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- 저자 : Basquin, Jé (검색결과 2 건)
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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.
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Structure of Full-Length SMC and Rearrangements Required for Chromosome Organization
Diebold-Durand, Marie-Laure,Lee, Hansol,Ruiz Avila, Laura B.,Noh, Haemin,Shin, Ho-Chul,Im, Haeri,Bock, Florian P.,Bü,rmann, Frank,Durand, Alexandre,Basfeld, Alrun,Ham, Sihyun,Basquin, Jé,r&o Cell Press 2017 Molecular cell Vol.67 No.2
<▼1><P><B>Summary</B></P><P>Multi-subunit SMC complexes control chromosome superstructure and promote chromosome disjunction, conceivably by actively translocating along DNA double helices. SMC subunits comprise an ABC ATPase “head” and a “hinge” dimerization domain connected by a 49 nm coiled-coil “arm.” The heads undergo ATP-dependent engagement and disengagement to drive SMC action on the chromosome. Here, we elucidate the architecture of prokaryotic Smc dimers by high-throughput cysteine cross-linking and crystallography. Co-alignment of the Smc arms tightly closes the interarm space and misaligns the Smc head domains at the end of the rod by close apposition of their ABC signature motifs. Sandwiching of ATP molecules between Smc heads requires them to substantially tilt and translate relative to each other, thereby opening up the Smc arms. We show that this mechanochemical gating reaction regulates chromosome targeting and propose a mechanism for DNA translocation based on the merging of DNA loops upon closure of Smc arms.</P></▼1><▼2><P><B>Highlights</B></P><P>•<P>Crystallography and in vivo cross-linking reveal the architecture of prokaryotic Smc</P>•<P>Juxtaposition of the Smc arms misaligns the two Smc ATPase domains</P>•<P>Smc head engagement mechanically opens an interarm space</P>•<P>A model for DNA loop extrusion driven by the SMC ATPase cycle is presented</P></P></▼2><▼3><P>By combining high-throughput in vivo cysteine cross-linking and crystallography, Diebold-Durand et al. construct a high-resolution model of full-length prokaryotic Smc. It reveals that the rod-shaped Smc dimer lacks chambers for DNA and features misaligned head domains. Smc head engagement mechanically opens an interarm space.</P></▼3>
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