Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Article
  • Published:

Acceleration of potato tuber sprouting by the expression of a bacterial pyrophosphatase

Nature Biotechnology volume 19, pages 268–272 (2001)Cite this article

Abstract

Potato is a globally important crop. Unfortunately, potato farming is plagued with problems associated with the sprouting behavior of seed tubers. The data presented here demonstrate that using transgenic technology can influence this behavior. Transgenic tubers cytosolically expressing an inorganic pyrophosphatase gene derived from Escherichia coli under the control of the tuber-specific patatin promoter display significantly accelerated sprouting. The period of presprouting dormancy for transgenic tubers planted immediately after harvest is reduced by six to seven weeks when compared to wild-type tubers. This study demonstrates a method with which to regulate dormancy, an important aspect of potato crop management.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Figure 1: Pyrophosphate concentration in developing tubers.
Figure 2: Sprouting behavior of nonstored (A) and cold-stored (B) tubers.
Figure 3: Early-sprouting behavior of PP lines.
Figure 4: Comparison of the sprouting behavior of tubers from transgenic plants expressing the pyrophosphatase gene under the control of either the tuber-specific promoter B33 (lines PP-51, PP-47, and PP-43) or the constitutive CaMV 35S promoter (lines (35S)ppa1-55 and (35S)ppa1-2).

Similar content being viewed by others

References

  1. Wiltshire, J.J.J. & Cobb, A.H. A review of the physiology of potato tuber dormancy. Ann. Appl. Biol. 129, 553–569 (1996).

    Article  Google Scholar 

  2. Suttle, J.C. Dormancy in tuberous organs: problems and perspectives. In Plant dormancy, physiology, biochemistry and molecular biology. (ed. Lang, G.A.) 133–143 (Lab International, Oxon, UK; 1996).

    Google Scholar 

  3. Hemberg, T. Potato rest. In Potato physiology. (ed. Li, P.H.) 353–388 (Academic Press, London, UK; 1985).

    Google Scholar 

  4. Turnbull, C.G.N. & Hanke, D.E. The control of bud dormancy in potato Solanum tuberosum cultivar majestic tubers: evidence for the primary role of cytokinins and a seasonal pattern of changing sensitivity to cytokinin. Planta 165, 359–365 (1985).

    Article  CAS  Google Scholar 

  5. Suttle, J.C. & Banowetz, G.M. Changes in cis-zeatin and cis-zeatin riboside levels and biological activity during potato tuber dormancy. Phys. Plant. 109, 68–74 (2000).

    Article  CAS  Google Scholar 

  6. Suttle, J.C. Postharvest changes in endogenous ABA levels and ABA metabolism in relation to dormancy in potato tubers. Physiol. Plant. 95, 233–240 (1995).

    Article  CAS  Google Scholar 

  7. Sorce, C., Lorenzi, R., Ceccarelli, N. & Ranalli, P. Changes in free and conjugated IAA during dormancy and sprouting of potato tubers. Australian J. Plant Phys. 27, 371–377 (2000).

    CAS  Google Scholar 

  8. Sorce, C., Piaggesi, A., Ceccarelli, N. & Lorenzi, R. Role and metabolism of abscisic acid in potato tuber dormancy and sprouting. J. Plant Physiol. 149, 548–552 (1996).

    Article  CAS  Google Scholar 

  9. Espen, L. et al. Changes in the potato (Solanum tuberosum L.) tuber at the onset of dormancy and during storage at 23 degrees C and 3 degrees C. I. Biochemical and physiological parameters. Potato Res. 42, 189–201 (1999).

    Article  CAS  Google Scholar 

  10. ap Rees, T. & Morrell, S. Carbohydrate metabolism in developing potatoes. Am. Potato J. 67, 835–847 (1990).

    Article  CAS  Google Scholar 

  11. Kornberg, A. DNA Replication. Trends Biochem. Sci. 9, 122–124 (1984).

    Article  Google Scholar 

  12. Sonnewald, U. Expression of E. coli inorganic pyrophosphatase in transgenic plants alters photoassimilate partitioning. Plant J. 2, 571–581 (1992).

    CAS  PubMed  Google Scholar 

  13. Rocha-Sosa, M. et al. Both developmental and metabolic signals activate the expression of a class I patatin gene. EMBO J. 8, 23–30 (1989).

    Article  CAS  Google Scholar 

  14. Jelitto, T., Sonnewald, U., Willmitzer, L., Hajerezai, M. & Stitt, M. Inorganic phosphate content and metabolites in potato and tobacco plants expressing E. coli pyrophosphatase in their cytosol. Planta 188, 238–244 (1992).

    Article  CAS  Google Scholar 

  15. Geigenberger, P. et al. Overexpression of pyrophosphatase leads to increased sucrose degradation and starch synthesis, increased activities of enzymes for sucrose–starch interconversions, and increased levels of nucleotides in growing potato tubers. Planta 205, 428–437 (1998).

    Article  CAS  Google Scholar 

  16. Preiss, J. Biology and molecular biology of starch synthesis and its regulation. In Oxford surveys of plant cellular and molecular biology, Vol. 7. (ed. Miflin, B.J.) 59–114 (Oxford University Press, Oxford, UK; 1991).

    Google Scholar 

  17. Abel, G.J.W., Springer, F., Willmitzer, L. & Kossmann, J. Cloning and functional analysis of a cDNA encoding a novel 139 kDa starch synthase from potato (Solanum tuberosum L.). Plant J. 10, 981–991 (1996).

    Article  CAS  Google Scholar 

  18. Gielen, J. et al. The complete nucleotide sequence of the T-DNA of the Agrobacterium tumefaciens plastid pTi Ach5. EMBO J. 3, 835–846 (1984).

    Article  CAS  Google Scholar 

  19. Gallie, D.R., Watts, J.W., Turner, P.C. & Wilson, A. A comparison of eucaryotic viral 5′-leader sequences as enhancers of mRNA expression in vivo. Nucleic Acids Res. 15, 8693–8711 (1987).

    Article  CAS  Google Scholar 

  20. Dietze, J., Blau, A. & Willmitzer, L. Agrobacterium-mediated transformation of potato. In Gene transfer to plants. (eds Potrykus, I. & Spangenberg, G.) 24–29 (Springer-Verlag, Berlin; 1995).

    Chapter  Google Scholar 

  21. Moore, S. & Stein, W.H. Photometric ninhydrin method for use in the chromatography of amino acids. J. Biol. Chem. 176, 367–388 (1948).

    CAS  PubMed  Google Scholar 

  22. Bradford, M.M. A rapid and sensitive method for the quantification of microgram quantities of protein using the principle of protein dye binding. Anal. Biochem. 72, 248–254 (1976).

    Article  CAS  Google Scholar 

  23. Stitt, M., Lilley, R.McC., Gerhardt, R. & Heldt, H.W. Metabolite levels in specific cells and subcellular compartments of plant leaves. Methods Enzymol. 174, 518–552 (1989).

    Article  CAS  Google Scholar 

  24. Geigenberger, P. & Stitt, M. Sucrose synthase catalyses a readily reversible reaction in vivo in developing potato tubers and other plant tissues. Planta 189, 329–339 (1993).

    Article  CAS  Google Scholar 

  25. Gross, P. & ap Rees, T. Alkaline inorganic pyrophosphatase and starch synthesis in amyloplasts. Planta 167, 140–145 (1986).

    Article  CAS  Google Scholar 

  26. Zrenner, R., Salnoubat, M., Willmitzer, L. & Sonnewald, U. Evidence of the crucial role of sucrose synthase for sink strength using transgenic potato plants (Solanum tuberosum L.). Plant J. 7, 97–107 (1995).

    Article  CAS  Google Scholar 

  27. Zrenner, R., Willmitzer, L. & Sonnewald, U. Analysis of the expression of potato uridinediphosphate–glucose pyrophosphorylase and its inhibition by antisense RNA. Planta 190, 247–252 (1993).

    Article  CAS  Google Scholar 

  28. Galloway, C.M. & Mack Dugger, W. Purification and characterization of phosphoglucomutase from peas. Physiol. Plantarum 92, 479–486 (1994).

    Article  CAS  Google Scholar 

  29. Burrell, M.M. et al. Genetic manipulation of 6-phosphofructokinase in potato tubers. Planta 194, 95–101 (1994).

    Article  CAS  Google Scholar 

  30. Müller-Röber, B., Sonnewald, U. & Willmitzer, L. Antisense inhibition of the ADP glucose pyrophosphorylase in transgenic potato leads to sugar-storing tubers and influences tuber formation and expression of tuber storage protein genes. EMBO J. 11, 1229–1238 (1992).

    Article  Google Scholar 

Download references

Acknowledgements

The authors would like to thank Jessyca Dietze for performing the plant transformation, Helga Fleischer-Notter for technical support, and Linda Bartetzko, Britta Hausmann, Kathrin Lepa, Olaf Woiwode, and Bruno Marty for excellent greenhouse work and Dr. U. Sonnewald for the (35S)ppa1 plants. This research was supported by a grant from the Max-Planck Society to E.M.F.

Author information

Author notes

  1. Richard N. Trethewey

    Present address: Metanomics GmbH & Co KGaA, Tegeler Weg 33, D-10589, Berlin, Germany

Authors and Affiliations

  1. Max-Planck-Institut für Molekulare Pflanzenphysiologie, Am Mühlenberg 1, Golm, D-14476, Germany

    Eva M. Farré, Antje Bachmann, Lothar Willmitzer & Richard N. Trethewey

Authors
  1. Eva M. Farré
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Antje Bachmann
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Lothar Willmitzer
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Richard N. Trethewey
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Eva M. Farré.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Farré, E., Bachmann, A., Willmitzer, L. et al. Acceleration of potato tuber sprouting by the expression of a bacterial pyrophosphatase. Nat Biotechnol 19, 268–272 (2001). https://doi.org/10.1038/85726

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/85726

This article is cited by

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing