Transformation/Transcription Domain-Associated Protein (TRRAP)-Mediated Regulation of Wee1

Calonge, Teresa M.; Eshaghi, Majid; Liu, Jianhua; Ronai, Ze’ev A.; O’Connell, Matthew J.

doi:10.1534/genetics.110.114769

Cited by 17 publications

(17 citation statements)

References 78 publications

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“…This sensitivity is in concordance with the DNA microarray analysis, which revealed that changes in the gene expression pattern upon the adaptation of eca39⌬ are negatively correlated with those observed in a tra1 mutant ( Fig. 2C; supplemental Table 3) (26). The involvement of spt8 ϩ and tra1 ϩ suggests that NH 4 Cl resistance is under the control of the whole SAGA complex, although smaller complexes such as the Ada2-Ada3-Gcn5 complex or Gcn5 alone have also been described (27).…”

Section: Deletion Of the Saga Hat Module Subunit In A Leucine Auxotrosupporting

confidence: 86%

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The SAGA Histone Acetyltransferase Complex Regulates Leucine Uptake through the Agp3 Permease in Fission Yeast

Takahashi

Sun

Hamamoto

et al. 2012

Journal of Biological Chemistry

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Background: SAGA is a multiprotein complex that possesses histone acetyltransferase activity. Results: Fission yeast strains with deletions in the SAGA acetyltransferase subunit exhibited increased leucine uptake in a manner dependent on an amino acid permease gene. Conclusion: SAGA regulates amino acid uptake in fission yeast. Significance: Regulation of nutrient uptake by SAGA provides a potential link between cellular metabolism and chromatin regulation.

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Section: Deletion Of the Saga Hat Module Subunit In A Leucine Auxotrosupporting

confidence: 86%

“…2C; supplemental Table 3) (13,15,23,25,26). In particular, the deletions of the SAGA HAT module subunits, including ada2 ϩ and ada3 ϩ (12, 27) as well as the catalytic subunit gcn5 ϩ , were most highly correlated.…”

Section: The Eca39⌬ Mutant Exhibits An Adaptive Growth Phenotype On Mmentioning

confidence: 96%

The SAGA Histone Acetyltransferase Complex Regulates Leucine Uptake through the Agp3 Permease in Fission Yeast

Takahashi

Sun

Hamamoto

et al. 2012

Journal of Biological Chemistry

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“…Samples were taken at appropriate intervals for the described assays. DNA content was determined with a FACS Caliber (Becton Dickinson) as described previously (Calonge et al, 2010). Mutation rates in can1 were calculated using the method of the median from 11 independent cultures as previously described (Lee et al, 2007).…”

Section: General 975hmentioning

confidence: 99%

Brc1-dependent recovery from replication stress

Bass

Murray

O’Connell

2012

Journal of Cell Science

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Summary BRCT-containing protein 1 (Brc1) is a multi-BRCT (BRCA1 carboxyl terminus) domain protein in Schizosaccharomyces pombe that is required for resistance to chronic replicative stress, but whether this reflects a repair or replication defect is unknown and the subject of this study. We show that brc1D cells are significantly delayed in recovery from replication pausing, though this does not activate a DNA damage checkpoint. DNA repair and recombination protein Rad52 is a homologous recombination protein that loads the Rad51 recombinase at resected double-stranded DNA (dsDNA) breaks and is also recruited to stalled replication forks, where it may stabilize structures through its strand annealing activity. Rad52 is required for the viability of brc1D cells, and brc1D cells accumulate Rad52 foci late in S phase that are potentiated by replication stress. However, these foci contain the single-stranded DNA (ssDNA) binding protein RPA, but not Rad51 or cH2A. Further, these foci are not associated with increased recombination between repeated sequences, or increased post-replication repair. Thus, these Rad52 foci do not represent sites of recombination. Following the initiation of DNA replication, the induction of these foci by replication stress is suppressed by defects in origin recognition complex (ORC) function, which is accompanied by loss of viability and severe mitotic defects. This suggests that cells lacking Brc1 undergo an ORC-dependent rescue of replication stress, presumably through the firing of dormant origins, and this generates RPA-coated ssDNA and recruits Rad52. However, as Rad51 is not recruited, and the checkpoint effector kinase Chk1 is not activated, these structures must not contain the unprotected primer ends found at sites of DNA damage that are required for recombination and checkpoint activation. IntroductionDuring DNA replication, cells are extremely vulnerable to DNA damage. This vulnerability is due to both the genomic lesions themselves, but also to the impediment these lesions cause to the completion of replication. Replication forks that encounter sites of DNA damage stall in the face of these lesions, a process that activates the DNA replication checkpoint to help maintain stalled fork stability, halt the cell cycle, and initiate DNA repair. The majority of replication forks are presumed to retain the full complement of replication machinery in a stable conformation at sites of fork stalling until the impeding lesion is repaired. However, some lesions are not readily resolved and so alternative mechanisms for the completion of replication have evolved. These include the collapse of the stalled replication fork and its repair through homologous recombination (HR), bypass of the DNA lesion through the post-replication repair (PRR) pathway, which includes both error-prone and error-free mechanisms, and the completion of replication through the firing of adjacent origins (Branzei and Foiani, 2008;Branzei and Foiani, 2009).PRR mediates lesion bypass through a two-step process. Initia...

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“…All other assays were performed on cells grown in minimal medium (EMM2). General methods for microscopy, transformation, Western blotting, and drug and radiation sensitivities were as described previously (17,(29)(30)(31). DNA was stained with 1 g/ml 4=,6-diamino-2-phenylindole (DAPI).…”

Section: Methodsmentioning

confidence: 99%

H2A.Z-Dependent Regulation of Cohesin Dynamics on Chromosome Arms

Tapia-Alveal

Lin

Yeoh

et al. 2014

Molecular and Cellular Biology

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Structural maintenance of chromosomes (SMC) complexes and DNA topoisomerases are major determinants of chromosome structure and dynamics. The cohesin complex embraces sister chromatids throughout interphase, but during mitosis most cohesin is stripped from chromosome arms by early prophase, while the remaining cohesin at kinetochores is cleaved at anaphase. This two-step removal of cohesin is required for sister chromatids to separate. The cohesin-related Smc5/6 complex has been studied mostly as a determinant of DNA repair via homologous recombination. However, chromosome segregation fails in Smc5/6 null mutants or cells treated with small interfering RNAs. This also occurs in Smc5/6 hypomorphs in the fission yeast Schizosaccharomyces pombe following genotoxic and replication stress, or topoisomerase II dysfunction, and these mitotic defects are due to the postanaphase retention of cohesin on chromosome arms. Here we show that mitotic and repair roles for Smc5/6 are genetically separable in S. pombe. Further, we identified the histone variant H2A.Z as a critical factor to modulate cohesin dynamics, and cells lacking H2A.Z suppress the mitotic defects conferred by Smc5/6 dysfunction. Together, H2A.Z and the SMC complexes ensure genome integrity through accurate chromosome segregation. Chromosomal integrity is essential for normal growth and development. In eukaryotes, there are three essential complexes of proteins that are central to chromosome dynamics. These are cohesin, condensin, and the Smc5/6 complex, known collectively as the structural maintenance of chromosomes (SMC) complex. Each complex shares a related architecture, and central to them are a heterodimer of SMC proteins: Smc1 and -3 in cohesin, Smc2 and -4 in condensin, and Smc5 and -6 in Smc5/6. These SMC proteins are large coiled-coil molecules with globular N and C termini containing Walker A and B ATP-binding motifs. They fold and interact at a flexible hinge, with ATP acting to hold the globular domains together. A kleisin protein bridges each heterodimer to form a putative ring-shaped structure, and each complex has specific additional non-SMC proteins that serve as regulators and effectors of function (1-3).Chromosome condensation and sister chromatid cohesion are the key roles for condensin and cohesin, respectively (1). However, defects in DNA repair have also been described for yeast strains harboring hypomorphic mutant alleles of condensin (4) and cohesin (5-7) subunits. In the case of cohesin, a role in DNA repair could stem from the fact that DNA repair by homologous recombination (HR) requires the sister chromatid to be in close proximity to the damaged chromatid. However, more recently cohesin in mammalian cells has been shown to also act as a transcriptional insulator in collaboration with CTCF (8, 9), and so the DNA repair function of cohesin may be more complex than a simple scaffolding mechanism. As its name suggests, deciphering Smc5/6 function has proved more elusive, though most studies have focused on a role for this complex in...

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Transformation/Transcription Domain-Associated Protein (TRRAP)-Mediated Regulation of Wee1

Cited by 17 publications

References 78 publications

The SAGA Histone Acetyltransferase Complex Regulates Leucine Uptake through the Agp3 Permease in Fission Yeast

The SAGA Histone Acetyltransferase Complex Regulates Leucine Uptake through the Agp3 Permease in Fission Yeast

Brc1-dependent recovery from replication stress

H2A.Z-Dependent Regulation of Cohesin Dynamics on Chromosome Arms

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