The F-box protein OsFBX156 positively regulates rice defence against the blast fungus Magnaporthe oryzae by mediating ubiquitination-dependent degradation of OsHSP71.1
文献类型： 外文期刊
作者： Zhao, Yudan 1 ; Zhong, Xionghui 2 ; Xu, Guojuan 1 ; Zhu, Xiaoying 1 ; Shi, Yanlong 1 ; Liu, Minghao 3 ; Wang, Ruyi 1 ; Kang, Houxiang 1 ; You, Xiaoman 1 ; Ning, Yuese 1 ; Wang, Guo-Liang 4 ; Wang, Xuli 1 ;
作者机构： 1.Chinese Acad Agr Sci, Inst Plant Protect, State Key Lab Biol Plant Dis & Insect Pests, Beijing 100193, Peoples R China
2.Beijing Acad Agr & Forestry Sci, Beijing Vegetable Res Ctr, Minist Agr, Key Lab Biol & Genet Improvement Hort Crops North, Beijing, Peoples R China
3.Chinese Acad Agr Sci, Shenzhen Branch, Agr Genom Inst Shenzhen, Minist Agr & Rural Affairs,Guangdong Lab Lingnan M, Shenzhen, Peoples R China
4.Ohio State Univ, Dept Plant Pathol, Columbus, OH USA
关键词： 26S proteasome pathway; F-box protein; heat shock protein; Magnaporthe oryzae; Oryza sativa; reactive oxygen species; rice blast
期刊名称：MOLECULAR PLANT PATHOLOGY （ 影响因子：4.9； 五年影响因子：5.9 ）
ISSN： 1464-6722
年卷期： 2024 年 25 卷 6 期
页码：
收录情况： SCI
摘要： F-box protein is a subunit of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex, which plays a critical role in regulating different pathways in plant immunity. In this study, we identified the rice (Oryza sativa) F-box protein OsFBX156, which targets the heat shock protein 70 (OsHSP71.1) to regulate resistance to the rice blast fungus Magnaporthe oryzae. Overexpression of OsFBX156 or knockout of OsHSP71.1 in rice resulted in the elevation of pathogenesis-related (PR) genes and an induction burst of reactive oxygen species (ROS) after flg22 and chitin treatments, thereby enhancing resistance to M. oryzae. Furthermore, OsFBX156 can promote the degradation of OsHSP71.1 through the 26S proteasome pathway. This study sheds lights on a novel mechanism wherein the F-box protein OsFBX156 targets OsHSP71.1 for degradation to promote ROS production and PR gene expression, thereby positively regulating rice innate immunity.
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