Establishment of Sister Chromatid Cohesion at the S. cerevisiae Replication Fork

Lengronne, Armelle; McIntyre, John; Katou, Yuki; Kanoh, Yutaka; Hopfner, Karl‐Peter; Shirahige, Katsuhiko; Uhlmann, Frank

doi:10.1016/j.molcel.2006.08.018

Cited by 266 publications

(359 citation statements)

References 41 publications

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“…29,30 These proteins locali�e to replication forks, at least when cells are arrested in early S phase by hydroxy urea (HU) treatment. 7 We confirmed that Ino80 and Arp8 are specifically enriched at an active replication origin, ARS607, but not at a late-firing origin, ARS609, under similar conditions ( Fig. 4A and B, Supplementary Fig.…”

Section: Ino80 Complex In Sister Chromatid Cohesion Chromosome XV Andsupporting

confidence: 74%

“…Ctf18 is part of the alternative RFC complex that can both load and unload PCNA from DNA in vitro. 31,32 Since PCNA binding around the early replication origin ARS607 is reported to be significantly weaker in HU-arrested ctf18 cells, 7 we expected that PCNA binding to ARS607 would be decreased in the arp8 mutant. To our surprise, PCNA accumulated rather than decreased near ARS607 in arp8 cells (Fig.…”

Section: Ino80 Complex In Sister Chromatid Cohesion Chromosome XV Andmentioning

confidence: 98%

“…7 Moreover, Moreover, Ctf18 is required for the efficient loading of PCNA around DNA replication forks. Cohesin-associated regions occur at intervals of 8-13 kb along chromosome arms, and cohesin preferentially associates with AT-rich intergenic regions.…”

Section: Introductionmentioning

confidence: 99%

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The INO80 Chromatin Remodeling Complex Functions in Sister Chromatid Cohesion

Ogiwara

Enomoto²,

Seki³

2007

Cell Cycle

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Previously published online as a Cell Cycle E-publication: http://www.landesbioscience.com/journals/cc/abstract.php?id=4130 KEy wOrdSIno80, Arp8, Ctf18, RFC, PCNA, cohesin, chromosome segregation/sister chromatid cohesion, chromatin remodeling, replication fork AcKnOwlEdgEMEnTSWe thank P. Hieter, A. Sugino, Y. Kawasaki, and M. Arisawa for strains, antibodies and plasmids used in this study. We thank all members of the Enomoto lab for their support. This work was supported by Grants-in-Aid for Scientific Research on Priority Areas from The Ministry of Education, Science, Sports and Culture of Japan. nOTESupplemental material can be found at: http://www.landesbioscience.com/supplement/ogiwaraCC6-9-sup.pdf AbSTrAcTHere we identify a defect in sister chromatid cohesion in the Saccharomyces serevisiae arp8 mutant, which impairs the chromatin remodeling activity of the INO80 complex, and we report the direct association of Ino80 with centromeres and cohesin-associated regions. In early S phase, Ino80 is recruited to replication forks along with Ctf18 and PCNA, both of which are involved in the establishment of sister chromatid cohesion. The arp8 mutation perturbs the association of Ctf18 and PCNA but not of cohesin with replication forks. We propose that the INO80 complex is required for the proper establishment of sister chromatid cohesion.

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Section: Ino80 Complex In Sister Chromatid Cohesion Chromosome XV Andsupporting

confidence: 74%

Section: Ino80 Complex In Sister Chromatid Cohesion Chromosome XV Andmentioning

confidence: 98%

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The INO80 Chromatin Remodeling Complex Functions in Sister Chromatid Cohesion

Ogiwara

Enomoto²,

Seki³

2007

Cell Cycle

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“…GAL-CDC20 was integrated into leu2:KAN using plasmid p453-GAL-CDC20 (ref. 54; a gift from F. Uhlmann). Strain GAL-CDH1-m11 was constructed in two steps, disruption of TRP1 by KAN and integration of GAL-CDH1-m11 into trp1:KAN 26 (a gift from W. Zachariae).…”

Section: Methodsmentioning

confidence: 99%

Degradation of Ndd1 by APC/CCdh1 generates a feed forward loop that times mitotic protein accumulation

et al. 2015

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Ndd1 activates the Mcm1-Fkh2 transcription factor to transcribe mitotic regulators. The anaphase-promoting complex/cyclosome activated by Cdh1 (APC/C Cdh1 ) mediates the degradation of proteins throughout G1. Here we show that the APC/C Cdh1 ubiquitinates Ndd1 and mediates its degradation, and that APC/C Cdh1 activity suppresses accumulation of Ndd1 targets. We confirm putative Ndd1 targets and identify novel ones, many of them APC/C Cdh1 substrates. The APC/C Cdh1 thus regulates these proteins in a dual manner-both pretranscriptionally and post-translationally, forming a multi-layered feedforward loop (FFL). We predict by mathematical modelling and verify experimentally that this FFL introduces a lag between APC/C Cdh1 inactivation at the end of G1 and accumulation of genes transcribed by Ndd1 in G2. This regulation generates two classes of APC/C Cdh1 substrates, early ones that accumulate in S and late ones that accumulate in G2. Our results show how the dual state APC/C Cdh1 activity is converted into multiple outputs by interactions between its substrates.

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“…One model predicts that cohesin permits replication fork passage through the inside of its ring. This passive mechanism finally allows a single cohesin to accommodate two replicated DNAs (Figure 2(a)) [66]. In budding yeast, the loader becomes dispensable for cell viability when inactivated just after, but not before, G1 phase, suggesting that the cohesin loaded onto G1 chromatin is capable of cohesion establishment.…”

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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Establishment of Sister Chromatid Cohesion at the S. cerevisiae Replication Fork

Cited by 266 publications

References 41 publications

The INO80 Chromatin Remodeling Complex Functions in Sister Chromatid Cohesion

The INO80 Chromatin Remodeling Complex Functions in Sister Chromatid Cohesion

Degradation of Ndd1 by APC/CCdh1 generates a feed forward loop that times mitotic protein accumulation

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

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