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A pollen-specific calmodulin-binding protein NPG1 interacts with putative pectate lyases

机译:花粉特异性钙调蛋白结合蛋白NPG1与假定的果胶裂解酶相互作用

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摘要

Previous genetic studies have revealed that a pollen-specific calmodulin-binding protein, No Pollen Germination 1 (NPG1), is required for pollen germination. However, its mode of action is unknown. Here we report direct interaction of NPG1 with pectate lyase-like proteins (PLLs). A truncated form of AtNPG1 lacking the N-terminal tetratricopeptide repeat 1 (TPR1) failed to interact with PLLs, suggesting that it is essential for NPG1 interaction with PLLs. Localization studies with AtNPG1 fused to a fluorescent reporter driven by its native promoter revealed its presence in the cytosol and cell wall of the pollen grain and the growing pollen tube of plasmolyzed pollen. Together, our data suggest that the function of NPG1 in regulating pollen germination is mediated through its interaction with PLLs, which may modify the pollen cell wall and regulate pollen tube emergence and growth.
机译:以前的遗传研究表明,花粉萌发需要花粉特异性钙调蛋白结合蛋白,即无花粉萌发1(NPG1)。但是,其作用方式未知。在这里,我们报告NPG1与果胶裂解酶样蛋白(PLLs)的直接相互作用。缺少N端四三肽重复序列1(TPR1)的截短形式的AtNPG1无法与PLL相互作用,这表明它对于NPG1与PLL相互作用至关重要。将AtNPG1融合到由其天然启动子驱动的荧光报告基因上的本地化研究表明,它存在于花粉粒的细胞质和细胞壁中以及溶血的花粉管中不断增长的花粉管中。在一起,我们的数据表明NPG1调节花粉萌发的功能是通过与PLL相互作用介导的,这可能会修饰花粉细胞壁并调节花粉管的出现和生长。

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