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Cohesin's DNA exit gate is distinct from its entrance gate and is regulated by acetylation.

Abstract:

Sister chromatid cohesion is mediated by entrapment of sister DNAs by a tripartite ring composed of cohesin's Smc1, Smc3, and α-kleisin subunits. Cohesion requires acetylation of Smc3 by Eco1, whose role is to counteract an inhibitory (antiestablishment) activity associated with cohesin's Wapl subunit. We show that mutations abrogating antiestablishment activity also reduce turnover of cohesin on pericentric chromatin. Our results reveal a "releasing" activity inherent to cohesin complexes tr...

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Publication status:
Published

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Publisher copy:
10.1016/j.cell.2012.07.028

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Journal:
Cell
Volume:
150
Issue:
5
Pages:
961-974
Publication date:
2012-08-05
DOI:
EISSN:
1097-4172
ISSN:
0092-8674
URN:
uuid:e99129a5-07de-4f69-bb79-53c245634447
Source identifiers:
348883
Local pid:
pubs:348883

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