Genetic control of damage-inducible restriction alleviation in Escherichia coli K12: an SOS function not repressed by lexA.
The alleviation of K-specific DNA restriction after treatment of cells by UV or nalidixic acid has been studied in mutants with various alleles of recA and lexA and combinations of these alleles and with recB and recF mutations. The studies show that induction of restriction alleviation by UV or nalidixic acid is abolished in mutants in which the recA protein is defective (recA13, recA56), its protease activity is altered (recA430) or in which it cannot be efficiently activated (recA142). Thermoinduction of restriction alleviation was observed in tif mutant (recA441). In lexA amber mutants restriction alleviation is not constitutive but is still inducible. In a lexA3 mutant restriction alleviation is inducible by nalidixic acid provided that recA protein is overproduced as a result of a recA operator mutation. Induction by UV depends on the recF function and an unidentified function (Y) which is controlled by the lexA protein. The recBC enzyme is necessary for induction by UV or by nalidixic acid. Temperature shift experiments with a thermosensitive recB mutant indicate that the recBC enzyme functions in an early step during UV-induction. It is concluded that the damage-inducible function which alleviates restriction is similar to other damage inducible repair (SOS) functions in the dependence on activated recA protease for induction, but that it differs from these functions by the absence of a direct control through the lexA repressor.
D001426:Bacterial Proteins / Q000502:physiology*; D004262:DNA Restriction Enzymes / Q000096:biosynthesis*; D015253:Deoxyribonucleases, Type I Site-Specific; D004790:Enzyme Induction / Q000187:drug effects / Q000528:radiation effects; D004926:Escherichia coli / Q000187:drug effects / Q000235:genetics* / Q000528:radiation effects; D029968:Escherichia coli Proteins; D043211:Exodeoxyribonuclease V; D005090:Exodeoxyribonucleases / Q000502:physiology; D009268:Nalidixic Acid / Q000494:pharmacology; D011938:Rec A Recombinases / Q000502:physiology; D012097:Repressor Proteins / Q000502:physiology*; D012697:Serine Endopeptidases; D014157:Transcription Factors / Q000502:physiology*; D014466:Ultraviolet Rays; D000099160:LexA Repressor Protein
D001426:Bacterial Proteins; D004262:DNA Restriction Enzymes; D015253:Deoxyribonucleases, Type I Site-Specific; D029968:Escherichia coli Proteins; D043211:Exodeoxyribonuclease V; D005090:Exodeoxyribonucleases; D009268:Nalidixic Acid; D011938:Rec A Recombinases; D012097:Repressor Proteins; D012697:Serine Endopeptidases; D014157:Transcription Factors; D000099160:LexA Repressor Protein; C468322:exodeoxyribonuclease V, E coli; C029602:endodeoxyribonuclease EcoK