{"title":"Protein Phosphatases MoPtc5, MoPtc1, and MoPtc2 Contribute to the Vegetative Growth, Stress Adaptation, and Virulence of <i>Magnaporthe oryzae</i>.","authors":"Jules Biregeya, Frankline Jagero Otieno, Meilian Chen, Anjago Wilfred Mabeche, Abah Felix, Nsanzinshuti Aimable, Yakubu Saddeeq Abubakar, Osakina Aron, Guodong Lu, Zonghua Wang, Yonghe Hong, Wei Tang","doi":"10.3390/jof11030231","DOIUrl":null,"url":null,"abstract":"<p><p>Protein phosphatases are crucial enzymes that regulate key cellular processes such as the cell cycle, gene transcription, and translation in eukaryotes. Seven PP2C protein phosphatases have been identified in <i>Magnaporthe oryzae</i>. However, their synergistic roles in the pathology and physiology of <i>M. oryzae</i> remain poorly investigated. By qRT-PCR analysis, we found that PTC1 and PTC2 are significantly upregulated in the PTC5 deletion mutant. The double deletion of the <i>MoPTC5</i>/<i>MoPTC1</i> and <i>MoPTC5</i>/<i>MoPTC2</i> genes significantly reduced hyphal growth, conidiophore formation, sporulation, and virulence in <i>M. oryzae</i>. In addition, the double-knockout mutants were increasingly sensitive to different osmotic, oxidative, and cell wall stresses. Western blot analysis revealed that MoPtc5 plays a synergistic function with MoPtc1 and MoPtc2 in the regulation of MoMps1 and MoOsm1 phosphorylation levels. Lastly, appressorium formation and turgor generation were remarkably affected in the Δ<i>Moptc5</i>Δ<i>Moptc1</i> and Δ<i>Moptc5</i>Δ<i>Moptc2</i> double-deletion mutants. These findings demonstrate the overlapping roles of PP2c protein phosphatase in the fungal development and pathogenesis of <i>M. oryzae</i>.</p>","PeriodicalId":15878,"journal":{"name":"Journal of Fungi","volume":"11 3","pages":""},"PeriodicalIF":4.2000,"publicationDate":"2025-03-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11943610/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Fungi","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.3390/jof11030231","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"MICROBIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Protein phosphatases are crucial enzymes that regulate key cellular processes such as the cell cycle, gene transcription, and translation in eukaryotes. Seven PP2C protein phosphatases have been identified in Magnaporthe oryzae. However, their synergistic roles in the pathology and physiology of M. oryzae remain poorly investigated. By qRT-PCR analysis, we found that PTC1 and PTC2 are significantly upregulated in the PTC5 deletion mutant. The double deletion of the MoPTC5/MoPTC1 and MoPTC5/MoPTC2 genes significantly reduced hyphal growth, conidiophore formation, sporulation, and virulence in M. oryzae. In addition, the double-knockout mutants were increasingly sensitive to different osmotic, oxidative, and cell wall stresses. Western blot analysis revealed that MoPtc5 plays a synergistic function with MoPtc1 and MoPtc2 in the regulation of MoMps1 and MoOsm1 phosphorylation levels. Lastly, appressorium formation and turgor generation were remarkably affected in the ΔMoptc5ΔMoptc1 and ΔMoptc5ΔMoptc2 double-deletion mutants. These findings demonstrate the overlapping roles of PP2c protein phosphatase in the fungal development and pathogenesis of M. oryzae.
期刊介绍:
Journal of Fungi (ISSN 2309-608X) is an international, peer-reviewed scientific open access journal that provides an advanced forum for studies related to pathogenic fungi, fungal biology, and all other aspects of fungal research. The journal publishes reviews, regular research papers, and communications in quarterly issues. Our aim is to encourage scientists to publish their experimental and theoretical results in as much detail as possible. Therefore, there is no restriction on paper length. Full experimental details must be provided so that the results can be reproduced.