Self-incompatibility in Papaver targets soluble inorganic pyrophosphatases in pollen

Barend H. J. de Graaf, Jason J. Rudd, Michael J. Wheeler, Ruth M. Perry, Elizabeth M. Bell, Kim Osman, F. Christopher H. Franklin and Vernonica E. Franklin-Tong ()
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Barend H. J. de Graaf: University of Birmingham
Jason J. Rudd: University of Birmingham
Michael J. Wheeler: 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

Nature, 2006, vol. 444, issue 7118, 490-493

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.

Date: 2006
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DOI: 10.1038/nature05311

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