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

FEBS letters | 2014

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.

Pubmed ID: 25171859 RIS Download

Research resources used in this publication

None found

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Associated grants

  • Agency: Cancer Research UK, United Kingdom
    Id: C573/A 12386
  • Agency: Wellcome Trust, United Kingdom
    Id: 091859/Z/10/Z
  • Agency: Medical Research Council, United Kingdom
    Id: U10518432
  • Agency: Wellcome Trust, United Kingdom
  • Agency: Wellcome Trust, United Kingdom
    Id: 095514
  • Agency: Cancer Research UK, United Kingdom
    Id: 12386
  • Agency: Wellcome Trust, United Kingdom
    Id: 095514/Z/11/Z
  • Agency: Medical Research Council, United Kingdom
    Id: MC_U105184326

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