The heat shock and ethanol stress responses of yeast exhibit extensive similarity and functional overlap

FEMS Microbiol Lett. 1995 Dec 15;134(2-3):121-7. doi: 10.1111/j.1574-6968.1995.tb07925.x.


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.

Publication types

  • Review

MeSH terms

  • Antioxidants / metabolism
  • Cell Membrane / drug effects
  • Cell Membrane / metabolism
  • Ethanol / toxicity*
  • Gene Expression Regulation, Fungal / drug effects
  • Genes, Fungal / drug effects
  • Heat-Shock Proteins / biosynthesis
  • Heat-Shock Proteins / genetics
  • Hot Temperature
  • Membrane Lipids / metabolism
  • Promoter Regions, Genetic / drug effects
  • Proton-Translocating ATPases / metabolism
  • Saccharomyces cerevisiae / drug effects*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Trehalose / pharmacology


  • Antioxidants
  • Heat-Shock Proteins
  • Membrane Lipids
  • Ethanol
  • Trehalose
  • Proton-Translocating ATPases