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. 1975 Dec;72(12):5021–5025. doi: 10.1073/pnas.72.12.5021

Regulation of histidine operon does not require hisG enzyme.

J F Scott, J R Roth, S W Artz
PMCID: PMC388867  PMID: 1108009

Abstract

Mutations are described which delete all or part of the first structural gene (hisG) of the histidine operon of Salmonella typhimurium. Physiological regulation of histidine enzymes occurs normally in strains carrying any deletion that has both endpoints within the hisG gene. Constitutive high operon expression is observed in strains carrying any hisG deletion and an unlinked regulatory mutation, hisT1504. These results strongly indicate that the hisG protein is not an essential component of the mechanism for regulating expression of the histidine operon.

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Selected References

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  1. Ames B. N., Garry B. COORDINATE REPRESSION OF THE SYNTHESIS OF FOUR HISTIDINE BIOSYNTHETIC ENZYMES BY HISTIDINE. Proc Natl Acad Sci U S A. 1959 Oct;45(10):1453–1461. doi: 10.1073/pnas.45.10.1453. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. 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]
  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. 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]
  5. 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]
  6. 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]
  7. 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]
  8. Fink G. R., Klopotowski T., Ames B. N. Histidine regulatory mutants in Salmonella typhimurium. IV. A positive selection for polar histidine-requiring mutants from histidine operator constitutive mutants. J Mol Biol. 1967 Nov 28;30(1):81–95. doi: 10.1016/0022-2836(67)90245-8. [DOI] [PubMed] [Google Scholar]
  9. 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]
  10. 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]
  11. HARTMAN P. E., LOPER J. C., SERMAN D. Fine structure mapping by complete transduction between histidine-requiring Salmonella mutants. J Gen Microbiol. 1960 Apr;22:323–353. doi: 10.1099/00221287-22-2-323. [DOI] [PubMed] [Google Scholar]
  12. Hilton J. L., Kearney P. C., Ames B. N. Mode of action of the herbicide, 3-amino-1,2,4-triazole(amitrole): inhibition of an enzyme of histidine biosynthesis. Arch Biochem Biophys. 1965 Dec;112(3):544–547. doi: 10.1016/0003-9861(65)90093-7. [DOI] [PubMed] [Google Scholar]
  13. Hiraga S., Yanofsky C. Normal repression in a deletion mutant lacking almost the entire operator-proximal gene of the tryptophan operon of E. coli. Nat New Biol. 1972 May 10;237(71):47–49. doi: 10.1038/newbio237047a0. [DOI] [PubMed] [Google Scholar]
  14. Hong J. S., Ames B. N. Localized mutagenesis of any specific small region of the bacterial chromosome. Proc Natl Acad Sci U S A. 1971 Dec;68(12):3158–3162. doi: 10.1073/pnas.68.12.3158. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Jackson E. N., Yanofsky C. Internal deletions in the tryptophan operon of Escherichia coli. J Mol Biol. 1972 Nov 14;71(2):149–161. doi: 10.1016/0022-2836(72)90343-9. [DOI] [PubMed] [Google Scholar]
  16. Kline E. L., Brown C. S., Coleman W. G., Jr, Umbarger H. E. Regulation of isoleucine-valine biosynthesis in an ilvDAC deletion strain of Escherichia coli K-12. Biochem Biophys Res Commun. 1974 Apr 23;57(4):1144–1151. doi: 10.1016/0006-291x(74)90816-x. [DOI] [PubMed] [Google Scholar]
  17. Kovach J. S., Ballesteros A. O., Meyers M., Soria M., Goldberger R. F. A cis-trans test of the effect of the first enzyme for histidine biosynthesis on regulation of the histidine operon. J Bacteriol. 1973 Apr;114(1):351–356. doi: 10.1128/jb.114.1.351-356.1973. [DOI] [PMC free article] [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., 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]
  20. Murray M. L., Hartman P. E. Overproduction of hisH and hisF gene products leads to inhibition of cell cell division in Salmonella. Can J Microbiol. 1972 May;18(5):671–681. doi: 10.1139/m72-105. [DOI] [PubMed] [Google Scholar]
  21. Roth J. R., Hartman P. E. Heterogeneity in P22 transducing particles. Virology. 1965 Nov;27(3):297–307. doi: 10.1016/0042-6822(65)90109-1. [DOI] [PubMed] [Google Scholar]
  22. Schmieger H. A method for detection of phage mutants with altered transducing ability. Mol Gen Genet. 1971;110(4):378–381. doi: 10.1007/BF00438281. [DOI] [PubMed] [Google Scholar]
  23. 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]
  24. Smith H. O., Levine M. A phage P22 gene controlling integration of prophage. Virology. 1967 Feb;31(2):207–216. doi: 10.1016/0042-6822(67)90164-x. [DOI] [PubMed] [Google Scholar]
  25. VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
  26. Vogel T., Meyers M., Kovach J. S., Goldberger R. F. Specificity of interaction between the first enzyme for histidine biosynthesis and aminoacylated histidine transfer ribonucleic acid. J Bacteriol. 1972 Oct;112(1):126–130. doi: 10.1128/jb.112.1.126-130.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]

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