Global Proteomic Analysis of Lysine Succinylation in Zebrafish (Danio rerio)

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.