Differential expression of SOS genes in an E. coli mutant producing unstable lexA protein enhances excision repair but inhibits mutagenesis.
The lexA41 mutant of E. coli is a UV-resistant derivative of another mutant, lexA3, which produces a repressor that is not cleaved following inducing treatments. lexA41 carried an additional mutation which changed amino acid 132 in the LexA protein from Ala to Thr. The resultant protein was unstable and was degraded both before and after an inducing treatment. This instability was greater at 42 degrees than at 30 degrees. The protein was more stable in Lon- mutants at both temperatures. lac operon fusions to most of the genes in the SOS regulon were used to show that the various damage-inducible genes were derepressed to different extents. uvrA, B, and D were almost fully derepressed. Consistant with this finding, the rate of removal of T4 endonuclease V-sensitive sites was more rapid in the UV-irradiated lexA41 mutant than in normal cells, suggesting a more active excision repair system. We propose that the instability of the LexA41 protein reduces the intracellular concentration of repressor to a level that allows a high level of excision repair. The additional observation that SOS mutagenesis was only weakly induced in a lexA41 uvrA- mutant implies that the mutant protein partially represses one or more genes whose products promote SOS mutagenesis.
D000483:Alleles; D001426:Bacterial Proteins / Q000235:genetics*; D003001:Cloning, Molecular; D004260:DNA Repair; D004262:DNA Restriction Enzymes; D004926:Escherichia coli / Q000235:genetics* / Q000528:radiation effects; D005796:Genes / Q000528:radiation effects*; D005798:Genes, Bacterial / Q000528:radiation effects*; D009154:Mutation; D010641:Phenotype; D012697:Serine Endopeptidases; D013489:Suppression, Genetic; D013696:Temperature; D014466:Ultraviolet Rays; D000099160:LexA Repressor Protein
D001426:Bacterial Proteins; D004262:DNA Restriction Enzymes; D012697:Serine Endopeptidases; D000099160:LexA Repressor Protein