Comprehensive analysis of lysine acetylation reveals the function of acetylated protein in the synthesis of Eu-rubber in Eucommia ulmoides Oliver leaves

Lysine acetylation (Kac), a highly direct and dy-namic post-translational modification, plays an im-portant regulatory role throughout the growth and development of plants during their entire lifecycle. Eucommia ulmoides is a prized and rare Chinese me-dicinal material. This plant also has practical value since it is the source of Eu-rubber. However, the syn-thetic process is complicated. Thus, the effects of Kac on the production of Eu-rubber in E. ulmoides remain unclear. Here, we adopted a new perspective by an-alyzing the proteins upstream and downstream of those used in the biosynthesis of Eu-rubber for their acetylation using proteomics. A total of 4,511 lysine modification sites in 2,115 proteins were found that were involved in metabolic and biosynthetic pro-cesses. Interestingly, 10 enzymes of the biosynthetic pathway of isopentenyl pyrophosphate (IPP), the pre-cursor of Eu-rubber biosynthesis, were acetylated. Secondly, four enzymes related to Eu-rubber biosyn-thesis were found to be acetylated. An analysis of the acetylation process indicated that the acetylation of lysine has an important regulatory effect on this pro-cess. In addition, a PPI analysis showed that various interactions were regulated by protein acetylation. In this study, we tested the acetylated group of proteins in the leaves of E. ulmoides, which provides an import-ant theoretical basis to explore the effects of lysine acetylation on Eu-rubber production in much greater detajl.