Altered patterns of protein synthesis induced by heat shock of yeast

L. McAlister, S. Strausberg, A. Kulaga, D. B. Finkelstein

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64 Scopus citations


The products of protein synthesis from exponential phase cultures of Saccharomyces cerevisiae grown at 23 °C or at 36 °C appear to be essentially identical. However, yeast cells respond to a shift in culture temperature from 23 °C to 36 °C with the rapid de novo synthesis of a polypeptide species of molecular weight 100,000. Within 60-90 min after the shift this polypeptide represents approximately 2.5% of the total cellular protein, a 5-10 fold increase over the preshift level. The level of this polypeptide then decreases with continued growth of the cells at 36 °C. Analyses by SDS-polyacrylamide gel electrophoresis of polypeptides obtained from cells pulse labeled with [35S]methionine demonstrate that following a temperature shift from 23 °C to 36 °C the synthetic rate of the 100,000 molecular weight polypeptide (as well as a number of other polypeptide species) increases to a level at least 10 fold higher than that observed prior to the shift. A concomittant decrease is observed in the synthesis of a large number of polypeptide species which were actively synthesized before the shift. Maximum changes in synthetic rates are observed 20-30 min after the shift and preshift synthetic patterns are regained within 60-90 min. Synthetic changes of the same magnitude and time course can be produced by short (20-30 min) exposures to 36 °C implicating a heat shock response. Several of the transiently induced polypeptides, including the 100,000 molecular weight species, show an affinity for DNA as determined by DNA-cellulose chromatography.

Original languageEnglish (US)
Pages (from-to)63-74
Number of pages12
JournalCurrent Genetics
Issue number1
StatePublished - Dec 1 1979


  • Coordinate regulation
  • Electrophoresis
  • Saccharomyces cerevisiae
  • Translation

ASJC Scopus subject areas

  • Genetics


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