title: A prokaryotic condensin/cohesin-like complex can actively compact chromosomes from a single position on the nucleoid and binds to DNA as a ring-like structure.
abstract: We show that Bacillus subtilis SMC (structural maintenance of chromosome protein) localizes to discrete foci in a cell cycle-dependent manner. Early in the cell cycle, SMC moves from the middle of the cell toward opposite cell poles in a rapid and dynamic manner and appears to interact with different regions on the chromosomes during the cell cycle. SMC colocalizes with its interacting partners, ScpA and ScpB, and the specific localization of SMC depends on both Scp proteins, showing that all three components of the SMC complex are required for proper localization. Cytological and biochemical experiments showed that dimeric ScpB stabilized the binding of ScpA to the SMC head domains. Purified SMC showed nonspecific binding to double-stranded DNA, independent of Scp proteins or ATP, and was retained on DNA after binding to closed DNA but not to linear DNA. The SMC head domains and hinge region did not show strong DNA binding activity, suggesting that the coiled-coil regions in SMC mediate an association with DNA and that SMC binds to DNA as a ring-like structure. The overproduction of SMC resulted in global chromosome compaction, while SMC was largely retained in bipolar foci, suggesting that the SMC complex forms condensation centers that actively affect global chromosome compaction from a defined position on the nucleoid.
authors.affiliation: Biochemie, Fachbereich Chemie, Philipps-Universität Marburg. Max-Planck Institut für Terrestrische Mikrobiologie, Marburg, Germany.
authors.forename: A
authors.initials: A
authors.lastname: Volkov
authors.forename: J
authors.initials: J
authors.lastname: Mascarenhas
authors.forename: C
authors.initials: C
authors.lastname: Andrei-Selmer
authors.forename: H D
authors.initials: HD
authors.lastname: Ulrich
authors.forename: P L
authors.initials: PL
authors.lastname: Graumann
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D018829:Adhesins, Bacterial; D001412:Bacillus subtilis / Q000502:physiology*; D001426:Bacterial Proteins / Q000235:genetics / Q000502:physiology*; D015153:Blotting, Western; D002453:Cell Cycle; D018797:Cell Cycle Proteins / Q000235:genetics / Q000502:physiology*; D002467:Cell Nucleus / Q000378:metabolism; D002499:Centrifugation, Density Gradient; D002850:Chromatography, Gel; D002875:Chromosomes / Q000648:ultrastructure; D004247:DNA / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism; D004996:Ethidium / Q000494:pharmacology; D005838:Genotype; D013058:Mass Spectrometry; D008856:Microscopy, Fluorescence; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D013395:Sucrose / Q000494:pharmacology; D020349:Surface Plasmon Resonance
chemical_list: D018829:Adhesins, Bacterial; D001426:Bacterial Proteins; D018797:Cell Cycle Proteins; C118650:SMC protein, Bacteria; D013395:Sucrose; D000255:Adenosine Triphosphate; D004247:DNA; D010450:Endopeptidases; C053088:C5a peptidase; D004996:Ethidium