Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1977 Nov;132(2):723–730. doi: 10.1128/jb.132.2.723-730.1977

Growth and cell division during nitrogen starvation of the yeast Saccharomyces cerevisiae.

G C Johnston, R A Singer, S McFarlane
PMCID: PMC221916  PMID: 334751

Abstract

During nitrogen starvation, cells of the yeast Saccharomyces cerevisiae increased threefold in number, and little ribonucleic acid (RNA) and protein were accumulated. Both RNA and protein were extensivley degraded during starvation, suggesting that intracellular macromolecules could supply most of the growth requirements. The types and proportions of stable RNA synthesized during nitrogen deprivation were characteristic of exponentially growing cells; however, the complement of proteins synthesized was different. We conclude that, once events in the deoxyribonucleic acid division cycle are initiated, cells can complete division with little dependence on continued net cell growth.

Full text

PDF
723

Images in this article

726Image
on p.726

Selected References

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

  1. Adman R., Schultz L. D., Hall B. D. Transcription in yeast: separation and properties of multiple FNA polymerases. Proc Natl Acad Sci U S A. 1972 Jul;69(7):1702–1706. doi: 10.1073/pnas.69.7.1702. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Becker H., Stanners C. P. Control of macromolecular synthesis in proliferating and resting Syrian hamster cells in monolayer culture. 3. Electrophoretic patters of newly synthesized proteins in synchronized proliferating cells and resting cells. J Cell Physiol. 1972 Aug;80(1):51–62. doi: 10.1002/jcp.1040800107. [DOI] [PubMed] [Google Scholar]
  3. Fox T. O., Pardee A. B. Proteins made in the mammalian cell cycle. J Biol Chem. 1971 Oct 25;246(20):6159–6165. [PubMed] [Google Scholar]
  4. Goldberg A. L., Dice J. F. Intracellular protein degradation in mammalian and bacterial cells. Annu Rev Biochem. 1974;43(0):835–869. doi: 10.1146/annurev.bi.43.070174.004155. [DOI] [PubMed] [Google Scholar]
  5. Goldberg A. L., St John A. C. Intracellular protein degradation in mammalian and bacterial cells: Part 2. Annu Rev Biochem. 1976;45:747–803. doi: 10.1146/annurev.bi.45.070176.003531. [DOI] [PubMed] [Google Scholar]
  6. HALVORSON H. Intracellular protein and nucleic acid turnover in resting yeast cells. Biochim Biophys Acta. 1958 Feb;27(2):255–266. doi: 10.1016/0006-3002(58)90332-9. [DOI] [PubMed] [Google Scholar]
  7. 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]
  8. Hartwell L. H. Periodic density fluctuation during the yeast cell cycle and the selection of synchronous cultures. J Bacteriol. 1970 Dec;104(3):1280–1285. doi: 10.1128/jb.104.3.1280-1285.1970. [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. Hopper A. K., Magee P. T., Welch S. K., Friedman M., Hall B. D. Macromolecule synthesis and breakdown in relation to sporulation and meiosis in yeast. J Bacteriol. 1974 Aug;119(2):619–628. doi: 10.1128/jb.119.2.619-628.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Johnson B. F. Morphometric analysis of yeast cells. II. Cell size of Schizosaccharomyces pombe during the growth cycle. Exp Cell Res. 1968 Jan;49(1):59–68. doi: 10.1016/0014-4827(68)90519-3. [DOI] [PubMed] [Google Scholar]
  12. Johnston G. C. Cell size and budding during starvation of the yeast Saccharomyces cerevisiae. J Bacteriol. 1977 Nov;132(2):738–739. doi: 10.1128/jb.132.2.738-739.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. 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]
  14. Kimball R. F., Perdue S. W., Chu E. H., Ortiz J. R. Microphotometric and autoradiographic studies on the cell cycle and cell size during growth and decline of Chinese hamster cell cultures. Exp Cell Res. 1971 May;66(1):17–32. doi: 10.1016/s0014-4827(71)80007-1. [DOI] [PubMed] [Google Scholar]
  15. MIDDELHOVEN W. J. THE PATHWAY OF ARGININE BREAKDOWN IN SACCHAROMYCES CEREVISIAE. Biochim Biophys Acta. 1964 Dec 9;93:650–652. doi: 10.1016/0304-4165(64)90349-6. [DOI] [PubMed] [Google Scholar]
  16. Middelhoven W. J. The derepression of arginase and of ornithine transaminase in nitrogen-starved baker's yeast. Biochim Biophys Acta. 1968 Mar 11;156(2):440–443. doi: 10.1016/0304-4165(68)90284-5. [DOI] [PubMed] [Google Scholar]
  17. Nurse P., Wiemken A. Amino acid pools and metabolism during the cell division cycle of arginine-grown Candida utilis. J Bacteriol. 1974 Mar;117(3):1108–1116. doi: 10.1128/jb.117.3.1108-1116.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. PRESCOTT D. M. Relation between cell growth and cell division. II. The effect of cell size on cell growth rate and generation time in Amoeba proteus. Exp Cell Res. 1956 Aug;11(1):86–94. doi: 10.1016/0014-4827(56)90192-6. [DOI] [PubMed] [Google Scholar]
  19. Pine M. J. Turnover of intracellular proteins. Annu Rev Microbiol. 1972;26:103–126. doi: 10.1146/annurev.mi.26.100172.000535. [DOI] [PubMed] [Google Scholar]
  20. Ponta H., Ponta U., Wintersberger E. Purification and properties of DNA-dependent RNA polymerases from yeast. Eur J Biochem. 1972 Aug 18;29(1):110–118. doi: 10.1111/j.1432-1033.1972.tb01964.x. [DOI] [PubMed] [Google Scholar]
  21. Pringle J. R. Methods for avoiding proteolytic artefacts in studies of enzymes and other proteins from yeasts. Methods Cell Biol. 1975;12:149–184. doi: 10.1016/s0091-679x(08)60956-5. [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. SALZMAN N. P. Systematic fluctuations in the cellular protein, RNA and DNA during growth of mammalian cell cultures. Biochim Biophys Acta. 1959 Jan;31(1):158–163. doi: 10.1016/0006-3002(59)90451-2. [DOI] [PubMed] [Google Scholar]
  24. SIEGEL M. R., SISLER H. D. SITE OF ACTION OF CYCLOHEXIMIDE IN CELLS OF SACCHAROMYCES PASTORIANUS. II. THE NATURE OF INHIBITION OF PROTEIN SYNTHESIS IN A CELL-FREE SYSTEM. Biochim Biophys Acta. 1964 May 18;87:83–89. [PubMed] [Google Scholar]
  25. Schimke R. T., Doyle D. Control of enzyme levels in animal tissues. Annu Rev Biochem. 1970;39:929–976. doi: 10.1146/annurev.bi.39.070170.004433. [DOI] [PubMed] [Google Scholar]
  26. Slater M., Schaechter M. Control of cell division in bacteria. Bacteriol Rev. 1974 Jun;38(2):199–221. doi: 10.1128/br.38.2.199-221.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. 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]
  28. Unger M. W., Hartwell L. H. Control of cell division in Saccharomyces cerevisiae by methionyl-tRNA. Proc Natl Acad Sci U S A. 1976 May;73(5):1664–1668. doi: 10.1073/pnas.73.5.1664. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Waldron C., Lacroute F. Effect of growth rate on the amounts of ribosomal and transfer ribonucleic acids in yeast. J Bacteriol. 1975 Jun;122(3):855–865. doi: 10.1128/jb.122.3.855-865.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Weber K., Pringle J. R., Osborn M. Measurement of molecular weights by electrophoresis on SDS-acrylamide gel. Methods Enzymol. 1972;26:3–27. doi: 10.1016/s0076-6879(72)26003-7. [DOI] [PubMed] [Google Scholar]
  31. Whitney P. A., Magasanik B. The induction of arginase in Saccharomyces cerevisiae. J Biol Chem. 1973 Sep 10;248(17):6197–6202. [PubMed] [Google Scholar]

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

RESOURCES