通过挖掘卵菌蛋白质组中的磷酸酶组,发现了卵菌中特异的扩增磷酸酶。

IF 4.8 1区 农林科学 Q1 PLANT SCIENCES
Min Qiu, Yaru Sun, Siqun Tu, Huaibo Li, Xin Yang, Haiyang Zhao, Maozhu Yin, Yaning Li, Wenwu Ye, Ming Wang, Yuanchao Wang
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引用次数: 0

摘要

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 oomycete 完整蛋白质组的全面分析揭示了大约 3833 种磷酸酶的存在,大多数物种估计有 100 到 300 种推定磷酸酶。对这些磷酸酶的进一步研究发现,卵菌中的蛋白丝氨酸/苏氨酸磷酸酶(PSP)显著增加。特别是,我们广泛研究了模式真菌 Phytophthora sojae 中 PSP 家族中的金属依赖性蛋白磷酸酶(PPM)。我们的研究结果表明,PPMs 在 P. sojae 的 10 个生命阶段中的表达模式存在显著差异,这表明它们在卵菌病原体的各个阶段都发挥着重要作用。此外,我们在 P. sojae 中发现了 29 个 PPMs,其中 8 个除了磷酸结构域外还具有附属结构域。我们研究了一个具有额外 PH 结构域的 PPM 蛋白(PPM1)的生物学功能;该蛋白在无性发育阶段和感染阶段都表现出较高的表达水平。我们的分析证实,PPM1 确实是一种活性蛋白磷酸酶,其附属结构域不会影响其磷酸酶活性。为了进一步研究其功能,我们生成了 PPM1 的基因敲除突变体,并验证了它在菌丝生长、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,这项研究首次全面盘点了卵菌中的磷酸酶,并在卵菌中的丝氨酸/苏氨酸磷酸酶群中发现了一种重要的磷酸酶。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Mining oomycete proteomes for phosphatome leads to the identification of specific expanded phosphatases in oomycetes.

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.

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来源期刊
Molecular plant pathology
Molecular plant pathology 生物-植物科学
CiteScore
9.40
自引率
4.10%
发文量
120
审稿时长
6-12 weeks
期刊介绍: Molecular Plant Pathology is now an open access journal. Authors pay an article processing charge to publish in the journal and all articles will be freely available to anyone. BSPP members will be granted a 20% discount on article charges. The Editorial focus and policy of the journal has not be changed and the editorial team will continue to apply the same rigorous standards of peer review and acceptance criteria.
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