Documentation of Auxotrophic Mutation in Blue-green Bacteria: Characterization of a Tryptophan Auxotroph in Agmenellum Quadruplicatum

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1972 Jul 1

PMID 4204902

Citations 15

Authors

L O Ingram

D Pierson

J F KANE

C Van Baalen

R A Jensen

Affiliations

Soon will be listed here.

Abstract

A tryptophan-requiring auxotroph of Agmenellum quadruplicatum strain BG1, a species of blue-green bacteria, was isolated by means of a nitrosoguanidine-penicillin procedure. Its growth characteristics were determined, and the enzymological block was identified in the A activity of tryptophan synthetase. Starvation of the auxotroph for tryptophan resulted in the derepression of the synthesis of all five enzymes. The first four enzymes derepressed 2- to 3-fold, and tryptophan synthetase B derepressed 20-fold. In the parental prototroph, BG1, anthranilate synthetase was active in crude extracts with ammonia as the amino donor reactant, but not with glutamine.

Citing Articles

Ancient origin of the tryptophan operon and the dynamics of evolutionary change.

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Active transport of amino acids in Thiobacillus thioparus is a low-affinity process.

Stark A, YANKOFSKY S J Bacteriol. 1981; 148(3):956-65.

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Enzymological basis for growth inhibition by L-phenylalanine in the cyanobacterium Synechocystis sp. 29108.

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Mis-regulation of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase does not account for growth inhibition by phenylalanine in Agmenellum quadruplicatum.

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