Interaction Between Histidyl Transfer Ribonucleic Acid and the First Enzyme for Histidine Biosynthesis of Salmonella Typhimurium

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1970 Nov 1

PMID 4923072

Citations 20

Authors

J S Kovach

J M Phang

F Blasi

R W Barton

R F GOLDBERGER

Affiliations

Soon will be listed here.

Abstract

Previous studies showed that the enzyme (phosphoribosyltransferase) which catalyzes the first step of the histidine pathway in Salmonella typhimurium plays a role in regulation of the histidine operon. Since histidyl transfer ribonucleic acid (His-tRNA) is required for repression of the histidine operon, we considered the possibility that the role of phosphoribosyltransferase might be realized through an interaction with His-tRNA. One prediction inherent in this idea is that the enzyme should interact with His-tRNA in vitro. Evidence is presented for such an interaction. Binding of (3)H-His-tRNA to purified phosphoribosyltransferase was tested on Sephadex columns and on nitrocellulose filters. The enzyme was found to have a high affinity for tRNA. Comparing the binding of (3)H-His-tRNA with that of tRNA aminoacylated with other (3)H-amino acids disclosed that the binding of the histidyl species of tRNA is favored over that of other species and is dependent upon magnesium-ion concentration.

Citing Articles

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Defective in vitro binding of histidyl-transfer ribonucleic acid to feedback resistant phosphoribosyl transferase of Salmonella typhimurium.

Smith O, MEYERS M, Vogel T, Deeley R, Goldberger R Nucleic Acids Res. 1974; 1(7):881-8.

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An aminoacyl-tRNA synthetase paralog with a catalytic role in histidine biosynthesis.

Sissler M, Delorme C, Bond J, Ehrlich S, Renault P, Francklyn C Proc Natl Acad Sci U S A. 1999; 96(16):8985-90.

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Possible regulation of the Salmonella typhimurium histidine operon by adenosine triphosphate phosphoribosyltransferase: large metabolic effects.

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The leader mRNA of the histidine attenuator region resembles tRNAHis: possible general regulatory implications.

Ames B, Tsang T, Buck M, Christman M Proc Natl Acad Sci U S A. 1983; 80(17):5240-2.

PMID: 6351055 PMC: 384228. DOI: 10.1073/pnas.80.17.5240.

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