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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.

Original publication




Journal article



Publication Date





3692 - 3702


Cohesin complex, Eco1 acetylation, Maintenance of cohesion, Releasing activity, SA/STAG domain, Scc3, Sister chromatid separation, Smc proteins, Acetylation, Amino Acid Sequence, Binding Sites, Cell Cycle Proteins, Chromosomal Proteins, Non-Histone, G2 Phase Cell Cycle Checkpoints, Molecular Sequence Data, Protein Subunits, Proteolysis, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins