Proteolytic activation of UmuD and MucA proteins for SOS mutagenesis.
SOS mutagenesis in Escherichia coli requires the functions of the umuD, C genes, or their functional analogues mucA, B derived from a plasmid pKM101, and the recA gene. However, mere derepression of these SOS genes does not increase the ability of the cell to perform mutagenesis. Activation of RecA protein to a form (RecA*) that mediates cleavage of the LexA repressor is required for mutagenesis. We present evidence that UmuD and MucA are proteolytically processed by RecA* and that the processed products are the active forms involved in mutagenesis.
Shiba
T
T
Department of Experimental Chemotherapy, Osaka University, Japan.
Iwasaki
H
H
Nakata
A
A
Shinagawa
H
H
D001426:Bacterial Proteins / Q000378:metabolism*; D004249:DNA Damage; D004260:DNA Repair; D004259:DNA-Directed DNA Polymerase; D004789:Enzyme Activation; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins; D015964:Gene Expression Regulation, Bacterial; D009154:Mutation; D011499:Protein Processing, Post-Translational; D011938:Rec A Recombinases / Q000378:metabolism*; D012697:Serine Endopeptidases; D000099160:LexA Repressor Protein
D001426:Bacterial Proteins; D004259:DNA-Directed DNA Polymerase; D029968:Escherichia coli Proteins; D011938:Rec A Recombinases; D012697:Serine Endopeptidases; D000099160:LexA Repressor Protein; C063757:MucA protein, Bacteria; C055218:UmuD protein, E coli