Self-incompatibility in Papaver targets soluble inorganic pyrophosphatases in pollen

Self-incompatibility in Papaver targets soluble inorganic pyrophosphatases in pollen
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DOI:
10.1038/nature05311
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发表时间:
2006-11-23
期刊:
影响因子:
64.8
通讯作者:
Franklin-Tong, Vernonica E.
Franklin-Tong, Vernonica E.
中科院分区:
综合性期刊1区
文献类型:
--
作者:
de Graaf, Barend H. J.;Rudd, Jason J.;Franklin-Tong, Vernonica E.

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在高等植物中,有性生殖涉及花粉和雌蕊之间的相互作用。防止近亲繁殖的一个关键机制是通过排斥不相容(“自我”)花粉的自交不亲和性(1)。在虞美人中,柱头编码的S蛋白与不亲和的花粉相互作用,触发Ca 2+依赖性信号网络(2-5),导致花粉管抑制和程序性细胞死亡(6)。在不亲和花粉中鉴定的胞质磷蛋白p26.1在体内表现出快速的、自交不亲和诱导的Ca 2+依赖性过度磷酸化(3)。在这里,我们发现p26. 1包含两个蛋白质,Pr-p26.1a和Pr-p26.1b,这是可溶性无机焦磷酸酶(sPPases)。这些蛋白质具有经典的Mg 2+依赖性sPP酶活性,其被Ca 2+抑制,并且出乎意料地可以在体外磷酸化。我们发现,磷酸化抑制sPPase活性,建立一个以前未知的机制,调节真核sPPases。降低sPPase活性的预测,导致许多生物合成途径的抑制,这表明可能有其他机制的自交不亲和介导的花粉管抑制。我们提供的证据表明,spPPases是生长所必需的,自交不亲和性导致无机焦磷酸盐的增加,这意味着Pr-p26.1的功能作用。
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.