title: Condensin but not cohesin SMC heterodimer induces DNA reannealing through protein-protein assembly.
abstract: Condensin and cohesin are chromosomal protein complexes required for chromosome condensation and sister chromatid cohesion, respectively. They commonly contain the SMC (structural maintenance of chromosomes) subunits consisting of a long coiled-coil with the terminal globular domains and the central hinge. Condensin and cohesin holo-complexes contain three and two non-SMC subunits, respectively. In this study, DNA interaction with cohesin and condensin complexes purified from fission yeast was investigated. The DNA reannealing activity is strong for condensin SMC heterodimer but weak for holo-condensin, whereas no annealing activity is found for cohesin heterodimer SMC and Rad21-bound heterotrimer complexes. One set of globular domains of the same condensin SMC is essential for the DNA reannealing activity. In addition, the coiled-coil and hinge region of another SMC are needed. Atomic force microscopy discloses the molecular events of DNA reannealing. SMC assembly that occurs on reannealing DNA seems to be a necessary intermediary step. SMC is eliminated from the completed double-stranded DNA. The ability of heterodimeric SMC to reanneal DNA may be regulated in vivo possibly through the non-SMC heterotrimeric complex.
authors.affiliation: Department of Biophysics, Graduate School of Science, Graduate School of Biostudies, Kyoto University, Kyoto 606-8502, Japan.
authors.forename: Akiko
authors.initials: A
authors.lastname: Sakai
authors.forename: Kohji
authors.initials: K
authors.lastname: Hizume
authors.forename: Takashi
authors.initials: T
authors.lastname: Sutani
authors.forename: Kunio
authors.initials: K
authors.lastname: Takeyasu
authors.forename: Mitsuhiro
authors.initials: M
authors.lastname: Yanagida
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism*; D018797:Cell Cycle Proteins; D002843:Chromatin / Q000378:metabolism; D002868:Chromosomal Proteins, Non-Histone; D004271:DNA, Fungal / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D019281:Dimerization; D005656:Fungal Proteins; D046912:Multiprotein Complexes; D009687:Nuclear Proteins / Q000737:chemistry* / Q000378:metabolism*; D009690:Nucleic Acid Conformation; D010750:Phosphoproteins / Q000378:metabolism; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012568:Schizosaccharomyces / Q000235:genetics / Q000378:metabolism; D029702:Schizosaccharomyces pombe Proteins / Q000737:chemistry* / Q000378:metabolism*; D000097722:Cohesins
chemical_list: D000251:Adenosine Triphosphatases; D018797:Cell Cycle Proteins; D002843:Chromatin; D002868:Chromosomal Proteins, Non-Histone; D004271:DNA, Fungal; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D046912:Multiprotein Complexes; D009687:Nuclear Proteins; D010750:Phosphoproteins; D021122:Protein Subunits; D011994:Recombinant Proteins; D029702:Schizosaccharomyces pombe Proteins; D000097722:Cohesins; C092957:Rad21 protein, S pombe; C108312:condensin complexes