Acquired thermotolerance following heat shock protein synthesis prevents impairment of mitochondrial ATPase activity at elevated temperatures in Saccharomyces cerevisiae
- PMID: 2143732
- DOI: 10.1016/0014-4827(90)90143-x
Acquired thermotolerance following heat shock protein synthesis prevents impairment of mitochondrial ATPase activity at elevated temperatures in Saccharomyces cerevisiae
Abstract
The complex molecular response of cells to sudden temperature changes is a well-characterized phenomenon. Although it is clear that the induction of heat shock proteins provides protection from heat in all of the organisms so far tested, very little is known about the role that this set of proteins plays in cellular homeostasis. Recently, putative roles for hsp60 and hsp70-like proteins have been proposed in Saccharomyces cerevisiae. hsp70-like proteins have been shown to be necessary for translocation of precursor polypeptides into mitochondria and endoplasmic reticulum, while hsp60 is required for the assembly of precursor polypeptides into oligomeric complexes following incorporation into the mitochondrial matrix. In this paper, we report that a brief temperature shock (44 degrees C) impairs coupling of oxidative phosphorylation in S. cerevisiae as measured indirectly by the Cl-CCP/oligomycin assay. Furthermore, at high temperature oligomycin stimulates rather than inhibits oxygen uptake under nonthermotolerant conditions. Pretreatment of cells for a short period of time at 37 degrees C, prior to exposure to higher temperatures rescues the capacity to maintain coupling between oxidative phosphorylation and electron transport. Inhibition of cytoplasmic RNA or protein synthesis during heat shock prevents the protection of this mitochondrial activity. We propose that one of the roles of the induction of heat shock proteins (or related activities) is to protect mitochondrial ATPase activity under conditions of further increase in temperature.
Similar articles
-
Mitochondrial activity and heat-shock response during morphogenesis in the pathogenic fungus Histoplasma capsulatum.Biochem Cell Biol. 1992 Mar-Apr;70(3-4):207-14. doi: 10.1139/o92-031. Biochem Cell Biol. 1992. PMID: 1387537
-
The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria.J Cell Biol. 1996 Sep;134(6):1375-86. doi: 10.1083/jcb.134.6.1375. J Cell Biol. 1996. PMID: 8830768 Free PMC article.
-
De novo protein synthesis is essential for thermotolerance acquisition in a Saccharomyces cerevisiae trehalose synthase mutant.Biochem Mol Biol Int. 1998 Jul;45(4):663-71. doi: 10.1080/15216549800203062. Biochem Mol Biol Int. 1998. PMID: 9713688
-
Molecular events associated with acquisition of heat tolerance by the yeast Saccharomyces cerevisiae.FEMS Microbiol Rev. 1993 Aug;11(4):339-55. doi: 10.1111/j.1574-6976.1993.tb00005.x. FEMS Microbiol Rev. 1993. PMID: 8398211 Review.
-
Heat shock proteins, thermotolerance, and their relevance to clinical hyperthermia.Int J Hyperthermia. 1995 Jul-Aug;11(4):459-88. doi: 10.3109/02656739509022483. Int J Hyperthermia. 1995. PMID: 7594802 Review.
Cited by
-
Membrane lipid perturbation modifies the set point of the temperature of heat shock response in yeast.Proc Natl Acad Sci U S A. 1996 Apr 30;93(9):3870-5. doi: 10.1073/pnas.93.9.3870. Proc Natl Acad Sci U S A. 1996. PMID: 8632982 Free PMC article.
-
Hsp70 in parasites: as an inducible protective protein and as an antigen.Experientia. 1994 Nov 30;50(11-12):1067-74. doi: 10.1007/BF01923463. Experientia. 1994. PMID: 7988666 Review.
-
Cyclophilins and their possible role in the stress response.Int J Exp Pathol. 1999 Dec;80(6):305-15. doi: 10.1046/j.1365-2613.1999.00128.x. Int J Exp Pathol. 1999. PMID: 10632780 Free PMC article. Review.
-
Heat Shock Proteins Are Essential Components in Transformation and Tumor Progression: Cancer Cell Intrinsic Pathways and Beyond.Int J Mol Sci. 2019 Sep 11;20(18):4507. doi: 10.3390/ijms20184507. Int J Mol Sci. 2019. PMID: 31514477 Free PMC article. Review.
-
Previous heat shock treatment attenuates bicuculline-induced convulsions in rats.Exp Brain Res. 1996 Feb;108(1):18-22. doi: 10.1007/BF00242900. Exp Brain Res. 1996. PMID: 8721151
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
Research Materials
Miscellaneous
