Reactive oxygen species as second messengers? Induction of the expression of yeast catalase T gene by heat and hyperosmotic stress does not require oxygen.

• Authors: Zdzisława Krawiec , Tomasz Biliński , Christoph Schüller , Helmut Ruis
• Languages of publication: EN

Abstracts

EN

It is shown that oxygen is not absolutely needed for stress-induced synthesis of catalase T in the yeast Saccharomyces cerevisiae. Yeast cells develop heat resistance after exposure to elevated temperatures in anoxia. The levels of catalase activity and thermotolerance are comparable to those in aerobically stressed cells. While these results obviously do not exclude a stress signaling role of reactive oxygen species in some systems, as postulated by other authors, they suggest that the question of the obligatory requirement for reactive oxygen species in other stress signaling systems should be rigorously re-investigated.

Keywords

EN

yeast.; osmotic stress; thermotolerance; catalase T; oxygen; Saccharomyces cerevisiae; stress response; heat shock

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2000
• Volume: 47
• Issue: 1
• Pages: 201-207

Dates

published

2000

received

1999-11-27

Contributors

author

Zdzisława Krawiec

• Zamość College of Agriculture, Szczebrzeska 102, 22-400 Zamość, Poland

author

Tomasz Biliński

• Pedagogical University of Rzeszów, T. Rejtana 16, 35-310 Rzeszów, Poland

author

Christoph Schüller

• Institute of Biochemistry and Molecular Cell Biology, University of Vienna and Ludwig Boltzmann-Forschungsstelle für Biochemie, Dr Bohr-Gasse 9, A-1030 Wien, Austria

author

Helmut Ruis

• Institute of Biochemistry and Molecular Cell Biology, University of Vienna and Ludwig Boltzmann-Forschungsstelle für Biochemie, Dr Bohr-Gasse 9, A-1030 Wien, Austria

References

• 1. Khan, A.U. & Wilson, T. (1995) Chem. Biol. 2, 437-445.
• 2. Chen, Z., Silva, H. & Klessig, D. (1993) Science 262, 1883-886.
• 3. Schreck, R., Rieber, P. & Baeuerle, P. (1991) EMBO J. 10, 2247-2258.
• 4. Sundaresan, M., Yu, Z.-X., Ferrans, V.J., Irani, K. & Finkel, T. (1995) Science 270, 296-299.
• 5. Sandstrom, P.A. & Buttke, T.M. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 4708-4712.
• 6. Jacobson, M.D. & Raff, M.C. (1995) Nature 374, 814-816.
• 7. Shimizu, S., Eguchi, Y., Kosaka, H., Kamiike, W., Matsuda, H. & Tsujimato, Y. (1995) Nature 374, 811-813.
• 8. Irani, K., Xia, Y., Zweier, J.L., Sollott, S.J., Der, C.J., Fearon, E.R., Sundaresan, M., Finkel, T. & Goldschmidt-Clermont, P.J. (1997) Science 275, 1649-1651.
• 9. Davidson, J.F., Whyte, B., Bissinger, P.H. & Schiestl, R.H. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 5116-5121.
• 10. Healy, A.M., Mariethoz, E., Pizurki, L. & Polla, B.S. (1992) Ann. N.Y. Acad. Sci. 663, 319-330.
• 11. Morimoto, R.I., Sarge, K.D. & Abravaya, K. (1992) J. Biol. Chem. 267, 21987-21990.
• 12. Morimoto, R.I. (1993) Science 259, 1409- 1410.
• 13. Wieser, R., Adam, G., Wagner, A., Schüller, Ch., Marchler, G., Ruis, H., Krawiec, Z. & Biliński, T. (1991) J. Biol. Chem. 266, 12406-12411.
• 14. Biliński, T., Łukaszkiewicz, J. & Śledziewski, A. (1978) Biochem. Biophys. Res. Commun. 83, 1225-1233.
• 15. Skoneczny, M. (1993) Ph.D. Thesis. Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw Poland.
• 16. Krawiec, Z. & Biliński, T. (1987) Bull. Pol. Ac.: Biol. 35, 285-291.
• 17. Rytka, J., Sledziewski, A., Łukaszkiewicz, J. & Biliński, T. (1978) Mol. Gen. Genet. 160, 51- 57.
• 18. Cross, H.S. & Ruis, H. (1978) Mol. Gen. Genet. 166, 37-43.
• 19. Schüller, C., Brewster, J.L., Alexander, M.R., Gustin, M.C. & Ruis, H. (1994) EMBO J. 13, 4382-4389.
• 20. Guarente, L. (1983) Methods Enzymol. 101, 181-191.
• 21. Beers, R.F. & Sizer, J.W. (1952) J. Biol. Chem. 195, 133-138.
• 22. Ruis, H. & Schüller, C. (1995) BioEssays 17, 959-965.
• 23. Winkler, H., Adam, G., Mattes, E., Schanz, H., Hartig, A. & Ruis, H. (1988) EMBO J. 7, 1799-1804.
• 24. Belazzi, T., Wagner, A., Wieser, R., Schanz, M., Adam, G., Hartig, A. & Ruis, H. (1991) EMBO J. 10, 585-592.
• 25. Barnes, C.A., Johnston, G.C. & Singer, R.A. (1990) J. Bacteriol. 172, 4352-4358.
• 26. Ruis, H. (1979) Can. J. Biochem. 57, 1122- 1130.
• 27. Zimniak, P., Hartter, E. & Ruis, H. (1975) FEBS Lett. 59, 300-304.
• 28. Porra, R.J. & Falk, J.E. (1964) Biochem. J. 90, 69-75.
• 29. Sano, S. & Granick, S. (1961) J. Biol. Chem. 236, 1173-1180.
• 30. Barlas, M., Ruis, H. & Śledziewski, A. (1978) FEBS Lett. 92, 195-199.
• 31. Moskvina, E., Imre, E.-M. & Ruis, H. (1999) Mol. Microbiol. 32, 1263-1272.
• 32. Sigler, K. & Gille, G. (1998) Folia Microbiol. 43, 369-372.
• 33. Storz, G. & Imlay, J.A. (1999) Curr. Opin. Microbiol. 2, 188-194.
• 34. Zheng, M., Aslund, F. & Storz, G. (1998) Science 279, 1718-1721.