Wang Jiajing, Gao Yizhou, Xiong Xiaohui, Yan Yuqing, Lou Jiajun, Guo Mengmeng, Noman Muhammad, Li Dayong, Song Fengming
Key Laboratory of Crop Diseases and Insect Pests of Ministry of Agriculture and Rural Affairs, Institute of Biotechnology, College of Agriculture and Biotechnology, Zhejiang University, Hangzhou 310058, People's Republic of China; Zhejiang Provincial Key Laboratory of Biology of Crop Pathogens and Insects, Institute of Biotechnology, College of Agriculture and Biotechnology, Zhejiang University, Hangzhou 310058, People's Republic of China; State Key Laboratory of Rice Biology and Breeding, Institute of Biotechnology, College of Agriculture and Biotechnology, Zhejiang University, Hangzhou 310058, People's Republic of China.
Key Laboratory of Crop Diseases and Insect Pests of Ministry of Agriculture and Rural Affairs, Institute of Biotechnology, College of Agriculture and Biotechnology, Zhejiang University, Hangzhou 310058, People's Republic of China; Zhejiang Provincial Key Laboratory of Biology of Crop Pathogens and Insects, Institute of Biotechnology, College of Agriculture and Biotechnology, Zhejiang University, Hangzhou 310058, People's Republic of China; State Key Laboratory of Rice Biology and Breeding, Institute of Biotechnology, College of Agriculture and Biotechnology, Zhejiang University, Hangzhou 310058, People's Republic of China; School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, People's Republic of China.
Int J Biol Macromol. 2025 Feb;291:139046. doi: 10.1016/j.ijbiomac.2024.139046. Epub 2024 Dec 19.
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.
聚（ADP - 核糖）化（PARylation）由聚（ADP - 核糖）聚合酶（PARPs）催化，并由聚（ADP - 核糖）糖苷水解酶（PARG）水解，是包括植物病原真菌在内的所有真核生物中一种重要的可逆翻译后蛋白质修饰。此前，我们揭示了活性PARP——尖孢镰刀菌西瓜专化型（Fon）的FonPARP1，对西瓜枯萎病病原菌尖孢镰刀菌西瓜专化型的致病性至关重要。本研究探讨了FonPARP1在调节Fon致病性方面的酶活性和底物。FonPARP1定位于Fon大分生孢子和菌丝的细胞核中。必需的保守结构域和第729位的关键谷氨酸残基对FonPARP1的酶活性和在Fon中的致病性功能至关重要。FonPARP1与蛋白质二硫键异构酶FonPdi1相互作用，并在13个谷氨酸残基处对其进行PARylation修饰，影响其相互作用能力、PDI活性、内质网稳态和致病性功能。FonPARG1与FonPARP1和FonPdi1都相互作用，从自身PARylated的FonPARP1和FonPARP1 - PARylated的FonPdi1上水解聚（ADP - 核糖）链。这些发现强调了FonPARP1催化的PARylation在调节Fon致病性中的作用及其在植物病原真菌中的重要性。
