Show simple item record

dc.contributor.authorBoyer, Laurie A.
dc.contributor.authorLogie, Colin
dc.contributor.authorBonte, Edgar
dc.contributor.authorBecker, Peter B.
dc.contributor.authorWade, Paul A.
dc.contributor.authorWolffe, Alan P.
dc.contributor.authorWu, Carl
dc.contributor.authorImbalzano, Anthony N.
dc.contributor.authorPeterson, Craig L.
dc.date2022-08-11T08:08:49.000
dc.date.accessioned2022-08-23T16:09:10Z
dc.date.available2022-08-23T16:09:10Z
dc.date.issued2000-04-26
dc.date.submitted2008-08-05
dc.identifier.citationJ Biol Chem. 2000 Jun 23;275(25):18864-70. <a href="http://dx.doi.org/10.1074/jbc.M002810200">Link to article on publisher's site</a>
dc.identifier.issn0021-9258 (Print)
dc.identifier.doi10.1074/jbc.M002810200
dc.identifier.pmid10779516
dc.identifier.urihttp://hdl.handle.net/20.500.14038/32628
dc.description.abstractATP-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.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10779516&dopt=Abstract ">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1074/jbc.M002810200
dc.subjectAdenosine Triphosphatases; Adenosine Triphosphate; Chromatin; Kinetics; Protein Conformation; Trans-Activators
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleFunctional delineation of three groups of the ATP-dependent family of chromatin remodeling enzymes
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume275
dc.source.issue25
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/119
dc.identifier.contextkey566373
html.description.abstract<p>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.</p>
dc.identifier.submissionpathgsbs_sp/119
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentDepartment of Cell Biology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages18864-70


This item appears in the following Collection(s)

Show simple item record