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Self-incompatibility in Papaver targets soluble inorganic pyrophosphatases in pollen.

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Title: Self-incompatibility in Papaver targets soluble inorganic pyrophosphatases in pollen.
Authors: de Graaf, Barend H. J., Rudd, Jason J., Wheeler, Michael J., Perry, Ruth M., Bell, Elizabeth M., Osman, Kim, Franklin, F. Christopher H., Franklin-Tong, Vernonica E.
Source: Nature. 11/23/2006, Vol. 444 Issue 7118, p490-493. 4p. 5 Black and White Photographs, 4 Graphs.
Subjects: Pollen, Phosphatases, Papaver, Proteins, Calcium ions, Phosphoproteins, Cell death
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’) pollen. In Papaver rhoeas, S proteins encoded by the stigma interact with incompatible pollen, triggering a Ca2+-dependent signalling network resulting in pollen tube inhibition and programmed cell death. The cytosolic phosphoprotein p26.1, which has been identified in incompatible pollen, shows rapid, self-incompatibility-induced Ca2+-dependent hyperphosphorylation in vivo. 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. [ABSTRACT FROM AUTHOR]
Copyright of Nature is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Psychology and Behavioral Sciences Collection
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  Data: Self-incompatibility in Papaver targets soluble inorganic pyrophosphatases in pollen.
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  Data: <searchLink fieldCode="JN" term="%22Nature%22">Nature</searchLink>. 11/23/2006, Vol. 444 Issue 7118, p490-493. 4p. 5 Black and White Photographs, 4 Graphs.
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  Data: <searchLink fieldCode="DE" term="%22Pollen%22">Pollen</searchLink><br /><searchLink fieldCode="DE" term="%22Phosphatases%22">Phosphatases</searchLink><br /><searchLink fieldCode="DE" term="%22Papaver%22">Papaver</searchLink><br /><searchLink fieldCode="DE" term="%22Proteins%22">Proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Calcium+ions%22">Calcium ions</searchLink><br /><searchLink fieldCode="DE" term="%22Phosphoproteins%22">Phosphoproteins</searchLink><br /><searchLink fieldCode="DE" term="%22Cell+death%22">Cell death</searchLink>
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  Data: 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. In Papaver rhoeas, S proteins encoded by the stigma interact with incompatible pollen, triggering a Ca2+-dependent signalling network resulting in pollen tube inhibition and programmed cell death. The cytosolic phosphoprotein p26.1, which has been identified in incompatible pollen, shows rapid, self-incompatibility-induced Ca2+-dependent hyperphosphorylation in vivo. 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. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Nature is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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              Text: 11/23/2006
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