title: A mutant LexA repressor harboring a cleavage motif cysteine-glycine remains inducible.
abstract: Using site-directed mutagenesis of the lexA gene we have changed the amino acid Ala-84 of the LexA repressor for a cysteine. The reason for this change was the striking homology between LexA and UmuD and the comparable size of the two amino acid side chains. Using an in vivo repression/induction assay it is shown that the LexA-Cys-84 mutant remains inducible by mitomycin C and UV irradiation essentially in the same way as the wild-type repressor.
mesh_terms: D001426:Bacterial Proteins / Q000096:biosynthesis / Q000235:genetics*; D003545:Cysteine; D005786:Gene Expression Regulation / Q000187:drug effects / Q000528:radiation effects; D005798:Genes, Bacterial; D005998:Glycine; D016685:Mitomycin; D008937:Mitomycins / Q000494:pharmacology; D012097:Repressor Proteins / Q000096:biosynthesis / Q000235:genetics*; D013014:SOS Response, Genetics; D012697:Serine Endopeptidases; D014157:Transcription Factors / Q000235:genetics*; D014466:Ultraviolet Rays; D000099160:LexA Repressor Protein
chemical_list: D001426:Bacterial Proteins; D003545:Cysteine; D005998:Glycine; D016685:Mitomycin; D008937:Mitomycins; D012097:Repressor Proteins; D012697:Serine Endopeptidases; D014157:Transcription Factors; D000099160:LexA Repressor Protein