J Integr Plant Biol. ›› 2021, Vol. 63 ›› Issue (2): 409-425.DOI: 10.1111/jipb.13066

Special Issue: Plant-biotic interaction Protein kinases

• Research Articles • Previous Articles    

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

Xiaoyang Chen1, Xiabing Li1, Pingping Li1, Xiaolin Chen1, Hao Liu1, Junbin Huang1, Chaoxi Luo1, Tom Hsiang2 and Lu Zheng1*   

  1. 1Hubei Key Laboratory of Plant Pathology, Huazhong Agricultural University, Wuhan 430070, China
    2School of Environmental Sciences, University of Guelph, Guelph, Ontario, N1G 2W1, Canada

    *Correspondence: Lu Zheng (luzheng@mail.hzau.edu.cn)
  • Received:2020-12-14 Accepted:2021-01-07 Online:2021-01-11 Published:2021-02-01

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.

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