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    Functional delineation of three groups of the ATP-dependent family of chromatin remodeling enzymes

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    Authors
    Boyer, Laurie A.
    Logie, Colin
    Bonte, Edgar
    Becker, Peter B.
    Wade, Paul A.
    Wolffe, Alan P.
    Wu, Carl
    Imbalzano, Anthony N.
    Peterson, Craig L.
    UMass Chan Affiliations
    Program in Molecular Medicine
    Department of Cell Biology
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    2000-04-26
    Keywords
    Adenosine Triphosphatases; Adenosine Triphosphate; Chromatin; Kinetics; Protein Conformation; Trans-Activators
    Life Sciences
    Medicine and Health Sciences
    
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    Link to Full Text
    http://dx.doi.org/10.1074/jbc.M002810200
    Abstract
    ATP-dependent chromatin remodeling enzymes antagonize the inhibitory effects of chromatin. We compare six different remodeling complexes: ySWI/SNF, yRSC, hSWI/SNF, xMi-2, dCHRAC, and dNURF. We find that each complex uses similar amounts of ATP to remodel nucleosomal arrays at nearly identical rates. We also perform assays with arrays reconstituted with hyperacetylated or trypsinized histones and isolated histone (H3/H4)(2) tetramers. The results define three groups of the ATP-dependent family of remodeling enzymes. In addition we investigate the ability of an acidic activator to recruit remodeling complexes to nucleosomal arrays. We propose that ATP-dependent chromatin remodeling enzymes share a common reaction mechanism and that a key distinction between complexes is in their mode of regulation or recruitment.
    Source
    J Biol Chem. 2000 Jun 23;275(25):18864-70. Link to article on publisher's site
    DOI
    10.1074/jbc.M002810200
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/32628
    PubMed ID
    10779516
    Related Resources
    Link to article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1074/jbc.M002810200
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    Morningside Graduate School of Biomedical Sciences Scholarly Publications

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