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dc.contributor.authorKelley, Julie A.
dc.contributor.authorKnight, Kendall L.
dc.date2022-08-11T08:08:59.000
dc.date.accessioned2022-08-23T16:14:47Z
dc.date.available2022-08-23T16:14:47Z
dc.date.issued1997-11-05
dc.date.submitted2008-10-09
dc.identifier.citation<p>J Biol Chem. 1997 Oct 10;272(41):25778-82.</p>
dc.identifier.issn0021-9258 (Print)
dc.identifier.doi10.1074/jbc.272.41.25778
dc.identifier.pmid9325305
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33945
dc.description.abstractBinding of ATP to the RecA protein induces a high affinity DNA binding required for activation of enzyme function. Screens for in vivo recombination and repressor cleavage activities show Gln194 to be intolerant of all substitutions. Analyses of three mutant proteins (Q194N, Q194E, and Q194A) show that although basal enzyme function is maintained, each protein no longer displays an ATP-induced increase in DNA binding affinity. High salt activation of RecA function is also disrupted by these mutations. In contrast, ATP-induced changes in the oligomeric structure of RecA are maintained in the mutant proteins. These results demonstrate that Gln194 is a critical "allosteric switch" for ATP-induced activation of RecA function but is not the exclusive mediator of ATP-induced changes in RecA.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=9325305&dopt=Abstract">Link to article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1074/jbc.272.41.25778
dc.subjectAdenosine Triphosphatases; Adenosine Triphosphate; Allosteric Regulation; Binding Sites; DNA, Single-Stranded; Glutamine; Hydrolysis; Models, Molecular; Mutagenesis, Site-Directed; Rec A Recombinases; Structure-Activity Relationship
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleAllosteric regulation of RecA protein function is mediated by Gln194
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume272
dc.source.issue41
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/599
dc.identifier.contextkey646784
html.description.abstract<p>Binding of ATP to the RecA protein induces a high affinity DNA binding required for activation of enzyme function. Screens for in vivo recombination and repressor cleavage activities show Gln194 to be intolerant of all substitutions. Analyses of three mutant proteins (Q194N, Q194E, and Q194A) show that although basal enzyme function is maintained, each protein no longer displays an ATP-induced increase in DNA binding affinity. High salt activation of RecA function is also disrupted by these mutations. In contrast, ATP-induced changes in the oligomeric structure of RecA are maintained in the mutant proteins. These results demonstrate that Gln194 is a critical "allosteric switch" for ATP-induced activation of RecA function but is not the exclusive mediator of ATP-induced changes in RecA.</p>
dc.identifier.submissionpathgsbs_sp/599
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages25778-82


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