Abstract
Exposure of a superoxide dismutase-null (sodA sodB) strain of Escherichia coli to aerobic heat stress (45 to 48 degrees C) caused a profound loss of viability, whereas the same heat stress applied anaerobically had a negligible effect. A superoxide dismutase-competent parental strain was resistant to the lethal effect of the aerobic heating. It follows that aerobic heating imposes an oxidative burden of which O2- must be a major component. This effect is not seen at 53 degrees C, presumably because, at this higher temperature, direct thermolability of vital cell components overrides the effect of superoxide radicals.
Full Text
The Full Text of this article is available as a PDF (228.6 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Amano A., Sharma A., Sojar H. T., Kuramitsu H. K., Genco R. J. Effects of temperature stress on expression of fimbriae and superoxide dismutase by Porphyromonas gingivalis. Infect Immun. 1994 Oct;62(10):4682–4685. doi: 10.1128/iai.62.10.4682-4685.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Begonia G. B., Salin M. L. Elevation of superoxide dismutase in Halobacterium halobium by heat shock. J Bacteriol. 1991 Sep;173(17):5582–5584. doi: 10.1128/jb.173.17.5582-5584.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Benov L. T., Fridovich I. Escherichia coli expresses a copper- and zinc-containing superoxide dismutase. J Biol Chem. 1994 Oct 14;269(41):25310–25314. [PubMed] [Google Scholar]
- Compton J. L., McCarthy B. J. Induction of the Drosophila heat shock response in isolated polytene nuclei. Cell. 1978 May;14(1):191–201. doi: 10.1016/0092-8674(78)90313-6. [DOI] [PubMed] [Google Scholar]
- Hass M. A., Massaro D. Regulation of the synthesis of superoxide dismutases in rat lungs during oxidant and hyperthermic stresses. J Biol Chem. 1988 Jan 15;263(2):776–781. [PubMed] [Google Scholar]
- Imlay J. A., Linn S. Mutagenesis and stress responses induced in Escherichia coli by hydrogen peroxide. J Bacteriol. 1987 Jul;169(7):2967–2976. doi: 10.1128/jb.169.7.2967-2976.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kogoma T., Yura T. Sensitization of Escherichia coli cells to oxidative stress by deletion of the rpoH gene, which encodes the heat shock sigma factor. J Bacteriol. 1992 Jan;174(2):630–632. doi: 10.1128/jb.174.2.630-632.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Lee P. C., Bochner B. R., Ames B. N. AppppA, heat-shock stress, and cell oxidation. Proc Natl Acad Sci U S A. 1983 Dec;80(24):7496–7500. doi: 10.1073/pnas.80.24.7496. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Leenders H. J., Berendes H. D. The effect of changes in the respiratory metabolism upon genome activity in Drosophila. I. The induction of gene activity. Chromosoma. 1972;37(4):433–444. doi: 10.1007/BF00284892. [DOI] [PubMed] [Google Scholar]
- Lindquist S. The heat-shock response. Annu Rev Biochem. 1986;55:1151–1191. doi: 10.1146/annurev.bi.55.070186.005443. [DOI] [PubMed] [Google Scholar]
- McCord J. M., Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049–6055. [PubMed] [Google Scholar]
- 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]