Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1992 Jan;174(2):630–632. doi: 10.1128/jb.174.2.630-632.1992

Sensitization of Escherichia coli cells to oxidative stress by deletion of the rpoH gene, which encodes the heat shock sigma factor.

T Kogoma 1, T Yura 1
PMCID: PMC205760  PMID: 1729253

Abstract

A deletion in the rpoH gene greatly increased the sensitivity of Escherichia coli sodA sodB mutants to oxidative stress. The effect of the rpoH deletion on sodA+ sodB+ cells was only marginal. Mutations in heat shock genes singly sensitized sodA sodB double mutant cells to plumbagin. sodA sodB double mutants were neither more sensitive nor more resistant to thermal stress than the wild type.

Full text

PDF
630

Selected References

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

  1. Ang D., Chandrasekhar G. N., Zylicz M., Georgopoulos C. Escherichia coli grpE gene codes for heat shock protein B25.3, essential for both lambda DNA replication at all temperatures and host growth at high temperature. J Bacteriol. 1986 Jul;167(1):25–29. doi: 10.1128/jb.167.1.25-29.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bochner B. R., Lee P. C., Wilson S. W., Cutler C. W., Ames B. N. AppppA and related adenylylated nucleotides are synthesized as a consequence of oxidation stress. Cell. 1984 May;37(1):225–232. doi: 10.1016/0092-8674(84)90318-0. [DOI] [PubMed] [Google Scholar]
  3. Carlioz A., Touati D. Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life? EMBO J. 1986 Mar;5(3):623–630. doi: 10.1002/j.1460-2075.1986.tb04256.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Christman M. F., Morgan R. W., Jacobson F. S., Ames B. N. Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium. Cell. 1985 Jul;41(3):753–762. doi: 10.1016/s0092-8674(85)80056-8. [DOI] [PubMed] [Google Scholar]
  5. Cowing D. W., Bardwell J. C., Craig E. A., Woolford C., Hendrix R. W., Gross C. A. Consensus sequence for Escherichia coli heat shock gene promoters. Proc Natl Acad Sci U S A. 1985 May;82(9):2679–2683. doi: 10.1073/pnas.82.9.2679. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Farr S. B., Kogoma T. Oxidative stress responses in Escherichia coli and Salmonella typhimurium. Microbiol Rev. 1991 Dec;55(4):561–585. doi: 10.1128/mr.55.4.561-585.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Georgopoulos C. P. A new bacterial gene (groPC) which affects lambda DNA replication. Mol Gen Genet. 1977 Feb 28;151(1):35–39. doi: 10.1007/BF00446910. [DOI] [PubMed] [Google Scholar]
  8. Grossman A. D., Erickson J. W., Gross C. A. The htpR gene product of E. coli is a sigma factor for heat-shock promoters. Cell. 1984 Sep;38(2):383–390. doi: 10.1016/0092-8674(84)90493-8. [DOI] [PubMed] [Google Scholar]
  9. Imlay J. A., Fridovich I. Assay of metabolic superoxide production in Escherichia coli. J Biol Chem. 1991 Apr 15;266(11):6957–6965. [PubMed] [Google Scholar]
  10. Kusukawa N., Yura T. Heat shock protein GroE of Escherichia coli: key protective roles against thermal stress. Genes Dev. 1988 Jul;2(7):874–882. doi: 10.1101/gad.2.7.874. [DOI] [PubMed] [Google Scholar]
  11. Kusukawa N., Yura T., Ueguchi C., Akiyama Y., Ito K. Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli. EMBO J. 1989 Nov;8(11):3517–3521. doi: 10.1002/j.1460-2075.1989.tb08517.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Morgan R. W., Christman M. F., Jacobson F. S., Storz G., Ames B. N. Hydrogen peroxide-inducible proteins in Salmonella typhimurium overlap with heat shock and other stress proteins. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8059–8063. doi: 10.1073/pnas.83.21.8059. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Palmer R., Gallagher P. M., Boyko W. L., Ganschow R. E. Genetic control of levels of murine kidney glucuronidase mRNA in response to androgen. Proc Natl Acad Sci U S A. 1983 Dec;80(24):7596–7600. doi: 10.1073/pnas.80.24.7596. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Privalle C. T., Fridovich I. Induction of superoxide dismutase in Escherichia coli by heat shock. Proc Natl Acad Sci U S A. 1987 May;84(9):2723–2726. doi: 10.1073/pnas.84.9.2723. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Tobe T., Ito K., Yura T. Isolation and physical mapping of temperature-sensitive mutants defective in heat-shock induction of proteins in Escherichia coli. Mol Gen Genet. 1984;195(1-2):10–16. doi: 10.1007/BF00332716. [DOI] [PubMed] [Google Scholar]
  16. Wilson G. G., Young K. Y., Edlin G. J., Konigsberg W. High-frequency generalised transduction by bacteriophage T4. Nature. 1979 Jul 5;280(5717):80–82. doi: 10.1038/280080a0. [DOI] [PubMed] [Google Scholar]
  17. Yamamori T., Yura T. Genetic control of heat-shock protein synthesis and its bearing on growth and thermal resistance in Escherichia coli K-12. Proc Natl Acad Sci U S A. 1982 Feb;79(3):860–864. doi: 10.1073/pnas.79.3.860. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Zhang Q. M., Yonei S. Induction of manganese-superoxide dismutase by membrane-binding drugs in Escherichia coli. J Bacteriol. 1991 Jun;173(11):3488–3491. doi: 10.1128/jb.173.11.3488-3491.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Zhou Y. N., Kusukawa N., Erickson J. W., Gross C. A., Yura T. Isolation and characterization of Escherichia coli mutants that lack the heat shock sigma factor sigma 32. J Bacteriol. 1988 Aug;170(8):3640–3649. doi: 10.1128/jb.170.8.3640-3649.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES