TRYPTOPHAN SYNTHETASE LEVELS IN ESCHERICHIA COLI, SHIGELLA DYSENTERIAE , AND TRANSDUCTION HYBRIDS

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Abstract
Eisenstein, Richard B. (Western Reserve University, Cleveland, Ohio) and Charles Yanofsky . Tryptophan synthetase levels in Escherichia coli, Shigella dysenteriae , and transduction hybrids. J. Bacteriol. 83: 193–204. 1962— Shigella dysenteriae and Escherichia coli , strains K-12 and B, were found to produce low levels of tryptophan synthetase, although some hybrids, formed by the introduction of the gene cluster concerned with tryptophan synthesis from S. dysenteriae into E. coli , produced high levels of this enzyme system. A revertant obtained from a tryptophan-requiring mutant also formed high levels of tryptophan synthetase. The gene or genes responsible for high enzyme production in these strains was shown to be linked to the cluster of genes concerned with tryptophan synthesis. The cause of high enzyme production was investigated. Various lines of evidence, including stimulation of growth by tryptophan precursors, sensitivity to inhibition by 5-methyltryptophan, absence of accumulation of tryptophan, and repression of enzyme formation by anthranilic acid and tryptophan, suggested that high enzyme production in the strains examined results from a partial block in the tryptophan pathway and not from resistance to repression by tryptophan. The conversion of shikimic acid-5-phosphate to anthranilic acid appears to be the partially blocked reaction in the strains studied.