Skip to main content
SpringerLink
Log in

Inorganic Polyphosphate and Physiological Properties of Saccharomyces cerevisiae Yeast Overexpressing Ppn2

  • Published:
Biochemistry (Moscow) Aims and scope Submit manuscript

Abstract

The effect of the yeast endopolyphosphatase Ppn2 overproduction on the metabolism of inorganic polyphosphates in Saccharomyces cerevisiae yeast was studied. Expression of the PPN2 gene under control of the strong constitutive promoter of glyceraldehyde 3-phosphate dehydrogenase gene (PKG1) led to a significant increase in the endopolyphosphatase activity stimulated by cobalt/zinc ions. This activity was present in both soluble and membrane subcellular fractions; it was higher toward long-chain polyphosphates and could be stimulated by ADP. The content of short-chain polyphosphates in the cells of the overexpressing strain was ~2.5 times higher compared to the parent strain. The cells overexpressing Ppn2 were more resistant to peroxide and alkali. The role of short-chain polyphosphates in the adaptation to these stress factors is discussed.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1.
Fig. 2.
Fig. 3.
Fig. 4.
Fig. 5.
Fig. 6.
Fig. 7.
Fig. 8.

Similar content being viewed by others

Abbreviations

polyP:

inorganic polyphosphate

REFERENCES

  1. Rao, N. N., Gómez-García, M. R., and Kornberg, A. (2009) Inorganic polyphosphate: essential for growth and survival, Ann. Rev. Biochem., 78, 605-647, doi: 10.1146/annurev.biochem.77.083007.093039.

    Article  CAS  PubMed  Google Scholar 

  2. Clotet, J. (2017) Polyphosphate: popping up from oblivion, Curr. Genet., 63, 15-18, doi: 10.1007/s00294-016-0611-5.

    Article  CAS  PubMed  Google Scholar 

  3. Baker, C. J., Smith, S. A., and Morrissey, J. H. (2018) Polyphosphate in thrombosis, hemostasis, and inflammation, Res. Pract. Thromb. Haemost., 3, 18-25, doi: 10.1002/rth2.12162.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  4. Xie, L., and Jakob, U. (2019) Inorganic polyphosphate, a multifunctional polyanionic protein scaffold, J. Biol. Chem., 294, 2180-2190, doi: 10.1074/jbc.REV118.002808.

    Article  CAS  PubMed  Google Scholar 

  5. Andreeva, N. A., and Okorokov, L. A. (1993) Purification and characterization of highly active and stable polyphosphatase from Saccharomyces cerevisiae cell envelope, Yeast, 9, 127-139.

    Article  CAS  Google Scholar 

  6. Wurst, H., Shiba, T., and Kornberg, A. (1995) The gene for a major exopolyphosphatase of Saccharomyces cerevisiae, J. Bacteriol., 177, 898-906.

    Article  CAS  Google Scholar 

  7. Sethuraman, A., Rao, N. N., and Kornberg, A. (2001) The endopolyphosphatase gene: essential in Saccharomyces cerevisiae, Proc. Natl. Acad. Sci. USA, 98, 8542-8547.

    Article  CAS  Google Scholar 

  8. Andreeva, N., Trilisenko, L., Eldarov, M., and Kulakovskaya, T. (2015) Polyphosphatase PPN1 of Saccharomyces cerevisiae: switching of exopolyphosphatase and endopolyphosphatase activities, PLoS One, 10, e0119594, doi: 10.1371/journal.pone.0119594.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  9. Lonetti, A., Szijgyarto, Z., Bosch, D., Loss, O., Azevedo, C., and Saiardi, A. (2011) Identification of an evolutionarily conserved family of inorganic polyphosphate endopolyphosphatases, J. Biol. Chem., 286, 31966-31974, doi: 10.1074/jbc.M111.266320.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  10. Gerasimait, R., and Mayer, A. (2017) Ppn2, a novel Zn2+-dependent polyphosphatase in the acidocalcisome-like yeast vacuole, J. Cell. Sci., 130, 1625-1636, doi: 10.1242/jcs.201061.

    Article  CAS  Google Scholar 

  11. Andreeva, N., Ledova, L., Ryazanova, L., Tomashevsky, A., Kulakovskaya, T., and Eldarov, M. (2019) Ppn2 endopolyphosphatase overexpressed in Saccharomyces cerevisiae: comparison with Ppn1, Ppx1, and Ddp1 polyphosphatases, Biochimie, 163, 101-107, doi: 10.1016/j.biochi.2019.06.001.

    Article  CAS  PubMed  Google Scholar 

  12. Lichko, L. P., Kulakovskaya, T. V., Kulakovskaya, E. V., and Kulaev, I. S. (2008) Inactivation of PPX1 and PPN1 genes encoding exopolyphosphatases of Saccharomyces cerevisiae does not prevent utilization of polyphosphates as phosphate reserve, Biochemistry (Moscow), 73, 985-989, doi: 10.1134/s0006297908090046.

    Article  CAS  Google Scholar 

  13. Lichko, L. P., Eldarov, M. A., Dumina, M. V., and Kulakovskaya, T. V. (2014) PPX1 gene overexpression has no influence on polyphosphates in Saccharomyces cerevisiae, Biochemistry (Moscow), 79, 1211-1215, doi: 10.1134/S000629791411008X.

    Article  CAS  Google Scholar 

  14. Eldarov, M. A., Baranov, M. V., Dumina, M. V., Shgun, A. A., Andreeva, N. A., Trilisenko, L. V., Kulakovskaya, T. V., Ryazanova, L. P., and Kulaev, I. S. (2013) Polyphosphates and exopolyphosphatase activities in the yeast Saccharomyces cerevisiae under overexpression of homologous and heterologous PPN1 genes, Biochemistry (Moscow), 78, 946-953, doi: 10.1134/S0006297913080129.

    Article  CAS  Google Scholar 

  15. Trilisenko, L. V., Andreeva, N. A., Eldarov, M. A., Dumina, M. V., and Kulakovskaya, T. V. (2015) Polyphosphates and polyphosphatase activity in the yeast Saccharomyces cerevisiae during overexpression of the DDP1 gene, Biochemistry (Moscow., 80, 1312-1317, doi: 10.1134/S0006297915100120.

    Article  CAS  Google Scholar 

  16. Trilisenko, L., Zvonarev, A., Valiakhmetov, A., Penin, A. A., Eliseeva, I. A., Ostroumov, V., Kulakovskiy, I. V., and Kulakovskaya, T. (2019) The reduced level of inorganic polyphosphate mobilizes antioxidant and manganese-resistance systems in Saccharomyces cerevisiae, Cells, 8, 461, doi: 10.3390/cells8050461.

    Article  CAS  PubMed Central  Google Scholar 

  17. Bensadoun, A., and Weinstein, D. (1976) Assay of proteins in the presence of interfering materials, Anal. Biochem., 70, 241-250.

    Article  CAS  Google Scholar 

  18. Vagabov, V. M., Trilisenko, L. V., and Kulaev, I. S. (2000) Dependence of inorganic polyphosphate chain length on the orthophosphate content in the culture medium of the yeast Saccharomyces cerevisiae, Biochemistry (Moscow), 65, 349-355.

    CAS  Google Scholar 

  19. Kulakovskaya, T. V., Andreeva, N. A., Karpov, A. V., Sidorov, I. A., and Kulaev, I. S. (1999) Hydrolysis of tripolyphosphate by purified exopolyphosphatase of Saccharomyces cerevisiae cytosol: kinetic model, Biochemistry (Moscow., 64, 990-993.

    CAS  Google Scholar 

  20. Andreeva, N., Trilisenko, L., Kulakovskaya, T., Dumina, M., and Eldarov, M. (2015) Purification and properties of recombinant exopolyphosphatase PPN1 and effects of its overexpression on polyphosphate in Saccharomyces cerevisiae, J. Biosci. Bioeng., 119, 52-56, doi: 10.1016/j.jbiosc.2014.06.006.

    Article  CAS  PubMed  Google Scholar 

  21. Trilisenko, L., Kulakovskaya, E., and Kulakovskaya, T. (2017) The cadmium tolerance in Saccharomyces cerevisiae depends on inorganic polyphosphate, J. Basic Microbiol., 57, 982-986, doi: 10.1002/jobm.201700257.

    Article  CAS  PubMed  Google Scholar 

  22. Gray, M. J., and Jakob, U. (2015) Oxidative stress protection by polyphosphate – new roles for an old player, Curr. Opin. Microbiol., 24, 1-6, doi: 10.1016/j.mib.2014.12.004.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  23. Lichko, L., Kulakovskaya, T., Pestov, N., and Kulaev, I. (2006) Inorganic polyphosphates and exopolyphosphatases in cell compartments of the yeast Saccharomyces cerevisiae under inactivation of PPX1 and PPN1 genes, Biosci. Rep., 26, 45-54, doi: 10.1007/s10540-006-9003-2.

    Article  CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Pushchino Scientific Center for Biological Research, Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 142290, Pushchino, Moscow Region, Russia

    L. P. Ryazanova, L. A. Ledova, N. A. Andreeva, A. N. Zvonarev & T. V. Kulakovskaya

  2. Institute of Bioengineering, Research Center of Biotechnology, Russian Academy of Sciences, 117312, Moscow, Russia

    M. A. Eldarov

Authors
  1. L. P. Ryazanova
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. L. A. Ledova
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. N. A. Andreeva
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. A. N. Zvonarev
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. M. A. Eldarov
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. T. V. Kulakovskaya
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to T. V. Kulakovskaya.

Ethics declarations

This article does not contain studies involving animals or human participants performed by any of the authors. The authors declare that they have no conflict of interest.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Ryazanova, L., Ledova, L., Andreeva, N. et al. Inorganic Polyphosphate and Physiological Properties of Saccharomyces cerevisiae Yeast Overexpressing Ppn2. Biochemistry Moscow 85, 516–522 (2020). https://doi.org/10.1134/S0006297920040124

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1134/S0006297920040124

Keywords

Search

Navigation