Effect of Tryptophan Analogs on Derepression of the Escherichia coli Tryptophan Operon by Indole-3-Propionic Acid
Format of Original
American Society for Microbiology
Journal of Bacteriology
Original Item ID
The abilities of 14 tryptophan analogs to repress the tryptophan (trp) operon have been studied in Escherichia coli cells derepressed by incubation with 0.25 mM indole-3-propionic acid (IPA). trp operon expression was monitored by measuring the specific activities of anthranilate synthase (EC 18.104.22.168) and the tryptophan synthase (EC 22.214.171.124) β subunit. Analogs characterized by modification or removal of the α-amino group or the α-carboxyl group did not repress the trp operon. The only analogs among this group that appeared to interact with the trp aporepressor were IPA, which derepressed the trp operon, and d-tryptophan. Analogs with modifications of the indole ring repressed the trp operon to various degrees. 7-Methyl-tryptophan inhibited anthranilate synthase activity and consequently derepressed the trp operon. Additionally, 7-methyltryptophan prevented IPA-mediated derepression but, unlike tryptophan, did so in a non-coordinate manner, with the later enzymes of the operon being relatively more repressed than the early enzymes. The effect of 7-methyltryptophan on IPA-mediated derepression was likely not due to the interaction of IPA with the allosteric site of anthranilate synthase, even though feedback-resistant mutants of anthranilate synthase were partially resistant to derepression by IPA. The effect of 7-methyltryptophan on derepression by IPA was probably due to the effect of the analog-aporepressor complex on trp operon expression.
Pauley, Robert J.; Fredricks, Walter W.; and Smith, Oliver H., "Effect of Tryptophan Analogs on Derepression of the Escherichia coli Tryptophan Operon by Indole-3-Propionic Acid" (1978). Biomedical Sciences Faculty Research and Publications. 101.