Skip to main content
PMC home page
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1984 Oct 1;99(4):1441–1450. doi: 10.1083/jcb.99.4.1441

A heat shock-resistant mutant of Saccharomyces cerevisiae shows constitutive synthesis of two heat shock proteins and altered growth

PMCID: PMC2113327  PMID: 6384238

Abstract

A heat shock-resistant mutant of the budding yeast Saccharomyces cerevisiae was isolated at the mutation frequency of 10(-7) from a culture treated with ethyl methane sulfonate. Cells of the mutant are approximately 1,000-fold more resistant to lethal heat shock than those of the parental strain. Tetrad analysis indicates that phenotypes revealed by this mutant segregated together in the ratio 2+:2- from heterozygotes constructed with the wild-type strain of the opposite mating type, and are, therefore, attributed to a single nuclear mutation. The mutated gene in the mutant was herein designated hsr1 (heat shock response). The hsr1 allele is recessive to the HSR1+ allele of the wild-type strain. Exponentially growing cells of hsr1 mutant were found to constitutively synthesize six proteins that are not synthesized or are synthesized at reduced rates in HSR1+ cells unless appropriately induced. These proteins include one hsp/G0-protein (hsp48A), one hsp (hsp48B), and two G0-proteins (p73, p56). Heterozygous diploid (hsr1/HSR1+) cells do not synthesize the proteins constitutively induced in hsr1 cells, which suggests that the product of the HSR1 gene might negatively regulate the synthesis of these proteins. The hsr1 mutation also led to altered growth of the mutant cells. The mutation elongated the duration of G1 period in the cell cycle and affected both growth arrest by sulfur starvation and growth recovery from it. We discuss the problem of which protein(s) among those constitutively expressed in growing cells of the hsr1 mutant is responsible for heat shock resistance and alterations in the growth control.

Full Text

The Full Text of this article is available as a PDF (2.1 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ashburner M., Bonner J. J. The induction of gene activity in drosophilia by heat shock. Cell. 1979 Jun;17(2):241–254. doi: 10.1016/0092-8674(79)90150-8. [DOI] [PubMed] [Google Scholar]
  2. Brooks R. F. Continuous protein synthesis is required to maintain the probability of entry into S phase. Cell. 1977 Sep;12(1):311–317. doi: 10.1016/0092-8674(77)90209-4. [DOI] [PubMed] [Google Scholar]
  3. Cleveland D. W., Fischer S. G., Kirschner M. W., Laemmli U. K. Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J Biol Chem. 1977 Feb 10;252(3):1102–1106. [PubMed] [Google Scholar]
  4. Compton J. L., Bonner J. J. An in vitro assay for the specific induction and regression of puffs in isolated polytene nuclei of Drosophila melanogaster. Cold Spring Harb Symp Quant Biol. 1978;42(Pt 2):835–838. doi: 10.1101/sqb.1978.042.01.084. [DOI] [PubMed] [Google Scholar]
  5. Compton J. L., McCarthy B. J. Induction of the Drosophila heat shock response in isolated polytene nuclei. Cell. 1978 May;14(1):191–201. doi: 10.1016/0092-8674(78)90313-6. [DOI] [PubMed] [Google Scholar]
  6. Finkelstein D. B., Strausberg S. Identification and expression of a cloned yeast heat shock gene. J Biol Chem. 1983 Feb 10;258(3):1908–1913. [PubMed] [Google Scholar]
  7. Iida H., Yahara I. Durable synthesis of high molecular weight heat shock proteins in G0 cells of the yeast and other eucaryotes. J Cell Biol. 1984 Jul;99(1 Pt 1):199–207. doi: 10.1083/jcb.99.1.199. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Iida H., Yahara I. Specific early-G1 blocks accompanied with stringent response in Saccharomyces cerevisiae lead to growth arrest in resting state similar to the G0 of higher eucaryotes. J Cell Biol. 1984 Apr;98(4):1185–1193. doi: 10.1083/jcb.98.4.1185. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Ireland R. C., Berger E. M. Synthesis of low molecular weight heat shock peptides stimulated by ecdysterone in a cultured Drosophila cell line. Proc Natl Acad Sci U S A. 1982 Feb;79(3):855–859. doi: 10.1073/pnas.79.3.855. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Li G. C., Hahn G. M. Ethanol-induced tolerance to heat and to adriamycin. Nature. 1978 Aug 17;274(5672):699–701. doi: 10.1038/274699a0. [DOI] [PubMed] [Google Scholar]
  11. Loomis W. F., Wheeler S. A. Chromatin-associated heat shock proteins of Dictyostelium. Dev Biol. 1982 Apr;90(2):412–418. doi: 10.1016/0012-1606(82)90390-6. [DOI] [PubMed] [Google Scholar]
  12. McAlister L., Finkelstein D. B. Heat shock proteins and thermal resistance in yeast. Biochem Biophys Res Commun. 1980 Apr 14;93(3):819–824. doi: 10.1016/0006-291x(80)91150-x. [DOI] [PubMed] [Google Scholar]
  13. O'Farrell P. Z., Goodman H. M., O'Farrell P. H. High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell. 1977 Dec;12(4):1133–1141. doi: 10.1016/0092-8674(77)90176-3. [DOI] [PubMed] [Google Scholar]
  14. Rivin C. J., Fangman W. L. Cell cycle phase expansion in nitrogen-limited cultures of Saccharomyces cerevisiae. J Cell Biol. 1980 Apr;85(1):96–107. doi: 10.1083/jcb.85.1.96. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Smith J. A., Martin L. Do cells cycle? Proc Natl Acad Sci U S A. 1973 Apr;70(4):1263–1267. doi: 10.1073/pnas.70.4.1263. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Stewart P. R. Analytical methods for yeasts. Methods Cell Biol. 1975;12:111–147. doi: 10.1016/s0091-679x(08)60955-3. [DOI] [PubMed] [Google Scholar]
  17. Yamamori T., Yura T. Genetic control of heat-shock protein synthesis and its bearing on growth and thermal resistance in Escherichia coli K-12. Proc Natl Acad Sci U S A. 1982 Feb;79(3):860–864. doi: 10.1073/pnas.79.3.860. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES