On the mechanism of inhibition of enzyme induction in Escherichia coli by distamycin A.
The mechanism of the interference of the antiviral antibiotic distamycin A with the bacterial cell has been investigated. Labelled distamycin A is firmly bound by E. coli cells and the binding process does not require metabolic energy as indicated by the use of inhibitors. The antibiotic does not induce gross alteration in the cell membrane but inhibits cyclic AMP accumulation in the cells exposed to a glucose-free medium. This inhibition is concomitant with that exerted on the synthesis of an inducible enzyme such as beta-galactosidase. By the method of pulse induction it appears that distamycin A exterts its inhibiting effect on inducible synthesis at the level of transcription. This effect is probably related to an interference with the positive control of enzyme synthesis performed via the system represented by cyclic AMP and the CRP protein.
D001665:Binding Sites; D000242:Cyclic AMP / Q000378:metabolism; D004214:Distamycins / Q000494:pharmacology*; D004790:Enzyme Induction / Q000187:drug effects*; D004926:Escherichia coli / Q000201:enzymology*; D005696:Galactosidases / Q000378:metabolism; D011758:Pyrroles / Q000494:pharmacology*; D012486:Salmonella typhimurium / Q000201:enzymology
D004214:Distamycins; D011758:Pyrroles; D000242:Cyclic AMP; D005696:Galactosidases