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. 1970 Nov;104(2):787–792. doi: 10.1128/jb.104.2.787-792.1970

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

John S Kovach a, James M Phang a,1, Francesco Blasi a,2, Robert W Barton a, Antonio Ballesteros-Olmo a,3, Robert F Goldberger a
PMCID: PMC285059  PMID: 4923072

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 3H-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 3H-His-tRNA with that of tRNA aminoacylated with other 3H-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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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