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    SMC complexes differentially compact mitotic chromosomes according to genomic context

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    Authors
    Schalbetter, Stephanie Andrea
    Goloborodko, Anton
    Fudenberg, Geoffrey
    Belton, Jon-Matthew
    Miles, Catrina
    Yu, Miao
    Dekker, Job
    Mirny, Leonid
    Baxter, Jonathan
    UMass Chan Affiliations
    Department of Biochemistry and Molecular Pharmacology
    Program in Systems Biology
    Document Type
    Journal Article
    Publication Date
    2017-09-01
    Keywords
    Chromosome condensation
    Chromosome conformation capture-based methods
    Cohesion
    DNA sequencing
    Mitosis
    Computational Biology
    Genomics
    Structural Biology
    Systems Biology
    
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    Link to Full Text
    https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5640152/
    Abstract
    Structural maintenance of chromosomes (SMC) protein complexes are key determinants of chromosome conformation. Using Hi-C and polymer modelling, we study how cohesin and condensin, two deeply conserved SMC complexes, organize chromosomes in the budding yeast Saccharomyces cerevisiae. The canonical role of cohesin is to co-align sister chromatids, while condensin generally compacts mitotic chromosomes. We find strikingly different roles for the two complexes in budding yeast mitosis. First, cohesin is responsible for compacting mitotic chromosome arms, independently of sister chromatid cohesion. Polymer simulations demonstrate that this role can be fully accounted for through cis-looping of chromatin. Second, condensin is generally dispensable for compaction along chromosome arms. Instead, it plays a targeted role compacting the rDNA proximal regions and promoting resolution of peri-centromeric regions. Our results argue that the conserved mechanism of SMC complexes is to form chromatin loops and that distinct SMC-dependent looping activities are selectively deployed to appropriately compact chromosomes.
    Source

    Nat Cell Biol. 2017 Sep;19(9):1071-1080. doi: 10.1038/ncb3594. Epub 2017 Aug 21. Link to article on publisher's site

    DOI
    10.1038/ncb3594
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/49843
    PubMed ID
    28825700
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    Link to Article in PubMed

    ae974a485f413a2113503eed53cd6c53
    10.1038/ncb3594
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