Allosteric regulation of RecA protein function is mediated by Gln194
UMass Chan Affiliations
Department of Biochemistry and Molecular PharmacologyGraduate School of Biomedical Sciences
Document Type
Journal ArticlePublication Date
1997-11-05Keywords
Adenosine Triphosphatases; Adenosine Triphosphate; Allosteric Regulation; Binding Sites; DNA, Single-Stranded; Glutamine; Hydrolysis; Models, Molecular; Mutagenesis, Site-Directed; Rec A Recombinases; Structure-Activity RelationshipLife Sciences
Medicine and Health Sciences
Metadata
Show full item recordAbstract
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.Source
J Biol Chem. 1997 Oct 10;272(41):25778-82.
DOI
10.1074/jbc.272.41.25778Permanent Link to this Item
http://hdl.handle.net/20.500.14038/33945PubMed ID
9325305Related Resources
ae974a485f413a2113503eed53cd6c53
10.1074/jbc.272.41.25778