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Article

Closing the cohesin ring: structure and function of its Smc3-kleisin interface.

Science (New York, N.Y.) - 21 Nov 2014

Gligoris Thomas G, Scheinost Johanna C, Bürmann Frank, Petela Naomi, Chan Kok-Lung, Uluocak Pelin, Beckouët Frédéric, Gruber Stephan, Nasmyth Kim, Löwe Jan

Abstract excerpt

Through their association with a kleisin subunit (Scc1), cohesin's Smc1 and Smc3 subunits are thought to form tripartite rings that mediate sister chromatid cohesion. Unlike the structure of Smc1/Smc3 and Smc1/Scc1 interfaces, that of Smc3/Scc1 is not known. Disconnection of this interface is thought to release cohesin from chromosomes in a process regulated by acetylation. We show here that the N-terminal domain...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 25414305
DOI: 10.1126/science.1256917
PMCID: PMC4300515

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Closing the cohesin ring: structure and function of its Smc3-kleisin interface.PMID 25414305Read ↗

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

Chromosome loading of cohesin depends on conserved residues in Scc3.Semantic proximity Read ↗

Suppressor mutation analysis combined with 3D modeling explains cohesin's capacity to hold and release DNA.Semantic proximity Read ↗

Building sister chromatid cohesion: smc3 acetylation counteracts an antiestablishment activity.Semantic proximity Read ↗

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