The heat shock and ethanol stress responses of yeast exhibit extensive similarity and functional overlap.
Sublethal heat and ethanol exposure induce essentially identical stress responses in yeast. These responses are characterized by the induction of heat shock proteins, proteins requiring a temperature above about 35 degrees C or ethanol levels above a threshold level of 4-6% (v/v) for strong induction. One induced protein, Hsp104, contributes to both thermotolerance and ethanol tolerance, while others are anti-oxidant enzymes. Heat and ethanol stress cause similar changes to plasma membrane protein composition, reducing the levels of plasma membrane H(+)-ATPase protein and inducing the plasma membrane-associated Hsp30. Both stresses also stimulate the activity of the fraction of H(+)-ATPase remaining in the plasma membrane. The resulting enhancement to catalysed proton efflux from the cell represents a considerable energy demand, yet may help to counteract the adverse effects for homeostasis of the increased membrane permeability that results from stress.
Piper
P W
PW
Department of Biochemistry and Molecular Biology, University College London, UK.
D000975:Antioxidants / Q000378:metabolism; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism; D000431:Ethanol / Q000633:toxicity*; D015966:Gene Expression Regulation, Fungal / Q000187:drug effects; D005800:Genes, Fungal / Q000187:drug effects; D006360:Heat-Shock Proteins / Q000096:biosynthesis / Q000235:genetics; D006358:Hot Temperature; D008563:Membrane Lipids / Q000378:metabolism; D011401:Promoter Regions, Genetic / Q000187:drug effects; D006180:Proton-Translocating ATPases / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000187:drug effects* / Q000235:genetics / Q000378:metabolism*; D014199:Trehalose / Q000494:pharmacology
D000975:Antioxidants; D006360:Heat-Shock Proteins; D008563:Membrane Lipids; D000431:Ethanol; D014199:Trehalose; D006180:Proton-Translocating ATPases