期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 20, 期 3, 页码 371-379出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2488
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资金
- Max Planck Society
- European Research Council ERC StG [260853]
- National Research Foundation of Korea [2012-0005612]
- European Research Council (ERC) [260853] Funding Source: European Research Council (ERC)
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 sub fills 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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