Increased Activity of Tryptophan Biosynthetic Enzymes in Histidine Mutants of Neurospora crassa

Author:

Carsiotis M.1,Lacy Ann M.2

Affiliation:

1. Department of Microbiology, College of Medicine, University of Cincinnati, Cincinnati, Ohio

2. Department of Biological Sciences, Goucher College, Baltimore, Maryland

Abstract

Carsiotis , M. (University of Cincinnati College of Medicine, Cincinnati, Ohio), and Ann M. Lacy . Increased activity of tryptophan biosynthetic enzymes in histidine mutants of Neurospora crassa . J. Bacteriol. 89: 1472–1477. 1965.—The activities of tryptophan synthetase and indoleglycerol phosphate synthetase, the last two enzymes in the tryptophan biosynthetic pathway, are elevated twofold or more in all histidine mutants of Neurospora crassa . The elevation occurs only when the mutants are grown in a histidine-limited medium. Several possible mechanisms for this elevation were disproved experimentally. The cause of the elevated enzyme activities remains unknown.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference31 articles.

1. The nature of complementation among mutants in the histidine-3 region of NAeurospora crassa;AHMED A.;Brookhaven Symp. Biol.,1964

2. Coordinate repression of the synthesis of four histidine biosynthetic enzymes by histidine. Proc. Nat];AMES B. N.;Acad. Sci. U.,1959

3. The histidine operon;AMES B. N.;Cold Spring Harbor Symp. Quant. Biol.,1963

4. The biosynthesis of histidine. Imidazoleglycerol phosphate, imidazoleacetol phosphate, and histidinol phosphate;AMES B. N.;J. Biol. Chem.,1955

5. Genetic fine structure and enzyme formation;BONNER D. M.;Federation Proc.,1960

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