Proteomic Insights into Lysine-Acetylation Mediated Innate Immunity in Rice (Oryza sativa)

Lysine acetylation is a dynamic and reversible post-translational modification that plays an important role in the gene transcription regulation. Previously, we combined a highly sensitive immune-affinity purification method (used pan anti-acetyl-lysine antibody conjugated agarose for immunoaffinity acetylated peptide enrichment) with high-resolution LC–MS/MS, and generated a high quality proteome-scale data for lysine-acetylation (Kac) sites and Kac proteins in the model monocot plant rice (Oryza sativa). A total of 1337 Kac sites in 716 Kac proteins with diverse biological functions and subcellular localizations were identified in rice seedlings. In addition, protein interaction network analysis revealed that a variety of signaling pathways are modulated by protein acetylation. KEGG pathway category enrichment analysis indicated that glyoxylate and dicarboxylate metabolism, carbon metabolism, and photosynthesis pathways are significantly enriched. To further understanding of how Kac functions in biotic stress responses in rice, we performed the label-free quantitative proteomics analysis of acetylome of rice in response to fungal and bacterial pathogen-associated molecular pattern (PAMPs) chitin and flg22 treatment. Further in-depth functionally studies of chitin and flg22 induced rice Kac proteins will provide insight into the function of acetylation in regulation of plant immunity.