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Sister chromatid cohesion is mediated by cohesin, whose Smc1, Smc3, and kleisin (Scc1) subunits form a ring structure that entraps sister DNAs. The ring is opened either by separase, which cleaves Scc1 during anaphase, or by a releasing activity involving Wapl, Scc3, and Pds5, which bind to Scc1 and open its interface with Smc3. We present crystal structures of Pds5 from the yeast L. thermotolerans in the presence and absence of the conserved Scc1 region that interacts with Pds5. Scc1 binds along the spine of the Pds5 HEAT repeat fold and is wedged between the spine and C-terminal hook of Pds5. We have isolated mutants that confirm the observed binding mode of Scc1 and verified their effect on cohesin by immunoprecipitation and calibrated ChIP-seq. The Pds5 structure also reveals architectural similarities to Scc3, the other large HEAT repeat protein of cohesin and, most likely, Scc2.

Original publication

DOI

10.1016/j.celrep.2016.02.020

Type

Journal article

Journal

Cell Rep

Publication Date

08/03/2016

Volume

14

Pages

2108 - 2115

Keywords

Scc3, Smc proteins, sister chromatid cohesion, Amino Acid Sequence, Binding Sites, Cell Cycle Proteins, Chromosomal Proteins, Non-Histone, Crystallography, X-Ray, Fungal Proteins, Models, Molecular, Protein Binding, Protein Conformation, alpha-Helical, Protein Interaction Domains and Motifs, Protein Structure, Quaternary, Saccharomycetales, Structural Homology, Protein