Changes in protein synthesis on mitomycin C induction of wild-type and mutant CloDF13 plasmids.
Mitomycin C treatment of Escherichia coli K-12 cells containing the nonconjugative plasmid CloDF13 resulted in inhibition of host chromosome protein synthesis and a high rate of synthesis of two CloDF13-specified proteins whose molecular weights correspond to cloacin and immunity protein. Five molecules of immunity protein were synthesized for each cloacin DF13 molecule. Mitomycin C-treated cells containing a copy mutant of CloDF13 made three to four times as much of each protein as cells containing wild-type CloDF13. CloDF13 plasmids that contained the transposon Tn1 were isolated. Two did not induce after mitomycin C treatment, failing both to inhibit host cell synthesis and to produce the two new proteins. In minicells, they showed reduced CloDF13-specified protein synthesis and produced three Tn1-specified proteins.
D001430:Bacteriocins / Q000096:biosynthesis*; D002989:Cloacin / Q000096:biosynthesis* / Q000235:genetics; D003087:Colicins / Q000096:biosynthesis; D004251:DNA Transposable Elements; D004926:Escherichia coli / Q000235:genetics; D007700:Kinetics; D007709:Klebsiella / Q000235:genetics; D016685:Mitomycin; D008937:Mitomycins / Q000494:pharmacology*; D008970:Molecular Weight; D009154:Mutation; D010957:Plasmids
D001430:Bacteriocins; D003087:Colicins; D004251:DNA Transposable Elements; D008937:Mitomycins; D002989:Cloacin; D016685:Mitomycin