Breaking symmetry in SMCs

descriptionPublicationkeyboard_double_arrow_right Article 01 Mar 2013 English Publisher:Springer Science and Business Media LLCJournal:Nature Structural & Molecular Biology, volume 20, pages 246-249 (issn: 1545-9993, eissn: 1545-9985,

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Authors: Amy L, Upton; David J, Sherratt;

doi: 10.1038/nsmb.2525

pmid: 23463306

Breaking symmetry in SMCs

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Abstract

SMC (structural maintenance of chromosomes) protein complexes act in chromosome processing in all domains of life. In this issue, a study of the prokaryotic SMC complex Smc–ScpAB reveals an unanticipated asymmetry despite Smc forming a symmetric homodimer. This asymmetry—contributed by two distinct binding sites in Smc for the kleisin ScpA—is crucial for function in vivo and bears similarities to the eukaryotic complexes formed by Smc heterodimers.

Related Organizations

University of Oxford
United Kingdom

Keywords

Adenosine Triphosphatases, DNA-Binding Proteins, Bacterial Proteins, Multiprotein Complexes, Cell Cycle Proteins

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