Functional delineation of three groups of the ATP-dependent family of chromatin remodeling enzymes
dc.contributor.author | Boyer, Laurie A. | |
dc.contributor.author | Logie, Colin | |
dc.contributor.author | Bonte, Edgar | |
dc.contributor.author | Becker, Peter B. | |
dc.contributor.author | Wade, Paul A. | |
dc.contributor.author | Wolffe, Alan P. | |
dc.contributor.author | Wu, Carl | |
dc.contributor.author | Imbalzano, Anthony N. | |
dc.contributor.author | Peterson, Craig L. | |
dc.date | 2022-08-11T08:08:49.000 | |
dc.date.accessioned | 2022-08-23T16:09:10Z | |
dc.date.available | 2022-08-23T16:09:10Z | |
dc.date.issued | 2000-04-26 | |
dc.date.submitted | 2008-08-05 | |
dc.identifier.citation | J 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.issn | 0021-9258 (Print) | |
dc.identifier.doi | 10.1074/jbc.M002810200 | |
dc.identifier.pmid | 10779516 | |
dc.identifier.uri | http://hdl.handle.net/20.500.14038/32628 | |
dc.description.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. | |
dc.language.iso | en_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.url | http://dx.doi.org/10.1074/jbc.M002810200 | |
dc.subject | Adenosine Triphosphatases; Adenosine Triphosphate; Chromatin; Kinetics; Protein Conformation; Trans-Activators | |
dc.subject | Life Sciences | |
dc.subject | Medicine and Health Sciences | |
dc.title | Functional delineation of three groups of the ATP-dependent family of chromatin remodeling enzymes | |
dc.type | Journal Article | |
dc.source.journaltitle | The Journal of biological chemistry | |
dc.source.volume | 275 | |
dc.source.issue | 25 | |
dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/gsbs_sp/119 | |
dc.identifier.contextkey | 566373 | |
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.submissionpath | gsbs_sp/119 | |
dc.contributor.department | Program in Molecular Medicine | |
dc.contributor.department | Department of Cell Biology | |
dc.contributor.department | Graduate School of Biomedical Sciences | |
dc.source.pages | 18864-70 |