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Dihydroorotase MoPyr4 is required for development, pathogenicity, and autophagy in rice blast fungus

文献类型： 外文期刊

作者： Wang, Jing-Yi 1 ; Cai, Ying-Ying 2 ; Li, Lin 2 ; Zhu, Xue-Ming 2 ; Shen, Zi-Fang 2 ; Wang, Zi-He 1 ; Liao, Jian 1 ; Lu, Jian-Ping 3 ; Liu, Xiao-Hong 1 ; Lin, Fu-Cheng 1 ;

作者机构： 1.Zhejiang Univ, Inst Biotechnol, Xianghu Lab, State Key Lab Managing Biot & Chem Treats Qual & S, Hangzhou 310058, Peoples R China

2.Zhejiang Acad Agr Sci, Inst Plant Protect & Microbiol, Xianghu Lab, State Key Lab Managing Biot & Chem Treats Qual & S, Hangzhou 310021, Peoples R China

3.Zhejiang Univ, Coll Life Sci, Hangzhou 310058, Peoples R China

关键词： Magnaporthe oryzae; Dihydroorotase; Pyrimidine nucleotide biosynthesis; Pathogenicity; Autophagy

期刊名称：CELL COMMUNICATION AND SIGNALING （ 影响因子：8.2； 五年影响因子：8.0 ）

ISSN：

年卷期： 2024 年 22 卷 1 期

页码：

收录情况： SCI

摘要： Dihydroorotase (DHOase) is the third enzyme in the six enzymatic reaction steps of the endogenous pyrimidine nucleotide de novo biosynthesis pathway, which is a metabolic pathway conserved in both bacteria and eukaryotes. However, research on the biological function of DHOase in plant pathogenic fungi is very limited. In this study, we identified and named MoPyr4, a homologous protein of Saccharomyces cerevisiae DHOase Ura4, in the rice blast fungus Magnaporthe oryzae and investigated its ability to regulate fungal growth, pathogenicity, and autophagy. Deletion of MoPYR4 led to defects in growth, conidiation, appressorium formation, the transfer and degradation of glycogen and lipid droplets, appressorium turgor accumulation, and invasive hypha expansion in M. oryzae, which eventually resulted in weakened fungal pathogenicity. Long-term replenishment of exogenous uridine-5'-phosphate (UMP) can effectively restore the phenotype and virulence of the Delta Mopyr4 mutant. Further study revealed that MoPyr4 also participated in the regulation of the Pmk1-MAPK signaling pathway, co-localized with peroxisomes for the oxidative stress response, and was involved in the regulation of the Osm1-MAPK signaling pathway in response to hyperosmotic stress. In addition, MoPyr4 interacted with MoAtg5, the core protein involved in autophagy, and positively regulated autophagic degradation. Taken together, our results suggested that MoPyr4 for UMP biosynthesis was crucial for the development and pathogenicity of M. oryzae. We also revealed that MoPyr4 played an essential role in the external stress response and pathogenic mechanism through participation in the Pmk1-MAPK signaling pathway, peroxisome-related oxidative stress response mechanism, the Osm1-MAPK signaling pathway and the autophagy pathway.

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