Dataset Information

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

ABSTRACT: Lysine succinylation (Ksu) is a novel identified post-translational modification that conserved from prokaryote to eukaryotes. As a kind of acylation, Ksu was reported to have different functions with others acylation at lysine residue. However, recently studies on the Ksu mainly focus on the plants and bacterial, there are still very rare studies in the vertebrate. Therefore, the biological role of succinylation remains largely unknown in mammal. In this study, we performed global Ksu mapping in Danio rerio (zebrafish) using mass spectrometry-based proteomics with enrichment of Ksu peptides by immunoprecipitation technology. As a result, we totally identified 552 Ksu sites in 164 proteins. Compared with our previous studies on lysine acetylation and crotonylation, Ksu plays a major role in a diverse metabolic process, such as carbon metabolism and tricarboxylic acid circle. In addition, we defined 5 new succinylation motifs: (su)KA, (suc)KxxxxA, (su)KxxxxL, (su)KxA, (su)KxV. In conclusion, our result provides proteome-wide database for study of Ksu in zebrafish and our bioinformatics result facilitated the understanding of the Ksu in the role of central metabolism.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Danio Rerio (zebrafish) (brachydanio Rerio)

TISSUE(S): Embryo

SUBMITTER: Yan Gao

LAB HEAD: Sangkyu Lee

PROVIDER: PXD013173 | Pride | 2019-09-09

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	20180321_Zebrafish-5D_Ksucc_2hr_0-6-23_1.raw	Raw
	20180321_Zebrafish-5D_Ksucc_2hr_0-6-23_3.raw	Raw
	20180323_zebrafish_5D_Ksucc_2hr_0-6-23_2.raw	Raw
	20180405_zebrafish_5D_Ksucc_2hr_0-6-23_4.raw	Raw
	Supplementltables1.xml	Xml

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Publications

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

Gao Yan Y Lee Hyojin H Kwon Oh Kwang OK Tan Minjia M Kim Ki-Tae KT Lee Sangkyu S

Journal of proteome research 20190916 10

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 <i>Danio reri ...[more]

PMID: 31483678

Similar Datasets

Project description:Background: Lysine succinylation is a newly identified PTM, which exists widely from prokaryotes to eukaryotes and participates in various cellular processes, especially in the metabolic processes. Staphylococcus epidermidis is a commensal bacterium in the skin, which attracts more attention as a pathogen, especially in immunocompromised patients and neonates by attaching to medical devices and forming biofilms. However, the significance of lysine succinylation in proteins of Staphylococcus epidermidis has not been investigated. Materials and methods: Using antibody affinity enrichment followed by LC-MS/MS analysis, we examined the succinylome of Staphylococcus epidermidis (ATCC®12228™). Then, bioinformatics analysis was performed, including Gene Ontology, KEGG enrichment, motif characterization, secondary structure, protein-protein interaction, and BLAST analysis. Results: A total of 1557 succinylated lysine sites in 649 proteins were identified in Staphylococcus epidermidis (ATCC 12228). Among these succinylation proteins, GO annotation showed that proteins related to metabolic processes and binding activity accounted for the most based on the analysis of biological process and molecular function, respectively. KEGG pathway characterization indicated that proteins associated with the glycolysis/ gluconeogenesis, and citrate cycle (TCA cycle) pathway were more likely to be succinylated. Moreover, 13 conserved motifs were identified. The specific motif KsuD was conserved in model prokaryotes and eukaryotes. Succinylated proteins with this motif were highly enriched in the glycolysis/gluconeogenesis pathway. One succinylation site(K144) was identified in S-ribosylhomocysteine lyase, a key enzyme in the quorum sensing system, indicating the regulatory role succinylation may play in bacterial processes. Furthermore, 15 succinyltransferases and 18 desuccinylases(erasers) were predicted in S.epidermidis by BLAST analysis. Conclusions: We performed the first comprehensive profile of succinylation in Staphylococcus epidermidis and illustrated the significant role succinylation may play in energy metabolism, QS system, and other bacterial behaviors. This study may be a fundamental basis to investigate the underlying mechanisms of colonization, virulence, and infection of S. epidermidis, as well as provide a new insight into regulatory effects succinylation may lay on metabolic processes.