title: Condensin II initiates sister chromatid resolution during S phase.
abstract: Condensins I and II are multisubunit complexes that play essential yet distinct functions in chromosome condensation and segregation in mitosis. Unlike condensin I, condensin II localizes to the nucleus during interphase, but it remains poorly understood what functions condensin II might have before mitotic entry. Here, we report that condensin II changes its chromatin-binding property during S phase. Remarkably, advanced premature chromosome condensation (PCC) assays enabled us to visualize condensin II forming "sister axes" in replicated regions of chromosomes in S phase cells. Depletion of condensin II compromised PCC-driven sister chromatid resolution during S phase. Moreover, fluorescence in situ hybridization assays revealed that condensin II, but not condensin I, promotes disjoining duplicated chromosomal loci during S phase. Application of mild replicative stress partially impaired this process and further exacerbated phenotypes arising from condensin II depletion. Our results suggest that condensin II initiates structural reorganization of duplicated chromosomes during S phase to prepare for their proper condensation and segregation in mitosis.
authors: Chromosome Dynamics Laboratory, RIKEN Advanced Science Institute, Wako, Saitama 351-0198, Japan.
authors: Takao
authors: T
authors: Ono
authors: Daisuke
authors: D
authors: Yamashita
authors: Tatsuya
authors: T
authors: Hirano
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism / Q000502:physiology*; D002842:Chromatids / Q000378:metabolism*; D004261:DNA Replication; D004268:DNA-Binding Proteins / Q000378:metabolism / Q000502:physiology*; D006367:HeLa Cells; D006801:Humans; D017404:In Situ Hybridization, Fluorescence; D046912:Multiprotein Complexes / Q000378:metabolism / Q000502:physiology*; D016196:S Phase; D013312:Stress, Physiological
chemical_list: D004268:DNA-Binding Proteins; D046912:Multiprotein Complexes; C108312:condensin complexes; D000251:Adenosine Triphosphatases
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