Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
권호 표지

Effect of Trehalose on Stabilization of Cellular Components and Critical Targets Against Heat Shock in Saccharomyces cerevisiae KNU5377

  • PAIK SANG-KYOO (Department of Microbiology, School of Life Sciences and Biotechnology, Kyungpook National University) ;
  • YUN HAE-SUN (Department of Microbiology, School of Life Sciences and Biotechnology, Kyungpook National University) ;
  • IWAHASHI HITOSHI (National Institute of Advanced Industrial Science and Technology) ;
  • OBUCHI KAORU (National Institute of Advanced Industrial Science and Technology) ;
  • JIN INGNYOL (Department of Microbiology, School of Life Sciences and Biotechnology, Kyungpook National University)
  • Published : 2005.10.01
Download PDF
⟨ Previous Next ⟩

Abstract

In our previous study [14], we found that heat-shock exposure did not stimulate the neutral trehalase activity in Sacchromyces cerevisiae KNU5377, but did in ATCC24858. Consequently, the trehalose content in KNU5377 became 2.6 times higher than that in ATCC24858. Because trehalose has been shown to stabilize the structure and function of some macromolecules, the present work was focused to elucidate the relationship between trehalose content of these strains and thermal stabilities of whole cells, through differential scanning calorimetry (DSC), and to predict critical targets calculated from the hyperthermic cell killing rates. These analyses showed that the prominent DSC transition of both strains gave identical $T_m$ (transition temperature) values in exponentially growing cells, and that the $T_m$ values of critical targets was about $3^{\circ}C$ higher in KNU5377 than in ATCC24858. Both heat-shocked KNU5377 and ATCC24858 cells displayed similar shifts in their DSC transition profiles. On the other hand, the $T_m$ value of the critical target of KNU5377 was decreased by $2.1^{\circ}C$, which was still higher than ATCC24858 showing no changes. In view of these results, the intrinsic thermotolerance of KNU5377 did not appear to result from the stability of entire cellular components, but rather possibly from that of particular macromolecules, including critical targets, even though it should be investigated in more details. Although the trehalose levels in heat-shocked cells are significantly different, as described in our previous study [14], the overall pattern of thermal stabilities and their predicted critical targets in two heat-shocked strains seemed to be identical. These data suggest that the trehalose levels examined before and after heat shock of exponentially growing cells are not closely correlated with the stabilities of whole cells and/or critical targets in both yeast strains.

Keywords

References

  1. Attfield, P. V. 1987. Trehalose accumulates in Saccharomyces cerevisiae during exposure to agents that induce heat shock response. FEBS Lett. 225: 257-263
  2. Gross, C. and K. Watson. 1996. Heat shock protein synthesis and trehalose accumulation are not required for induced thermotolerance in depressed Saccharomyces cerevisiae. Biochem. Biophys. Res. Comm. 220: 766-772 https://doi.org/10.1006/bbrc.1996.0478
  3. Gross, C. and K. Watson. 1998. Application of mRNA differential display to investigate gene expression in thermotolerant cells of Saccharomyces cerevisiae. Yeast 14: 431-432 https://doi.org/10.1002/(SICI)1097-0061(19980330)14:5<431::AID-YEA242>3.0.CO;2-V
  4. Hottiger, T., P. Schmutz, and A. Wiemken. 1987. Heat-induced accumulation and futile cycling of trehalose in Saccharomyces cerevisiae. J. Bacteriol. 169: 5518-5522 https://doi.org/10.1128/jb.169.12.5518-5522.1987
  5. Iwahashi, H., K. Obuchi, S. Fujii, and Y. Komatsu. 1995. The correlative evidence suggesting that trehalose stabilizes membrane structure in the yeast Saccharomyces cerevisiae. Cell. Mol. Biol. 41: 763-769
  6. Kim, J. W., I. N. Jin, and J. H. Seu. 1995. Isolation of Saccharomyces cerevisiae F 38-1 (renamed to KNU5377), a thermotolerant yeast for fuel alcohol production at elevated temperature. Kor. J. Appl. Microbiol. Biotechnol. 23: 617-623
  7. Lepock, J. R. and J. Kruuv. 1992. Mechanisms of thermal cytotoxicity. In Gerner, E. W. and Cetas, C. T. (eds.). Hyperthermic Oncology. Vol. 2. Arizona Board of Regents, Tuscon, Arizona
  8. Lepock, J. R., H. E. A. Frey, M. Rodhal, and J. Kruuv. 1988. Thermal analysis of CHL V79 cells using differential scanning calorimetry: Implication for hyperthermic cell killing and the heat shock response. J. Cell. Physiol. 137: 14-24 https://doi.org/10.1002/jcp.1041370103
  9. Lindquist, S. 1986. The heat-shock response. Annu. Rev. Biochem. 55: 1151-1191 https://doi.org/10.1146/annurev.bi.55.070186.005443
  10. Miles, D. A., L. Knott, I. G. Sumner, and A. Bailey. 1998. Differences between the thermal stabilities of the three triple-helicle domains of type IX collagen. J. Mol. Biol. 27: 135-144
  11. Nwaka, S. and H. Holzer. 1998. Molecular biology of trehalose and the trehalases in the yeast Saccharomyces cerevisiae. Prog. Nucleic Acid Res. Mol. Biol. 58: 197-237 https://doi.org/10.1016/S0079-6603(08)60037-9
  12. Obuchi, K., H. Iwahashi, J. R. Lepock, and Y. Komatsu. 1998. Stabilization of two families of critical targets for hyperthermic cell killing and acquired thermotolerance of yeast cells. Yeast 14: 1249-1255 https://doi.org/10.1002/(SICI)1097-0061(1998100)14:14<1249::AID-YEA323>3.0.CO;2-A
  13. Obuchi, K., H. Iwahashi, J. R. Lepock, and Y. Komatsu. 2000. Calorimetric characterization of critical targets for killing and acquired thermotolerance in yeast. Yeast 16: 111-119 https://doi.org/10.1002/(SICI)1097-0061(20000130)16:2<111::AID-YEA507>3.0.CO;2-V
  14. Paik, S. K., H. S. Yun, H. Y. Sohn, and I. Jin. 2003. Effects of trehalose accumulation on the intrinsic and acquired thermotolerance in a natural isolate Saccharomyces cerevisiae KNU5377. J. Microbiol. Biotechnol. 13: 85-89
  15. Ribeiro, M. J. S., J. T. Silva, and A. D. Panek. 1994. Trehalose metabolism in Saccharomyces cerevisiae during heat shock. Biochem. Biophys. Acta 1200: 139-147 https://doi.org/10.1016/0304-4165(94)90128-7
  16. Singer, M. A. and S. Lindquist. 1998. Thermotolerance in Saccharomyces cerevisiae: The Yin and Yang of trehalose. Trends Biotechnol. 16: 460-468 https://doi.org/10.1016/S0167-7799(98)01251-7
  17. Sola-Penna, M. and J. R. Meyer-Fernandes. 1998. Stabilization against thermal inactivation promoted by sugars on enzyme structure and function: Why is trehalose more effective than other sugars? Arch. Biochem. Biophys. 360: 10-14 https://doi.org/10.1006/abbi.1998.0906
  18. Wiemken, A. 1990. Trehalose in Yeast, stress protectant rather than reserve carbohydrate. Antonie Van Leeuwenhoek 58: 209-217 https://doi.org/10.1007/BF00548935
  19. Yun, H. S., S. K. Paik, I. S. Kim, I. Jin, and H. Y. Sohn. 2004. Direct evidence of intracellular alkalinization in Saccharomyces cerevisiae KNU5377 exposed to inorganic sulfuric acid. J. Microbiol. Biotechnol. 14: 243-249