Effects of the umuDC, mucAB, and samAB operons on the mutational specificity of chemical mutagenesis in Escherichia coli: I. Frameshift mutagenesis.
The specificity of frameshift mutations induced by several classes of chemical mutagens was determined using a collection of mutant E. coli lacZ genes. This collection can detect each of five kinds of specific frameshift events by scoring Lac+ revertant colonies. In addition, the mutational spectra were characterized in backgrounds carrying plasmids that encode the umuDC, mucAB, or samAB operon. 4-Nitroquinoline 1-oxide (4-NQO) and furylfuramide (AF-2) induced efficiently -1G, -2(C-G), and +1A frameshift mutations. 4-NQO and AF-2 differed in the ability for the induction of -1A and +1G frameshifts. +1A and -1A frameshift mutations induced by 4-NQO or AF-2 were enhanced by the introduction of the mucAB plasmid, and, to a lesser extent, the umuDC plasmid. The enhancing effect of the umuDC or mucAB plasmid on -1G and -2(C-G) frameshifts was weak or else not observed. 9-Aminoacridine was a potent inducer of +1G, -1G and -1A frameshifts, whereas ICR-191 induced all types of frameshift mutations. A mutation enhancing effect was observed only on ICR-191-induced +1A frameshift mutations by the introduction of the mucAB plasmid. Mitomycin C caused no appreciable induction of frameshift mutations to the tester strains without plasmid. However, all types of frameshifts, except -1G, were induced in the strains carrying the mucAB plasmid. N-methyl-N'-nitro-N-nitrosoguanidine induced all types of frameshift mutations. The mucAB plasmid enhanced mutagenesis in strains designed to detect the addition or loss of A.T base pair, indicating that the formation of +1A and -1A frameshifts was partly dependent on an error-prone SOS repair. Any frameshift mutagenesis was not affected by the samAB plasmid. In general, frameshifts in adenine runs were enhanced more preferentially by the mucAB and umuDC plasmids than frameshifts at runs of guanine were.
Watanabe
M
M
Institute of Environmental Toxicology, Tokyo, Japan.
Nohmi
T
T
Ohta
T
T
D015112:4-Nitroquinoline-1-oxide / Q000633:toxicity; D000483:Alleles; D000585:Aminacrine / Q000031:analogs & derivatives / Q000633:toxicity; D004252:DNA Mutational Analysis; D004269:DNA, Bacterial / Q000187:drug effects*; D004926:Escherichia coli / Q000187:drug effects / Q000235:genetics; D016368:Frameshift Mutation; D005668:Furylfuramide / Q000633:toxicity; D007763:Lac Operon / Q000187:drug effects* / Q000235:genetics; D008769:Methylnitronitrosoguanidine / Q000633:toxicity; D016685:Mitomycin / Q000633:toxicity; D016297:Mutagenesis, Site-Directed; D009153:Mutagens / Q000633:toxicity*; D009588:Nitrogen Mustard Compounds / Q000633:toxicity; D009876:Operon / Q000235:genetics; D010957:Plasmids; D013014:SOS Response, Genetics; D013489:Suppression, Genetic
D004269:DNA, Bacterial; D009153:Mutagens; D009588:Nitrogen Mustard Compounds; D005668:Furylfuramide; D008769:Methylnitronitrosoguanidine; D016685:Mitomycin; D015112:4-Nitroquinoline-1-oxide; D000585:Aminacrine; C004294:acridine half-mustard