Ultraviolet light-induced mutation in UV-resistant, thermosensitive derivatives of lexA-strains of Escherichia coli K-12.
It was shown previously that a major class of UV-resistant derivatives of lexA- strains of E. coli K-12 is defective in cell division at 42.5 degrees. The thermosensitive mutations, judging by genetic mapping and complementation tests, are believed to be intragenic suppressor mutations that lower the activity of the diffusible product that results in the LexA- phenotype (Mount et al., 1973). Several thermosensitive derivatives have been characterized in regard to their susceptibility to mutation induction by UV at the permissive growth temperature (30 degrees). Although the strains tested are approximately as resistant to UV as lexA+ strains, they showed a level of mutation induction that was considerably lower. By means of genetic complementation tests it was demonstrated that the low levels of UV mutagenesis in lexA- strains and their thermosensitive derivatives result from the synthesis of a diffusible product. One possible interpretation of these results is that a diffusible product in lexA- strains prevents the induction of error-prone repair. Altering the activity of this product by tsl mutations can lead to increased, but not normal, levels of error-prone repair.
Mount
D W
DW
Department of Microbiology, College of Medicine, University of Arizona, Tucson, Arizona 85724, USA.
Kosel
C
C
D001426:Bacterial Proteins / Q000235:genetics*; D004260:DNA Repair; D004269:DNA, Bacterial / Q000235:genetics; D048168:Escherichia coli K12 / Q000235:genetics* / Q000528:radiation effects; D012697:Serine Endopeptidases / Q000235:genetics*; D013489:Suppression, Genetic; D013696:Temperature; D014466:Ultraviolet Rays; D000099160:LexA Repressor Protein
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D012697:Serine Endopeptidases; D000099160:LexA Repressor Protein