Comprehensive identification of lysine 2?hydroxyisobutyrylated proteins in <i>Ustilaginoidea virens</i> reveals the involvement of lysine 2?hydroxyisobutyrylation in fungal virulence

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