{"title":"The OsFBX388‐OsFIP1‐OsCatA module regulates ROS homeostasis and disease resistance in rice","authors":"Tiancheng Qiu, Yixin Li, Qingyuan Bai, Yapu Cheng, Kexing Fang, Yayan Feng, Mengni Yang, Vijai Bhadauria, You‐Liang Peng, Wensheng Zhao","doi":"10.1111/nph.70383","DOIUrl":null,"url":null,"abstract":"Summary<jats:list list-type=\"bullet\"> <jats:list-item>Plants are exposed to various biotic and abiotic environmental stresses, resulting in the generation of reactive oxygen species (ROS). One of the enzymes responsible for neutralizing excess ROS is catalase (CAT), which breaks down hydrogen peroxide (H<jats:sub>2</jats:sub>O<jats:sub>2</jats:sub>). However, the regulation of CAT in mediating H<jats:sub>2</jats:sub>O<jats:sub>2</jats:sub> homeostasis remains unclear.</jats:list-item> <jats:list-item>Here, we report that the DUF1644‐containing protein OsFIP1 modulates H<jats:sub>2</jats:sub>O<jats:sub>2</jats:sub> homeostasis and positively regulates rice immunity. Overexpression (OE) of <jats:italic>OsFIP1</jats:italic> leads to enhanced resistance against rice blast disease, accompanied by upregulation of defense‐related genes, enhanced chitin‐induced ROS burst and H<jats:sub>2</jats:sub>O<jats:sub>2</jats:sub> accumulation.</jats:list-item> <jats:list-item>Furthermore, OsFIP1 interacts with OsCatA. OE of <jats:italic>OsFIP1</jats:italic> dramatically reduces accumulation of OsCatA in cytoplasm. Presence of OsFIP1 reduces OsCatA's tetramerization and CAT activity. Consistently, the knockout (KN) of <jats:italic>OsCatA</jats:italic> leads to enhanced resistance to rice blast. The E3 ligase OsFBX388 interacts with and ubiquitinates OsFIP1 for degradation. KN of <jats:italic>OsFBX388</jats:italic> leads to overaccumulation of OsFIP1 and reduced CAT activity, thereby resulting in enhanced ROS burst and blast resistance.</jats:list-item> <jats:list-item>These findings highlight the crucial role of the OsFBX388‐OsFIP1‐OsCatA module in mediating ROS homeostasis and disease resistance, offering new insights into the mechanisms underlying immunity.</jats:list-item> </jats:list>","PeriodicalId":214,"journal":{"name":"New Phytologist","volume":"12 1","pages":""},"PeriodicalIF":8.3000,"publicationDate":"2025-07-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"New Phytologist","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1111/nph.70383","RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"PLANT SCIENCES","Score":null,"Total":0}
引用次数: 0
Abstract
SummaryPlants are exposed to various biotic and abiotic environmental stresses, resulting in the generation of reactive oxygen species (ROS). One of the enzymes responsible for neutralizing excess ROS is catalase (CAT), which breaks down hydrogen peroxide (H2O2). However, the regulation of CAT in mediating H2O2 homeostasis remains unclear.Here, we report that the DUF1644‐containing protein OsFIP1 modulates H2O2 homeostasis and positively regulates rice immunity. Overexpression (OE) of OsFIP1 leads to enhanced resistance against rice blast disease, accompanied by upregulation of defense‐related genes, enhanced chitin‐induced ROS burst and H2O2 accumulation.Furthermore, OsFIP1 interacts with OsCatA. OE of OsFIP1 dramatically reduces accumulation of OsCatA in cytoplasm. Presence of OsFIP1 reduces OsCatA's tetramerization and CAT activity. Consistently, the knockout (KN) of OsCatA leads to enhanced resistance to rice blast. The E3 ligase OsFBX388 interacts with and ubiquitinates OsFIP1 for degradation. KN of OsFBX388 leads to overaccumulation of OsFIP1 and reduced CAT activity, thereby resulting in enhanced ROS burst and blast resistance.These findings highlight the crucial role of the OsFBX388‐OsFIP1‐OsCatA module in mediating ROS homeostasis and disease resistance, offering new insights into the mechanisms underlying immunity.
期刊介绍:
New Phytologist is an international electronic journal published 24 times a year. It is owned by the New Phytologist Foundation, a non-profit-making charitable organization dedicated to promoting plant science. The journal publishes excellent, novel, rigorous, and timely research and scholarship in plant science and its applications. The articles cover topics in five sections: Physiology & Development, Environment, Interaction, Evolution, and Transformative Plant Biotechnology. These sections encompass intracellular processes, global environmental change, and encourage cross-disciplinary approaches. The journal recognizes the use of techniques from molecular and cell biology, functional genomics, modeling, and system-based approaches in plant science. Abstracting and Indexing Information for New Phytologist includes Academic Search, AgBiotech News & Information, Agroforestry Abstracts, Biochemistry & Biophysics Citation Index, Botanical Pesticides, CAB Abstracts®, Environment Index, Global Health, and Plant Breeding Abstracts, and others.