Sister-chromatid cohesion mediated by the alternative RF-CCtf18/Dcc1/Ctf8, the helicase Chl1 and the polymerase-α-associated protein Ctf4 is essential for chromatid disjunction during meiosis II

Petronczki, Mark; Chwalla, Barbara; Siomos, Maria F.; Yokobayashi, Shihori; Helmhart, Wolfgang; Deutschbauer, Adam M.; Davis, Ronald W.; Watanabe, Yoshinori; Nasmyth, Kim

doi:10.1242/jcs.01231

Cited by 128 publications

(122 citation statements)

References 77 publications

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“…TRF4 and TRF5 have also been suggested to have an essential role in the coordination between DNA replication and sister chromatid cohesion (25). In another study, the deletion of TRF4 alone was found to have no effect on sister chromatid cohesion in mitotic metaphase cells or on chromosome segregation during meiosis; in this study, however, the possibility that TRF5 compensates for the absence of TRF4 has not been excluded (18).…”

contrasting

confidence: 52%

Trf4 and Trf5 Proteins of Saccharomyces cerevisiae Exhibit Poly(A) RNA Polymerase Activity but No DNA Polymerase Activity

Haracska

Johnson

Prakash

et al. 2005

Molecular and Cellular Biology

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The Saccharomyces cerevisiae Trf4 and Trf5 proteins are members of a distinct family of eukaryotic DNA polymerase ␤-like nucleotidyltransferases, and a template-dependent DNA polymerase activity has been reported for Trf4. To define the nucleotidyltransferase activities associated with Trf4 and Tr5, we purified these proteins from yeast cells and show that whereas both proteins exhibit a robust poly(A) polymerase activity, neither of them shows any evidence of a DNA polymerase activity. The poly(A) polymerase activity, as determined for Trf4, is strictly Mn 2؉ dependent and highly ATP specific, incorporating AMP onto the free 3-hydroxyl end of an RNA primer. Unlike the related poly(A) polymerases from other eukaryotes, which are located in the cytoplasm and regulate the stability and translation efficiency of specific mRNAs, the Trf4 and Trf5 proteins are nuclear, and a multiprotein complex associated with Trf4 has been recently shown to polyadenylate a variety of misfolded or inappropriately expressed RNAs which activate their degradation by the exosome. To account for the effects of Trf4/Trf5 proteins on the various aspects of DNA metabolism, including chromosome condensation, DNA replication, and sister chromatid cohesion, we suggest an additional and essential role for the Trf4 and Trf5 protein complexes in generating functional mRNA poly(A) tails in the nucleus.The TRF4 gene of Saccharomyces cerevisiae was first identified in a genetic screen for mutations that are synthetically lethal with mutations in DNA topoisomerase I (20). TRF5 is a homolog of TRF4, and deletion of both genes is lethal, indicating that their functions are overlapping and essential for cell viability (5). A role for TRF4 in chromosome condensation is indicated from the observation that a top1 trf4 ts double mutant fails to establish and maintain chromosome condensation in rRNA genes at mitosis (4). Furthermore, the Trf4 protein interacts physically with the Smc1 and Smc2 proteins that bind chromosomes and cause condensation (4). TRF4 and TRF5 have also been suggested to have an essential role in the coordination between DNA replication and sister chromatid cohesion (25). In another study, the deletion of TRF4 alone was found to have no effect on sister chromatid cohesion in mitotic metaphase cells or on chromosome segregation during meiosis; in this study, however, the possibility that TRF5 compensates for the absence of TRF4 has not been excluded (18).Trf4 and Trf5 are members of a distinct family of eukaryotic DNA polymerase (Pol) ␤-like nucleotidyltransferases (1), and a template-dependent DNA polymerase activity has been reported for Trf4 and named DNA polymerase (3, 25). More recently, the Trf4 and Trf5 proteins have been shown to interact with the C-terminal domain of Pol2, the catalytic subunit of Polε, and stimulation of Polε DNA synthetic activity was observed in the presence of Trf4 (7). In keeping with these observations, the Trf4/Trf5 proteins are located in the nucleus (12, 23).The Trf4/Trf5-related proteins from other euk...

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contrasting

confidence: 52%

Trf4 and Trf5 Proteins of Saccharomyces cerevisiae Exhibit Poly(A) RNA Polymerase Activity but No DNA Polymerase Activity

Haracska

Johnson

Prakash

et al. 2005

Molecular and Cellular Biology

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“…In budding yeast, Chl1p is required for the establishment of sisterchromatid cohesion during S-phase. 8 Recent studies in budding yeast have shown that Chl1p binds both PCNA 2 and Ctf7p, 7 two molecules that are essential for the establishment of cohesion. Based on the yeast studies, it is reasonable to predict that mammalian ChlR1 might also participate in the establishment of chromosome cohesion.…”

Section: Discussionmentioning

confidence: 99%

“…6,7 Furthermore, a complex containing Chl1, Ctf8 and Ctf4 is required for the establishment of sister-chromatid cohesion during S-phase. 8 Humans have two CHL1-related genes, DDX11 and DDX12, which encode the proteins ChlR1 and ChlR2, respectively (hereafter the term ChlR will refer to both human proteins). These two genes, located on the short arm of chromosome 12, are greater than 90% identical and are more closely related to CHL1 than any other family member.…”

mentioning

confidence: 99%

Loss of ChlR1 Helicase in Mouse Causes Lethality Due to the Accumulation of Aneuploid Cells Generated by Cohesion Defects and Placental Malformation

Inoue¹,

Li²,

Roby³

et al. 2007

Cell Cycle

112

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“…CHL1 is not a donor preference-specific gene; it was identified .20 years ago because chl1D causes a large increase in both the loss and gain of chromosomes and is therefore most likely a nondisjunction mutation (Liras et al 1978;Gerring et al 1990). Subsequent studies have shown that CHL1 encodes a nuclear protein with presumed but undemonstrated helicase activity that is implicated in the establishment and maintenance of sister-chromatid cohesion (Petronczki et al 2004). It is possible that if sister-chromatid cohesion is reduced, some cells in which MATa is repaired after DNA replication might allow the two sisters to search independently for a donor.…”

Section: Re Binds Fkh1 and Swi4/swi6mentioning

confidence: 99%

Mating-Type Genes andMATSwitching inSaccharomyces cerevisiae

2012

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Mating type in Saccharomyces cerevisiae is determined by two nonhomologous alleles, MATa and MATa. These sequences encode regulators of the two different haploid mating types and of the diploids formed by their conjugation. Analysis of the MATa1, MATa1, and MATa2 alleles provided one of the earliest models of cell-type specification by transcriptional activators and repressors. Remarkably, homothallic yeast cells can switch their mating type as often as every generation by a highly choreographed, site-specific homologous recombination event that replaces one MAT allele with different DNA sequences encoding the opposite MAT allele. This replacement process involves the participation of two intact but unexpressed copies of mating-type information at the heterochromatic loci, HMLa and HMRa, which are located at opposite ends of the same chromosome-encoding MAT. The study of MAT switching has yielded important insights into the control of cell lineage, the silencing of gene expression, the formation of heterochromatin, and the regulation of accessibility of the donor sequences. Real-time analysis of MAT switching has provided the most detailed description of the molecular events that occur during the homologous recombinational repair of a programmed double-strand chromosome break. TABLE OF CONTENTS Abstract 33Introduction 34

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Sister-chromatid cohesion mediated by the alternative RF-CCtf18/Dcc1/Ctf8, the helicase Chl1 and the polymerase-α-associated protein Ctf4 is essential for chromatid disjunction during meiosis II

Cited by 128 publications

References 77 publications

Trf4 and Trf5 Proteins of Saccharomyces cerevisiae Exhibit Poly(A) RNA Polymerase Activity but No DNA Polymerase Activity

Trf4 and Trf5 Proteins of Saccharomyces cerevisiae Exhibit Poly(A) RNA Polymerase Activity but No DNA Polymerase Activity

Loss of ChlR1 Helicase in Mouse Causes Lethality Due to the Accumulation of Aneuploid Cells Generated by Cohesion Defects and Placental Malformation

Mating-Type Genes andMATSwitching inSaccharomyces cerevisiae

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