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Self-incompatibility in Papaver targets soluble inorganic pyrophosphatases in pollen

De Graaf, Barend H. J., Rudd, Jason J., Wheeler, M. J., Perry, R. M., Bell, E. M., Osman, K., Franklin, F. C. H. and Franklin-Tong, V. E. 2006. Self-incompatibility in Papaver targets soluble inorganic pyrophosphatases in pollen. Nature 444 , pp. 490-493. 10.1038/nature05311

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Abstract

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') pollen1. In Papaver rhoeas, S proteins encoded by the stigma interact with incompatible pollen, triggering a Ca2+-dependent signalling network2, 3, 4, 5 resulting in pollen tube inhibition and programmed cell death6. The cytosolic phosphoprotein p26.1, which has been identified in incompatible pollen, shows rapid, self-incompatibility-induced Ca2+-dependent hyperphosphorylation in vivo3. 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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Publisher: Nature Publishing Group
ISSN: 0028-0836
Last Modified: 04 Jun 2017 06:30
URI: http://orca.cf.ac.uk/id/eprint/61165

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