Project description:Lysine acetylation and succinylation are post-translational modifications of proteins, and have been shown to play roles in plant response to pathogen infection. Phytoplasma infection can directly alter multiple metabolic processes in Paulownia and lead to Paulownia witches’ broom (PaWB), the major cause of Paulownia mortality worldwide. To explore the extent and function of lysine acylations during phytoplasma infection, we investigated global proteome, acetylome, and succinylome of phytoplasma-infected Paulownia tomentosa seedlings. In total, we globally yield 8963 proteins, 2893 acetylated, and 1271 succinylated proteins. Among them, 425 substrates were simultaneously acetylated and succinylated. Comparative analysis revealed that 276 proteins, 546 acetylated proteins and 5 succinylated proteins were associated with PaWB. Our results suggested that acetylation may be more important than succinylation in response to phytoplasma infection. Enzymatic assays showed that acetylation modified the activities of protochlorophyllide reductase and RuBisCO in phytoplasma-infected seedlings. On the basis of these results, a model to elucidate the molecular mechanism responses to PaWB was proposed and this research offer a resource for functional studies on the effects of acetylation on protein function.
