Phosphatases are important regulators of protein phosphorylation and various cellular processes, and they serve as counterparts to kinases. In this study, our comprehensive analysis of oomycete complete proteomes unveiled the presence of approximately 3833 phosphatases, with most species estimated to have between 100 and 300 putative phosphatases. Further investigation of these phosphatases revealed a significant increase in protein serine/threonine phosphatases (PSP) within oomycetes. In particular, we extensively studied the metallo‐dependent protein phosphatase (PPM) within the PSP family in the model oomycete Phytophthora sojae. Our results showed notable differences in the expression patterns of PPMs throughout 10 life stages of P. sojae, indicating their vital roles in various stages of oomycete pathogens. Moreover, we identified 29 PPMs in P. sojae, and eight of them possessed accessory domains in addition to phosphate domains. We investigated the biological function of one PPM protein with an extra PH domain (PPM1); this protein exhibited high expression levels in both asexual developmental and infectious stages. Our analysis confirmed that PPM1 is indeed an active protein phosphatase, and its accessory domain does not affect its phosphatase activity. To delve further into its function, we generated knockout mutants of PPM1 and validated its essential roles in mycelial growth, sporangia and oospore production, as well as infectious stages. To the best of our knowledge, this study provides the first comprehensive inventory of phosphatases in oomycetes and identifies an important phosphatase within the expanded serine/threonine phosphatase group in oomycetes.

中文翻译：

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挖掘卵菌蛋白质组的磷酸组可鉴定卵菌中特定的扩展磷酸酶

磷酸酶是蛋白质磷酸化和各种细胞过程的重要调节剂，它们是激酶的对应物。在这项研究中，我们对卵菌完整蛋白质组的综合分析揭示了大约 3833 种磷酸酶的存在，大多数物种估计具有 100 到 300 种假定的磷酸酶。对这些磷酸酶的进一步研究表明，卵菌内蛋白质丝氨酸/苏氨酸磷酸酶（PSP）显着增加。特别是，我们在卵菌模型中广泛研究了 PSP 家族中的金属依赖性蛋白磷酸酶 (PPM)大豆疫霉。我们的结果显示，在 10 个生命阶段，PPM 的表达模式存在显着差异。酱油，表明它们在卵菌病原体的各个阶段中的重要作用。此外，我们还确定了 29 个 PPM酱油，其中八个除了磷酸盐结构域外还具有辅助结构域。我们研究了一种带有额外 PH 结构域的 PPM 蛋白 (PPM1) 的生物学功能；该蛋白在无性发育和感染阶段均表现出高表达水平。我们的分析证实PPM1确实是一种活性蛋白磷酸酶，其辅助结构域不影响其磷酸酶活性。为了进一步深入研究其功能，我们生成了 PPM1 的敲除突变体，并验证了其在菌丝生长、孢子囊和卵孢子产生以及感染阶段的重要作用。据我们所知，这项研究提供了卵菌中磷酸酶的第一个全面清单，并鉴定了卵菌中扩展的丝氨酸/苏氨酸磷酸酶组中的重要磷酸酶。