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http://purl.uniprot.org/citations/23353789http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23353789http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23353789http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/23353789http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.2488"xsd:string
http://purl.uniprot.org/citations/23353789http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.2488"xsd:string
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/author"Oh B.H."xsd:string
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/author"Oh B.H."xsd:string
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/author"Basquin J."xsd:string
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/author"Basquin J."xsd:string
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/author"Kim Y.G."xsd:string
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/author"Kim Y.G."xsd:string
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/author"Gruber S."xsd:string
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/author"Gruber S."xsd:string
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/author"Soh Y.M."xsd:string
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/author"Soh Y.M."xsd:string
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/author"Shin H.C."xsd:string
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/author"Shin H.C."xsd:string
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/author"Burmann F."xsd:string
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/author"Burmann F."xsd:string
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/author"Gimenez-Oya V."xsd:string
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/author"Gimenez-Oya V."xsd:string
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/23353789http://purl.uniprot.org/core/name"Nat Struct Mol Biol"xsd:string