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. 1991 Sep;173(17):5582–5584. doi: 10.1128/jb.173.17.5582-5584.1991

Elevation of superoxide dismutase in Halobacterium halobium by heat shock.

G B Begonia 1, M L Salin 1
PMCID: PMC208277  PMID: 1885535

Abstract

Exposure of Halobacterium halobium to 50 degrees C for 2.5 h in an aerobic environment resulted in a greater than twofold increase in the activity of the manganese-containing superoxide dismutase. Nondenaturing polyacrylamide gels stained for enzymatic activity did not reveal any additional isozymes of superoxide dismutase induced by the heat shock. The maximal effect was observed at 50 degrees C, and the elevated levels of activity remained constant during 5 h of recovery at 40 degrees C. The induction of enzymatic activity was sensitive to protein synthesis inhibitors. The results are discussed relative to heat shock and stress-related proteins as well as alterations in metabolism brought about by elevated temperatures.

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Selected References

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  1. Ashburner M., Bonner J. J. The induction of gene activity in drosophilia by heat shock. Cell. 1979 Jun;17(2):241–254. doi: 10.1016/0092-8674(79)90150-8. [DOI] [PubMed] [Google Scholar]
  2. BEERS R. F., Jr, SIZER I. W. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem. 1952 Mar;195(1):133–140. [PubMed] [Google Scholar]
  3. Beauchamp C., Fridovich I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem. 1971 Nov;44(1):276–287. doi: 10.1016/0003-2697(71)90370-8. [DOI] [PubMed] [Google Scholar]
  4. 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]
  5. Bucker E. R., Martin S. E. Superoxide dismutase activity in thermally stressed Staphylococcus aureus. Appl Environ Microbiol. 1981 Feb;41(2):449–454. doi: 10.1128/aem.41.2.449-454.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. 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]
  7. Daniels C. J., McKee A. H., Doolittle W. F. Archaebacterial heat-shock proteins. EMBO J. 1984 Apr;3(4):745–749. doi: 10.1002/j.1460-2075.1984.tb01878.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hassan H. M., Fridovich I. Regulation of the synthesis of superoxide dismutase in Escherichia coli. Induction by methyl viologen. J Biol Chem. 1977 Nov 10;252(21):7667–7672. [PubMed] [Google Scholar]
  9. Kapoor M., Lewis J. Heat shock induces peroxidase activity in Neurospora crassa and confers tolerance toward oxidative stress. Biochem Biophys Res Commun. 1987 Sep 30;147(3):904–910. doi: 10.1016/s0006-291x(87)80156-0. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. 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]
  12. Loven D. P., Leeper D. B., Oberley L. W. Superoxide dismutase levels in Chinese hamster ovary cells and ovarian carcinoma cells after hyperthermia or exposure to cycloheximide. Cancer Res. 1985 Jul;45(7):3029–3033. [PubMed] [Google Scholar]
  13. 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]
  14. Oesterhelt D., Krippahl G. Phototrophic growth of halobacteria and its use for isolation of photosynthetically-deficient mutants. Ann Microbiol (Paris) 1983 Jul-Aug;134B(1):137–150. doi: 10.1016/s0769-2609(83)80101-x. [DOI] [PubMed] [Google Scholar]
  15. Pelham H. R. A regulatory upstream promoter element in the Drosophila hsp 70 heat-shock gene. Cell. 1982 Sep;30(2):517–528. doi: 10.1016/0092-8674(82)90249-5. [DOI] [PubMed] [Google Scholar]
  16. 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]
  17. Salin M. L., Duke M. V., Oesterhelt D., Ma D. P. Cloning and determination of the nucleotide sequence of the Mn-containing superoxide dismutase gene from Halobacterium halobium. Gene. 1988 Oct 15;70(1):153–159. doi: 10.1016/0378-1119(88)90113-8. [DOI] [PubMed] [Google Scholar]
  18. Salin M. L., Oesterhelt D. Purification of a manganese-containing superoxide dismutase from Halobacterium halobium. Arch Biochem Biophys. 1988 Feb 1;260(2):806–810. doi: 10.1016/0003-9861(88)90511-5. [DOI] [PubMed] [Google Scholar]
  19. Schlesinger M. J. Heat shock proteins. J Biol Chem. 1990 Jul 25;265(21):12111–12114. [PubMed] [Google Scholar]
  20. Sciandra J. J., Subjeck J. R., Hughes C. S. Induction of glucose-regulated proteins during anaerobic exposure and of heat-shock proteins after reoxygenation. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4843–4847. doi: 10.1073/pnas.81.15.4843. [DOI] [PMC free article] [PubMed] [Google Scholar]

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