Dataset Information

Succinylation proteome analysis of seedling leaves of Bd21

ABSTRACT: Protein lysine succinylation, an emerging protein post-translational modification widespread among microbiology, animals and plants, represents an important regulator of cellular processes. In our study, we took the first succinylation proteome analysis in the seedling leaves of Bd21 to draw a schematic map. With high accuracy nano LC-MS/MS combined with affinity purification, a total of 605 succinylated peptides in 323 proteins were identified and were implicated in various molecular functions and cellular biological processes. More than half (53.4%) of the proteins only have one lysine succinylated site. These identified proteins are involved in a variety of cellular functions such as amino acids transport/metabolism, post-translational modification, translation/ribosomal structure and lipid metabolism, especially energy and carbohydrate metabolism via GO, conservation analysis, protein interaction network and other bioinformatics analysis. Motif-X analysis of the succinylation sites identified fourteen significantly enriched succinylation motifs (-Ksucc-----K-, -Ksucc------G- etc) for the first time in plants and will provide possible succinylation binding locus for future studies. Secondary structure analysis showed that the succinylation sites occurred predominantly in alpha helix and coil structures which similar with acetylation. 155 (59.2%) of the homologous succinylated proteins were also identified in other three species (E. coli, S. cerevisiae and H. sapiens). 119 (45.4%) succinylated proteins and 115 (19%) sites were also to be acetylated at the same time. Our succinylated protein data set provides a promising starting point for further functional analysis of succinylation in B. distachyon, which could facilitate the elucidation of the entire metabolic network in the model monocot plant.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Brachypodium Distachyon (purple False Brome) (trachynia Distachya)

TISSUE(S): Leaf

SUBMITTER: Shoumin Zhen

LAB HEAD: Yueming Yan

PROVIDER: PXD003428 | Pride | 2018-10-26

REPOSITORIES: Pride

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Publications

First Comprehensive Proteome Analyses of Lysine Acetylation and Succinylation in Seedling Leaves of Brachypodium distachyon L.

Zhen Shoumin S Deng Xiong X Wang Jian J Zhu Gengrui G Cao Hui H Yuan Linlin L Yan Yueming Y

Scientific reports 20160812

Protein acetylation and succinylation are the most crucial protein post-translational modifications (PTMs) involved in the regulation of plant growth and development. In this study, we present the first lysine-acetylation and lysine-succinylation proteome analysis of seedling leaves in Brachypodium distachyon L (Bd). Using high accuracy nano LC-MS/MS combined with affinity purification, we identified a total of 636 lysine-acetylated sites in 353 proteins and 605 lysine-succinylated sites in 262 ...[more]

PMID: 27515067

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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.

Project description:Background Hypothyroidism is a common disease, and its molecular mechanism still needs further investigation. Succinylation, as a newly identified protein posttranslational modification, is found to be involved in various metabolisms and cellular processes. In the present study, we performed quantitative analysis of the lysine succinylome in the thyroid of rats with hypothyroxinemia. Methods Hypothyroxinemia was induced in rats through the administration of a high-fat diet and then the thyroid tissues were taken out for further analysis. Affinity enrichment and liquid chromatography-tandem mass spectrometry techniques were applied for the quantitative proteome and succinylome analyses, respectively. Bioinformatic analyses were performed to decipher the differentially expressed proteins and succinylated sites, including the gene ontology (GO) annotation-based classification, Wolfpsort-based subcellular localization prediction, Kyoto Encyclopedia of Genes and Genomes (KEGG)-based functional pathway enrichment, and conserved domains of protein and succinylation sites prediction. Finally, the mitochondrial oxygen consumption rates of human normal thyroid epithelial cells were measured to further verify the role of lysine succinylation in vitro. Results Overall, 3869 proteins were identified, among which 129 differentially expressed proteins were quantified. Downregulated expressed proteins were enriched in the thyroid hormone synthesis and thyroid hormone signaling pathways and were mainly localized to the mitochondria and ATPase complex. In addition, 685 lysine succinylation sites on 250 proteins were identified, of which 172 lysine succinylation sites on 104 proteins were obvious changed (7 upregulated on 5 proteins and 165 downregulated on 99 proteins). Decreased succinylated proteins were involved in diverse metabolic pathways and biological processes, including the tricarboxylic acid cycle (TCA cycle), cellular respiration, energy derivation by oxidation of organic compounds and aerobic respiration. Moreover, these decreased succinylated proteins were primarily localized to the mitochondria. Finally, OCRs related to basal respiration, ATP production and maximal respiration were markedly blunted in the normal thyroid epithelial cells treated with palmitic acid (all p < 0.05), and the changes were reversed when the cells were treated with palmitic acid and desuccinylase inhibitor together (all p < 0.05). Conclusions The thyroid differentially expressed proteins and changed succinylation levels played a potential role in the mitochondria-mediated energy metabolism in the HFD-induced hypothyroxinemia rat model.

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Dataset Information

Succinylation proteome analysis of seedling leaves of Bd21

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Publications

First Comprehensive Proteome Analyses of Lysine Acetylation and Succinylation in Seedling Leaves of Brachypodium distachyon L.

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