Induction of major heat-shock proteins of Saccharomyces cerevisiae, including plasma membrane Hsp30, by ethanol levels above a critical threshold.

Abstract

Many of the changes induced in yeast by sublethal yet stressful amounts of ethanol are the same as those resulting from sublethal heat stress. They include an inhibition of fermentation, increased induction of petites and stimulation of plasma membrane ATPase activity. Ethanol, at concentrations (4-10%, v/v) that affect growth and fermentation rates, is also a potent inducer of heat-shock proteins including those members of the Hsp70 protein family induced by heat shock. This induction occurs above a threshold level of about 4% ethanol, although different heat-shock proteins and heat-shock gene promoters are optimally induced at different higher ethanol levels. In addition ethanol (6-8%) causes the same two major changes to integral plasma-membrane protein composition that result from a sublethal heat stress, reduction in levels of the plasma membrane ATPase protein and acquisition of the plasma membrane heat-shock protein Hsp30.