TRYPTOPHAN- AND INDOLE-EXCRETING PROTOTROPHIC MUTANT OF ESCHERICHIA COLI

Abstract

Lim , P. G. (Massachusetts Institute of Technology, Cambridge), and R. I. Mateles . Tryptophan- and indole-excreting prototrophic mutant of Escherichia coli . J. Bacteriol. 87: 1051–1055. 1964.—A mutant of Escherichia coli K-12, capable of excreting 350 mg of indole and 50 mg of tryptophan per liter when grown on minimal medium, was found to have a level of 3-deoxy- d - arabino -heptulosonic acid-7-phosphate (DAHP) synthetase 60% higher than the parent, and to have a 10- to 15-fold elevation of the levels of enzymes in the tryptophan branch of the pathway for aromatic amino acid biosynthesis. Contrary to what previous investigators found in E. coli W, the presence of a tyrosine-repressible component of DAHP synthetase sensitive to end-product inhibition by tyrosine could not be demonstrated in either strain K-12 or the mutant. The mutant strain is an example of a microorganism which excretes biosynthetic end products solely because of genetic derepression, as opposed to most previously reported amino acid accumulators which require a combination of genetic and physiological manipulation to achieve derepression.