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Scc2 is a potent activator of Cohesin’s ATPase that promotes loading by binding Scc1 without Pds5

Abstract:

Cohesin organizes DNA into chromatids, regulates enhancer-promoter interactions, and confers sister chromatid cohesion. Its association with chromosomes is regulated by hook-shaped HEAT repeat proteins that bind Scc1, namely Scc3, Pds5, and Scc2. Unlike Pds5, Scc2 is not a stable cohesin constituent but, as shown here, transiently replaces Pds5. Scc1 mutations that compromise its interaction with Scc2 adversely affect cohesin's ATPase activity and loading. Moreover, Scc2 mutations that alter ...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1016/j.molcel.2018.05.022

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Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
Role:
Author
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Howard Hughes Medical Institute More from this funder
Publisher:
Elsevier Publisher's website
Journal:
Molecular cell Journal website
Volume:
70
Issue:
6
Pages:
1134-1148.e7
Publication date:
2018-06-21
Acceptance date:
2018-05-18
DOI:
EISSN:
1097-4164
ISSN:
1097-2765
Pmid:
29932904
Source identifiers:
859108
Language:
English
Keywords:
Pubs id:
pubs:859108
UUID:
uuid:4e61e11b-9c8c-4e6b-b33f-ebe7214ff2e8
Local pid:
pubs:859108
Deposit date:
2019-02-27

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