Self-incompatibility in Papaver targets soluble inorganic pyrophosphatases in pollen

Bernardus De Graaf, JJ Rudd, Michael Wheeler, Ruth Perry, EM Bell, Kim Osman, Frederick Franklin, Vernonica Franklin Tong

Research output: Contribution to journalArticle

59 Citations (Scopus)


In higher plants, sexual reproduction involves interactions between pollen and pistil. A key mechanism to prevent inbreeding is self-incompatibility through rejection of incompatible ('self') pollen(1). In Papaver rhoeas, S proteins encoded by the stigma interact with incompatible pollen, triggering a Ca2+-dependent signalling network(2-5) resulting in pollen tube inhibition and programmed cell death(6). The cytosolic phosphoprotein p26.1, which has been identified in incompatible pollen, shows rapid, self-incompatibility-induced Ca2+-dependent hyperphosphorylation in vivo(3). Here we show that p26.1 comprises two proteins, Pr-p26.1a and Pr-p26.1b, which are soluble inorganic pyrophosphatases (sPPases). These proteins have classic Mg2+-dependent sPPase activity, which is inhibited by Ca2+, and unexpectedly can be phosphorylated in vitro. We show that phosphorylation inhibits sPPase activity, establishing a previously unknown mechanism for regulating eukaryotic sPPases. Reduced sPPase activity is predicted to result in the inhibition of many biosynthetic pathways, suggesting that there may be additional mechanisms of self-incompatibility-mediated pollen tube inhibition. We provide evidence that sPPases are required for growth and that self-incompatibility results in an increase in inorganic pyrophosphate, implying a functional role for Pr-p26.1.
Original languageEnglish
Pages (from-to)490-493
Number of pages4
Publication statusPublished - 5 Nov 2006


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