Control of Arginine Biosynthesis in Escherichia Coli: Characterization of Arginyl-transfer Ribonucleic Acid Synthetase Mutants

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1973 Mar 1

PMID 4570786

Citations 4

Authors

A L Williams

L S Williams

Affiliations

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Abstract

The arginyl-transfer ribonucleic acid (Arg-tRNA) synthetase (EC 6.1.1.13, arginine: RNA ligase adenosine monophosphate) mutants, exhibiting nonrepressible synthesis of arginine by exogenous arginine, were employed in studies of several biochemical properties. Two of these mutants possessed Arg-tRNA synthetases with a reduced affinity for arginine, and this enzyme of another mutant had a reduced affinity for arginine-tRNA (tRNA(arg)). The mutant possessing an Arg-tRNA synthetase with an altered K(m) for tRNA(arg) was found to have reduced in vivo aminoacylation of two of the five isoaccepting species of tRNA(arg) and complete absence of aminoacylation of one of the isoaccepting species.

Citing Articles

Control of arginine biosynthesis in Escherichia coli: inhibition of arginyl-transfer ribonucleic acid synthetase activity.

Williams A, Yem D, McGinnis E, Williams L J Bacteriol. 1973; 115(1):228-34.

PMID: 4577743 PMC: 246234. DOI: 10.1128/jb.115.1.228-234.1973.

Properties and developmental roles of the lysyl- and tryptophanyl-transfer ribonucleic acid synthetases of Bacillus subtilis: common genetic origin of the corresponding spore and vegetative enzymes.

Steinberg W J Bacteriol. 1974; 118(1):70-82.

PMID: 4206876 PMC: 246641. DOI: 10.1128/jb.118.1.70-82.1974.

Temperature-induced derepression of tryptophan biosynthesis in a tryptophanyl-transfer ribonucleic acid synthetase mutant of Bacillus subtilis.

Steinberg W J Bacteriol. 1974; 117(3):1023-34.

PMID: 4205189 PMC: 246581. DOI: 10.1128/jb.117.3.1023-1034.1974.

Dual regulation by arginine of the expression of the Escherichia coli argECBH operon.

Kryzek R, Rogers P J Bacteriol. 1976; 126(1):348-64.

PMID: 770426 PMC: 233292. DOI: 10.1128/jb.126.1.348-364.1976.

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