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Nat Struct Mol Biol. 2013 Mar;20(3):371-9. doi: 10.1038/nsmb.2488. Epub 2013 Jan 27.

An asymmetric SMC-kleisin bridge in prokaryotic condensin.

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1
Max Planck Research Group Chromosome Organization and Dynamics, Max Planck Institute of Biochemistry, Martinsried, Germany.

Abstract

Eukaryotic structural maintenance of chromosomes (SMC)-kleisin complexes form large, ring-shaped assemblies that promote accurate chromosome segregation. Their asymmetric structural core comprises SMC heterodimers that associate with both ends of a kleisin subunit. However, prokaryotic condensin Smc-ScpAB is composed of symmetric Smc homodimers associated with the kleisin ScpA in a postulated symmetrical manner. Here, we demonstrate that Smc molecules have two distinct binding sites for ScpA. The N terminus of ScpA binds the Smc coiled coil, whereas the C terminus binds the Smc ATPase domain. We show that in Bacillus subtilis cells, an Smc dimer is bridged by a single ScpAB to generate asymmetric tripartite rings analogous to eukaryotic SMC complexes. We define a molecular mechanism that ensures asymmetric assembly, and we conclude that the basic architecture of SMC-kleisin rings evolved before the emergence of eukaryotes.

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PMID:
23353789
DOI:
10.1038/nsmb.2488
[Indexed for MEDLINE]

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