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Article

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

Molecular cell - 18 Feb 2016

Beckouët Frederic, Srinivasan Madhusudhan, Roig Maurici Brunet, Chan Kok-Lung, Scheinost Johanna C, Batty Paul, Hu Bin, Petela Naomi, Gligoris Thomas, Smith Alexandra C, Strmecki Lana, Rowland Benjamin D, Nasmyth Kim

Abstract excerpt

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....

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Share to Acetylation
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Chromosomal Proteins, Non-Histone

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Source

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Identifiers

PMID: 26895425
DOI: 10.1016/j.molcel.2016.01.026
PMCID: PMC4769318

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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