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dc.contributor.authorPollard, Kerri Jeanne
dc.contributor.authorPeterson, Craig L.
dc.date2022-08-11T08:09:03.000
dc.date.accessioned2022-08-23T16:16:30Z
dc.date.available2022-08-23T16:16:30Z
dc.date.issued1998-11-20
dc.date.submitted2008-11-26
dc.identifier.citationBioessays. 1998 Sep;20(9):771-80. <a href="http://dx.doi.org/10.1002/(SICI)1521-1878(199809)20:9<771::AID-BIES10>3.0.CO;2-V ">Link to article on publisher's site</a>
dc.identifier.issn0265-9247 (Print)
dc.identifier.doi10.1002/(SICI)1521-1878(199809)20:9<771::AID-BIES10>3.0.CO;2-V
dc.identifier.pmid9819566
dc.identifier.urihttp://hdl.handle.net/20.500.14038/34348
dc.description.abstractThe compaction of the eukaryotic genome into a highly folded chromatin structure necessitates cellular mechanisms for allowing access of regulatory proteins to the DNA template. Recent advances in the fields of gene silencing, transcription, recombination, and DNA repair have led to the identification of two distinct families of chromatin remodeling enzymes--nuclear histone acetyltransferases and multisubunit complexes that harbor a SWI2/SNF2 ATPase family member. This paper reviews the current notion of how these enzymes function in remodeling chromatin; we then discuss some tantalizing lines of evidence that lead to the hypothesis that members of both families may actually function in concert to facilitate cellular processes in the context of chromatin.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=9819566&dopt=Abstract">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1002/(SICI)1521-1878(199809)20:9<771::AID-BIES10>3.0.CO;2-V
dc.subjectAcetylation; Acetyltransferases; Adenosine Triphosphatases; Animals; Chromatin; Chromosomal Proteins, Non-Histone; DNA Helicases; DNA-Binding Proteins; Fungal Proteins; *Gene Expression Regulation; Histone Acetyltransferases; Histones; Humans; Macromolecular Substances; Models, Genetic; Multienzyme Complexes; Multigene Family; *Nuclear Proteins; Nucleosomes; Protein Processing, Post-Translational; *Saccharomyces cerevisiae Proteins; Transcription Factors; Transcription, Genetic
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleChromatin remodeling: a marriage between two families
dc.typeJournal Article
dc.source.journaltitleBioEssays : news and reviews in molecular, cellular and developmental biology
dc.source.volume20
dc.source.issue9
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/995
dc.identifier.contextkey673211
html.description.abstract<p>The compaction of the eukaryotic genome into a highly folded chromatin structure necessitates cellular mechanisms for allowing access of regulatory proteins to the DNA template. Recent advances in the fields of gene silencing, transcription, recombination, and DNA repair have led to the identification of two distinct families of chromatin remodeling enzymes--nuclear histone acetyltransferases and multisubunit complexes that harbor a SWI2/SNF2 ATPase family member. This paper reviews the current notion of how these enzymes function in remodeling chromatin; we then discuss some tantalizing lines of evidence that lead to the hypothesis that members of both families may actually function in concert to facilitate cellular processes in the context of chromatin.</p>
dc.identifier.submissionpathgsbs_sp/995
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentDepartment of Biochemistry and Molecular Biology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages771-80


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