Proteome-Wide Analysis of Lysine 2-Hydroxyisobutyrylated Proteins in .

Protein lysine 2-hydroxyisobutyrylation (K ), a new type of post-translational modification, occurs in histones and non-histone proteins and plays an important role in almost all aspects of both eukaryotic and prokaryotic living cells. , a soil-borne fungal pathogen, can cause disease in more than 150 plants. However, little is currently known about the functions of K in this plant pathogenic fungus. Here, we report a systematic analysis of 2-hydroxyisobutyrylated proteins in . In this study, 3782 K sites in 1299 proteins were identified in . The bioinformatics analysis showed that 2-hydroxyisobutyrylated proteins are involved in different biological processes and functions and are located in diverse subcellular localizations. The enrichment analysis revealed that K participates in a variety of pathways, including the ribosome, oxidative phosphorylation, and proteasome pathways. The protein interaction network analysis showed that 2-hydroxyisobutyrylated protein complexes are involved in diverse interactions. Notably, several 2-hydroxyisobutyrylated proteins, including three kinds of protein kinases, were involved in the virulence or conidiation of , suggesting that K plays regulatory roles in pathogenesis. Moreover, our study shows that there are different K levels of in conidial and mycelial stages. These findings provide evidence of K in , an important filamentous plant pathogenic fungus, and serve as a resource for further exploration of the potential functions of K in species and other filamentous pathogenic fungi.