1887

Abstract

Exponentially growing cells are more sensitive to oxidants such as hydrogen peroxide and superoxides than stationary phase cells. Using disruption mutations in the genes encoding the two . superoxide dismutases, we show that the principal mechanism of toxicity of redox-cycling compounds, such as menadione and plumbagin, is via the production of superoxide anions. Using two-dimensional polyacrylamide gel electrophoresis we have compared the pattern of protein expression in cells labelled with -[S]methionine and stressed with either HOor menadione. Three groups of proteins were evident: those whose levels are elevated by both HOand menadione, and those specifically induced by either HOor menadione. Experiments with promoter fusions demonstrated that one of the heat inducible forms of HSP70 () was inducible with HO. Furthermore, induction of the yeast HO-responsive promoter by menadione required the metabolism of menadione.

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1994-12-01
2024-04-19
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References

  1. Baggioloini M., Thelen M. In Oxidative Stress: Oxidants and Antioxidants 1991 Edited by Sies H. London: Academic Press; pp 399–420
    [Google Scholar]
  2. Bermingham-McDonogh O., Gralla E.B., Valentine J.S. The copper,zinc-superoxide dismutase gene of Saccharomyces cerevisiae: cloning, sequencing, and biological activity. Proc Natl Acad Sci USA 1988; 85:4789–4793
    [Google Scholar]
  3. Bonneaud N., Ozier-Kalogeropoulos O., Li G., Labouesse M., Minivielle-Sebastia L., Lacroute F. A family of low and high copy replicative, integrative and single-stranded A. cerevisiae ¡PL. coli shuttle vectors. Yeast 1991; 7:609–615
    [Google Scholar]
  4. Collinson L.P., Dawes I.W. Inducibility of the response of yeast cells to peroxide stress. J Gen Microbiol 1992; 138:329–335
    [Google Scholar]
  5. Demple B. Regulation of bacterial oxidative stress genes. Amu Rev Genet 1991; 25:315–337
    [Google Scholar]
  6. Demple B., Amabile-Cuevas C.F. Redox redux: the control of oxidative stress responses. Cell 1991; 67:837–839
    [Google Scholar]
  7. Dowds B.C.A., Murphy P., McConnell D.J., Devine K.M. Relationship among oxidative stress, growth cycle, and sporulation in Bacillus subtilis. J Bacteriol 1987; 169:5771–5775
    [Google Scholar]
  8. Flattery-O'Brien J., Collinson L.P., Dawes I.W. Saccharomyces cerevisiae has an inducible response to menadione which differs from that to hydrogen peroxide. J Gen Microbiol 1993; 139:501–507
    [Google Scholar]
  9. Guarente L. Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast. Methods Enzymol 1983; 101:181–191
    [Google Scholar]
  10. Guidot D.M., McCord J.M., Wright R.M., Repine J.E. Absence of electron transport (Rho° state) restores growth of a manganese-superoxide dismutase-deficient Sacharomyces cerevisiae in hyperoxia. J Biol Chem 1993; 268:26699–26703
    [Google Scholar]
  11. Greenberg J.T., Demple B. A global response induced in Escherichia coli by redox-cycling agents overlaps with that induced by peroxide stress. J Bacteriol 1989; 171:3933–3939
    [Google Scholar]
  12. Halliwell B., Gutteridge J.M.C. Oxygen-toxicity, oxygen radicals, transition-metals and disease. Biochem J 1984; 219:1–14
    [Google Scholar]
  13. Ito H., Fukuda Y., Murata K., Kimura A. Transformation of intact yeast cells treated with alkali cations. J Bacteriol 1983; 153:163–168
    [Google Scholar]
  14. Jamieson D.J. Saccharomyces cerevisiae has distinct adaptive responses to both hydrogen peroxide and menadione. J Bacteriol 1992; 174:6678–6681
    [Google Scholar]
  15. Kuge S., Jones N. YAP1 dependent activation of TRX2 is essential for the response of Saccharomyces cerevisiae to oxidative stress by hydroperoxides. EMBO J 1994; 13:655–664
    [Google Scholar]
  16. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680–685
    [Google Scholar]
  17. Lee J.-S., Hah Y.-C., Roe J.-H. The induction of oxidative enzymes in Streptomyces coelicolor upon hydrogen peroxide treatment. J Gen Microbiol 1993; 139:1013–1018
    [Google Scholar]
  18. Marchler G., Schuller C., Adam G., Ruis H. A Saccharomyces cerevisiae UAS element controlled by protein kinase A activates transcription in response to a variety of stress conditions. EMBO J 1993; 12:1997–2003
    [Google Scholar]
  19. McCord J.M., Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 1969; 244:6049–6055
    [Google Scholar]
  20. Petko L., Lindquist S. HSP26 is not required for growth at high temperatures, nor for thermotolerance, spore development, or germination. Cell 1986; 45:885–894
    [Google Scholar]
  21. Rose M.D., Winston F., Hieter P. Methods in Yeast Genetics 1990 Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
  22. Rothstein R.J. One-step gene disruption in yeast. Methods Enzymol 1983; 101:202–211
    [Google Scholar]
  23. Ruis H., Hamilton B. Regulation of yeast catalase genes. In Molecular Biology of Free Radical Scavenging Systems 1992 Cold Spring Harbor, NY: Cold Spring Harbor Laboratory; pp 153–172
    [Google Scholar]
  24. Scott M.D., Meshnick S.R., Eaton J.W. Superoxide dismutase-rich bacteria. J Biol Chem 1987; 262:3640–3645
    [Google Scholar]
  25. Sherman F., Fink G.R., Hicks J.B. Methods in Yeast Genetics 1982 Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
  26. Slater M.R., Craig E.A. Transcriptional regulation of an hsp70 heat shock gene in the yeast Saccharomyces cerevisiae. Mol Cell Biol 1987; 7:1906–1916
    [Google Scholar]
  27. Storz G., Christman M.F., Sies H., Ames B.N. Spontaneous mutagenesis and oxidative damage to DNA in Salmonella typhimurium. Proc Natl Acad Sei USA 1987; 84:8917–8921
    [Google Scholar]
  28. Storz G., Tartaglia L.A., Farr S.B., Ames B.N. Bacterial defenses against oxidative stress. Trends Genet 1990; 6:363–368
    [Google Scholar]
  29. Van Loon A.P.G.M., Pesold-Hurt B., Schatz G. A yeast mutant lacking mitochondrial manganese-superoxide dismutase is hypersensitive to oxygen. Proc Natl Acad Sei USA 1986; 83:3820–3824
    [Google Scholar]
  30. Varela J.C.S., Van-Beekvelt C., Planta R.J., Mager W.H. Osmostress-induced changes in yeast gene expression. Mol Microbiol 1992; 6:2183–2190
    [Google Scholar]
  31. Weesterbeek-Marres C.A.M., Moore M.M., Autor A.P. Regulation of manganese superoxide dismutase in Saccharomyces cerevisiae. Fur J Biochem 1988; 174:611–620
    [Google Scholar]
  32. Wolff S.P., Garner A., Dean R.T. Free radicals, lipids and protein degradation. Trends Biochem Sei 1986; 11:27–31
    [Google Scholar]
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