Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1985 Jan;161(1):385–392. doi: 10.1128/jb.161.1.385-392.1985

Protein synthesis during transition and stationary phases under glucose limitation in Saccharomyces cerevisiae.

H Boucherie
PMCID: PMC214883  PMID: 3881394

Abstract

Metabolic changes have been investigated during continuous growth of yeast cells inoculated in glucose-containing medium until the cells entered the stationary phase in response to glucose exhaustion. Well in advance of glucose exhaustion, a transition phase was observed, characterized by a decrease in the growth rate and a progressive reduction of protein and RNA accumulation. Two-dimensional gel analysis of the proteins synthesized during this stage showed that the pattern of proteins remained similar to that of log-phase cells. When the cells entered the stationary phase, protein accumulation was 10% of that in log-phase cells, and incorporation of labeled RNA precursor was undetectable. Analysis of protein synthesis gave evidence that the synthesis of 95% of the proteins present in log-phase cells was arrested in stationary-phase cells. Among the 20 proteins whose synthesis continues throughout the stationary phase were identified actin, aldehyde dehydrogenase, enolase, hexokinase, glyceraldehyde-3-phosphate dehydrogenase, and five heat shock proteins. In addition, the synthesis of six new proteins was observed. The occurrence of these new proteins in stationary-phase cells is presumed to result from the release of carbon catabolite repression due to glucose exhaustion.

Full text

PDF
385

Images in this article

388Image
on p.388
389Image
on p.389
390Image
on p.390

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. Beck C., von Meyenburg H. K. Enzyme pattern and aerobic growth of Saccharomyces cerevisiae under various degrees of glucose limitation. J Bacteriol. 1968 Aug;96(2):479–486. doi: 10.1128/jb.96.2.479-486.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. CHESTER V. E. The dissimilation of the carbohydrate reserves of a strain of Saccharomyces cerevisiae. Biochem J. 1963 Jan;86:153–160. doi: 10.1042/bj0860153. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Duntze W., Neumann D., Gancedo J. M., Atzpodien W., Holzer H. Studies on the regulation and localization of the glyoxylate cycle enzymes in Saccharomyces cerevisiae. Eur J Biochem. 1969 Aug;10(1):83–89. doi: 10.1111/j.1432-1033.1969.tb00658.x. [DOI] [PubMed] [Google Scholar]
  5. Elliott S. G., McLaughlin C. S. Rate of macromolecular synthesis through the cell cycle of the yeast Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1978 Sep;75(9):4384–4388. doi: 10.1073/pnas.75.9.4384. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Elliott S. G., McLaughlin C. S. Synthesis and modification of proteins during the cell cycle of the yeast Saccharomyces cerevisiae. J Bacteriol. 1979 Mar;137(3):1185–1190. doi: 10.1128/jb.137.3.1185-1190.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Haarasilta S., Oura E. On the activity and regulation of anaplerotic and gluconeogenetic enzymes during the growth process of baker's yeast. The biphasic growth. Eur J Biochem. 1975 Mar 3;52(1):1–7. doi: 10.1111/j.1432-1033.1975.tb03966.x. [DOI] [PubMed] [Google Scholar]
  8. Hartwell L. H. Macromolecule synthesis in temperature-sensitive mutants of yeast. J Bacteriol. 1967 May;93(5):1662–1670. doi: 10.1128/jb.93.5.1662-1670.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hartwell L. H. Saccharomyces cerevisiae cell cycle. Bacteriol Rev. 1974 Jun;38(2):164–198. doi: 10.1128/br.38.2.164-198.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hereford L. M., Rosbash M. Number and distribution of polyadenylated RNA sequences in yeast. Cell. 1977 Mar;10(3):453–462. doi: 10.1016/0092-8674(77)90032-0. [DOI] [PubMed] [Google Scholar]
  11. Johnston G. C., Pringle J. R., Hartwell L. H. Coordination of growth with cell division in the yeast Saccharomyces cerevisiae. Exp Cell Res. 1977 Mar 1;105(1):79–98. doi: 10.1016/0014-4827(77)90154-9. [DOI] [PubMed] [Google Scholar]
  12. Johnston G. C., Singer R. A., McFarlane S. Growth and cell division during nitrogen starvation of the yeast Saccharomyces cerevisiae. J Bacteriol. 1977 Nov;132(2):723–730. doi: 10.1128/jb.132.2.723-730.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Lillie S. H., Pringle J. R. Reserve carbohydrate metabolism in Saccharomyces cerevisiae: responses to nutrient limitation. J Bacteriol. 1980 Sep;143(3):1384–1394. doi: 10.1128/jb.143.3.1384-1394.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Ludwig J. R., 2nd, Foy J. J., Elliott S. G., McLaughlin C. S. Synthesis of specific identified, phosphorylated, heat shock, and heat stroke proteins through the cell cycle of Saccharomyces cerevisiae. Mol Cell Biol. 1982 Feb;2(2):117–126. doi: 10.1128/mcb.2.2.117. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Lutstorf U., Megnet R. Multiple forms of alcohol dehydrogenase in Saccharomyces cerevisiae. I. Physiological control of ADH-2 and properties of ADH-2 and ADH-4. Arch Biochem Biophys. 1968 Sep 10;126(3):933–944. doi: 10.1016/0003-9861(68)90487-6. [DOI] [PubMed] [Google Scholar]
  16. McFarlane E. S. Ribonuclease activity during G1 arrest of the yeast Saccharomyces cerevisiae. Arch Microbiol. 1980 Feb;124(2-3):243–247. doi: 10.1007/BF00427733. [DOI] [PubMed] [Google Scholar]
  17. Mills D. Effect of pH on adenine and amino acid uptake during sporulation in Saccharomyces cerevisiae. J Bacteriol. 1972 Oct;112(1):519–526. doi: 10.1128/jb.112.1.519-526.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. O'Farrell P. H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975 May 25;250(10):4007–4021. [PMC free article] [PubMed] [Google Scholar]
  19. Piedra D., Herrera L. Selection of auxotrophic mutants in Saccharomyces cerebisiae by a snail enzyme digestion method. Folia Microbiol (Praha) 1976;21(5):337–341. doi: 10.1007/BF02876959. [DOI] [PubMed] [Google Scholar]
  20. Piñon R. Folded chromosomes in non-cycling yeast cells: evidence for a characteristic g0 form. Chromosoma. 1978 Jul 31;67(3):263–274. doi: 10.1007/BF02569039. [DOI] [PubMed] [Google Scholar]
  21. Piñon R., Pratt D. Folded chromosomes of Saccharomyces cerevisiae: comparison of response to sporulation medium, arrest at start, and G0 arrest. Chromosoma. 1980;81(3):379–391. doi: 10.1007/BF00368150. [DOI] [PubMed] [Google Scholar]
  22. Pringle J. R., Mor J. R. Methods for monitoring the growth of yeast cultures and for dealing with the clumping problem. Methods Cell Biol. 1975;11:131–168. doi: 10.1016/s0091-679x(08)60320-9. [DOI] [PubMed] [Google Scholar]
  23. Schenberg-Frascino A., Moustacchi E. Lethal and mutagenic effects of elevated temperature on haploid yeast. I. Variations in sensitivity during the cell cycle. Mol Gen Genet. 1972;115(3):243–257. doi: 10.1007/BF00268888. [DOI] [PubMed] [Google Scholar]
  24. Sogin S. J., Saunders C. A. Fluctuation in polyadenylate size and content in exponential- and stationary-phase cells of Saccharomyces cerevisiae. J Bacteriol. 1980 Oct;144(1):74–81. doi: 10.1128/jb.144.1.74-81.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Sumrada R., Cooper T. G. Control of vacuole permeability and protein degradation by the cell cycle arrest signal in Saccharomyces cerevisiae. J Bacteriol. 1978 Oct;136(1):234–246. doi: 10.1128/jb.136.1.234-246.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Swida U., Schulz-Harder B., Kücherer C., Käufer N. The occurrence of two ribosomal ribonucleases depending on growth phase in yeast. Induction of ribonuclease in glucose-starved cells. Biochim Biophys Acta. 1981 Jan 29;652(1):129–138. doi: 10.1016/0005-2787(81)90216-1. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES