Proteome-wide and lysine crotonylation profiling reveals the importance of crotonylation in chrysanthemum (Dendranthema grandiforum) under low-temperature

Abstract Background Low-temperature severely affects the growth and development of chrysanthemum which is one kind ornamental plant well-known widely used in world. Lysine crotonylation a recently identified post-translational modification (PTM) with multiple cellular functions. However, lysine under low-temperature stress has not been studied. Results Proteome-wide at was analyzed using TMT (Tandem Mass Tag) labeling, sensitive immuno-precipitation, high-resolution LC-MS/MS. The results showed that 2017 sites were 1199 proteins. Treatment 4 °C for 24 h − resulted 393 upregulated proteins 500 downregulated (1.2-fold threshold P < 0.05). Analysis biological information involved photosynthesis, ribosomes, antioxidant systems. crotonylated motifs compared other plants to obtain orthologous conserved motifs. To further understand how K136 affected APX (ascorbate peroxidase), we performed site-directed mutation APX. Site-directed decrotonylation reduced activity, complete increased activity. Conclusion In summary, our study comparatively proteome-wide provided insights into mechanisms positively regulated activity reduce oxidative damage caused by stress. These data an important basis studying regulate enzyme response new research ideas chilling-tolerance freezing-tolerance molecular breeding.