Releasing Activity Disengages Cohesin’s Smc3/Scc1 Interface in a Process Blocked by Acetylation

@inproceedings{Beckout2016ReleasingAD,
  title={Releasing Activity Disengages Cohesin’s Smc3/Scc1 Interface in a Process Blocked by Acetylation},
  author={Fr{\'e}d{\'e}ric Beckou{\"e}t and Madhusudhan Srinivasan and Maurici Brunet Roig and Kok-Lung Chan and Johanna C. Scheinost and Paul Batty and Bin Hu and Naomi J. Petela and Thomas G. Gligoris and Alexandra C.H. Smith and Lana Strmecki and Benjamin D. Rowland and Kim Nasmyth},
  booktitle={Molecular cell},
  year={2016}
}
Sister chromatid cohesion conferred by entrapment of sister DNAs within a tripartite ring formed between cohesin's Scc1, Smc1, and Smc3 subunits is created during S and destroyed at anaphase through Scc1 cleavage by separase. Cohesin's association with chromosomes is controlled by opposing activities: loading by Scc2/4 complex and release by a separase-independent releasing activity as well as by cleavage. Coentrapment of sister DNAs at replication is accompanied by acetylation of Smc3 by Eco1… CONTINUE READING
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Citations

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Structural basis for Scc3-dependent cohesin recruitment to chromatin

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  • 2018
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Mechanisms of Cohesin Function Revealed by Analysis of Smc3

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DNA binding to SMC ATPases-trapped for release.

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CITES BACKGROUND
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