Poly(ADP-ribose) polymerase FonPARP1-catalyzed PARylation of protein disulfide isomerase FonPdi1 regulates pathogenicity of Fusarium oxysporum f. sp. niveum on watermelon
文献类型： 外文期刊
作者： Wang, Jiajing 1 ; Gao, Yizhou 1 ; Xiong, Xiaohui 1 ; Yan, Yuqing 1 ; Lou, Jiajun 1 ; Guo, Mengmeng 1 ; Noman, Muhammad 1 ; Li, Dayong 1 ; Song, Fengming 1 ;
作者机构： 1.Zhejiang Univ, Inst Biotechnol, Coll Agr & Biotechnol, Key Lab Crop Dis & Insect Pests Minist Agr & Rural, Hangzhou 310058, Peoples R China
2.Zhejiang Univ, Inst Biotechnol, Coll Agr & Biotechnol, Zhejiang Prov Key Lab Biol Crop Pathogens & Insect, Hangzhou 310058, Peoples R China
3.Zhejiang Univ, Inst Biotechnol, Coll Agr & Biotechnol, State Key Lab Rice Biol & Breeding, Hangzhou 310058, Peoples R China
4.Zhejiang Univ Sci & Technol, Sch Biol & Chem Engn, Hangzhou 310023, Peoples R China
5.Zhejiang Acad Agr Sci, Inst Plant Protect & Microbiol, State Key Lab Managing Biot & Chem Treats Qual & S, Hangzhou 310022, Peoples R China
关键词： FonPARP1; FonPdi1; PARylation; Pathogenicity; Watermelon Fusarium wilt
期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.5； 五年影响因子：8.7 ）
ISSN： 0141-8130
年卷期： 2025 年 291 卷
页码：
收录情况： SCI
摘要： Poly(ADP-ribosyl)ation (PARylation), catalyzed by poly(ADP-ribose) polymerases (PARPs) and hydrolyzed by poly(ADP-ribose) glycohydrolase (PARG), is an important reversible post-translational protein modification in all eukaryotes, including plant pathogenic fungi. Previously, we revealed that FonPARP1, an active PARP, is crucial for the pathogenicity of Fusarium oxysporum f. sp. niveum (Fon), the causative agent of watermelon Fusarium wilt. This study explores the enzymatic activity and substrates of FonPARP1 in regulating Fon pathogenicity. FonPARP1 is localized in nuclei of Fon macroconidia and hyphae. Essential conserved domains and a key glutamic acid residue at position 729 are critical for FonPARP1 enzyme activity and pathogenicity function in Fon. FonPARP1 interacts with protein disulfide isomerase FonPdi1 and PARylates it at 13 glutamic acid residues, affecting the interaction ability, PDI activity, ER homeostasis, and pathogenicity function. FonPARG1, interacting with both FonPARP1 and FonPdi1, hydrolyzes poly(ADP-ribose) chains from auto-PARylated FonPARP1 and FonPARP1-PARylated FonPdi1. These findings underscore the role of FonPARP1-catalyzed PARylation in regulating Fon pathogenicity and its significance in plant pathogenic fungi.
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