Structural highlights
FunctionSCC3_YEAST Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the MCD1/SCC1 subunit of the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Publication Abstract from PubMedSister 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 alpha 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. Structure and function of cohesin's Scc3/SA regulatory subunit.,Roig MB, Lowe J, Chan KL, Beckouet F, Metson J, Nasmyth K FEBS Lett. 2014 Aug 27. pii: S0014-5793(14)00617-6. doi:, 10.1016/j.febslet.2014.08.015. PMID:25171859[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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