Ctf4 Links DNA Replication with Sister Chromatid Cohesion Establishment by Recruiting the Chl1 Helicase to the Replisome

Samora, Catarina P.; Saksouk, Julie; Goswami, Panchali; Wade, Ben O.; Singleton, Martin R.; Bates, Paul A.; Lengronne, Armelle; Costa, Alessandro; Uhlmann, Frank

doi:10.1016/j.molcel.2016.05.036

Cited by 117 publications

(190 citation statements)

References 51 publications

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“…The human Ctf4 homolog AND-1 shows additional interactions with Pol δ (142). Other replication proteins, such as Dna2 and the sister chromatin cohesion protein Chl1, also bind Ctf4, marking this factor as an important interaction hub within the replisome (141, 143). Surprisingly, a deletion of CTF4 , or of the S. pombe homolog mcl1 + , is viable.…”

Section: Replisome Coordinationmentioning

confidence: 99%

Eukaryotic DNA Replication Fork

Burgers

Kunkel

2017

Annu. Rev. Biochem.

412

407

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This review focuses on the biogenesis and composition of the eukaryotic DNA replication fork, with an emphasis on the enzymes that synthesize DNA and repair discontinuities on the lagging strand of the replication fork. Physical and genetic methodologies aimed at understanding these processes are discussed. The preponderance of evidence supports a model in which DNA polymerase ε (Pol ε) carries out the bulk of leading strand DNA synthesis at an undisturbed replication fork. DNA polymerases α and β carry out the initiation of Okazaki fragment synthesis and its elongation and maturation, respectively. This review also discusses alternative proposals, including cellular processes during which alternative forks may be utilized, and new biochemical studies with purified proteins that are aimed at reconstituting leading and lagging strand DNA synthesis separately and as an integrated replication fork.

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Section: Replisome Coordinationmentioning

confidence: 99%

Eukaryotic DNA Replication Fork

Burgers

Kunkel

2017

Annu. Rev. Biochem.

412

407

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“…Mutants in many replication fork-associated cohesion factors show reduced acetylated Smc3 in budding yeast [13-15]. This observation can be explained by a multitude of mechanisms, including defects in cell cycle, altered residence time of cohesin on chromatin, and/or reduced accessibility of the Eco1 acetyltransferase to cohesin.…”

Section: Introductionmentioning

confidence: 99%

Chromatin determinants of the inner-centromere rely on replication factors with functions that impart cohesion

et al. 2016

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Replication fork-associated factors promote genome integrity and protect against cancer. Mutations in the DDX11 helicase and the ESCO2 acetyltransferase also cause related developmental disorders classified as cohesinopathies. Here we generated vertebrate model cell lines of these disorders and cohesinopathies-related genes. We found that vertebrate DDX11 and Tim-Tipin are individually needed to compensate for ESCO2 loss in chromosome segregation, with DDX11 also playing complementary roles with ESCO2 in centromeric cohesion. Our study reveals that overt centromeric cohesion loss does not necessarily precede chromosome missegregation, while both these problems correlate with, and possibly originate from, inner-centromere defects involving reduced phosphorylation of histone H3T3 (pH3T3) in the region. Interestingly, the mitotic pH3T3 mark was defective in all analyzed replication-related mutants with functions in cohesion. The results pinpoint mitotic pH3T3 as a postreplicative chromatin mark that is sensitive to replication stress and conducts with different kinetics to robust centromeric cohesion and correct chromosome segregation.

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“…Indeed, it has been demonstrated that cohesin colocalizes with replication forks in budding yeast [68] and is recruited to replication forks in Xenopus egg extracts and human cells [69,70]. In addition, cohesin also interacts with the fork-associated Chl1 helicase [71]. Surprisingly, and in contrast to ctf18 and chl4 , the RPA mutation did not suppress the cohesion defect of the chl1 mutant.…”

Section: Implications For Sister Chromatid Cohesionmentioning

confidence: 99%

DNA entry, exit and second DNA capture by cohesin: insights from biochemical experiments

Murayama

2018

Nucleus

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Cohesin is a ring-shaped, multi-subunit ATPase assembly that is fundamental to the spatiotemporal organization of chromosomes. The ring establishes a variety of chromosomal structures including sister chromatid cohesion and chromatin loops. At the core of the ring is a pair of highly conserved SMC (Structural Maintenance of Chromosomes) proteins, which are closed by the flexible kleisin subunit. In common with other essential SMC complexes including condensin and the SMC5-6 complex, cohesin encircles DNA inside its cavity, with the aid of HEAT (Huntingtin, elongation factor 3, protein phosphatase 2A and TOR) repeat auxiliary proteins. Through this topological embrace, cohesin is thought to establish a series of intra- and interchromosomal interactions by tethering more than one DNA molecule. Recent progress in biochemical reconstitution of cohesin provides molecular insights into how this ring complex topologically binds and mediates DNA-DNA interactions. Here, I review these studies and discuss how cohesin mediates such chromosome interactions.

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Ctf4 Links DNA Replication with Sister Chromatid Cohesion Establishment by Recruiting the Chl1 Helicase to the Replisome

Cited by 117 publications

References 51 publications

Eukaryotic DNA Replication Fork

Eukaryotic DNA Replication Fork

Chromatin determinants of the inner-centromere rely on replication factors with functions that impart cohesion

DNA entry, exit and second DNA capture by cohesin: insights from biochemical experiments

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