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Microbiology 140 (1994), 3031-3038; DOI  10.1099/13500872-140-11-3031
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Induction of major heat-shock proteins of Saccharomyces cerevisiae, including plasma membrane Hsp30, by ethanol levels above a critical threshold

P. W. Piper1, K. Talreja1, B. Panaretou1, P. Moradas-Ferreira2, K. Byrne3, U. M. Praekelt3, P. Meacock3, M. Récnacq4 and H. Boucherie4

1Department of Biochemistry and Molecular Biology, University College London, London WC1E 6BT, UK
2Instituto de Ciencias Biomedicas de Abel Salazar, Universidade do Porto, 4000 Porto, Portugal
3Department of Genetics, University of Leicester, Leicester LE1 7RH, UK
4Institut de Biochemie et Genetique Cellulaires, Université de Bourdeaux II, France

Author for correspondence: P. W. Piper. Tel: +44 71 387 7050 ext. 2212. Fax: +44 71 380 7193.

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.


Keywords: Saccharomyces cerevisiae, stress response, ethanol, heat-shock proteins, plasma-membrane proteins




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