Archives of Microbiology

, Volume 121, Issue 2, pp 169–175 | Cite as

Sequestration of arginine by polyphosphate in vacuoles of yeast (Saccharomyces cerevisiae)

  • M. Dürr
  • K. Urech
  • Th. Boller
  • A. Wiemken
  • J. Schwencke
  • M. Nagy


Isolated and purified vacuoles from yeast protoplasts contain the bulk of the cellular pool of arginine. The arginine is firmly retained in the isolated vacuoles despite of the presence of a permease which mediates arginine diffusion through the vacuolar membrane (Boller et al., 1975). It is shown, mainly by equilibrium dialysis, on vacuolar extracts, that the retention of arginine in the vacuoles is due to binding by polyphosphate. The polyphosphate appears to be located exclusively in the vacuoles. Enzymes hydrolysing polyphosphate are also located in the vacuoles. Isolated vacuoles from arginine grown cells contain about three times as much polyphosphate as vacuoles from ammonium grown cells; the vacuolar pool of arginine is correspondingly greater. Thus there seems to be a close correlation between the storage of arginine and polyphosphate. This confirms the observation that under conditions provoking “polyphosphate overcompensation” (Liss and Langen, 1962) the accumulation of enormous quantities of polyphosphate is associated with that of corresponding quantities of arginine, provided this amino acid is supplied in the medium. Yet, under certain growth conditions the cells are able to store, and to mobilize, both arginine and polyphosphate independently.

Key words

Yeast Vacuoles Compartmentation Polyphosphate Arginine 

Non-Standard Abbreviations






piperazine-N,N′-bis-2-ethanesulfonic acid


N-2-hydroxyethyl-piperazine-N′-2-ethanesulfonic acid




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  1. Boller, Th., Dürr, M., Wiemken, A.: Characterization of a specific transport system for arginine in isolated yeast vacuoles. Eur. J. Biochem.54, 81–91 (1975)Google Scholar
  2. Dürr, M., Boller, Th., Wiemken, A.: Action of proteinases on the arginine transport of purified vacuoles fromSaccharomyces cerevisiae. Biochem. Biophys. Res. Commun.73, 193–199 (1976)Google Scholar
  3. Huber-Wälchli, V., Wiemken, A.: Differential extraction of soluble pools from the cytosol and the vacuoles of yeast (Candida utilis) using DEAE-dextran. Arch. Microbiol.120, 141–149 (1979)Google Scholar
  4. Indge, K. J.: Polyphosphate of the yeast cell vacuole. J. Gen. Microbiol.51, 447–455 (1968)Google Scholar
  5. Liss, E., Langen, P.: Versuche zur Polyphosphat-Überkompensation in Hefezellen nach Polyphosphatverarmung. Archiv f. Mikrobiol.41, 383–392 (1962)Google Scholar
  6. Lowry, O. H., Rosebrough, N. J., Farr, J. C., Randall, R.: Protein measurement with the Folin phenol reagent. J. Biol. Chem.193, 265–275 (1951)Google Scholar
  7. Ludwig, J. R., Olivier, S. G., McLaughlin, C. S.: The effect of amino acids on growth and phosphate metabolism in a prototrophic yeast strain. Biochem. Biophys. Res. Commun.79, 16–23 (1977)Google Scholar
  8. Ohnishi, T., Gall, R. S., Mayer, M. L.: An improved assay of inorganic phosphate in the presence of extralabile phosphate compounds: Application to the adenosinetriphosphatase assay in the presence of phosphocreatine. Analyt. Biochem.69, 261–267 (1975)Google Scholar
  9. Peterson, G. L.: A simplification of the protein method of Lowry et al. which is more generally applicable. Anal. Biochem.83, 346 (1978)Google Scholar
  10. Ramos, F., Thuriaux, P., Wiame, J. M., Béchet, J.: The participation of ornithine and citrulline in the regulation of arginine metabolism ofSaccharomyces cerevisiae. Eur. J. Biochem.12, 40–47 (1970)Google Scholar
  11. Riemersma, J. C., Alsbach, E. J. J.: Proton translocation during anaerobic energy production inSaccharomyces cerevisiae. Biochim. Biophys. Acta339, 274–284 (1974)Google Scholar
  12. Roush, A. H.: Crystallization of purines in the vacuoles ofCandida utilis. Nature (Lond.)190, 449 (1961)Google Scholar
  13. Schwencke, J., deRobichon-Szulmajster, H.: The transport of Sadenosyl-l-methionine in isolated yeast vacuoles and spheroplasts. Eur. J. Biochem.65, 49–60 (1976)Google Scholar
  14. Seaston, A., Carr, G., Eddy, A. A.: The concentration of glycine by preparation of the yeastSaccharomyces carlsbergiensis depleated of ATP. Effect of proton gradients and uncoupling agents. Biochem. J.154, 669–676 (1976)Google Scholar
  15. Shabalin, A. Y., Vagabov, V. N., Tsiomenko, A. B., Zemlenukhina, O. A., Kulaev, J. S.: Polyphosphate kinase activity in yeast vacuoles. Biochemistry (USSR)42, 1291–1296 (1977)Google Scholar
  16. Svihla, G., Dainko, J. C., Schlenk, F.: Ultraviolet microscopy of purine compounds in the yeast vacuole. J. Bact.83, 399–402 (1963)Google Scholar
  17. Urech, K., Dürr, M., Boller, Th., Wiemken, A., Schwencke, J.: Localization of polyphosphate in vacuoles ofSaccharomyces cerevisiae. Arch. Microbiol.116, 275–278 (1978)Google Scholar
  18. Wiame, J. M.: Accumulation de l'acide phosphorique (phytine, polyphosphate). In: Encylopedia of plant physiology, Vol. IX (W. Ruhland, ed.), pp. 136–146 Berlin-Göttingen-Heidelberg: Springer 1958Google Scholar
  19. Weimberg, R.: Polyphosphate level in nongrowing cells ofSaccharomyces cerevisiae as determined by magnesium ion and the phenomenon of “Überkompensation”. J. Bact.121, 1122–1130 (1975)Google Scholar
  20. Wiemken, A.: Eigenschaften der Hefevakuole. Thesis, ETH Nr. 4340, Swiss Federal Institute Technol. Zürich (1969)Google Scholar
  21. Wiemken, A., Matile, Ph., Moor, H.: Vacuolar dynamics in synchronously budding yeast. Arch. Microbiol.70, 89–103 (1970)Google Scholar
  22. Wiemken, A., Dürr, M.: Characterization of amino acid pools in the vacuolar compartment ofSaccharomyces cerevisiae. Arch. Microbiol.101, 45–57 (1974)Google Scholar
  23. Yemm, E. W., Cocking, E. C.: The determination of amino acids with ninhydrin. Analyst (Lond.)80, 209–213 (1955)Google Scholar
  24. Zacharsky, C. A., Cooper, T. G.: Metabolite compartmentation inSaccharomyces cerevisiae. J. Bact.135, 490–497 (1978)Google Scholar

Copyright information

© Springer-Verlag 1979

Authors and Affiliations

  • M. Dürr
    • 1
  • K. Urech
    • 1
  • Th. Boller
    • 1
  • A. Wiemken
    • 1
  • J. Schwencke
    • 2
  • M. Nagy
    • 2
  1. 1.Labor für PflanzenphysiologieInstitut für Allgemeine Botanik der ETHZürichSwitzerland
  2. 2.Laboratoire d'EnzymologieCNRSGif-sur-YvetteFrance

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