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The Ser/Thr protein kinase FonKin4-poly(ADP-ribose) polymerase FonPARP1 phosphorylation cascade is required for the pathogenicity of watermelon fusarium wilt fungus Fusarium oxysporum f. sp. niveum

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 ; Noman, Muhammad 3 ; Li, Dayong 1 ; Song, Fengming 1 ;

作者机构： 1.Zhejiang Univ, Inst Biotechnol, Zhejiang Prov Key Lab Biol Crop Pathogens & Insect, Hangzhou, Peoples R China

2.Zhejiang Univ, Inst Biotechnol, Key Lab Crop Dis & Insect Pests, Minist Agr & Rural Affairs, Hangzhou, Peoples R China

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

4.Zhejiang Univ, Inst Biotechnol, State Key Lab Rice Biol & Breeding, Hangzhou, Peoples R China

关键词： watermelon; fusarium wilt (Fusarium oxysporum f. sp. niveum); PARylation; FonPARP1; FonKin4; pathogenicity

期刊名称：FRONTIERS IN MICROBIOLOGY （ 影响因子：5.2； 五年影响因子：6.2 ）

ISSN：

年卷期： 2024 年 15 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 a kind of post-translational protein modification that is involved in various cellular processes in fungi, plants, and mammals. However, the function of PARPs in plant pathogenic fungi remains unknown. The present study investigated the roles and mechanisms of FonPARP1 in watermelon Fusarium wilt fungus Fusarium oxysporum f. sp. niveum (Fon). Fon has a single PARP FonPARP1 and one PARG FonPARG1. FonPARP1 is an active PARP and contributes to Fon pathogenicity through regulating its invasive growth within watermelon plants, while FonPARG1 is not required for Fon pathogenicity. A serine/threonine protein kinase, FonKin4, was identified as a FonPARP1-interacting partner by LC-MS/MS. FonKin4 is required for vegetative growth, conidiation, macroconidia morphology, abiotic stress response and pathogenicity of Fon. The S_TKc domain is sufficient for both enzyme activity and pathogenicity function of FonKin4 in Fon. FonKin4 phosphorylates FonPARP1 in vitro to enhance its poly(ADP-ribose) polymerase activity; however, FonPARP1 does not PARylate FonKin4. These results establish the FonKin4-FonPARP1 phosphorylation cascade that positively contributes to Fon pathogenicity. The present study highlights the importance of PARP-catalyzed protein PARylation in regulating the pathogenicity of Fon and other plant pathogenic fungi.

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