1A,B PMID:28545058 Fig1A,B PMID:28545058 Fig1A,B PMID:28552615 (Fig. S1C) PMID:28552615 (Fig. 2h) PMID:28552615 (Fig. 2h) PMID:28552615 (Fig. 2h) PMID:28552615 (Fig. 2i) PMID:28552615 (Fig. 3a) PMID:28552615 (Fig. S1C, 3A) PMID:28552615 3F and G PMID:28552615 "Is this translocase activaty or ""dislocase activity?"" Fig 5 (val, added substrate top2, this term will probably merge into displacement activityu). GO:0061995" PMID:28552615 (Fig. S1B) PMID:28552615 (Fig. S1B) PMID:28552615 (Fig. S1B) PMID:28552615 (Fig. S1B) PMID:28552615 (Fig. S1C) PMID:28552615 (Fig. S1C) PMID:28552615 (Fig. S1C) PMID:28552615 (Fig. S1C) PMID:28552615 (Fig. S1C) PMID:28552615 (Fig. S1C) PMID:28552615 (Fig. S1E) PMID:28552615 s2e PMID:28572514 fig 6 PMID:28572514 fig7 PMID:28572514 fig5 PMID:28572514 fig 9 PMID:28572514 fig7 PMID:28572514 vw: made more specific, during copper starvation PMID:28572514 vw: moved down to new FYPO:0006212 before germ outgrowth, during copper starvation PMID:28572514 fig7 PMID:28572514 Fig. 7 PMID:28572514 vw: moved down to new FYPO:0006212 before germ outgrowth, during copper starvation PMID:28572514 vw: moved down to new FYPO:0006212 PMID:28572514 see comment above PMID:28572514 fig 6 PMID:28572514 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 see comment above PMID:28572514 fig7 PMID:28586299 Figure 4B; decreased frequency of deletions at direct repeat recombination reporter PMID:28586299 Figure 4A; decreased frequency of deletions and gene conversions at direct repeat recombination reporter PMID:28586299 Figure 4C; increased frequency of deletions at direct repeat recombination reporter PMID:28586299 Figure 2; decreased frequency of gene conversions but unaltered frequency of deletions at direct repeat recombination reporter; deletions in a rad51∆ mutant depend on Rad52 PMID:28586299 Figure 4C; decreased frequency of gene conversions at direct repeat recombination reporter PMID:28600551 fig 5 PMID:28600551 fig 1 PMID:28600551 fig 1 PMID:28600551 I can never remember why e.g. sodium chloride isn't a child to salt stress PMID:28600551 fig 1 c PMID:28600551 fig 1 - They say they use YES in methods and fig2 PMID:28600551 fig 1 - They say they use YES in methods and fig2 PMID:28600551 fig 1 - They say they use YES in methods and fig2 PMID:28600551 fig 1 - They say they use YES in methods and fig2 PMID:28600551 fig 1 - They say they use YES in methods and fig2 PMID:28600551 fig 1 - They say they use YES in methods and fig2 PMID:28600551 fig 1 - They say they use YES in methods and fig2 PMID:28600551 fig 5 PMID:28600551 fig 1 - They say they use YES in methods and fig2 PMID:28600551 fig 5 PMID:28600551 fig 5 PMID:28600551 fig 5 PMID:28600551 fig 5 PMID:28600551 fig 5 PMID:28600551 fig 5 PMID:28600551 fig 5 PMID:28600551 fig 5 PMID:28600551 fig 5 PMID:28600551 fig 5 PMID:28600551 fig 5 PMID:28600551 fig 5 PMID:28600551 fig 2d PMID:28600551 fig 5 PMID:28600551 fig 4 PMID:28600551 fig 4 PMID:28600551 fig 2d PMID:28600551 fig 2e PMID:28600551 fig 2e PMID:28600551 fig 3d PMID:28600551 fig 5 PMID:28600551 fig 5 PMID:28600551 fig 5 PMID:28600551 fig 3d PMID:28600551 fig 1 - They say they use YES in methods and fig2 PMID:28600551 fig 1 - They say they use YES in methods and fig2 PMID:28600551 fig 2a PMID:28600551 fig 2a PMID:28600551 fig 3c PMID:28600551 fig 4 PMID:28600551 fig 4 PMID:28600551 fig 2a PMID:28600551 fig 4 PMID:28600551 fig 4 PMID:28600551 fig 4 PMID:28600551 fig 4 PMID:28600551 fig 5 PMID:28600551 fig 2c PMID:28600551 fig 2c PMID:28600551 fig 2a PMID:28600551 fig 2a PMID:28600551 fig 1d PMID:28600551 fig 1d PMID:28600551 fig 1d PMID:28619713 Fig. S1 B PMID:28619713 Fig. S1 B PMID:28619713 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 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 fig 6 C PMID:28619713 fig 6 C PMID:28631612 """poison"" product of shorter alternative transcript;assayed by expressing S.k. ortholog in S.p." PMID:28631612 """antidote"" product of longer alternative transcript; assayed by expressing S.k. ortholog in S.p." PMID:28640807 aerobic conditions PMID:28640807 aerobic conditions PMID:28640807 aerobic conditions PMID:28640807 aerobic conditions PMID:28640807 aerobic conditions PMID:28640807 Increased Cdc22 oxidation attenuated by 2 mM Glutathione. Increased Cdc22 oxidation attenuated by deleting tpx1. PMID:28640807 Increased Cdc22 oxidation attenuated by 2 mM Glutathione. Increased Cdc22 oxidation attenuated by deleting tpx1. PMID:28640807 2 mM Glutathione restores aerobic growth. PMID:28640807 2 mM Glutathione restores aerobic growth. PMID:28640807 aerobic conditions PMID:28640807 aerobic conditions PMID:28652406 whereas the expression of all stress genes in cells expressing HAAtf1.10D was not altered by sty1 deletion. Concomitantly PMID:28652406 expression of HA-Atf1.10D fully suppressed all stress defects of cells lacking Sty1 (Fig. 2C). PMID:28652406 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 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 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 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 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 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 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 vw, I deleted Caludias annotation by mistake when comparing to the older partially completed session by Laura, so adding back ! PMID:28652406 ditto PMID:28652406 that Pap1 is dispensable for the activation of gpd1 and hsp9 but required for ctt1 and srx1 (Fig. 5A) PMID:28652406 ditto PMID:28652406 ditto PMID:28652406 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 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 ditto PMID:28652406 Atf1.7M-HA are constitutively bound to the gpd1 and hsp9 promoters both before and after stress PMID:28652406 ditto PMID:28652406 ditto PMID:28652406 ditto PMID:28652406 ditto PMID:28652406 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 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 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 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 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 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 whereas the expression of all stress genes in cells expressing HAAtf1.10D was not altered by sty1 deletion. Concomitantly PMID:28652406 whereas the expression of all stress genes in cells expressing HAAtf1.10D was not altered by sty1 deletion. Concomitantly PMID:28652406 whereas the expression of all stress genes in cells expressing HAAtf1.10D was not altered by sty1 deletion. Concomitantly PMID:28652406 Atf1 is constitutively bound to srx1 and ctt1 in strain trr1.... PMID:28652406 ....whereas it is never recruited to these promoters in cells expressing Pap1.C523D (Fig. 5D). PMID:28656962 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 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 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 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 figure 5 b PMID:28656962 figure 5 b PMID:28656962 figure 5 b PMID:28656962 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 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 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 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 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 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 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 We observed that loss of Bhd1 and Ypt71, but not Ypt7, resulted in increased TORC1 activity, as determined by an increase in Rps6 and p70 S6K phosphorylation levels when cells were deprived of amino acids (Fig. 5a, compare lanes 1, 3, 5 and 7). PMID:28659415 Pil1p form filaments. Pil1 exchanges rapidly at the ends of these filaments in vivo. PMID:28659415 Pil1p form filaments. Pil1 exchanges rapidly at the ends of these filaments in vivo. PMID:28667014 LC-MS/MS PMID:28667014 LC-MS/MS and enzymatic assays were used to measure gluconate accumulation in wild-type and idn1Δ PMID:28667014 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:28674280 same as snf22delta alone PMID:28674280 same as snf22delta alone PMID:28674280 same as snf22delta alone PMID:28765164 fig2e PMID:28765280 3b PMID:28765280 figure 1D PMID:28765280 Fig. 7A PMID:28765280 Fig. 7A PMID:28765280 Fig 7A PMID:28765280 Fig 7A PMID:28765280 (Fig. 6G). PMID:28765280 6 ef PMID:28765280 Fig 6C PMID:28765280 Fig 6C PMID:28765280 Fig 6A PMID:28765280 3b PMID:28765280 Fig 1B PMID:28765280 Fig 2A PMID:28765280 Fig 1B PMID:28765280 Fig. 1EF PMID:28765280 figure 1B PMID:28765280 Fig 1A PMID:28765280 figure 2 PMID:28765280 we could probly go to increased degradation because of the bortezombin exp PMID:28771613 2B PMID:28771613 The preRC- loading delay was abolished in the irradiated gcn1Δ cells (Fig 3C), PMID:28771613 The preRC- loading delay was abolished in the irradiated gcn1Δ cells (Fig 3C), PMID:28771613 unfortunately no direct binding data, but physical interactions have been shown in other organisms PMID:28771613 1E PMID:28771613 1E PMID:28771613 1E PMID:28775153 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 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 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 Fig. S1, C and D) PMID:28784611 Figure 1C PMID:28784611 Figure 1C PMID:28784611 Figure S2E PMID:28784611 Figure S2A-B PMID:28784611 Figure S2A-B PMID:28784611 Figure S1C PMID:28784611 Figure S1D PMID:28784611 Figure 3D PMID:28784611 Figure 3B PMID:28784611 naintenence PMID:28784611 Figure 3E PMID:28784611 "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 Figure 1B PMID:28784611 Fig 1B PMID:28784611 fig S2C PMID:28784611 fig 5A PMID:28784611 fig 1 A&B PMID:28784611 Figure 1A PMID:28784611 Figure 1B PMID:28784611 Figure 3C PMID:28784611 phospholipid biosynthesis? PMID:28784611 fig 5 B CR slid- ing events no longer occurred in myo51Δ efr3Δ PMID:28784611 fig 5 B CR slid- ing events no longer occurred in myo51Δ efr3Δ PMID:28784611 Fig 3 A (in table, data not shown) PMID:28784611 Fig. S2 D PMID:28784611 Fig 2 A-C PMID:28784611 Fig 2 A-C PMID:28784611 Fig 2 A-C PMID:28784611 Fig. S1, C and D) PMID:28806726 replication forks stall with partial dependence on intra-S checkpoint (fig. 6) PMID:28806726 inhibition of origin firing requires intra-S checkpoint (fig. 5) PMID:28806726 replication forks stall with partial dependence on intra-S checkpoint (fig. 6) PMID:28806726 untreated (table S1) PMID:28806726 replication forks slow independently of intra-S checkpoint (fig. 6) PMID:28806726 inhibition of origin firing requires intra-S checkpoint (fig. 5) PMID:28806726 inhibition of origin firing requires intra-S checkpoint (fig. 5) PMID:28806726 replication forks stall with partial dependence on intra-S checkpoint (fig. 6) PMID:28811350 consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA PMID:28811350 consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA PMID:28811350 consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA PMID:28811350 consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA PMID:28821619 generated from MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28821619 generated by MMS mutagenesis PMID:28825727 (vw made more specific) Hi-C Supplementary Figs. 1b,f and 4a–c PMID:28825727 Cnd3 depletion following promoter shut-off and auxin-induced degron activation PMID:28825727 Cnd3 depletion following promoter shut-off and auxin-induced degron activation PMID:28825727 Supplementary Figs. 1b,f and 4a–c Cnd3 depletion following promoter shut-off and auxin-induced degron activation PMID:28825727 fig 2b hi-C difference assay PMID:28825727 hi C????? Supplementary Figs. 1b,f and 4a–c PMID:28825727 hic and 3C pcr fig 2d increased mitotic intra centromere connection PMID:28825727 fig 3 hi-C PMID:28827290 fig 3 PMID:28827290 fig 3 PMID:28827290 fig 3 PMID:28827290 fig 3 PMID:28827290 fig 3 PMID:28827290 fig 3 PMID:28827290 fig 3 PMID:28827290 fig 3 PMID:28827290 fig 3 PMID:28827290 fig 2D PMID:28827290 fig 6 PMID:28827290 fig 2C PMID:28827290 fig 2B PMID:28827290 figure 2B PMID:28827290 fig 2 PMID:28827290 fig 2 PMID:28827290 fig 1B PMID:28827290 fig 1B PMID:28827290 wt 68% fig 2C PMID:28827290 fig 5 PMID:28827290 fig 5 PMID:28827290 fig 5 PMID:28827290 fig 4 PMID:28827290 fig 4 PMID:28827290 fig 4 PMID:28827290 fig 3 PMID:28827290 fig 8 PMID:28827290 fig 7 PMID:28827290 fig 6 PMID:28827290 fig 6 PMID:28827290 fig 6 PMID:28827290 fig 6 PMID:28827290 fig 6 PMID:28841135 mRNA co-immunoprecipitated with ribosomes PMID:28882432 fig 3 PMID:28904333 especially at centromere; also at other regions where Ino80 complex normally binds PMID:28904333 especially at centromere; also at other regions where Ino80 complex normally binds PMID:28904333 25 degrees PMID:28904333 30 degrees PMID:28914606 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 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:28914606 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:28924043 Cdr1-K41A remains in nodes; Cdr1+ not tagged PMID:28924043 Cdr2 does not exit nodes (unlike Cdr1) upon osmotic stress PMID:28924043 Cdr1-K41A remains unphosphorylated; Cdr1+ not tagged PMID:28924043 combination of in vitro kinase assay and mutant phenotypes PMID:28934464 fig 3C PMID:28934464 fig 3C PMID:28934464 fig 3C PMID:28934464 fig 3D PMID:28934464 fig 3D PMID:28934464 fig 3E PMID:28934464 fig 3E PMID:28934464 5D a bit tenuous but we don't have this annotated.. PMID:28934464 5D a bit tenuous but we don't have this annotated.. PMID:28934464 I replaced GO:0090579 dsDNA loop formation as per https://github.com/geneontology/go-annotation/issues/3610 PMID:28934464 fig 3B PMID:28934464 fig S2D PMID:28934464 fig 3B PMID:28934464 fig 3C PMID:28944093 can't disambiguate salt from specific calcium sensitivity in these experiments PMID:28944093 can't disambiguate salt from specific calcium sensitivity in these experiments PMID:28944093 can't disambiguate salt from specific calcium sensitivity in these experiments PMID:28944093 can't disambiguate salt from specific calcium sensitivity in these experiments PMID:28947618 normal processing, complements partially sde2Δ PMID:28947618 Fig EV2B processing defective, does not complement sde2Δ PMID:28947618 Fig EV2B processing defective, does not complement sde2Δ PMID:28947618 Fig EV2B processing defective, does not complement sde2Δ PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 Fig 5B; Appendix Fig S5A and B PMID:28947618 (endo) mutant does not cleave Sde2 precursor PMID:28947618 (endo) mutant does not cleave Sde2 precursor PMID:28947618 assayed_using SPBC1778.02 | assayed_using SPAC227.16C | assayed_using SPBP16F5.02 PMID:28947618 fig 1B PMID:28947618 fig 1B PMID:28947618 Appendix Fig S2A PMID:28947618 Fig 2A &B PMID:28947618 Fig 2D PMID:28947618 Fig 2D PMID:28947618 Fig 3E (N-end rule pathway substrate) assayed_using(LysSde2-C) PMID:28947618 Fig 3E LysSde2-C (pro-obo/term-requests/119/), is N-end rule substrate PMID:28947618 Fig 4A PMID:28947618 (Fig 7A) PMID:28947618 (Fig 7A) PMID:28947618 (Fig 7A) PMID:28947618 Fig 8B in spliceosome PMID:28947618 Intron-Specific pre-mRNA Splicing PMID:28947618 Intron-Specific pre-mRNA Splicing PMID:28947618 column_17 Sde2UBL PMID:28947618 does not grow at high temperature, defective pre-mRNA splicing, assayed_using SPBC1778.02 | assayed_using SPAC227.16C | assayed_using SPBP16F5.02 PMID:28947618 decreased cell population growth at high temperature PMID:28947618 does not complement sde2Δ, defective in telomeric silencing and genome stability PMID:28947618 normal processing, protein very stable, complements partially sde2Δ PMID:28947618 normal processing, complements partially sde2Δ PMID:28947618 processing defective, does not complement sde2Δ PMID:28947618 fig 1 D does not complement sde2Δ PMID:28947618 fig 1 D complements partially sde2Δ PMID:28947618 normal processing, protein very stable, does not complement sde2Δ PMID:28947618 normal processing, protein unstable, complements partially sde2Δ PMID:28947618 normal processing, protein unstable, complements partially sde2Δ PMID:28947618 normal processing, protein stable, complements partially sde2Δ PMID:28947618 normal processing, protein very stable, complements partially sde2Δ PMID:28947618 normal processing, complements partially sde2Δ PMID:28947618 normal processing, protein stable, complements partially sde2Δ PMID:28947618 normal processing, protein very stable, complements partially sde2Δ PMID:28947618 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 normal processing, complements partially sde2Δ PMID:28947618 processing defective, does not complement sde2Δ PMID:28947618 normal processing, protein very stable, complements partially sde2Δ PMID:28947618 normal processing, protein unstable,complements partially sde2Δ PMID:28947618 normal processing, protein stable, complements partially sde2Δ PMID:28947618 normal processing, protein very stable, complements partially sde2Δ PMID:28947618 normal processing, complements partially sde2Δ PMID:28947618 normal processing, complements partially sde2Δ PMID:28947618 reduced processing, complements partially sde2Δ PMID:28947618 processing defective, does not complement sde2Δ PMID:28947618 Fig EV2B normal processing, complements sde2Δ PMID:28947618 Fig EV2B normal processing, complements sde2Δ PMID:28947618 Fig EV2B processing defective, does not complement sde2Δ PMID:28974540 Fig. S3, G and H PMID:28974540 Fig. S3 I additive, do we know %? PMID:28974540 added affected genes as extensions fig 3 E PMID:28974540 s3 E PMID:28974540 Fig. S2 A & 1E PMID:28974540 added affected genes as extensions fig 3 A-C PMID:28974540 added affected genes as extensions fig 3 A-C PMID:28974540 added affected genes as extensions fig 3 A-C PMID:28974540 Fig. S3 PMID:28974540 fig 1b PMID:28974540 added affected genes as extensions fig 3 E PMID:28974540 fig 3 PMID:28974540 fig 3 PMID:28974540 fig 3 G PMID:28974540 fig 4a PMID:28974540 fig 4c PMID:28974540 fig 4e PMID:28974540 (Fig. 4 G and see the Ubiquitin pull-down section of Materials and methods). PMID:28974540 5A PMID:28974540 fig 5b nuclear envelope PMID:28974540 fig 5b PMID:28974540 fig 5 D-G nuclear envelope PMID:28974540 fig 5 D-G nuclear envelope PMID:28974540 fig 6 PMID:28974540 fig 6 PMID:28974540 fig 6 PMID:28974540 fig 2E PMID:28974540 fig 2E PMID:28974540 fig 2E PMID:28974540 fig 2E PMID:28974540 vw: moved down to elongated (update fypo?) fig 1e PMID:28974540 fig 1a + others PMID:28974540 fig 1C PMID:28974540 fig 1 PMID:28974540 fig S2 PMID:28974540 s3 C PMID:28974540 Fig. S2 B PMID:28974540 fig 2E PMID:28974540 fig 2E PMID:28974540 fig 2E PMID:28974540 fig 2E PMID:28974540 fig1 PMID:28974540 5A PMID:28974540 added affected genes as extensions fig 3 A-C PMID:28974540 added affected genes as extensions fig 3 A-C PMID:28974540 added affected genes as extensions fig 3 A-C PMID:28974540 added affected genes as extensions fig 3 A-C PMID:28974540 added affected genes as extensions fig 3 A-C PMID:28976798 fig1 PMID:28976798 fig1 PMID:28976798 fig1 PMID:28976798 fig1 PMID:28976798 fig 1 D PMID:28977643 mhf1-L78R PMID:28977649 Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU PMID:28977649 Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU PMID:28977649 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 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 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 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 tRNA-Ser GCU and tRNA-Ser AGA unaffected PMID:28977649 tRNA-Ser GCU and tRNA-Ser AGA unaffected PMID:28977649 tRNA-Ser GCU and tRNA-Ser AGA unaffected PMID:28977649 tRNA-Ser GCU and tRNA-Ser AGA unaffected PMID:28977649 tRNA-Ser GCU and tRNA-Ser AGA unaffected PMID:28977649 Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU PMID:28977649 Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU PMID:28977649 tRNA-Ser GCU and tRNA-Ser AGA unaffected PMID:28977649 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 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 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 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 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 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:28982178 40 fold less PMID:29021344 Figure 4A and Supplemental Figure S4 PMID:29021344 Figure 1F PMID:29021344 Figure 2G PMID:29021344 (Supplemental Figure S1A). PMID:29021344 Figure 2E PMID:29021344 fig3C PMID:29021344 Figure S5D PMID:29021344 Figure S5D PMID:29021344 Figure 4B PMID:29021344 Figure 4A and Supplemental Figure S4 PMID:29021344 Figure 4A and Supplemental Figure S4 PMID:29021344 Figure 4A and Supplemental Figure S4 PMID:29032152 fig 2a PMID:29032152 fig2 PMID:29032152 fig2 b,c PMID:29032152 inferred from combined experiments PMID:29032152 fig 4 PMID:29032152 fig 4 PMID:29032152 Table 3 PMID:29032152 Table 3 PMID:29032152 Table 3 PMID:29032152 Table 3 PMID:29032152 Table 3 PMID:29032152 fig 4 PMID:29032152 fig4 PMID:29032152 fig 2 PMID:29032152 fig 3e PMID:29032152 fig 3e PMID:29032152 fig 3e PMID:29032152 fig 3b PMID:29032152 fig 3b PMID:29032152 fig 3b PMID:29032152 fig 3b PMID:29032152 fig 3b PMID:29032152 fig 1, 3b PMID:29032152 fig 2 PMID:29032152 fig 1 PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig6 PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 To conclude, upon nutrient starvation, TORC2 functions as both an activator and an inhibitor of sexual differentiation, the latter being mediated by Taf12 phosphorylation. PMID:29079657 fig1 PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:29079657 fig2 and supp table PMID:2908246 mild over expression of cdc13+ on multi copy plasmid pYep13 rescues the cdc13-117 ts phenotype. . PMID:2908246 Fig 3 PMID:2908246 mild over expression of cdc2+ on multi copy plasmid rescues the cdc13-117 ts phenotype PMID:2908246 mild over expression of cdc13+ on multi copy plasmid pYep13 causes slow growth PMID:2908246 Fig 3 PMID:29084823 Fig3A deletion of puc1 increases mating efficiency of zfs1 delta to WT PMID:29084823 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 Fig3C PMID:29084823 Fig7A shows that puc1delta shows increased mating efficiency at nitrogen levels which suppress mating in wild type cells PMID:29084823 Fig6A,B PMID:29084823 Fig6A,B PMID:29084823 Fig6A,B PMID:29084823 RNA PMID:29084823 Fig3C PMID:29084823 Fig3C, Fig7A shows that zfs1delta shows high mating efficiency at nitrogen levels which suppress mating in wild type cells wild type cells PMID:29084823 Fig4A,B about 10%? of Zfs1 is phosphorylated during vegetative growth PMID:29084823 Fig5E PMID:29084823 Fig5E PMID:29084823 Fig5C,D PMID:29084823 Fig5C,D PMID:29084823 Fig 5B, construct 3 PMID:29084823 Fig4A,B Zfs is hyperphosphorylated in response to nitrogen depletion PMID:29084823 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 Fig6 A,B PMID:29084823 Fig6A,B PMID:29084823 Fig6A PMID:29084823 Fig6A PMID:29084823 Fig5E PMID:29084823 Fig5E PMID:29084823 Fig3A deletion of cig2 does not rescue mating efficiency zfs1delta PMID:29084823 Fig3A deletion of cig1 does not rescue mating efficiency of zfs1 delta PMID:29084823 Fig6A,B PMID:29084823 Fig6A PMID:29084823 Fig6A PMID:29084823 Fig6A PMID:29084823 Figure 1A Sup Fig1 PMID:29084823 Figure 1C PMID:29084823 "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 Figure 1C PMID:29084823 Fig 2B,C fig6a PMID:29084823 Fig 2D, E, Sup Fig 2 PMID:29084823 Fig3A PMID:29109278 otr1R(SphI)::ura4+ PMID:29109278 otr1R(SphI)::ura4+ PMID:29109278 otr1R(SphI)::ura4+ PMID:29109278 otr1R(SphI)::ura4+ PMID:29109278 otr1R(SphI)::ura4+ PMID:29109278 otr1R(SphI)::ura4+ PMID:29109278 otr1R(SphI)::ura4+ PMID:29109278 tel2L::ura4+ PMID:29109278 mat3M::ura4+ PMID:29109278 otr1R(SphI)::ura4+ PMID:29109278 otr1R(SphI)::ura4+ PMID:29109278 otr1R(SphI)::ura4+ PMID:29123917 Later stage of meiotic prophase, observed by co-localisation with Taz1 PMID:29123917 S10 E and F PMID:29123917 fig6 PMID:29123917 Later stage of meiotic prophase, observed by co-localisation with Taz1 PMID:29134248 plasma membrane fusion during conjugation PMID:29134248 Fusion domain PMID:29134248 plasma membrane fusion during conjugation PMID:29136238 Fig4/5 PMID:29136238 fig7 PMID:29136238 Fig4/5 PMID:29136238 Fig3 PMID:29136238 Fig2 PMID:29136238 Fig2 PMID:29136238 Fig2 PMID:29136238 Fig2 PMID:29136238 Fig2 PMID:29136238 Fig3 PMID:29136238 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 Fig3 PMID:29136238 Fig1 PMID:29136238 Fig1 PMID:29136238 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 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 Fig4 PMID:29136238 Fig3 PMID:29136238 Fig4 PMID:29149597 The localization of Poz1, Tpz1 and Rap1 proteins are assayed. PMID:29149597 The localization of Poz1, Tpz1 and Rap1 proteins are assayed. PMID:29149597 The localization of Poz1, Tpz1 and Rap1 proteins are assayed. PMID:29149597 The localization of Poz1, Tpz1 and Rap1 proteins are assayed. PMID:29149597 The localization of Poz1, Tpz1 and Rap1 proteins are assayed. PMID:29149597 The localization of Poz1, Tpz1 and Rap1 proteins are assayed. PMID:29167352 often in a punctate manner PMID:29167352 (Fig. 1C PMID:29167352 (Fig. 1C PMID:29167352 (Fig. 1C 28 Celcius PMID:29167352 fig 4. Klp2 is not required, but acts collaboratively with Pkl1, in anchoring the spindle microtubule to the mitotic SPB PMID:29167352 ~30% of the double mutant cells exhibited the monopolar spindle phenotype. PMID:29167352 (Fig. 1C PMID:29167352 (Fig. 1C PMID:29167352 (Fig. 1C PMID:29167352 28 celcius PMID:29167439 increase with telomere shortening and time in quiescence PMID:29167439 increase with telomere shortening and time in quiescence PMID:29167439 require for subtelomeric DNA amplification in G0 PMID:29167439 limit subtelomeric DNA amplification in G0 PMID:29167439 Require for subtelomeric DNA amplification in G0 PMID:29180432 fig 5 (measured at 4 um spindle. WT has 6%) PMID:29180432 fig 4 PMID:29180432 fig 3 PMID:29180432 figure 3 PMID:29180432 fig 5f PMID:29180432 increased duration of metaphase Fig. 5E PMID:29180432 Fig. 5 B and D PMID:29180432 figure 3 PMID:29180432 fig3 PMID:29180432 fig 6 PMID:29180432 fig 2G PMID:29180432 fig 2G PMID:29180432 fig 2G PMID:29180432 fig6 PMID:29194511 fig 1b &C PMID:29194511 Figure S1A and B PMID:29194511 fig 1b &C PMID:29194511 fig 1b &C and 3H PMID:29194511 fig 1b &C and 3H PMID:29194511 fig 1b &C PMID:29194511 Figure S1A and B PMID:29194511 Figure S1A and B PMID:29194511 Figure S1A and B PMID:29194511 Figure 3C-D, Supplementary Figure 8A-B PMID:29194511 Figure 2A,B,C PMID:29194511 fig 1b &C PMID:29194511 fig 1b &C PMID:29194511 fig 4a PMID:29194511 fig 4b PMID:29194511 fig 4b PMID:29194511 Figure 2E-F, supplementary figure 5 PMID:29194511 fig 5 PMID:29194511 fig 4a PMID:29194511 Figure 2G, supplementary figure 4 PMID:29194511 fig 1b &C PMID:29194511 fig 1b &C PMID:29194511 Figure 3E-F, Supplementary figure 8 C-D PMID:29214404 at telomeres 1L, 1R, 2L, 2R PMID:29214404 at telomere 1R PMID:29214404 greater decrease at telomeres 1R and 2L than at 1L and 2R PMID:29214404 at telomeres 1L, 2R PMID:29215009 same as either single mutant PMID:29215009 same as exo1delta alone PMID:29215009 upstream reporter PMID:29215009 upstream reporter PMID:29216371 IMP evidence for part_of extension PMID:29216371 IMP evidence for part_of extension PMID:29249658 figure S4C PMID:29249658 figure 1c PMID:29249658 fig 1 `D,E ~55% PMID:29249658 fig 1 PMID:29249658 fig 1 PMID:29249658 fig 1 PMID:29249658 CHeCK phenotypes PMID:29249658 fig 2A PMID:29249658 fig 2A PMID:29249658 figure 2D PMID:29249658 fig 2A PMID:29249658 fig 2A PMID:29249658 fig 3h PMID:29249658 fig 3D PMID:29249658 Figure 3D PMID:29249658 Figure S-3F PMID:29249658 Figure S-3F PMID:29249658 Figure S-3F PMID:29249658 Figure S-3F PMID:29249658 Figure S-3F PMID:29249658 Figure S-3F PMID:29249658 Fig 4F (lasso) PMID:29249658 Fig 4F PMID:29249658 fig 1B PMID:29249658 figure S4C PMID:29249658 figure S4C PMID:29249658 figure S4C PMID:29249658 Fig 4C D PMID:29249658 Fig 4C D PMID:29249658 Figure 3H PMID:29249658 fig 3 PMID:29249658 fig 3 PMID:29249658 fig 3D PMID:29249658 fig S3A PMID:29249658 fig 3c PMID:29249658 fig 3B PMID:29249658 fig 3A PMID:29249658 fig 2A PMID:29249658 figure 2 PMID:29249658 figure 2 PMID:29249658 figure 2 PMID:29249658 fig 2 PMID:29249658 fig 2A PMID:29249658 fig 2A PMID:29249658 fig 1B PMID:29259000 fig2A PMID:29259000 fig5 PMID:29259000 fig 7D,E,F PMID:29259000 Figure 6 PMID:29259000 fig 5E PMID:29259000 fig S5A PMID:29259000 fig 5D PMID:29259000 fig 5 PMID:29259000 Figure 4 PMID:29259000 Figure 4A and B: MI NDJ PMID:29259000 Figure 4A and B: MI NDJ PMID:29259000 Figure S3C-E PMID:29259000 Figure S3C-E PMID:29259000 Figure 3F PMID:29259000 fig 3D PMID:29259000 fig 3D PMID:29259000 fig2 abolished asci formation PMID:29259000 fig2 PMID:29259000 fig 2A abolished entry into meiosis (at pre meiosis?) PMID:29259000 fig 2A abolished entry into meiosis (at pre meiosis?) PMID:29290560 (Figure 1F) ER-PM uncoupling PMID:29290560 Figures 1D and S1F ER-PM uncoupling *********lateral PM PMID:29290560 Figures 1D and S1F PMID:29290560 fig1 ER plasma membrane tethering ER-PM contact removal OR abnormal ER-PM contact formation PMID:29290560 Fig 2A PMID:29290560 Figure 2E PMID:29290560 FIg 3C PMID:29290560 Figure 3C PMID:29290560 Figure 3C PMID:29290560 Fig 3D PMID:29290560 Fig 3D PMID:29290560 Fig 3D PMID:29290560 fig1 PMID:29290560 Figures 1C and S1C ER-PM contact removal PMID:29292846 fig5 PMID:29292846 DNA binding site: 1-60 a.a. PMID:29292846 fig5 PMID:29292846 fig4 PMID:29292846 fig4 PMID:29292846 fig4 PMID:29292846 fig5 PMID:29292846 fig5 PMID:29292846 fig5 PMID:29292846 fig 5 PMID:29292846 fig3 PMID:29292846 fig3 PMID:29292846 fig5 PMID:29292846 fig3 PMID:29292846 Deletion of LEM domain decreases the association of Lem2 at the centromere PMID:29292846 fig 1a residues 200-307 PMID:29292846 fig2 PMID:29292846 fig2 PMID:29292846 fig2 PMID:29292846 fig2 PMID:29292846 fig2 PMID:29319508 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 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 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 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 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 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 fig3 PMID:29330317 fig3 PMID:29343550 Figure 4A LifeAct-mcherry PMID:29343550 Figure 1A-B PMID:29343550 Figure 1C PMID:29343550 Figure 2C DAPI, methyl blue PMID:29343550 Figure 4A LifeAct-mcherry issues/3215 PMID:29343550 Figure 4A LifeAct-mcherry PMID:29343550 Figure 4E-F tagged with GFP PMID:29343550 Figure 4C 4Cmcherry PMID:29343550 Figure 4Cmcherry PMID:29343550 Figure 4E tagged with GFP PMID:29343550 Figure 3A allele tagged with mNeonGreen PMID:29343550 Figure 3A allele tagged with mNeonGreen PMID:29343550 Figure 4A LifeAct-mcherry PMID:29343550 Figure 2C DAPI, methyl blue PMID:29343550 Figure 5 PMID:29343550 Figure 5 PMID:29343550 Figure 5 PMID:29343550 Figure 5 PMID:29352077 figure 3 PMID:29352077 figure 3 PMID:29352077 figure 3 PMID:29352077 figure 3 PMID:29352077 figure 2 PMID:29352077 figure 2 PMID:29352077 figure 4 PMID:29352077 figure 4 PMID:29352077 figure 4 PMID:29352077 figure 4 PMID:29352077 figure 4 PMID:29352077 figure 3 PMID:29352077 figure 3 PMID:29352077 figure 3 PMID:29352077 figure 3 PMID:29352077 figure 3 PMID:29352077 figure 3 PMID:29352077 figure 3 PMID:29352077 figure 4 PMID:29352077 figure 4 PMID:29352077 figure 4F PMID:29352077 figure 3 PMID:29352077 figure 3 PMID:29352077 figure 3 PMID:29414789 8c PMID:29414789 Northern blot and primer extension analysis PMID:29414789 Northern blot and primer extension analysis PMID:29414789 Northern blot and primer extension analysis PMID:29414789 Northern blot and primer extension analysis PMID:29414789 Northern blot and primer extension analysis PMID:29414789 Primer extension analysis PMID:29414789 Primer extension analysis PMID:29414789 Primer extension analysis PMID:29414789 GONEW: negative regulation of cellular response to phosphate starvation PMID:29414789 Primer extension analysis PMID:29414789 Primer extension analysis PMID:29414789 Primer Extension Analysis PMID:29414789 Primer extension analysis PMID:29414789 Primer extension analysis PMID:29414789 Primer extension analysis PMID:29422501 fig2 PMID:29422501 fig 3a PMID:29422501 fig 1 a PMID:29422501 fig1 c PMID:29422501 fig1 c PMID:29422501 fig 1c PMID:29422501 fig2 PMID:29422501 fig 1c PMID:29422501 fig2 PMID:29422503 Lsm3 protein level was not affected by est1∆. PMID:29422503 Fig. 4f Lsm3 binding to telomeres was not affected by est1∆. PMID:29422503 Lsm3 protein level was not affected by trt1∆. PMID:29422503 Fig. 4f Lsm3 binding to telomeres was not affected by trt1∆. PMID:29422503 Lsm3 protein level was not affected by ter1∆. PMID:29422503 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 (created to replace WT phenotype) PMID:29422503 (created to replace WT phenotype) PMID:29422503 (created to replace WT phenotype annotation) lsm3-myc chip PMID:29422503 Fig. 4f Lsm3 binding at telomeres is increased by ter1∆. PMID:29422503 Lsm3 protein level was not affected by pof8∆. PMID:29422503 Fig. 4f PMID:29422503 Fig. 4c Lsm3-TER1 interaction is abolished in pof8∆ cells. PMID:29422503 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 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 Fig. 3a Pof8-TER1 interaction is not affected by est1∆. PMID:29422503 Fig. 3a) Pof8-TER1 interaction is reduced but not eliminated in trt1∆ cells. PMID:29422503 figure 1 a PMID:29422503 Trt1 binding is reduced to ~58% of pof8+ cells, but not as severely reduced as pof8∆ cells (~35%). PMID:29422503 fig 6 b PMID:29422503 Fig. 3a Pof8-TER1 interaction is reduced but not eliminated in ccq1∆. PMID:29422503 Pof8 expression was not affected by est1∆. PMID:29422503 fig 1 e Localization of Pof8 at telomeres is reduced but not eliminated in est1∆. PMID:29422503 fig 6 PMID:29422503 fig 6 PMID:29422503 Supplementary Fig. 4 PMID:29422503 fig 5 PMID:29422503 figs 1-3 PMID:29422503 Supplementary Fig. 4 PMID:29422503 Pof8 expression level is not affected by trt1∆. PMID:29422503 fig 1 e Localization of Pof8 at telomeres is reduced but not eliminated in trt1∆. PMID:29422503 Pof8 expression level is not affected in ccq1∆. PMID:29422503 fig 1 e Localization of Pof8 at telomeres is reduced but not eliminated in ccq1∆. PMID:29422503 Pof8 expression level was not altered in ter1∆ cells. PMID:29422503 fig 1 e Localization of Pof8 at telomeres is reduced but not eliminated in ter1∆. PMID:29422503 (created to replace WT phenotype annotation) PMID:29422503 (created to replace WT phenotype annotation) fig 3 b PMID:29422503 (created to replace WT phenotype annotation) est1-myc chip PMID:29422503 (created to replace WT phenotype annotation) trt1-myc chip PMID:29422503 fig 3a (created to replace WT phenotype annotation) PMID:29422503 fig 1 e PMID:29422503 fig 1 e PMID:29422503 fig 1 e PMID:29422503 fig 1 c/d PMID:29422503 fig 1 c/d PMID:29422503 fig 1 c/d PMID:29422503 (created to replace WT phenotype annotation) Fig. 1e PMID:29422503 Fig 1 PMID:29422503 Trt1 binding is reduced to ~80% of pof8+ cells, but not as severely reduced as pof8∆ cells (~35%). PMID:29422503 Trt1 binding is reduced to ~70% of pof8+ cells, but not as severely reduced as pof8∆ cells (~35%). PMID:29422503 Est1 expression level detected by western in ter1∆ cells was similar to Est1 level in ter1+ (wild-type) cells. PMID:29422503 Est1 binding to telomeres is reduced to near no binding in ter1∆, based on ChIP assay. PMID:29422503 fig 3 b PMID:29422503 Fig. 3c Interaction between Est1 and TER1 was not affected by pof8∆. PMID:29422503 Est1 showed similar expression level in pof8∆ cells as wild-type cells. PMID:29422503 moderately reduced less severe thanin ter1∆ cells. PMID:29422503 Telomere binding of Est1 is reduced in pof8∆ cells. PMID:29422503 Trt1 expression level detected by western blot is reduced in ter1∆ cells. PMID:29422503 Based on ChIP, ter1∆ cause loss of telomerase (Trt1) localization at telomeres. PMID:29422503 fig 1 c/d Trt1-myc ChIP PMID:29422503 pof8∆ rif1∆ cells showed short telomeres, very similar to pof8∆ cells. PMID:29422503 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 pof8∆ rap1∆ cells showed shortened telomeres, more similar to pof8∆, rather than highly elongated telomeres in rap1∆ cells. PMID:29422503 pof8∆ taz1∆ showed much shorter telomere length (almost like wild-type cells) than taz1∆ cells, but showed some rearrangement in sub-telomeres. PMID:29422503 figure 1a Telomere shortening is similar to pof8∆ cells. PMID:29422503 fig1 Lose telomere signal, much like trt1∆ cells. PMID:29422503 Supplementary Fig. 4 PMID:29422503 Supplementary Fig. 4 PMID:29422503 figs 1-3 PMID:29422503 (created to replace WT phenotype annotation) PMID:29422503 fig 6 pof8-∆[289-402] cells show as short telomere as pof8∆ cells. PMID:29422503 fig 6 pof8-∆[390-402] cells show as short telomere as pof8∆ cells. PMID:29422503 fig 6 pof8-R343A cells show as short telomere as pof8∆ cells. PMID:29422503 fig 6 pof8-Y330A cells show as short telomere as pof8∆ cells. PMID:29422503 Trt1 binding is reduced to ~69% of pof8+ cells, but not as severely reduced as pof8∆ cells (~35%). PMID:29422503 fig 5 PMID:29422503 fig 5 PMID:29422503 fig 5 PMID:29422503 fig 5 PMID:29422503 Fig. 4e PMID:29422503 Fig. 4d PMID:29424342 ts background fig5 PMID:29424342 4 PMID:29424342 fig5 PMID:29424342 fig5 PMID:29424342 6 PMID:29424342 6 PMID:29424342 6 PMID:29424342 ts background fig5 PMID:29424342 4 PMID:29424342 4 PMID:29424342 4 PMID:29424342 fig2 PMID:29424342 4b PMID:29424342 4 PMID:29432178 Can we say somewhere - overexpresses genes involved by amino acid starvation, or something similar? PMID:29432178 Fig. 3A PMID:29432178 Fig. 3A PMID:29432178 Fig. 3E PMID:29432178 Fig. 3B during normal growth PMID:29432178 Fig. 3A PMID:29432178 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 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:29453312 ras1 mutant cells undergo precocious fusion resulting in cell lysis PMID:29453312 Ras activity increases during the mating process and is maximum at the fusion site just before the fusion event. PMID:29453312 Active Ras1 is localized to cell poles during mitotic growth PMID:29453312 In the absence of efc25 Ras1 is not activated at the cell cortex PMID:29453312 Ative Ras1 localizes to septa during mitotic growth PMID:29453312 Active Ras1 co-localizes with the actin fusion focus during the process of cell-cell fusion PMID:29453312 Ste6 co-localizes with the actin fusion focus during the process of cell-cell fusion PMID:29453312 Active Ras1 is localized to cell poles during mitotic growth PMID:29453312 In the absence of efc25 Ras1 is not activated at the cell cortex PMID:29453312 In the absence of gap1 Ras activity increases and decorates the entire cortex of vegetative growing cells PMID:29453312 Active Ras1 is localized to cell poles during mitotic growth PMID:29453312 ras1 mutant cells undergo precocious fusion resulting in cell lysis PMID:29458562 fig4 PMID:29458562 fig4 PMID:29458562 fig3 PMID:29458562 fig3 PMID:29458562 DNS PMID:29458562 Fig. 2 PMID:29458562 Fig. 2 PMID:29458562 Fig. 2 PMID:29458562 Fig. 2 PMID:29458562 fig3 abolished PMID:29458562 fig2 (likey due to intron encoded maturase) PMID:29458562 fig4 PMID:29458562 fig4 PMID:29458562 fig4 PMID:29458562 fig3 PMID:29514920 Fig. 1A PMID:29514920 Fig 1A PMID:29514920 Fig 1A PMID:29514920 Fig 1C PMID:29514920 fig2B PMID:29514920 figure 2B PMID:29514920 Fig. 1A PMID:29514920 Fig 1A PMID:29514920 Fig 1A PMID:29514920 Fig 2C protein localizes to cytoplasm, nucleus, and spindle-pole body. PMID:29514920 figure 2D Epistatic to cdr2delta PMID:29514920 affecting Cdr1 vw:ig. S2, F and G PMID:29514920 fig 3D Affecting Wee1 PMID:29514920 figure 2B PMID:29514920 Affecting Wee1 vw Increased , term pending PMID:29514920 figure 2B PMID:29514920 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 affecting Wee1 PMID:29514920 figure 2D Epistatic to cdr2delta PMID:29514920 Fig 1B PMID:29529046 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 Fig 8 PMID:29529046 Fig 8 PMID:29529046 Fig 8 PMID:29529046 Fig 8 PMID:29529046 "We made the term ""zinc ion import into organelle""in GO becuse it fits better witht the descendants" PMID:29529046 "We made the term ""zinc ion import into organelle""in GO becuse it fits better witht the descendants" PMID:29529046 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 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 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 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 Zrg17 also transports zinc out of the cytosol when zinc is available (as well as when it is limiting) PMID:29529046 Fig 4 BE PMID:29529046 Figure 1 (EDTA, zinc chelator) PMID:29529046 Figure 1 (EDTA, zinc chelator) PMID:29529046 fig6 PMID:29529046 Fig 8 PMID:29529046 Fig 8 PMID:29529046 Fig 8 PMID:29529046 Fig 8 PMID:29529046 The experiment performed was to measure total cellular zinc ion levels in a zrt1D strain during a zinc shock (Figure 4A) PMID:29529046 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 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 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:29549126 fig6 PMID:29549126 assayed using heme analog ZnMP PMID:29549126 assayed using heme analog ZnMP PMID:29549126 assayed using heme analog ZnMP PMID:29549126 fig7 PMID:29549126 fig7 PMID:29549126 3B,C, PMID:29549126 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 fig6 PMID:29596413 fig 7C PMID:29596413 fig 7 PMID:29596413 fig 7 PMID:29596413 fig 7C PMID:29596413 fig 7C PMID:29596413 fig 7C supression of trm7-delta PMID:29596413 fig 7C supression of trm7-delta PMID:29596413 fig 7 PMID:29596413 fig 7C PMID:29596413 fig 7C supression of trm7-delta PMID:29596413 fig 7C supression of trm7-delta PMID:29596413 fig 7C supression of trm7-delta PMID:29596413 fig 7C supression of trm7-delta PMID:29596413 fig 7 PMID:29610759 at MPS1 PMID:29610759 fig 1 PMID:29610759 fig 1 PMID:29610759 fig 5 PMID:29610759 figs 1 & 4 PMID:29610759 figs 1 & 4 PMID:29610759 enriched at mat1 right border and cenH left border; fig 1 PMID:29610759 fig 2 PMID:29632066 fig S1B PMID:29632066 fig S1B PMID:29632066 fig S1B PMID:29641590 fig3 PMID:29641590 fig3 PMID:29641590 fig3 PMID:29641590 A1 cleavage PMID:29641590 A2 cleavage PMID:29641590 A0 cleavage PMID:29641590 fig3 PMID:29689193 figure 3B PMID:29689193 thicker and thinner, disrupted homeostasis PMID:29689193 figure 2 F PMID:29689193 Promotes cell wall thickness hoemostasis PMID:29689193 Promotes cell wall thickness hoemostasis PMID:29689193 Promotes cell wall thickness hoemostasis PMID:29689193 fig 3C PMID:29689193 figure 3B PMID:29689193 thicker and thinner, disrupted homeostasis PMID:29689193 thicker and thinner, disrupted homeostasis PMID:29699848 abolished interaction with gad8 PMID:29699848 affect interaction with Tor1 PMID:29735656 figure 3c PMID:29735656 fig 4e PMID:29735656 figure 4d PMID:29735656 figure 3, figure S1B PMID:29735656 figure 1 A PMID:29735656 figure 1 A PMID:29735656 figure 1 A PMID:29735656 figure 1 A PMID:29735656 figure 1 A PMID:29735656 figure 1 A PMID:29735656 figure 2 AB inactive separase, uncleavable kleisin PMID:29735656 figure 3, figure S1B PMID:29735656 figure 3, figure S1B PMID:29735656 figure 3, figure S1B PMID:29735656 figure 3, figure S1B PMID:29735656 figure 3, figure S1B PMID:29735656 figure 3, figure S1B PMID:29735656 figure 3, figure S1B PMID:29735656 figure 3, figure S1B PMID:29735656 figure 3, figure S1B PMID:29735656 fig 4b PMID:29735656 fig 4b PMID:29735656 fig 4b PMID:29735656 figure 3, figure S1B PMID:29735656 figure 3, figure S1B PMID:29735656 figure 2 AB inactive separase, uncleavable kleisin PMID:29735656 figure 3, figure S1B PMID:29735656 figure 1A, supp S1A PMID:29735656 figure 1A, supp S1A PMID:29735656 figure 1 A PMID:29735656 figure 2 AB inactive separase, uncleavable kleisin PMID:29735656 figure 2 AB inactive separase, uncleavable kleisin PMID:29735656 figure 1 A PMID:29735656 figure 1 A PMID:29735656 figure 1 A PMID:29735656 figure 1 A PMID:29735656 S4 PMID:29735656 S4 PMID:29735745 Fig 2 B PMID:29735745 binds to the consensus sequence CCCCAY (Fig. 4) PMID:29735745 binds to the consensus sequence CCCCAY (Fig. 4) PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 5 A, 5 C PMID:29735745 Fig. 5 A PMID:29735745 Fig. 5 A PMID:29735745 Fig. 5 A PMID:29735745 Fig. 5 B PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 2 D PMID:29735745 Fig. 2 D PMID:29735745 Fig. 2 D PMID:29735745 Fig. 2 D PMID:29735745 Fig. 1 C PMID:29735745 Fig. 1 E PMID:29735745 Fig. 1 D PMID:29735745 Fig. 1 E PMID:29735745 Fig. 1 E PMID:29735745 Fig. 1 C PMID:29735745 Fig. 1 C PMID:29735745 Fig. 1 D PMID:29735745 Fig. S2 D PMID:29735745 Fig. S2 D PMID:29735745 Fig. 7 D PMID:29735745 Fig. 5G PMID:29735745 Fig. 5 G PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 5 B PMID:29735745 Fig. 5 B PMID:29735745 Fig. 5 C PMID:29735745 Fig. 5 B PMID:29735745 Fig. 5 C PMID:29735745 Fig. 5 F PMID:29735745 Fig. 6 B, C PMID:29735745 Fig. 6 B, C PMID:29735745 Fig. 6 B, C PMID:29735745 Fig. 6 B, C PMID:29735745 Fig. 6 B, C PMID:29735745 Fig. 6 B, C PMID:29735745 Fig. 6 B, C PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 5 A, B, C; Fig. 7 C PMID:29735745 Fig. 5 A, B, C; Fig. 7 C PMID:29735745 binds to the consensus sequence CCCCAY (Fig. 4) PMID:29735745 binds to the consensus sequence CCCCAY (Fig. 4) PMID:29735745 Video S2 PMID:29735745 Video S2 PMID:29735745 Fig. 2 C PMID:29735745 Fig. 2 C PMID:29735745 Fig. 5 H PMID:29735745 Fig. 5 H PMID:29735745 Fig S2 F PMID:29735745 Fig. S2 F PMID:29735745 Fig S2 F PMID:29735745 Fig. S2 F PMID:29735745 Fig. S2 F PMID:29735745 Fig. S2 F PMID:29735745 Fig. S2 D PMID:29735745 Fig. S2 D PMID:29735745 Fig. S2 D PMID:29735745 Fig. S2 D PMID:29735745 Fig. S2 D PMID:29735745 Fig S2 D PMID:29735745 Fig. S2 D PMID:29735745 Fig 7 D PMID:29735745 Fig. 7 C PMID:29735745 Fig. 7 B PMID:29735745 Fig. 7 B PMID:29735745 Fig. 7 C PMID:29735745 Fig. 7 B PMID:29735745 Fig. 7 B PMID:29735745 Fig. 7 B PMID:29735745 Fig. 6 B PMID:29735745 Fig. 6 D PMID:29735745 Fig 6 B, C PMID:29735745 Fig. 6 B, C PMID:29735745 Fig. 6 B, C PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig. 3 D PMID:29735745 Fig 2 B PMID:29735745 Fig. 2 D PMID:29742018 in vitro, casein substrate PMID:29742018 normal with and without spindle checkpoint activation PMID:29742018 in vitro, casein substrate PMID:29742018 normal with and without spindle checkpoint activation PMID:29742018 in vitro, casein substrate PMID:29742018 in vitro, casein substrate PMID:29742018 in vitro, casein substrate PMID:29742018 in vitro, casein substrate PMID:29742018 in vitro, casein substrate PMID:29742018 in vitro, casein substrate PMID:29742018 Hhp1 accumulates at SPB when spindle checkpoint activated PMID:29774234 Sensitive to HU, CPT and MMS PMID:29774234 slightly better growth than stn1-226 alone PMID:29774234 same as stn1-226 alone PMID:29774234 Exacerbated at high temperature PMID:29774234 loss of telomeric and subtelomeric sequences at high temperature PMID:29804820 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 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 (Figures 6A and 6B). PMID:29804820 A Homodimer of the Mis18 C-Terminal Domain Interacts with a Mis16-Eic1 Heterodimer PMID:29804820 The Stoichiometry of the S. pombe Mis18 Holo-Complex Is (Mis16)2:(Eic1)2:(Mis18)4 T PMID:29804820 The Stoichiometry of the S. pombe Mis18 Holo-Complex Is (Mis16)2:(Eic1)2:(Mis18)4 T PMID:29804820 The Stoichiometry of the S. pombe Mis18 Holo-Complex Is (Mis16)2:(Eic1)2:(Mis18)4 T PMID:29804820 FIgure 4D PMID:29804820 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 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 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 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 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 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 Fig S3D. The timing of septation onset depends on the AR function. The start of septation is delayed when the function of the AR unconventional type II myosin Myp2 is compromised. PMID:29813053 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 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 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 Fig 2. The start of septation scales with anaphase B progression and correlates linearly with the cell length. PMID:29813053 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 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 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 Fig 3 PMID:29813053 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 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 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 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 Fig 3 PMID:29813053 Fig 4D & E PMID:29813053 Fig 5B, Table 1; also inferred from localization timing PMID:29813053 Fig 56A-D; also inferred from localization timing PMID:29813053 Fig 56E; also inferred from localization timing PMID:29844133 beware using old strains, phenotypic changes observed. PMID:29844133 Beware using aged colonies, cell size recovery observed. PMID:29851556 in the presence or absence of Nbs1 PMID:29851556 localization of mutated protein assayed PMID:29866182 Myc-Ago1 PMID:29866182 FLAG-Ago1, Arb1-Myc PMID:29866182 FLAG-Ago1 PMID:29866182 FLAG-Ago1, Arb1-Myc PMID:29866182 Tas3-Myc PMID:29866182 Myc-Ago1 PMID:29866182 FLAG-Ago1 PMID:29898918 slightly worse than srs2delta alone PMID:29898918 Required for cellular resistance to MMS and CPT. PMID:29898918 present in cycling cells and meiosis I cells. Required for cellular resistance to MMS and CPT. PMID:29898918 Epistatic genetic interaction (same as mus81delta alone) PMID:29898918 Epistatic genetic interaction (same as eme1delta alone) PMID:29898918 Epistatic genetic interaction (same as mus81delta alone) PMID:29898918 Epistatic genetic interaction (same as eme1delta alone) PMID:29898918 slightly worse than srs2delta alone PMID:29898918 Epistatic genetic interaction (same as mus81delta alone) PMID:29898918 Epistatic genetic interaction (same as mus81delta alone) PMID:29899453 Extended Data Fig 4d Added Dis2 extension PMID:29899453 Fig 1b PMID:29899453 Fig 3e PMID:29899453 Extended Data Fig 4d (vw: fixed allele) PMID:29899453 Extended Data Fig 5a vw: fixed allele and target PMID:29899453 Extended Data Fig 5a vw: fixed allele and target PMID:29899453 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 Fig. 2d, PMID:29899453 Fig S2, Extended Data Fig. 2d PMID:29899453 Fig S2, Extended Data Fig. 2c PMID:29899453 check this addition Fig. 2a, Extended Data Fig. 2a PMID:29899453 Fig. 1d, Extended Data Fig. 1d) PMID:29899453 FIgure 3d. Extended fig 8d (vw: some suppression?) PMID:29899453 fig 6a.b PMID:29899453 Fig. 2e, Extended Data Fig. 4c PMID:29899453 Fig. 2e, Extended Data Fig. 4b PMID:29899453 Extended Data Fig 3a ig. 2c, Extended Data Fig. 3b–d) PMID:29899453 Extended Data Fig 2f PMID:29899453 Extended Data Fig 2f PMID:29899453 Fig. 1d, Extended Data Fig. 1d) PMID:29899453 fig 1c PMID:29899453 Fig 1c, Extended Data Fig 2a PMID:29899453 fig 1c PMID:29899453 fig 1b PMID:29899453 Fig 1B vw: corrected back to dis2 not cdk9! PMID:29899453 fig 1b PMID:29899453 Fig 3e PMID:29899453 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 Extended Data Fig 2f .(cdk9as, cdk9as ssu72C13S, ssu72C13S) PMID:29899453 Extended Data Fig 5d . PMID:29899453 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 Extended Data Fig 6e Cdk9 does not restrict chromatin recruitment of Sds21. PMID:29899453 Extended Data Fig 4a Cdk9 inhibition increased chromatin recruitment of Dis2 PMID:29899453 fig 1d PMID:29899453 fig 1d PMID:29899453 figure 3 e PMID:29899453 figure 3 e Also increased termination index Fig. 4e PMID:29899453 Extended Data Fig 3a ig. 2c, Extended Data Fig. 3b–d) PMID:29899453 Extended data figure 9 PMID:29899453 extended data figure 9 decreased RNA pol2 localization to chromatin (occurs at termination sites) PMID:29899453 fig 6a.b PMID:29899453 Extended Data Fig 10 PMID:29899453 Extended Data Fig 10 PMID:29899453 Extended Data Fig 10 PMID:29899453 Fig 5c. PMID:29899453 fig 1d PMID:29914874 Supplementary Fig. S3 PMID:29914874 Supplementary Fig. S3 PMID:29914874 Supplementary Fig. S3 PMID:29914874 Supplementary Fig. S3 PMID:29914874 Supplementary Table S3 PMID:29914874 Supplementary Fig. S3 PMID:29914874 Supplementary Fig. S3 PMID:29914874 Supplementary Figure S3 PMID:29930085 Figure 5, Figure S4, Movie 5 PMID:29930085 fig 7c PMID:29930085 figure 7d PMID:29930085 figure 7D PMID:29930085 Portli Figure 7, Movie 9 https://github.com/pombase/fypo/issues/3339 PMID:29930085 PORTLI Growth Figure 6, Figure S6, Movie 7 https://github.com/pombase/fypo/issues/3339 PMID:29930085 (PORTLI GROWTH) fig 6 c https://github.com/pombase/fypo/issues/3339 PMID:29930085 PORTLI GROWTH Fig S6 https://github.com/pombase/fypo/issues/3339 PMID:29930085 PORTLI GROWTH Fig S6 https://github.com/pombase/fypo/issues/3339 PMID:29930085 Fig. 5B PMID:29930085 Fig. 5B PMID:29930085 Figure 4, Movie 4 PMID:29930085 Figure S3 PMID:29930085 Figure 4,AB PMID:29930085 PORTLI GROWTH (Figs 3B and 4B; Movie 2) https://github.com/pombase/fypo/issues/3339 PMID:29930085 PORTLI GROWTH (Figs 3B and 4B; Movie 2) https://github.com/pombase/fypo/issues/3339 PMID:29930085 fig 3 PMID:29930085 fig 3 PMID:29930085 (PORTLI GROWTH) fig 2 interphase arrest https://github.com/pombase/fypo/issues/3339 PMID:29930085 fig 2 interphase arrest PMID:29930085 fig 1 interphase arrest PMID:29930085 fig 1 interphase arrest PMID:29930085 fig 1 interphase arrest (requested during interphase) PMID:29930085 fig 1 interphase arrest (requested during interphase) PMID:29930085 fig 1 interphase arrest (requested during interphase) PMID:29930085 fig 1 interphase arrest (requested during interphase) PMID:29930085 fig 1 interphase arrest PMID:29930085 fig2 movie1 PMID:29930085 S1 PMID:29930085 Figure 7, Figure S8 PMID:29930085 Figure 7, Figure S8 PMID:29930085 Figure S6, Movie 8 PMID:29930085 Figure S6, Movie 8 PMID:29930085 Figure S3 PMID:29930085 Figure S3 PMID:29930085 Figure 7, Movie 9 PMID:29930085 Figure 6, Figure S6, Movie 7 PMID:29930085 Figure 4, Movie 4 PMID:29930085 Figure 4, Figure S3, Movie 4 PMID:29930085 Figure 4, Movie 4 PMID:29930085 Figure 3, Movie 2 PMID:29930085 Figure 3, Figure 4, Figure S2, Movie 2, Movie 3, Movie 4 PMID:29930085 Figure 2 PMID:29930085 Figure 1 PMID:29930085 Figure 1 PMID:29930085 Figure 1 PMID:29930085 Figure 1 PMID:29930085 Figure 1 PMID:29930085 Figure 1 PMID:29930085 Figure 1 PMID:29930085 Figure 1 PMID:29930085 Figure 5, Figure S4, Movie 5 PMID:29975113 Figure 1B and S1B PMID:29975113 (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 Figure 2B and C PMID:29975113 Figure S2B PMID:29975113 (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 [ 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:29975113 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 Figure 2D in vivo PMID:29975113 Figure S2A PMID:29975113 Figure S2D PMID:29975113 temporal localization pattern Figure S2B PMID:29975113 Figure 2D PMID:29975113 These data are consistent with auto-ubiquitination triggering Dma1 destruction. PMID:29975113 Figure 2G PMID:29975113 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 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:29975157 Fig. 1B; DAPI and methyl blue staining PMID:29975157 Fig. 2D; live cell imaging PMID:29975157 Fig. 3; live cell imaging PMID:29975157 Fig. 4A; live cell imaging PMID:29975157 Fig. 4B; live cell imaging PMID:29975157 Fig. 4C; live cell imaging PMID:29975157 Fig. 4D; live cell imaging PMID:29975157 Fig. 5B; Live cell imaging of PIP3 sensor PMID:29975157 Fig. 5B; Live cell imaging of PIP3 sensor PMID:29975157 Fig. 5B; Live cell imaging of PIP3 sensor PMID:29975157 Fig. 5B; Live cell imaging of PIP3 sensor PMID:29975157 Fig. 5B; Live cell imaging of PIP3 sensor PMID:29975157 Fig. 5C; Live cell imaging of PIP2 lipid sensor PMID:29975157 Fig. 1B; DAPI and methyl blue staining PMID:29975157 Fig. 1B; DAPI and methyl blue staining PMID:29975157 Fig. 1B; DAPI and methyl blue staining PMID:29975157 Fig. 1B; DAPI and methyl blue staining PMID:29975157 Fig. 1B; DAPI and methyl blue staining PMID:29975157 Fig. 2A-C; live cell imaging PMID:29975157 Fig. 5C; Live cell imaging of PIP2 lipid sensor PMID:29975157 Fig. 5C; Live cell imaging of PIP2 lipid sensor PMID:29975157 Fig. 5C; Live cell imaging of PIP2 lipid sensor PMID:29975157 Fig. 5A; Live cell imaging of PIP4 lipid sensor PMID:29975157 Fig. 5A; Live cell imaging of PIP4 lipid sensor PMID:29975157 Fig. 5A; Live cell imaging of PIP4 lipid sensor PMID:29975157 Fig. 5A; Live cell imaging of PIP4 lipid sensor PMID:29975157 Fig. S2C,D PMID:29975157 Fig. 5A; Live cell imaging of PIP4 lipid sensor PMID:29975157 Fig. S1F; DAPI and methyl blue staining PMID:29975157 Fig. 1B; DAPI and methyl blue staining PMID:29975157 Fig. S1F; DAPI and methyl blue staining PMID:29975157 Fig. S2A-D PMID:29975157 Fig. 1B PMID:29975157 Fig. S2E PMID:29975157 Fig. 1B; DAPI and methyl blue staining PMID:29975157 Fig. S1F; DAPI and methyl blue staining PMID:29975157 Fig. S1F; DAPI and methyl blue staining PMID:29975157 Fig. 1B; DAPI and methyl blue staining PMID:29975157 Fig. 2A-C; live cell imaging PMID:29975157 Fig. 1B; DAPI and methyl blue staining PMID:29975157 Fig. 1B; DAPI and methyl blue staining PMID:29975157 Fig. 1B; DAPI and methyl blue staining PMID:29975157 Fig. 1B; DAPI and methyl blue staining PMID:29975157 Fig. 1B; DAPI and methyl blue staining PMID:29975157 Fig. 1B; DAPI and methyl blue staining PMID:29975157 Fig. S2A PMID:30003614 increased number of lipid droples/cell fig 3b/c PMID:30003614 fig 4 PMID:30003614 fig 4 PMID:30003614 fig 4 PMID:30003614 fig 4 normal level of free fatty acid PMID:30003614 fig 5 = cerulenin PMID:30044717 fig S2 PMID:30044717 Fig 5 PMID:30044717 fig 5B PMID:30044717 fig 5B PMID:30044717 Figure 7 PMID:30044717 Fig 7E PMID:30044717 Fig 7E PMID:30044717 Figure 6E PMID:30044717 Fig. S6B PMID:30044717 Fig5D and Movie 5 PMID:30044717 fig 5b PMID:30044717 fig 5B PMID:30044717 Fig S2,E PMID:30044717 Fig2a (vw: average survival ~ 7 cell cycles) PMID:30044717 Fig 2B PMID:30044717 Figure 1 PMID:30044717 fig1 PMID:30044717 fig S4E PMID:30044717 fig S4E PMID:30044717 fig 2b PMID:30044717 fig 2a PMID:30044717 Fig S3 DE PMID:30044717 Fig S3 DE PMID:30044717 Fig S2,E PMID:30044717 Fig S4C PMID:30044717 Fig S4C PMID:30044717 Fig S4C PMID:30044717 Fig S4C PMID:30044717 Fig 5C PMID:30044717 fig 6A PMID:30044717 Fig 5C PMID:30044717 fig 4 PMID:30044717 Figure 1 PMID:30044717 Supp S1F PMID:30044717 Supp S1G PMID:30044717 fig S2 PMID:30044717 Fig S2C,E PMID:30053106 requires long flap (binding affinity much higher with 27-nt than 15-nt flap) PMID:30072377 Fig. 4C. Resistant to 1mM spermidine at 37C. PMID:30072377 Fig. 4C Resistant to 1 mM spermidine at 37C. PMID:30072377 Fig. 3B, Fig. 4A,B PMID:30072377 Fig. 3C, D; Fig. 4A,B PMID:30072377 Fig. 4A,B PMID:30072439 Revealed by thin layer chromatography PMID:30072439 Lack of lipid droplet formation PMID:30072439 Lack of lipid droplet formation PMID:30072439 Synthetic growth defect between cwh43-G753R mutant and dga1Δ plh1Δ double deletion mutant. PMID:30072439 Suppression of temperature sensitivity by 1.2M sorbitol PMID:30072439 Suppression of temperature sensitivity by 1.2M sorbitol PMID:30072439 Partial suppression of growth defect in the presence of sorbitol PMID:30072439 Synthetic growth defect between cwh43-G753R mutant and dga1Δ plh1Δ double deletion mutant. PMID:30072439 decreased cellular diphosphoglycerate level PMID:30072439 increased cellular dimethyl-histidine level during vegetative growth PMID:30072439 Suppression of temperature sensitivity by 1.2M sorbitol PMID:30072439 Partial suppression of growth defect in the presence of sorbitol PMID:30072439 Suppression of temperature sensitivity by 1.2M sorbitol PMID:30072439 Sorbitol addition partly suppresses beta-glucan accumulation in cwh43-G753R mutant cells PMID:30072439 Normal glucose consumption, but cell division is sensitive to low glucose condition PMID:30072439 However, in scs2Δ scs22Δ double deletion mutant cells, localization of both Cwh43–GFP and AHDL– mCherry at the plasma membrane disappeared, and, instead, accumulated in the cytoplasm PMID:30072439 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 Revealed by lipidomic analysis using mass spectrometry, thin layer chromatography, and lipid droplet staining PMID:30076928 transcription read through by PCR PMID:30076928 transcription read through by PCR PMID:30076928 RT-PCR PMID:30076928 RT-PCR PMID:30076928 mini-chromosome loss assay PMID:30089114 Heterochromatin structure protects native CENP-A from ubiquitin-mediated degradation. PMID:30089114 polyubiquitylated PMID:30089908 *******to nucleus of opposite mating type cell****** PMID:30089908 Fig. 3d, Supplementary Video 5b PMID:30089908 Fig. 4a, Extended Data Fig. 4c, Supplementary Video 7b PMID:30089908 go-ontology/issues/16327 PMID:30089908 ******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 Fig. 1a, type IIIb PMID:30089908 Fig. 1g PMID:30089908 Extended data figure 1 F dominant over shk2 downstream sporulation phenotypes PMID:30089908 Figure 1c PMID:30089908 abolished karyogamy with transient cytogamy (this is a bit like twin haploid meiosis? should be siblings? also looks like karyogamy failure) PMID:30089908 abolished karyogamy with transient cytogamy (this is a bit like twin haploid meiosis? should be siblings? also looks like karyogamy failure) PMID:30089908 Fig. 4a, Extended Data Fig. 4c, Supplementary Video 7b PMID:30089908 Fig. 4a, Extended Data Fig. 4c, Supplementary Video 7b PMID:30089908 Fig. 2c never ending search for mating partner PMID:30089908 never ending search for mating partner by P cell PMID:30089908 in M-cell PMID:30089908 Extended Data Fig. 5e, f, Supplementary Video 9; see also ref. 1 PMID:30089908 Extended Data Fig. 5e, f, Supplementary Video 9; see also ref. 1 PMID:30089908 Regulation of asymmetric gene expression from parental genomes PMID:30089908 Regulation of asymmetric gene expression from parental genomes PMID:30089908 Regulation of asymmetric gene expression from parental genomes Factor that regulates differential gene expression of homologous parental gene copies PMID:30089908 (Fig. 1a, type IIIa PMID:30089908 Fig. 1a, type IIIb PMID:30089908 GO:0140538 +name: negative regulation of conjugation with zygote https://github.com/geneontology/go-ontology/issues/16329 PMID:30089908 GO:0140538 +name: negative regulation of conjugation with zygote https://github.com/geneontology/go-ontology/issues/16329 PMID:30089908 Extended Data Fig. 3b, Supplementary Video 5a PMID:30089908 P-cells (rapid) M-cells (delayed) PMID:30089908 M-cells PMID:30089908 Regulation of asymmetric gene expression from parental genomes Factor that regulates differential gene expression of homologous parental gene copies PMID:30089908 fig 1 II PMID:30089908 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:30102332 also inferred from orthology, interactions, and chromatin localization (ChIP) PMID:30102332 also inferred from orthology, interactions, and chromatin localization (ChIP) PMID:30102332 Figures 4 & 5. PMID:30102332 also inferred from orthology, interactions, and chromatin localization (ChIP) PMID:30102332 Figures 4 & 5. PMID:30102332 Figure 5. PMID:30102332 Figures 4 & 5. PMID:30102332 Figure 5. PMID:30102332 Figure 5. PMID:30104346 evidence is combination of ChIP in this paper plus data in other publications showing that Rad52 binds DNA directly PMID:30104346 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 evidence is combination of ChIP in this paper plus data in other publications showing that Ctp1 binds DNA directly PMID:30110338 H3 K9me3 https://github.com/geneontology/go-ontology/issues/16331 PMID:30110338 H3 K9me3 https://github.com/geneontology/go-ontology/issues/16331 PMID:30110338 H3 K9me3 PMID:30110338 H3 K9me3 https://github.com/geneontology/go-ontology/issues/16331 PMID:30116786 fig 3B PMID:30116786 Fig 3 PMID:30116786 Fig 4E PMID:30116786 Fig 4E PMID:30116786 Fig 4C PMID:30116786 Fig 4E PMID:30116786 Fig 3 PMID:30116786 Fig 4E PMID:30116786 Fig 4E PMID:30116786 Fig 4E PMID:30116786 Fig 4E PMID:30116786 Fig 4E PMID:30116786 Fig 4E PMID:30116786 Fig 4E PMID:30116786 Fig 4E PMID:30116786 Fig 4E PMID:30116786 Fig 4E *******during quiesence PMID:30116786 Fig 4E PMID:30116786 Fig 4E PMID:30116786 Fig. 3F loss of mitotic competence PMID:30116786 Fig S3 PMID:30116786 Fig 4A,E PMID:30116786 fig 3B PMID:30116786 fig 3C *********during G0 PMID:30116786 Fig. 3F loss of mitotic competence PMID:30116786 Fig 3 PMID:30116786 Fig 3 PMID:30134042 assayed at cdc18 and cdc22 PMID:30134042 assayed at cdc18 and cdc22 PMID:30134042 assayed at cdc18 and cdc22 PMID:30134042 assayed at cdc18 and cdc22 PMID:30134042 assayed at cdc18 and cdc22 PMID:30134042 assayed at cdc18 and cdc22 PMID:30134042 assayed at cdc18 and cdc22 PMID:30134042 assayed at cdc18 and cdc22 PMID:30134042 assayed at cdc18 and cdc22 PMID:30134042 assayed at cdc18 and cdc22 PMID:30134042 assayed at cdc18 and cdc22 PMID:30134042 assayed at cdc18 and cdc22 PMID:30201262 Temperature was shifted at prophase or metaphase. PMID:30201262 Temperature was shifted at anaphase B. PMID:30201262 SFig5 PMID:30201262 fig6 PMID:30201262 fig6 PMID:30201262 fig6 PMID:30201262 fig 1. PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30212894 correlation with gel shift assays PMID:30217891 S14 PMID:30217891 fig3 PMID:30217891 fig3 PMID:30279276 Cdc42-GTP assayed with CRIB; broad zones of activity PMID:30280012 Fig 6 PMID:30280012 Fig 6 PMID:30280012 Figure S5A, S5B, PMID:30280012 Fig 6 PMID:30280012 Fig 6 PMID:30280012 Fig 6 PMID:30280012 Fig S5C, S6 PMID:30280012 Fig 6 PMID:30282034 at transcription_termination_signal PMID:30282034 at transcription_termination_signal PMID:30282034 at transcription_termination_signal PMID:30282034 at transcription_termination_signal PMID:30332655 inferred from phenotypes and from direct assay using human calcineurin PMID:30348841 deletion of Nse6 strongly reduced Nse4 residence at binding sites tested under normal and genotoxic stress PMID:30348841 deletion of Brc1 significantly reduced Nse4 residence at binding sites tested under normal and genotoxic stress PMID:30348841 Nse4 sumoylation undetectable in nse6Δ PMID:30348841 Nse4 sumoylation reduced in brc1Δ PMID:30348841 physical interaction between brc1-T672A and Nse6 PMID:30348841 fig 1 a: brc1 mutant abolishes Nse4 nuclear foci in HU/MMS treated cells PMID:30348841 fig 1 brc1 mutant cells expressing brc1-T672A are deficient in Nse4 foci formation PMID:30348841 Nse4 foci gone in nse6 mutant cells; Nts1 overexpression background to mitigate nse6Δ genotoxin sensitivity PMID:30348841 Nse4 sumoylation at wild type level PMID:30348841 mutations in brc1 weaken interaction with nse6 PMID:30348841 nse2-SA brc1 cells are more sensitive to genotoxins than either single mutant (Fig. 4C). PMID:30348841 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 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 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 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 deletion of Nse5 strongly reduced Nse4 residence at binding sites tested under normal and genotoxic stress PMID:30348841 Nse4 foci gone in nse6 mutant cells; Nts1 overexpression background to mitigate nse6Δ genotoxin sensitivity PMID:30348841 physical interaction between brc1-T672A and Smc5 PMID:30355493 2d PMID:30355493 S3C PMID:30355493 2d PMID:30355493 2d PMID:30355493 fig4 PMID:30355493 3c PMID:30355493 2d PMID:30355493 2d PMID:30355493 2d PMID:30355493 2d PMID:30355493 2d PMID:30355493 2d PMID:30355770 Fig. 2A PMID:30355770 Fig. 7D PMID:30355770 Fig. 7D PMID:30355770 Fig. 7D PMID:30355770 Fig. 7D PMID:30355770 Fig. 7D PMID:30355770 Fig. 7D PMID:30355770 Fig. S8 PMID:30355770 Fig. S8 PMID:30355770 Fig. S8 PMID:30355770 Fig. 4B PMID:30355770 Fig. 4B PMID:30355770 Fig. 4B PMID:30355770 Fig. 4B PMID:30355770 Fig. S5 PMID:30355770 Fig. S5 PMID:30355770 Fig. S5 PMID:30355770 Fig. S6 PMID:30355770 Fig. S6 PMID:30355770 Fig. S6 PMID:30355770 Fig. 2A PMID:30355770 Fig. 2A PMID:30355770 Fig. 2A PMID:30355770 Fig. 2A PMID:30355770 Fig. 2A PMID:30355770 Fig. 2A PMID:30355770 Fig. 2A PMID:30355770 Fig. 2A PMID:30355770 Fig. 2A PMID:30355770 Fig. 2A PMID:30355770 Fig. 2A PMID:30355770 Fig. 2B PMID:30355770 Fig. 2B PMID:30355770 Fig. 2B PMID:30355770 Fig. 2B PMID:30355770 Fig. 2B PMID:30355770 Fig. 2A PMID:30355770 Fig. 2A PMID:30355770 Fig. 2A PMID:30355770 Fig. 2A PMID:30355770 Fig. 2A PMID:30355770 Fig. 2A PMID:30355770 Fig. 2A PMID:30389790 fig 3b PMID:30389790 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 fig 6 PMID:30389790 fig 5b PMID:30389790 fig 5b PMID:30389790 fig 2b PMID:30389790 fig 2b PMID:30389790 figure 5 and 11 (no loss of viability ) PMID:30389790 figure 5c hypoglycosylation PMID:30389790 figure 5c PMID:30389790 figure 5c PMID:30389790 figure 5b and S2 PMID:30389790 fig 10 PMID:30389790 fig 10 PMID:30389790 fig 10 PMID:30389790 fig S4 PMID:30389790 fig S4 PMID:30389790 fig 6 PMID:30389790 fig 5b PMID:30389790 fig 5b PMID:30393157 Fig. 2C/D PMID:30393157 fig 4 PMID:30393157 table2 PMID:30393157 table2 PMID:30393157 table2 PMID:30393157 table2 PMID:30393157 table2 PMID:30393157 table2 PMID:30393157 table2 PMID:30393157 table2 PMID:30393157 table2 PMID:30393157 table2 PMID:30393157 table2 PMID:30393157 table2 PMID:30393157 table2 PMID:30393157 table2 PMID:30393157 table2 PMID:30393157 table2 PMID:30393157 table2 PMID:30393157 table2 PMID:30393157 fig 4 PMID:30393157 fig 2E/F PMID:30393157 fig 2E/F PMID:30393157 fig 2E/F PMID:30393157 fig 2E/F PMID:30393157 figure 3D PMID:30393157 Fig. 2C/D PMID:30393157 figure 3D PMID:30393157 fig 4 PMID:30393157 Fig. 5A PMID:30393157 Fig. 5A PMID:30393157 Fig. 5A PMID:30393157 Fig. 5A PMID:30393157 Fig. 5A PMID:30393157 Fig. 5A PMID:30393157 Fig. 5A PMID:30393157 fig 1A PMID:30393157 fig 1C/D PMID:30393157 Fig. 2B PMID:30393157 Fig. 2B PMID:30393157 Fig. 2B PMID:30393157 Fig. 2B PMID:30393157 Fig. 2C/D PMID:30393157 Fig. 2C/D PMID:30393157 Fig. 2C/D PMID:3040264 2b PMID:3040264 fig 2 a PMID:3040264 table1 PMID:3040264 table1 PMID:3040264 fig 2 a no spindle rod like chromsomes PMID:3040264 fig 2 a no spindle rod like chromsomes PMID:3040264 fig 2 b (uncondensed chromosomes) PMID:3040264 fig 2 B PMID:3040264 fig 2 b (uncondensed chromosomes) PMID:3040264 fig 2 a no spindle rod like chromsomes PMID:3040264 table1 PMID:30427751 figure 1 PMID:30427751 figure 2 A with increased loc to spb PMID:30427751 figure 2 B PMID:30427751 figure 2 A with increased loc to spb PMID:30427751 figure 1 G/H (from preexisting microtubules) PMID:30427751 figure6AC PMID:30427751 figure6AC PMID:30427751 figure6D PMID:30427751 figure 5I PMID:30427751 Therefore, we concluded that Rsp1 is required to prevent excessive accumulation of Mto1 PMID:30427751 figure 5GH PMID:30427751 fig 5A (recruitment) PMID:30427751 figure 5A PMID:30427751 figure 5A PMID:30427751 Therefore, we concluded that Rsp1 is required to prevent excessive accumulation of Mto1 PMID:30427751 figure 2 B PMID:30427751 figure 2 B PMID:30451685 Figures 2C, 2D, and Figure 2—figure supplement 2 PMID:30451685 Figures 2C, 2D, and Figure 2—figure supplement 2 PMID:30451685 Figures 2A and 2B; assayed_using cpy1 PMID:30451685 Figure 1 (direct assay for vacuolar membrane) and Figure 1-figure supplement 1 (sequence feature evidence for transmembrane) PMID:30451685 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 Figure 2 PMID:30451685 Figure 2 and Figure 2-figure supplement 1 PMID:30451685 Figure 3—figure supplement 1A, 2B PMID:30451685 Figure 3—figure supplement 1A, 2B PMID:30451685 Figure 3—figure supplement 1B, 2B; assayed_using cpy1 PMID:30451685 Figure 3—figure supplement 1B, 2B; assayed_using cpy1 PMID:30451685 Figure 3—figure supplement 1B, 2B; assayed_using cpy1 PMID:30451685 Figure 3—figure supplement 1B, 2B; assayed_using cpy1 PMID:30451685 Figure 3—figure supplement 1A, 2B PMID:30451685 Figure 3—figure supplement 1B PMID:30451685 Figure 4C,D PMID:30451685 Figure 4C,D PMID:30451685 Figure 4C,D PMID:30451685 Figure 4C,D PMID:30451685 Figure 4C,D PMID:30451685 Figure 3—figure supplement 1A, 2B PMID:30451685 Figure 3—figure supplement 1A, 2B PMID:30451685 Figure 3—figure supplement 1B, 2B; assayed__using cpy1 PMID:30451685 Figure 4A; isothermal titration calorimetry (ITC) PMID:30451685 Figure 4—figure supplement 1C; isothermal titration calorimetry (ITC) PMID:30451685 Figure 4A; isothermal titration calorimetry (ITC) PMID:30451685 Figure 3—figure supplement 2 PMID:30451685 Figure 3—figure supplement 2 PMID:30451685 Figure 3—figure supplement 2 PMID:30451685 Figure 3—figure supplement 1A PMID:30451685 Figure 3—figure supplement 1A, 2B PMID:30451685 Figure 3—figure supplement 1A, 2B PMID:30451685 Figure 3—figure supplement 1A, 2B PMID:30451685 Figure 4—figure supplement 1B; isothermal titration calorimetry (ITC) PMID:30451685 Figure 3—figure supplement 1A, 2B PMID:30451685 Figure 3—figure supplement 1A, 2B PMID:30451685 Figure 3—figure supplement 2 PMID:30451685 Figure 3—figure supplement 2 PMID:30451685 Figure 3—figure supplement 1A, 2B PMID:30451685 Figures 2C, 2D, and Figure 2—figure supplement 2; same as either single mutant PMID:30451685 Figures 2C, 2D, and Figure 2—figure supplement 2; same as either single mutant PMID:30451685 Figures 2C, 2D, and Figure 2—figure supplement 2; same as either single mutant PMID:30451685 Figure 2—figure supplement 1A PMID:30451685 Figure 3—figure supplement 1 PMID:30451685 Figure 2D and Figure 2—figure supplement 2 PMID:30451685 Figure 2—figure supplement 2 PMID:30451685 Figure 2D and Figure 2—figure supplement 2 PMID:30451685 Figure 2—figure supplement 2 PMID:30451685 Figure 2D and Figure 2—figure supplement 2 PMID:30451685 Figure 2D and Figure 2—figure supplement 2 PMID:30451685 Figure 4C,D PMID:30451685 Figure 4C,D PMID:30451685 Figure 4B PMID:30451685 Figure 4B PMID:30451685 Figure 4B PMID:30451685 Figure 4B PMID:30451685 Figure 4B PMID:30451685 Figure 4B PMID:30451685 Figure 4B PMID:30451685 Figure 4—figure supplement 1B; isothermal titration calorimetry (ITC) PMID:30451685 Figure 4—figure supplement 1B; isothermal titration calorimetry (ITC) PMID:30451685 Figure 4A; isothermal titration calorimetry (ITC) PMID:30451685 Figure 4—figure supplement 1B; isothermal titration calorimetry (ITC) PMID:30451685 Figure 4—figure supplement 1B; isothermal titration calorimetry (ITC) PMID:30451685 Figure 2D and Figure 2—figure supplement 2 PMID:30451685 Figure 4E PMID:30451685 Figure 4E PMID:30451685 Figures 4C and 4D; assayed_using cpy1 PMID:30451685 Figure 2—figure supplement 2 PMID:30451685 Figure 2D and Figure 2—figure supplement 2 PMID:30451685 Figure 2—figure supplement 1D PMID:30451685 Figures 2C, 2D, and Figure 2—figure supplement 2 PMID:30451685 Figures 2C, 2D, and Figure 2—figure supplement 2 PMID:30451685 Figures 2C, 2D, and Figure 2—figure supplement 2 PMID:30451685 Figures 2A and 2B; assayed_using cpy1 PMID:30451685 Figures 2C, 2D, and Figure 2—figure supplement 2 PMID:30462301 Supplementary Figure S1A-E PMID:30462301 suggested by Junko PMID:30462301 Figure 6B and Supplementary Figure S8C PMID:30462301 Figure 6B and Supple- mentary Figure S8B PMID:30462301 Figure 6B and Supple- mentary Figure S8B PMID:30462301 Figure 6B and Supplementary Figure S8C) PMID:30462301 Figure 6B and Supplementary Fig- ure S8B PMID:30462301 Figure 6B and Supplementary Fig- ure S8B PMID:30462301 Figure 6B and Supplementary Fig- ure S8B PMID:30462301 competatively with lem2 PMID:30462301 Figure 4F and Supplementary Figure S7F PMID:30462301 Supplementary Figure S7E PMID:30462301 Supplementary Figure S7E PMID:30462301 Figure 4A PMID:30462301 Supplementary Figure S7E PMID:30462301 Figure 4A PMID:30462301 Figure 4A PMID:30462301 Figure 4A PMID:30462301 competatively with sad1 PMID:30462301 Supplementary Figure S7A-D) PMID:30462301 Figure 3 PMID:30462301 Figure 3 PMID:30462301 Figure 3 PMID:30462301 Figure 3 PMID:30462301 Figure 3B and Supplementary Figure S6 PMID:30462301 Figure 3B and Supplementary Figure S6 PMID:30462301 Figure 3B and Supplementary Figure S6 PMID:30462301 Figure 3B and Supplementary Figure S6 PMID:30462301 Figure 3A PMID:30462301 Figure 3A PMID:30462301 Figure 3A PMID:30462301 Figure 3A PMID:30462301 Supple- mentary Figure S5B PMID:30462301 Supple- mentary Figure S5B PMID:30462301 Supple- mentary Figure S5B PMID:30462301 Supple- mentary Figure S5B PMID:30462301 Supple- mentary Figure S5B PMID:30462301 Supple- mentary Figure S4A) PMID:30462301 Figure 2E and Supple- mentary Figure S4B PMID:30462301 Supple- mentary Figure S4A) PMID:30462301 Supple- mentary Figure S4A) PMID:30462301 Supple- mentary Figure S4A) PMID:30462301 Figure 2C, D, Supple- mentary Figure S3A and C PMID:30462301 Figure 2C, D, Supple- mentary Figure S3A and C PMID:30462301 (Fig- ure 2D, Supplementary Figure S3B and C PMID:30462301 (Fig- ure 2D, Supplementary Figure S3B and C PMID:30462301 Figure 2C, Supplementary Figure S3A and C PMID:30462301 Figure 2C, Supplementary Figure S3A and C PMID:30462301 Figure 2C, Supplementary Figure S3A and C PMID:30463883 figure 2 AB PMID:30463883 figure 2 AB PMID:30463883 The mitotic spindle has two poles but is thicker than normal. PMID:30463883 The mitotic spindle has two poles but is thicker than normal. PMID:30463883 figure 2 AB PMID:30463883 at 36 degrees Celsius PMID:30463883 at 36 degrees Celsius PMID:30463883 at 36 degrees Celsius PMID:30463883 at 36 degrees Celsius PMID:30463883 at 36 degrees Celsius PMID:30463883 at 33 degrees Celsius PMID:30463883 at 36 degrees Celsius PMID:30463883 at 33 degrees Celsius PMID:30463883 at 33 degrees Celsius PMID:30463883 at 33 degrees Celsius PMID:30463883 figure 2 AB PMID:30463883 figure 2 AB PMID:30471998 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 when wtf13 antidote not present (homozygous, wtf13poison/wtf13+, or wtf13poison/wtf13Δ PMID:30475921 wtf13 driver, wtf18 suppressor PMID:30475921 wtf13 driver, wtf18 suppressor PMID:30475921 wtf13 driver, wtf18 suppressor PMID:30475921 wtf13 driver, wtf18 suppressor PMID:30475921 wtf18-2 allele assayed PMID:30475921 suppresses wtf13 drive PMID:30503780 fig S5B (southern blot) PMID:30503780 Figures 5A and 5B PMID:30503780 fig 2 D PMID:30503780 figure3 (incompatible with rap1 binding) PMID:30503780 fig S5B PMID:30503780 fig S5B PMID:30503780 incompatible with DNA binding PMID:30503780 fig4 PMID:30503780 fig4 PMID:30503780 figure 2D PMID:30503780 figure 2D PMID:30503780 figure 2D PMID:30503780 (transeferred from Junk's session PMID:30462301) PMID:30503780 (transeferred from Junk's session PMID:30462301) PMID:30503780 (transeferred from Junk's session PMID:30462301) PMID:30503780 (transeferred from Junk's session PMID:30462301) PMID:30503780 Figures 5C PMID:30503780 Figures 5C PMID:30503780 Figures 5A and 5B PMID:30503780 Figures 5A and 5B PMID:30503780 fig S5B PMID:30503780 fig S5B PMID:30503780 fig S5B PMID:30528393 although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA PMID:30528393 although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA PMID:30528393 although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA PMID:30528393 although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA PMID:30530492 glucosylceramide, galactosylceramide PMID:30530492 glycosphingolipid transport PMID:30573453 (Figure 2c) PMID:30573453 (Figure S7) PMID:30573453 (Figure S7) PMID:30573453 FIgure S7 PMID:30573453 fig6 PMID:30573453 fig6 PMID:30573453 (figure S8) PMID:30573453 (Figure S8) PMID:30573453 FIgure S8 PMID:30573453 FIgure S8 PMID:30573453 fig6 PMID:30573453 fig6 PMID:30573453 fig6 PMID:30573453 fig6 PMID:30573453 fig6 PMID:30573453 fig6 PMID:30573453 fig6 PMID:30573453 fig6 PMID:30573453 fig5 PMID:30573453 fig5 PMID:30573453 fig5 PMID:30573453 fig5 PMID:30573453 fig5 PMID:30573453 (Figure 4c) PMID:30573453 (Figure 4d) PMID:30573453 FIgure 4C PMID:30573453 (Figure 2c) PMID:30573453 FIgure S4 PMID:30573453 (Figure 3a) PMID:30573453 (Figure 3a) PMID:30573453 (Figure 3a) PMID:30573453 (Figure 2c) PMID:30573453 2d PMID:30573453 2d PMID:30573453 (Figure 2c) PMID:30573453 fig5 PMID:30601114 Figure 1–figure supplement 1A PMID:30601114 Figure 2A and Figure 2–figure supplement 1B-E PMID:30601114 Figure 2A and Figure 2–figure supplement 1B-E PMID:30601114 ADD DOMAIN WHEN SO TERM AVAILABLE Figure 2A and Figure 2–figure supplement 1B-E PMID:30601114 figure 2 B PMID:30601114 figure 2 B PMID:30601114 figure 2 PMID:30601114 figure 2 B PMID:30601114 figure 2 B PMID:30601114 figure 2 B PMID:30601114 Figure 1–figure supplement 1A PMID:30601114 Non-adenosine residues upstream of the poly(A) tail were also rapidly removed by Ccr4-Not when Puf3 or Zfs1 were present PMID:30601114 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 Figure 1A and Figure 1–figure supplement 1D- E) PMID:30601114 Figure 1A and Figure 1–figure supplement 1D- E) PMID:30601114 PRE element Figure 1–figure supplement 1B/Figure 1–figure supplement 1C PMID:30601114 Figure 1–figure supplement 1B/Figure 1–figure supplement 1C PMID:30601114 Non-adenosine residues upstream of the poly(A) tail were also rapidly removed by Ccr4-Not when Puf3 or Zfs1 were present PMID:30601114 figure 2 B PMID:30601114 figure 2 B PMID:30601114 figure 2 B PMID:30601114 figure 2 B PMID:30601114 figure 2 B PMID:30601114 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:30602572 Fig 1C observed that Klp5/Klp6 contained only 2.3 0.4 (mean S.E.). PMID:30602572 Klp5/Klp6 cells exhibited a fission frequency that was half that of WT PMID:30602572 (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 WT cells highly overex- pressing Dnm1 had 11.6 0.2 mitochondria (mean S.E.), which is twice that of WT cells PMID:30602572 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 Figure 2C the mitochondria have a fission frequency that is almost double that of wild-type PMID:30602572 Figure 1B the anti-parallel microtubule bundles are only about half the length of wild-type bundles PMID:30602572 Figure 6B PMID:30602572 Figure 1C-D PMID:30602572 Figure 6C-D Increased mitochondrial numbers and decreased mitochondrial sizes with overall mitochondrial volume same as what is observed in wild-type cells PMID:30626735 Andres SN et al. (2019) PMID:30626735 75 J/m^2; Andres SN et al. (2019) PMID:30626735 200 Gy; Andres SN et al. (2019) PMID:30635402 Identified by mass spectrometry PMID:30635402 Identified by mass spectrometry PMID:30635402 also assayed directly using human CKII PMID:30635402 Identified by mass spectrometry PMID:30635402 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 Identified by mass spectrometry PMID:30635402 These phosphorylation sites were identified by the phos-tag analysis, phospho-specific antibodies, and in vitro phosphorylation assay PMID:30635402 ICRF-193, a bisdioxopiperazine derivative [meso-4,4-(2,3-butanediyl)-bis (2,6-piperazinedione)], is a catalytic topo II inhibitor PMID:30635402 Identified by mass spectrometry PMID:30635402 Identified by mass spectrometry PMID:30640914 mbs1 hotspot quantification PMID:30640914 s1 PMID:30640914 S2 PMID:30640914 fig s4 PMID:30640914 fig8 PMID:30640914 S4 PMID:30640914 fig8 PMID:30640914 mbs1 hotspot quantification PMID:30640914 S2 PMID:30640914 S2 PMID:30640914 S2 PMID:30640914 S1A PMID:30640914 S1A PMID:30640914 S1A PMID:30640914 S1A PMID:30640914 Recombination assay; assayed region: ade6 gene PMID:30640914 Recombination assay; assayed region: ade6 gene PMID:30640914 Recombination assay; assayed region: ade6 gene PMID:30640914 Recombination assay; assayed region: ade6 gene PMID:30640914 Recombination assay; assayed region: ade6 gene PMID:30640914 Recombination assay; assayed region: ade6 gene PMID:30640914 Recombination assay; assayed region: ade6 gene PMID:30640914 Recombination assay; assayed region: ade6 gene PMID:30640914 Recombination assay; assayed region: ade6 gene PMID:30640914 Recombination assay; assayed region: ade6 gene PMID:30640914 Recombination assay; assayed region: ade6 gene PMID:30640914 Recombination assay; assayed region: ade6 gene PMID:30640914 Cellular fractionation; affecting Rec25 PMID:30640914 Rec25 visualization PMID:30640914 mbs1 hotspot quantification PMID:30640914 Recombination assay; assayed region: leu1-his5 interval PMID:30640914 Recombination assay; assayed region: ade6 gene PMID:30640914 mbs1 hotspot quantification PMID:30640914 Cellular fractionation; affecting Rec25 PMID:30640914 Cellular fractionation; affecting Rec25 PMID:30640914 Rec25 visualization PMID:30640914 Rec25 visualization PMID:30640914 mbs1 hotspot quantification PMID:30640914 Recombination assay; assayed region: leu1-his5 interval PMID:30640914 Recombination assay; assayed region: ade6 gene PMID:30640914 mbs1 hotspot quantification PMID:30640914 Recombination assay; assayed region: leu1-his5 interval PMID:30640914 Recombination assay; assayed region: ade6 gene PMID:30640914 mbs1 hotspot quantification PMID:30640914 Recombination assay; assayed region: leu1-his5 interval PMID:30646830 Abolished tRNA cytosine-5 methylation of C49 and C50 (tRNA bisulphite sequencing) PMID:30646830 abolished tRNA C34, C48 methylation (trna bisulphite sequencing) PMID:30646830 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 trm402 (Trm4b) methylates C49 and C50 of tRNAs PMID:30649994 S3 PMID:30649994 3E PMID:30649994 3E PMID:30649994 4b PMID:30649994 3E PMID:30649994 3E PMID:30649994 Supplemental Figure S2 PMID:30649994 Supplemental Figure S2 PMID:30652128 Pulse-field gel electrophoresis (PFGE), Polymerase chain reaction (PCR), Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 tfs1∆ reduced centromere noncoding RNA in the clr4∆ strain. Northern blot assay PMID:30652128 rpd1-S7A reduced centromere noncoding RNA in the clr4∆ strain. Northern blot assay PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 rpd1-S7A increased the rate of gross chromosomal rearrangement in the otherwise wild-type background. Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Monitoring an extra-chromosome ChL PMID:30652128 Pulse-field gel electrophoresis (PFGE), Polymerase chain reaction (PCR), Monitoring an extra-chromosome ChL PMID:30652128 Pulse-field gel electrophoresis (PFGE), Polymerase chain reaction (PCR), Monitoring an extra-chromosome ChL PMID:30658998 supressed dna fragmentation PMID:30658998 fig 1B PMID:30658998 fig 1B PMID:30658998 fig 1B PMID:30658998 supressed dna fragmentation PMID:30658998 fig 1D supressed by hexestrol or clomifene PMID:30658998 fig 1C supressed by hexestrol PMID:30658998 fig 1B PMID:30658998 fig 1B PMID:30658998 fig 1D PMID:30658998 fig 1C PMID:30658998 fig 1B PMID:30659798 fig 2f PMID:30659798 fig2 PMID:30667359 Figure 6C PMID:30667359 Figure 6C PMID:30667359 Figure 6B PMID:30667359 Figure 6B PMID:30667359 Figure 6C PMID:30667359 Figure 2B PMID:30667359 Figure 2B PMID:30667359 Figure 2B PMID:30667359 Figure 2B PMID:30667359 Figure 6C PMID:30667359 Figure 6C PMID:30667359 Figure 6c PMID:30667359 Figure 6C PMID:30715423 ... Q-modification in tRNAs is to improve translation ofC-ending codons relative to U-ending codons in S. pombe. PMID:30715423 ... Q-modification in tRNAs is to improve translation ofC-ending codons relative to U-ending codons in S. pombe. PMID:30715423 Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆. PMID:30715423 Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆. PMID:30715423 Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆. PMID:30715423 Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆. PMID:30715423 Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆. PMID:30715423 No queuosine-mediated reduction of translational errors at GGC (Gly) and UGC (Tyr) codons PMID:30715423 Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆. PMID:30726745 Figure 7C, 7D PMID:30726745 Figure 7A PMID:30726745 Figure 6 PMID:30726745 Figure 7A PMID:30726745 Figure 7A PMID:30726745 Figure 7C, 7D PMID:30726745 Figure 7C, 7D PMID:30726745 Figure 7A PMID:30726745 Figure S5 PMID:30726745 Figure 2, Figure 3 PMID:30726745 Figure 1 PMID:30726745 Figure 2, Figure 3. PMID:30726745 Figure 7C, 7D PMID:30759079 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 Fig6 The nuclear envelope is marked with Cut11-GFP PMID:30759079 data not shown PMID:30759079 data not shown PMID:30759079 data not shown PMID:30759079 Fig6 The nuclear envelope is marked with Cut11-GFP PMID:30759079 Fig6 The nuclear envelope is marked with Cut11-GFP PMID:30759079 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 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 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 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 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 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:30773398 homodimer PMID:30773398 Figure 1E PMID:30773398 Figure 1E PMID:30773398 Fig 1a PMID:30773398 Fig 1a PMID:30773398 Figs 1C, S1 PMID:30773398 Figs 1B, 1D, 1F, S1, S2 PMID:30773398 Figs 1B, 1D, 1F, S1, S2 PMID:30773398 Figure S2 PMID:30773398 Figure S2 PMID:30773398 Figure S2 PMID:30773398 Figure 1E PMID:30773398 Figure 1E PMID:30773398 Figs 1B, 1D, 1F, S1, S2 PMID:30773398 Figure S2 PMID:30773398 Figure S2 PMID:30773398 Figure S2 PMID:30773398 Fig 3 PMID:30796050 also inferred from orthology and various genetic interactions PMID:30796050 Fig 3 PMID:30796050 Fig 4 PMID:30796050 Fig 4 PMID:30796050 Fig S3 PMID:30796050 Fig S3 PMID:30796050 Fig S3 PMID:30796050 Fig S3 PMID:30796050 Fig S3 PMID:30796050 Fig S3 PMID:30796050 Fig 1 PMID:30796050 Fig 4 PMID:30796050 Fig 1 PMID:30796050 Fig 2 PMID:30796050 Fig 3 PMID:30796050 Fig EV3 PMID:30796050 Fig 1 PMID:30796050 Fig 1 PMID:30796050 Fig 1 PMID:30796050 Fig 2 PMID:30796050 Fig 2, S2 PMID:30796050 Fig 3 PMID:30796050 Fig 3; less intense Y arc in 2D gel PMID:30796050 Fig 3; less intense Y arc in 2D gel PMID:30796050 Fig 4 PMID:30796050 Fig 4 PMID:30796050 Fig 1 PMID:30796050 Fig 1 PMID:30796050 Fig S1 PMID:30796050 Fig S1 PMID:30796050 Fig S2 PMID:30796050 Fig S2 PMID:30796050 Fig EV2 PMID:30796050 Fig EV3; restrictive temperature for cdc2-M68 PMID:30796050 Fig S2 PMID:30796050 Fig S2 PMID:30796050 Fig 2 PMID:30796050 Fig 2 PMID:30796050 Fig EV3 PMID:30806623 Fig. 6 PMID:30806623 Fig. 6 PMID:30806623 Fig. 6 PMID:30806623 Fig. 6 PMID:30806623 Fig. 1 PMID:30806623 Fig. 6 PMID:30806623 Fig. 1 PMID:30806623 Fig. 5 PMID:30806623 Fig. 1 PMID:30806623 Fig. 1 PMID:30806623 Fig. 1 PMID:30806623 Fig. 1 PMID:30806623 Fig. 3 PMID:30806623 Fig. 3 PMID:30810475 fig4 PMID:30810475 fig1b - for dga1 normal splicing of intonr 3, abnormal intron 2, S4 PMID:30810475 fig1b - for dga1 normal splicing of intonr 3, abnormal intron 2, S4 PMID:30810475 fig1b PMID:30810475 fig1b PMID:30810475 fig6 PMID:30810475 fig6 PMID:30810475 fig1b PMID:30810475 fig1b PMID:30810475 fig1 PMID:30810475 fig1 PMID:30810475 fig1 PMID:30810475 fig1 PMID:30810475 fig1 PMID:30810475 Required for splicing of introns with strong 5' splice site - U6 snRNA and branch site - U2 snRNA interactions PMID:30810475 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 In vitro RNA helicase activity using recombinant protein encoded by the helicase domain of Prp16 PMID:30810475 fig7 PMID:30810475 fig1b - for dga1 normal splicing of intonr 3, abnormal intron 2, S4 PMID:30810475 fig1 PMID:30810475 fig1 PMID:30810475 In vitro RNA helicase activity using recombinant protein encoded by the helicase domain of Prp16 PMID:30810475 fig1b - for dga1 normal splicing of intonr 3, abnormal intron 2, S4 PMID:30810475 fig7 PMID:30810475 fig1b - for dga1 normal splicing of intonr 3, abnormal intron 2, S4 PMID:30810475 fig7 PMID:30810475 fig7 PMID:30810475 fig4 PMID:30810475 fig7 PMID:30810475 figS6,7 PMID:30810475 figS6,7 PMID:30810475 figS6,7 PMID:30810475 figS6,7 PMID:30810475 fig7 PMID:30810475 fig7 they say fragmented nucleus but they stained chromosomes, not nuclear envelope PMID:30810475 fig7 PMID:30810475 fig7 PMID:30810475 fig4 PMID:30810475 fig1 PMID:30810475 fig4 PMID:30810475 fig4 PMID:30840879 fig 3 e PMID:30840879 fig 1B PMID:30840879 fig 2A Figure 2A PMID:30840879 fig 1B PMID:30840879 Figure 2A PMID:30840879 fig 3e PMID:30840879 fig 3e PMID:30840879 fig 3 c PMID:30840879 fig 3 c PMID:30840879 fig 3c PMID:30840879 fig 2b PMID:30840879 fig 4 PMID:30840879 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 F-BAR/BAR domain adaptors Rng10(751–950) interacts directly with the Rga7 F-BAR domain PMID:30840879 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 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 1F PMID:30840879 2b normal lpid binding PMID:30840879 fig 2A Figure 2A PMID:30840879 MEMBRANE LIPID BINDING Rga7 F-BAR preferred membranes rich in PI(4)P and PI(4,5)P2 (Figure 3D) PMID:30840879 MEMBRANE LIPID BINDING Rga7 F-BAR preferred membranes rich in PI(4)P and PI(4,5)P2 (Figure 3D) PMID:30840879 fig 4e PMID:30853434 Figure S4A (live cell imaging) PMID:30853434 Figure 3C-D (live cell DIC) PMID:30853434 FIg 1 D PMID:30853434 FIg 1 D PMID:30853434 FIg 1 D PMID:30853434 Fig 2 E-F PMID:30853434 Figure S4A PMID:30853434 Figure 4E (moved from wee) (skewed towards small, low severity) PMID:30853434 increased binding by about 2 fold from Figure 4C-D PMID:30853434 Figure 3A-B (Live-cell time-lapse imaging) PMID:30853434 Figure 1D-G (live cell imaging) PMID:30853434 Figure 2A-B (vw changed to cell division site during M-phase from septum) (live cell imaging) PMID:30853434 Figure 3A-B (Live-cell time-lapse imaging) PMID:30853434 Figure 3A-B (Live-cell time-lapse imaging) PMID:30853434 Figure 4A-B (live cell imaging) PMID:30853434 Figure 2E-F (live cell imaging) PMID:30853434 Figure 4G (live cell DIC) PMID:30853434 Figure S4F&H (live cell DIC) PMID:30853434 Figure S4F and G (vw move to FYPO:0006822 and requested parentage fix in FYPO) (live cell DIC) PMID:30853434 Figure S4F and G (vw move to FYPO:0006822 and requested parentage fix in FYPO) (live cell DIC) PMID:30853434 Figure S4C-D PMID:30853434 Figure 3D (live cell DIC) PMID:30853434 Figure 3C-D PMID:30853434 Figure 1H-I (live cell imaging) PMID:30853434 Figure 1C PMID:30853434 Figure S2A-B (vw changed from FYPO:0001677 to FYPO:0002874 to match rlc1) (live cell imaging) PMID:30853434 Figure S2A-B (vw changed from FYPO:0001677 to FYPO:0002874 to match rlc1) (live cell imaging) PMID:30853434 Figure S2A-B (vw changed from FYPO:0001677 to FYPO:0002874 to match rlc1) (live cell imaging) PMID:30853434 Figure S2A-B (live cell imaging) PMID:30853434 Figure S2C (live cell imaging) PMID:30853434 Figure S3A (live cell imaging) PMID:30853434 Figure S3C-D (live cell imaging) PMID:30853434 Figure S1 PMID:30853434 Figure S1 PMID:30853434 Figure S1 PMID:30853434 Figure S1 PMID:30853434 Figure S1 PMID:30853434 Figure S1 PMID:30853434 Figure 4I (Live-cell time-lapse imaging) PMID:30853434 Figure 4G (live cell DIC) PMID:30853434 Figure 4G (live cell DIC) PMID:30853434 Figure 4G (live cell DIC) PMID:30853434 Figure 4H (vw moved down to FYPO:0003481) (live cell DIC) PMID:30853434 Figure S4G (vw moved down to FYPO:0003481) (live cell DIC) PMID:30853434 Figure S4F & H (vw move to FYPO:0006822 and requested parentage fix in FYPO) (live cell DIC) PMID:30853434 Figure S4A (live cell imaging) PMID:30853434 Figure S3A (live cell imaging) PMID:30853434 Figure S3C-D (live cell imaging) PMID:30853434 Figure 1H-I (live cell imaging) PMID:30862564 converted from bp by cc PMID:30862564 converted from bp by cc PMID:30967422 figure2b PMID:30967422 figure2b PMID:30967422 figure2b PMID:30967422 figure2b PMID:30973898 figure 1B PMID:30973898 Fig 1D PMID:30973898 Fig 1D PMID:30973898 figure 5A PMID:30973898 figure 5A PMID:30973898 figure S2B PMID:30973898 figure S2A PMID:30973898 figure 5A PMID:30973898 figure 5A PMID:30973898 figure 5A PMID:30973898 figure 4C PMID:30973898 figure 4C PMID:30973898 figure 3A PMID:30973898 figure 3A PMID:30973898 figure 3A PMID:30973898 figure 3A PMID:30973898 figure 2D PMID:30973898 figure 2D PMID:30973898 Figure 2D PMID:30973898 Figure 2D PMID:30973898 figure 2C PMID:30973898 figure 2C PMID:30973898 figure 2C PMID:30973898 figure 2C PMID:30973898 figure 2B (two hybrid) PMID:30973898 figure 2B (two hybrid) PMID:30973898 figure 2B (two hybrid) PMID:30973898 figure 2B (two hybrid) PMID:30973898 figure S2B PMID:30973898 figure S2A PMID:30973898 figure 3A PMID:30973898 figure1 B PMID:30973898 figure1 A PMID:30973898 figure1 A PMID:30973898 figure1 A PMID:30973898 figure1 A PMID:30973898 figure1 A PMID:30973898 figure1 A PMID:30973898 figure1 A PMID:30973898 figure1 A PMID:30973898 figure 4 DAPI staining PMID:30973898 figure 4 C mini-chromosome Ch16 loss assay PMID:30973898 figure 5A PMID:30973898 mini-chromosome Ch16 loss assay PMID:30975915 figure 1A PMID:30975915 Figure 1 PMID:30975915 Figure 1 PMID:30975915 Figure 1 PMID:30975915 Fig 4 PMID:30975915 Fig 4 PMID:30975915 Fig. 4B PMID:30975915 Fig. 4B PMID:30975915 Figure 3 PMID:30975915 Figure 1 PMID:30975915 Figure 3 PMID:30975915 Fig. 4A PMID:30975915 Fig. 4B PMID:30975915 Fig. 2B PMID:30975915 figure3 PMID:30992049 hhf2 and hhf3 are wild-type. Only hhf2 is mutated. PMID:30992049 hhf1 and hhf3 are wild-type. Only hhf2 is mutated. PMID:30992049 hhf1 and hhf3 are wild-type. Only hhf2 is mutated. PMID:30992049 hhf1 and hhf3 are wild-type. Only hhf2 is mutated. PMID:30992049 hhf1 and hhf3 are wild-type. Only hhf2 is mutated. PMID:30992049 grows normally at 25 degrees but not at 30 degrees PMID:30992049 grows normally at 25 degrees but not at 30 degrees PMID:30992049 grows normally at 25 degrees but not at 30 degrees PMID:30992049 same as swi1delta alone PMID:30992049 grows normally at 25 degrees but not at 30 degrees PMID:30992049 hhf2 and hhf3 are wild-type. Only hhf2 is mutated. PMID:30992049 25 degrees; same as mst1-L344S alone PMID:30992049 same as nmt81-vid21 alone PMID:30996236 Fig 2 PMID:30996236 Fig 2 PMID:30996236 Fig 3 PMID:30996236 Fig 3 PMID:30996236 Fig 3 PMID:30996236 Fig 3 PMID:30996236 Fig 3 PMID:30996236 Fig 3 PMID:30996236 Fig 3 PMID:30996236 Fig 2 PMID:30996236 Fig 2 PMID:30996236 Fig 2 PMID:30996236 Fig 2 PMID:30996236 Fig 3 PMID:30996236 Fig 2 PMID:30996236 Fig 2 PMID:30996236 Fig 2 PMID:30996236 Fig 2 PMID:30996236 Fig 2 PMID:30996236 Fig 2 PMID:30996236 Fig 2 PMID:30996236 Fig 3 PMID:30996236 Fig 3 PMID:30996236 Fig 2 PMID:30996236 Fig 2 PMID:30996236 Fig 3 PMID:30996236 Fig 3 PMID:30996236 Fig 3 PMID:31000521 5B abolish Swi6 protein localization to centromere during vegetative growth PMID:31000521 5B PMID:31000521 SUPP S1 PMID:31000521 Figure 3B PMID:31000521 Figure 3B PMID:31000521 Figure 3B PMID:31000521 fig 3B PMID:31000521 Figure 3B PMID:31000521 Fig-2C PMID:31000521 Fig-2C PMID:31000521 Fig-2C PMID:31000521 Fig-2A Spindle pole-to-pole distance was measured based on the distance of duplicated SPBs revealed by Sad1-DsRed. PMID:31000521 (vw 3B? changed from normal to lagging, added penetrance) dfp1-CFP-2CD rescues minichromosome loss in the absence of Swi6. PMID:31000521 Fig-2A Spindle pole-to-pole distance was measured based on the distance of duplicated SPBs revealed by Sad1-DsRed. PMID:31000521 (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 Fig 7B PMID:31000521 fig 7B PMID:31000521 fig 7 B PMID:31000521 Fig 7 using minichromosome PMID:31000521 Fig 7 using minichromosome PMID:31000521 Fig 7 using minichromosome PMID:31000521 (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 (Figure 3B Chp1 fails to accumulate at noncentromeric location in the absence of Chp2 and Swi6. PMID:31000521 (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 ) Rad21 locates to centromere in dfp1-3A mutants. PMID:31000521 5C PMID:31000521 Fig 7 using minichromosome PMID:31000521 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 fig 7 B PMID:31000521 fig 7 B PMID:31000521 Rad21-GFP enrichment at the centromere is unaffected in swi6-sm1 (Figure S4C) PMID:31000521 5E PMID:31015410 Fig2 d,e,f,g,h supp fig6b PMID:31015410 Fig3a,b PMID:31015410 Fig 3c PMID:31015410 Fig3c,d, OE SUPRESSOR OF NEM1delta lem2 supresses the increased NC ratio of nem1 delta PMID:31015410 Fig3f PMID:31015410 supp Fig6a PMID:31015410 Supp Fig6 PMID:31015410 Fig4 a,c PMID:31015410 Fig2a,b,c PMID:31015410 Fig 1a shows the lem2 chromatin binding domain is not required to restrict enhancement of the NC ratio of rae1-167 PMID:31015410 Fig 1a,b,c PMID:31015410 Fig 1 PMID:31015410 Fig1 supp data PMID:31015410 Fig1 supp data PMID:31015410 Fig 4,b,c ENHANCER OF N/C ratio of lem2/rae1 PMID:31015410 Fig 4a,c PMID:31015410 Fig3f PMID:31015410 Fig 3c PMID:31015410 Fig 3c PMID:31015410 supp Fig 7 supression of lem2delta PMID:31015410 supp data Fig 1b,c PMID:31015410 Fig1 and Fig1supp data PMID:31015410 Fig3d PMID:31015410 Fig3d, OE lem2 supresses the increased NC ratio of rae1-167 PMID:31015410 Fig3e suppression of nem1delta PMID:31015410 Fig 3e PMID:31015410 Fig 1 (normal compaction) PMID:31015410 Fig 4a,c PMID:31015410 Fig4 a,c PMID:31015410 Fig1 supp data PMID:31015410 Fig1 supp data PMID:31015410 Fig1 supp data PMID:31015410 Fig1 supp data PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 Fig6 PMID:31030285 cell growth is slower than wild type in glycerol and ethanol medium PMID:31030285 Coq4 protein is decreased but Dlp1, Coq3, Coq5 and Coq8 are not PMID:31030285 Coq4 protein is increased but Dlp1, Coq3, Coq5, and Coq8 are not PMID:31030285 cell growth is faster than wild type in glycerol and ethanol medium PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig8 PMID:31030285 not shown PMID:31030285 Fig7 PMID:31030285 Fig7 PMID:31030285 Fig7 PMID:31030285 Fig7 PMID:31030285 Fig7 PMID:31030285 Fig7 PMID:31030285 Fig7 PMID:31030285 Fig7 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31030285 fig S1 PMID:31041892 Figure 3 PMID:31041892 Figure 4; blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants PMID:31041892 Figure 4; blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants PMID:31041892 Figure 3 PMID:31041892 Figure 3 PMID:31041892 Figure 2 PMID:31041892 Figure 2 PMID:31041892 Figure 3; blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants PMID:31041892 Figure 2; blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants PMID:31041892 fig1 PMID:31041892 Figure 4 PMID:31041892 Figure 5 PMID:31041892 Figure 4 PMID:31041892 Figure 2 PMID:31041892 Figure 2 PMID:31041892 Figure 5 PMID:31041892 Figure 3 PMID:31041892 fig1 PMID:31041892 fig1 PMID:31041892 blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants PMID:31041892 Figure 3; blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants PMID:31041892 Figure 2; blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants PMID:31041892 Figure 4; blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants PMID:31041892 Figure 4; blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants PMID:31053915 catechol O-methyltransferase activity (Vw I kept this as o-methytransferase since no report of catachols in fission yeast) PMID:31053915 catechol O-methyltransferase activity PMID:31072933 figure 6c PMID:31072933 figure S3 PMID:31072933 figure S3 PMID:31072933 figure S3 PMID:31072933 figure S3 PMID:31072933 figure S3 PMID:31072933 figure S3 PMID:31072933 figure S3 PMID:31072933 figure S3 PMID:31072933 figure S3 PMID:31072933 figure S3 PMID:31072933 figure S3 PMID:31072933 figure S3 PMID:31072933 figure S3 PMID:31072933 figure S3 PMID:31072933 figure S3 PMID:31072933 figure S3 PMID:31072933 figure S3 PMID:31072933 figure S4 PMID:31072933 figure S4 PMID:31072933 figure S4 PMID:31072933 fig 3 B PMID:31072933 fig 3 B PMID:31072933 fig 3 B PMID:31072933 figure 1c PMID:31072933 figure 3A PMID:31072933 figure 3A PMID:31072933 figure 3A PMID:31072933 figure 3A PMID:31072933 figure 3A PMID:31072933 figure 3A PMID:31072933 figure 3A PMID:31072933 figure 3A PMID:31072933 figure 3F PMID:31072933 figure 4 AB PMID:31072933 figure 4 AB PMID:31072933 figure 4 AB PMID:31072933 figure 4 AB PMID:31072933 figure 4 AB PMID:31072933 figure 4D-H PMID:31072933 figure 4D-H PMID:31072933 figure 4D-H PMID:31072933 figure 5C PMID:31072933 Fig 5C PMID:31072933 figure 5C PMID:31072933 figure S8 PMID:31072933 figure S8 PMID:31072933 figure S3 PMID:31072933 figure S3 PMID:31072933 figure S3 PMID:31072933 figure 2C PMID:31072933 figure2 PMID:31072933 figure 1e PMID:31072933 figure 1e PMID:31072933 figure 1e PMID:31072933 figure 1c PMID:31072933 figure 1c PMID:31072933 figure 1c PMID:31072933 figure 1c PMID:31072933 figure 1c PMID:31072933 figure 1c PMID:31072933 figure 1c PMID:31072933 figure 1c PMID:31072933 figure 1c PMID:31072933 figure 1c PMID:31072933 figure 1c PMID:31072933 figure 1c PMID:31072933 figure 1c PMID:31072933 figure 1c PMID:31072933 figure 1c PMID:31072933 figure 1c PMID:31072933 figure 1c PMID:31072933 figure 1c PMID:31072933 figure 1c PMID:31072933 (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 figure S7A PMID:31072933 figure S7A PMID:31072933 figure S7A PMID:31072933 figure S7A PMID:31072933 figure 6c PMID:31072933 figure 6c PMID:31072933 figure 6c PMID:31072933 figure 6c PMID:31072933 figure 6c PMID:31072933 figure 6c PMID:31072933 figure 6c PMID:31072933 figure 1G PMID:31072933 figure 1G PMID:31072933 figure 1G PMID:31072933 fig 2 PMID:31072933 figure 1G PMID:31072933 figure 1G PMID:31072933 Figure 1G/ figur2 PMID:31072933 figure S3 PMID:31089172 Figure 4A PMID:31089172 Fig. 6 PMID:31089172 Fig. 6 PMID:31089172 fig 6 PMID:31089172 Figure 6C-E PMID:31089172 Figure 6C-E PMID:31089172 Figure 5E PMID:31089172 Figure 5E PMID:31089172 Figure 5E PMID:31089172 Figure 5E PMID:31089172 Fig. 5D and Supplementary Fig. S2A,C PMID:31089172 Fig. 5D and Supplementary Fig. S2A,C PMID:31089172 Fig. 5D and Supplementary Fig. S2A,C PMID:31089172 Fig. 5D and Supplementary Fig. S2A,C PMID:31089172 Fig. 5B,C) PMID:31089172 Fig. 5B,C) PMID:31089172 Fig. 5B,C) PMID:31089172 Fig. 5B,C) PMID:31089172 Figure 4A PMID:31089172 fig 4 PMID:31089172 fig 4 PMID:31089172 fig 4 PMID:31089172 Figure 4AB PMID:31089172 Fig. 6 PMID:31089172 fig 2 A/B PMID:31089172 fig 2 A/B PMID:31089172 fig 2 C/D PMID:31089172 fig 2 C/D PMID:31089172 fig 2 C/D PMID:31089172 fig 2 E PMID:31089172 fig 2 E PMID:31089172 fig 2 E PMID:31089172 Fig. 3A top PMID:31089172 Fig. 3 PMID:31089172 Fig. 3 PMID:31089172 Fig. 3 PMID:31089172 Fig. 3 PMID:31089172 Fig. 3 PMID:31089172 Fig. 4A PMID:31089172 Figure 4A PMID:31089172 Figure 4A PMID:31089172 Figure 4A PMID:31089172 Figure 4A PMID:31089172 Figure 4AB PMID:31089172 Figure 4AB PMID:31089172 Figure 4AB PMID:31089172 Figure 4AB PMID:31089172 Figure 4AB PMID:31089172 Figure 4AB PMID:31089172 Figure 4AB PMID:31089172 Figure 4AB PMID:31089172 Figure 4AB PMID:31089172 Figure 4AB PMID:31089172 Fig. 4A PMID:31089172 Fig. 4A PMID:31089172 Fig. 4A PMID:31089172 Figure 4A PMID:31116668 fig 5 PMID:31116668 1d (vw: localized by the secretory pathway) PMID:31116668 1e PMID:31116668 fig4 PMID:31116668 5c PMID:31131414 Southern blot; same as rap1-7A single mutant PMID:31149897 Fig 6 PMID:31149897 Fig 4 PMID:31149897 Fig 3 PMID:31149897 Fig 5 PMID:31149897 Fig 5 PMID:31149897 PCNA foci persist longer than normal, and form large bright patches before disappearing (Fig 2). PMID:31149897 Figure 3A; increased spontaneous direct repeat recombination PMID:31149897 elg1∆ exhibits reduced direct repeat recombination associated with replication fork collapse at the RTS1 replication fork barrier PMID:31149897 Fig 4 PMID:31149897 Fig 4; very small difference from fbh1delta alone PMID:31149897 Fig 6 PMID:31149897 Fig 4 PMID:31178220 SpTam41 interacts strongly with cardiolipin (CL) PMID:31201205 Fig. 2BC PMID:31201205 Fig. 2BC PMID:31201205 small viable PMID:31201205 Figure 6 PMID:31201205 Figure 5 (vw: changed to pear, descendent of spherical) PMID:31201205 Figure 5, (VW: I made this more specific- figure 1E (36) this phenotype in increased in the presence of magnesium PMID:31201205 Figure 4 PMID:31201205 Figure 4 PMID:31201205 Fig.3 PMID:31201205 figure 7 PMID:31201205 Figure 6 PMID:31201205 Figure 6 PMID:31201205 Figure 4 PMID:31201205 Figure 4 PMID:31201205 Figure 4 PMID:31201205 Figure 4 PMID:31201205 Figure 4 PMID:31201205 Fig.3 PMID:31201205 figure 7B small viable PMID:31201205 Fig.3 PMID:31201205 Fig.3 PMID:31201205 Fig.3 PMID:31201205 Fig.3 PMID:31201205 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 Fig. 2BC PMID:31201205 Fig. 2BC PMID:31201205 Fig. 2BC PMID:31201205 figure 7B PMID:31201205 figure 7B PMID:31201205 figure 7B small, viable PMID:31239353 10-100 micromolar PMID:31239353 fig1 PMID:31239353 Figure 1A PMID:31239353 fig1 PMID:31239353 Figure 1A Zinc-dependen PMID:31239353 (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 figure 8 PMID:31239353 Figure 5D PMID:31239353 Figure 5D PMID:31239353 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 Figure 1B and 1C PMID:31239353 abolished ? PMID:31239353 fig1 abolished? PMID:31239353 fig1 PMID:31239353 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 Pho8 abundance is increased in high zinc in a loz1 deletion strain (Figure 2B and 2C) PMID:31239353 consistent with Loz1 facilitating the repression of pho8 gene expression in high zinc (Figure 2A) PMID:31239353 figure 7 PMID:31239353 figure 7 PMID:31239353 reduced alkaline phosphatase activity and Pho8 dimerization (assayed via an EGS cross linking experiment - see Figures 6C and 6D) PMID:31239353 reduced alkaline phosphatase activity and Pho8 dimerization (assayed via an EGS cross linking experiment - see Figures 6C and 6D) PMID:31239353 figure 7 PMID:31239353 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 Figure 5B PMID:31239353 figure 5B PMID:31239353 Figure 2B PMID:31239353 Figure 1B and 1C PMID:31239353 pho8 transcript and protein levels are increased in high zinc BUT ZINC DEPENDENT CHAnges are independent of transcript levels PMID:31257143 3b 80% 12 hours PMID:31257143 Figures S3B and S3D PMID:31257143 Figure S4 PMID:31257143 Figure S4 PMID:31257143 Figure 2B demonstrates robust arres 3b 80% 12 hours PMID:31257143 figure 2D PMID:31257143 figure 2d PMID:31257143 figure 2d PMID:31257143 Figure 2B demonstrates robust arres PMID:31257143 Figures S3B and S3C PMID:31260531 Rep2 locates SAGA complex at MBF-regulated promoters. PMID:31260531 chromatin association at MCBs is part of positive regulation of G1/S transition of mitotic cell cycle PMID:31269446 non-canonical termination sites PMID:31269446 18 °C PMID:31269446 18 °C PMID:31269446 18 °C PMID:31269446 18 °C PMID:31269446 18 °C PMID:31269446 18 °C PMID:31269446 18 °C PMID:31269446 18 °C PMID:31269446 non-canonical termination sites PMID:31269446 18 °C PMID:31269446 18 °C PMID:31269446 18 °C PMID:31269446 18 °C PMID:31269446 18 °C PMID:31269446 non-canonical termination sites PMID:31269446 18 °C PMID:31269446 18 °C PMID:31276301 Figure S1a PMID:31276301 Fig 4e PMID:31276301 Table 2 Figures 5a–d and S2) PMID:31276301 fig 4d PMID:31276301 fig 6 PMID:31276301 Furthermore, abnormally elon- gated cytoplasmic and spindle MTs were frequently observed in these cells (Figure 6). PMID:31276301 Fig 4a PMID:31276301 fig. 4e PMID:31276301 fig. 4e PMID:31276301 (Table 3) PMID:31276301 Fig 4b PMID:31276301 Figure S1a PMID:31276301 Figure S1a PMID:31276301 Figure S1a PMID:31276301 Figure S1a PMID:31276301 fig 6 PMID:31276301 Furthermore, abnormally elon- gated cytoplasmic and spindle MTs were frequently observed in these cells (Figure 6). PMID:31276301 Table 3 PMID:31276301 Figure 7b PMID:31276301 Fig 4a PMID:31276588 Figure 2C PMID:31276588 Figure 2C PMID:31276588 Figure 1E PMID:31276588 Figure 1E PMID:31276588 Figure 1F PMID:31276588 Figure 1F. PMID:31276588 Figure 1C PMID:31276588 Figure 1D PMID:31276588 Figure 1C PMID:31276588 Figure 1B PMID:31276588 Figure 1C PMID:31276588 Figure 1B PMID:31276588 Figure 2C PMID:31276588 Figure 2A PMID:31276588 Figure 1D PMID:31276588 Octo phosphatase IP8 is a relevant substrate for the Aps1 pyrophos- phatase with respect to phosphate homeostasis. PMID:31276588 reporter system PMID:31276588 Figure 1D PMID:31276588 Figure 1D PMID:31276588 Figure 1D PMID:31276588 Figure 1D PMID:31276588 Figure 1B PMID:31276588 Figure 1B PMID:31276588 Figure 1C PMID:31276588 Figure 2C PMID:31276588 Figure 2C PMID:31276588 Figure 2C PMID:31276588 Figure 2C PMID:31276588 Figure 2C PMID:31276588 Figure 2C PMID:31276588 Figure 2C PMID:31278118 Figure 4A https://github.com/pombase/fypo/issues/3693 PMID:31278118 table1 PMID:31278118 table 1 PMID:31278118 fig7 PMID:31278118 fig7 PMID:31278118 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 Figure 6B PMID:31278118 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 Fig 5 B vw: moved pds5 to assayed target PMID:31278118 Figure 6A) PMID:31278118 fig1 d PMID:31278118 fig 1D/E PMID:31278118 fig 1D/E PMID:31278118 fig 1D/E PMID:31278118 cells revealed that H3K9me2 was notably decreased at cen- tromeres and telomeres in pds5D (Figure 3, A and B). PMID:31278118 cells revealed that H3K9me2 was notably decreased at cen- tromeres and telomeres in pds5D (Figure 3, A and B). PMID:31278118 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 However, the localization of Pds5 to euchromatic locations was unaffected in hetero- chromatin-deficient cells (Figure 5E) PMID:31278118 However, the localization of Pds5 to euchromatic locations was unaffected in hetero- chromatin-deficient cells (Figure 5E) PMID:31278118 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 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 Figure S5 PMID:31278118 Figure 6B PMID:31278118 Figure 6B PMID:31285271 2d PMID:31285271 Fig.2 Asc1 associates with polysomes. PMID:31285271 cytoplasmic translation is a parent to this term PMID:31285271 3e PMID:31285271 3e PMID:31285271 3a PMID:31285271 3a PMID:31285271 2d PMID:31285271 2d PMID:31285271 1e PMID:31285271 1d PMID:31285271 Fig5. Asc1 colocalized with stress granule proteins in response to heat shock. PMID:31285271 2d PMID:31285271 2d PMID:31285271 6f PMID:31285271 6 PMID:31285271 fig4h PMID:31285271 fig4h PMID:31285271 fig4 PMID:31289327 4a PMID:31289327 S2 PMID:31289327 S2 PMID:31289327 S2 PMID:31289327 5 PMID:31289327 5 PMID:31289327 S2 PMID:31294478 4 PMID:31294478 4 PMID:31294478 4 PMID:31294478 4 PMID:31294478 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 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 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 coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472 PMID:31294478 coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472 PMID:31294478 coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472 PMID:31294478 coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472 PMID:31294478 2b PMID:31294478 Figure 5B PMID:31294478 COINCIDENT WITH 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472 PMID:31294478 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 fig 1 A and F PMID:31294478 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 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 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 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 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 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 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 ChIP-qPCR of Dbl8 indicates that Dbl8 is enriched at the rDNA and at highly-expressed RNAPII-transcribed genes PMID:31294478 2c, 5d PMID:31294478 2c, 5d PMID:31294478 2c, 5d PMID:31294478 2c, 5d PMID:31294478 2b PMID:31294478 2b PMID:31294478 2b PMID:31294478 2b PMID:31294478 2b PMID:31294478 2b PMID:31294478 2b PMID:31294478 3 PMID:31294478 3 PMID:31294800 UAAU motif PMID:31315658 Additional file 1: Fig. S1b, c PMID:31315658 n sharp contrast, the H3K9me2 levels remained constant in leo1∆ cells throughout G0 phase (Fig. 2; Additional file 2: Fig. S2 PMID:31315658 Additional file 1: Fig. S1b, c PMID:31315658 (Fig. 1c) PMID:31315658 Additional file 1: Fig. S1b, c PMID:31332096 reduced chk1 phosphorylation PMID:31332096 elimination of Rad3-specific phosphorylation PMID:31341193 fig 1 Increased colocalization with Cfr1 PMID:31341193 Microscopy PMID:31341193 Fig 1 a-c PMID:31341193 Fig 1 a-c PMID:31341193 fig 1d PMID:31341193 fig5 PMID:31341193 Dot-Blot assay PMID:31341193 Evaluated by measuring the size of Vps10-GFP foci PMID:31341193 37ºC PMID:31341193 28ºC PMID:31341193 Reduced co-localyzation with the PI3P probe Cherry-FYVE PMID:31341193 Co-localization with TGN marker PMID:31341193 FIg 3 Increased co-localization with Cfr1 PMID:31341193 Reduced co-localization with the PI3P probe Cherry-FYVE PMID:31341193 Increased co-localization with Cfr1 PMID:31341193 Reduced co-localization with the PI3P probe Cherry-FYVE PMID:31341193 Increased co-localization with Cfr1 PMID:31341193 Dot-Blot test PMID:31341193 fig 7 Syb1 co-localizes with late endosome markers PMID:31341193 fig 7 PMID:31341193 Reduced growth at 37ºC on YES agar plates PMID:31341193 Reduced growth on 0.6M KCl plates PMID:31341193 isp6 delta supresses the abnormal Vps10 proessing detected in gga21 delta gga22 delta strain PMID:31341193 isp6 delta suppresses Vps10 abnormal processing observed in ent3 delta gga22 delta strain PMID:31341193 isp6 delta supresses the abnormal Vps10 processing detected in ent3 delta gga21 delta gga22 delta strain PMID:31341193 Microscopy PMID:31341193 Microscopy PMID:31341193 isp6 delta supresses the abnormal Vps10 processing detected in vps35 delta strain PMID:31341193 Fig1 (minor) PMID:31341193 Fig1 (major) PMID:31341193 fig1 PMID:31341193 fig1 PMID:31341193 fig1 PMID:31341193 fig5 PMID:31341193 fig1 PMID:31341193 fig1 PMID:31341193 this is in a mutant but I guess it occurs physiologicall? PMID:31350787 fig5 PMID:31350787 "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:31350787 fig2A The Dmti2 mutant was not able to grow at all on medium containing glycerol at the restrictive temperature of 37 °C PMID:31350787 figb PMID:31350787 fig1 PMID:31350787 Fig. 3 PMID:31350787 Fig. 3 PMID:31350787 fig4B PMID:31350787 fig5 PMID:31350787 fig6 PMID:31350787 fig1 PMID:31350787 fig1 PMID:31350787 fig1 PMID:31350787 fig1 PMID:31350787 fig1 PMID:31350787 fig1 PMID:31350787 "fig 1A """ PMID:31350787 "fig 1A """ PMID:31350787 "fig 1A """ PMID:31366733 fig7 PMID:31366733 fig7 PMID:31366733 fig7 PMID:31366733 fig7 PMID:31366733 fig7 PMID:31371524 figure 6 PMID:31371524 inhinits hhf4 binding PMID:31371524 figure 2 PMID:31371524 figure 2 PMID:31371524 figure 2 PMID:31371524 figure 4 PMID:31371524 figure 6 PMID:31427431 s2 PMID:31427431 7, type II cells PMID:31427431 7 PMID:31427431 7 PMID:31427431 7 PMID:31427431 7 PMID:31427431 7 PMID:31427431 7 PMID:31427431 6 PMID:31427431 6 PMID:31427431 6 PMID:31427431 6 PMID:31427431 6 PMID:31427431 6 PMID:31427431 6 PMID:31427431 6 PMID:31427431 6 PMID:31427431 5 PMID:31427431 5 PMID:31427431 5 PMID:31427431 4 PMID:31427431 s2 PMID:31427431 2f PMID:31427431 2f PMID:31427431 2f PMID:31427431 2f PMID:31427431 2 PMID:31427431 2 PMID:31427431 2 PMID:31427431 2 PMID:31427431 2 PMID:31427431 2 PMID:31427431 1f PMID:31427431 1e PMID:31427431 1e PMID:31427431 S1 PMID:31427431 1b PMID:31427431 1b PMID:31427431 1b PMID:31427431 1b PMID:31427431 1b PMID:31427431 1b PMID:31427431 1b PMID:31427431 1b PMID:31427431 1b PMID:31427431 1b PMID:31427431 1b PMID:31427431 1b PMID:31427431 1 PMID:31456006 leucine auxotroph background PMID:31456006 bunch of auxotrophic backgrounds shown - indicative of a.a. starvation PMID:31456006 leucine auxotroph background PMID:31468675 measured by cell growth spot assay PMID:31468675 colocalizes with H3K9me2 PMID:31468675 colocalizes with H3K9me2 PMID:31468675 colocalizes with H3K9me2 PMID:31468675 measured by cell growth spot assay PMID:31468675 partial derepression of marker gene at silent mating-type cassette; measured by cell growth spot assay PMID:31468675 spot assay PMID:31468675 measured by cell growth spot assay PMID:31477575 fig2b PMID:31477575 S1 PMID:31477575 fig2b PMID:31477575 fig1 PMID:31477575 fig1 PMID:31477575 fig1 PMID:31477575 S1 PMID:31477575 fig2b PMID:31477575 S3B PMID:31477575 S3B PMID:31477575 S3B PMID:31477575 S1 PMID:31477575 3c PMID:31477575 S1 PMID:31477575 fig2b PMID:31477575 3c PMID:31477575 S1 PMID:31477575 fig1 PMID:31477575 S1 PMID:31477575 S1 PMID:31477575 fig2b PMID:31477575 S1 PMID:31477575 S1 PMID:31483748 Recombination rates were decreased by 10-fold in mto1∆ strains in both recombination substrates (Figure 4B) PMID:31483748 issues/3588 decreased PMID:31483748 Figure 2C PMID:31483748 Figure 2C PMID:31483748 Figure 2C No increase in severity to mto1 delete PMID:31483748 fig2 PMID:31483748 fig2 PMID:31483748 fig2 PMID:31483748 issues/3588 Figure 5, A–E PMID:31483748 Figure 2A PMID:31483748 fig2 PMID:31483748 fig2 PMID:31483748 fig2 PMID:31483748 Figure S1A PMID:31483748 Figure S1A PMID:31483748 Figure 3, A and B . number and intensity PMID:31483748 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 Figure 3, A and B PMID:31483748 fig2 PMID:31483748 fig2 PMID:31483748 fig2 PMID:31483748 fig1 B–G PMID:31483748 Recombination rates were decreased by 10-fold in mto1∆ strains in both recombination substrates (Figure 4B) PMID:31483748 Reduced Rad21 binding to chromosome arms PMID:31495586 Figure2, Increased 1.5-fold, assayed using CHD PMID:31495586 Figure5 PMID:31495586 Figure 4 and 6 PMID:31495586 Figure 4 PMID:31495586 Figure 3 PMID:31495586 FigureS5, assayed using LifeAct PMID:31495586 FigureS5, assayed using LifeAct PMID:31495586 Figure S6 PMID:31495586 Figure S6 PMID:31495586 Figure S6 PMID:31495586 Figure S6 PMID:31495586 1.1 fold, Figure S2 PMID:31495586 Figure S3 PMID:31495586 Figure S3 PMID:31495586 Figure S3 PMID:31495586 Figure S3 PMID:31495586 Figure S1, assayed using CHD PMID:31495586 Figure3, S4, assayed using Myo52 and Fus1 PMID:31495586 Figure S5, assayed using LifeAct PMID:31495586 FigureS3 PMID:31495586 FigureS3 PMID:31495586 FigureS3 PMID:31495586 FigureS3 PMID:31495586 Figure 3 PMID:31495586 Figure 6 PMID:31495586 Figure 6 PMID:31495586 Figure6 PMID:31495586 Figure 6 PMID:31495586 Figure 4 PMID:31495586 Figure 4 and 6 PMID:31495586 Figure 4 and 6 PMID:31495586 Figure 4 and 6 PMID:31495586 Figure1 PMID:31495586 Figure1 PMID:31495586 Increased 4-fold, Figure2 PMID:31495586 Figure 3 PMID:31495586 Figure 3 PMID:31495586 Figure 1 PMID:31495586 Figure 2 PMID:31495586 Increased 4-fold, FigureS1 PMID:31495586 Figure6 PMID:31495586 Figure6 PMID:31495586 Figure6 PMID:31495586 assayed using CHD, FigureS1 PMID:31495586 Figure6 PMID:31495586 Increased 4-fold, Figure2 PMID:31495586 Figure 3 PMID:31495586 Figure 3 PMID:31495586 Figure 3, assayed using Myo52 PMID:31495586 Figure 5 PMID:31495586 Figure 3 PMID:31495586 Figure 3, assayed using Myo52 PMID:31495586 Figure 5, assayed using Myo52 PMID:31495586 Figure 5, assayed using Myo52 PMID:31495586 Figure 5, assayed using Myo52 PMID:31495586 Figure 2 PMID:31495586 Figure 2 PMID:31495586 Figure 2 PMID:31495586 Figure 2 PMID:31495586 Figure 2 PMID:31495586 Figure 2 PMID:31495586 Figure 2 PMID:31495586 Figure 2 PMID:31495586 Figure5 PMID:31509478 fig 1 PMID:31509478 figure1 PMID:31509478 fig2 PMID:31509478 fig3 PMID:31509478 figS3C PMID:31509478 figS3C PMID:31509478 fig3 PMID:31509478 Figure 3E) PMID:31509478 figS3C PMID:31509478 fig3 PMID:31509478 figS3C PMID:31509478 fig3 PMID:31509478 synonym =ring collapse fig3F PMID:31509478 fig6 PMID:31509478 3F PMID:31509478 fig1 PMID:31509478 Figure 6A PMID:31509478 fig3 PMID:31509478 Figure 3E) PMID:31515876 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 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 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 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 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 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 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 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 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 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 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 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 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 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:31532702 Figure S5 PMID:31532702 figure 1B PMID:31532702 single nucleus PMID:31532702 Figure 1D, E . monopolar? PMID:31532702 Figure figure 1B, D PMID:31532702 Figure 2A PMID:31532702 I didn't check the supp, but probably can only make this annotation? PMID:31532702 top, Figure 3B, C) PMID:31532702 meiosis I inital Figure 3B, C PMID:31532702 Figure 2A PMID:31532702 Figure S3B, C pentrance, frequently like quadruple PMID:31532702 28 ~ 32 min, Figure 3B; and 24 ~ 28 min, Figure S3B) PMID:31532702 28 ~ 32 min, Figure 3B; and 24 ~ 28 min, Figure S3B) PMID:31532702 Figure 5B PMID:31532702 Figure 5C, D PMID:31532702 Figure 5E PMID:31532702 Figure 5E PMID:31532702 Figure S6 PMID:31532702 Figure 5G (this term referes to initial PMID:31532702 Figure 5H PMID:31532702 Figure 5I PMID:31532702 Figure 6A PMID:31532702 Figure 6D, E PMID:31532702 meiotic . The Nuf2-containing kinetochore complex serves as a physical fulcrum for microtubule-dependent SPB separation PMID:31532702 figure 1B PMID:31532702 The Nuf2-containing kinetochore complex serves as a physical fulcrum for microtubule-dependent SPB separation PMID:31538680 Mutant proliferates faster and with shorter lag than wildtype in sublethal concentrations of hydroxyurea, phleomycin or doxorubicin PMID:31538680 Mutant proliferates faster and with shorter lag than wildtype in sublethal concentrations of hydroxyurea, phleomycin or doxorubicin PMID:31538680 Mutant proliferates faster and with shorter lag than wildtype in sublethal concentrations of hydroxyurea, phleomycin or doxorubicin PMID:31562247 fig 3a PMID:31562247 (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 figure 4c PMID:31562247 figure 4c PMID:31562247 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 Indeed, no noticeable change in mitochondrial morphology or altered mitochondrion numbers were found in the three mutant cells cultured in glucose-rich EMM (Fig. 5, C and D). PMID:31562247 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 figure 4ab PMID:31562247 figure 4ab PMID:31575705 fig1 PMID:31575705 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 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 Fig 1A growth inhibited by 0.005% MMS after 4 days PMID:31575705 Fig 2 C RTS1-RFB assay PMID:31575705 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 RTS1-RFB assay PMID:31575705 Figure 1A PMID:31575705 Figure 1A PMID:31575705 constitutive PMID:31582398 Figure. 3C, D, E, F and Video 5 mitochondrial mixing during meiosis PMID:31582398 Figure. 5C, D normal (increased mitochondrial segregation during meiosis) PMID:31582398 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 Figure. 3C, D, E, F and Video 5 mitochondrial mixing during meiosis PMID:31582398 "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:31584934 fig. 6 PMID:31584934 fig. 6 PMID:31584934 fig. 7 PMID:31584934 fig. 6 PMID:31584934 fig. 6 PMID:31584934 fig. 6 PMID:31584934 fig. 6 PMID:31584934 fig. 6 PMID:31584934 fig. 6 PMID:31584934 fig. 6 PMID:31584934 fig. 6 PMID:31584934 fig. 6 PMID:31584934 coincident with replication fork barrier but dependent on JM formation - not sure if we can be more specific here than nuclear chromatin? PMID:31584934 fig. 3c PMID:31584934 fig. 3 PMID:31584934 fig. 3,4 PMID:31584934 fig. 3 PMID:31584934 """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 """Reciprocally, H3-H113D-HA association with wt H3 and H4 were severely reduced""" PMID:31584934 fig. 2 PMID:31584934 "changed to decreased from abolished based on ""H3-FLAG association with H3-H113D-HA was severely reduced""" PMID:31584934 fig. 6 PMID:31615333 Figure S3 PMID:31615333 Figure S1 PMID:31615333 Figure S3 PMID:31615333 Figure 2 and 3 PMID:31615333 Figure 2 and 3 PMID:31615333 Figure 2, detected by northern blot analysis PMID:31615333 Figure 2 and S3 PMID:31615333 Figure S3 PMID:31615333 Figure 1c PMID:31615333 Figure 2 and S3 PMID:31615333 Figure 2 and S3 PMID:31615768 fig 4 PMID:31615768 S2A/4 PMID:31615768 S2A PMID:31615768 fig 3I PMID:31615768 fig 3 PMID:31615768 fig 3 PMID:31615768 fig 1C PMID:31615768 fig 3 PMID:31615768 fig 1C PMID:31615768 figureS4 PMID:31615768 1A PMID:31615768 S2 PMID:31615768 S2A/4 PMID:31615768 S1 PMID:31615768 fig3a by cen2-GFP observation PMID:31615768 1E unbundled microtubules seen in early mitosis PMID:31615768 1E unbundled microtubules seen in early mitosis PMID:31615768 fig 4 PMID:31618856 fig1 PMID:31618856 Figure 2D PMID:31618856 defective in microtubule growth during both interphase and mitosis PMID:31618856 appears to retain normal microtubule nucleation activity PMID:31618856 fig 3 PMID:31618856 fig 4 PMID:31618856 fig 4 PMID:31618856 fig 4 PMID:31641022 "chnaged from ""increased rate of sporulation""" PMID:31641022 fig2 PMID:31644361 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:31644361 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 Figure 1 D Phosphorylation of Wee1 in fission yeast cells was reduced in the catalytically inactive mutant cdr1(K41A) PMID:31644361 Cdr1 directly phosphory- lated Wee1, but Cdr1(K41A) did not (Figure 1H). PMID:31644361 Figure 1H (in vitro) Cdr1 directly phosphory- lated Wee1, but Cdr1(K41A) did not (). PMID:31644361 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 deed, cdr1∆ wee1(4A) cells divided at the same size as cdr1∆ cells PMID:31644361 (Figure 3C) Both wee1(4A) and cdr1∆ were synthetically lethal with cdc25-dD PMID:31644361 (Figure 4A). We confirmed that S. pombe Cdk1- asM17 directly thiophosphorylates Wee1 and Wee1(K596L) PMID:31644361 (Figure 3C) Both wee1(4A) and cdr1∆ were synthetically lethal with cdc25-dD PMID:31644361 Accordingly, the size of wee1(4A) cells was largely (but not entirely) insensitive to Cdr1 overexpression (Figure 3G). PMID:31644361 (Figure 3, A and D). We confirmed that wee1(4A) protein level does not increase and still localizes to cortical nodes PMID:31644361 Fig 1C overexpression of Cdr1 but not of Cdr2 re- sulted in reduced cell size in cdr1∆cdr2∆ cells (Figure 1C PMID:31644361 Fig1B Cdr1 overexpression induced hyperphosphorylation of Wee1 and loss of Cdk1-pY15, indicating inhibition of Wee1 kinase activity, PMID:31644361 Fig1B. In contrast, Cdr2 overexpression induced hyperphosphoryla- tion of Wee1 but no change in Cdk1-pY15 PMID:31644361 Fig1B Cdr1 overexpression induced hyperphosphorylation of Wee1 and loss of Cdk1-pY15, indicating inhibition of Wee1 kinase activity, PMID:31644361 Fig 1B Cdr1 overexpression induced hyperphosphorylation of Wee1 and loss of Cdk1-pY15, indicating inhibition of Wee1 kinase activity, PMID:31644361 Figure 3 B PMID:31644361 Fig1 In contrast, Cdr2 overexpression induced hyperphosphoryla- tion of Wee1 but no change in Cdk1-pY15 PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Table PMID:31657618 Fig. 3 PMID:31657618 Fig. 3 PMID:31657618 Fig. 3 PMID:31657618 Fig. 3 PMID:31657618 Fig. 3 PMID:31657618 Fig. 3 PMID:31657618 Fig. 4 PMID:31657618 Fig. 4 PMID:31657618 Fig. 4 PMID:31712578 Table S3 PMID:31712578 Table S3; spore viability lower than wild type (~50% of wild-type viability) PMID:31712578 Table S3 PMID:31712578 Table S3 PMID:31712578 Table S3 PMID:31712578 Table S3; spore viability similar to wild type PMID:31712578 Table S3 PMID:31712578 Table S3 PMID:31712578 Table S3; spore viability similar to wild type PMID:31712578 Table S3; spore viability similar to wild type PMID:31712578 Table S3; spore viability similar to wild type PMID:31712578 Table S3; spore viability similar to wild type PMID:31712578 Table S3 PMID:31712578 Table S3; spore viability similar to wild type PMID:31712578 Table S3; spore viability similar to wild type PMID:31712578 Table S3 PMID:31719112 temperature permissive for mcm4/cdc21-M68 PMID:31719112 temperature restrictive for cdc22-M45 PMID:31719163 localizes to division site after Gef1 and Scd2, but before contractile ring constriction begins PMID:31719163 localizes to division site before Scd1, and before contractile ring constriction begins PMID:31719163 localizes to division site before Scd1, and before contractile ring constriction begins PMID:31748520 . Similarly, we observed about a twofold reduction of Tra2 levels from NuA4 (Fig. 2b). PMID:31748520 RNA-seq PMID:31748520 RNA-seq PMID:31748520 Decreased Tra1 interaction with SAGA complex PMID:31748520 Silver staining analysis showed that Hsp90 inactivation causes a specific decrease of Tra1 in Spt7 purification eluates (Supplementary Fig. 6). effect is modest in this hypomorphic mutant, this observation supports the conclusion that Hsp90, like TTT, contributes to the de novo assembly of Tra1 into SAGA. PMID:31748520 Tra2 contributes to the scaffolding and stabilisation of the entire NuA4 complex. PMID:31748520 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 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 (Fig. 5d) PMID:31748520 RNA-seq PMID:31748520 RNA-seq PMID:31748520 RNA-seq PMID:31748520 (Fig.1e, f) spt7/tra1 pho84 and mei2 promoters. and spt7/tras ssa2 promoter PMID:31748520 (Fig.1e, f) spt7/tra1 pho84 and mei2 promoters. and spt7/tras ssa2 promoter PMID:31748520 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 whereas tra1-Sctra1 strains show no growth defects, as compared with wild-type cells (Fig. 5d). PMID:31748520 whereas tra1-Sctra1 strains show no growth defects, as compared with wild-type cells (Fig. 5d). PMID:31748520 RNA-seq PMID:31748520 Normal Tra1 interaction with SAGA complex PMID:31748520 Decreased levels of Tra1 and Tra2 in SAGA and NuA4 complexes, respectively Figure 2 PMID:31748520 Abolished Tra1 interaction with SAGA complex PMID:31748520 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 Abolished Tra1 interaction with SAGA complex PMID:31748520 RNA-seq PMID:31748520 (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 See Figure 4 PMID:31748520 See Figure 3c-d PMID:31748520 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 Decreased levels of Tra1 and Tra2 in SAGA and NuA4 complexes, respectively Figure 2 PMID:31748520 (Fig.1e, f) spt7/tra1 pho84 and mei2 promoters. and spt7/tras ssa2 promoter PMID:31748520 Abolished Tra1 interaction with SAGA complex PMID:31748520 Abolished Tra1 interaction with SAGA complex PMID:31777937 A novel 5′-hydroxyl dinucleotide hydrolase activity for the DXO/Rai1 family of enzymes PMID:31811152 Figure 4a PMID:31811152 Figure 1b (live cell observation) PMID:31811152 Figure 1b (live cell observation) PMID:31811152 Figure 4a. homologous pairing examined at C24 locus PMID:31811152 Figure 1b, (live cell observation) PMID:31811152 fig2 PMID:31811152 Figure 1b (live cell observation) PMID:31811152 C24 locus. fig2 PMID:31811152 C24 locus. fig2 PMID:31811152 Figure 1b (live cell observation) PMID:31811152 fig2 PMID:31811152 Figure 1b (live cell observation) PMID:31811152 Figure 1b, Figure 4b (live cell observation) PMID:31811152 Figure 4b (live cell observation) PMID:31811152 Figure 1b (live cell observation) PMID:31811152 Figure 1b (live cell observation) PMID:31811152 Figure 1c PMID:31811152 Figure 1c PMID:31811152 Figure 4b (live cell observation) PMID:31811152 Figure 4b, PMID:31833215 same as maf1delta alone PMID:31837996 similar to pob3delta alone PMID:31837996 RNA-seq PMID:31837996 RNA-seq PMID:31837996 RNA-seq PMID:31837996 RNA-seq PMID:31837996 similar to pob3delta alone PMID:31837996 RNA-seq PMID:31837996 assayed using bulk histones PMID:31837996 assayed using bulk histones PMID:31848341 binds H3-H4 dimer; assayed in vitro using Xenopus histones PMID:31895039 Fig.2 supp1 PMID:31895039 "Figure 5Dm : ""In vitro Rad21 phosphorylation was abolished when Pef1 was purified from psl1 deleted cells""" PMID:31895039 (Figure 5E and Figure 5—figure supplement 1). Replacement of T262 by an alanine abolished in vitro Rad21 phosphorylation by Pef1-GFP PMID:31895039 fig 5g PMID:31895039 antagonises pef1 PMID:31895039 Fig.1b PMID:31895039 Fig.7. Phenotype suppressed by the deletion of the pef1 gene PMID:31895039 Fig.7. Phenotype suppressed by the deletion of the pef1 gene PMID:31895039 Fig.4 PMID:31895039 Fig.4 PMID:31895039 Fig.7 PMID:31895039 Fig.7 PMID:31895039 Fig.6 PMID:31895039 Fig.1 PMID:31895039 Fig.1 PMID:31895039 Fig.1 PMID:31895039 Fig.8 PMID:31895039 Fig.8 PMID:31895039 Fig.8 PMID:31895039 Fig.8 PMID:31895039 Fig.8 PMID:31895039 Fig.8 PMID:31895039 Fig.8 PMID:31895039 Fig.5 PMID:31895039 34°C, Fig.7 PMID:31895039 34°C, Fig.7 PMID:31895039 Fig.7. Phenotype suppressed by the deletion of pef1 PMID:31895039 Fig.7. Phenotype suppressed by the deletion of pef1 PMID:31895039 Fig.7 PMID:31895039 Fig.7 34°C PMID:31895039 Fig.7 PMID:31895039 Fig.7 PMID:31895039 Phosphorylates Rad21 on threonine 262. Fig.5 PMID:31895039 Fig.5 PMID:31895039 "Figure 1—figure supplement 1. ""although colonies were tiny and grew very slowly""" PMID:31895039 Figure 1—figure supplement 1 PMID:31895039 Figure 1—figure supplement 1 PMID:31895039 Fig.1 PMID:31895039 Fig.1 PMID:31895039 fig1c PMID:31895039 Fig. 1 36.5°C PMID:31895039 Fig. 2 PMID:31895039 Fig.1 36.5°C PMID:31895039 36.5°C PMID:31895039 Figure 2—figure supplement 1 PMID:31895039 Fig. 7. The phenotype is exacerbated by pph3 deletion and rescued by pef1 deletion PMID:31895039 Psm1 and Mis4 are found in Pef1 immunoprecipitates (Fig. 5AB) PMID:31895039 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:31911490 I think these can be mopre specific decreased catabolism (ie increased stability in contract ti increased expression)) PMID:31911490 I think these can be mopre specific decreased catabolism (ie increased stability in contract ti increased expression)) PMID:31911490 fig 5C PMID:31911490 fig 5e PMID:31911490 Fig. 5B PMID:31911490 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 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 I think these can be mopre specific decreased catabolism (ie increased stability in contract ti increased expression)) PMID:31911490 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 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 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 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 12.13 + 0.1 PMID:31911490 fig 4h PMID:31911490 Fig. 4B PMID:31911490 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 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 FIg2 PMID:31911490 fig 3f PMID:31911490 Fig. 1B PMID:31911490 (Fig. 1B) PMID:31911490 and enhanced expression of Wak1, Wis1, and Pyp1 proteins during unperturbed growth (Fig. 5C) a PMID:31911490 (Fig. 1B) PMID:31911490 (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 Fig 2B PMID:31911490 Fig. 1B Fig. 1C (14.040.25 versus 11.980.29m, respectively) PMID:31911490 I think these can be mopre specific decreased catabolism (ie increased stability in contract ti increased expression)) PMID:31911490 fig 1B PMID:31911490 fig2C PMID:31932483 Fig. 6E PMID:31932483 Fig. 2 PMID:31932483 Fig 4B; 1 M KCl in agar PMID:31932483 Fig 4B; 1 M KCl in agar PMID:31932483 Fig 4B; 1 M KCl in agar PMID:31932483 Fig 4B; 1 M KCl in agar PMID:31932483 Fig 4B; 1 M KCl in agar PMID:31932483 Fig 4B; 0.5 mM H2O2 in agar PMID:31932483 Fig 4B; 0.5 mM H2O2 in agar PMID:31932483 Fig 4B; 0.5 mM H2O2 in agar PMID:31932483 Fig 4B; 0.5 mM H2O2 in agar PMID:31932483 Fig 4B; 0.5 mM H2O2 in agar PMID:31932483 Fig 4B; 0.5 mM H2O2 in agar PMID:31932483 Fig 4B; 0.5 mM H2O2 in agar PMID:31932483 Fig 4B; 1 M KCl in agar PMID:31932483 Fig 4B; 1 M KCl in agar PMID:31932483 Fig. 6F PMID:31932483 Fig. 7E PMID:31932483 Fig. 4A PMID:31932483 Fig. 3 PMID:31941401 Pho8Δ60 assay (Fig. S3A). PMID:31941401 Figure 1E PMID:31941401 Figure 3A,B ut reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8 PMID:31941401 Figure 3A,B ut reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8 PMID:31941401 Figure 1F PMID:31941401 Figure 1G) PMID:31941401 Figure 3A,B ut reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8 PMID:31941401 Pho8Δ60 assay (Fig. S3A). PMID:31941401 Fig. S2) PMID:31941401 Fig. S2 PMID:31941401 Figure 1G) PMID:31941401 Figure 3A,B ut reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8 PMID:31941401 Figure 3A,B ut reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8 PMID:31941401 Figure 1B PMID:31941401 Fig. S2) PMID:31941401 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 Figure 3A,B ut reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8 PMID:31941401 Figure 1G) PMID:31941401 Figure 1G) PMID:31941401 Figure 1G) PMID:31941401 Figure 3A,B PMID:31941401 Figure 2A Pho8Δ60 autophagy assay PMID:31980821 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 5A. bqt4delta/ telomerase + cells exhibited wild-type telomeres that were stable in post-mitotic cells PMID:31980821 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 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 2B PMID:31980821 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 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 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 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 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 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 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 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 accumulation of TERRA depends on Cid14, a RNA poly adenyl-transferase, (Supplementary Figure S5) PMID:31980821 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 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:32012158 figure 1 a PMID:32012158 figure 1 a PMID:32012158 figure 1 a PMID:32012158 figure 1 a PMID:32012158 figure S3A COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED IN GENOME PMID:32012158 figure S3A COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED PMID:32012158 figure S3A COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED PMID:32012158 figure 1 a PMID:32012158 figure 2 PMID:32012158 figure S3A PMID:32012158 figure S3A PMID:32012158 The interaction between these proteins was abolished in the absence of red1 (Fig 3A), suggesting that Red1 physically links Mmi1 with the exosome. and Fig 4B The direct binding of Red1 with Rrp6 was also observed (Fig 4B). PMID:32012158 figure 3A PMID:32012158 figure S3A PMID:32012158 figure S3A COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED PMID:32012158 figure 2 PMID:32012158 figure S3A PMID:32012158 figure S3A PMID:32012158 figure 5A PMID:32012158 figure 5B PMID:32012158 figure 5B PMID:32012158 figure 6 a PMID:32012158 figure 1 a PMID:32012158 figure 5A PMID:32012158 figure S3A PMID:32012158 figure S3A PMID:32012158 figure S3A PMID:32023460 decreased Pil1 protein abundance Figure S1F PMID:32023460 Figure S3D) VW CHANGED GENOTYPE TO INCLUDE pil1 delta background. sey1 deleta is impled PMID:32023460 (Figure 4 S4B). PMID:32023460 (Figure 4 S4B). PMID:32023460 (Figure 4 S4B). PMID:32023460 increased cortical ER remodeling dynamics PMID:32023460 increased cortical ER remodeling dynamics PMID:32023460 the cortical tubular ER pattern changes slower than wild type PMID:32023460 (Figure 4 S4B). PMID:32023460 resulting in the formation of fewer punctate eisosomes (Figure S1B). PMID:32023460 decreased Pil1 protein abundance Figure S1F PMID:32023460 cortical PMID:32023460 Pil1 lacking the C terminus failed to interact with Scs2 (Figure S5F PMID:32023460 (Figure 4 S4B). PMID:32023460 (Figure S1F). increased Pil1 phosphorylation was detected in these cells PMID:32023460 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 (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 fig2 the cortical tubular ER pattern changes faster than wild type PMID:32023460 fig2 increased cortical ER remodeling dynamics PMID:32023460 the cortical tubular ER pattern changes slower than wild type PMID:32023460 fig2 increased cortical ER remodeling dynamics PMID:32023460 (Fig- ure S5G). the cortical tubular ER pattern changes faster than wild type PMID:32023460 (Figure 3A) the cortical tubular ER pattern changes slower than wild type PMID:32023460 (Figure S3C). the cortical tubular ER pattern changes slower than wild type PMID:32023460 the cortical tubular ER pattern changes slower than wild type PMID:32023460 increased cortical ER remodeling dynamics the cortical tubular ER pattern changes faster than wild type PMID:32023460 (Figure 3A) decreased cortical ER remodeling dynamics the cortical tubular ER pattern changes slower than wild type PMID:32023460 (Figure S1F). Pil1 mis-assembled into fewer and longer filaments PMID:32032353 S.p. wtf13 assayed; doesn't specify which isoform (or if it's both) PMID:32032353 inferred from crosses involving hemizygous diploids PMID:32032353 assayed by expressing S.k. ortholog in S.p. PMID:32032353 assayed by expressing S.k. ortholog in S.p. PMID:32032353 assayed by expressing S.k. ortholog in S.p. PMID:32032353 inferred from crosses involving hemizygous diploids PMID:32032353 S.p. wtf13 assayed; doesn't specify which isoform (or if it's both) PMID:32032353 Both wtf21 alleles were found at equal frequency in the viable spores. PMID:32047038 (Fig. 5H) This defect in UV-resistance can be rescued by wild-type SpCsn2, but not its IP6 binding-deficient K70E mutant . PMID:32047038 (Fig. 5H) This defect in UV-resistance can be rescued by wild-type SpCsn2, but not its IP6 binding-deficient K70E mutant . PMID:32047038 (Fig. 5H) This defect in UV-resistance can be rescued by wild-type SpCsn2, but not its IP6 binding-deficient K70E mutant . PMID:32047038 (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:32053662 6bc PMID:32053662 6bc PMID:32053662 6d PMID:32053662 6bc PMID:32053662 figure5 a-c PMID:32053662 figure5 a-c PMID:32053662 figure5 a-c PMID:32053662 figure5 a-c PMID:32053662 6d PMID:32053662 6d PMID:32053662 6bc PMID:32053662 6bc PMID:32053662 figure5 a-c PMID:32053662 figure5 a-c PMID:32053662 figure5 a-c PMID:32053662 figure5 a-c PMID:32062975 fig 6B PMID:32062975 Figure 6A PMID:32062975 Figure 6A PMID:32062975 Figure 6A PMID:32071154 vw: changed from slow growth (6hr) PMID:32071154 polysome profile PMID:32071154 fig 2B PMID:32071154 figure 2C PMID:32071154 fig4 PMID:32071154 fig 4 PMID:32071154 fig4 PMID:32071154 fig 4 PMID:32071154 fig 5C PMID:32071154 fig 5C PMID:32071154 fig 5C PMID:32071154 fig 5C PMID:32071154 Fig 6a PMID:32071154 Fig 6a PMID:32071154 Fig 6a PMID:32071154 Fig 6a PMID:32071154 Figure 6E PMID:32071154 Figure 6E PMID:32071154 figure 6F PMID:32071154 figure 6F PMID:32071154 Fig 7 PMID:32071154 Fig 7 PMID:32071154 Fig 7 PMID:32071154 Fig 7 PMID:32071154 Fig 7B PMID:32071154 Fig 7B PMID:32071154 Fig 7B PMID:32071154 Fig 7B PMID:32071154 polysome profile PMID:32071154 fig 4 PMID:32071154 fig 4 PMID:32071154 fig 4 PMID:32075773 Figure 1B PMID:32075773 fig2B S2B-D PMID:32075773 Fig S2 PMID:32075773 fig 4D PMID:32075773 Fig S2 PMID:32075773 fig 4D PMID:32075773 Fig S2 PMID:32075773 fig2B S2B-D PMID:32075773 fig2B S2B-D PMID:32075773 fig 3D) Lack of Mas5 abolishes both PAC formation and the assembly of stress granules. PMID:32075773 fig2B S2B-D PMID:32075773 Fig S2 PMID:32075773 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 Fig S2A PMID:32075773 fig2B S2B-D PMID:32075773 fig2B S2B-D PMID:32075773 fig2B S2B-D PMID:32075773 Figure 1B. PMID:32084401 cdc13HPM mutant can localise to SPB in mitosis PMID:32084401 Fig2A cells are unable to enter mitosis in absence of cdc13+ expression-no septated cells PMID:32084401 Fig2A cells expressing only cdc13HPM are unable to form colonies PMID:32084401 cdc13HPM mutant fails to localise to the SPB during G2 PMID:32084401 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 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 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 Fig S1D cdc13+ and cdc13HPM are not differentially sensitive to rum1. S phase same in both strains in absence of rum1 PMID:32084401 Fig 2G when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced PMID:32084401 Fig 2G when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced PMID:32084401 Fig 2G when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced PMID:32084401 FIGURE S1E Wee1-dependent CDK-Y15 phosphorylation was similar between Cdc13HPM-CDK and Cdc13WT-CDK PMID:32084401 Fig2H cdc13HPM localisation to SPB in mitosis is dependent on plo1 activity PMID:32084401 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 Fig1B cells blocked in G1 by nitrogen starvation and released in presence of nitrogen into S phase with cdc13+ switched off PMID:32084401 Fig 2G when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced PMID:32084401 Fig2H cdc13HPM localisation to SPB in mitosis is dependent on plo1 activity PMID:32084401 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 Fig 2G when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced PMID:32084401 Fig 2G when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced PMID:32101481 Figure 6, A and B PMID:32101481 Indeed, the percentage of tip septa was significantly reduced in mid1Δ pom1as1 cdc15-22D cells (Figure 4G). PMID:32101481 Figure 6E PMID:32101481 Figure 6D Indeed, deleting components of the CR scaffolded by Cdc15 (e.g., pxl1 or fic1) suppressed tip septation in mid1Δ pom1as1cells to a similar degree as cdc15-22D (Figure 6, D and E). PMID:32101481 Figure 1A and 1B PMID:32101481 Figure 2D PMID:32101481 (Figure 2, C and PMID:32101481 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 Figure 6, A and B PMID:32101481 4B? PMID:32101481 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:32101745 figure 3A/B PMID:32101745 figure 3A PMID:32101745 Figure S5 However, the truncation did not reduce Iss1 interaction with Rrp6 PMID:32101745 figure 3E PMID:32101745 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 figure 3F PMID:32101745 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 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 fig 4g & S4. /Figure 5A) PMID:32101745 fig 4g & S4. /Figure 5A) PMID:32101745 Figure 5B the iss1-DC mutation significantly reduced H3K9me2 at both ssm4 and mei4). PMID:32101745 Figure 5F the iss1-DC truncation did disrupt its interaction with Mmi1. PMID:32101745 Figure 5B the iss1-DC mutation significantly reduced H3K9me2 at both ssm4 and mei4). PMID:32142608 plate-based screen PMID:32142608 spot assay PMID:32142608 spot assay PMID:32142608 Phosphorylated during growth in media containing heavy water. PMID:32142608 plate-based screen PMID:32142608 spot assay PMID:32142608 spot assay PMID:32142608 plate-based screen, spot assay PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 plate-based screen, spot assay PMID:32142608 plate-based screen PMID:32142608 plate-based screen, spot assay PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 plate-based screen, spot assay PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 plate-based screen, spot assay PMID:32142608 plate-based screen, spot assay PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 spot assay PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 spot assay PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 spot assay PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 spot assay PMID:32142608 spot assay PMID:32142608 plate-based screen PMID:32142608 plate-based screen PMID:32142608 plate-based screen, spot assay PMID:32142608 spot assay PMID:32168916 Figure 3 & S4(ALSO TFIIH but not sure which sunbunit) PMID:32168916 Figure S4 PMID:32168916 Figure S4 PMID:32168916 fig3 PMID:32168916 fig3 PMID:32168916 Figure 4 SAP155K700E restopred splicing to prp10-1 PMID:32168916 Figure 3 & S4(ALSO TFIIH but not sure which sunbunit) PMID:32168916 Figure S4 PMID:32168916 Figure S4 PMID:32168916 Figure 4 (ALSO TFIIH but not sure which sunbunit) PMID:32168916 Figure 4 (ALSO TFIIH but not sure which sunbunit) PMID:32204793 Figure 1—figure supplement 1A; spot test PMID:32204793 Figure 7—figure supplement 1B; spot test PMID:32204793 Figure 1—figure supplement 1A, Figure 7C,D, Figure 7—figure supplement 1A; spot test and survival assay PMID:32204793 Figure 7—figure supplement 1B; spot test PMID:32204793 Figure 5B, Figure 5—figure supplement 1C PMID:32204793 Figure 7—figure supplement 1B; spot test PMID:32204793 Figure 7C,D; spot test and survival assay PMID:32204793 Figure 7C,D; spot test and survival assay PMID:32204793 Figure 7C,D; spot test and survival assay PMID:32204793 Figure 1D, Figure 1—figure supplement 1; spot test and survival assay PMID:32204793 Figure 1D, Figure 1—figure supplement 1; spot test and survival assay PMID:32204793 Figure 6—figure supplement 1 PMID:32204793 Figure 5B, Figure 5—figure supplement 1C PMID:32204793 Figure 7A,B; spot test and survival assay PMID:32204793 Figure 5B, Figure 5—figure supplement 1C PMID:32204793 Figure 6—figure supplement 1 PMID:32204793 Figure 5B, Figure 5—figure supplement 1C PMID:32204793 Figure 7A,B; spot test and survival assay PMID:32204793 Figure 7A,B; spot test and survival assay PMID:32204793 actually inferred from combination of in vitro assay and phenotypes; Figures 1 & 5, including supplements PMID:32204793 actually inferred from combination of in vitro assay and phenotypes; Figures 1 & 5, including supplements PMID:32204793 in complex with Sfr1; Figure 6 PMID:32204793 in complex with Swi5; Figure 6 PMID:32204793 Figure 1—figure supplement 1A; spot test PMID:32269268 "25 degrees C; using ""low temperature"" to distinguish from 30 degrees C; Fig 1" PMID:32269268 Fig 5 PMID:32269268 Fig 5 PMID:32269268 Fig 2 PMID:32269268 Fig 4 PMID:32269268 Fig 5 PMID:32269268 Fig 1 PMID:32269268 Fig 1 PMID:32269268 "25 degrees C; using ""low temperature"" to distinguish from 30 degrees C; Fig 1" PMID:32269268 Fig 1 PMID:32269268 Fig S2 PMID:32269268 Fig 5 PMID:32269268 Fig 1 PMID:32269268 "25 degrees C; using ""low temperature"" to distinguish from 30 degrees C; Fig 1" PMID:32269268 Fig 2, S1 PMID:32269268 Fig 1 PMID:32269268 Fig 1 PMID:32269268 "25 degrees C; using ""low temperature"" to distinguish from 30 degrees C; Fig 1" PMID:32269268 Fig 1 PMID:32269268 Fig 1 PMID:32269268 Fig 1 PMID:32269268 Fig 4 PMID:32277274 fig2 PMID:32277274 figb PMID:32277274 figa PMID:32282918 Figure 10 PMID:32282918 Figure 1 PMID:32282918 Figure 1 PMID:32282918 Figure 1 PMID:32282918 Figure 1 PMID:32282918 Figure 1 PMID:32282918 Figure 1 PMID:32282918 Figure 1 PMID:32282918 Figure 1 PMID:32282918 Figure 1 PMID:32282918 Figure 1 PMID:32282918 Figure 1 PMID:32282918 Figure 1 PMID:32282918 Figure 2 PMID:32282918 Figure 2 PMID:32282918 Figure 2 PMID:32282918 Figure 2 PMID:32282918 Figure 2 PMID:32282918 Figure 2 PMID:32282918 Figure 2 PMID:32282918 Figure 3A PMID:32282918 Figure 3A and 9C PMID:32282918 Figure 3A PMID:32282918 Figure 3B & Figure 10 PMID:32282918 Figure 3B Figure 10 PMID:32282918 Figure 3B PMID:32282918 Figure 3B PMID:32282918 Figure 3B PMID:32282918 Figure 3B PMID:32282918 Figure 3B PMID:32282918 Figure 3B PMID:32282918 Figure 5A PMID:32282918 Figure 5A PMID:32282918 Figure 5A PMID:32282918 Figure 5A PMID:32282918 Figure 5A PMID:32282918 Figure 5A PMID:32282918 Figure 5A PMID:32282918 Figure 5A PMID:32282918 Figure 5A PMID:32282918 Figure 5A PMID:32282918 Figure 5A PMID:32282918 Figure 5B PMID:32282918 Figure 5B PMID:32282918 Figure 5B PMID:32282918 Figure 5B PMID:32282918 Figure 5B PMID:32282918 Figure 6B PMID:32282918 Figure 6B PMID:32282918 Figure 6B PMID:32282918 Figure 6B PMID:32282918 Figure 6B PMID:32282918 Figure 6A PMID:32282918 Figure 6A PMID:32282918 Figure 6A PMID:32282918 Figure 6A PMID:32282918 Figure 6A PMID:32282918 Figure 6B PMID:32282918 Figure 6B PMID:32282918 Figure 6B PMID:32282918 Figure 6B PMID:32282918 Figure 6B PMID:32282918 Figure 7A PMID:32282918 Figure 7A, pin∆ rescues the lethality of aps1∆ asp1-H397A PMID:32282918 Figure 7B PMID:32282918 Figure 7A PMID:32282918 Figure 7A PMID:32282918 Figure 7A PMID:32282918 Figure 7A PMID:32282918 Figure 8A PMID:32282918 Figure 8A PMID:32282918 Figure 8A PMID:32282918 Figure 8A PMID:32282918 Figure 8A PMID:32282918 Figure 8B PMID:32282918 Figure 8B PMID:32282918 Figure 8B PMID:32282918 Figure 1 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure 8B PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 PMID:32282918 Figure S7 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PMID:32295063 compared to lsd1-ao single mutant PMID:32295063 KΔ::ade6+ monitored by qRT-PCR PMID:32295063 compared to Lsd1-ao single mutant PMID:32319721 CFU counts PMID:32320462 Sterols do not accumulate in endosomes after treatement with CK-666 PMID:32320462 Sterols do not accumulate in endosomes PMID:32320462 Eisosomes protruding towards cell interior PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor; internal structures PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Evaluated with D4H sterol sensor PMID:32320462 Sterols accumulate in endosomes PMID:32320462 Sterols do not accumulate in endosomes after treatement with CK-666 PMID:32327557 Fig. 2 PMID:32327557 Fig. 2 PMID:32327557 Fig. 2 PMID:32327557 Fig. 2 PMID:32327557 Fig. 2 PMID:32327557 Fig. 3 PMID:32327557 Fig. 3 PMID:32327557 Fig. 3 PMID:32327557 Fig. 3 PMID:32327557 Fig. 3 PMID:32327557 Fig. 3 PMID:32327557 Fig. 3 PMID:32327557 Fig. 3 PMID:32327557 Fig. 3 PMID:32327557 Fig. 3 PMID:32327557 Fig. 3 PMID:32327557 Fig. 4 PMID:32327557 Fig. 4 PMID:32327557 Fig. 4 PMID:32327557 Small rescue of cut7D pkl1D PMID:32327557 5ug/mL PMID:32327557 Fig. 2 PMID:32341083 HU absent PMID:32341083 HU absent PMID:32341083 HU absent PMID:32341083 HU absent PMID:32355220 ade6B/ade6X at cen1 PMID:32355220 ade6B/ade6X at cen1 PMID:32355220 ade6B/ade6X at cen1 PMID:32355220 ade6B/ade6X at cen1 PMID:32355220 ade6B/ade6X at cen1 PMID:32355220 ade6B/ade6X at the ura4 locus PMID:32355220 ade6B/ade6X at the ura4 locus PMID:32355220 An extrachromosome ChLC PMID:32355220 ade6B/ade6X at the ura4 locus PMID:32355220 ade6B/ade6X at the ura4 locus PMID:32355220 PFGE; An extrachromosome ChLC PMID:32355220 PFGE; An extrachromosome ChLC PMID:32355220 ade6B/ade6X at cen1 PMID:32355220 PFGE; An extrachromosome ChLC PMID:32355220 ade6B/ade6X at cen1 PMID:32355220 ade6B/ade6X at cen1 PMID:32355220 ade6B/ade6X at cen1 PMID:32355220 An extrachromosome ChLC PMID:32355220 An extrachromosome ChLC PMID:32355220 An extrachromosome ChLC PMID:32355220 ade6B/ade6X at cen1 PMID:32355220 An extrachromosome ChLC PMID:32355220 An extrachromosome ChLC PMID:32355220 ade6B/ade6X at the ura4 locus PMID:32355220 An extrachromosome ChLC PMID:32355220 An extrachromosome ChLC PMID:32355220 An extrachromosome ChLC PMID:32355220 ade6B/ade6X at cen1 PMID:32355220 ade6B/ade6X at cen1 PMID:32355220 PFGE; An extrachromosome ChLC PMID:32355220 PFGE; An extrachromosome ChLC PMID:32355220 An extrachromosome ChLC PMID:32355220 An extrachromosome ChLC PMID:32355220 An extrachromosome ChLC PMID:32355220 An extrachromosome ChLC PMID:32355220 An extrachromosome ChLC PMID:32355220 ade6B/ade6X at the ura4 locus PMID:32355220 An extrachromosome ChLC PMID:32355220 ade6B/ade6X at the ura4 locus PMID:32355220 An extrachromosome ChLC PMID:32355220 ade6B/ade6X at cen1 PMID:32355220 An extrachromosome ChLC PMID:32355220 ade6B/ade6X at cen1 PMID:32355220 An extrachromosome ChLC PMID:32355220 ade6B/ade6X at the ura4 locus PMID:32355220 ade6B/ade6X at cen1 PMID:32361273 fig1 PMID:32361273 fig S2 B PMID:32361273 fig 2E, S2A PMID:32361273 fig 2D length is 10.299 micron cf WT 12.7 in same conditions PMID:32361273 fig 2D length is 7.5 micron cf WT 6.2 in same conditions PMID:32361273 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 fig 2 PMID:32361273 fig 2 PMID:32361273 fig 1C (i.e normal TOR signalloing) PMID:32361273 fig S1A PMID:32361273 fig S1A PMID:32361273 fig1 PMID:32361273 fig1 PMID:32361273 Delay in the dephosphoryaltion of Ste9 and defect in the degradation of the cyclin Cdc13 in nitrogen starvation PMID:32361273 fig7A PMID:32361273 2G. the use of cdc10 mutant backgrounds is common for checking the ability of cells to arrest in G1 PMID:32361273 1D. The cells also presented a defect in the degradation of the cyclin Cdc13 and a delay in the dephosphorylation of Ste9 PMID:32361273 fig1 PMID:32361273 fig 7 PMID:32361273 protein phophatase substrate adaptor PMID:32361273 (TAP-Par1F314Q), this interaction was reduced (Figure 6C) PMID:32361273 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 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 fig 4 Notably, loss of cig1 and cig2 utterly overrode these defects, PMID:32361273 fig 2 PMID:32361273 Figure S4D PMID:32361273 Figure S4D PMID:32361273 Figure S4D PMID:32361273 fig 2F PMID:32361273 fig3 PMID:32361273 fig 3 PMID:32361273 fig 2F PMID:32361273 fig3b PMID:32361273 fig3 PMID:32361273 deletion mutants of either ste9 or rum1 fail to degrade Cdc13 (Figures S4A and S4B). PMID:32361273 deletion mutants of either ste9 or rum1 fail to degrade Cdc13 (Figures S4A and S4B). PMID:32361273 Figure S4D PMID:32414915 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 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:32441227 Overexpression of Mal3 (1-241 Q89E) fragmentary mutant using the nmt1 promoter PMID:32441227 using the nmt1 promoter PMID:32441227 using the nmt1 promoter PMID:32441227 using the nmt1 promoter PMID:32441227 using the nmt1 promoter PMID:32441227 using the nmt1 promoter PMID:32441227 using the nmt1 promoter PMID:32441227 using the nmt1 promoter PMID:32441227 using the nmt1 promoter PMID:32441227 using the nmt1 promoter PMID:32441227 using the nmt1 promoter PMID:32441227 Overexpession of Mal3(1-241) fragment using the nmt1 promoter PMID:32441227 Overexpession of Mal3(Q89R) mutant using the nmt1 promoter PMID:32441227 overexpression of Mal3(1-241) fragment using the nmt1 promoter PMID:32441227 Overexpression of Mal3 (135-241) fragment using the nmt1 promoter PMID:32441227 Overexpression of Mal3 (135-241) fragment using the nmt1 promoter PMID:32441227 Overexpression of Mal3 (135-308) fragment using the nmt1 promoter PMID:32441227 Overexpression of Mal3 (135-308) fragment using the nmt1 promoter PMID:32441227 Overexpression of Mal3 (135-308) fragment using the nmt1 promoter PMID:32441227 overexpression of Mal3(Q89R) mutant using the nmt1 promoter PMID:32441227 Overexpression of Mal3(1-241) fragment using the nmt1 promoter PMID:32441227 Overexpression of Mal3(Q89R) mutant using the nmt1 promoter PMID:32441227 wild type under the nmt1 promoter PMID:32441227 wild type under the nmt41 promoter PMID:32441227 using the nmt1 promoter PMID:32441227 Overexpression of Mal3 (1-197) fragment using the nmt1 promoter PMID:32441227 Overexpression of Mal3 (135-308) fragment using the nmt1 promoter PMID:32441227 Overexpression of Mal3 (135-241) fragment using the nmt1 promoter PMID:32441227 Overexpression of Mal3 (Q89E) mutant using the nmt1 promoter PMID:32441227 Overexpression of Mal3 (1-241 Q89E) fragmentary mutant using the nmt1 promoter PMID:32441227 using the nmt1 promoter PMID:32441227 using the nmt1 promoter PMID:32441227 Overexpression of Mal3(1-241) fragment using the nmt1 promoter PMID:32441227 Overexpression of Mal3 (1-241 Q89E) fragmentary mutant using the nmt1 promoter PMID:32441227 Overexpression of Mal3 (Q89E) mutant using the nmt1 promoter PMID:32441227 Overexpression of Mal3 (Q89E) mutant using the nmt1 promoter PMID:32441227 Overexpression of Mal3 (Q89E) mutant using the nmt1 promoter PMID:32441227 Overexpression of Mal3(Q89R) mutant using the nmt1 promoter PMID:32441227 overexpression of Mal3(Q89R) mutant using the nmt1 promoter PMID:32441227 Overexpession of Mal3(Q89R) mutant using the nmt1 promoter PMID:32441227 Overexpression of Mal3 (135-241) fragment using the nmt1 promoter PMID:32441227 overexpression of Mal3(1-241) fragment using the nmt1 promoter PMID:32441227 Overexpession of Mal3(1-241) fragment using the nmt1 promoter PMID:32441227 wild type under the nmt41 promoter PMID:32441227 Overexpression of Mal3 (1-197) fragment using the nmt1 promoter PMID:32441227 Overexpression of Mal3 (1-197) fragment using the nmt1 promoter PMID:32441227 Overexpression of Mal3 (1-197) fragment using the nmt1 promoter PMID:32441227 wild type under the nmt1 promoter PMID:32441227 wild type under the nmt1 promoter PMID:32441227 wild type under the nmt1 promoter PMID:32441227 wild type under the nmt1 promoter; DAPI staining PMID:32441227 Overexpression of Mal3 (1-241 Q89E) fragmentary mutant using the nmt1 promoter PMID:32441227 decreased cell population viability under overexpession of Mal3(1-241) fragment using the nmt1 promoter PMID:32441227 decreased cell population viability under overexpession of Mal3(Q89R) fragment using the nmt1 promoter PMID:32496538 Figure 6 and Supplementary Fig S8 PMID:32496538 Strand-specific RT-qPCR; Figure 2 PMID:32496538 Strand-specific RT-qPCR; Figure 2 PMID:32496538 Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5 PMID:32496538 Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5 PMID:32496538 Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5 PMID:32496538 Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5 PMID:32496538 Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5 PMID:32496538 Figure 6 and Supplementary Fig S8 PMID:32496538 Supplementary Fig S7 PMID:32496538 Supplementary Fig S8 PMID:32496538 Figure 6 and Supplementary Fig S8 PMID:32496538 Supplementary Fig S7 PMID:32496538 Supplementary Fig S8 PMID:32496538 Supplementary Fig S7 PMID:32496538 Supplementary Fig S7 PMID:32496538 Supplementary Fig S7 PMID:32496538 Supplementary Fig S7 PMID:32496538 Figure 5; rbp1 also Figure 7 PMID:32496538 Figure 5; rbp1 also Figure 7 PMID:32496538 Figure 5; rbp1 also Figure 7 PMID:32496538 Figure 5; rbp1 also Figure 7 PMID:32496538 Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5 PMID:32496538 Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5 PMID:32496538 Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5 PMID:32496538 Strand-specific RT-qPCR; Figure 4 and Supplementary Fig S5 PMID:32496538 Supplementary Fig S8 PMID:32496538 Strand-specific RNA-seq analysis, RT-PCR, Strand-specific RT-qPCR; Figure 1, 2 and 4; Supplementary Fig S1, S3 and S5 PMID:32496538 Strand-specific RNA-seq analysis, RT-PCR, Strand-specific RT-qPCR; Figure 1, 2 and 4; Supplementary Fig S1, S3 and S5 PMID:32496538 Strand-specific RNA-seq analysis, RT-PCR, Strand-specific RT-qPCR; Figure 1, 2 and 4; Supplementary Fig S1, S3 and S5 PMID:32496538 Strand-specific RT-qPCR; Figure 2 PMID:32496538 Strand-specific RT-qPCR; Figure 2 PMID:32496538 Strand-specific RT-qPCR; Figure 2 PMID:32496538 Figure 5 PMID:32496538 Figure 5 PMID:32496538 Strand-specific RT-qPCR; Figure 2 PMID:32499400 at lncRNAs upstream of PHO regulon genes (nc-tgp1, nc-pho1, prt1) PMID:32499400 also assayed genome-wide PMID:32499400 100 ug/mL MPA PMID:32499400 EMM -U agar plates, supplemeted with 6AU concentration ranging from 3.6 to 150 ug/mL PMID:32499400 also assayed genome-wide PMID:32499400 at tgp1 promoter PMID:32499400 at different lncRNA polyadenylation sites PMID:32499400 at lncRNAs upstream of PHO regulon genes (nc-tgp1, nc-pho1, prt1) PMID:32499408 Figure 1B-E and supplementary Figure S1B PMID:32499408 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 Figure 3 PMID:32499408 Figure 2E PMID:32499408 Figure 1B-E and supplementary Figure S1B PMID:32499408 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 Figure 7A PMID:32499408 fig 5e PMID:32499408 Figure 1B-E and supplementary Figure S1B PMID:32499408 Figure 1B-E and supplementary Figure S1B PMID:32499408 Figure 3 PMID:32499408 Figure 1B-E and supplementary Figure S1B PMID:32499408 Figure 1B-E and supplementary Figure S1B PMID:32499408 It is noteworthy that the amount of Arb1 was also drastically decreased in hsp90-G84C cells at high temperatures (Figure 4E) PMID:32499408 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 Figure 1B-E and supplementary Figure S1B PMID:32499408 (Figure 4B) PMID:32502403 ase1D cells that elongated the spindle, the MMD was not properly formed, and the number of NPCs was variable (Figure S2B PMID:32502403 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 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 The coalescence of daughter nuclei was also observed in apq12D cells that failed to undergo nuclear division (Figure 4F). PMID:32502403 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:32502403 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 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 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 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 Figure 1A PMID:32502403 ase1D cells that elongated the spindle, the MMD was not properly formed, and the number of NPCs was variable (Figure S2B PMID:32502403 Consistently, these cells showed a higher fre- quency of asymmetric NE divisions (Figure S2C) PMID:32502403 causally upstreasm of? PMID:32518066 We conclude that the carboxy-terminal 12 amino acids of Lsm1 are important for the binding specificity of Lsm1–7. PMID:32518066 These data indicate that high affinity binding sites for the Lsm1–7 complex must be at the 3′ termini of RNA. On PMID:32518066 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 Figure 4B PMID:32546512 Figure 4B PMID:32546512 (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 (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 Figure 4 PMID:32546512 Figure 4 PMID:32546512 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 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 Figure 4 PMID:32546512 Figure 4 PMID:32546512 Figure 2B PMID:32546512 Figure 4 PMID:32546512 Figure 4 PMID:32546512 Figure 4 PMID:32546512 Figure 5 PMID:32546512 Figure 2C PMID:32546512 Figure 2B PMID:32546512 Figure 4 PMID:32546512 Figure 2 vw changed from decreased to normal (compared to WT) PMID:32546512 Figure 2 vw changed from decreased to normal (compared to WT) PMID:32546512 Northern blotting, Figure 6 PMID:32546512 Figure 2C PMID:32546512 Figure S1 PMID:32546512 Figure 4 PMID:32546512 Figure S1 PMID:32546512 Figure S1 PMID:32546512 Figure S1 PMID:32546512 Figure 8 PMID:32546512 Figure 8 PMID:32546512 Figure 8 PMID:32546512 Figure 8 PMID:32546512 Figure S1 PMID:32546512 Figure 2A PMID:32546512 Figure 2A PMID:32546512 Figure 2 PMID:32546512 Northern blotting and primer extension, Figure 6 PMID:32546512 Figure 5 PMID:32546512 Figure 5 PMID:32546512 Figure 5 PMID:32546512 Figure 5 PMID:32546512 Figure S1 PMID:32546512 Figure S1 PMID:32546512 Figure S1 PMID:32546512 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 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 Figure S1 PMID:32546512 Figure S1 PMID:32546512 Figure 5 PMID:32546512 Figure 5 PMID:32546512 Figure S1 PMID:32546512 Figure S1 PMID:32546512 Figure 2 PMID:32546512 Figure S1 PMID:32546512 Figure S1 PMID:32546512 Figure 4 PMID:32546512 Figure 4 PMID:32546512 Figure 4 PMID:32546512 Figure 5 PMID:32546512 Figure 4B PMID:32546512 Figure 4B PMID:32546512 Figure 4B PMID:32546512 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 Figure 4B PMID:32546512 Figure 8 PMID:32546512 Figure 5 PMID:32546512 Figure S1 PMID:32546512 Figure 5 PMID:32546512 Figure 5 PMID:32546512 Figure S1 PMID:32546512 Figure 4 PMID:32546512 Figure 2A PMID:32546512 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 suggest ... Erh1 acts as a brake on Mmi1’s ability to promote CPF-de- pendent termination during prt lncRNA synthesis. PMID:32546830 Figure 2 PMID:32546830 linker PMID:32546830 Figure 2E tetrad analysis PMID:32571823 figure3C PMID:32571823 figure 2 PMID:32571823 figure 2 PMID:32571823 figure 2 PMID:32571823 figure 2 PMID:32571823 figure 2 PMID:32571823 figure 2 PMID:32571823 figure 2 PMID:32571823 figure 2 PMID:32571823 figure 1 PMID:32571823 figure 1 PMID:32571823 figure 2 PMID:32571823 figure 2 PMID:32571823 figure 2 PMID:32571823 figure 2 PMID:32571823 figure 2 PMID:32571823 figure 2 PMID:32571823 figure 2 PMID:32571823 figure 2c PMID:32571823 figure 2d PMID:32571823 figure 2d PMID:32571823 figure 2d PMID:32571823 figure 2d PMID:32571823 figure 2d PMID:32571823 figure 2d PMID:32571823 figure 2d PMID:32571823 figure 2d PMID:32571823 figure 2d PMID:32571823 figure 2d PMID:32571823 figure3A (increased cacineurin signalling) PMID:32571823 figure3B PMID:32571823 figure3D PMID:32571823 FIG 4 Ccr1 is a molecular target of TAM. PMID:32571823 figure 1 PMID:32571823 figure 2b PMID:32571823 figure 2b PMID:32571823 fig5 PMID:32594847 DNS PMID:32594847 DNS PMID:32594847 DNS PMID:32650974 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:32650974 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 M-Pol I complex PMID:32650974 M-Pol I complex PMID:32650974 swollen PMID:32650974 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 split YFP and affinity capture PMID:32692737 regulates pathway choice PMID:32723864 Figure 7 PMID:32723864 Figure 7 PMID:32723864 Figure 7 PMID:32723864 Figure 7 PMID:32723864 Figure 7 PMID:32723864 Ase1 is required for promoting spindle elongation during mitotic prophase but synergizes with Klp2 to maintain spindle stability during metaphase I. PMID:32723864 Ase1 is required for promoting spindle elongation during mitotic prophase but synergizes with Klp2 to maintain spindle stability during metaphase I. PMID:32723864 Figure 6 PMID:32723864 Figure 6 PMID:32723864 Figure 6 PMID:32723864 Ase1 is required for promoting spindle elongation during mitotic prophase but synergizes with Klp2 to maintain spindle stability during metaphase I. PMID:32723864 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 Figure 5 PMID:32723864 Figure 5 PMID:32723864 Figure 5 PMID:32723864 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 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 In both mitotic and meiotic cells, the absence of Klp2 slightly but significantly prolonged the duration of preanaphase (Fig. 2, F and G). PMID:32723864 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 Figure S1. PMID:32723864 Figure S1. PMID:32723864 Figure S1. PMID:32723864 Figure S1. In contrast, 50% of the spindles in klp2D cells underwent abrupt collapse during metaphase I (Fig. 2, A, C, and E, 3A) PMID:32735772 Fig. S1B PMID:32735772 Fig 3 PMID:32735772 Figure 2B, 2G, 2H PMID:32735772 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 Figure S1E nitrogen starvation-induced ER-phagy appeared to be normal in epr1D PMID:32735772 Figure S1E PMID:32735772 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 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 (Figure 3D) As expected, in cells lacking both Scs2 and Scs22, Epr1 became diffusely distributed in the cytoplasm PMID:32735772 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 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 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 Figure 2a PMID:32735772 Figure 1C PMID:32735772 Figure 1C PMID:32735772 ER- autophagosome anchor requested https://github.com/geneontology/go-ontology/issues/19873 PMID:32735772 Figure 1C PMID:32735772 Mutating the FFAT motif or the AIM abolished the ability of Epr1-C to rescue epr1D (Figures 4A, 4B, and S3D). PMID:32735772 Mutating the FFAT motif or the AIM abolished the ability of Epr1-C to rescue epr1D (Figures 4A, 4B, and S3D). PMID:32735772 Fig. S1B PMID:32735772 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 Fig. S1B PMID:32735772 Figure 6A PMID:32735772 Figure 6A PMID:32735772 Remarkably, Epr1-C, but not Epr1-N, could completely rescue the defects of epr1D in DTT-induced ER- phagy PMID:32735772 fig 6b PMID:32735772 Figure 6A PMID:32735772 fig 6b PMID:32735772 Figure 7E the ER-phagy defect of ire1D was largely rescued (Figure 7E). PMID:32735772 figure 3D PMID:32735772 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 Figure 3C Epr1 interacted with both Scs2 and Scs22 in the Y2H assay PMID:32735772 Figures 1B and S1C PMID:32735772 Figures 2G and 2H PMID:32735772 Figure 2a PMID:32735772 Figures 1B and S1C PMID:32735772 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 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 Figure 3D ******check with DAN, is this an overexpression allele? PMID:32735772 Figure 6A PMID:32735772 Figure 6A PMID:32735772 Figure 6A PMID:32735772 Figure 6A PMID:32735772 ER- autophagosome anchor requested https://github.com/geneontology/go-ontology/issues/19873 PMID:32735772 (Figure 5A) reduced in scs2D and abolished in scs2D scs22D PMID:32735772 (Figure 5A) reduced in scs2D and abolished in scs2D scs22D PMID:32735772 (Figure S6B), indicating that Ire1 is dispensable for DTT-induced bulk autophagy but is essential for DTT-induced ER-phagy. PMID:32790622 viable spore yield assay; 16% of the surviving spores had inherited two copies of chromosome 3 and were thus aneuploid/diploid. PMID:32790622 viable spore yield assay PMID:32790622 viable spore yield assay PMID:32790622 viable spore yield assay; 30% of the surviving spores had inherited the two centromere 3-linked markers suggesting they are aneuploid/diploid. PMID:32790622 viable spore yield assay PMID:32790622 viable spore yield assay; 20% of the surviving spores had inherited the two centromere 3-linked markers suggesting they are aneuploid/diploid. PMID:32790622 viable spore yield assay PMID:32817556 Phenotype is greatly enhanced by mutation of the IR-R boundary element PMID:32841241 CCU codon/AGG anticodon tRNA PMID:32841241 CCU codon/AGG anticodon tRNA PMID:32841241 UAC codon/GUA anticodon tRNA PMID:32841241 CCU codon/AGG anticodon tRNA PMID:32841241 UAC codon/GUA anticodon tRNA PMID:32841241 UAC codon/GUA anticodon tRNA PMID:32841241 CCU codon/AGG anticodon tRNA PMID:32841241 UAC codon/GUA anticodon tRNA PMID:32841241 CCU codon/AGG anticodon tRNA PMID:32841241 UAC codon/GUA anticodon tRNA PMID:32841241 CCU codon/AGG anticodon tRNA PMID:32841241 UAC codon/GUA anticodon tRNA PMID:32841241 ACU codon/AGU anticodon tRNA PMID:32848252 fig 4/6 PMID:32848252 Fig. 3a, Extended Data Fig. 4a–c Removed from nuclear basket in bridge midzone during nuclear division PMID:32848252 fig 3b PMID:32848252 causally upstream? PMID:32848252 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 extended fig4 PMID:32848252 Extended Data Figure 8 PMID:32848252 fig 3g PMID:32848252 Fig. 4, Extended Data Fig. 7 PMID:32848252 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 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 extended data 6 c,d PMID:32848252 Fig. 3a, Extended Data Fig. 4a–c Removed from nuclear basket in bridge midzone during nuclear division PMID:32848252 Extended Data Figure 2 (nucleoplasmic side) PMID:32848252 lem2 (which encodes Lem2, the binding partner of Cmp7) is also SL with les1 PMID:32848252 Fig. 3a, Extended Data Fig. 4a–c Removed from nuclear basket in bridge midzone during nuclear division PMID:32848252 fig 4/6 PMID:32848252 Fig. 3a, Extended Data Fig. 4a–c Removed from nuclear basket in bridge midzone during nuclear division PMID:32878942 Fig. S3A PMID:32878942 Fig 3D PMID:32878942 Fig 3D PMID:32878942 Figure 2D&E PMID:32878942 Figure 2F-H PMID:32878942 Figure 2I (vw changed tp FYPO:0002559) PMID:32878942 Fig S3B&C PMID:32878942 Fig S3B&C PMID:32878942 Fig S3F PMID:32878942 Fig S3F&G PMID:32878942 Fig S3B,C,&D PMID:32878942 Fig 4D,E&F PMID:32878942 Fig S3E PMID:32878942 Fig S3E PMID:32878942 Fig S3E PMID:32878942 Fig S3E PMID:32878942 Fig 4H&I and S3F&G PMID:32878942 Fig 4H&I and S3F&G PMID:32878942 fig4 PMID:32878942 Fig. S3A PMID:32878942 Fig. S3A PMID:32878942 Fig. S3A PMID:32878942 Fig 3D PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototroph deletion library. PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 Data from screening of prototroph deletion library PMID:32896087 Liquid media growth assay. Mutant isolated from deletion collection. PMID:32896087 Liquid media growth assay. Mutant isolated from deletion collection. PMID:32896087 Liquid media growth assay. Mutant isolated from deletion collection. PMID:32896087 Liquid media growth assay. Mutant isolated from deletion collection. PMID:32896087 Liquid media growth assay. Mutant isolated from deletion collection. PMID:32896087 arg3-GFP fusion localisation in minimal media (EMM) PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 solid media screen using prototrophic deletion library PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32896087 EMM media with arginine PMID:32908306 Cup1-GFP immunofluorescence PMID:32909946 Fig 1 a PMID:32909946 Fig 1a PMID:32909946 Figure 1C). Such a band was not observed for D193A and T208A mutants, confirming that they are indeed kinase dead ( PMID:32909946 in vitro autophosphorylation activity of Atg1 from atg11D mutant was almost undetectable (Figure 1D PMID:32909946 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:32915139 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 fig1 SuppF PMID:32915139 fig 5b PMID:32915139 25% PMID:32915139 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 Figure 1C PMID:32915139 fig1 SuppF PMID:32915139 fig1 SuppF PMID:32915139 fig 3a PMID:32915139 fig3c PMID:32915139 fig 4d PMID:32915139 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 fig 3a PMID:32915139 fig3b PMID:32915139 Overexpression under the control of B-estradiol promoter (vw: I added an allele synonym, later these will be searchable and visible) PMID:32915139 (Figure 2—figure supplement 5). ngs formed and constricted correctly in >85% of sty1D cells (Figure 2D). PMID:32915139 Figure 2A and C) check, has synonym increased stability (better than increased length?) PMID:32915139 figure 5B PMID:32915139 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 fig2-supp1 PMID:32915139 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 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 Figure 5—figure supplement 4 PMID:32915139 Figure 5—figure supplement 4 PMID:32915139 Figure 1C PMID:32915139 Figure 1C PMID:32915139 replaces wt annotation PMID:32915139 replaces wt annotation PMID:32915139 fi1 supp5 PMID:32915139 fig 5b PMID:32915139 cells lacking Sty1 grew in these low LatA concentrations (Figure 1B). PMID:32915139 fig 1F PMID:32915139 50% PMID:32915139 fig 5c PMID:32915139 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:33010152 Fig. 8 PMID:33010152 Fig. 6 PMID:33010152 Fig. 6 PMID:33010152 Fig. 6 PMID:33010152 Fig. 6 PMID:33010152 Fig. 6 PMID:33010152 Fig. 6 PMID:33010152 Fig. 6 PMID:33010152 Fig. 6 PMID:33010152 Fig. 6 PMID:33010152 Fig. 6 PMID:33010152 Fig. 6 PMID:33010152 Fig. 6 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 5 PMID:33010152 Fig. 8 PMID:33010152 Fig. 8 PMID:33010152 Fig. 4 PMID:33010152 Fig. 4 PMID:33010152 Fig. 4 PMID:33010152 Fig. 4 PMID:33010152 Fig. 4 PMID:33010152 Fig. 4 PMID:33010152 Fig. 4 PMID:33010152 Fig. 4 PMID:33010152 Fig. 4 PMID:33010152 Fig. 4 PMID:33010152 Fig. 3 PMID:33010152 Fig. 8 PMID:33010152 Fig. 8 PMID:33010152 Fig. 8 PMID:33010152 Fig. 8 PMID:33010152 Fig. 4 PMID:33010152 Fig. 4 PMID:33010152 Fig. 4 PMID:33010152 Fig. 4 PMID:33010152 Fig. 4 PMID:33010152 Fig. 4 PMID:33010152 Fig. 8 PMID:33010152 Fig. 8 PMID:33010152 Fig. 8 PMID:33010152 Fig. 1, Fig. 8 PMID:33010152 Fig. 1 PMID:33010152 Fig. 1 PMID:33010152 Fig. 1 PMID:33010152 Fig. 1 PMID:33010152 Fig. 1 PMID:33010152 Fig. 1 PMID:33010152 Fig. 1 PMID:33010152 Fig. 4 PMID:33010152 Fig. 1 PMID:33049028 fig4 PMID:33049028 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 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 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 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:33108274 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 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 Fig. 4B PMID:33109728 Fig. 4B PMID:33109728 Fig. 4B PMID:33109728 Fig. 4B PMID:33109728 Fig. 4B PMID:33109728 Fig. 4B PMID:33109728 Fig. 4B PMID:33109728 Fig. 4B PMID:33109728 Fig. 4B PMID:33109728 Fig. 4B PMID:33125111 (Fig. 3). PMID:33125111 (Fig. 1C). PMID:33125111 (Fig. 1B). decreasing slows after 6 hours PMID:33125111 (Fig. 1A). PMID:33125111 (Fig. 3). PMID:33125111 (Fig. 1C). PMID:33131769 *****(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 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 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 fig1c PMID:33137119 fig 6b PMID:33137119 fig 6b PMID:33137119 pREP81-gad8-K263C PMID:33137119 fig2 PMID:33137119 pREP81-gad8-Q298L fig 5a PMID:33137119 pREP81-gad8-Q298L fig6D PMID:33137119 pREP81-gad8-Q298L PMID:33137119 Fig3A. affecting substrate Fkh2 in vitro PMID:33137119 affecting substrate Fkh2 in vitro PMID:33137119 affecting Gad8-S546 phosphorylation PMID:33137119 affecting Gad8-S546 phosphorylation PMID:33137119 affecting Gad8-S546 phosphorylation PMID:33137119 Following release from campthotecin PMID:33137119 fig 3B PMID:33137119 pREP81-gad8-K263C PMID:33137119 pREP81-gad8-T260C fig2 PMID:33137119 affecting substrate Fkh2 in vitro PMID:33137119 pREP81-gad8-K263C PMID:33137119 pREP81-gad8-K263C figure 2 PMID:33137119 pREP81-gad8-T260C. fig1a PMID:33137119 7B. PMID:33137119 fig 6c dominent negative effect PMID:33137119 fig 6c L fig6D PMID:33137119 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 (S5A Fig) PMID:33137119 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 Fig3C. we found that Gad8-K263C is phosphorylated at T387 in Δtor1 cells under normal or low-glucose growth conditions. PMID:33137119 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 Fig3A. affecting substrate Fkh2 in vitro PMID:33137119 fig 3b PMID:33137119 fig 3b PMID:33137119 figure 3d. I CHANGED THIS ONE< IS IT CORRECT? PMID:33137119 pREP81-gad8-T260C fig 2B PMID:33137119 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 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 Fig3A. affecting substrate Fkh2 in vitro PMID:33137119 Fig3C. we found that Gad8-K263C is phosphorylated at T387 in Δtor1 cells under normal or low-glucose growth conditions. PMID:33137119 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 fig1c PMID:33137119 affecting substrate Fkh2 in vitro PMID:33137119 pREP81-gad8-T260C fig1a PMID:33137119 affecting substrate Fkh2 in vitro PMID:33137119 pREP81-gad8-T260C fig 2B PMID:33138913 check genotype. ***********figure 3c PMID:33138913 fig3 supp1b&c PMID:33138913 figure 4B Atg43 lacking the 20 C-terminal aa exhibited only a partial defect in mitophagy, PMID:33138913 fig 4c PMID:33138913 figure 4G PMID:33138913 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 MIM complex (requrested) PMID:33138913 This raises the possibility that the MIM complex assists Atg43 through facilitating its mitochondrial localization. PMID:33138913 This raises the possibility that the MIM complex assists Atg43 through facilitating its mitochondrial localization. PMID:33138913 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 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 Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—figure supplement 1I) PMID:33138913 Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—figure supplement 1I) PMID:33138913 Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—figure supplement 1I) PMID:33138913 Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—figure supplement 1I) PMID:33138913 Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—figure supplement 1I) PMID:33138913 Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—figure supplement 1I) PMID:33138913 Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—figure supplement 1I) PMID:33138913 Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—figure supplement 1I) PMID:33138913 This raises the possibility that the MIM complex assists Atg43 through facilitating its mitochondrial localization. PMID:33138913 This raises the possibility that the MIM complex assists Atg43 through facilitating its mitochondrial localization. PMID:33138913 figure 6B,D PMID:33138913 figure 6B PMID:33138913 figure 6B PMID:33138913 By contrast, the atg7D and atg43DAIM mutants did not exhibit such an increased in superoxide (Figure 7D) PMID:33138913 By contrast, the atg7D and atg43DAIM mutants did not exhibit such an increased in superoxide (Figure 7D) PMID:33138913 whereas Atg43 with a truncation of the 60 C-terminal aa was defective in mitophagy (Figure 4B) PMID:33138913 figure 4B PMID:33138913 fig 4D PMID:33138913 fig 4D PMID:33138913 fig 3K PMID:33138913 fig 3i PMID:33138913 figure 3I PMID:33138913 fig 3H PMID:33138913 fig 3H PMID:33138913 fig 3H PMID:33138913 figure 3D PMID:33138913 figure 3D PMID:33138913 figure 3D PMID:33138913 fig 3b/4b PMID:33138913 fig 3b PMID:33138913 fig 2. PMID:33138913 fig1 PMID:33138913 fig1 PMID:33138913 fig1a PMID:33138913 Consistent with this, mitophagy was impaired in the mim1D and mim2D mutants (Figure 5D) PMID:33138913 Fig- ure 5—figure supplement 1F PMID:33138913 In the absence of Mim1 or Mim2, the GFP-Atg43 signal at the mitochondria was severely decreased (Figure 5C PMID:33138913 Consistent with this, mitophagy was impaired in the mim1D and mim2D mutants (Figure 5D) PMID:33138913 In the absence of Mim1 or Mim2, the GFP-Atg43 signal at the mitochondria was severely decreased (Figure 5C PMID:33138913 Fig- ure 5—figure supplement 1F PMID:33138913 2A PMID:33138913 fig1D PMID:33138913 fig1 PMID:33138913 figure 2F, 2G, 2H PMID:33138913 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:33153481 Fig.S2; G2 arrested cells by cdc2-asM17 PMID:33153481 Fig.2,3,S4; Hi-C, G2 arrested cells by cdc2-asM17 PMID:33153481 Fig.4,S5; G2 arrested cells by cdc2-asM17 PMID:33153481 Fig.6e; 3D quantification of DAPI stained DNA, G2 arrested cells by cdc2-asM17, + Thiolutin PMID:33153481 Fig. 6b-d; Rad52 foci quantification, G2 arrested cells by cdc2-asM17 PMID:33153481 Fig. 6b-d; Rad52 foci quantification, G2 arrested cells by cdc2-asM17, + Thiolutin PMID:33153481 Fig. 6b-d; Rad52 foci quantification, G2 arrested cells by cdc2-asM17, + Thiolutin PMID:33153481 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:33159083 also assayed using ChIP to detect Rts1 binding to Npp106 PMID:33159083 also assayed using ChIP to detect Rts1 binding to Npp106 PMID:33159083 also assayed using ChIP to detect Rts1 binding to Npp106 PMID:33159083 also assayed using ChIP to detect Rts1 binding to Npp106 PMID:33159083 also assayed using ChIP to detect Rts1 binding to Npp106 PMID:33159083 also assayed using ChIP to detect Rts1 binding to Npp106 PMID:33159083 also assayed using ChIP to detect Rts1 binding to Npp106 PMID:33159083 also assayed using ChIP to detect Rts1 binding to Npp106 PMID:33159083 also assayed using ChIP to detect Rts1 binding to Npp106 PMID:33159083 FISH; same as nup132delta alone PMID:33159083 FISH PMID:33159083 pmt3-D81R pmt3-KallR PMID:33159083 also assayed using ChIP to detect Rts1 binding to Npp106 PMID:33159083 also assayed using ChIP to detect Rts1 binding to Npp106 PMID:33159083 also assayed using ChIP to detect Rts1 binding to Npp106 PMID:33159083 also assayed using ChIP to detect Rts1 binding to Npp106 PMID:33159083 also assayed using ChIP to detect Rts1 binding to Npp106 PMID:33172987 Figure S1 PMID:33172987 Fig. 1D-E PMID:33172987 (Fig. 1F-G PMID:33172987 Figure 3A PMID:33172987 Figure 4E-F PMID:33172987 Figure S2 PMID:33172987 Figure S2 PMID:33172987 Figure S2 PMID:33172987 Figure S1 PMID:33172987 Figure S1 PMID:33172987 Figure S1 PMID:33172987 Figure S2 PMID:33172987 Figure S2 PMID:33172987 Figure S3 PMID:33172987 Figure S3 PMID:33172987 Figure 3 PMID:33172987 Opy1 PH1 (aa1-128) can directly bind phospholipids in vitro Figure 1 PMID:33172987 I changed the function annotation to this process annotation because it precisely negates the SGD annotation PMID:33172987 Figure1C (requested normal membrane lipid binding) PMID:33172987 Figure 1C PMID:33172987 PH1 domain Fig. 2A, Table S2 PMID:33172987 Figure S2 PMID:33172987 (Fig. S2B). PMID:33172987 THIS IS A GUESS I COULD NOT ACCESS THE SUPP SO ANNOTATED TO THE Snider ITS3-1 growth phenotype PMID:33172987 Figure S2 PMID:33172987 Figure S2 PMID:33172987 Figure S2 PMID:33172987 Figure S2 PMID:33172987 Figure S2 PMID:33172987 Figure S3 PMID:33176147 Figures 4E and 4F PMID:33176147 figS2A PMID:33176147 Figures 4E and 4F PMID:33176147 fig1E PMID:33176147 fig1E PMID:33176147 fig1E PMID:33176147 fig1F PMID:33176147 fig1F PMID:33176147 fig1F/figS2A PMID:33176147 fig1F PMID:33176147 fig 2A PMID:33176147 Figures 4E and 4F PMID:33176147 fig 2A PMID:33176147 figure 2c Figures 3B and S3B Figures 4C and 4D PMID:33176147 figure 2c Figures 3B and S3B Figures 4C and 4D PMID:33202882 intron 2 PMID:33225241 same as mas5delta alone PMID:33225241 background: Pyp1-GFP PMID:33225241 Background Sty1-GFP PMID:33225241 same as mas5delta alone PMID:33357436 Figure 3A PMID:33357436 In vitro binding assay with Cdc15 F-BAR domain and full length Pxl1 PMID:33357436 Figure 4F PMID:33357436 Figure S2B electron microscopy of purified Cdc15 F-BAR domain PMID:33357436 Figure S2C PMID:33357436 moved down from abnormal localization PMID:33357436 These results indicate that the Cdc15 F-BAR domain can position Cdc12 directly at the PM by binding membrane and Cdc12 simultaneously. PMID:33357436 Figure S2E PMID:33357436 additional cewlll. poles PMID:33357436 Figures 3C and 3D PMID:33357436 fig 2B in vitro binding assay with Cdc15 F-BAR domain and Cdc12 peptide aa20-40 PMID:33378674 at pericentromeric regions PMID:33378677 inferred from abolished interaction between Pof8 and Lsm subunits PMID:33378677 inferred from decreased interaction between Pof8 and Lsm subunits PMID:33378677 inferred from abolished interaction between Pof8 and Lsm subunits PMID:33386485 Background Rho1.C17R-mCherry PMID:33386485 background Hsp104-GFP and Rho1.C17R-mCherry PMID:33386485 background Hsp104-GFP and Rho1.C17R-mCherry PMID:33386485 background Hsp104-GFP and Rho1.C17R-mCherry PMID:33400299 transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j). PMID:33400299 Table1 PMID:33400299 Table1 PMID:33400299 transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j). PMID:33400299 transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j). PMID:33400299 transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j). PMID:33400299 transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j). PMID:33400299 transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j). PMID:33400299 transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j). PMID:33400299 transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j). PMID:33400299 transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j). PMID:33400299 transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j). PMID:33400299 Table1 PMID:33400299 figure 4b PMID:33400299 figure 4b PMID:33400299 figure 4b PMID:33400299 figure 4b PMID:33400299 figure 4b PMID:33400299 figure 4b PMID:33400299 figure 4b PMID:33400299 figure 4b PMID:33400299 figure 4b PMID:33400299 figure 4b PMID:33400299 figure 4b PMID:33400299 figure 4b PMID:33400299 3a glucose starve PMID:33400299 3a glucose starve PMID:33400299 3a glucose r excess PMID:33400299 Figure 2n PMID:33400299 Figure 2n PMID:33400299 Figure 2n PMID:33400299 (Figure 2k–m). PMID:33400299 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 Figure 1m PMID:33400299 Figure 1m PMID:33400299 transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j). PMID:33410907 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 Figure 2c (this replaces the sty1 WT annotation Should this be normal? i.e. normal for the conditions? ) PMID:33410907 6c PMID:33410907 These results suggested that, in addition to the binding to theRpb1-CTD, the isomerization activity was also required for the fu PMID:33410907 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 PHOSPHORYLATED CTD Following H2O2 stress, Pin1 bound phosphorylated CTD to promote Sty1 dissociation from it to facilitate oxidative stress induced transcription. PMID:33410907 Sty1 associated with Rpb1 in S. pombe as demonstrated by co-immunoprecipitation beforeH2O2 stress. This result suggested that the interaction between Sty1 andRpb1 did not require the activation of Sty1 PMID:33410907 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 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 As shown in Figure 3C and D, upon H2O2 stress, Rpb1 was recruited to the promoter and extensively phosphorylated at Ser5. PMID:33410907 Figure 4. Sty1 interacted and phosphorylated Rpb1-CTD at Ser5. PMID:33410907 fig? (under calf alkaline phosphatase treated) PMID:33410907 fig2a PMID:33410907 Figure 5 PMID:33410907 Figure 5 PMID:33410907 Figure 5e PMID:33410907 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 Figure 1 PMID:33410907 Figure 1 PMID:33410907 Figure 1 PMID:33410907 ( Figure 5D **I moved this from a WT phenotype) PMID:33410907 Figure 1C PMID:33410907 Figure 1C PMID:33410907 Figure 1C PMID:33410907 2B PMID:33410907 2B PMID:33410907 2B PMID:33410907 As shown in Figure 3C and D, upon H2O2 stress, Rpb1 was recruited to the promoter and extensively phosphorylated at Ser5. PMID:33410907 (is thsi |+h2os, check) the intracellular level of ROS was elevated in pin1 and ssu72 mutants (Figure 6H), PMID:33410907 (is this +H2o2, check) the intracellular level of ROS was elevated in pin1 and ssu72 mutants (Figure 6H), PMID:33410907 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 Figure 4. Sty1 interacted and phosphorylated Rpb1-CTD at Ser5. PMID:33410907 Figure 1 PMID:33410907 Figure 4. Sty1 interacted and phosphorylated Rpb1-CTD at Ser5. PMID:33410907 Figure 2c (this replaces the sty1 WT annotation Should this be normal? i.e. normal for the conditions? ) PMID:33410907 Figure 1 PMID:33419777 Fig 3I same in wild type background PMID:33419777 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 Fig3H same in wild type background PMID:33419777 Fig 3A-F same result in Wild type background PMID:33419777 Fig3A-F same result in wild type background PMID:33419777 Fig 2, Table 2 PMID:33419777 Fig5A PMID:33419777 Fig1A PMID:33419777 Fig1B, C Table 1 PMID:33419777 Fig1B, C Table 1 PMID:33419777 Fig1B, C Table 1 PMID:33419777 Fig1B, C Table 1 PMID:33419777 Fig4A. PMID:33419777 negative regulation (check relationship to membrane reassembly) PMID:33419777 Fig1B, C Table 1 PMID:33419777 Fig 2, Table 2 PMID:33419777 Fig5A PMID:33419777 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 Fig5C compare 7 and 9 When cdc2 is not tyrosine phosphorylation mga2 delta does not increase the cell size variability any further. PMID:33419777 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 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 FigS1. delayed septation, Cellular phenotype where cells initiate growth before septation has taken place, resulting in variable cell size at division. PMID:33419777 Fig4A PMID:33419777 Fig5C Table 3 PMID:33419777 Fig5 E,F abnormal protein localisation in multinucleated cells PMID:33419777 negative regulation (check relationship to membrane reassembly) PMID:33419777 Fig5A PMID:33434270 Figure. 6A PMID:33434270 Figure. 5A PMID:33468217 inferred from silencing and H3-K9 methylation phenotypes PMID:33468217 inferred from silencing and H3-K9 methylation phenotypes PMID:33483504 fig. 1b n=344 PMID:33483504 fig. 1a PMID:33483504 fig1 (cox4-GFP to label Mt) PMID:33483504 fig 4d though the expression levels of Mdm12 were comparable in WT and emr1Δ Cells PMID:33483504 fig 5 PMID:33483504 fig 1c PMID:33483504 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 integral 2a,b,c,d PMID:33483504 figure 3a PMID:33483504 figure 3a PMID:33483504 figure 3b PMID:33483504 fig. 3b PMID:33483504 fig 4 significantly decreased the number of Mdm12 (a constitutive component of the ERMES complex) foci PMID:33483504 fig. 3d PMID:33483504 er to mitochondria PMID:33483504 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 fig. 1b n=344 PMID:33496728 Figure 6 PMID:33496728 Figure 1 PMID:33496728 Figure S1 PMID:33496728 Figure S1 PMID:33496728 (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 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 Figure S3 PMID:33496728 Figure S3 PMID:33496728 Figure S3 PMID:33496728 Figure 5 PMID:33496728 Figure 5 PMID:33496728 Figure 1, Figure 5. +5 min, a 15-min delay compared with wild-type cells PMID:33496728 Figure 5 PMID:33496728 Figure 5 (VW: changed severity from high to low as this seems to partially rescue mid1-delta?) PMID:33496728 Figure 1E, F PMID:33496728 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 Figure S1 PMID:33496728 Figure S1 PMID:33496728 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 Figure 1A, B PMID:33496728 Figure 2 Figure 3 Figure 4 Figure S2 PMID:33496728 Figure 3 Figure 4 Figure S2 PMID:33496728 Figure 1 PMID:33506191 fig1 PMID:33506191 fig1 PMID:33506191 fig1 PMID:33506191 fig1 PMID:33506191 fig1 PMID:33506191 fig1 PMID:33506191 fig1 PMID:33506191 fig1 PMID:33506191 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 "fig4 If possible, please add the following comment - “The nucleus is retained in the center of the cell during mitosis.""" PMID:33506191 fig4 PMID:33506191 fig4 PMID:33506191 fig6 PMID:33506191 fig2 live cell imaging PMID:33506191 fig2 live cell imaging PMID:33506191 Fig7 PMID:33506191 fig1 PMID:33506191 fig1 PMID:33506191 fig1 PMID:33506191 fig1 PMID:33506191 fig1 PMID:33511417 genome-wide average; slightly increased amplitudes of the -2, -1, +1 nucleosome peaks (relative to NDR) PMID:33511417 genome-wide average PMID:33526714 figure 2 PMID:33526714 figure2 PMID:33526714 figure2 PMID:33526714 figure2 PMID:33526714 figure2 PMID:33526714 figure2 PMID:33526714 figure2 PMID:33526714 figure2 PMID:33526714 figure2 PMID:33526714 figure 2 PMID:33526714 figure2 PMID:33526714 figure2 PMID:33526714 figure2 PMID:33526714 figure2 PMID:33529549 Figure 1. Increased equational segregation in the sgo1∆ background. PMID:33529549 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 Decreased equational segregation in the diploid sgo1∆ rec12∆ background or the haploid sgo1∆ background. PMID:33529549 Figure 1. Increased equational segregation in sgo1∆ background. PMID:33529549 Anaphase A chromosome movement is completely abolished and only anaphase B chromosome movement occurs. PMID:33529549 Figure 1. Increased equational segregation in sgo1∆ background. PMID:33529549 ***** 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 The elevated frequency of sister centromere splitting in chiasma-lacking cells confirms that chiasmata prevent bi-oriented attachment of sister chromatids. PMID:33529549 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 FIgure 1. Decreased equational segregation in the sgo1∆ rec12∆ background or the haploid sgo1∆ background. PMID:33529549 Importantly, the dam1Δ mutation impaired disjunction of homologous chromosomes (figure 5a), as seen in mad2Δ and ark1-so mutants [25,52]. PMID:33534698 However, no GFP accumulation was detected in gcn2D cells under leucine starvation (Figure 4C), demonstrating that the autophagy induced by leucine starvation is dependent on the Gcn2 kinase. PMID:33534698 Figure 2a PMID:33534698 Moreover, S. pombe cells lacking Gcn3 (Figure 4D) or Fil1 (Figure 4F) displayed autophagy defects during leucine starvation. PMID:33534698 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 Figure 2a PMID:33534698 fig4a PMID:33534698 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 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 Autophagy in response to leucine starvation was abrogated by the gcn1D, but not gcn20D, mutation (Figure 4D), PMID:33534698 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 vw I edited to make the response the extension to GCN2 mediated signalling, but I hope to improve these GO terms. PMID:33534698 Figure 1, Supp 1 PMID:33534698 Figure 1, Supp 1 PMID:33534698 Figure 1, Supp 1 PMID:33534698 Figure 1, Supp 1 PMID:33534698 Figure 1, Supp 1 PMID:33534698 Figure 1, Supp 1 PMID:33534698 Figure 1, Supp 1 PMID:33534698 Figure 1 PMID:33534698 Figure 1 PMID:33534698 Figure 1 PMID:33534698 Figure 1 PMID:33534698 Figure 1 PMID:33534698 Figure 1 PMID:33534698 Figure 1 PMID:33534698 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 (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 Figure 2a PMID:33534698 Figure 2a PMID:33534698 (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 (Figure 3—figure supplement 3A), indicating that Arg854 of S. pombe Iml1 is not essential for the GATOR1 function. PMID:33534698 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 (Figure 3—figure supplement 2E,F and G), PMID:33534698 (Figure 3—figure supplement 2E,F and G), PMID:33534698 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 (Figure 3—figure supplement 1C–E). PMID:33534698 (Figure 3—figure supplement 1C–E). PMID:33534698 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 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 Figure 2a PMID:33534698 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 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 Figure 2a PMID:33534698 Figure 2b PMID:33534698 Figure 2b (any1 reescues) PMID:33534698 Figure 2b (any1 rescues) PMID:33534698 Figure 2e (sea3 rescued by gtr1 GDP-locked) PMID:33534698 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 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 Figure 2g PMID:33534698 Figure 2e (sea3 rescued by gtr1 GDP-locked) PMID:33534698 Figure 2f PMID:33534698 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 Moreover, the autophagy defect of the gcn2D mutant was complemented by TORC1 inactivation by the TORC1 inhibitors, rapamycin and caffeine (Figure 5B). PMID:33534698 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 (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 Figure 2a PMID:33534698 Figure 2a PMID:33534698 Figure 2a PMID:33536395 Fig. 3C PMID:33536395 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 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:33536395 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 changed from protein retention in ER lumen PMID:33536395 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 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 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 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 Fig. 3B PMID:33536434 GI Redundancy PMID:33568651 Polymerase usage sequencing PMID:33568651 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 Polymerase usage sequencing PMID:33568651 Polymerase usage sequencing PMID:33568651 replication dynamic analysis demonstrates that the priming strand is stable in the absence of Ku (previous work has shown resection is increased behind the arrested fork). Replication restart is slightly delayed, confirming previous work. Assayed by polymerase usage sequencing PMID:33574613 restores the MTREC and Rrp6 association with Mmi1 and Erh1 during meiosis (Fig. 5d). PMID:33574613 Fig 1 b (me2) PMID:33574613 Fig 1 b (1.5x) (me2) PMID:33574613 Extended data Fig 1 b c (also at MTREC independent islands) PMID:33574613 figure 1c PMID:33574613 figure 1e PMID:33574613 Fig 1 a PMID:33574613 The restoration of silencing required Pir1, as a loss of Ubi4 failed to silence ade6-DSR in pir1∆ cells (Fig. 3g). PMID:33574613 The restoration of silencing required Pir1, as a loss of Ubi4 failed to silence ade6-DSR in pir1∆ cells (Fig. 3g). PMID:33574613 the deletion of ubi4, ddb1 or cul4 restored ade6-DSR silencing (Fig. 3g and Extended Data Fig. 3d). PMID:33574613 the deletion of ubi4, ddb1 or cul4 restored ade6-DSR silencing (Fig. 3g and Extended Data Fig. 3d). PMID:33574613 the deletion of ubi4, ddb1 or cul4 restored ade6-DSR silencing (Fig. 3g and Extended Data Fig. 3d). PMID:33574613 which? PMID:33574613 which? PMID:33574613 The addition of ubi4∆, cul4∆ or ddb1∆ dramatically reduced Pir1 ubiquitination in tor2-ts6 mts2-1 cells (Fig. 3f). PMID:33574613 The addition of ubi4∆, cul4∆ or ddb1∆ dramatically reduced Pir1 ubiquitination in tor2-ts6 mts2-1 cells (Fig. 3f). PMID:33574613 The addition of ubi4∆, cul4∆ or ddb1∆ dramatically reduced Pir1 ubiquitination in tor2-ts6 mts2-1 cells (Fig. 3f). PMID:33574613 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 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 ubi4 gene, which encodes polyubiquitin implicated in sexual development34, was upregulate in tor2-ts6 cells (Fig. 3a). PMID:33574613 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 Consistently, ubiquitination of Pir1-SD in the tor2-ts6 mts2-1 mutant was reduced (Fig. 2e). PMID:33574613 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 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 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 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 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 abnormal asci containing fewer than four, or no, spores were frequently generated (Fig. 7c). PMID:33574613 Defective chromosome segregation and reduced spore viability were also noted (Fig. 7a and Supplementary Videos 1–3) PMID:33574613 Defective chromosome segregation and reduced spore viability were also noted (Fig. 7a and Supplementary Videos 1–3) PMID:33574613 cells showed impaired oscillation of chromosomes and a prolonged horsetail stage (approximately 160min compared with approximately 120min; Fig. 7a,b). PMID:33574613 Compared with the WT, cells expressing Pir1-SD showed a marked decrease in recombination frequency (Fig. 6f). PMID:33574613 Compared with the WT, cells expressing Pir1-SD showed a marked decrease in recombination frequency (Fig. 6f). PMID:33574613 Compared with the WT, cells expressing Pir1-SD showed a marked decrease in recombination frequency (Fig. 6f). PMID:33574613 Figure 6B DSBs; for example, rec25, rec27 and mug20), which are critical for recombination and proper chromosome segregation during meiosis-I4 PMID:33574613 Figure 6B DSBs; for example, rec25, rec27 and mug20), which are critical for recombination and proper chromosome segregation during meiosis-I4 PMID:33574613 Fig 1 a PMID:33574613 Fig. 1f,g PMID:33574613 figure 1h PMID:33574613 Moreover, ubiquitination of Pir1 was detected in tor2-ts6 cells and increased in the tor2-ts6 mts2-1 mutant (Fig. 1h) PMID:33574613 Fig 1 a PMID:33574613 Fig 1 a PMID:33574613 Extended Data Fig. 2a,c PMID:33574613 Figure 6B DSBs; for example, rec25, rec27 and mug20), which are critical for recombination and proper chromosome segregation during meiosis-I4 PMID:33574613 restores the MTREC and Rrp6 association with Mmi1 and Erh1 during meiosis (Fig. 5d). PMID:33574613 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 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 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 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 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 Fig 1 b (me2) PMID:33574613 Notably, Pir1 was depleted during early meiosis (Fig. 5a) but gradually recov- ered by middle meiosis. PMID:33574613 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 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 We indeed observed that pir1∆ cells exhibited a growth defect on minimal medium PMID:33574613 We indeed observed that pir1∆ cells exhibited a growth defect on minimal medium PMID:33574613 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:33579781 Fig. 5B PMID:33579781 Fig. 5B PMID:33579781 Fig. 5B PMID:33579781 Fig. 5B PMID:33579781 Fig. 5B PMID:33579781 Fig. 5A PMID:33579781 Fig. 4A PMID:33579781 Fig. 4A PMID:33579781 Fig. 4A PMID:33579781 Fig. 4A PMID:33579781 Fig. 4A PMID:33579781 Fig. 5B PMID:33579781 Fig. 5B PMID:33579781 Fig. 4A PMID:33579781 Fig. 5B PMID:33579781 Fig. 5B PMID:33579781 Fig. 5B PMID:33579781 Fig. 4A PMID:33579781 Fig. 4A PMID:33579781 Fig. 4A PMID:33579781 Fig. 2 PMID:33579781 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 Fig. 4A PMID:33579781 Fig. 4A PMID:33579781 Fig. 4A PMID:33579781 Fig. 4A PMID:33579781 Fig. 5B PMID:33579781 Fig. 5B PMID:33579781 Need to add modified version PMID:33579781 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 Fig. 4A PMID:33658433 vw:added nucleosome assembly PMID:33670267 TAP co-purification, Western blot for histone H3 PMID:33670267 ATPase assay PMID:33670267 ATPase assay PMID:33670267 TAP co-purification, Western blot for histone H3 PMID:33670267 ATPase assay PMID:33670267 TAP co-purification, Western blot for histone H3 PMID:33670267 TAP co-purification, Western blot for histone H3 PMID:33670267 ATPase assay PMID:33683349 figure 4 PMID:33683349 fig 6a PMID:33683349 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 fig 5 PMID:33683349 fig3 PMID:33683349 fig3 PMID:33683349 fig3 PMID:33683349 fig3 (i.e wee?) PMID:33683349 fig2 (30 degrees) wee1-50ts mik1D cells divide at a smaller size than wee1-50ts mik1D cig2D cells PMID:33683349 figure 6b PMID:33683349 fig 5a PMID:33683349 "fig1 &2 Nick suggested ""mitotic catastrophe""We would make this a related synonym?" PMID:33683349 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 figure 4 PMID:33711009 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 20° PMID:33711009 20° PMID:33711009 20° PMID:33711009 20° PMID:33711009 20° PMID:33711009 Neither the N-terminal segment from aa 1–496 nor the C-terminal fragment from 578–710 was able to bind to Dis2 or Swd22 in the 2-hybrid format (Fig 11A) PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 25ºC PMID:33723569 25ºC PMID:33723569 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 25ºC PMID:33723569 25ºC PMID:33723569 25ºC PMID:33723569 25ºC, live-cell imaging, cell length at septation PMID:33723569 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 25ºC PMID:33723569 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 32ºC PMID:33723569 32ºC PMID:33723569 32ºC PMID:33723569 32ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 32ºC PMID:33723569 32ºC PMID:33723569 32ºC PMID:33723569 32ºC PMID:33723569 32ºC PMID:33723569 25ºC, live-cell imaging, cell length at septation PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33723569 live-cell imaging, 25ºC PMID:33754639 temperature sensitive 37° PMID:33771877 fig 3 At exg1, ecm33, eng1 et gas1, condensin is redistributed throughout the gene body instead of accumulating around transcription termination sites. PMID:33771877 fig 1 PMID:33771877 Fig 2 PMID:33771877 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 fig 3 At exg1, ecm33, eng1 et gas1, condensin is redistributed throughout the gene body instead of accumulating around transcription termination sites. PMID:33771877 fig 3 At exg1, ecm33, eng1 et gas1, condensin is redistributed throughout the gene body instead of accumulating around transcription termination sites. PMID:33771877 Fig 2 PMID:33771877 Fig 2b PMID:33771877 fig 3 At exg1, ecm33, eng1 et gas1, condensin is redistributed throughout the gene body instead of accumulating around transcription termination sites. PMID:33771877 fig3. PMID:33771877 fig3. PMID:33771877 fig3. PMID:33771877 fig3. PMID:33771877 fig 1 PMID:33775921 highest overexpression level PMID:33788833 The mutant protein is observed at the vacuolar surface PMID:33788833 The mutant protein is observed at the vacuolar surface PMID:33788833 The mutant protein is observed at the vacuolar surface PMID:33788833 same as vps35delta alone PMID:33788833 The mutant protein is observed at the vacuolar surface PMID:33788833 Affecting Cps1 carboxypeptidase PMID:33788833 Affecting Cps1 carboxypeptidase PMID:33788833 Affecting Cps1 carboxypeptidase PMID:33788833 Affecting Cps1 carboxypeptidase PMID:33788833 same as fsv1delta alone PMID:33788833 The mutant protein is observed faintly at the vacuolar surface of a low percentage of cells PMID:33788833 The mutant protein is observed at the vacuolar surface PMID:33788833 The mutant protein is observed at the vacuolar surface PMID:33788833 The mutant protein is observed at the vacuolar surface PMID:33788833 The mutant protein is observed at the vacuolar surface PMID:33788833 The mutant protein is observed at the vacuolar surface PMID:33788833 The mutant protein is observed at the vacuolar surface PMID:33788833 co-localization with Cfr1 PMID:33788833 80 mM MgCl2 PMID:33788833 1.0 M KCl PMID:33788833 Affecting Cps1 carboxypeptidase PMID:33788833 Affecting Cps1 carboxypeptidase PMID:33788833 Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE PMID:33788833 Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE PMID:33788833 Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE PMID:33788833 Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE PMID:33788833 Affecting Vps10 and the PI(3) probe Cherry-FYVE PMID:33788833 The mutant protein is observed at the vacuolar surface PMID:33788833 The mutant protein is observed faintly at the vacuolar surface of a low percentage of cells PMID:33788833 same as vps35delta alone PMID:33788833 The mutant protein is observed at the vacuolar surface PMID:33788833 The mutant protein is observed at the vacuolar surface PMID:33788833 The mutant protein is observed faintly at the vacuolar surface of a low percentage of cells PMID:33788833 The mutant protein is observed at the vacuolar surface PMID:33788833 The mutant protein is observed at the vacuolar surface PMID:33788833 The mutant protein is observed faintly at the vacuolar surface of a low percentage of cells PMID:33788833 The mutant protein is observed at the vacuolar surface PMID:33788833 The mutant protein is observed at the vacuolar surface PMID:33788833 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 co-localization with Vps35 and with Vps27 PMID:33823663 figure9 PMID:33823663 DNS PMID:33823663 DNS PMID:33823663 figure 9 modified form is activated for sexual differentiation PMID:33825974 live cell imaging with 3D structured illumination microscopy (3D-SIM) PMID:33825974 live cell imaging with 3D structured illumination microscopy (3D-SIM) PMID:33825974 Figure 4d, 4e; Figure s3b; live cell imaging with 3D structured illumination microscopy (3D-SIM) PMID:33825974 live cell imaging with 3D structured illumination microscopy (3D-SIM) PMID:33825974 Figure s2 (c); live cell imaging with 3D structured illumination microscopy (3D-SIM) PMID:33825974 live cell imaging with 3D structured illumination microscopy (3D-SIM) PMID:33825974 live cell imaging with 3D structured illumination microscopy (3D-SIM) PMID:33836577 figure 1 PMID:33836577 figure 2 PMID:33836577 figure 2 requires phosphorylated T89, T154, T155 to bind Nbs1 FHA domain PMID:33836577 figure 2 PMID:33836577 figure 3B PMID:33836577 figure 3B PMID:33836577 figure 3B PMID:33836577 figure 3B PMID:33836577 figure 3B PMID:33836577 figure 3C PMID:33836577 figure 3C PMID:33836577 figure 3C PMID:33836577 figure 3C PMID:33836577 figure 3C PMID:33836577 figure 3D PMID:33836577 figure 3D PMID:33836577 figure 3D PMID:33836577 figure 3D PMID:33836577 figure 3D PMID:33836577 figure 3D PMID:33836577 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 figure 1 PMID:33836577 figure 1 PMID:33836577 figure 2D PMID:33836577 figure 2D PMID:33836577 figure 2E PMID:33836577 figure 2E PMID:33888556 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 Figure 2D PMID:33888556 Figure 2A cohesion protection defect PMID:33888556 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 Figure 3D. PMID:33888556 Figure 1B/C PMID:33888556 Figure 1C PMID:33888556 figure 4 PMID:33888556 To further examine this possibility, we reconstituted Rec8 dephosphorylation in vitro using immunoprecipitated Par1-containing PP2A complexes. PMID:33888556 To further examine this possibility, we reconstituted Rec8 dephosphorylation in vitro using immunoprecipitated Par1-containing PP2A complexes. PMID:33888556 figure 4 (no rescue by sgo3) PMID:33888556 Figure 1C PMID:33888556 Figure 1C PMID:33888556 figure 4 PMID:33888556 Figure 3D. phosphomimetic rec8 PMID:33888556 Figure 3D. PMID:33888556 Figure 3D. phosphomimetic rec8 PMID:33888556 Figure 1C PMID:33888556 Figure 1C PMID:33888556 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 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 Figure 3 PMID:33888556 Figure 1C PMID:33888556 Figure 2A PMID:33888556 Figure 2F PMID:33909078 alpha-1,2-galactosylation of O-linked glycan PMID:33909078 alpha-1,3-galactosylation of O-linked glycan PMID:33909078 alpha-1,3-galactosylation of O-linked glycan PMID:33909078 alpha-1,2-galactosylation of O-linked glycan PMID:33909078 alpha-1,2-galactosylation of N-linked glycan PMID:33909078 alpha-1,2-galactosylation of N-linked glycan PMID:33909078 alpha-1,2-galactosylation of N-linked glycan PMID:33909078 alpha-1,3-galactosylation of O-linked glycan PMID:33925026 same as alp14delta alone PMID:33925026 same as alp14delta alone PMID:33925026 same as alp14delta alone PMID:33925026 same as klp6delta alone PMID:33925026 same as klp6delta alone PMID:33925026 same as alp14delta alone PMID:33925026 reduced frequency of microtubule catastrophe PMID:33925026 reduced frequency of microtubule rescue PMID:33925026 same as alp14delta alone PMID:33925026 Assays were done in the MDR-sup (multi-drug resistance-suppressed) genetic background together with nda3-TB101 PMID:33946513 fig S4a PMID:33946513 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 Figure 2D PMID:33946513 Klp2 levels on spindle microtubules were significantly lower than those in cut7-22 (which are increased compared to WT) PMID:33946513 Figure 2A,B PMID:33946513 fig1 PMID:33946513 fig1a PMID:33946513 fig 1c dri1 supresses cut7 PMID:33946513 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 Figure 3A PMID:33946513 Figure 4a PMID:33946513 Klp2 levels on spindle microtubules were significantly lower than those in cut7-22 (which are increased compared to WT) PMID:33946513 to pac PMID:33946513 to pac PMID:33946513 Figure 2A,B PMID:33946513 Figure 2D PMID:33946513 Figure 3A PMID:33946513 Figure 3A PMID:33946513 to pac PMID:33946513 to pac PMID:33970532 to capture target of ecl1 PMID:33970532 only amino acid auxotrophic cell PMID:33970532 only amino acid auxotrophic cell PMID:33970532 only amino acid auxotrophic cell PMID:33970532 The control strain ED668 expressed ecl1+ when Mg2+ was depleted but not in a strain lacking fil1+ (Figure 2a) PMID:34010645 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 Figure 2 PMID:34010645 Figure 2. PMID:34010645 Figure 2. PMID:34019809 fix catalytic activity PMID:34019809 fix catalytic activity PMID:34019809 structure, fig2 PMID:34028542 fig6 PMID:34028542 fig 5 PMID:34028542 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 top panel, Fig. 6A; Fig. S3B,C). PMID:34028542 Cytoplasmic Ght5-GFP was observed within the vacuolar membrane stained with FM4-64. PMID:34028542 Fig1 aly3 rescues PMID:34028542 Proliferation defect of gad8ts aly1 mutant in low glucose was similar to that of gad8ts mutant. PMID:34028542 Proliferation defect of gad8ts aly2 mutant in low glucose was similar to that of gad8ts mutant. PMID:34028542 Proliferation defect of gad8ts rod1 mutant in low glucose was similar to that of gad8ts mutant. PMID:34028542 Proliferation defect of gad8ts mutant in low glucose was restored by SPCC584.15c deletion. PMID:34028542 fig6 PMID:34028542 although not shown directly , genetic interactions are consistent with this activity PMID:34028542 fig6 (phenocopies WT) PMID:34080538 Fig. 4 PMID:34080538 Fig. 4 PMID:34080538 Fig. 4 PMID:34080538 Fig. 4 PMID:34080538 Fig. 4 PMID:34080538 Fig. 4 PMID:34080538 Fig. 4 PMID:34080538 Fig. 4 PMID:34080538 Fig. 4 PMID:34080538 Fig. 5 PMID:34080538 Fig. 5 supp 3 PMID:34080538 Fig. 5 supp 3 PMID:34080538 Fig. 5 PMID:34080538 Fig. 5 PMID:34080538 Fig. 5 PMID:34080538 Fig. 4 PMID:34080538 Fig. 4 PMID:34080538 Fig. 4 PMID:34080538 Fig. 4 PMID:34080538 Fig. 5 - Dephosph form PMID:34080538 Fig. 5 - Dephosph form PMID:34080538 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 Fig. 4 PMID:34086083 YES, YES (low-glucose) PMID:34086083 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 YES, YES (low-glucose) PMID:34133210 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 Figure 4, A and B PMID:34133210 fig1 PMID:34133210 Cdk1 phosphorylation of Pxl1 reduced binding to the F-BAR domain of Cdc15 (Figure 5A), but not to Cdc15C (Figure 5B). PMID:34133210 although not IDA, there is experimental data to support this inference PMID:34133210 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 Constriction took longer in pxl1(9A) PMID:34169534 also assayed using Pil1 co-tethering with microscopy PMID:34169534 also assayed using Pil1 co-tethering with microscopy PMID:34209806 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 The interactions of the Nrl1(NRDE-2) and the Nrl1(C-term) domain constructs with Mtl1 were significantly lower PMID:34209806 Need to curate ref42 for earlier part of this story, but this can be. inferred here from the interactions PMID:34209806 i added as good to have multiple support. PMID:34209806 We observed similar intensities of interaction of the Nrl1(N-term) and the Nrl1(N-term + NRDE-2) constructs with Mtl1 (1511.2 89.4 or 1558.2 159.3 Miller units for the N-terminal region and the N-terminus with NRDE2 domain and Mtl1, respectively), PMID:34228709 equivalent substitution to cdc20-P287R PMID:34228709 DNA combing PMID:34228709 Cds1 is partially phosphorylated PMID:34228709 Chk1 is partially phosphorylated PMID:34228709 hypermutator PMID:34250083 Phenotype determined with robotics-based CFU assay. PMID:34250083 Phenotype determined with robotics-based CFU assay. PMID:34250083 Phenotype determined with robotics-based CFU assay. PMID:34250083 Phenotype determined with robotics-based CFU assay. PMID:34250083 Phenotype determined with robotics-based CFU assay. PMID:34250083 Phenotype determined with robotics-based CFU assay. PMID:34250083 Phenotype determined with robotics-based CFU assay. PMID:3428262 mitotic G2/M transition delay PMID:34292936 worse than rad51delta alone PMID:34292936 worse than rad51delta alone PMID:34296454 Please refer to Fig. 5E&F from paper for partial inhibition protein synthesis phenotype PMID:34296454 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 For the Torin1-resistant mutant, the phosphorylation levels remained constant throughout the time course PMID:34296454 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 For the Torin1-resistant mutant, the phosphorylation levels remained constant throughout the time course PMID:34309513 in vitro (Figure 4A, Video 1). PMID:34309513 in vitro (Figure 4A, Video 1). PMID:34309513 in vitro (Figure 4A, Video 1). PMID:34309513 in vitro (Figure 4A, Video 1). PMID:34309513 in vitro (Figure 4A, Video 1). PMID:34309513 in vitro (Figure 4A, Video 1). PMID:34346498 Figure 1 (see above) PMID:34346498 Figure 2F PMID:34346498 Figure 6B PMID:34346498 Figure 7 PMID:34346498 Figure 7 PMID:34346498 Figure 2F PMID:34346498 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 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 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 figure7 C PMID:34346498 decreased abnormal SPB-independent meiosis II PMID:34346498 Figure 2 PMID:34346498 Figure 3A PMID:34346498 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 Figure 1 PMID:34346498 Figure 1 (see above) PMID:34346498 Figure 2E PMID:34346498 Figure 2E PMID:34346498 Figure 3 PMID:34346498 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 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 Figure 2F PMID:34346498 figure 7C PMID:34346498 figure 7C PMID:34346498 late spindle elongation (move down /when GO reflect stages of meiotic spindle elongation) PMID:34352089 figure 1c PMID:34352089 MOVE DOWN PMID:34352089 MOVE DOWN PMID:34352089 5' extended precursors, C/C box (but not H/ACA box) PMID:34352089 Pac1 strain (Pac1-AA) that allowed rapid rapamycin-dependent nuclear exclusion of Pac1 (Figure 1B). PMID:34352089 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 waiting for GO:NEW.inferred from association with prremature termination sites PMID:34352089 Figure 3A and Supplementary Fig- ure S5A PMID:34352089 waiting for GO:NEW. We show this for only two mRNA: mfs2 and SPBC530.02. Can this be added in the annotation extension ? PMID:34352089 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 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 Supplementary Figure S5B PMID:34352089 Figure 3A and Supplementary Fig- ure S5A PMID:34352089 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 5' extended precursors, C/C box (but not H/ACA box) PMID:34382912 figure 2 PMID:34382912 fig 5 PMID:34382912 fig 5 PMID:34382912 fig 5 PMID:34382912 fig 5 PMID:34382912 fig 5 PMID:34382912 fig 5 PMID:34382912 fig4 PMID:34382912 fig4 PMID:34382912 fig4 PMID:34382996 figure5 PMID:34382996 no assembly of vesicles by electron microscopy (Because cell fu- sion completely fails when both partner cells lack fus1) PMID:34382996 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 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 figure5 PMID:34382996 Fig. 6 E and Fig. S4 D. By LM, Myo52 and Exo84 also showed strong signal reduction in fus1Δ . PMID:34382996 Stronger phenotype in h+ than h- cell PMID:34382996 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 Only when gpd1∆ is in h- cell PMID:34389684 Figue 1C PMID:34389684 Random spore analysis PMID:34389684 Fig 7A PMID:34389684 Fig 7A PMID:34389684 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 this can be inferred from the experiments PMID:34389684 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 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 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 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 Fig 7 compared to WT PMID:34389684 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 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 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 Figure 1c PMID:34389684 NorthernBlotting PMID:34389684 Random spore analysis PMID:34389684 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 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 (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 ..... while rhn1Δ rescued the cs growth defect of seb1-G476S at 20 °C PMID:34389684 Figue 3A Notable findings were that seb1-G476S rescued the ts growth defect of rhn1Δ at 37 °C...... PMID:34389684 The seb1-G476S and aps1Δ alleles were synthetically lethal; PMID:34389684 Random spore analysis PMID:34389684 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 Fig 7a PMID:34389684 Random spore analysis PMID:34389684 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 Random spore analysis (DNS) PMID:34389684 Random spore analysis PMID:34389684 Random spore analysis PMID:34389684 Random spore analysis (DNS) PMID:34389684 Figure 1A (vw changed to increased with low serverity as we compare to WT) PMID:34389684 similar to wt PMID:34389684 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 Random spore analysis PMID:34389684 compared to WT PMID:34389684 compared to WT PMID:34389684 compared to WT PMID:34389684 Fig 7 compared to WT PMID:34389684 Random spore analysis (DNS) PMID:34389684 Figure 1A PMID:34402513 Figure 2F PMID:34402513 Figure 4 PMID:34402513 Figure S3B-C PMID:34402513 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 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 Figure 2G However, mutation of 3 additional Cdk1 consensus sites abolished Imp2 phosphorylation by Cdk1 (Imp2-11A, Fig. 2C). PMID:34402513 Figure 2G, H PMID:34402513 Figure 2D PMID:34402513 Figure 4 PMID:34402513 Figure 4 PMID:34402513 Figure 4 PMID:34402513 Figure 3. Imp2-11A-mNG was recruited to the CR earlier (ca. 4 minutes) than Imp2-mNG (Fig. 3A, B, and C). PMID:34402513 Figure SA and C PMID:34402513 Figure S2D and F PMID:34402513 Figure S2D-E PMID:34402513 Figure S3B-C PMID:34402513 Figure S2D-E PMID:34402513 Figure S2D and F PMID:34402513 Figure S2A and C PMID:34402513 Figure 4 PMID:34402513 Figure 4 PMID:34402513 Figure 4 PMID:34402513 Figure 3 PMID:34402513 Figure 2E PMID:34402513 Figure S4B PMID:34402513 Figure S4A PMID:34402513 Figure S4A PMID:34402513 Figure S4A PMID:34402513 Figure S4A PMID:34402513 Figure S4B PMID:34402513 Figure S2F PMID:34402513 Figure S4B PMID:34402513 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 Figure S2A-B PMID:34402513 Figure S2A-B PMID:34402513 Figure S2A-B PMID:34402513 Figure S2A-B PMID:34402513 Figure S2D-E PMID:34402513 Figure 2G PMID:34402513 Figure 4A-B PMID:34402513 Figure 4A-B PMID:34402513 Figure 4A-B PMID:34402513 Figure S2D-E PMID:34402513 Figure S2A and C PMID:34402513 Figure S3B-C PMID:34402513 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 Figure S2A and C PMID:34402513 Figure S2A and C PMID:34402513 Figure S2A-B PMID:34402513 Figure S2A-C PMID:34402513 Figure 1A-C PMID:34402513 Figure 1A-C PMID:34402513 Figure 1A-C PMID:34402513 Figure 1A-C PMID:34402513 Figure 1A-C PMID:34402513 Figure 1A-C PMID:34402513 Figure 1A-C PMID:34402513 Figure 1A-C PMID:34402513 Figure 1A-C PMID:34402513 Figure 1A-C PMID:34402513 Figure 1A-C PMID:34402513 Figure 1A-C PMID:34402513 Figure 1A-C PMID:34402513 Figure 1A-C PMID:34402513 Figure 1A-C PMID:34402513 Figure 1A-C PMID:34402513 Figure 1A-C PMID:34402513 vw added extensions to link MF to BP & phase PMID:34402513 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 Figure S2A-B PMID:34402513 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 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 Figure S2C PMID:34402513 Figure S3B-C PMID:34402513 Figure 4 PMID:34460892 Evidence from RNA-seq data PMID:34460892 Evidence from RNA-seq data PMID:34460892 Evidence from RNA-seq data PMID:34460892 Evidence form RNA-seq data PMID:34460892 Evidence form RNA-seq data PMID:34460892 Evidence from RNA-seq data PMID:34460892 Evidence from RNA-seq data PMID:34460892 Evidence from RNA-seq data PMID:34460892 Evidence from RNA-seq data PMID:34460892 Evidence from RNA-seq data PMID:34460892 Evidence from RNA-seq data PMID:34460892 Evidence from RNA-seq data PMID:34460892 Evidence from RNA-seq data PMID:34460892 Evidence from RNA-seq data PMID:34460892 Evidence was from RNA-seq not from microarray PMID:34460892 Evidence code was RNA-seq PMID:34460892 Evidence from RNA-seq data PMID:34460892 Evidence from RNA-seq data PMID:34460892 Evidence from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence from RNA-seq data PMID:34460892 Evidence from RNA-seq data PMID:34460892 Evidence from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence was from RNA-seq data PMID:34460892 Evidence form RNA-seq data PMID:34460892 Evidence form RNA-seq data PMID:34460892 Evidence form RNA-seq data PMID:34460892 Evidence form RNA-seq data PMID:34460892 Evidence form RNA-seq data PMID:34460892 Evidence form RNA-seq data PMID:34460892 Evidence form RNA-seq data PMID:34460892 Evidence form RNA-seq data PMID:34460892 Evidence form RNA-seq data PMID:34460892 Evidence form RNA-seq data PMID:34464389 during stationary phase. Figure 6C In fact, the protein levels of Scw1 markedly decreased in ageing cells. PMID:34464389 Figure S7B The proportion of junctions down- stream of tlh2 was higher in the tlh2 overexpression strain compared to wild-type PMID:34464389 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 Fig 5A Given the increased lifespan of rnh1Δ rnh201Δ cells PMID:34464389 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 Figure S7C Moreover, the tlh2 overexpression strain was substantially shorter-lived than wild-type cells PMID:34464389 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 Figure 5A Cells lacking Sir2 showed a subtle extension of chronological lifespan compared to wild-type, especially at later timepoints PMID:34464389 Figure 4B Accordingly, our smFISH experiment showed that tlh2 was de-repressed in sir2 deletion cells PMID:3448096 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 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 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 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 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 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 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 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 Figure 2 PMID:34499159 Figure 1 PMID:34499159 Figure 5A PMID:34499159 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 Figure 3c PMID:34499159 Figure 4b PMID:34499159 Figure 3d PMID:34499159 Figure 3C PMID:34499159 Figure 3c PMID:34499159 Figure 4B PMID:34499159 Figure 5D These observations indicate that the mip1 mutation does not affect the TORC1-dependent phosphorylation of Sck1, Sck2 and Maf1. PMID:34499159 Figure 5E PMID:34499159 Figure 2 PMID:34499159 Figure 2 PMID:34499159 Figure 5A PMID:34499159 Figure S2B PMID:34499159 Figure 4B PMID:34499159 Figure 4c PMID:34524082 hht-ub14 substrate which both manifest a similar degree of strong stimulation by H3K14ub (Figure 1C, Figure 1—figure supplement 1E–H). PMID:34524082 Fig. 4E PMID:34524082 Fig. 4E PMID:34524082 Fig. 4E PMID:34524082 Fig. 4E PMID:34524082 Fig. 4D PMID:34524082 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 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 Fig. 4D PMID:34524082 Fig. 4A PMID:34524082 Fig. 4D PMID:34524082 Fig. 4D PMID:34524082 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 Fig. 4E REQUESTED ABOLISHED PMID:34524082 Fig. 4A PMID:34524082 Fig. 4D PMID:34524082 Figure 3F /fig1 PMID:34524082 Figure 3F /fig1 PMID:34524082 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:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34580178 figure 1B PMID:34608864 presence or absence of HU PMID:34608864 presence or absence of MMS PMID:34608864 presence or absence of MMS PMID:34608864 presence or absence of HU PMID:34608864 presence or absence of HU PMID:34608864 presence or absence of MMS PMID:34608864 presence or absence of HU PMID:34608864 in presence or absence of MMS PMID:34613787 We conclude that type II myosins contribute to both the assembly and disassembly of actin filaments in contractile rings. PMID:34613787 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 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 WHY ISNNT THIS PART. OF ????FYPO:0000230 abnormal actomyosin contractile ring actin filament organization PMID:34613787 WHY ISNNT THIS PART. OF ????FYPO:0000230 abnormal actomyosin contractile ring actin filament organization PMID:34613787 We conclude that type II myosins contribute to both the assembly and disassembly of actin filaments in contractile rings. PMID:34613787 We conclude that type II myosins contribute to both the assembly and disassembly of actin filaments in contractile rings. PMID:34613787 Figure 2B PMID:34613787 We conclude that type II myosins contribute to both the assembly and disassembly of actin filaments in contractile rings. PMID:34613787 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 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 Therefore, mature rings of the mutant had on average about 1.9 times as much actin as wild-type cells PMID:34613787 Figure 2B PMID:34613787 (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 (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 (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 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 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:34666001 figure 5 PMID:34666001 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 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 figure 5 PMID:34666001 figure 5 PMID:34666001 figure 5 PMID:34666001 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 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 figure 5 PMID:34666001 figure 5 PMID:34666001 figure 5 PMID:34666001 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 (vw: 25% cell death) PMID:34666001 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 figure 5 PMID:34666001 figure 5 PMID:34666001 figure 5 PMID:34666001 figure 5 PMID:34666001 figure 5 PMID:34666001 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 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 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 figure 5 PMID:34666001 figure 5 PMID:34666001 figure 5 PMID:34666001 figure 5 PMID:34666001 figure 5 PMID:34666001 figure 5 PMID:34666001 figure 5 PMID:34666001 figure 5 PMID:34666001 figure 5 PMID:34666001 figure 5 PMID:34674264 (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 in vivo phosphorylation sites identified by mass spectrometry PMID:34674264 Normal localization to medial cortical nodes, mitotic contractile ring, SPB, and septum as wildtype PMID:34674264 Normal localization to medial cortical nodes, SPB, and division septum as wildtype PMID:34674264 (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 Fig. 2B). Almost abolished Dma1 auto-ubiquitination by in vitro assay PMID:34674264 Decreased Dma1 auto-ubiquitination by in vitro assay PMID:34674264 in vitro assay PMID:34674264 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 Fig 4a PMID:34674264 Localization to SPBs at the same level as wildtype during spindle stress PMID:34674264 Localization to SPBs at the same level as wildtype during spindle stress PMID:34674264 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 Normal localization to medial cortical nodes, SPB, and division septum as wildtype PMID:34674264 in vivo phosphorylation site identified by mass spectrometry PMID:34674264 in vitro kinase assay showed S166 is phosphorylated by Cdk1 PMID:34674264 in vitro kinase assay showed S251 is phosphorylated by Plo1 PMID:34674264 in vitro kinase assay showed T18, S20, and S266 are phosphorylated by CK2 PMID:34674264 in vitro kinase assay showed T18, S20, and S266 are phosphorylated by CK2 PMID:34674264 in vitro kinase assay showed T18, S20, and S266 are phosphorylated by CK2 PMID:34674264 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:34686329 (Figure 6H) PMID:34686329 (figure 6F) PMID:34686329 RNA-seq PMID:34686329 Tti1 caused a strong decrease of Tti2 and Tel2 binding (Fig- ure 2J). PMID:34686329 (Figures S1E and S1F) PMID:34686329 (Figures S1E and S1F) PMID:34686329 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 Tel2 does not localize to the nucleus in standard growth conditions (Figure S2B). PMID:34686329 (Figure S2B). PMID:34686329 We conclude that Tti1, and to a lesser extent Tti2, re- cruits TTT to nascent Tra1 polypeptides PMID:34686329 Finally, our published tran- scriptomic analysis of tti2-CKO mutants showed that PIKK mRNA levels remain unaffected following Tti2 depletion (Fig- ureS1H) PMID:34686329 Finally, our published tran- scriptomic analysis of tti2-CKO mutants showed that PIKK mRNA levels remain unaffected following Tti2 depletion (Fig- ureS1H) PMID:34686329 We conclude that Tti1, and to a lesser extent Tti2, re- cruits TTT to nascent Tra1 polypeptides PMID:34686329 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 (Figures S1C and S1D). PMID:34686329 (Figure 3D) PMID:34686329 (Figures S1C and S1D). PMID:34686329 Depletion of each protein re- duces S. pombe viability and proliferation compared with control strains and culture conditions (Figures S1C and S1D). PMID:34686329 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 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 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 (Figure 3D) PMID:34686329 (Figure 3D) PMID:34686329 (Figure 3C) PMID:34686329 (Figure 3C) PMID:34686329 RNA-seq PMID:34686329 (Figure 6B) PMID:34686329 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 (Figure 2H) PMID:34686329 In contrast, Tti2 and Tti1 interaction with tra1+ does not change in the absence of Tel2 (Figure 2I), PMID:34686329 (Figure 6B) PMID:34686329 (Figure 6B) PMID:34686329 (Figure S1G) PMID:34686329 (Figure S1G) PMID:34686329 (Figure S1G) PMID:34686329 (Figure S1G) PMID:34686329 figure 6I PMID:34686329 figure 6I PMID:34686329 (Figure 7A) PMID:34686329 (Figure 7A) PMID:34686329 Abolished incorporation of Tra1 into SAGA complex PMID:34686329 Abolished incorporation of Tra1 into SAGA complex PMID:34686329 Abolished incorporation of Tra1 into SAGA complex PMID:34686329 Abolished incorporation of Tra1 into SAGA complex PMID:34686329 Abolished incorporation of Tra1 into SAGA complex PMID:34686329 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 (Figure 1A) PMID:34686329 (Figure 1A) PMID:34686329 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 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:34686329 (Figure S4C) PMID:34686329 (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 (Figure S4C) PMID:34686329 (Figure S5) PMID:34686329 (Figure 3C) PMID:34686329 (Figure S4C) PMID:34686329 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 (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 (Figures S1E and S1F) PMID:34686329 (Figures S1E and S1F) PMID:34686329 (Figure 6B) PMID:34686329 (Figure 6B) PMID:34686329 Figure 2C) Abolished interaction between Tti2 protein and tra1 mRNA PMID:34686329 (Figure 3E) PMID:34686329 (Figure 3E) PMID:34686329 (Figure 3E) PMID:34686329 Finally, our published tran- scriptomic analysis of tti2-CKO mutants showed that PIKK mRNA levels remain unaffected following Tti2 depletion (Fig- ureS1H) PMID:34686329 Finally, our published tran- scriptomic analysis of tti2-CKO mutants showed that PIKK mRNA levels remain unaffected following Tti2 depletion (Fig- ureS1H) PMID:34686329 (Figure 3E) PMID:34686329 (Figure 3E) PMID:34686329 (Figure 6B) PMID:34686329 (Figure 6B) PMID:34686329 (Figure 6J) PMID:34686329 RNA-seq PMID:34686329 (Figure 6H) PMID:34731638 (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 Figure 4E PMID:34731638 Figure 4E PMID:34731638 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 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 (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 (Figures 1B, 1C, S1D) only a subtle change of H3K9me2 at pericentromere PMID:34731638 (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 (Figure 2D) reduced heterochromatin spreading at mating-type and subtelomeric heterochromatin PMID:34731638 synthetic defect in the silencing of dg and tlh1/2 transcripts (Figure 4C) PMID:34731638 (figure 1 f) PMID:34731638 (figure 1 f) PMID:34731638 Figure 4E PMID:34731638 we observed derepression of several subtelomeric genes (Figures 2E and S2G). PMID:34731638 Figure 4E PMID:34731638 we observed derepression of several subtelomeric genes (Figures 2E and S2G). PMID:34731638 (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 (Figure 2D) reduced heterochromatin spreading at mating-type and subtelomeric heterochromatin PMID:34731638 (Figures S4A–S4C) Histone H3 ChIP-seq revealed a small but reproducible reduction of H3 at subtelomeres in pob3Δ PMID:34731638 (Figure S2F) PMID:34731638 (Figures S4A–S4C) Histone H3 ChIP-seq revealed a small but reproducible reduction of H3 at subtelomeres in pob3Δ PMID:34731638 (Figures S4A–S4C) Histone H3 ChIP-seq revealed a small but reproducible reduction of H3 at subtelomeres in pob3Δ PMID:34731638 found reduced Swi6 binding in spt16–1 at subtelomeric genes close to the heterochromatin boundary (SPAC212.12, SPAC212.06c; Figure 4D). PMID:34731638 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 Figures S2C–S2E in chromatin/euchromatin PMID:34731638 Moreover, epe1Δ reduced the expression of several subtelomeric genes in pob3Δ, suggesting that it also counteracts heterochromatin spreading (Figure 3G) PMID:34731638 Figures S2C–S2E in chromatin/euchromatin PMID:34731638 (Figure S1E) PMID:34731638 Partial suppression of pob3∆ silencing phenotype. PMID:34731638 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 (fig1G ) vw changed to increased (compared to WT) PMID:34731638 (fig1G) (fig1G ) vw changed to increased (compared to WT) PMID:34731638 (Figure 1 G) PMID:34731638 (Figure 1 G) PMID:34731638 vw changed from decreased to normal because look WT? PMID:34738170 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 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 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 Figure S1 D PMID:34798057 (Figure S7A) PMID:34798057 (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 (Figure S7A), PMID:34798057 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 V348A PMID:34798057 Figures 6I and 6J PMID:34798057 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:34805795 (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 (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 (Figure S1A) PMID:34805795 (Figure S1A) PMID:34805795 (Figure 4F) (vw: ph9) PMID:34805795 (Figure 4F) (vw: ph9) PMID:34805795 (figure 4d) (vw: assayed vacuolar pH as a surrogate for V-ATPase activity) PMID:34805795 Figure S1A PMID:34805795 Figure 5 PMID:34805795 Figure 5 PMID:34805795 during amino acid starvation PMID:34805795 Figure S1A PMID:34805795 results in a significant growth advantage of BFC mutant over wild-type strains when equal number of log phase cells are grown on rapamycin-containing EMM plates supplemented with amino acids (Figures S1A and S1B). Moreover, treating cells with 125 or 150 ng/mL of rapamycin for 90 min revealed that the growth advantage of BFC mutants correlates with an increase in P-Rps6 levels compared to wild-type cells (Figure S5C). Together, these data support a model in which BFC participates in TORC1 repression. PMID:34805795 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 (figure 4d) (vw: assayed vacuolar pH as a surrogate for V-ATPase activity) PMID:34805795 during amino acid starvation PMID:34805795 BFC augments TORC1 activation in response to amino acid stimulation PMID:34805795 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 during amino acid supplementation. (Figures 2G and S4), demonstrating that the BFC, is required for efficient activation of TORC1 following amino acid supplementation. PMID:34810257 (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 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 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 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 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 Cnp20-14A showed a strong interaction with Ccp1 (Fig. 5F) PMID:34810257 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 (Fig. 4 E and F). PMID:34810257 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 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 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 (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 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 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 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 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 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 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 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 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:34849791 Figure 4 PMID:34849791 Supplemental Figure S5B PMID:34849791 Supplemental Figure S5B PMID:34849791 Figure 4 PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S5B PMID:34849791 Supplemental Figure S5B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S5B PMID:34849791 Supplemental Figure S5B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S5B PMID:34849791 Supplemental Figure S5B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S5B PMID:34849791 Supplemental Figure S5B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S5B PMID:34849791 Supplemental Figure S5B PMID:34849791 Figure 3A PMID:34849791 Figure 3B PMID:34849791 Figure 4 PMID:34849791 Figure 4 PMID:34849791 Figure 3A PMID:34849791 Figure 3B PMID:34849791 Figure 4 PMID:34849791 Figure 3A PMID:34849791 Figure 3B PMID:34849791 Figure 4 PMID:34849791 Figure 3A PMID:34849791 Figure 3B PMID:34849791 Figure 4 PMID:34849791 Figure 3A PMID:34849791 Figure 3B PMID:34849791 Figure 4 PMID:34849791 Figure 3A PMID:34849791 Figure 3B PMID:34849791 Supplemental Figure S4B PMID:34849791 Supplemental Figure S4B PMID:34849791 Figure 4 PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S4B PMID:34849791 Supplemental Figure S4B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S4B PMID:34849791 Supplemental Figure S4B PMID:34849791 Supplemental Figure S4B PMID:34849791 Supplemental Figure S4B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S4B PMID:34849791 Supplemental Figure S4B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S4B PMID:34849791 Supplemental Figure S4B PMID:34849791 Supplemental Figure S6B PMID:34849791 Supplemental Figure S6B PMID:34849791 Figure 4 PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S6B PMID:34849791 Supplemental Figure S6B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S6B PMID:34849791 Supplemental Figure S6B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S6B PMID:34849791 Supplemental Figure S6B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S6B PMID:34849791 Supplemental Figure S6B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S6B PMID:34849791 Supplemental Figure S6B PMID:34849791 Supplemental Figure S1B PMID:34849791 Supplemental Figure S1B PMID:34849791 Figure 4 PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S1B PMID:34849791 Supplemental Figure S1B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S1B PMID:34849791 Supplemental Figure S1B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S1B PMID:34849791 Supplemental Figure S1B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S1B PMID:34849791 Supplemental Figure S1B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S1B PMID:34849791 Supplemental Figure S1B PMID:34849791 Supplemental Figure S2B PMID:34849791 Supplemental Figure S2B PMID:34849791 Figure 4 PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S2B PMID:34849791 Supplemental Figure S2B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S2B PMID:34849791 Supplemental Figure S2B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S2B PMID:34849791 Supplemental Figure S2B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S2B PMID:34849791 Supplemental Figure S2B PMID:34849791 Supplemental Figure S2B PMID:34849791 Supplemental Figure S2B PMID:34849791 Supplemental Figure S3B PMID:34849791 Supplemental Figure S3B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S3B PMID:34849791 Supplemental Figure S3B PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S3B PMID:34849791 Supplemental Figure S3B PMID:34849791 Supplemental Figure S3B PMID:34849791 Supplemental Figure S3B PMID:34849791 Supplemental Figure S3B PMID:34849791 Supplemental Figure S3B PMID:34849791 Figure 4 PMID:34849791 Figure 4 PMID:34849791 Figure 4 PMID:34849791 Supplemental Figure S3B PMID:34849791 Supplemental Figure S3B PMID:34849791 Figure 4 PMID:34849791 Figure 4 PMID:34849791 Figure 4 PMID:34849791 Figure 3A PMID:34849791 Figure 3B PMID:34849791 Figure 4 PMID:34849791 Figure 3A PMID:34849791 Figure 3B PMID:34849791 Figure 4 PMID:34849791 Figure 3A PMID:34849791 Figure 3B PMID:34849791 Figure 4 PMID:34849791 Figure 3A PMID:34849791 Figure 3B PMID:34849791 Figure 4 PMID:34849791 Figure 3A PMID:34849791 Figure 3B PMID:34849791 Figure 3A PMID:34849791 Figure 3B PMID:34849791 Figure 4 PMID:34851403 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 Non-separated signals were found to be significantly or nearly significantly wider than in wild-type cells (Fig. 3E,F;) PMID:34851403 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 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:34910579 see above PMID:34910579 Figure 1, C and D restrictive temperature mutant. PMID:34910579 36 degrees PMID:34910579 36 degrees PMID:34910579 recruits glucanases and glucan synthases to division site PMID:34910579 36 degrees PMID:34910579 36 degrees PMID:34910579 36 degrees PMID:34910579 Supplemental Figure S2, A–D PMID:34910579 Supplemental Figure S2, A–D PMID:34910579 36 degrees PMID:34910579 Figure 2A PMID:34910579 36 degrees PMID:34910579 36 degrees PMID:34910579 36 degrees PMID:34910579 38.5% cf WT 11.5% Figure 1F PMID:34910579 36 degrees PMID:34910579 recruits glucanases and glucan synthases to division site PMID:34910579 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 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:34951983 required for spindle repair following laser ablation PMID:34951983 Not required for spindle repair following laser ablation PMID:34951983 Microtubule dynamics required for spindle repair following laser ablation PMID:34951983 required for spindle repair following laser ablation PMID:34958661 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 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 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 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 Arf6 node localization required Cdr2 but not other node proteins (Figs. 2 E and S2 B). PMID:34958661 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 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 A GDP-locked mutant arf6(T52N)-mNG lost node localization, (Fig. 2 F) PMID:34958661 but the GTP-locked allele arf6(Q75L)-mNG remained at nodes (Fig. 2 F) PMID:34958661 Further, Arf6 localization to nodes was lost upon deletion of its GEF Syt22 (Fig. 2 G PMID:34958661 Indeed, arf6(Q75L)-mNG localized to nodes even in syt22Δ cells (Fig. 2 G) PMID:34958661 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 The resulting arf6 alleles reduced node localization and instead enriched at the cytoplasm (Fig. S2, H and I) PMID:34958661 The resulting arf6 alleles reduced node localization and instead enriched at the cytoplasm (Fig. S2, H and I) PMID:34958661 The resulting arf6 alleles reduced node localization and instead enriched at the cytoplasm (Fig. S2, H and I) PMID:34958661 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 "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 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 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 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 (actually mid1-Nter) PMID:34958661 The resulting arf6 alleles reduced node localization and instead enriched at the cytoplasm (Fig. S2, H and I) PMID:34958661 Thus, Arf6 and Mid1 are partially over- lapping anchors for Cdr2 nodes. PMID:34958661 Figure 1 PMID:34958661 Figure 1 PMID:34958661 Fig S1A; 27 micron PMID:34958661 Fig S1A; 26.6 micron PMID:34958661 Fig S1A; 24.6 micron PMID:34958661 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 The cell length at division phenotype for arf6Δ was minor, but these cells were wider than wild type (Fig. S1 E). PMID:34958661 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:34959732 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 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 (Sub lethal and lethat doese) Figure 5 and Figure S3. Also in the Table 3. PMID:34959732 Figure 4A and Figure S2A Sublethal concentrations of caspofungin PMID:34959732 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 Figure 3A and Figure S1A. Table 3. Suppression of the lytic phenotype at cytokinesis PMID:34959732 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 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 Figure 4A and Figure S2A Sublethal concentrations of caspofungin PMID:34959732 (Sub lethal and lethat doese) Figure 5 and Figure S3. Also in the Table 3. PMID:34967420 RNA-Seq PMID:34967420 Northern Blotting, RNA-Seq PMID:34967420 RNA-Seq PMID:34967420 RNA-Seq PMID:34967420 RNA-Seq PMID:34967420 RNA-Seq PMID:34967420 RNA-Seq PMID:34967420 RNA-Seq PMID:34967420 RNA-Seq PMID:34967420 RNA-Seq PMID:34967420 RNA-Seq PMID:34967420 RNA-Seq PMID:34967420 RNA-Seq PMID:34967420 RNA-Seq PMID:34967420 RNA-Seq PMID:34967420 RNA-Seq PMID:34967420 RNA-Seq PMID:34967420 RNA-Seq PMID:34967420 RNA-Seq PMID:35008733 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 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 (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 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 fig 5 b. (thin-layer chromatography) We detected an accumulation of PHS and sphingoid bases-1-phosphate levels (PHS-1P or DHS-1P) PMID:35011726 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 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 (Figure 3A) ubiquitin ligase mutant PMID:35011726 severe growth defects with smc6-X and nse6∆ PMID:35011726 (Figure 3A) ubiquitin ligase mutant PMID:35011726 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 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 These synthetic phenotypes were again suppressed by the nse1-C216S mutation (Figure S5). PMID:35011726 Figure 1A PMID:35011726 Figure 1A PMID:35011726 (Figure 2D PMID:35011726 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 Nse1- R188E mutant shows synthetic lethality with smc6-74 PMID:35011726 severe growth defects with smc6-X and nse6∆ PMID:35011726 Nse1- R188E mutant shows synthetic lethality with smc6-74 PMID:35011726 severe growth defects with smc6-X and nse6∆ PMID:35011726 Nse4 ubiquitination at K181 and Nse3 at K195 (Data Files S3 and S4). PMID:35011726 Nse4 ubiquitination at K181 and Nse3 at K195 (Data Files S3 and S4). PMID:35011726 severe growth defects with smc6-X and nse6∆ PMID:35011726 Interestingly, the addition of nse1- C216S mutation suppressed the R188E phenotypes (Figure 3A), suggesting that it leads to a ubiquitin-ligase-independent outcome. PMID:35012333 Fig 10A PMID:35012333 Fig 10A PMID:35012333 Fig 10A PMID:35012333 Fig 10A PMID:35012333 Fig 10A PMID:35012333 Fig 10A PMID:35012333 Fig 10A PMID:35012333 Fig 10A PMID:35012333 Fig 10A PMID:35012333 Fig 4 PMID:35012333 Fig 10B PMID:35012333 Fig 10B PMID:35012333 Fig 10B PMID:35012333 Fig 10B PMID:35012333 Fig 10B PMID:35012333 Fig 10B PMID:35012333 Fig 10B PMID:35012333 Fig 10B PMID:35012333 Fig 10B PMID:35012333 Fig 10B PMID:35012333 Fig 10B PMID:35012333 Fig 10B PMID:35012333 Fig 4 PMID:35012333 Fig 8A PMID:35012333 Fig 8A PMID:35012333 Fig 8B PMID:35012333 Fig 8B PMID:35012333 Fig 7A PMID:35012333 Fig 7A PMID:35012333 Fig 7A PMID:35012333 Fig 7A PMID:35012333 Fig 7B PMID:35012333 Fig 7B PMID:35012333 Fig 7B PMID:35012333 Fig 7B PMID:35012333 Fig 7B PMID:35012333 Fig 7B PMID:35012333 Fig 7A PMID:35012333 Fig 7A PMID:35012333 Fig 7A PMID:35012333 Fig 6A PMID:35012333 Fig 6A PMID:35012333 Fig 6B PMID:35012333 Fig 6B PMID:35012333 Fig 5A PMID:35012333 Fig 5A PMID:35012333 Fig 5A PMID:35012333 Fig 5A PMID:35012333 Fig 5A PMID:35012333 Fig 5A PMID:35012333 Fig 5A PMID:35012333 Fig 5A PMID:35012333 Fig 5A PMID:35012333 Fig 5A PMID:35012333 Fig 5A PMID:35012333 Fig 5A PMID:35012333 Fig 5A PMID:35012333 Fig 5A PMID:35012333 Fig 5A PMID:35012333 Fig 5A PMID:35012333 Fig 5A PMID:35012333 Fig 5A PMID:35012333 Fig 5B PMID:35012333 Fig 5B PMID:35012333 Fig 5B PMID:35012333 Fig 5B PMID:35012333 Fig 5B PMID:35012333 Fig 5B PMID:35012333 Fig 5B PMID:35012333 Fig 5B PMID:35012333 Fig 4B PMID:35012333 Fig 4B PMID:35012333 Fig 4B PMID:35012333 Fig 4B PMID:35012333 Fig 5B PMID:35012333 Fig 5B PMID:35012333 Fig 5B PMID:35012333 Fig 4A PMID:35012333 Fig 4A PMID:35012333 Fig 4A PMID:35012333 Fig 4A PMID:35012333 Fig 4A PMID:35012333 Fig 4A PMID:35012333 Fig 4A PMID:35012333 Fig 4A PMID:35012333 Fig 4A PMID:35012333 Fig 2A PMID:35012333 Fig 10A PMID:35012333 Fig 10A PMID:35012333 Fig 10A PMID:35012333 Described in Garg et al. (NAR 2020) -PMID: 33010152 PMID:35012333 Described in Garg et al. (NAR 2020) -PMID: 33010152 PMID:35012333 Fig 11B PMID:35012333 Fig 11B PMID:35012333 Fig 11B PMID:35012333 Fig 11B PMID:35012333 Fig 11B PMID:35012333 Fig 11B PMID:35012333 Fig 11B PMID:35012333 Fig 11B PMID:35012333 Fig 11A PMID:35012333 Fig 11A PMID:35012333 Fig 11A PMID:35012333 Fig 11A PMID:35012333 Fig 11A PMID:35012333 Fig 11A PMID:35012333 Fig 11A PMID:35012333 Fig 11A PMID:35012333 Fig 11A PMID:35012333 Fig 11A PMID:35012333 Fig 11A PMID:35012333 Fig 11A PMID:35012333 Fig 11A PMID:35012333 Fig 13 PMID:35012333 Fig 13 PMID:35012333 Fig 13 PMID:35012333 Fig 13, new term suggested PMID:35012333 Fig 13, new term suggested PMID:35012333 Fig 13, new term suggested PMID:35012333 Fig 13, new term suggested PMID:35012333 Fig 13, new term suggested PMID:35012333 Fig 13 PMID:35012333 Fig 13 PMID:35012333 Fig 13 PMID:35012333 Fig 12A PMID:35012333 Fig 13 PMID:35012333 Fig S2 PMID:35012333 Fig S3 PMID:35012333 Fig S3 PMID:35012333 Fig S3 PMID:35012333 Fig S3 PMID:35012333 Fig S4 PMID:35012333 Fig S4 PMID:35012333 Fig S4 PMID:35012333 Fig S4 PMID:35012333 Fig S4 PMID:35012333 Fig S4 PMID:35012333 Fig S5B PMID:35012333 Fig S5B PMID:35012333 Fig S5A PMID:35012333 Fig S5A PMID:35012333 Fig 12B PMID:35012333 Fig 12B PMID:35012333 Fig 2B PMID:35012333 Fig 2A PMID:35012333 Fig 2A PMID:35012333 Fig 2A PMID:35012333 Fig 2B PMID:35012333 Fig 2B PMID:35012333 Fig 2B PMID:35012333 Fig 1A PMID:35012333 Fig 1A PMID:35012333 Fig 1A PMID:35012333 Fig 1A PMID:35012333 Fig 1A PMID:35012333 Fig 1A PMID:35012333 Fig 1A PMID:35012333 Fig 12B PMID:35012333 Fig S6, new term suggested PMID:35012333 Fig S6 PMID:35012333 Fig S7 PMID:35012333 Fig S7 PMID:35012333 Fig S7 PMID:35012333 Fig S7 PMID:35012333 Fig S7 PMID:35012333 Fig S7 PMID:35012333 Fig 1A PMID:35024575 Conclusion is dawn by comparing Fig. 1H and Fig. 1I in https://www.micropublication.org/journals/biology/micropub-biology-000508. PMID:35024575 Conclusion is dawn by comparing Fig. 1H and Fig. 1I in https://www.micropublication.org/journals/biology/micropub-biology-000508. PMID:35075549 (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 (Fig. 5) We found that when Fzo1 protein was overexpressed, it was no longer degraded at late time points PMID:35075549 -v regulation, stationary phase PMID:35075549 ****STATIONARY PhASE**** the protein level of Fzo1 is unstable during the stationary phase. PMID:35075549 -ve regulation stat phase PMID:35075549 (Fig. 3). We found that Fzo1 protein was not degraded at late time points in the ∆rsv2 mutant PMID:35079912 (Figure 3A) Fe2(SO4)3 was added to YES media for a final concentration of 2.75 mM. PMID:35079912 (Figure 3A) 25 µM of iron chelator bathophenanthroline disulfonate (BPS) was added to YES media to create iron-depleted condition. PMID:35079912 We found that only Δfio1 cells were sensitive to Cu2+ PMID:35079912 (Figure 3A) Fe2(SO4)3 was added to YES media for a final concentration of 2.75 mM. PMID:35079912 (Figure 3A) 25 µM of iron chelator bathophenanthroline disulfonate (BPS) was added to YES media to create iron-depleted condition. PMID:35082773 (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 (Figures 3A,B) overexpression of cdr2+ also reversed the defects in the cell length and the septation index of ksg1-208 cells PMID:35082773 (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 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 (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 (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 Figure 1A PMID:35082773 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 Figure 1A PMID:35082773 (Figure 2A) significantly longer than that of wild-type cells at 27◦C PMID:35082773 (Figure 2B) ...which was recovered by the overexpression of ppk21+ PMID:35082773 Figure 2B...which was recovered by the overexpression of ppk21+ PMID:35082773 (Figure 2C) 33 degrees PMID:35082773 (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:35082773 (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 (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 (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:35099006 The growth rate of pkd2-B42 at the restrictive temperature of 36C or higher is 80% lower than wild-type cells. PMID:35099006 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:35099006 Increased percentage of septated cells at both permissive and restrictive temperature. PMID:35108037 Fig S2D PMID:35108037 Figure S3A (25C) PMID:35108037 Figure S3A (25C) PMID:35108037 Figure S3A (25C) PMID:35108037 Mutant bound Cdc15C1(aa600-end) as well as wildtype Pxl1 (Figure S1A) PMID:35108037 Mutant reduced binding to Cdc15C1(aa600-end) compared to wild type Pxl1 (Figure S1A) PMID:35108037 Mutant reduced binding to Cdc15C1(aa600-end) compared to wild type Pxl1 (Figure S1A) PMID:35108037 Mutant reduced binding to Cdc15C1(aa600-end) compared to wild type Pxl1 (Figure S1A) PMID:35108037 Pxl1-AxxA1-3 bound Cdc15C1(aa600-end) just as well as wild type Pxl1 (Figure S1A) PMID:35108037 Pxl1-P18A reduced binding to full-length Cdc15 compared to wild-type Pxl1 (Figure 3A) PMID:35108037 Pxl1-P18A+AxxA6 reduced binding to full-length Cdc15 compared to wild type Pxl1 (Figure 3A) PMID:35108037 Pxl1-AxxA6 reduced binding to full-length Cdc15 (Figure 3A) and Cdc15 C1 (Figure S1A) PMID:35108037 Figure S2D PMID:35108037 Figure S2D PMID:35108037 Figure S2D PMID:35108037 Figure S2D PMID:35108037 Figure S2D (25,29,32) PMID:35108037 Figure S2D (25,29,32) PMID:35108037 Pxl1 (aa177-188 P181A, P184A) abolished binding to Cdc15 SH3 and Cdc15C1(aa600-end), Figure 2D PMID:35108037 Figure 2B - Pxl1(AxxA1-6) reduced binding to Cdc15C(aa441-end) compared to wildtype Pxl1 PMID:35108037 Figure S2A-C PMID:35108037 Figure S2A-C PMID:35108037 Figure S2A-C PMID:35108037 Figure S2A-C PMID:35108037 Figure S2A-C PMID:35108037 Figure S2A-C PMID:35108037 Fig S2D PMID:35108037 Fig S2D PMID:35108037 Figure S2D PMID:35108037 Figure 1B, 1D-F, 2B-E, 3A-B, S1A-B PMID:35108037 in vitro binding assay, Figure 3B PMID:35108037 Figure S2D PMID:35108037 in vitro binding assay with purified Cdc15 F-BAR domain and purified Pxl1 (Fig 1E) PMID:35108037 Figure S2E PMID:35108037 Figure S2E PMID:35108037 Figure S2E PMID:35108037 Figure S2E PMID:35108037 Figure S2E PMID:35108037 Figure S2E PMID:35108037 Figure S2E PMID:35108037 Figure S2E PMID:35108037 Figure S2E PMID:35108037 Figure S2E PMID:35108037 Figure S2E PMID:35108037 Figure S2E PMID:35108037 Figure S2E PMID:35108037 Figure S2E PMID:35108037 Figure S2E PMID:35108037 Figure S2E PMID:35108037 Figure S2E PMID:35108037 Figure S2E PMID:35108037 Figure S3B (25C) PMID:35108037 Figure S3A (25C) PMID:35108037 Figure S3A (25C) PMID:35108037 Figure S3A (25C) PMID:35108037 Figure S3A (25C) PMID:35108037 Figure S3A PMID:35108037 Figure S3A (25C) PMID:35108037 Figure 4A,C PMID:35108037 Figure 4A,C PMID:35108037 Figure 4B,D PMID:35108037 Figure 4B,D PMID:35108037 Figure 4B,D PMID:35108037 Figure S1D-E PMID:35108037 Figure S2D (19c) PMID:35108037 Figure S2D PMID:35108037 Figure S2D(25,29,32) PMID:35108037 Figure S2D PMID:35157728 Figure2 A PMID:35157728 The Δbdf2 muta- tion also suppresses the elevated levels of Gcn5 at the subtelomeric chromatin in Δtor1 cells (Fig 4E). PMID:35157728 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 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 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 24% PMID:35157728 Figure2 A PMID:35157728 Figure2 A PMID:35157728 Figure2 A PMID:35157728 Figure2 A PMID:35157728 Figure2 A PMID:35157728 Figure2 A PMID:35157728 25% PMID:35157728 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 Figure2 A PMID:35157728 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 Tor1 inhibits the binding of Gcn5 at sub-telomeric genes and MBF promoters PMID:35157728 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 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 no supression PMID:35157728 30 fold. Fig 2 PMID:35157728 280 fold. Fig 2 PMID:35157728 120 fold. Fig 2 PMID:35157728 Figure2 A PMID:35157728 Figure2 A PMID:35157728 Figure2 A PMID:35157728 Figure2 A PMID:35157728 Figure2 A PMID:35157728 Figure2 A PMID:35157728 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 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 Figure2 A PMID:3516412 activated_by(CHEBI:18420) PMID:35171902 polysome profiling PMID:35171902 polysome profiling PMID:35171902 . Interestingly, although git3Δ nmt41-epe1+ cells form heterochromatin at pericentric repeats, PMID:35171902 nterestingly, we found that Epe1 protein levels are significantly reduced in git3Δ nmt41-epe1+ and pka1Δ nmt41-epe1+ cells (Fig 2F) PMID:35171902 H3K9me2 levels at dh repeats are restored close to wild-type levels in git3Δ nmt41-epe1+ cells (Fig 1E). PMID:35171902 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:35194019 Figure 5C forward strand RT-qPCR (dh repeat) PMID:35194019 Fig S10 (tetrad analysis) PMID:35194019 Fig S10 (tetrad analysis) PMID:35194019 Fig S10 (tetrad analysis) PMID:35194019 Fig S10 (tetrad analysis) PMID:35194019 Fig S10 (tetrad analysis) PMID:35194019 Fig S10 (tetrad analysis) PMID:35194019 Fig S10 (tetrad analysis) PMID:35194019 TBZ 15ug/ml PMID:35194019 TBZ 15ug/ml PMID:35194019 TBZ 15ug/ml PMID:35194019 TBZ 15ug/ml PMID:35194019 TBZ 15ug/ml PMID:35194019 Figur 5C forward strand RT-qPCR (dh repeat) PMID:35194019 Figur 5C forward strand RT-qPCR (dh repeat) PMID:35194019 Figure 5C forward strand RT-qPCR (dh repeat) PMID:35194019 Figure 5C forward strand RT-qPCR (dh repeat) PMID:35194019 Figure 5C forward strand RT-qPCR (dh repeat) PMID:35194019 Figur 5D PMID:35194019 Figur 5D PMID:35277511 growth >48 hrs, growth to exponential phase PMID:35277511 telomere southern (experiment) PMID:35277511 telomere southern (experiment) PMID:35286199 Fig. 1 PMID:35286199 Fig. 1 PMID:35286199 Fig. 1 PMID:35286199 Fig. 1 PMID:35286199 Fig. 1 PMID:35286199 Fig. 1 PMID:35286199 Fig. 1 PMID:35286199 Fig. 1 PMID:35286199 Fig. 4 PMID:35286199 Fig. 4 PMID:35286199 Fig. 5 PMID:35286199 Fig. 5 PMID:35286199 Fig. 4 PMID:35286199 Fig. 4 PMID:35286199 Fig. 4 PMID:35286199 Fig. 4 PMID:35286199 Fig. 1 PMID:35286199 Fig. 3 PMID:35286199 Fig. 1 PMID:35286199 Fig. 1 PMID:35286199 Fig. 1 PMID:35286199 Fig. 1 PMID:35286199 Fig. 1 PMID:35286199 Fig. 2 PMID:35286199 Fig. 1 PMID:35286199 Fig. 1 PMID:35286199 Fig. 2 PMID:35286199 Fig. 1 PMID:35286199 Fig. 1 PMID:35286199 Fig. 1 PMID:35286199 Fig. 1 PMID:35293864 Fig. 2 - Figure supplement 2F PMID:35293864 mal3Δ cells exhibited lower microtubule growth speed throughout anaphase B Fig. 2G PMID:35293864 Fig. 2 - Figure supplement 1 klp5Δklp6Δ cells exhibited slightly longer microtubule growth events PMID:35293864 Fig. 2 - Figure supplement 2E PMID:35293864 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 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 Fig. 5E Ase1 is required for normal rescue distribution PMID:35293864 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 Note: not sure about the term name and the child. Fig. 3 supp 1 A, C PMID:35293864 Fig. 5 supp 3E PMID:35293864 Fig. 5F,G The decrease in growth speed associated with internalisation of microtubules in the nuclear membrane bridge is reduced upon Ase1 deletion PMID:35300005 100 ug/ml canavanine PMID:35314193 Figure 10 PMID:35314193 Figure 8 PMID:35314193 Figure 8 PMID:35314193 Figure 8 PMID:35314193 Figure 8 PMID:35314193 Figure 8 PMID:35314193 Figure 12 PMID:35314193 Figure 12 PMID:35314193 Figure 12 PMID:35314193 Figure 12 PMID:35314193 Figure 12 PMID:35314193 Cobalt/nickel-dependent inorganic pyrophosphatase activity, Figure 3 PMID:35314193 Cobalt/nickel-dependent inorganic pyrophosphatase activity, Figure 4 PMID:35314193 Cobalt/nickel-dependent inorganic pyrophosphatase activity, Figure 1 PMID:35314193 Cobalt/nickel-dependent inorganic pyrophosphatase activity, Figure 4 PMID:35314193 Figures 1 and 3 PMID:35314193 Figures 1 and 3 PMID:35314193 Figure 10 PMID:35320724 Figure 3, S1 PMID:35320724 Figure 2C PMID:35320724 Figure S1 PMID:35320724 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 Figure 2C PMID:35320724 Figure 4 PMID:35320724 Figure 4 PMID:35320724 Figure 4 PMID:35320724 Figure 5 PMID:35320724 Figure 5 PMID:35320724 Figure 5 PMID:35320724 Figure 6 PMID:35320724 Figure 1B, 5B PMID:35320724 Figure 6 PMID:35320724 Figure 6 PMID:35320724 Figure 6 PMID:35320724 Figure 6 PMID:35320724 Figure 6 PMID:35320724 Figure 7 PMID:35320724 Figure 7 PMID:35320724 Figure 7 PMID:35320724 Figure 7 PMID:35320724 Figure 7 PMID:35320724 Figure 7 PMID:35320724 Figure 4 PMID:35320724 Figure 4 PMID:35320724 Figure S4 PMID:35320724 Figure 2C PMID:35320724 Figure 3, S1 PMID:35320724 Figure 6 PMID:35320724 Figure S6B PMID:35320724 Figure S5 PMID:35320724 Figure S5 PMID:35320724 Figure S7 PMID:35320724 Figure 6 PMID:35320724 Figure 5 PMID:35320724 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 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 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 Figure 1B, 5B PMID:35320724 Figure 1B, 2D, 5B, 6C, 7B, 7C PMID:35320724 Figure S6G PMID:35320724 Figure 4 PMID:35320724 Figure 4 PMID:35320724 Figure 4 PMID:35320724 Figure 4 PMID:35320724 Figure 4 PMID:35320724 Figure 4 PMID:35320724 Figure 4 PMID:35320724 Figure 5 PMID:35320724 Figure 5 PMID:35320724 Figure S6D PMID:35325114 TERM REQUESTED growth auxotrophic for isoleucine PMID:35325114 TERM REQUESTED growth auxotrophic for valine PMID:35333350 These results suggest that Wpl1 plays a role in alignment of homologs through Rec8-dependent formation of axis-loop chromatin structure. PMID:35333350 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 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 during horsetail/ prophase PMID:35333350 (Figure S5B) PMID:35333350 (Figure S5B) PMID:35333350 These results suggest that Wpl1 plays a role in alignment of homologs through Rec8-dependent formation of axis-loop chromatin structure. PMID:35333350 (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 (Figure 7) rec8-F204S mutant is defective in LinE formation and recombination PMID:35333350 (Figure 5C) The rec8-F204S mutant maintained sister chromatid cohesion as assessed at the cut3 gene locus PMID:35333350 (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 (Figure 7) PMID:35333350 (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 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 Figure S4B PMID:35333350 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 (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 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 (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:35416247 in presence of tschimganine PMID:35416247 in presence of tschimganine PMID:35416247 in presence of tschimganine PMID:35416247 in presence of tschimganine PMID:35416247 in presence of tschimganine PMID:35416247 in presence of tschimganine PMID:35416247 in presence of tschimganine PMID:35416247 in presence of tschimganine PMID:35512546 RRM3 PMID:35536002 Fig. 8 PMID:35536002 Fig. 7 PMID:35536002 Fig. 7 PMID:35536002 Fig. 7 PMID:35536002 Fig. 7 PMID:35536002 Fig. 7 PMID:35536002 Fig. 12 (Note how the levels are the same as when the pyrophosphatase is inactivated in the full-length protein) PMID:35536002 Fig. 8 & 12 PMID:35536002 Fig. 12 PMID:35536002 Fig. 8 PMID:35536002 Fig. 7 PMID:35536002 Fig. 8 and text PMID:35536002 Fig. 7 PMID:35536002 Fig. 7 PMID:35536002 Fig. 7 PMID:35536002 Fig. 8 PMID:35536002 Fig. 7 PMID:35536002 Fig. 7 PMID:35536002 Fig. 7 PMID:35536002 Fig. 8 PMID:35536002 Fig. 12 PMID:35536002 Fig. 12 PMID:35609605 Figure 3 COMPACTION PMID:35609605 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 "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 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:35609605 figure 4D PMID:35609605 figure 4D PMID:35609605 COMPACTION Figures 3A, 3B, and S3A PMID:35609605 COMPACTION Figures 3A, 3B, and S3A (inhibiting exocytosis rescues defect of compaction) PMID:35609605 (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:35622906 OLD SPB PMID:35639710 Figure 2A PMID:35639710 Figure3 confirms dominance of can1-1 PMID:35639710 Fig 1 PMID:35639710 Figure 1 (same as WT) PMID:35639710 Figure1 PMID:35639710 Increased protein ubiquitination. PMID:35639710 Fig 1 PMID:35639710 Second, Any1R175C does not show an increase but rather a strong decrease in its ubiquiti- nation level. PMID:35673994 Fig. 6 PMID:35673994 Fig. 5 PMID:35673994 Fig. 6 PMID:35673994 Fig. 6 PMID:35673994 Fig. 6 PMID:35673994 Fig. 6 PMID:35673994 Fig. 6 PMID:35673994 Fig. 5 PMID:35673994 Fig. 5F PMID:35673994 Fig. 5C PMID:35673994 Fig. 5 PMID:35673994 Fig. 5 PMID:35673994 Fig. 2B PMID:35673994 Fig. 5 PMID:35673994 Fig. 5 PMID:35673994 Fig. 4E PMID:35673994 Fig. 2D PMID:35673994 Fig. 3 PMID:35673994 Fig. 3 PMID:35673994 Fig. 2B PMID:35673994 Fig. 6 PMID:35673994 Fig. 2C PMID:35673994 Fig. 2H PMID:35673994 Fig. 4E PMID:35673994 chimera expressed from the ura4 locus (@ura4) - kept because not assayed from fus1 locus PMID:35673994 Fig. 4E PMID:35673994 Fig. 4E PMID:35673994 Fig. 2B PMID:35673994 Fig. 2B PMID:35673994 Fig. 2B PMID:35673994 Fig. 2A PMID:35673994 Fig. 5 PMID:35673994 Fig. 5 PMID:35673994 Fig. 5 PMID:35673994 Fig. 5 PMID:35673994 Fig. 5 PMID:35781263 decreased PMID:35781263 "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:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Fig. 6 PMID:35924983 Fig. 6 PMID:35924983 Figure 3 PMID:35924983 through nuclear exclusion PMID:35924983 through nuclear exclusion PMID:35924983 through degradation by ubiquitination PMID:35924983 through degradation by ubiquitination PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Figure 3 PMID:35924983 Figure 3 PMID:35924983 Figure 6 PMID:35924983 Figure 6 PMID:35924983 Figure 6 PMID:35924983 Figure 6 PMID:35924983 Figure 6 PMID:35924983 Figure 6 PMID:35924983 Figure 7 PMID:35924983 Figure 7 PMID:35924983 Figure 7 PMID:35924983 Figure 7 PMID:35924983 Figure 7 PMID:35924983 Figure 7 PMID:35924983 Figure 7 PMID:35924983 Figure 7 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 6 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4, Table 1 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35924983 Supplemental Figure 4 PMID:35940128 Queuosine absent from tRNA when cells are supplied with queuosine nucleoside, but not when supplied with queuine nucleobase PMID:35940128 term requested Queuosine nucleosidase activity PMID:35970865 Fig. 2a PMID:35970865 Fig. 2a PMID:35970865 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 figure4 PMID:35970865 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 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 "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 Fig. 2a PMID:35970865 Fig. 2a PMID:35970865 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 normal CENP-A maintenance PMID:35970865 figure4 PMID:35970865 (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 normal CENP-A maintenance PMID:35970865 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 Figure 2a (during M-phase) PMID:35970865 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 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 (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 (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 decreased CENP-A maintenance PMID:35970865 normal CENP-A maintenance PMID:35970865 normal CENP-A maintenance PMID:36006032 figure 1 D PMID:36006032 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 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 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 figure 1 D PMID:36006032 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 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 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 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 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 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 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 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 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 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 figure 1 D PMID:36006032 figure 1 D PMID:36006032 figure 1 D PMID:36006032 figure 1 D PMID:36006032 figure 1 D PMID:36006032 figure 1 D PMID:36006032 figure 1 D PMID:36090151 1.6 mM PMID:36090151 1.6 mM PMID:36095128 A shorter form of the protein translated from intron-retained transcript PMID:36095128 Figure S13. C PMID:36095128 Figure S13. C PMID:36095128 Semi quantitative RT-PCR followed by gel electrophoresis; Intron retention observed in absence of sde2, cay1 and tls1 PMID:36095128 Semi quantitative RT-PCR followed by gel electrophoresis; Intron retention observed in absence of sde2, cay1 and tls1 PMID:36095128 figure 1 PMID:36095128 Figure S12.B PMID:36095128 Figure S12.B PMID:36095128 Figure S12.B PMID:36095128 Figure S12.B PMID:36095128 Figure S12.B PMID:36095128 Figure S12.B PMID:36095128 Figure S12.B PMID:36095128 Figure S12.B PMID:36095128 Figure S12.B PMID:36095128 Figure S12.B PMID:36095128 Figure S12.B PMID:36095128 Figure S12.B PMID:36095128 (Supplementary Figures S6 and S7A). mug5 intron 2 PMID:36095128 (Supplementary Figures S6 and S7A). rap1 intron 2 PMID:36095128 (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 Semi quantitative RT-PCR followed by gel electrophoresis; Intron retention observed in absence of sde2, cay1 and tls1 PMID:36095128 Semi quantitative RT-PCR followed by gel electrophoresis; Intron retention observed in absence of sde2, cay1 and tls1 PMID:36095128 figure 1 (rap1 intron2, ftp105 intron 3 and pyp3 intron 1) PMID:36095128 Among the mutants studied, Δcay1 and Δtls1 strains also showed splicing defects spe- cific for rap1 intron 2 (Supplementary Figure S10A). PMID:36095128 Among the mutants studied, Δcay1 and Δtls1 strains also showed splicing defects spe- cific for rap1 intron 2 (Supplementary Figure S10A). PMID:36095128 Figure S13. C A shorter form of the protein translated from intron-retained transcript PMID:36095128 Figure S13. C A shorter form of the protein translated from intron-retained transcript PMID:36095128 figure 1 (rap1 intron2, ftp105 intron 3 and pyp3 intron 1) PMID:36095128 figure 1 (rap1 intron2, ftp105 intron 3 and pyp3 intron 1) PMID:36095128 figure 1 PMID:36095128 figure 1 PMID:36095128 figure 1 (rap1 intron2 branch site distance decreased) PMID:36095128 figure 1 (rap1 intron2 branch site distance decreased) PMID:36095128 Figure S13. C PMID:36095128 Figure S13. C PMID:36095128 Figure S13. C PMID:36095128 Figure S13. C PMID:36095128 Figure S13. C PMID:36095128 Figure S13. C PMID:36095128 Figure S13. C PMID:36095128 Figure S13. C PMID:36095128 Figure S13. C PMID:36095128 A shorter form of the protein translated from intron-retained transcript PMID:36095128 A shorter form of the protein translated from intron-retained transcript PMID:36095128 A shorter form of the protein translated from intron-retained transcript PMID:36095128 A shorter form of the protein translated from intron-retained transcript PMID:36095128 A shorter form of the protein translated from intron-retained transcript PMID:36095128 A shorter form of the protein translated from intron-retained transcript PMID:36095128 A shorter form of the protein translated from intron-retained transcript PMID:36095128 A shorter form of the protein translated from intron-retained transcript PMID:36095128 A shorter form of the protein translated from intron-retained transcript PMID:36095128 A shorter form of the protein translated from intron-retained transcript PMID:36095128 A shorter form of the protein translated from intron-retained transcript PMID:36095128 A shorter form of the protein translated from intron-retained transcript PMID:36108046 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 (****NEW TERM REQUESTED->ACTIVATION) but dnt1Δ cells stayed for extended length of time at ana- phase B (Fig 1D–1F) PMID:36108046 I changed to decreased. becasue the phenotype is compared to WT, PMID:36108046 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 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 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 I changed to decreased. becasue the phenotype is compared to WT, PMID:36108046 but dnt1Δ cells stayed for extended length of time at ana- phase B (Fig 1D–1F) PMID:36112198 figure 2 PMID:36112198 figure 2 PMID:36112198 figure 2 PMID:36112198 figure 2b PMID:36112198 figure 2b PMID:36112198 cgs1∆ partially rescues plb1∆ on KCl PMID:36112198 Fig.1 Overexpression of Pka1 restores the KCl-sensitive pheno- type of the plb1∆ strain. PMID:36112198 Fig.1 Overexpression of Pka1 restores the KCl-sensitive pheno- type of the plb1∆ strain. PMID:36112198 cgs1∆ rescues cyr1∆ plb1∆ on sorbitol PMID:36112198 cgs1∆ partially rescues cyr1∆ plb1∆ on KCl PMID:36112198 rst2∆ rescues pka1∆ on KCl PMID:36112198 rst2∆ rescues pka1∆ on KCl PMID:36112198 Fig 4 rst2∆ partially rescues plb1∆ on KCl PMID:36112198 Fig 4 rst2∆ partially rescues plb1∆ on KCl PMID:36112198 cgs1∆ partially rescues plb1∆ on KCl PMID:36112198 observed Pka1-GFP PMID:36112198 observed Pka1-GFP PMID:36112198 rst2∆ rescues pka1∆ plb1∆ on KCl PMID:36112198 rst2∆ partially rescues pka1∆ plb1∆ on KCl PMID:36112198 observed Pka1-GFP PMID:36112198 low glucose MM PMID:36112198 glucose MM PMID:36112198 Fig 1b PMID:36112198 glucose MM PMID:36112198 observed Pka1-GFP PMID:36112198 fig5 PMID:36112198 Fig. S2 PMID:36112198 Fig. S2 PMID:36112198 figure 3 PMID:36112198 fig4 PMID:36112198 figure 2 PMID:36112198 figure 2 PMID:36112198 Fig. S2 PMID:36112198 figure S2 PMID:36112198 fig1 (double mutant with cyr1 is more sensitive) PMID:36112198 figure 2 PMID:36112198 Fig. S2 PMID:36112198 Fig. S2 PMID:36112198 figure 2 PMID:36112198 Fig. S2 PMID:36112198 Fig S2 PMID:36112198 Fig. S2 PMID:36138017 (Fig. 2d) PMID:36138017 Dma1 ubiquitinates Tip1 PMID:36138017 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 (Fig. 4) PMID:36138017 (Fig. 4) PMID:36138017 though HU treatment caused equally efficient arrest at S phase in both wild-type and dma1Δ cells (Supplementary Fig. 4) PMID:36138017 figure 1D. PMID:36138017 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 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:36174923 fig S2 PMID:36174923 Fig. 7b partial rescue - still loses viabiltiy at 48 hours PMID:36174923 Fig. 7b partial rescue - still loses viabiltiy at 48 hours PMID:36174923 Fig. 5. PMID:36174923 Fig. 5. PMID:36174923 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 Fig. 5. PMID:36174923 Fig. 5. PMID:36174923 fig 4 PMID:36174923 fig S2 PMID:36174923 fig S2 PMID:36174923 fig S2 PMID:36174923 fig S2 PMID:36174923 figure1 PMID:36174923 Fig 6 PMID:36174923 Fig. 5. PMID:36174923 Fig. S5. PMID:36174923 Fig. 5. PMID:36174923 Fig. S5. PMID:36174923 Fig. S5. PMID:36200823 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 Importantly, no significant dif- ference in the level of Cnp1 protein or mRNA was seen in sfh1-13 cells (Figure 1E). PMID:36200823 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 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 However, the sfh1-13 mutation had only a mild influence on H3K9me levels (Figure 1C), as we re- ported previously (12). PMID:36200823 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 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 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 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 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 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 (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:36200823 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 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 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 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 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 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 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:36200871 ********** move to new decreased immediate intracellular calcium spike following osmotic shock :: The peak amplitude of the cal- cium spikes in pkd2-B42 cells was similarly reduced by 62% (Figure 4D). PMID:36200871 ********* move to new decreased immediate intracellular calcium spike following osmotic shock PMID:36200871 Supplemental Figure S5A). We concluded that the calcium-permeable Pkd2 primarily localizes to the plasma membrane. PMID:36200871 Figure 2, E and F). We concluded that Pkd2 is calcium-permeable under the mechanical stimulus of membrane stretching. PMID:36200871 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 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 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 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 data not shown, related data in Figure 2A PMID:36302945 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 Figure 3, this phenotype was observed for cat1_delta leu1-32 double mutant. PMID:36361590 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 figure3 PMID:36361590 Gpl1-Gih35-Wdr83 complex PMID:36361590 Gpl1-Gih35-Wdr83 complex PMID:36361590 Gpl1-Gih35-Wdr83 complex PMID:36361590 Figure 2 PMID:36361590 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:36361590 figure3 PMID:36361590 figure3 PMID:36361590 figure3 PMID:36408846 figure 4a PMID:36408846 (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 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 (Check tomorrow should this be tri methylation) PMID:36408846 clr4F449Y/clr4F449Y cells displayed strongly ele- vated H3K9me2 levels when in mitosis, while H3K9me3 was absent (Figs 2A and EV3A). PMID:36408846 clr4F449Y/clr4F449Y cells displayed strongly ele- vated H3K9me2 levels when in mitosis, while H3K9me3 was absent (Figs 2A and EV3A). PMID:36408846 (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 This revealed reduced H3K9me2, but increased H3K9me3 levels upon 1-NM-PP1 addition in cdk1-as cells specifi- cally (Fig 6F), PMID:36408846 clr4F449Y/clr4F449Y cells displayed strongly ele- vated H3K9me2 levels when in mitosis, while H3K9me3 was absent (Figs 2A and EV3A). PMID:36408846 figure 3F PMID:36408846 figure 4a PMID:36408846 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 Furthermore, fewer clr4F449Y/clr4F449Y cells displayed lagging DNA upon expression of Swi6Chp1-like-CD (Fig 4C and D). PMID:36408846 spores formed colonies again (Fig 4G). PMID:36408846 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 Indeed, CDK1/Cyclin B phosphorylated recombinant Clr4 specifically at S458 (Fig 6E). PMID:36435910 Dis1 uses its TOG domains to induce microtubule catastrophe, in which polymerisation turns into depolymerisation PMID:36435910 Evidence: in vitro biochemical assays using purified tubulin and recombinant Dis1 protein / New GO term requested: microtubule destabilization activity PMID:36435910 Figure 2a PMID:36435910 Figure 2a PMID:36435910 Figure 2a PMID:36435910 Figure 2a PMID:36481249 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 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 figure 1a PMID:36481249 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 wat1Δ and wat1-17 mutant cells were a little elongated with an average size of 18.5 μm (Fig. 3A and 3B). PMID:36481249 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 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 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 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 wat1Δ and wat1-17 mutant cells were a little elongated with an average size of 18.5 μm (Fig. 3A and 3B). PMID:36481249 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 abolished Mhf1 localization PMID:36537249 binds to Mhf1 PMID:36537249 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 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 binds to Mhf2 PMID:36537249 mitotic prophase PMID:36617881 These results suggest that Epe1 promotes assembly of the RNAi machinery at constitutive heterochromatin by expressing dg/dh ncRNAs. PMID:36626373 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 Fig. 3B PMID:36633091 Fig. 5C PMID:36633091 Fig. 1A, 1B, S1A PMID:36633091 Fig. 1A, 1B, S1A PMID:36633091 Fig. 1A, 1B, S1A PMID:36633091 Fig. S1D and S1E PMID:36633091 Fig. 2A and 2C PMID:36633091 Fig. 5C PMID:36633091 Fig. 5C PMID:36633091 Fig. 2C PMID:36633091 Fig. 1C, ID and 1E PMID:36633091 Fig. 2A and 2C PMID:36633091 Fig. 3B PMID:36633091 Fig. 2A and 2B PMID:36633091 Fig. 2D PMID:36633091 Fig. 2C PMID:36633091 Fig. 1C, 1D and 1E PMID:36633091 Fig. 1C, Fig. 1D and Fig. 1E PMID:36633091 Supplementary Fig. S1D and S1E PMID:36633091 Fig. 3B PMID:36633091 Fig. 5C PMID:36650056 Lower levels in the akr1 mutant PMID:36650056 Change to: Nuclear congression without nuclear fusion PMID:36650056 change to: twin horsetail nucleus PMID:36650056 Change to: Nuclear congression without nuclear fusion PMID:36650056 palmitoylation of tht1D is reduced by ark1D PMID:36650056 change to: twin horsetail nucleus PMID:36650056 Was annotated as normal meiosis PMID:36650056 Change to: Nuclear congression without nuclear fusion PMID:36650056 change to: twin horsetail nucleus PMID:36650056 akr1Δ affecting tht1 PMID:36650056 Lower levels in the akr1 mutant PMID:36695178 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 Very high levels of diploidization in minimal medium PMID:36695178 Very prominent in minimal medium due to the lack of the Kennedy pathway precursors PMID:36695178 Very prominent in minimal medium due to the lack of the Kennedy pathway precursors PMID:36695178 Very prominent in minimal medium due to the lack of the Kennedy pathway precursors PMID:36695178 Sub-lethal phenotype, with only 10% of expected double mutants recovered. PMID:36695178 LC-MS PMID:36695178 LC-MS PMID:36695178 LC-MS PMID:36695178 LC-MS PMID:36695178 LC-MS PMID:36695178 LC-MS PMID:36695178 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:36705602 Figure 3 summarizes data PMID:36705602 Figure 3 summarizes data PMID:36705602 Figure 3 summarizes data PMID:36705602 Figure 3 summarizes data PMID:36705602 Figure 3 summarizes data PMID:36705602 Figure 3 summarizes data PMID:36705602 Figure 3 summarizes data PMID:36705602 Figure 3 summarizes data PMID:36705602 Figure 3 summarizes data PMID:36749320 Figure 5A PMID:36749320 Figure 3 PMID:36749320 Figure 3 PMID:36749320 Figure 3 PMID:36749320 Figure 3 PMID:36749320 Figure 3 PMID:36749320 Figure 3 PMID:36749320 Figure 3 PMID:36749320 Figure 3 PMID:36749320 Figure 3 PMID:36749320 Figure 3 PMID:36749320 Figure 3 PMID:36749320 Figure 3 PMID:36749320 Figure 3 PMID:36749320 Figure 3 PMID:36749320 Figure 3 PMID:36749320 Figure 3 PMID:36749320 Figure 3 PMID:36749320 Figure 10 PMID:36749320 Figure 10 PMID:36749320 Figure 4 PMID:36749320 Figure 5 PMID:36749320 Figure 5C PMID:36749320 Figure 5A PMID:36749320 Figure 5A PMID:36749320 Figure 5A PMID:36749320 Figure 5A PMID:36749320 Figure 5A PMID:36749320 Figure 5A PMID:36749320 Figure 5A PMID:36749320 Figure 5A PMID:36749320 Figure 5A PMID:36749320 Figure 5A PMID:36749320 Figure 5A PMID:36749320 Figure 5A PMID:36749320 Figure 5A PMID:36749320 Figure 5A PMID:36749320 Figure 5A PMID:36749320 Figure 5A PMID:36749320 Figure 5A PMID:36749320 Figure 5A PMID:36749320 Figure 5B PMID:36749320 Figure 10 - Manu: transfer to FYPO:0008075 PMID:36749320 Figure 10 - Manu: Transfer to FYPO:0008075 PMID:36749320 Figure 5C PMID:36749320 Figure 5C PMID:36749320 Figure 10 PMID:36749320 Figure 10 PMID:36749320 Fig. 5 S2 PMID:36749320 Fig. 5 S2 PMID:36749320 Fig. 5 S2 PMID:36749320 Fig. 5 S2 PMID:36749320 Fig. 5 S2 PMID:36749320 Fig. 5 S2 PMID:36749320 Fig. 5 S2 PMID:36749320 Fig. 5 S2 PMID:36749320 Fig. 3E PMID:36779416 non detectable Fig. 1. Phosphate starvation induces ecl3+ expression in a pho7+-dependent manner. PMID:36779416 non detectable Fig. 1. Phosphate starvation induces ecl3+ expression in a pho7+-dependent manner. PMID:36779416 Phosphate starvation did not induce ecl3+ expression in Δckb1 cells, indicating that the induction was dependent on Ckb1 (Fig. 2B) PMID:36779416 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 figure 1A,B PMID:36779416 non detectable Fig. 1. Phosphate starvation induces ecl3+ expression in a pho7+-dependent manner. PMID:36793083 Fig. 3 PMID:36793083 Fig. 3 PMID:36793083 Fig. 3 PMID:36793083 Fig. 4D PMID:36793083 Fig. 4D PMID:36793083 Fig. 4D PMID:36793083 Fig. 4D PMID:36793083 Fig. 4D PMID:36793083 Fig. 4D PMID:36793083 Fig. 4D PMID:36793083 Fig. 4D PMID:36793083 Fig. 4D PMID:36793083 Fig. 3 PMID:36793083 Fig. 3 PMID:36793083 Fig. 3 PMID:36793083 Fig. 3 PMID:36793083 Fig. 3 PMID:36793083 Fig. 3 PMID:36793083 Fig. 3 PMID:36793083 Fig. 3 PMID:36793083 Fig. 3 PMID:36793083 Fig. 3 PMID:36793083 Fig. 3 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36794724 Figure 5B ****NEW TERM PENDING******decreased chronological lifespan of phosphate-starved cells PMID:36794724 Figure 5D ang G PMID:36794724 Figure 1B PMID:36794724 Figure 3A PMID:36794724 Figure 3B PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 3C PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 2 PMID:36794724 Figure 6 PMID:36794724 Figure 6 PMID:36794724 Figure 6 PMID:36794724 Figure 6 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S4 PMID:36794724 Figure S3 PMID:36794724 Figure S3 PMID:36794724 Figure S3 PMID:36794724 Figure 8 PMID:36794724 Figure 6, 7, 9 and 10 PMID:36799444 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 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 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 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 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 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 Fig.3D PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Fig.1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Fig.1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Fig.1 PMID:36820394 Fig.1 PMID:36820394 Table 1 PMID:36820394 Table 1 PMID:36820394 Fig.1 PMID:36820394 Fig.1 PMID:36820394 Fig.1 PMID:36820394 Fig.1 PMID:36820394 Fig.1 PMID:36820394 Table 1 PMID:36882296 Fig. 6A PMID:36882296 Fig. 13 PMID:36882296 Fig. 13 PMID:36882296 Fig. 13 PMID:36882296 Fig. 13 PMID:36882296 Fig. 9A PMID:36882296 Fig. 4 PMID:36882296 Fig. 4 PMID:36882296 Fig. 4 PMID:36882296 Fig. 4 PMID:36882296 Fig. 3 PMID:36882296 Fig. 3 PMID:36882296 Fig. 1A. Redundancy with rpb1-T4A PMID:36882296 Fig. S8 PMID:36882296 Fig. S8 PMID:36882296 Fig. S8 PMID:36882296 Fig. S8 PMID:36882296 Fig. S8 PMID:36882296 Fig. S8 PMID:36882296 Fig. S8 PMID:36882296 Fig. S8 PMID:36882296 Fig. S8 PMID:36882296 Fig. S8 PMID:36882296 Fig. S8 PMID:36882296 Fig. S8 PMID:36882296 Fig. S7B PMID:36882296 Fig. S7B PMID:36882296 Fig. S7B PMID:36882296 Fig. S7A PMID:36882296 Fig. S7A PMID:36882296 Fig. S7A PMID:36882296 Fig. S6B PMID:36882296 Fig. S6B PMID:36882296 Fig. S6A PMID:36882296 Fig. S6A PMID:36882296 Fig. S5B PMID:36882296 Fig. S5A PMID:36882296 Fig. S3 PMID:36882296 Fig. S3 PMID:36882296 Fig. S3 PMID:36882296 Fig. S3 PMID:36882296 Fig. S3 PMID:36882296 Fig. S3 PMID:36882296 Fig. S3 PMID:36882296 Fig. S3 PMID:36882296 Fig. S3 PMID:36882296 Fig. S3 PMID:36882296 Fig. S3 PMID:36882296 Fig. S3 PMID:36882296 Fig. S3 PMID:36882296 Fig. S3 PMID:36882296 Fig. S3 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. 12A PMID:36882296 Fig. 12B PMID:36882296 Fig. 12A PMID:36882296 Fig. 9B PMID:36882296 Fig. 7B PMID:36882296 Fig. 12B PMID:36882296 Fig. 12A PMID:36882296 Fig. 11B PMID:36882296 Fig. 11B PMID:36882296 Fig. 11B PMID:36882296 Fig. 11B PMID:36882296 Fig. 11A PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. S4 PMID:36882296 Fig. 10B PMID:36882296 Fig. 10B PMID:36882296 Fig. 10A PMID:36882296 Fig. 6B PMID:36882296 Fig. 6B PMID:36882296 Fig. 6B PMID:36882296 Fig. 6B PMID:36882296 Fig. 6B PMID:36882296 Fig. 6B PMID:36882296 Fig. 6A PMID:36882296 Fig. 6A PMID:36882296 Fig. 6A, 10A PMID:36882296 Fig. 6A PMID:36882296 Fig. 6A PMID:36882296 Fig. 6B PMID:36882296 Fig. 6B PMID:36882296 Fig. 10A PMID:36882296 Fig. 10A PMID:36882296 Fig. 10A PMID:36882296 Fig. 9B PMID:36882296 Fig. 9B PMID:36882296 Fig. 9B PMID:36882296 Fig. 9B PMID:36882296 Fig. 9B PMID:36882296 Fig. 9B PMID:36882296 Fig. 9B PMID:36882296 Fig. 9A PMID:36882296 Fig. 9A PMID:36882296 Fig. 9A PMID:36882296 Fig. 9A PMID:36882296 Fig. 9A PMID:36882296 Fig. 9A PMID:36882296 Fig. 9A PMID:36882296 Fig. 8B PMID:36882296 Fig. 8A PMID:36882296 Fig. 8B PMID:36882296 Fig. 8A PMID:36882296 Fig. 7B PMID:36882296 Fig. 7B PMID:36882296 Fig. 7B PMID:36882296 Fig. 7B PMID:36882296 Fig. 7B PMID:36882296 Fig. 7B PMID:36882296 Fig. 7A PMID:36882296 Fig. 7A PMID:36882296 Fig. 7A PMID:36882296 Fig. 7A PMID:36882296 Fig. 7A PMID:36882296 Fig. 7A PMID:36882296 Fig. 1A PMID:36882296 Fig. 1A PMID:36882296 Figs. 1A, 5A, 6A, 7A, 8A PMID:36882296 Fig. 1A PMID:36882296 Figs. 1B, 5B, 6B, 7B, 8B, 9B, 10B PMID:36882296 Fig. 7A PMID:36882296 Fig. 7B, 10B, 12B PMID:36882296 Fig. 1A PMID:36882296 Fig. 1A PMID:36882296 Fig. 1B PMID:36882296 Fig. 1B PMID:36882296 Fig. 1B PMID:36882296 Fig. 1A PMID:36882296 Fig. 1B PMID:36882296 Fig. 1B PMID:36882296 Fig. 1B PMID:36882296 Fig. 5A PMID:36882296 Fig. 5A PMID:36882296 Fig. 6B PMID:36882296 Fig. 6B PMID:36882296 Fig. 6B PMID:36882296 Fig. 6B PMID:36882296 Fig. 5A PMID:36882296 Fig. 5A PMID:36882296 Fig. 5A PMID:36882296 Fig. 5A PMID:36882296 Fig. 5A PMID:36882296 Fig. 5A PMID:36882296 Fig. 5B PMID:36882296 Fig. 5B PMID:36882296 Fig. 5B PMID:36882296 Fig. 5B PMID:36882296 Fig. 5B PMID:36882296 Fig. 6A PMID:36882296 Fig. 6B PMID:36882296 Fig. 6B PMID:36882296 Fig. 13 PMID:37052630 Main text Table S1 PMID:37052630 Main text Table S1 PMID:37052630 Fig. 2b - control is the overexpressed pka1D with overexpressed wild-type (nmt81) PMID:37052630 Main text Table S1 PMID:37052630 Main text Table S1 PMID:37052630 Fig. 2b - control is the overexpressed pka1D with overexpressed wild-type (nmt81) PMID:37052630 Fig. 2b - control is the overexpressed pka1D with overexpressed wild-type (nmt81) PMID:37052630 Fig. S1 PMID:37052630 Fig. S1 PMID:37052630 Fig. S1 PMID:37052630 Fig. 2b - control is the overexpressed pka1D with overexpressed wild-type (nmt81) PMID:37052630 Fig. 2b - control is the overexpressed pka1D with overexpressed wild-type (nmt81) PMID:37052630 Fig. 2b - control is the overexpressed pka1D with overexpressed wild-type (nmt81) PMID:37052630 Fig. 2b - control PMID:37052630 Main text Table S1 PMID:37076472 Figure 1. PMID:37076472 Figure 3. PMID:37076472 Figure 3. PMID:37076472 Figure 3. PMID:37076472 Figure 3. PMID:37076472 Figure 1. PMID:37076472 Figure 1. PMID:37076472 Figure 1. PMID:37076472 Figure 1. PMID:37076472 Figure 1. PMID:37076472 Figure 1. PMID:37076472 Figure 1. PMID:37076472 Figure 1. PMID:37076472 Figure 3. PMID:37076472 Figure 3. PMID:37099380 Closer to ring PMID:37099380 Closer to tip PMID:37099380 Closer to tip PMID:37120429 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 Using this system, we observed that SpHsp90-EA supported viability of Sz. pombe cells (Fig. 1b). PMID:37120429 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 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 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:37128864 Loss of viability is evident only when cells are exposed to 32 degree before and upon entry into stationary phase. PMID:37128864 Localization depends on Cdc2 kinase activity but not on Clp1. PMID:37128864 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 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 Cell length increases during log and stationary phases at 32 degree. PMID:37128864 The phenotype can be seen at 32 degree. PMID:37156397 Figs. 2B, S1B PMID:37156397 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 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 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 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 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 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 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 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 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 Interestingly, NAD+ reduction activity was clearly detected in purified Coq12-8xHis from S. pombe (Fig. 9A) PMID:37156397 Figs. 2B, S1B PMID:37156397 Figs. 2B, S1B PMID:37156397 The amount of Coq4 was significantly reduced in ∆coq11 and ∆coq12 single mutants PMID:37156397 (Fig. 4) The results revealed higher sulfide levels in both Δcoq11 and Δcoq12 strains PMID:37156397 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 ********growth auxotrophic for para-hydroxy benzoic acid PMID:37156397 (Fig. 2A) By contrast, the ∆coq12 strain showed almost no growth on PMLU medium containing cysteine. PMID:37156397 LC-MS PMID:37156397 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 low CoQ10 level PMID:37156397 The amount of Coq4 was significantly reduced in ∆coq11 and ∆coq12 single mutants PMID:37156397 (Fig. 4) The results revealed higher sulfide levels in both Δcoq11 and Δcoq12 strains PMID:37156397 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 Figs. 2B, S1B PMID:37156397 Figs. 2B, S1B PMID:37156397 Figs. 2B, S1B PMID:37156397 Figs. 2B, S1B PMID:37156397 (Figs. 2A, S1A) Like other mutants lacking CoQ, the ∆coq11 strain showed better growth on cysteine-containing medium. PMID:37156397 LC-MS analysis PMID:37156397 low CoQ10 level PMID:37156397 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 Figs. 2B, S1B PMID:37156397 Figs. 2B, S1B PMID:37156397 Figs. 2B, S1B PMID:37156397 Figs. 2B, S1B PMID:37156397 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:37158439 Figure S1 PMID:37158439 Figure 3C PMID:37158439 Figure 1 PMID:37158439 Figure 1 PMID:37158439 Figure 4A PMID:37158439 Figure 4A PMID:37158439 Figure 4A PMID:37158439 Figure 4C PMID:37158439 Figure 4C PMID:37158439 Figure 4C PMID:37158439 Figure S3 PMID:37158439 Figure S3 PMID:37158439 Figure S3 PMID:37158439 Figure S3 PMID:37158439 Figure S3 PMID:37158439 Figure S1 PMID:37158439 Figure S2 PMID:37158439 Figure S2 PMID:37158439 Figure S2 PMID:37158439 Figure S2 PMID:37158439 Figure S3 PMID:37158439 Figure 4C PMID:37158439 Figure 4C PMID:37158439 Figure 4C PMID:37158439 Figure 4D PMID:37158439 Figure 4D PMID:37158439 Figure 4D PMID:37158439 Figure S1 PMID:37158439 Figure S1 PMID:37158439 Figure S1 PMID:37158439 Figure S1 PMID:37158439 Figure S1 PMID:37158439 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 Figure 2 Fig. 2. fic1-2A myo2-E1 cells can achieve membrane ingression and cell separation at myo2-E1’s restrictive temperature PMID:37158439 Figure 2 PMID:37158439 Figure 4A PMID:37158439 Figure 4A PMID:37158439 Figure 3B PMID:37158439 Figure 3B PMID:37158439 Figure 3C PMID:37158439 Figure 4A PMID:37158439 Figure 3B PMID:37158439 Figure 2 Fig. 2. fic1-2A myo2-E1 cells can achieve membrane ingression and cell separation at myo2-E1’s restrictive temperature PMID:37158439 Figure 3C PMID:37158439 Figure 3C PMID:37158439 Figure 4A PMID:37158439 Figure 2 PMID:37158439 Figure 2 PMID:37158439 Figure 2 PMID:37158439 Figure 1 PMID:37158439 From this screen we observed one significant interaction: fic1’s phospho-ablating mutant, fic1-2A, suppressed myo2-E1 PMID:37158439 From this screen we observed one significant interaction: fic1’s phospho-ablating mutant, fic1-2A, suppressed myo2-E1 PMID:37158439 Figure S3 PMID:37158439 Figure 1B PMID:37158439 Figure 1B. From this screen we observed one significant interaction: fic1’s phospho-ablating mutant, fic1-2A, suppressed myo2-E1 PMID:37158439 Figure 1C PMID:37158439 Figure 1C PMID:37158439 Figure 1E and G PMID:37158439 Figure 1 E and G PMID:37158439 Figure 1E and G PMID:37160462 Phenotype complementation by human RAD23A PMID:37162093 Figure 3AD, Figure 6ACE PMID:37162093 Figure 4BD, Figure 6BDE PMID:37162093 Figure 3BE, Figure 6ACE PMID:37162093 Figure 4AC PMID:37162093 Figure 4AC PMID:37162093 Figure 4AC, Figure 6BDE PMID:37162093 Figure 7 PMID:37162093 Figure 3CF, Figure 6ACE PMID:37162093 Figure 4BD PMID:37162093 Figure 7 PMID:37162093 Figure 7 PMID:37162093 Figure 7 PMID:37162093 Figure 4BD PMID:37162093 Figure 5AB PMID:37162093 Figure 5AB, Figure S3 PMID:37162093 Figure 7 PMID:37162093 Figure 6BDE, Figure S2 PMID:37162093 Figure 7 PMID:37162093 Figure 5AB PMID:37162093 Figure S2 PMID:37162093 Figure S2 PMID:37164017 Growth rate improved by addition of either glutamate, glutamine, or arginine PMID:37164017 Growth rate improved by addition of arginine PMID:37191320 Consistently, Hva22 was observed on the ER under both nitrogen-rich and starvation conditions (Figure 3C). PMID:37191320 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 In hva22Δ cells, reticulophagy was abolished, similar to cells lacking the core autophagy protein Atg1 (Figure 1B). PMID:37191320 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 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 (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 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 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 (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 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 In atg44D cells, mitophagy was completely blocked similarly to cells lacking Atg1, a core autophagy protein (Figures 1A and S1B). PMID:37192628 Based on these results, we conclude that Atg44 localizes in the IMS and is not a transmembrane protein. PMID:37192628 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 As expected, in S. pombe atg44D cellslacking Mgm1, some of the mitochondria became fragmentedand mitophagy was partially rescued (Figures 4A and S3F). PMID:37192628 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 Overexpression of Atg44 in both species caused mitochondrial fragmentation not only in wild-type cells but also in Dnm1-deficient cells (Figures 3E and 3F). PMID:37192628 As expected, in S. pombe atg44D cellslacking Mgm1, some of the mitochondria became fragmentedand mitophagy was partially rescued (Figures 4A and S3F). PMID:37192628 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:37200372 Fig. 6B PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 1 PMID:37200372 Fig. 2 PMID:37200372 Fig. 2 PMID:37200372 Fig. 2 PMID:37200372 Fig. 2 PMID:37200372 Fig. 2 PMID:37200372 Fig. 2 PMID:37200372 Fig. 2 PMID:37200372 Fig. 2 PMID:37200372 Fig. 2 PMID:37200372 Fig. 2 PMID:37200372 Fig. 2 PMID:37200372 Fig. 2 PMID:37200372 Fig. S2 and text PMID:37200372 Fig. S2 and text PMID:37200372 Fig. S2 and text PMID:37200372 Fig. S2 and text PMID:37200372 Fig. 6 PMID:37200372 Fig. 6 PMID:37200372 Fig. 6 PMID:37200372 Fig. 6B PMID:37200372 Fig. 6 PMID:37200372 Fig. 6 PMID:37200372 Fig. 6 PMID:37200372 Fig. 6 PMID:37200372 Fig. 6 PMID:37200372 Fig. 6 PMID:37200372 Fig. 6 PMID:37200372 Fig. 6 PMID:37200372 Fig. 6 PMID:37200372 Fig. 6 PMID:37200372 Fig. 6 PMID:37200372 Fig. S12 PMID:37200372 Fig. S12 PMID:37200372 Fig. S12 PMID:37200372 Fig. S12 PMID:37200372 Fig. S12 PMID:37200372 Fig. 7 PMID:37200372 Fig. 7 PMID:37200372 Fig. 7 PMID:37200372 Fig. 7 PMID:37200372 Fig. 7 PMID:37200372 Fig. 7 PMID:37200372 Fig. 7 PMID:37200372 Fig. 7 PMID:37200372 Fig. 7 PMID:37200372 Fig. 7 PMID:37200372 Fig. 7 PMID:37200372 Fig. 7 PMID:37200372 Fig. 7 PMID:37200372 Fig. 7 PMID:37237082 figure 3a PMID:37237082 Both srr1-D111A,P112A and srr1- H148A mutations reduced GCR rates (Fig. 5d). PMID:37237082 Both srr1-D111A,P112A and srr1- H148A mutations reduced GCR rates (Fig. 5d). PMID:37237082 figure 5e PMID:37237082 figure 5e PMID:37237082 figure 3a PMID:37237082 figure 3a PMID:37237082 figure 3a PMID:37237082 figure 3a PMID:37237082 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 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 Normal Chk1 phosphorylation and cell cycle arrest PMID:37237082 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 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 figure 3a PMID:37237082 figure 3a PMID:37237082 figure 5e PMID:37237082 figure 5e PMID:37237082 figure 5e PMID:37237082 figure 3a PMID:37237082 (Fig. 3e). PMID:37237082 Normal Chk1 phosphorylation and cell cycle arrest PMID:37237082 We crossed srr1Δ and rad52Δ haploid strains and dissected the tetrads but failed to obtain srr1Δ rad52Δ progenies (Fig. 4b), PMID:37237082 We crossed srr1Δ and rad52Δ haploid strains and dissected the tetrads but failed to obtain srr1Δ rad52Δ progenies (Fig. 4b), PMID:37237082 figure 3a PMID:37237082 skb1∆ and srr1∆ additively reduce the rate of gross chromosomal rearrangements in rad51 deletion background. PMID:37237082 figure 5e PMID:37237082 skb1∆ and srr1∆ additively reduce the rate of gross chromosomal rearrangements in rad51 deletion background. PMID:37237082 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 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 (Fig. 6a) In wild-type and rad51 deletion backgrounds PMID:37237082 (Fig. 6a) In wild-type and rad51 deletion backgrounds PMID:37237082 (Fig. 3e). PMID:37237082 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 (Fig. 3e). We found that srr1Δ and srr1-W157R increased the rate of chromosome loss. (In WT and rad51 backgrounds) PMID:37237082 (Fig. 3e). We found that srr1Δ and srr1-W157R increased the rate of chromosome loss. (In WT and rad51 backgrounds) PMID:37237082 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 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 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 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 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 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 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 Figure 2 PMID:37279920 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 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 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:37400983 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 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 mat3M::ura4+ reporter silencing PMID:37400983 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 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 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 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 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 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 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 ****NEED TO FIX allele description*****. The N-terminal disordered region of Swi6 (Swi6-N) bound weakly to DNA (Fig. 2D and L), PMID:37400983 whereas no DNA binding activity was detected for Swi6-CD or Swi6-CSD (Fig. 2E, G and L). PMID:37400983 whereas no DNA binding activity was detected for Swi6-CD or Swi6-CSD (Fig. 2E, G and L). PMID:37400983 Interest- ingly, we found that Chp2 in the chromatin-enriched pellet fraction was not affected by the Mit1I11R mutation (Fig. 1B). PMID:37400983 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 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 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 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 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 mat3M::ura4+ reporter silencing PMID:37400983 mat3M::ura4+ reporter silencing PMID:37400983 Inter- estingly, we found that Chp2-CSD exhibited a robust DNA binding activity (Fig. 2K and M), PMID:37400983 no detectable DNA-binding activity was observed for Chp2-CD (Fig. 2I and M). PMID:37400983 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 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 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:37403782 U6 PMID:37403782 we found that all three proteins are neces- sary for an interaction with U6 (Figure 1A, Supplemen- tary Figure S1B). PMID:37403782 U6 PMID:37403782 U6 PMID:37403782 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 reproducible decrease in modification at several other sites, most notably A64 (Figure 1C, D, Sup- plementary Figure S3). PMID:37403782 we found that all three proteins are neces- sary for an interaction with U6 (Figure 1A, Supplemen- tary Figure S1B). PMID:37403782 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 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 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 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 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 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 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 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 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 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 reproducible decrease in modification at several other sites, most notably A64 (Figure 1C, D, Sup- plementary Figure S3). PMID:37403782 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 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 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 we found that all three proteins are neces- sary for an interaction with U6 (Figure 1A, Supplemen- tary Figure S1B). PMID:37403782 reproducible decrease in modification at several other sites, most notably A64 (Figure 1C, D, Sup- plementary Figure S3). PMID:37531259 Figure S1D (vw: same pathway) PMID:37531259 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 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 Figure 1C PMID:37531259 Figure 1C PMID:37531259 Figure 1C PMID:37531259 Figure 1C PMID:37531259 Figure S1D PMID:37531259 Figure S1D PMID:37531259 Figure 1F PMID:37531259 Figure 1D PMID:37531259 Figure 1C PMID:37531259 Figure 1C PMID:37531259 Figure 1C PMID:37531259 Figure S1D PMID:37531259 Figure S1D PMID:37531259 Figure 1C PMID:37531259 Figure 1C PMID:37531259 Figure S1C PMID:37531259 Figure S1C PMID:37531259 Figure S1A PMID:37531259 Figure S1B PMID:37531259 Fig. 1, Fig. 1B, Fig. 2D PMID:37531259 Figure 1C &F PMID:37531259 Figure 3C PMID:37531259 Figure 3E PMID:37531259 Figure 3E PMID:37531259 Figure 3C PMID:37531259 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 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 Figure 3A PMID:37531259 Figure 1E PMID:37531259 Figure 1E PMID:37540145 Figure 4G PMID:37540145 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 Figure 4F mitochondrial net-like morphology PMID:37540145 Figure 4G PMID:37540145 Figure 4F mitochondrial net-like morphology PMID:37540145 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:37550452 Figure 6 PMID:37550452 Extended Data Figure 9e PMID:37550452 Figure 5 PMID:37550452 Figure 5 PMID:37550452 Figure 5 PMID:37550452 Figure 6 PMID:37550452 Figure 6 PMID:37550452 Figure 6 PMID:37590302 Figure 1 PMID:37590302 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 increased 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 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 Quantification showed that the expression levels of endogenous Dnm1 were comparable in WT and yta4Δ cells (Fig 3B) PMID:37590302 Yta4(EQ) impaired the for- mation of Dnm1 foci on mitochondria but unexpectedly caused mitochondria to aggregate (Figs 4D and S1C) PMID:37590302 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 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 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 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 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 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 Figure 1 PMID:37590302 Hence, these results show the character- istic property of Yta4 in reducing the affinity of Dnm1 for GTP and in inhibiting Dnm1 assembly. PMID:37637271 Figure 1H PMID:37637271 Figure 1E PMID:37637271 Figure 1D PMID:37637271 Figure 1H PMID:37637271 Figure 1G PMID:37637271 Figure 1H PMID:37637271 Figure 1D PMID:37637271 Figure 1H PMID:37637271 Figure 1E PMID:37637271 Figure 1G PMID:37637271 Figure 1E PMID:37637271 Figure 1E PMID:37637271 Figure 1E PMID:37637271 Figure 1E PMID:37637271 Figure 1E PMID:37637271 Figure 1E PMID:37746062 Figure1 G-H PMID:37746062 Figure1 G-H PMID:37746062 Figure1 G-H PMID:37746062 Figure 1G-H PMID:3870979 done in h- cells kinetics depend on medium composition (see fig 6B) PMID:3870979 at 33.5 degrees, which is restrictive for cdc2-33 but allows sporulation PMID:3870979 at 33.5 degrees, which is restrictive for cdc2-33 but allows sporulation PMID:3870979 at 33.5 degrees, which is restrictive for cdc10-129 but allows sporulation PMID:3870979 homozygous diploid PMID:3870979 homozygous diploid PMID:3870979 homozygous diploid PMID:3870979 homozygous diploid PMID:3870979 homozygous diploid PMID:3870979 at 33.5 degrees, which is restrictive for cdc10129 but allows sporulation PMID:3870979 Saccharomyces LEU2 used for disruption PMID:4154968 "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 activated by ATP PMID:4698209 inhibited_by CHEBI:17191 PMID:4698210 inhibited_by CHEBI:27266 PMID:4708672 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 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 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 activated_by FAD , inhibited_by L-valine PMID:6094012 parent child relationship with term above requested PMID:6094012 actually this only occurs in 30% of cells.. I don't know if it is viable or inviable PMID:6526818 inhibited by methionine PMID:6828164 cell size at septation is 8.4µm PMID:6828164 cell size at septation is 8.5µm PMID:6828164 "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 fig1A TTable 1 cdc27 transition point is 0.62 using a cdc27.K3 mutant PMID:6828164 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 fig1A The transition point for cdc2 is 0.65 using cdc2.33 PMID:6828164 fig1A The transition point for cdc2 is 0.68 using cdc2.L7 PMID:6828164 fig1A The transition point for cdc2 is 0.70 using cdc2.M63 PMID:6828164 fig1A The transition point for cdc2 is 0.65 using cdc2.M26 PMID:6828164 fig1A The transition point for cdc2 is 0.66 using cdc2.M35 PMID:6828164 fig1A The transition point for cdc2 is 0.65 using cdc2.M55 PMID:6828164 fig1A The transition point for cdc2 is advanced from 0.69 to 0.48 using a cdc2.33 wee1 [more...] PMID:6828164 The transition point for cdc2 is advanced from 0.68 to 0.47 using a cdc2.L7 wee1.6 mutant PMID:6828164 The transition point for cdc2 is advanced from 0.65 to 0.53 using a cdc2.M26 wee1.6 mutant PMID:6828164 fig1A PMID:6828164 fig1A The transition point for cdc2 (0.68) is not advanced using a cdc2.M63 wee1.6 mutant PMID:6828164 The transition point for cdc1 is advanced in a cdc1.P13 wee1.6 mutant from 0.62 to 0.33. An asynchronous population of a cdc1-P13 wee1.6 mutant was shifted from 25°C to the restrictive temperature of 36°C to inactivate the cdc1 gene and the number of cells that went on to divide was increased compared to a cdc1-7 mutant PMID:6828164 fig1A Table 1 cdc13 transition point is 0.69 using a cdc13-117 mutant PMID:6828164 cell size at septation is 10.3µm PMID:6828164 fig1A Table 1 cdc13 transition point (0.78) is not advanced in a cdc13-117 wee1.6 mutant PMID:6828164 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 TP. 0.33 PMID:6828164 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 fig1A The transition point for cdc2 (0.74) is not advanced using a cdc2.M35 wee1.6 mutant PMID:6828164 cell size at septation is 9.6µm PMID:6828164 cell size at separation is 22.4µm compared to 12.8µm for wild type PMID:6828164 cell size at separation is 16.7µm compared to 12.8µm for wild type PMID:6828164 ??? PMID:6828164 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 cell size at septation is 9.5µm in cdc2-1w (9.7µm in cdc2-2w) PMID:6828164 cell size at septation is 8.7µm PMID:6828164 cell size at septation is 8.9µm PMID:6828164 cell size at septation is 8.9µm PMID:689088 at division PMID:6943408 abolished PMID:6943408 abolished DNA replication PMID:6961452 This was really IGI complemetnation of E-coli pyrB PMID:7262540 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 cells divide at 51% of control cell length at division PMID:7262540 cells divide at 75% of wild type diploid cell length at division at 25°C PMID:7262540 cells divide at 9% longer than wild diploid cells at division PMID:7262540 cells divide at 8% longer than wild diploid cells at division PMID:7262540 cells divide at 10% longer than wild diploid cells at division PMID:7262540 cells divide at 6% longer than wild diploid cells at division PMID:7262540 cells divide at 11% longer than wild diploid cells at division PMID:7262540 cells divide at 11% longer than wild diploid cells at division PMID:7262540 cells divide at 10% longer than wild diploid cells at division PMID:7262540 cells divide at 12% longer than wild diploid cells at division PMID:7262540 cells divide at 7% longer than wild diploid cells at division PMID:7262540 cells divide at 82% of wild diploid size at division PMID:7262540 cells divide at 56% of the size at division of wild type diploids PMID:7262540 Cells divide at 65% of wild type diploid cell length PMID:7262540 cells divide at 16.7µm at 25°C PMID:7262540 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 cells divide at 10.2µm at 25°C PMID:7262540 cells divide at 22.4µm at 25°C PMID:7262540 cdc2-1w was previously called wee2-1 PMID:7262540 cells septate at 56% of wild type diploid length PMID:7262540 cells septate at 58% of wild type diploid length PMID:7262540 cells septate at 54% of wild type diploid length PMID:7262540 cells septate at 58% of wild type diploid length PMID:7262540 cells septate at 52% of wild type diploid length PMID:7262540 cells septate at 81% of wild type diploid length PMID:7262540 cells septate at 82% of wild type diploid length PMID:7262540 cells septate at 85% of wild type diploid length PMID:7262540 cells septate at 77% of wild type diploid length PMID:7262540 cells septate at 87% of wild type diploid length PMID:7498507 activated_by(CHEBI:16356) PMID:7501024 non-ionic osmotic stress PMID:7501024 salt stress PMID:7501024 salt stress PMID:7501454 hyperphosphorylated in late S phase; phosphorylated on different sites in S versus G2/M PMID:7501454 constant throughout cell cycle PMID:7501454 higher affinity during S phase than G2/M PMID:7559598 not shown PMID:7559598 not shown PMID:7588609 heterozygous diploid PMID:7596817 polysome profile PMID:7596817 polysome profile PMID:7622618 evidence is essentially IC, as I inferred sterility from the lack of shmoo formation (h- cells) PMID:7626804 data not shown PMID:7626804 Fig1A PMID:7626804 Fig 4A right panel cells average size 16.6µm This strain is a gene replacement of cdc2+ PMID:7626804 Fig 4B absence of peptide 3 This strain is a gene replacement of cdc2+ PMID:7626804 Fig 4B middle right panel presence of peptide 3 This strain is a gene replacement of cdc2+ PMID:7626804 Fig 4B absence of peptide 3 Overexpression of wee1 does not phosphorylate T14A residue. This strain is a gene replacement of cdc2+ PMID:7626804 Fig 4B increased peptide 3 compared to when wee1 is not overexpressed . This strain is a gene replacement of cdc2+ PMID:7626804 Fig5 B wee1 is necessary for T14 phosphorylation no peptide 3 is observed when wee1 is deleted PMID:7626804 Fig7A,B At restrictive temperature T14 is not phosphorylated (no peptide when cells blocked at RT.) PMID:7626804 Fig7A, B At shift to permissive temperature T14 becomes phosphorylated. Peptide 3 is only present at low stoichiometry PMID:7626804 Fig8 PMID:7626804 Fig8 PMID:7626804 Fig3 chk1 1 is not required for T14 phosphorylation by wee1 PMID:7626804 Fig1D peptide 2 PMID:7626804 Fig1B, C and D x = a small phospho peptide of T14Y15. T14 phosphorylation only occurs when wee1 is overexpressed PMID:7626804 Fig1D peptide 3 and peptide1 PMID:7626804 Fig1D peptide 3 PMID:7626804 Table 2 cdc2-T14A is present on multicopy plasmid cells are viable and have a normal cell size phenotype PMID:7626804 Table 2 cdc2-T14A is present on multicopy plasmid cells are viable but have a semi wee phenotype PMID:7626804 Fig 4A middle panel cells average size 11.6µm This strain is a gene replacement of cdc2+ PMID:7651412 switches specificity from direct repeats to inverted repeats PMID:7651414 matmi and matpi PMID:7651414 matmi and matpi PMID:7651414 matmi and matpi PMID:7651414 matmi and matpi PMID:7651414 matmi and matpi PMID:7657164 residue not determined, but probably Y173 PMID:7687541 fig4 PMID:7706287 assayed for bulk poly(A)+ RNA PMID:7706287 assayed for bulk poly(A)+ RNA PMID:7706287 arrest point determined by H1 kinase activity peak PMID:7739540 (Figure 3b) PMID:7739540 (Figure 3b) PMID:7739540 (Figure 3b) PMID:7773104 NADP-GDH-defective PMID:7774573 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 pREP5cdc2-DL41 is integrated. cdc2-DL45 has same phenotype but it is not clear if it is under the same conditions PMID:7774573 pREP5cdc2-DL41 is integrated. cdc2-DL45 has same phenotype but it is not clear if it is under the same conditions PMID:7774573 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 pREP5cdc2-DL41 is integrated. cdc2-DL45 has same phenotype but it is not clear if it is under the same conditions PMID:7774573 pRIP45cdc2-DL41 is integrated PMID:7774573 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 pREP41cdc2-DL50 is integrated PMID:7774573 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 pREP41cdc2-DL50 is integrated PMID:7774573 pREP5-DL41 is integrated. cdc2+ is expressed from its own promoter on a multi copy plasmid PMID:7774573 pREP5-DL45 is integrated. cdc2+ is expressed from its own promoter on a multi copy plasmid PMID:7774573 pREP41-DL50 is integrated PMID:7774573 pREP41cdc2-DL50 is integrated PMID:7774573 pREP41cdc2-DL50 is integrated PMID:7774573 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 pRIP45cdc2-DL45 is integrated PMID:7774573 pRIP45cdc2+ is integrated PMID:7774573 pREP41cdc2-DL45 is a multi copy plasmid . No data shown PMID:7774573 pREP41cdc2-DL45 is a multi copy plasmid. No data shown PMID:7774573 pREP41cdc2-DL41 is a multi copy plasmid . No data shown PMID:7774573 pREP41cdc2-DL41 is a multi copy plasmid . No data shown PMID:7774573 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 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 pREP5cdc2-DL41 is integrated. cdc2-DL45 has same phenotype but it is not clear if it is under the same conditions PMID:7796804 Fig5A PMID:7796804 Fig 6, Fig7B panel 8, PMID:7796804 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 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 Fig 6 bottom panels Fig7B panel 6 cells examined 7 hour after refeeding with nitrogen PMID:7796804 Fig 6 bottom panels Fig7B panel 5 cells nitrogen starved and examined 7 hour after refeeding with nitrogen PMID:7796804 Fig 7C PMID:7796804 Fig 6 top panels, Fig7B panel 1 cells examined 7 hour after refeeding with nitrogen PMID:7796804 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 Fig7A panel 2 PMID:7796804 Fig7A panel 1 PMID:7796804 Fig7A panel 6 PMID:7796804 Fig7A panel 3 PMID:7796804 Fig7A panel 5 PMID:7796804 Fig5B cdc10-129 cells blocked in G1 PMID:7796804 Figure 1, 4,5 PMID:7796804 Fig7A panel 4 PMID:7796804 Figure 1, 4,5 PMID:7796804 Fig7C PMID:7796804 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 Fig 7C PMID:7796804 Figure 1, 4,5 PMID:7796804 Fig7A 8, PMID:7796804 Fig 5B cdc22-M45 blocks in G1/S PMID:7796804 Fig 6 middle panels Fig7B panel 4 cells examined 7 hour after refeeding with nitrogen PMID:7796804 Fig 6 middle panels Fig7B panel 3 cells examined 7 hour after refeeding with nitrogen PMID:7796804 Fig 5B cdc22-M45 blocked in G1/S PMID:7796804 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 Fig 5A PMID:7796804 Fig 5A PMID:7796804 Figure 1, 4,5 PMID:7813446 not arrested like wee1-50 overexp alone PMID:7813446 higher than wee1 not overexp, but lower than wee1-50 overexp in wt bkg PMID:7813446 not arrested like wee1-50 overexp alone PMID:7813446 not arrested like wee1+ overexp alone PMID:7859738 Figure 4 PMID:7859738 Figure 4 PMID:7859738 Figure 4 PMID:7859738 Figure 4 PMID:7859738 Figure 4 PMID:7859738 Figure 4 PMID:7859738 Figure 4 PMID:7876257 endoglycosidase-H cleaves N-linked glycosylation PMID:7883794 Table 1, Figure 2C PMID:7883794 Figure 2B PMID:7883794 Table 1, Figure 1B appearance of IC peak at early timepoint PMID:7883794 Figure 1A PMID:7883794 Fig1 B PMID:7883794 Figure 3B PMID:7883794 Data not shown PMID:7883794 Figure 3A PMID:7883794 Figure 2C PMID:7889932 crystal structure PMID:7903653 ABOLISHED PMID:7903653 ABOLISHED PMID:7903653 ABOLISHED PMID:7909513 3 kb transcript PMID:7909513 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:7916653 deletion with expressed plasmid, after plasmid loss PMID:7916658 constitutive cdc18+ expression PMID:7916658 constitutive cdc18+ expression PMID:7916658 inferred from combination of phenotype shown in this paper with background knowledge PMID:7916658 constitutive cdc18+ expression PMID:7923372 they interacted in the Y2H experiment, so inferring this relationship PMID:7957097 inhibits PMID:7957097 no mitotic spindle PMID:7957098 same as rad4 cut5 allele alone PMID:7957098 same as cdc10-129 alone PMID:7957098 same as cdc2-33 alone PMID:7957098 same as cdc13-117 alone PMID:7957098 same as rad4 cut5 allele alone PMID:7957098 same as rad4 cut5 allele alone PMID:7957098 same as rad4 cut5 allele alone PMID:7957098 same as cdc25-22 alone PMID:7957098 same as rad4 cut5 allele alone PMID:7957098 same as rad4 cut5 allele alone PMID:7957098 same as rad4 cut5 allele alone PMID:7957098 same as rad4 cut5 allele alone PMID:7957098 same as rad4 cut5 allele alone PMID:7975894 increased transcription from TR box SO:0001858 PMID:7975894 increased transcriptional response to nitrogen starvation PMID:7975894 increased transcriptional response to nitrogen starvation PMID:7983142 33 degrees (may be standard for them) PMID:7983142 33 degrees (may be standard for them) PMID:7983142 33 degrees (may be standard for them) PMID:7983142 33 degrees (may be standard for them) PMID:7983142 33 degrees (may be standard for them) PMID:7983142 33 degrees (may be standard for them) PMID:7983142 33 degrees (may be standard for them); morphology same as ppe1delta alone PMID:8006074 fig8 PMID:8006074 fig8 PMID:8006074 fig8 PMID:8006074 fig8 PMID:8026462 assayed using casein PMID:8039497 also some genetic interactions that cannot be described with biogrid PMID:8039497 also some genetic interactions that cannot be described with biogrid PMID:8039497 unstable plasmid loss experiment PMID:8087848 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 cdc13delete cells were kept alive by episomal pSM2 cdc13. Cell phenotype was observed after plasmid loss. Figure 2C PMID:8087848 cells are induced to increase their ploidy by a specific treatment e.g. heat shock or drug treatment PMID:8087848 cells are induced to increase their ploidy by a specific treatment e.g. heat shock or drug treatment PMID:8087848 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 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 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 cells are induced to increase their ploidy by a specific treatment e.g. heat shock or drug treatment PMID:8087848 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:8187760 same as cdc2-33 alone PMID:8187760 same as cdc25-22 alone PMID:8187760 grows in three dimensions instead of just at cell ends PMID:8187760 assayed in vitro using casein PMID:8196631 NEG REG OF PHEROMONE RESPONSE MAPK PMID:8223442 fig 1 PMID:8223442 fig 1 PMID:8227198 response curve differs from wt and other git mutants PMID:8264625 casein substrate PMID:8264625 casein substrate (vw changed from GO:0004674 with contributes to) PMID:8292390 same as cps8-185 alone PMID:8299169 C868T (nt) PMID:8319772 present throughout cell cycle PMID:8334988 binucleate fypo/issues/#2400 fypo/issues/#2401 PMID:8346915 inhibiyted by CHEBI:43040 PMID:8413241 tyrosine; residue not determined PMID:8413241 tyrosine; residue not determined PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 Table1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 partially supresses the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 Fig 2 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 partially suppresses the ts phenotype PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 surpresses the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 partially supresses the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table1 mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 mutant expressed from multi copy plasmid has dominant negative phenotype Table 1 PMID:8437586 mutant expressed from multi copy plasmid has dominant negative phenotype Table 1 PMID:8437586 Table 1 mutant expressed from multi copy plasmid has dominant negative phenotype Table 1 PMID:8437586 Table 1 mutant expressed from multi copy plasmid has dominant negative phenotype Table 1 PMID:8437586 mutant expressed from multi copy plasmid has dominant negative phenotype Table 1 PMID:8437586 mutant expressed from multi copy plasmid has dominant negative phenotype Table 1 PMID:8437586 mutant expressed from multi copy plasmid has dominant negative phenotype Table 1 PMID:8437586 mutant expressed from multi copy plasmid has dominant negative phenotype Table 1 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 partially supresses the ts phenotype PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 give partial suppression PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 no suppression PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 no suppression PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 no suppression PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 no suppression PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 no suppression PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Fig 4 nmt1 promoter ON PMID:8437586 Fig 4 nmt1 promoter ON PMID:8437586 Table 1 nmt1 promoter ON PMID:8437586 Table 1 nmt1 promoter ON PMID:8437586 Fig 4 Table 1 nmt1 promoter ON PMID:8437586 Fig 4 Table 1 nmt1 promoter ON PMID:8437586 Table 1 Fig 4 nmt1 promoter ON PMID:8437586 Table 1 Fig 4 nmt1 promoter ON PMID:8437586 Table 1 nmt1 promoter ON PMID:8437586 Table 1 nmt1 promoter ON PMID:8437586 Table 1 nmt1 promoter ON PMID:8437586 Table 1 nmt1 promoter ON PMID:8437586 Table 1 nmt1 promoter ON PMID:8437586 Table 1 nmt1 promoter ON PMID:8437586 Fig 5 nmt1 promoter ON PMID:8437586 Fig 5 nmt1 promoter ON PMID:8437586 Fig 5 nmt1 promoter ON PMID:8437586 Table 1 Fig 4 nmt1 ON PMID:8437586 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 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 Fig 5 increased duration of G1 phase PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 Fig 2 mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype PMID:8437586 Table 1, Fig2 mutant gene expressed from multicopy plasmid pIRT2 partially suppresses the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype PMID:8437586 Table 1 mutant expressed from multi copy plasmid pIRT2 PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype PMID:8437586 Table 1 mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype PMID:8443406 NEG REG PHEROMONE RESPONSIVE MAPK CASC PMID:8463273 kinase assay, and hybridization with S. cerevisiae PKC PMID:8485317 like dis1-288 alone PMID:8485317 like dis1-288 alone PMID:8496185 inhibited by P(1),P(5)-bis(5'-adenosyl) pentaphosphate(5-)? PMID:8497322 fig 4 PMID:8497322 fig 3 cells fail to separate and are clupmed together, multiple rounds of nuclear division PMID:8497322 fig 2 c PMID:8497322 fig 2 c PMID:8497322 fig 3 fypo/issues/2818 PMID:8497322 fig 3 fypo/issues/2818 PMID:8497322 fig 3 PMID:8497322 partial rescue of chk1, fig 2 b PMID:8497322 fig 2a DROPS TO ZERO PMID:8497322 fig 2 c PMID:8497322 data not shown PMID:8497322 fig 3 a PMID:8497322 fig 2 c PMID:8497322 fig 2a PMID:8515818 data not shown ref16 PMID:8515818 (directly inhibits) Fig4a,b together with data from fig 2,3 PMID:8515818 Fig2b 2x serine phos to T phos PMID:8515818 Fig 2b PMID:8515818 Fig2b PMID:8515818 Fig1b top R panel, top cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor PMID:8515818 Fig1b top R panel bottom L cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor PMID:8515818 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 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 Fig1b bottom R panel, top PMID:8515818 Fig1b top R panel bottom L cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor PMID:8515818 Fig1b top R panel, top cdc25 is constituitively OP behind ADH promoter and nim1 is behind thiamine repressible promotor PMID:8515818 Fig2a lane1 PMID:8515818 Fig2a lane 3 PMID:8515818 Fig2b, PMID:8515818 Fig1b bottom R panel, top PMID:8515818 Fig1b bottom R panel, bottom L PMID:8515818 Fig1b bottom R panel, bottom L PMID:8515818 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 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:8521469 same as cdc18+ oe alone PMID:8521469 same as cdc18+ oe alone PMID:8521500 [ move to specific cyclin] Fig6 2.6nM rum1 inhibits cig2 associated cdc2 kinase activity by ~50% PMID:8521500 Fig5B over expression abolishes cdc13 associated kinase activity even in absence of added rum1 protein PMID:8521500 FigB over expression reduces cdc2 kinase activity even in absence of added rum1 protein PMID:8521500 Fig5A PMID:8521500 Fig5A PMID:8521500 Fig 3C PMID:8521500 Fig 3C PMID:8521500 Fig3A PMID:8521500 Fig3A PMID:8521500 Fig3A PMID:8521500 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 Fig3B PMID:8521500 Fig3A PMID:8521500 Fig3A PMID:8521500 Fig3B PMID:8521500 Fig2C rum1+ driven by nmt1 promoter in pREP6X is integrated PMID:8521500 [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 Fig1 Histone H1 used as substrate PMID:8521500 Fig 1 Histone H1 used as substrate PMID:8521500 Fig 6 cdc2-cig1 complex is insensitive to inhibition by rum1. There is ~100% activity in the presence of 26nM rum PMID:8522609 same as cdc2-33 alone PMID:8522609 same as orb3-167 alone PMID:8522609 same as orb2-34 alone PMID:8522609 same as orb2-34 alone PMID:8522609 same as orb3-167 alone PMID:8522609 same as orb3-167 alone PMID:8552670 , activated_by(CHEBI:18420) PMID:8557036 assayed in S. cerevisiae cell extracts, with S.c. CTD substrate PMID:8557036 assayed in S. cerevisiae cell extracts, with S.c. CDK2 substrate PMID:8557037 activated_by(CHEBI:63041) PMID:8569679 fig2 PMID:8569679 fig2 PMID:8569679 fig2 PMID:8569679 fig2 PMID:8569679 fig2 PMID:8569679 fig2 PMID:8569679 fig2 PMID:8569679 fig2 PMID:8590464 inhibited_by L-lysine PMID:8590474 partial rescuie PMID:8618924 also inferred from orthology to all other Orc1s in the world PMID:8621436 transient phenotype, they then attempt to divide without segregation PMID:8621436 they show it is not abnormal regulation of rereplication in cdc25 double mutant expts PMID:8621436 they show it is not abnormal regulation of rereplication in cdc25 double mutant expts PMID:8621436 transient phenotype, they then attempt to divide without segregation PMID:8621436 transient phenotype, they then attempt to divide without segregation PMID:8621436 transient phenotype, they then attempt to divide without segregation PMID:8649397 Can't say if they are viable vegetative because it is in a pyp2+ background PMID:8654750 PHEROMONE PMID:8668131 func comps S cer ABC1 PMID:8688826 Val: changed from nuclear lumen to nuclear periphery PMID:872890 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 Table 1, Fig1 PMID:872890 Table 1, DNA replication initiated at low protein content PMID:872890 Table 1 PMID:872890 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 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 Fig 2 This shows that wee1-50 has a direct effect on the G2-M transition because cells now at the permissive temperature (active wee1) detect that they are too small to enter mitosis and the G2/M transition is inhibited PMID:872890 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 Table 1, Fig1 PMID:8799335 present with ammonium, allantoin, or proline nitrogen source PMID:8799851 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 Fig 9 PMID:8799851 Fig10 PMID:8799851 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:8811082 thymine glycols, urea PMID:8811082 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 also has AP1 binding site PMID:8834798 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 Fig2 PMID:8876193 Fig4 PMID:8876193 Fig3 PMID:8876193 Fig3 PMID:8876193 73% asymmetric distribution at old end by 5 hours asymmetric mitochondrial aggregation at old cell end PMID:8876193 data not shown PMID:8876193 data not shown, cells blocked at G1/S, cells need to complete cell cycle to observe asymmetry PMID:8876193 data not shown, cells blocked in S phase, cells need to complete cell cycle to observe asymmetry PMID:8876193 Fig 1 77% asymmetric distribution by 5 hours, aggregation observed after 1 hour PMID:8876193 data not shown, cells blocked at G2/M, cells need to complete cell cycle to observe asymmetry PMID:8876193 data not shown, cells blocked in absence of septation, cells need to complete cell cycle to observe asymmetry PMID:8876193 Fig2 1% of cells still have a short mitotic spindle after 5h at restrictive temperature PMID:8879048 NEG REG PHEROMONE MAPK PMID:8918598 ubiquitin conjugate PMID:8918598 ubiquitin conjugate PMID:8918880 fig 1 PMID:8918880 fig 1 PMID:8918880 fig 5 PMID:8918880 fig 1 PMID:8918880 fig 1 PMID:8943330 not sure this annotation is 100% supported, can revise later if needed. PMID:8943330 tyrosine; position(s) not determined PMID:8946912 fig 2a PMID:8946912 fig 2a PMID:8946912 fig 2a PMID:8946912 fig 3 PMID:8978670 figure 1 PMID:8978670 figure 1 PMID:8978670 figure 1 PMID:8978670 figure 1 PMID:8978687 figure 2 PMID:8978687 fig 7 PMID:8978687 fig 6 a PMID:8978687 fig 6 a PMID:8978687 fig 6 a PMID:8978687 fig 6 c PMID:8978687 figure 6 PMID:8978687 figure 5 PMID:8978687 figure 5 PMID:8978687 figure 5 PMID:8978687 figure 5 PMID:8978687 fig 4 b PMID:8978687 figure 1a PMID:8978687 fig 7 PMID:9024682 sporulation of homozygous diploid PMID:9024682 sporulation of homozygous diploid PMID:9024682 severe when both cells are cpb1delta PMID:9034337 Fig 3B PMID:9034337 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 Fig 5, Fig6 PMID:9034337 Fig 4, PMID:9034337 Data not shown chk1+ over expression phenotype is suppressed by over expressing cdc25+ independently of cdr1 PMID:9034337 Fig 3B PMID:9034337 Fig 3A PMID:9034337 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 Fig 3C cell elongation as a result of chk1 over expression is dependent on wee1+ PMID:9034337 Fig 2 D PMID:9034337 Fig 2 D PMID:9034337 Fig 2 A PMID:9034337 Fig 2C PMID:9034337 Fig 2B Histone H1 used as cdc2 substrate Chk2 expressed from nmt1 promoter PMID:9034337 Fig1 PMID:9042863 dephosphorylation of Cdc2 Y15 by Cdc25 delayed in response to ionising radiation PMID:9042863 temperature restrictive for wee1-50 PMID:9042863 temperature permissive for wee1-50; unirradiated PMID:9042863 Activity inhibited in response to mitotic G2 DNA damage checkpoint PMID:9062192 mei2 promotes g1 arrest, premeiotic dna replication and meiosis I PMID:9078365 homozygous diploid PMID:9078390 fig 3a PMID:9078390 fig 2 C PMID:9078390 fig 3a PMID:9078390 fig 3a PMID:9078390 fig 2 C PMID:9078390 fig 3a PMID:9078390 fig 2 C PMID:9078390 fig 2 C PMID:9078390 fig 2 C PMID:9078390 fig 3a PMID:9078390 fig 2 C PMID:9090050 inhibition by CCCP and DCCD PMID:9105045 cdc12 froms a cortical spot PMID:9111307 not sure if this is the right term, sent a question PMID:9125114 also increased (WT overexppression) normal (WT) PMID:9135147 tyrosine; residue not determined PMID:9135148 inferring that residue is Y15, though not shown experimentally PMID:9136929 not annotated to other stresses as subsequent papers show it is critical for assembly of signaling MAPKKK-MAPKKmodule PMID:9153313 same as rad3delta alone PMID:9153313 same as crb2delta alone PMID:9153313 same as rad26delta alone PMID:9154834 residue not determined, but probably Y173 PMID:9154834 residue not determined, but probably Y173 PMID:9154834 doesn't resume normally PMID:9154838 has condensed chromosomes PMID:9177184 as cyclin-CDK complex with Cdc13 or Cig2 PMID:9182664 this might be dumbbell ask Jacky PMID:9182664 swollen PMID:9182664 swollen PMID:9191273 PHEROMONE MAPK PMID:9200612 Fig1C iii PMID:9200612 Fig1C ii PMID:9200612 Fig1C iii PMID:9200612 data not shown PMID:9200612 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 data not shown. tea1 on multi copy plasmid -R2 suppresses the cell shape defect of tea1 delta PMID:9200612 Fig2B C PMID:9200612 Fig 2B,C PMID:9200612 Fig 2C protein localised to both cell tips PMID:9200612 Fig 2C Protein localised to both cell tips during monopolar growth PMID:9200612 Fig 2D Protein localised to both cell tips during monopolar growth PMID:9200612 Fig3A PMID:9200612 Fig3A PMID:9200612 Fig4 A PMID:9200612 Fig4 A PMID:9200612 Fig4 A PMID:9200612 Fig4 A PMID:9200612 Fig5 shown using TBZ treatment and wash out and by cold shock and relocalization PMID:9200612 Fig5C PMID:9200612 Fig5C PMID:9200612 Fig5C PMID:9200612 Fig5C cells blocked in mitosis so have no interphase MTs PMID:9200612 Fig 6D PMID:9200612 Fig6D PMID:9200612 Fig1C ii PMID:9200612 Fig1C iii PMID:9201720 physically interacts with and IMP evidence PMID:9201720 physically interacts with and IMP evidence PMID:9201720 not shown that it is ser/thr kinase activity, just that it is kinase activity PMID:9211982 truncated Gar2 accumulates in this dense body PMID:9252327 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:9252327 Cells look normal in early generation, but show many elongated cells in later generation due to telomere shortening. PMID:9252327 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 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 Cells show progressive telomere shortening. PMID:9252327 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:9278510 fig 2 b PMID:9278510 fig 1 PMID:9278510 fig 2 b PMID:9285594 Fig 1 PMID:9285594 Fig 1 PMID:9285594 in vitro PMID:9287302 vw: I deleted accidintally , then readded PMID:9287302 vw: I deleted accidintally , then readded PMID:9301023 (Figure 2b) PMID:9301023 (Figure 2a) PMID:9301025 just getting the allele in the database (they used it in the exp) PMID:9303310 Fig2 PMID:9303310 Fig7B PMID:9303310 Fig2, Fig3 PMID:9303310 Fig2, Fig3 PMID:9303310 Fig5 (vw, I edited the extensions) PMID:9303310 Fig 8 added by cig1 associated CDK1 PMID:9303310 Fig7A PMID:9303310 Fig2 PMID:9303310 Fig 1 exponentially growing cells mainly in G2 PMID:9303310 Fig 1 cells blocked in G1 at the restrictive temp PMID:9303312 Fig8 C PMID:9303312 Fig 1A and C cdc18 transcription is not dependent on cdc2 function PMID:9303312 Fig 1 B cdc2-M26 has no detectable kinase activity in G1 at restrictive temperature PMID:9303312 Fig 1D cdc2-M26 does not enter S phase even though cdc18 transcription is presence PMID:9303312 Fig2 B PMID:9303312 Fig2 B PMID:9303312 Fig2 B cells do not undergo re replication at restrictive temperature PMID:9303312 Fig2A cells do not undergo re replication at restrictive temperature but cdc18 transcript increases PMID:9303312 Fig2 B PMID:9303312 Fig3A cdc18 transcript accumulates in absence of cig1, cig2 and cdc13 PMID:9303312 Fig3A cdc18 transcript accumulates in absence of cdc13 PMID:9303312 Fig3B cdc18 protein accumulates in absence of cig1, cig2 and cdc13 PMID:9303312 Fig3C no DNA replication in absence of all 3 cyclins PMID:9303312 Fig3C DNA replication in presence of cig1 and cig2 PMID:9303312 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 Fig3C, D Absence of cdc2 kinase activity in absence cig1, cig2 and cdc13 PMID:9303312 Fig3C, D cdc13 promoter ON cdc2 kinase activity acts after the accumulation of cdc18 protein to bring about the G1/S transition PMID:9303312 Fig4B decreased cdc18 transcript level as cells proceed through S phase and G2 and increases as cell go though G1 PMID:9303312 Fig 4C Cdc2 not required for active cdc10 dependent transcription during S phase PMID:9303312 Fig 4C Cdc18 transcript is low during G2 PMID:9303312 Fig 4C Cdc18 transcript is low during G2 PMID:9303312 Cdc2 kinase activity is low during G2 data not shown PMID:9303312 Fig 4D PMID:9303312 Fig 4D PMID:9303312 Fig5A, B decreased cdc18 transcript in HU block and on release PMID:9303312 Fig5A decreased cdc18 transcript in HU block and on release PMID:9303312 Fig5A, B decreased cdc18 transcript in HU block and on release PMID:9303312 Fig5A, B level of cdc18 transcript does not decreased after release from HU block PMID:9303312 Fig 5C PMID:9303312 Fig5C rep2delta has no effect on cdc18 transcript levels in the absence of res2 PMID:9303312 Fig6A cdc18 transcript maximal around peak of septation PMID:9303312 Fig6C PMID:9303312 Fig6C PMID:9303312 Fig6D PMID:9303312 Fig6D PMID:9303312 Fig6B PMID:9303312 Fig6B PMID:9303312 Data not shown PMID:9303312 Fig7 res1 on multi copy pREP3X ON PMID:9303312 Fig7 res1 on multi copy pREP3X ON PMID:9303312 Fig7 res1 on multi copy pREP3X ON PMID:9303312 Fig7 PMID:9303312 Fig7 res2 on multi copy pREP3X ON PMID:9303312 Fig7 res2 on multi copy pREP3X ON PMID:9303312 Fig8 DSC1 is now called MBF PMID:9303312 Fig8B DSC1 is now called MBF PMID:9303312 Fig8 DSC1 is now called MBF PMID:9303312 Fig8B DSC1 is now called MBF PMID:9303312 Fig 5, 6, 7, PMID:9303312 Fig 5, 6, 7, PMID:9303312 Fig8 Presence of MBF is correlated with cdc10 dependent transcription repression during G2 PMID:9303312 Fig8 Presence of MBF is correlated with cdc10 dependent transcription repression during G2 PMID:9303312 Fig8 Presence of MBF is correlated with cdc10 dependent transcription repression during G2 PMID:9303312 Fig8 Presence of MBF is correlated with cdc10 dependent transcription repression during G2 PMID:9303312 Fig8 C PMID:9303312 Fig2 B PMID:9303312 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:9312055 fig 1b PMID:9312055 fig 1c PMID:9312055 fig 1b PMID:9312055 fig 1b PMID:9312055 fig 1c PMID:9312055 fig 2 (synthetic rescue) PMID:9312055 fig 2 PMID:9312055 fig 1c PMID:9312055 fig 1c PMID:9312055 fig 1c PMID:9312055 fig 1c PMID:9312055 fig9 PMID:9312055 fig9 PMID:9312055 poly... PMID:9312055 fig7 PMID:9312055 fig 6 PMID:9312055 fig 6 PMID:9312055 fig 4 b-d PMID:9312055 fig 4a PMID:9312055 fig 4 PMID:9312055 fig 4 PMID:9312055 fig 3b (rescue) PMID:9312055 fig 1b PMID:9312055 fig 1b PMID:9312055 fig 3b (rescue) PMID:9312055 fig 3b PMID:9312055 fig 3b PMID:9312055 fig 3b PMID:9312055 fig 2 (synthetic rescue) PMID:9315645 fig7, sort of indirect - kinase dead mutant doesn't activate PMID:9315645 "This one comes in ""from the side"", see Ladds, Bond post 2010 publication summary" PMID:9321395 (Figure 5) PMID:9321395 (Figure 4) PMID:9321395 data not shown PMID:9321395 (Figure 4) PMID:9321395 (Figure 4) PMID:9321395 (Figure 4) PMID:9321395 (Figure 5) PMID:9321395 (Figure 5) PMID:9321395 (Figure 5) PMID:9321395 not shown PMID:9321395 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 activated_by(CHEBI:18420)| activated_by(CHEBI:29035) PMID:9325304 via purification assay PMID:9325304 via purification assay PMID:9325304 3B PMID:9325304 3B PMID:9325316 binds DNA in complex (2,3,11) PMID:9325316 author intent PMID:9325316 author intent PMID:9325316 binds DNA in complex (2,3,11) PMID:9325316 binds DNA in complex (2,3,11) PMID:9325316 binds DNA on its own PMID:9325316 author intent PMID:9325316 author intent PMID:9325316 author intent PMID:9325316 author intent PMID:9325316 author intent PMID:9325316 author intent PMID:9371883 two-hybrid assay PMID:9371883 two-hybrid assay PMID:9371883 two-hybrid assay PMID:9371883 two-hybrid assay PMID:9372936 assayed using SV40 NLS-GFP-LacZ reporter protein PMID:9372936 same as rae1-167 single mutant PMID:9372936 assayed using SV40 NLS-GFP-LacZ reporter protein PMID:9372936 same as rae1-167 single mutant PMID:9398669 fig 5a PMID:9398669 because slp1 can bypass wee1 it must independently inhibit cd2 PMID:9398669 add penetrance? PMID:9398669 fig 5c switched from conjugtion freqeuncy to sterility as can only capture penetance on cell phenotypes PMID:9398669 nitrogen induced arrest PMID:9398669 G1 phase nitrogen induced arrest PMID:9398669 because slp1 can bypass wee1 it must independently inhibit cd2 PMID:9420333 Fig 6C in late anaphase cdc7 is normally localized only one SPB PMID:9420333 "Fig 1 vw interpretation for ""active form""" PMID:9420333 Fig2A loss of cdc16 function does not affect cdc7 kinase activity PMID:9420333 Fig2A loss of spg1 function does not affect cdc7 kinase activity PMID:9420333 Fig3A,C spg1-HA observed at SPB throughout the mitotic cell cycle PMID:9420333 Fig3A,C spg1-HA observed at SPB throughout the mitotic cell cycle PMID:9420333 Fig5A PMID:9420333 Fig5A PMID:9420333 Fig5B PMID:9420333 Fig 6A in late anaphase cdc7 is normally localized only one SPB PMID:9420333 (GTP bound) PMID:9420333 (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 cdc7 is associated with both SPBs when a short spindle is present PMID:9428701 MBP substrate, activated_by(CHEBI:29035) PMID:9430640 Fig5 PMID:9430640 Fig2 PMID:9430640 Fig2 PMID:9430640 Fig3, data not shown phenotype similar to rum+OP PMID:9430640 Fig3B, similar to rum1+OP more severe than either single mutant. expressed from muliticopy plasmid. Colonies were integrants PMID:9430640 Fig3C integrated copy PMID:9430640 Fig 4B inhibitory for cdc2/cdc13 and cdc2/cig2 but not cdc2/cig1. Both Rum1+ and Rum1-A58A62 can inhibit cdk1 activity PMID:9430640 Fig3C PMID:9430640 Fig5B PMID:9430640 this isn't quite the right way to capture this target, still thinking PMID:9430640 this isn't quite the right way to capture this target, still thinking PMID:9430640 Fig1B PMID:9430640 Fig1C Peaks at the end of G2 40 min before peak of rum1 protein PMID:9430640 Fig1B PMID:9430640 Fig 4B inhibitory for cdc2/cdc13 and cdc2/cig2 but not cdc2/cig1. Both Rum1+ and Rum1-A58A62 can inhibit cdk1 activity PMID:9430640 Fig1B PMID:9430640 Fig7B rum1 A58A62 mutant protein is unable to be phosphorylated by cdc2/cig1 PMID:9430640 Fig 10 PMID:9430640 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 Fig6 PMID:9450991 figure 1A PMID:9450991 figure 1A PMID:9450991 figure 1A PMID:9450991 figure 1A PMID:9450991 figure 1A PMID:9450991 figure 2A/B PMID:9450991 fig 4A PMID:9450991 figure 4B PMID:9450991 30x figure 4B PMID:9459302 is this OK? its aseptate? PMID:9468529 inhibited_by CHEBI:29035 PMID:9488736 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 expressed Clostridium botulinum C3 protein to ADP-ribosylate Rho proteins including Rho1 PMID:9524127 (Fig. 3) PMID:9524127 (Fig. 3a) PMID:9524127 (Fig. 3a) PMID:9524127 (Fig. 3a) PMID:9524127 (Fig. 3a) PMID:9524127 (Fig. 3a) PMID:9524127 (Fig. 3a) PMID:9524127 (Fig. 3a) PMID:9524127 (Fig. 3a) PMID:9531532 over 25 PMID:9531532 over 25 PMID:9531532 over 25 PMID:9531532 over 25 PMID:9531532 over 35 PMID:9535817 inferred from FYPO:0000825, FYPO:0001117, FYPO:0005743, FYPO:0007674 phenotypes (including conditions) PMID:9552380 cig2-cdc2 PMID:9560390 osmotic stress PMID:9560390 osmotic stress PMID:9571240 4e PMID:9571240 fig3 PMID:9571240 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 4e PMID:9585506 salt stress PMID:9585506 salt stress PMID:9585506 salt stress PMID:9585506 salt stress PMID:9585506 western but we know this happens and I wanted to capture the extension PMID:9585506 western but we know this happens and I wanted to capture the extension PMID:9599405 PEHROMONE PMID:9601094 medium level of mph1 OEX (high is lethal) PMID:9601094 fig 2D PMID:9601094 Fig 3C at metaphase/anaphase transiton PMID:9601094 (Fig. 4D PMID:9601094 fig 4B PMID:9601094 figure 6 PMID:9601094 figure 6 PMID:9601094 fig 4B PMID:9601094 fig 4B PMID:9601094 dph1∆ cells were not hypersensitive to TBZ, compared to wild-type cells (Fig. 6C) PMID:9601094 figure 6 PMID:9601094 Figure 4A PMID:9601094 Fig 3C at metaphase/anaphase transiton PMID:9606213 fig1 PMID:9606213 fig7 PMID:9606213 (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 (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 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 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 fig1 PMID:9606213 fig1 PMID:9606213 DNS actin distributed in cytoplasm PMID:9606213 polarization, in shmoo DNS PMID:9606213 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 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:9614176 Fig3D loss of cig2 does not restore P factor induced G1 arrest PMID:9614176 Fig4 - sows proteasome involvment as well PMID:9614176 Fig5A PMID:9614176 Fig5B PMID:9614176 Fig5C PMID:9614176 Fig5C PMID:9614176 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 Fig6A transcript assayed was Mat1-Mm PMID:9614176 Fig4 PMID:9614176 Fig5C PMID:9614176 Fig5C PMID:9614176 Fig1 A PMID:9614176 Fig3 A In absence of rum1 cdc2-cdc13 kinase activity remains high in presence of P factor PMID:9614178 residue not determined experimentally, but probably Y173 PMID:9614178 residue not determined experimentally, but probably Y173 PMID:9614178 residue not determined experimentally, but probably Y173 PMID:9614178 residue not determined experimentally, but probably Y173 PMID:9614178 residue not determined experimentally, but probably Y173 PMID:9614178 residue not determined experimentally, but probably Y173 PMID:9622480 very mild as shown in xp PMID:9635188 independent of F-actin (assayed using Latrunculin A) PMID:9635188 29 degrees; permissive for either single mutant PMID:9635188 24 degrees PMID:9635188 independent of F-actin (assayed using Latrunculin A) PMID:9635188 independent of F-actin (assayed using Latrunculin A) PMID:9635188 dependent on F-actin (assayed using Latrunculin A) PMID:9635190 Figure 2a PMID:9635190 Figure 2c PMID:9635190 cytoplasm in interphase (Figure 4a, I) PMID:9635190 Figure 4b PMID:9635190 fig 5 during mitotic M-phase PMID:9635190 fig 5 during mitotic M-phase PMID:9635190 fig 5 during mitotic M-phase PMID:9635190 fig 5 during mitotic M-phase PMID:9635190 fig 5 during mitotic M-phase PMID:9635190 fig 5 during mitotic M-phase PMID:9635190 cytoplasm during interphase (with nuclear localization) PMID:9635190 fig 5 during interphase PMID:9635190 fig 5 during mitosis PMID:9635190 (Fig 1i) PMID:9635190 Figure 2b PMID:9635190 (Fig 1i) PMID:9636183 same severity as wee1-50 alone PMID:9658208 just to get the allele details of -P in the database PMID:9660817 data not shown PMID:9660817 data not shown PMID:9660817 data not shown PMID:9660818 including plasma membrane (GO:0005886) PMID:9660818 when crossed with shk1delta overexpressing shk2+ or wild type PMID:9660818 when crossed with partner overexpressing shk1-deltaN; normal in cross with wild type PMID:9660818 same severity when crossed with wild type or shk1delta PMID:9660818 assayed using myelin basic protein PMID:9660818 assayed using myelin basic protein; interaction shown in separate experiment PMID:9671458 h90 background PMID:9671458 h- background PMID:9671458 assayed in both h- and h90 backgrounds PMID:9679144 Fig2A cdc25-22 arrest released cells ie post NETO do not branch PMID:9679144 Fig2 B cells were pre NETO after temperature block PMID:9679144 Fig2B cells were pre NETO after temperature block PMID:9679144 Fig2B cells were pre NETO after temperature block PMID:9679144 Fig2C cells were pre NETO after temperature block about 5% cells are already branched at release PMID:9679144 Fig2C cells were pre NETO after temperature block about 5% cells are already branched at release PMID:9679144 Fig2C arrest released cells are pre NETO but only branch at low level. PMID:9679144 Fig2C arrest released cells have NETO defect and do not branch. PMID:9679144 Fig 3A-C pre NETO blocked cells do not branch if TBZ is added at shift down PMID:9679144 Fig 3C cell length does not affect branching showing its not because cells are longer at high temp PMID:9679144 Fig 4 Short interphase microtubules located in the cell centre PMID:9679144 Fig5 C,D PMID:9679144 Fig 6 abnormal septum in branched cell PMID:9679144 Fig 9 tea1 can relocalise to cell ends in absence of microtubules PMID:9679144 Fig 6 F-actin localised to branch site in presence of TBZ PMID:9679144 Fig 11 absence of microtubules PMID:9679144 Fig5 C,D Fig 12 Normal protein localisation in presence of TBZ PMID:9679144 Fig 8A-D Actin relocalisation to old or new cell end after microtubule disruption PMID:9679144 Fig 11 in the absence of microtubules and actin PMID:9679144 Fig1 F, H cells were pre NETO after temperature block PMID:9693363 increased 25S/18S ration PMID:9693384 probably Y173, but not determined experimentally PMID:9693384 probably Y173, but not determined experimentally PMID:9693384 probably Y173, but not determined experimentally PMID:9718372 probably Y173, but not determined experimentally PMID:9718372 probably Y173, but not determined experimentally PMID:9718372 probably Y173, but not determined experimentally PMID:9722643 fig4 PMID:9722643 fig1 PMID:9722643 fig5 PMID:9722643 fig3 PMID:9722643 table2 PMID:9722643 fig2 PMID:9739083 Fig2B cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C PMID:9739083 cdc18-1-141 when expressed on multi copy plasmid does not rescue cdc18-K46 PMID:9739083 cdc18-150-577 when expressed on multi copy plasmid does not rescue cdc18-K46 PMID:9739083 cdc18-150-577(T374A) when expressed on multi copy plasmid does not rescue cdc18-K46 PMID:9739083 cdc1-577 (NTP) when expressed on multi copy plasmid does not rescue cdc18-K46 PMID:9739083 Fig 2A cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C PMID:9739083 Fig 2A cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C PMID:9739083 Fig 2A cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C PMID:9739083 Fig 2A cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C PMID:9739083 Fig 2B cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C PMID:9739083 Fig 3 the kinase assay substrate used is Histone H1 PMID:9739083 Fig 3 the kinase assay substrate used is Histone H1 PMID:9739083 data not shown the kinase assay substrate used is Histone H1 PMID:9739083 Fig 3 cdc18 expressed from pREP3X and assayed for 20 hours after removal of thiamine at 32°C PMID:9739083 Fig 3 cdc18 expressed from pREP3X and assayed for 20 hours after removal of thiamine at 32°C PMID:9739083 Fig 3 cdc18 expressed from pREP3X and assayed for 20 hours after removal of thiamine at 32°C PMID:9739083 Fig 3 not strictly a co-immunoprecitation experiment as they used suc1 beads to pull down cdc2 then a western blot PMID:9739083 Fig 3 not strictly a co-immunoprecitation experiment as they used suc1 beads to pull down cdc2 then a western blot PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 2A cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Fig 4 cdc18 expressed from nmt1 on multi copy plasmid PMID:9739083 Data not shown Cdc18 expressed from nmt1 promoter on multi copy plasmid PMID:9739083 Data not shown Cdc18 expressed from nmt1 promoter on multi copy plasmid PMID:9739083 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 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 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 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 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 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 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 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 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 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 Fig 6 cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal. PMID:9739083 Fig 6 cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal. PMID:9739083 Fig 6 cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal. PMID:9739083 Fig 6 cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal. PMID:9739083 Fig 6 cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal. PMID:9739083 Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid PMID:9739083 Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid PMID:9739083 Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid PMID:9739083 Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid PMID:9739083 Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid PMID:9739083 Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid PMID:9739083 Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid PMID:9739083 Fig 6 and cell phenotype data not shown. cdc18 expressed from nmt1 promoter on multi copy plasmid PMID:9739083 Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid PMID:9739083 Fig 6. cdc18 expressed from nmt1 promoter on multi copy plasmid PMID:9740803 also assayed with GFP-NLS construct PMID:9740803 can't use IPI because we don't have identifiers for human importin alpha or the GST-NLS construct PMID:9740803 actually combination of in vitro assay, interactions, and sequence similarity PMID:9745017 inferred from decreased nda3 mRNA level PMID:9745017 inferred from decreased nda3 mRNA level PMID:9755169 Fig5C PMID:9755169 Fig 2C, cdc10 dependent transcription occurs during mitotic exit PMID:9755169 Fig 2C, cdc10 dependent transcription occurs during mitotic exit PMID:9755169 Fig 2C, cdc10 dependent transcription occurs during mitotic exit PMID:9755169 Fig3A cdc10 is a cdc18 transcriptional regulator see Fig2C PMID:9755169 Fig3B cdc10 is a cdc18 transcriptional regulator see Fig2C PMID:9755169 Fig3B PMID:9755169 Fig4C cd18 N term deletion can accumulate in a metaphase arrest PMID:9755169 Fig4E cdc18 lacking cdc2 phosphorylation sites accumulates immediately as cells progress into mitosis PMID:9755169 Fig5B PMID:9755169 Fig5A nmt1 promoter OFF cdc18 is more stable when 5/6 P sites are mutated PMID:9755169 Fig5B PMID:9755169 Fig5C PMID:9755169 Fig4C cd18 N term deletion can accumulate in a metaphase arrest PMID:9755169 Fig5D PMID:9755190 requested chromatin silencing term but advised to use this one PMID:9755190 vw: from chromatin organization to heterochromatin assembly : inconclusion this study implicates histone deacetylases in heterochromnatin assembly PMID:9755190 vw: from chromatin organization to heterochromatin assembly : inconclusion this study implicates histone deacetylases in heterochromnatin assembly PMID:9755190 vw: from chromatin organization to heterochromatin assembly : inconclusion this study implicates histone deacetylases in heterochromnatin assembly PMID:9755190 requested chromatin silencing term but advised to use this one PMID:9755190 requested chromatin silencing term but advised to use this one PMID:9755190 requested chromatin silencing term but advised to use this one PMID:9755190 requested chromatin silencing term but advised to use this one PMID:9771717 not shown PMID:9774107 fig2 PMID:9774107 fig2 PMID:9774107 fig2 PMID:9774107 fig2 PMID:9774107 fig2e PMID:9774107 fig2e PMID:9774107 data not shown PMID:9774107 fig 2 e PMID:9774107 fig 4a PMID:9774107 fig 4a PMID:9778252 Precise observation revealed that Mei2p dots could be visible in conjugating cells that completed cell fusion but did not undergo karyogamy yet. PMID:9786952 4a PMID:9786952 4de PMID:9786952 fig6 PMID:9786952 fig 2b PMID:9786952 fig 2a PMID:9786952 fig 2b PMID:9786952 fig 2e PMID:9786952 4a PMID:9786952 4ab PMID:9790887 activated_by(CHEBI:18420), activated_by(CHEBI:29103) PMID:9794798 mutant Cdc6 is not positively regulated by PCNA to the same extent as Cdc6+ PMID:9794798 mutant Cdc6 is not positively regulated by PCNA to the same extent as Cdc6+ PMID:9802907 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, ô°8 ô°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 (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 (included because different/new method) To observe the SPB in living cells, GFP-tagged Sad1 (designated hereafter Sad1âGFP) 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 (Fig. 2D) PMID:9808627 G2 block PMID:9808627 G1 block PMID:9832516 severity estimated because wt (i.e. not overexpressing cdc25) not shown PMID:9832516 severity estimated because wt (i.e. not overexpressing cdc25) not shown PMID:9832516 severity estimated because wt (i.e. not overexpressing cdc25) not shown PMID:9832516 severity estimated because wt (i.e. not overexpressing cdc25) not shown PMID:9839953 at the second po- sition (Gal-Man-O) PMID:9839953 low activity PMID:9839953 at the second po- sition (Gal-Man-O) PMID:9843572 (Figure 1 PMID:9843572 Figure 7A PMID:9843572 Figure 6B PMID:9843572 Figure 6A PMID:9843572 figure 3 B (additive) PMID:9843572 figure 3 A&B PMID:9843572 figure 3 A&B PMID:9843572 (Figure 3B) PMID:9843572 (Figure 3B) PMID:9843572 (Figure 3B) PMID:9843572 (Figure 3B) PMID:9843572 Figure 9A PMID:9843572 Figure 8 PMID:9843572 Figure 8 PMID:9843577 single micrograph, so can't tell if they're viable PMID:9843577 single micrograph, so can't tell if they're viable PMID:9843966 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 biologically relevant? it can also cut these PMID:9857040 biologically relevant? it can also cut these PMID:9862966 Fig3 CD PMID:9862966 https://github.com/pombase/fypo/issues/3931 PMID:9864354 indicated by high level of H1 kinase activity PMID:9864354 Fig. 2 E PMID:9864354 Fig. 2 E PMID:9864354 Fig. 2 D PMID:9872416 figure 2. PMID:9872416 figure 2. PMID:9872416 figure 2. PMID:9872416 figure 2. PMID:9872416 figure 2. PMID:9872416 figure 2. PMID:9872416 figure 2. PMID:9891039 worse than cdc24-M38 alone (wt not shown) PMID:9891039 worse than cdc24-M38 alone (wt not shown) PMID:9891039 worse than cdc24-M38 alone (wt not shown) PMID:9891039 worse than cdc24-M38 alone (wt not shown) PMID:9891047 temperature permissive for single mutant without rad2delta PMID:9891047 temperature permissive for single mutant without cds1delta PMID:9891047 temperature permissive for single mutant without cds1delta PMID:9891047 temperature permissive for single mutant without cds1delta PMID:9891047 temperature permissive for single mutant without cds1delta PMID:9891047 temperature permissive for single mutant without cds1delta PMID:9891047 temperature permissive for single mutant without cds1delta PMID:9891047 temperature permissive for single mutant without cds1delta PMID:9891047 temperature permissive for single mutant without cds1delta PMID:9891047 temperature permissive for single mutant without rad26delta PMID:9891047 temperature permissive for single mutant without rad26delta PMID:9891047 temperature permissive for single mutant without rad26delta PMID:9891047 temperature permissive for single mutant without rad26delta PMID:9891047 temperature permissive for single mutant without rad26delta PMID:9891047 temperature permissive for single mutant without rad26delta PMID:9891047 temperature permissive for single mutant without rad2delta PMID:9891047 temperature permissive for single mutant without rad2delta PMID:9891047 temperature permissive for single mutant without rad2delta PMID:9891047 temperature permissive for single mutant without rad2delta PMID:9891047 temperature permissive for single mutant without rad2delta PMID:9891047 temperature permissive for single mutant without rad2delta PMID:9891047 temperature permissive for single mutant without cds1delta PMID:9891047 temperature permissive for single mutant without cds1delta PMID:9891047 temperature permissive for single mutant without cds1delta PMID:9891047 temperature permissive for single mutant without rad2delta PMID:9891047 temperature permissive for single mutant without cds1delta PMID:9891047 temperature permissive for single mutant without rad2delta PMID:9891047 temperature permissive for single mutant without rad26delta PMID:9891047 temperature permissive for single mutant without rad26delta PMID:9891047 temperature permissive for single mutant without rad26delta PMID:9891047 temperature permissive for single mutant without rad2delta PMID:9891047 temperature permissive for single mutant without rad26delta PMID:9950674 fig 9 PMID:9950674 fig 9 PMID:9973368 galactose specific flocculation should have cell-cell ahdesion parentage PMID:9973368 non-flocculating cells