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dc.contributor.authorRichmond, Emilie
dc.contributor.authorPeterson, Craig L.
dc.date2022-08-11T08:09:35.000
dc.date.accessioned2022-08-23T16:36:47Z
dc.date.available2022-08-23T16:36:47Z
dc.date.issued1996-10-01
dc.date.submitted2009-04-02
dc.identifier.citationNucleic Acids Res. 1996 Oct 1;24(19):3685-92.
dc.identifier.issn0305-1048 (Print)
dc.identifier.pmid8871545
dc.identifier.urihttp://hdl.handle.net/20.500.14038/38866
dc.description.abstractThe yeast SWI2/SNF2 polypeptide is a subunit of the SWI/SNF protein complex that is required for many transcriptional activators to function in a chromatin context. SWI2 is believed to be the founding member of a new subfamily of DNA-stimulated ATPases/DNA helicases that includes proteins that function in DNA repair (RAD5, RAD16, ERCC6), recombination (RAD54), transcription (MOT1, ISWI, brm, BRG1, hBRM) and cell cycle control (STH1). We have created a set of 16 mutations within the SWI2 ATPase domain and have analyzed the functional consequences of these mutations in vivo. We have identified residues within each of the seven ATPase motifs that are required for SWI2 function. We have also identified crucial residues that are interspersed between the known ATPase motifs. In contrast, we identify other highly conserved residues that appear to be dispensable for SWI2 function. We also find that single amino acid changes in ATPase motifs IV and VI lead to a dominant negative phenotype. None of the 12 SWI2 mutations that disrupt SWI2 activity in vivo alter the assembly of the SWI/SNF complex. These studies provide an invaluable framework for biochemical analysis of the SWI2 ATPase and for functional analysis of other SWI2 family members.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=8871545&dopt=Abstract">Link to Article in PubMed</a>
dc.subjectAdenosine Triphosphatases
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectCarrier Proteins
dc.subjectDNA
dc.subjectDNA Helicases
dc.subjectDNA-Binding Proteins
dc.subjectEnzyme Activation
dc.subjectFungal Proteins
dc.subjectHumans
dc.subject*Membrane Transport Proteins
dc.subjectMolecular Sequence Data
dc.subject*Nuclear Proteins
dc.subjectPlant Proteins
dc.subjectPoint Mutation
dc.subjectSaccharomyces cerevisiae
dc.subject*Saccharomyces cerevisiae Proteins
dc.subjectSequence Homology, Amino Acid
dc.subjectTrans-Activation (Genetics)
dc.subjectTranscription Factors
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleFunctional analysis of the DNA-stimulated ATPase domain of yeast SWI2/SNF2
dc.typeArticle
dc.source.journaltitleNucleic acids research
dc.source.volume24
dc.source.issue19
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=2702&amp;context=oapubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/1703
dc.identifier.contextkey808466
refterms.dateFOA2022-08-23T16:36:47Z
html.description.abstract<p>The yeast SWI2/SNF2 polypeptide is a subunit of the SWI/SNF protein complex that is required for many transcriptional activators to function in a chromatin context. SWI2 is believed to be the founding member of a new subfamily of DNA-stimulated ATPases/DNA helicases that includes proteins that function in DNA repair (RAD5, RAD16, ERCC6), recombination (RAD54), transcription (MOT1, ISWI, brm, BRG1, hBRM) and cell cycle control (STH1). We have created a set of 16 mutations within the SWI2 ATPase domain and have analyzed the functional consequences of these mutations in vivo. We have identified residues within each of the seven ATPase motifs that are required for SWI2 function. We have also identified crucial residues that are interspersed between the known ATPase motifs. In contrast, we identify other highly conserved residues that appear to be dispensable for SWI2 function. We also find that single amino acid changes in ATPase motifs IV and VI lead to a dominant negative phenotype. None of the 12 SWI2 mutations that disrupt SWI2 activity in vivo alter the assembly of the SWI/SNF complex. These studies provide an invaluable framework for biochemical analysis of the SWI2 ATPase and for functional analysis of other SWI2 family members.</p>
dc.identifier.submissionpathoapubs/1703
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentDepartment of Biochemistry and Molecular Biology
dc.source.pages3685-92


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