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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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Publisher copy:
10.1016/j.cell.2012.07.028

Authors


Journal:
Cell More from this journal
Volume:
150
Issue:
5
Pages:
961-974
Publication date:
2012-08-31
DOI:
EISSN:
1097-4172
ISSN:
0092-8674
Pubs id:
pubs:350923
UUID:
uuid:90561590-faba-498b-87ad-e41a541140a9
Local pid:
pubs:350923
Source identifiers:
350923
Deposit date:
2013-11-16

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