PMID:8513500

Citation	Kim, B and Little, JW (1993) LexA and lambda Cl repressors as enzymes: specific cleavage in an intermolecular reaction. Cell 73:1165-73
Abstract	During the SOS response, LexA repressor is inactivated by specific cleavage. Although cleavage requires RecA protein in vivo, RecA acts indirectly as a coprotease by stimulating an inherent self-cleavage activity of LexA. In lambda lysogens, cleavage of lambda Cl repressor in a similar but far slower reaction results in prophage induction. We describe an intermolecular cleavage reaction in which the C-terminal fragment of LexA acted as an enzyme to cleave other molecules of LexA. The C-terminal fragment of lambda repressor cleaved the LexA substrates about as efficiently as did the LexA enzyme, suggesting that the slow rate of Cl self-cleavage results from a weak interaction between its cleavage site and the active site.
Links	PubMed
Keywords	Bacterial Proteins/metabolism; Binding Sites; DNA-Binding Proteins; Enzyme Activation; Enzymes/metabolism; Escherichia coli/enzymology; Gene Expression Regulation, Bacterial; Mutation; Rec A Recombinases/metabolism; Repressor Proteins/metabolism; Serine Endopeptidases; Substrate Specificity; Viral Proteins; Viral Regulatory and Accessory Proteins
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