Allosteric regulation of RecA protein function is mediated by Gln194
UMass Chan AffiliationsDepartment of Biochemistry and Molecular Pharmacology
Graduate School of Biomedical Sciences
Document TypeJournal Article
KeywordsAdenosine Triphosphatases; Adenosine Triphosphate; Allosteric Regulation; Binding Sites; DNA, Single-Stranded; Glutamine; Hydrolysis; Models, Molecular; Mutagenesis, Site-Directed; Rec A Recombinases; Structure-Activity Relationship
Medicine and Health Sciences
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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.
J Biol Chem. 1997 Oct 10;272(41):25778-82.
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/33945