Succinyl-proteome profiling of Dendrobium officinale, an important traditional Chinese orchid herb, revealed involvement of succinylation in the glycolysis pathway

BMC Genomics. 2017 Aug 10;18(1):598. doi: 10.1186/s12864-017-3978-x. Feng S1,2, Jiao K1,2, Guo H1,2, Jiang M1,2, Hao J1,2, Wang H3,4, Shen C5,6. Author information 1 College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, 310036, China. 2 Zhejiang Provincial Key Laboratory for Genetic Improvement and Quality Control of Medicinal Plants, Hangzhou Normal University, Hangzhou, 310036, China. 3 College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, 310036, China. whz62@163.com. 4 Zhejiang Provincial Key Laboratory for Genetic Improvement and Quality Control of Medicinal Plants, Hangzhou Normal University, Hangzhou, 310036, China. whz62@163.com. 5 College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, 310036, China. shencj@hznu.edu.cn. 6 Zhejiang Provincial Key Laboratory for Genetic Improvement and Quality Control of Medicinal Plants, Hangzhou Normal University, Hangzhou, 310036, China. shencj@hznu.edu.cn. Abstract BACKGROUND: Lysine succinylation is a ubiquitous and important protein post-translational modification in various eukaryotic and prokaryotic cells. However, its functions in Dendrobium officinale, an important traditional Chinese orchid herb with high polysaccharide contents, are largely unknown. RESULTS: In our study, LC-MS/MS was used to identify the peptides that were enriched by immune-purification with a high-efficiency succinyl-lysine antibody. In total, 314 lysine succinylation sites in 207 proteins were identified. A gene ontology analysis showed that these proteins are associated with a wide range of cellular functions, from metabolic processes to stimuli responses. Moreover, two types of conserved succinylation motifs, '***Ksuc******K**' and '****EKsuc***', were identified. Our data showed that lysine succinylation occurred on five key enzymes in the glycolysis pathway. The numbers of average succinylation sites on these five enzymes in plants were lower than those in bacteria and mammals. Interestingly, two active site amino acids residues, K103 and K225, could be succinylated in fructose-bisphosphate aldolase, indicating a potential function of lysine succinylation in the regulation of glycolytic enzyme activities. Furthermore, the protein-protein interaction network for the succinylated proteins showed that several functional terms, such as glycolysis, TCA cycle, oxidative phosphorylation and ribosome, are consisted. CONCLUSIONS: Our results provide the first comprehensive view of the succinylome of D. officinale and may accelerate future biological investigations of succinylation in the synthesis of polysaccharides, which are major active ingredients. KEYWORDS: D. officinale; Glycolysis pathway; LC-MS/MS; Metabolic pathway; Succinylation PMID: 28797234 PMCID: PMC5553593 DOI: 10.1186/s12864-017-3978-x Free PMC Article