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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1977 Apr;74(4):1535–1537. doi: 10.1073/pnas.74.4.1535

Inhibition of histidyl-tRNA-adenosine triphosphate phosphoribosyltransferase complex formation by histidine and by guanosine tetraphosphate.

J E Kleeman, S M Parsons
PMCID: PMC430824  PMID: 323857

Abstract

Formation of the complex between the first enzyme of histidine biosynthesis from Salmonella typhimurium, ATP phosphoribosyltransferase [1-(5'-phosphoribosyl)-ATP: pyrophosphate phosphoribosyltransferase; EC 2.4.2.17], and histidyl-tRNA is shown to be inhibited by L-histidine and by guanosine-5'-diphosphate-3'-diphosphate in the presence of histidine. Higher histodine levels make guanosine tetraphosphate a more effective inhibitor. Relatively high concentrations of guanosine-5'-triphosphate also inhibit complex formation, but this inhibition is not enhanced by histidine. The possible implications of these observations with respect to the gene regulatory activity of this enzyme are discussed.

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Selected References

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

  1. Artz S. W., Broach J. R. Histidine regulation in Salmonella typhimurium: an activator attenuator model of gene regulation. Proc Natl Acad Sci U S A. 1975 Sep;72(9):3453–3457. doi: 10.1073/pnas.72.9.3453. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Blasi F., Aloj S. M., Goldberger R. F. Effect of histidine on the enzyme which catalyzes the first step of histidine biosynthesis in Salmonella typhimurium. Biochemistry. 1971 Apr 13;10(8):1409–1417. doi: 10.1021/bi00784a021. [DOI] [PubMed] [Google Scholar]
  3. Blasi F., Barton R. W., Kovach J. S., Goldberger R. F. Interaction between the first enzyme for histidine biosynthesis and histidyl transfer ribonucleic acid. J Bacteriol. 1971 May;106(2):508–513. doi: 10.1128/jb.106.2.508-513.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Brenner M., Lewis J. A., Straus D. S., De Lorenzo F., Ames B. N. Histidine regulation in salmonella typhimurium. XIV. Interaction of the histidyl transfer ribonucleic acid synthetase with histidine transfer ribonucleic acid. J Biol Chem. 1972 Jul 10;247(13):4333–4339. [PubMed] [Google Scholar]
  5. Calhoun D. H. Autoregulation of gene expression. Annu Rev Microbiol. 1975;29:275–299. doi: 10.1146/annurev.mi.29.100175.001423. [DOI] [PubMed] [Google Scholar]
  6. De Lorenzo F., Ames B. N. Histidine regulation in Salmonella typhimurium. VII. Purification and general properties of the histidyl transfer ribonucleic acid synthetase. J Biol Chem. 1970 Apr 10;245(7):1710–1716. [PubMed] [Google Scholar]
  7. Deeley R. G., Goldberger R. F., Kovach J. S., Meyers M. M., Mullinix K. P. Interaction between phosphoribosyltransferase and purified histidine tRNA from wild type Salmonella typhimurium and a derepressed hisT mutant strain. Nucleic Acids Res. 1975 Apr;2(4):545–554. doi: 10.1093/nar/2.4.545. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Di Nocera P. P., Avitabile A., Blasi F. In vitro transcription of the Escherichia coli histidine operon primed by dinucleotides. Effect of the first histidine biosynthetic enzyme. J Biol Chem. 1975 Nov 10;250(21):8376–8381. [PubMed] [Google Scholar]
  9. Goldberger R. F. Autogenous regulation of gene expression. Science. 1974 Mar 1;183(4127):810–816. doi: 10.1126/science.183.4127.810. [DOI] [PubMed] [Google Scholar]
  10. Goldberger R. F., Kovach J. S. Regulation of histidine biosynthesis in Salmonella typhimurium. Curr Top Cell Regul. 1972;5:285–308. doi: 10.1016/b978-0-12-152805-8.50014-9. [DOI] [PubMed] [Google Scholar]
  11. Harada F., Sato S., Nishimura S. Unusual CCA-stem structure of E. coli B tRNAH(His)(1). FEBS Lett. 1972 Jan 1;19(4):352–354. doi: 10.1016/0014-5793(72)80078-4. [DOI] [PubMed] [Google Scholar]
  12. Kasai T. Regulation of the expression of the histidine operon in Salmonella typhimurium. Nature. 1974 Jun 7;249(457):523–527. doi: 10.1038/249523a0. [DOI] [PubMed] [Google Scholar]
  13. Lewis J. A., Ames B. N. Histidine regulation in Salmonella typhimurium. XI. The percentage of transfer RNA His charged in vivo and its relation to the repression of the histidine operon. J Mol Biol. 1972 Apr 28;66(1):131–142. doi: 10.1016/s0022-2836(72)80011-1. [DOI] [PubMed] [Google Scholar]
  14. Meyers M., Blasi F., Bruni C. B., Deeley R. G., Kovach J. S., Levinthal M., Mullinix K. P., Vogel T., Goldberger R. F. Specific binding of the first enzyme for histidine biosynthesis to the DNA of histidine operon. Nucleic Acids Res. 1975 Nov;2(11):2021–2036. doi: 10.1093/nar/2.11.2021. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Morton D. P., Parsons S. M. Synergistic inhibition of ATP phosphoribosyltransferase by guanosine tetraphosphate and histidine. Biochem Biophys Res Commun. 1977 Jan 10;74(1):172–177. doi: 10.1016/0006-291x(77)91390-0. [DOI] [PubMed] [Google Scholar]
  16. Parsons S. M., Koshland D. E., Jr A rapid isolation of phosphoribosyladenosine triphosphate synthetase and comparison to native enzyme. J Biol Chem. 1974 Jul 10;249(13):4104–4109. [PubMed] [Google Scholar]
  17. Scott J. F., Roth J. R., Artz S. W. Regulation of histidine operon does not require hisG enzyme. Proc Natl Acad Sci U S A. 1975 Dec;72(12):5021–5025. doi: 10.1073/pnas.72.12.5021. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Stephens J. C., Artz S. W., Ames B. N. Guanosine 5'-diphosphate 3'-diphosphate (ppGpp): positive effector for histidine operon transcription and general signal for amino-acid deficiency. Proc Natl Acad Sci U S A. 1975 Nov;72(11):4389–4393. doi: 10.1073/pnas.72.11.4389. [DOI] [PMC free article] [PubMed] [Google Scholar]

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