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An asymmetric SMC–kleisin bridge in prokaryotic condensin
Bü,rmann, Frank,Shin, Ho-Chul,Basquin, Jé,rô,me,Soh, Young-Min,Gimé,nez-Oya, Victor,Kim, Yeon-Gil,Oh, Byung-Ha,Gruber, Stephan Nature Publishing Group, a division of Macmillan P 2013 Nature structural & molecular biology Vol.20 No.3
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.