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Self-incompatibility in Papaver targets soluble inorganic pyrophosphatases in pollen

Author

Listed:
  • Barend H. J. de Graaf

    (University of Birmingham)

  • Jason J. Rudd

    (University of Birmingham
    Rothamsted Research)

  • Michael J. Wheeler

    (University of Birmingham
    Institute of Cancer Studies, University of Birmingham)

  • Ruth M. Perry

    (University of Birmingham)

  • Elizabeth M. Bell

    (University of Birmingham)

  • Kim Osman

    (University of Birmingham)

  • F. Christopher H. Franklin

    (University of Birmingham)

  • Vernonica E. Franklin-Tong

    (University of Birmingham)

Abstract

Acting themselves Self-incompatibility is an important tactic used by higher plants to avoid self fertilization, thereby ensuring the production of new genotypes. In the corn poppy Papaver rhoeas, the self-incompatibility response triggers a Ca2+-dependent signalling network, resulting in the rapid arrest of 'self' pollen tube growth. The pollen protein p26 is one of the earliest targets for self-incompatibility signals. Now de Graaf et al. show that p26 is made up of two soluble inorganic pyrophosphatases (sPPases). PPases are highly conserved across prokaryotes and eukaryotes; via hydrolysis of inorganic pyrophosphate, they provide the driving force for many metabolic reactions. This work marks out PPases as important regulators of pollen growth, and also identifies a previously unreported regulatory mechanism for the inhibition of this important class of enzymes.

Suggested Citation

  • Barend H. J. de Graaf & Jason J. Rudd & Michael J. Wheeler & Ruth M. Perry & Elizabeth M. Bell & Kim Osman & F. Christopher H. Franklin & Vernonica E. Franklin-Tong, 2006. "Self-incompatibility in Papaver targets soluble inorganic pyrophosphatases in pollen," Nature, Nature, vol. 444(7118), pages 490-493, November.
    • Handle: RePEc:nat:nature:v:444:y:2006:i:7118:d:10.1038_nature05311
    DOI: 10.1038/nature05311
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