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Gene Review

oxyR  -  oxidative and nitrosative stress...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3953, JW3933, momR, mor
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Disease relevance of oxyR

  • Mutations in oxyR or rob, known regulators of several stress promoters in E. coli, had no effect on the induction of hmp by paraquat [1].
  • The oxyR gene is required for the induction of a regulon of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium [2].
  • To identify genes which might confer resistance by detoxifying or sequestering INH, we transformed the Escherichia coli oxyR mutant, which is relatively sensitive to INH, with a Mycobacterium tuberculosis plasmid library and selected for INH-resistant clones [3].
  • The oxyR gene from the pathogenic bacterium Erwinia chrysanthemi has been characterized [4].
  • CONCLUSIONS: The presented findings indicate major differences between M. tuberculosis and the paradigms of oxidative stress response in enteric bacteria, and are consistent with the multiple lesions found in oxyR of this organism [5].

High impact information on oxyR

  • The oxyR gene positively regulates genes induced by oxidative stress in Salmonella typhimurium and Escherichia coli [6].
  • Mutations that suppressed the H2O2 sensitivity of Escherichia coli oxyR- strains caused elevated levels of one three enzymes that destroy organic and hydrogen peroxides: catalase-hydroperoxidase I (the katG gene product), catalase-hydroperoxidase II (controlled by katEF) or alkyl hydroperoxide reductase (specified by the ahp genes) [7].
  • The E. coli delta oxyR strains also exhibited a strongly elevated frequency of spontaneous mutagenesis, as reported for such mutants in Salmonella typhimurium [7].
  • The continuous high-level expression of any one of these enzymes also conferred resistance in an oxyR deletion mutant against other compounds such as N-ethylmaleimide and the superoxide-generator menadione [7].
  • One critical protein was Dps, an iron-sequestration protein, because Hpx- dps mutants exhibited sensitivity similar to that of the Hpx- oxyR mutant [8].

Chemical compound and disease context of oxyR


Biological context of oxyR


Anatomical context of oxyR


Associations of oxyR with chemical compounds

  • In stark contrast, the inactivation of both oxyR and rpoS genes dramatically decreased the viability of glucose-starved cells [16].
  • The oxyR mutant was hypersusceptible to oxidative stress-generating agents, including H(2)O(2) and paraquat, in spite of total KatA catalase activity being comparable to that of the wild type [17].
  • These results suggest that UV-A generates 1O2 or the hydroxyl radical to produce lipid peroxides intracellularly in the delta oxyR mutant and that O2- stress may be generated in the sodAB mutant after 8hr of exposure to UV-A [18].
  • Catalase (HPI), but not manganese-superoxide dismutase, was over-expressed under anaerobic conditions in a strain harboring a constitutive oxyR mutation [10].
  • Spermidine acetylation does not appear to be associated with known stress regulons, such as htpR, oxyR, and SOS [19].

Other interactions of oxyR

  • Strains bearing mutations in oxyR and rpoH were the most hypersensitive to these compounds [20].
  • Comparisons were made both by traditional and QPCR methods with similar results and indicate that the survival defect of an oxyR and oxyS mutant described previously can be attributed to the loss of oxyR alone [21].
  • Mutants affected in recG but not oxyR were dramatically impaired in DNA damage repair as measured by sensitivity to UV irradiation [17].
  • The peroxide-dependent topA P1 activation is independent of oxyR, but is mediated by Fis. This nucleoid-associated protein binds to the promoter region of topA [22].
  • The proteins induced included only five proteins that have been previously associated with stress responses, consisting of endonuclease IV (Nfo), three oxyR-regulated proteins, and one heat shock protein [23].

Analytical, diagnostic and therapeutic context of oxyR


  1. Paraquat regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12 is SoxRS independent but modulated by sigma S. Membrillo-Hernández, J., Kim, S.O., Cook, G.M., Poole, R.K. J. Bacteriol. (1997) [Pubmed]
  2. OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins. Christman, M.F., Storz, G., Ames, B.N. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  3. Novel selection for isoniazid (INH) resistance genes supports a role for NAD+-binding proteins in mycobacterial INH resistance. Chen, P., Bishai, W.R. Infect. Immun. (1998) [Pubmed]
  4. Evidence against a direct antimicrobial role of H2O2 in the infection of plants by Erwinia chrysanthemi. Miguel, E., Poza-Carrión, C., López-Solanilla, E., Aguilar, I., Llama-Palacios, A., García-Olmedo, F., Rodríguez-Palenzuela, P. Mol. Plant Microbe Interact. (2000) [Pubmed]
  5. Response of Mycobacterium tuberculosis to reactive oxygen and nitrogen intermediates. Garbe, T.R., Hibler, N.S., Deretic, V. Mol. Med. (1996) [Pubmed]
  6. Transcriptional regulator of oxidative stress-inducible genes: direct activation by oxidation. Storz, G., Tartaglia, L.A., Ames, B.N. Science (1990) [Pubmed]
  7. Overproduction of peroxide-scavenging enzymes in Escherichia coli suppresses spontaneous mutagenesis and sensitivity to redox-cycling agents in oxyR-mutants. Greenberg, J.T., Demple, B. EMBO J. (1988) [Pubmed]
  8. Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hpx- mutants of Escherichia coli. Park, S., You, X., Imlay, J.A. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  9. Identification and molecular analysis of oxyR-regulated promoters important for the bacterial adaptation to oxidative stress. Tartaglia, L.A., Storz, G., Ames, B.N. J. Mol. Biol. (1989) [Pubmed]
  10. Induction of the manganese-containing superoxide dismutase in Escherichia coli is independent of the oxidative stress (oxyR-controlled) regulon. Bowen, S.W., Hassan, H.M. J. Biol. Chem. (1988) [Pubmed]
  11. Susceptibilities of oxyR regulon mutants of Escherichia coli and Salmonella typhimurium to isoniazid. Rosner, J.L. Antimicrob. Agents Chemother. (1993) [Pubmed]
  12. Effect of inactivation of the global oxidative stress regulator oxyR on the colonization ability of Escherichia coli O1:K1:H7 in a mouse model of ascending urinary tract infection. Johnson, J.R., Clabots, C., Rosen, H. Infect. Immun. (2006) [Pubmed]
  13. Identification and characterization of a gene that controls colony morphology and auto-aggregation in Escherichia coli K12. Warne, S.R., Varley, J.M., Boulnois, G.J., Norton, M.G. J. Gen. Microbiol. (1990) [Pubmed]
  14. Oxy5, a novel protein from Arabidopsis thaliana, protects mammalian cells from oxidative stress. Kush, A., Sabapathy, K. Int. J. Biochem. Cell Biol. (2001) [Pubmed]
  15. Participation of stress-inducible systems and enzymes involved in BER and NER in the protection of Escherichia coli against cumene hydroperoxide. Asad, L.M., Medeiros, D.C., Felzenszwalb, I., Leitão, A.C., Asad, N.R. Mutat. Res. (2000) [Pubmed]
  16. Non-growing Escherichia coli cells starved for glucose or phosphate use different mechanisms to survive oxidative stress. Moreau, P.L., Gérard, F., Lutz, N.W., Cozzone, P. Mol. Microbiol. (2001) [Pubmed]
  17. Role of the Pseudomonas aeruginosa oxyR-recG operon in oxidative stress defense and DNA repair: OxyR-dependent regulation of katB-ankB, ahpB, and ahpC-ahpF. Ochsner, U.A., Vasil, M.L., Alsabbagh, E., Parvatiyar, K., Hassett, D.J. J. Bacteriol. (2000) [Pubmed]
  18. Effect of NaN3 on oxygen-dependent lethality of UV-A in Escherichia coli mutants lacking active oxygen-defence and DNA-repair systems. Yamada, K., Ono, T., Nishioka, H. J. Radiat. Res. (1996) [Pubmed]
  19. Spermidine acetylation in response to a variety of stresses in Escherichia coli. Carper, S.W., Willis, D.G., Manning, K.A., Gerner, E.W. J. Biol. Chem. (1991) [Pubmed]
  20. Interaction of lead nitrate and cadmium chloride with Escherichia coli K-12 and Salmonella typhimurium global regulatory mutants. LaRossa, R.A., Smulski, D.R., Van Dyk, T.K. J. Ind. Microbiol. (1995) [Pubmed]
  21. Neutrophil microbicidal activity: screening bacterial mutants for survival after phagocytosis using quantitative PCR. Rosen, H., Lewis, P.J., Nitzel, C.M. Jpn. J. Infect. Dis. (2004) [Pubmed]
  22. Escherichia coli response to hydrogen peroxide: a role for DNA supercoiling, topoisomerase I and Fis. Weinstein-Fischer, D., Elgrably-Weiss, M., Altuvia, S. Mol. Microbiol. (2000) [Pubmed]
  23. Escherichia coli proteins inducible by oxidative stress mediated by the superoxide radical. Walkup, L.K., Kogoma, T. J. Bacteriol. (1989) [Pubmed]
  24. A global response induced in Escherichia coli by redox-cycling agents overlaps with that induced by peroxide stress. Greenberg, J.T., Demple, B. J. Bacteriol. (1989) [Pubmed]
  25. The oxyR gene from Erwinia carotovora: cloning, sequence analysis and expression in Escherichia coli. Calcutt, M.J., Lewis, M.S., Eisenstark, A. FEMS Microbiol. Lett. (1998) [Pubmed]
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