Abstract
Three indole analogues, 5-methylindole, 5-fluoroindole, and 7-methylindole, and the tryptophan analogue 5-fluorotryptophan were found to inhibit the growth of wild-type Pseudomonas putida. Mutants resistant to these analogues were obtained. Some of the 5-fluoroindole- and 5-fluorotryptophan-resistant strains exhibit an abnormality in the regulation of certain trp genes. These strains excrete anthranilate when grown in minimal medium in the presence or absence of the inhibitor. In these strains, the trpA, B, and D gene products, the first, second, and fourth enzymes of the tryptophan pathway, are produced in 20-fold excess over the normal wild-type level. The other enzymes of the pathway are unaffected. Exogenous tryptophan is still able to repress the expression of the trpABD cluster somewhat. Similarity between the 5-fluoroindole- and 5-fluorotryptophan-resistant strains suggests that the former compound becomes effective through conversion to the latter. Repression and derepression experiments with two anthranilate-excreting, 5-fluoroindole-resistant strains showed coordinate variation of the affected enzymes. The locus conferring resistance and excretion is not linked by transduction to any of the trp genes.