Mining Oomycete Proteomes for Phosphatome Leads to the Identification of Specific Expanded Phosphatases in Oomycetes

Overview

Journal Mol Plant Pathol

Specialty Molecular Biology

Date 2024 Mar 11

PMID 38462784

Authors

Min Qiu

Yaru Sun

Siqun Tu

Huaibo Li

Xin Yang

Haiyang Zhao

Maozhu Yin

Yaning Li

Wenwu Ye

Ming Wang

Yuanchao Wang

Affiliations

Soon will be listed here.

Abstract

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.

Citing Articles

Mining oomycete proteomes for phosphatome leads to the identification of specific expanded phosphatases in oomycetes.

Qiu M, Sun Y, Tu S, Li H, Yang X, Zhao H Mol Plant Pathol. 2024; 25(3):e13425.

PMID: 38462784 PMC: 10925823. DOI: 10.1111/mpp.13425.

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