title: Control of Smc Coiled Coil Architecture by the ATPase Heads Facilitates Targeting to Chromosomal ParB/parS and Release onto Flanking DNA.
abstract: Smc/ScpAB promotes chromosome segregation in prokaryotes, presumably by compacting and resolving nascent sister chromosomes. The underlying mechanisms, however, are poorly understood. Here, we investigate the role of the Smc ATPase activity in the recruitment of Smc/ScpAB to the Bacillus subtilis chromosome. We demonstrate that targeting of Smc/ScpAB to ParB/parS loading sites is strictly dependent on engagement of Smc head domains and relies on an open organization of the Smc coiled coils. We find that dimerization of the Smc hinge domain stabilizes closed Smc rods and hinders head engagement as well as chromosomal targeting. Conversely, the ScpAB sub-complex promotes head engagement and Smc rod opening and thereby facilitates recruitment of Smc to parS sites. Upon ATP hydrolysis, Smc/ScpAB is released from loading sites and relocates within the chromosome-presumably through translocation along DNA double helices. Our findings define an intermediate state in the process of chromosome organization by Smc.
authors.affiliation: Research Group 'Chromosome Organization and Dynamics', Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
authors.forename: Anita
authors.initials: A
authors.lastname: Minnen
authors.affiliation: Research Group 'Chromosome Organization and Dynamics', Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
authors.forename: Frank
authors.initials: F
authors.lastname: Bürmann
authors.affiliation: Research Group 'Chromosome Organization and Dynamics', Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
authors.forename: Larissa
authors.initials: L
authors.lastname: Wilhelm
authors.affiliation: Research Group 'Chromosome Organization and Dynamics', Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
authors.forename: Anna
authors.initials: A
authors.lastname: Anchimiuk
authors.affiliation: Research Group 'Chromosome Organization and Dynamics', Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
authors.forename: Marie-Laure
authors.initials: ML
authors.lastname: Diebold-Durand
authors.affiliation: Research Group 'Chromosome Organization and Dynamics', Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany. Electronic address: sgruber@biochem.mpg.de.
authors.forename: Stephan
authors.initials: S
authors.lastname: Gruber
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism*; D002455:Cell Division; D020090:Chromosome Segregation; D002876:Chromosomes, Bacterial / Q000737:chemistry* / Q000648:ultrastructure; D019915:DNA Primase / Q000235:genetics / Q000378:metabolism*; D004269:DNA, Bacterial / Q000235:genetics / Q000378:metabolism*; D006868:Hydrolysis; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D000072417:Protein Domains; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D021381:Protein Transport; D016415:Sequence Alignment
chemical_list: D001426:Bacterial Proteins; D018797:Cell Cycle Proteins; D004269:DNA, Bacterial; D007527:Isoenzymes; C118650:SMC protein, Bacteria; C509375:ScpA protein, Bacillus subtilis; D000255:Adenosine Triphosphate; D019915:DNA Primase