First analyses of lysine succinylation proteome and overlap between succinylation and acetylation in Solenopsis invicta Buren (Hymenoptera: Formicidae)

Jingwen Ye,Jun Li

doi:10.1186/s12864-021-08285-8

Jingwen Ye, Jun Li

Open Access

https://doi.org/10.1186/s12864-021-08285-8

Copy DOI

Journal: BMC Genomics	Publication Date: Jan 17, 2022
Citations: 3	License type: open-access

Affiliation: Institute of Zoology, Guangdong Academy of Sciences

Abstract

BackgroundLysine succinylation (Ksu) exists in both eukaryotes and prokaryotes, and influences a variety of metabolism processes. However, little attention has been paid to Ksu in insects, especially the notorious invasive pest Solenopsis invicta.ResultsIn this study, the first analyses of Ksu proteome and overlap between Ksu and lysine acetylation (Kac) in S. invicta were presented. 3753 succinylated sites in 893 succinylated proteins were tested. The dihydrolipoyl dehydrogenase, V-type proton ATPase subunit G, and tubulin alpha chain all had evolutionary conservatism among diverse ant or bee species. Immunoblotting validation showed that there were many Ksu protein bands with a wide range of molecular mass. In addition, 1230 sites in 439 proteins were highly overlapped between Ksu and Kac. 54.05% of Ksu proteins in cytoplasm were acetylated. The results demonstrated that Ksu may play a vital part in the allergization, redox metabolism, sugar, fat, and protein metabolism, energy production, immune response, and biosynthesis of various secondary metabolites.ConclusionsKsu and Kac were two ubiquitous protein post-translational modifications participated in a variety of biological processes. Our results may supply rich resources and a starting point for the molecular basic research of regulation on metabolic pathways and other biological processes by succinylation and acetylation.

Highlights

Lysine succinylation (Ksu) exists in both eukaryotes and prokaryotes, and influences a variety of metabolism processes
The comprehensive succinylome was first reported in the traditional Chinese medicine herb Pogostemon cablin (Blanco) Benth, which broadened the range of Ksu in plants [7]
Gene ontology (GO) classification and subcellular distribution of succinylated proteins In order to understand the possible roles of Ksu, GO classification of the identified proteins was conducted

Summary

Introduction

Lysine succinylation (Ksu) exists in both eukaryotes and prokaryotes, and influences a variety of metabolism processes. Lysine residues can be modified by a large number of post-translational protein acylation modifications, namely, succinylation, acetylation, β-hydroxybutyrylation, 2-hydroxyisobutyrylation, and biotinylation [1]. Protein sucinylome, whose aim was to determine the comprehensive Ksu sites at the proteomic level, was carried out in plants, microorganisms, and animals [6]. The proteomes of Ksu and Kac were analyzed, and these two modifications were widely involved in the metabolism of the seed embryos of germinating rice Oryza sativa [6]. Zhen et al [10] firstly analyzed the proteomes of Ksu and Kac in the seedling leaves of Brachypodium distachyon L, and showed that Ksu and Kac could be used as switches to control the activities of some key enzymes and ensure the proper developmental function of B. distachyon accession 21. The first succinyl and acetyl groups of Pseudomonas aeruginosa PA14, which were cultured at the exits of four diverse carbon sources, were presented [11]

Methods

Results

Conclusion