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. 1991 Jun;173(12):3930–3932. doi: 10.1128/jb.173.12.3930-3932.1991

The tyrosine repressor negatively regulates aroH expression in Escherichia coli.

G K Muday 1, D I Johnson 1, R L Somerville 1, K M Herrmann 1
PMCID: PMC208031  PMID: 1675635

Abstract

The levels of the tryptophan-sensitive isoenzyme of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase of Escherichia coli, encoded by the aroH gene, were elevated in tyrR and/or trpR mutants. The effect of tyrR and trpR lesions on aroH expression was confirmed by using a lacZ reporter system. The mutational elimination of either repressor led to a threefold increase in beta-galactosidase.

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Selected References

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  1. Baseggio N., Davies W. D., Davidson B. E. Identification of the promoter, operator, and 5' and 3' ends of the mRNA of the Escherichia coli K-12 gene aroG. J Bacteriol. 1990 May;172(5):2547–2557. doi: 10.1128/jb.172.5.2547-2557.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bass S., Sugiono P., Arvidson D. N., Gunsalus R. P., Youderian P. DNA specificity determinants of Escherichia coli tryptophan repressor binding. Genes Dev. 1987 Aug;1(6):565–572. doi: 10.1101/gad.1.6.565. [DOI] [PubMed] [Google Scholar]
  3. Bennett G. N., Yanofsky C. Sequence analysis of operator constitutive mutants of the tryptophan operon of Escherichia coli. J Mol Biol. 1978 May 15;121(2):179–192. doi: 10.1016/s0022-2836(78)80004-7. [DOI] [PubMed] [Google Scholar]
  4. Bochner B. R., Huang H. C., Schieven G. L., Ames B. N. Positive selection for loss of tetracycline resistance. J Bacteriol. 1980 Aug;143(2):926–933. doi: 10.1128/jb.143.2.926-933.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bogosian G., Somerville R. L. Analysis in vivo of factors affecting the control of transcription initiation at promoters containing target sites for trp repressor. Mol Gen Genet. 1984;193(1):110–118. doi: 10.1007/BF00327423. [DOI] [PubMed] [Google Scholar]
  6. Bogosian G., Somerville R. L., Nishi K., Kano Y., Imamoto F. Transcription of the trpR gene of Escherichia coli: an autogeneously regulated system studied by direct measurements of mRNA levels in vivo. Mol Gen Genet. 1984;193(2):244–250. doi: 10.1007/BF00330675. [DOI] [PubMed] [Google Scholar]
  7. Brown K. D., Somerville R. L. Repression of aromatic amino acid biosynthesis in Escherichia coli K-12. J Bacteriol. 1971 Oct;108(1):386–399. doi: 10.1128/jb.108.1.386-399.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Chye M. L., Pittard J. Transcription control of the aroP gene in Escherichia coli K-12: analysis of operator mutants. J Bacteriol. 1987 Jan;169(1):386–393. doi: 10.1128/jb.169.1.386-393.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Cobbett C. S., Delbridge M. L. Regulatory mutants of the aroF-tyrA operon of Escherichia coli K-12. J Bacteriol. 1987 Jun;169(6):2500–2506. doi: 10.1128/jb.169.6.2500-2506.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Davies W. D., Davidson B. E. The nucleotide sequence of aroG, the gene for 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase (phe) in Escherichia coli K12. Nucleic Acids Res. 1982 Jul 10;10(13):4045–4058. doi: 10.1093/nar/10.13.4045. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. DeFeyter R. C., Davidson B. E., Pittard J. Nucleotide sequence of the transcription unit containing the aroL and aroM genes from Escherichia coli K-12. J Bacteriol. 1986 Jan;165(1):233–239. doi: 10.1128/jb.165.1.233-239.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Garner C. C., Herrmann K. M. Operator mutations of the Escherichia coli aroF gene. J Biol Chem. 1985 Mar 25;260(6):3820–3825. [PubMed] [Google Scholar]
  13. Grove C. L., Gunsalus R. P. Regulation of the aroH operon of Escherichia coli by the tryptophan repressor. J Bacteriol. 1987 May;169(5):2158–2164. doi: 10.1128/jb.169.5.2158-2164.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Heatwole V. M., Somerville R. L. Cloning, nucleotide sequence, and characterization of mtr, the structural gene for a tryptophan-specific permease of Escherichia coli K-12. J Bacteriol. 1991 Jan;173(1):108–115. doi: 10.1128/jb.173.1.108-115.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Heatwole V. M., Somerville R. L. The tryptophan-specific permease gene, mtr, is differentially regulated by the tryptophan and tyrosine repressors in Escherichia coli K-12. J Bacteriol. 1991 Jun;173(11):3601–3604. doi: 10.1128/jb.173.11.3601-3604.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Kasian P. A., Pittard J. Construction of a tyrP-lac operon fusion strain and its use in the isolation and analysis of mutants derepressed for tyrP expression. J Bacteriol. 1984 Oct;160(1):175–183. doi: 10.1128/jb.160.1.175-183.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Klig L. S., Carey J., Yanofsky C. trp repressor interactions with the trp aroH and trpR operators. Comparison of repressor binding in vitro and repression in vivo. J Mol Biol. 1988 Aug 20;202(4):769–777. doi: 10.1016/0022-2836(88)90557-8. [DOI] [PubMed] [Google Scholar]
  18. Muday G. K., Herrmann K. M. Regulation of the Salmonella typhimurium aroF gene in Escherichia coli. J Bacteriol. 1990 May;172(5):2259–2266. doi: 10.1128/jb.172.5.2259-2266.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Ogino T., Garner C., Markley J. L., Herrmann K. M. Biosynthesis of aromatic compounds: 13C NMR spectroscopy of whole Escherichia coli cells. Proc Natl Acad Sci U S A. 1982 Oct;79(19):5828–5832. doi: 10.1073/pnas.79.19.5828. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Ray J. M., Yanofsky C., Bauerle R. Mutational analysis of the catalytic and feedback sites of the tryptophan-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase of Escherichia coli. J Bacteriol. 1988 Dec;170(12):5500–5506. doi: 10.1128/jb.170.12.5500-5506.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Schoner R., Herrmann K. M. 3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification, properties, and kinetics of the tyrosine-sensitive isoenzyme from Escherichia coli. J Biol Chem. 1976 Sep 25;251(18):5440–5447. [PubMed] [Google Scholar]
  22. Shultz J., Hermodson M. A., Garner C. C., Herrmann K. M. The nucleotide sequence of the aroF gene of Escherichia coli and the amino acid sequence of the encoded protein, the tyrosine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase. J Biol Chem. 1984 Aug 10;259(15):9655–9661. [PubMed] [Google Scholar]
  23. Whipp M. J., Pittard A. J. Regulation of aromatic amino acid transport systems in Escherichia coli K-12. J Bacteriol. 1977 Nov;132(2):453–461. doi: 10.1128/jb.132.2.453-461.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Yang J., Pittard J. Molecular analysis of the regulatory region of the Escherichia coli K-12 tyrB gene. J Bacteriol. 1987 Oct;169(10):4710–4715. doi: 10.1128/jb.169.10.4710-4715.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Zurawski G., Gunsalus R. P., Brown K. D., Yanofsky C. Structure and regulation of aroH, the structural gene for the tryptophan-repressible 3-deoxy-D-arabino-heptulosonic acid-7-phosphate synthetase of Escherichia coli. J Mol Biol. 1981 Jan 5;145(1):47–73. doi: 10.1016/0022-2836(81)90334-x. [DOI] [PubMed] [Google Scholar]

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