Comprehensive identification of lysine 2-hydroxyisobutyrylated proteins in Ustilaginoidea virens reveals the involvement of lysine 2-hydroxyisobutyrylation in fungal virulence

作     者：Xiaoyang Chen Xiabing Li Pingping Li Xiaolin Chen Hao Liu Junbin Huang Chaoxi Luo Tom Hsiang Lu Zheng Xiaoyang Chen;Xiabing Li;Pingping Li;Xiaolin Chen;Hao Liu;Junbin Huang;Chaoxi Luo;Tom Hsiang;Lu Zheng

作者机构：Hubei Key Laboratory of Plant PathologyHuazhong Agricultural UniversityWuhan 430070China School of Environmental SciencesUniversity of GuelphGuelphOntarioN1G 2W1Canada 

出 版 物：《Journal of Integrative Plant Biology》 (植物学报（英文版）)

年 卷 期：2021年第63卷第2期

页      面：409-425页

核心收录：

学科分类：09[农学] 0904[农学-植物保护] 090401[农学-植物病理学] 

基　　金：supported by the National Natural Science Foundation of China (32072371) the National Key Research and Development Program (2016YFD0300700, 2017YFD0301400) the Fundamental Research Funds for the Central Universities of China (2662018JC051) 

主　　题：Khib Ustilaginoidea virens virulence 

摘      要：Lysine 2-hydroxyisobutyrylation(Khib) is a newly identified post-translational modification(PTM) that plays important roles in transcription and cell proliferation in eukaryotes. However, its function remains unknown in phytopathogenic fungi. Here,we performed a comprehensive assessment of Khibin the rice false smut fungus Ustilaginoidea virens, using Tandem Mass Tag(TMT)-based quantitative proteomics approach. A total of 3 426 Khibsites were identified in 977 proteins, sugg esting that Khibis a common and complex PTM in U. virens. Our data demonstrated that the2-hydroxyisobutyrylated proteins are involved in diverse biological processes. Network analysis of the modified proteins revealed a highly interconnected protein network that included many well-studied virulence factors. We confirmed that the Zn-binding reduced potassium dependency3-type histone deacetylase(UvRpd3) is a major enzyme that removes 2-hydroxyisobutyrylation and acetylation in U. virens. Notably, mutations of Khib sites in the mitogen-activated protein kinase(MAPK)UvSlt2 significantly reduced fungal virulence and decreased the enzymatic activity of UvSlt2. Molecular dynamics simulations demonstrated that 2-hydroxyisobutyrylation in UvSlt2 increased the hydrophobic solvent-accessible surface area and thereby affected binding between the UvSlt2 enzyme and its substrates. Our findings thus establish Khibas a major post-translational modification in U. virens and point to an important role for Khibin the virulence of this phytopathogenic fungus.