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. 1971 May;106(2):508–513. doi: 10.1128/jb.106.2.508-513.1971

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

Francesco Blasi a,1, Robert W Barton a,2, John S Kovach a, Robert F Goldberger a
PMCID: PMC285123  PMID: 4929863

Abstract

Previous studies suggested that phosphoribosyltransferase, which catalyzes the first step of the pathway for histidine biosynthesis in Salmonella typhimurium and which is sensitive to inhibition by histidine, plays a role in repression of the histidine operon. Recently, we showed that the enzyme has a high affinity for histidyl transfer ribonucleic acid (His-tRNA), which is known to participate in the repression process. In the present study, we have investigated further the interaction between the enzyme and His-tRNA. We found that His-tRNA binds at a site on phosphoribosyltransferase distinct from the catalytic site and the histidine-sensitive site; that the substrates of the enzyme inhibit the binding of His-tRNA, whereas histidine does not do so; that, once a complex has been formed between phosphoribosyltransferase and His-tRNA, the substrates of the enzyme decrease the stability of the complex, whereas histidine is without effect; and that purified phosphoribosyltransferase which has a defect in its inhibition by histidine (produced by mutation) displays an altered ability to bind His-tRNA, a finding which may be a reflection of the fact that mutants producing such a defective enzyme display an alteration of the repression process.

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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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