Comprehensive identification of lysine 2‐hydroxyisobutyrylated proteins in Ustilaginoidea virens reveals the involvement of lysine 2‐hydroxyisobutyrylation in fungal virulence. Issue 2 (12th February 2021)

• Record Type: Journal Article
• Authors: Chen, Xiaoyang; Li, Xiabing; Li, Pingping; Chen, Xiaolin; Liu, Hao; Huang, Junbin; Luo, Chaoxi; Hsiang, Tom; Zheng, Lu
• Other Names: Dong Suomeng guestEditor.; Lozano‐Duran Rosa guestEditor.
• Is Part Of: Journal of integrative plant biology. Volume 63:Issue 2(2021)
• Page Start: 409
• Page End: 425
• Publication Date: 2021-02-12
• Subjects: Khib -- Ustilaginoidea virens -- virulence; Plants -- Periodicals; Plants -- China -- Periodicals; Electronic journals; 580.5
• DOI: 10.1111/jipb.13066
• Languages: English
• ISSNs: 1672-9072

Abstract

Abstract: 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 Khib in the rice false smut fungus Ustilaginoidea virens, using Tandem Mass Tag (TMT)‐based quantitative proteomics approach. A total of 3 426 Khib sites were identified in 977 proteins, suggesting that Khib is a common and complex PTM in U. virens . Our data demonstrated that the 2‐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 Khib as a major post‐translational modification in U. virens and point to an important role for Khib in the virulence of this phytopathogenic fungus. Abstract : Lysine 2‐hydroxyisobutyrylation (Khib ) is a newly identified post‐translational modification (PTM) in eukaryotes. However, its function remains unknown in phytopathogenic fungi. Our findings establish Khib as a major PTM in rice false smut fungus Ustilaginoidea virens and point to an important role for Khib in fungal virulence.