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An asymmetric SMC-kleisin bridge in prokaryotic condensin.
- Source :
- Nature Structural & Molecular Biology; Mar2013, Vol. 20 Issue 3, p371-379, 9p, 7 Diagrams, 2 Charts
- Publication Year :
- 2013
-
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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 15459993
- Volume :
- 20
- Issue :
- 3
- Database :
- Complementary Index
- Journal :
- Nature Structural & Molecular Biology
- Publication Type :
- Academic Journal
- Accession number :
- 85891702
- Full Text :
- https://doi.org/10.1038/nsmb.2488