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Breaking symmetry in SMCs

Nature Structural & Molecular Biology volume 20, pages 246–249 (2013)Cite this article

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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.

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Figure 1: Schematic of Smc complex organization.
Figure 2: A single ScpA bridges an Smc dimer in a tripartite ring in vivo.

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Authors and Affiliations

  1. Amy L. Upton and David J. Sherratt are in the Department of Biochemistry, University of Oxford, Oxford, UK.,

    Amy L Upton & David J Sherratt

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  1. Amy L Upton
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  2. David J Sherratt
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Correspondence to David J Sherratt.

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The authors declare no competing financial interests.

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Upton, A., Sherratt, D. Breaking symmetry in SMCs. Nat Struct Mol Biol 20, 246–249 (2013). https://doi.org/10.1038/nsmb.2525

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