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. 1975 Sep;72(9):3453–3457. doi: 10.1073/pnas.72.9.3453

Histidine regulation in Salmonella typhimurium: an activator attenuator model of gene regulation.

S W Artz, J R Broach
PMCID: PMC433012  PMID: 1103149

Abstract

An activator-attenuator model of positive control, a s opposed to the classic repressor-operator model of negative control, is proposed for the major operon-specific mechanism governing expression of the histidine gene cluster of Salmonella typhimurium. Evidence for this mechanism is derived from experiments performed with a coupled in vitro transcription-translation system, as well as with a minimal in vitro transcription system [Kasai, T. (1974) Nature 249, 523--527]. The product (G enzyme, or N-1-[5'-phosphoribosyl]adenosine triphosphate:pyrophosphate phosphoribosyltransferase; EC 2.4.2.17) of the first structural gene (hisG) of the histidine operon is not involved in the positive control mechanism. However, a possible role for G enzyme as an accessory negative control element interacting at the attenuator can be accommodated in our model. The operon-specific mechanism works in conjunction with an independent mechanism involving guanosine 5'-diphosphate 3'-diphosphate (ppGpp) which appears to be a positive effector involved in regulating amino-acid-producing systems, in general [Stephens, J.C., Artz, S.W. & Ames, B.N. (1975) Proc. Nat. Acad. Sci. USA, in press].

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Selected References

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

  1. Bertrand K., Korn L., Lee F., Platt T., Squires C. L., Squires C., Yanofsky C. New features of the regulation of the tryptophan operon. Science. 1975 Jul 4;189(4196):22–26. doi: 10.1126/science.1094538. [DOI] [PubMed] [Google Scholar]
  2. Blasi F., Bruni C. B., Avitabile A., Deeley R. G., Goldberger R. F., Meyers M. M. Inhibition of transcription of the histidine operon in vitro by the first enzyme of the histidine pathway. Proc Natl Acad Sci U S A. 1973 Sep;70(9):2692–2696. doi: 10.1073/pnas.70.9.2692. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Brenner M., Ames B. N. Histidine regulation in Salmonella typhimurium. IX. Histidine transfer ribonucleic acid of the regulatory mutants. J Biol Chem. 1972 Feb 25;247(4):1080–1088. [PubMed] [Google Scholar]
  4. Bronson M. J., Squires C., Yanofsky C. Nucleotide sequences from tryptophan messenger RNA of Escherichia coli: the sequence corresponding to the amino-terminal region of the first polypeptide specified by the operon. Proc Natl Acad Sci U S A. 1973 Aug;70(8):2335–2339. doi: 10.1073/pnas.70.8.2335. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cashel M. Preparation of guanosine tetraphosphate (ppGpp) and guanosine pentaphosphate (pppGpp) from Escherichia coli ribosomes. Anal Biochem. 1974 Jan;57(1):100–107. doi: 10.1016/0003-2697(74)90056-6. [DOI] [PubMed] [Google Scholar]
  6. Chang G. W., Roth J. R., Ames B. N. Histidine regulation in Salmonella typhimurium. 8. Mutations of the hisT gene. J Bacteriol. 1971 Oct;108(1):410–414. doi: 10.1128/jb.108.1.410-414.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Cieslà Z., Salvatore F., Broach J. R., Artz S. W., Ames B. N. Histidine regulation in Salmonella typhimurium. XVI. A sensitive radiochemical assay for histidinol dehydrogenase. Anal Biochem. 1975 Jan;63(1):44–55. doi: 10.1016/0003-2697(75)90187-6. [DOI] [PubMed] [Google Scholar]
  8. Cortese R., Landsberg R., Haar R. A., Umbarger H. E., Ames B. N. Pleiotropy of hisT mutants blocked in pseudouridine synthesis in tRNA: leucine and isoleucine-valine operons. Proc Natl Acad Sci U S A. 1974 May;71(5):1857–1861. doi: 10.1073/pnas.71.5.1857. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Ely B., Fankhauser D. B., Hartman P. E. A fine structure map of the salmonella histidine operator-promoter. Genetics. 1974 Oct;78(2):607–631. doi: 10.1093/genetics/78.2.607. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Ely B. Physiological studies of salmonella histidine operator-promoter mutants. Genetics. 1974 Oct;78(2):593–606. doi: 10.1093/genetics/78.2.593. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Fink G. R., Roth J. R. Histidine regulatory mutants in Salmonella typhiumium. VI. Dominance studies. J Mol Biol. 1968 May 14;33(3):547–557. doi: 10.1016/0022-2836(68)90305-7. [DOI] [PubMed] [Google Scholar]
  12. 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]
  13. Imamoto F. Diversity of regulation of genetic transcription. I. Effect of antibiotics which inhibit the process of translation on RNA metabolism in Escherichia coli. J Mol Biol. 1973 Feb 25;74(2):113–136. doi: 10.1016/0022-2836(73)90102-2. [DOI] [PubMed] [Google Scholar]
  14. Ito J., Imamoto F. Sequential derepression and repression of the tryptophan operon in E. coli. Nature. 1968 Nov 2;220(5166):441–444. doi: 10.1038/220441a0. [DOI] [PubMed] [Google Scholar]
  15. JACOB F., MONOD J. Genetic regulatory mechanisms in the synthesis of proteins. J Mol Biol. 1961 Jun;3:318–356. doi: 10.1016/s0022-2836(61)80072-7. [DOI] [PubMed] [Google Scholar]
  16. Jackson E. N., Yanofsky C. Thr region between the operator and first structural gene of the tryptophan operon of Escherichia coli may have a regulatory function. J Mol Biol. 1973 May 5;76(1):89–101. doi: 10.1016/0022-2836(73)90082-x. [DOI] [PubMed] [Google Scholar]
  17. 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]
  18. Kovach J. S., Berberich M. A., Venetianer P., Goldberger R. F. Repression of the histidine operon: effect of the first enzyme on the kinetics of repression. J Bacteriol. 1969 Mar;97(3):1283–1290. doi: 10.1128/jb.97.3.1283-1290.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Kovach J. S., Phang J. M., Blasi F., Barton R. W., Ballesteros-Olmo A., Goldberger R. F. Interaction between histidyl transfer ribonucleic acid and the first enzyme for histidine biosynthesis of Salmonella typhimurium. J Bacteriol. 1970 Nov;104(2):787–792. doi: 10.1128/jb.104.2.787-792.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Kovach J. S., Phang J. M., Ference M., Goldberger R. F. Studies on repression of the histidine operon. II. The role of the first enzyme in control of the histidine system. Proc Natl Acad Sci U S A. 1969 Jun;63(2):481–488. doi: 10.1073/pnas.63.2.481. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. 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]
  22. Singer C. E., Smith G. R., Cortese R., Ames B. N. [Mutant tRNA His ineffective in repression and lacking two pseudouridine modifications]. Nat New Biol. 1972 Jul 19;238(81):72–74. doi: 10.1038/newbio238072a0. [DOI] [PubMed] [Google Scholar]
  23. Smith G. R., Tong B. Construction of phi80 dhis carrying Salmonella typhimurium histidine operon mutations. J Bacteriol. 1974 Dec;120(3):1223–1226. doi: 10.1128/jb.120.3.1223-1226.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Voll M. J. Derivation of an F-merogenote and a phi-80 high-frequency transducing phage carrying the histidine operon os Salmonella. J Bacteriol. 1972 Feb;109(2):741–750. doi: 10.1128/jb.109.2.741-750.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Voll M. J. Translation and polarity in the histidine operon. 3. The isolation of prototrophic polar mutations. J Mol Biol. 1967 Nov 28;30(1):109–124. doi: 10.1016/0022-2836(67)90247-1. [DOI] [PubMed] [Google Scholar]
  26. Wyche J. H., Ely B., Cebula T. A., Snead M. C., Hartman P. E. Histidyl-transfer ribonucleic acid synthetase in positive control of the histidine operon in Salmonella typhimurium. J Bacteriol. 1974 Feb;117(2):708–716. doi: 10.1128/jb.117.2.708-716.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]

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