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FEBS Lett. 2014 Oct 16;588(20):3692-702. doi: 10.1016/j.febslet.2014.08.015. Epub 2014 Aug 27.

Structure and function of cohesin's Scc3/SA regulatory subunit.

Author information

1
Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.
2
MRC Laboratory of Molecular Biology, Structural Studies Division, Francis Crick Avenue, Cambridge CB2 0QH, United Kingdom. Electronic address: jyl@mrc-lmb.cam.ac.uk.
3
Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom. Electronic address: kim.nasmyth@bioch.ox.ac.uk.

Abstract

Sister chromatid cohesion involves entrapment of sister DNAs by a cohesin ring created through association of a kleisin subunit (Scc1) with ATPase heads of Smc1/Smc3 heterodimers. Cohesin's association with chromatin involves subunits recruited by Scc1: Wapl, Pds5, and Scc3/SA, in addition to Scc2/4 loading complex. Unlike Pds5, Wapl, and Scc2/4, Scc3s are encoded by all eukaryotic genomes. Here, a crystal structure of Scc3 reveals a hook-shaped protein composed of tandem α helices. Its N-terminal domain contains a conserved and essential surface (CES) present even in organisms lacking Pds5, Wapl, and Scc2/4, while its C-terminal domain binds a section of the kleisin Scc1. Scc3 turns over in G2/M while maintaining cohesin's association with chromosomes and it promotes de-acetylation of Smc3 upon Scc1 cleavage.

KEYWORDS:

Cohesin complex; Eco1 acetylation; Maintenance of cohesion; Releasing activity; SA/STAG domain; Scc3; Sister chromatid separation; Smc proteins

PMID:
25171859
PMCID:
PMC4175184
DOI:
10.1016/j.febslet.2014.08.015
[Indexed for MEDLINE]
Free PMC Article

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