Global Proteomic Analysis of Lysine Succinylation in Zebrafish (<i>Danio rerio</i>)

Abstract

Lysine succinylation (Ksu) is a novel identified post-translational modification that is conserved from prokaryotes to eukaryotes. As a kind of acylation, Ksu was reported to have different functions than other acylations at lysine residues. However, recent studies on Ksu have mainly focused on plants and bacteria. Ksu studies in vertebrates are still rare; thus, the biological function of Ksu in mammals needs to be studied further. In this study, we performed global Ksu mapping in Danio rerio (zebrafish) using mass spectrometry-based proteomics with the enrichment of Ksu peptides by immunoprecipitation technology. As a result, we identified 552 Ksu sites in 164 proteins. The raw data are available via ProteomeXchange with the identifier PXD013173. Compared with our previous studies on lysine acetylation and crotonylation, Ksu plays a major role in diverse metabolic processes such as carbon metabolism and the tricarboxylic acid circle. In addition, we defined five new succinylation motifs: (su)KA, (su)KxxxxA, (su)KxxxxL, (su)KxA, and (su)KxV. In conclusion, our results provide a proteome-wide database to study Ksu in zebrafish, and our bioinformatics results facilitated the understanding of the role of Ksu in central metabolism.