Dataset Information

Yeast mitochondrial succinylome: Implications for mitochondrial DNA maintenance

ABSTRACT: Together with other post-translational modifications, acylation of proteins is a powerful means of regulation of their activity. Some acylation types occur nonenzymatically and are driven by an increase in the concentration of acyl group donors. Lysine succinylation has a profound effect on the corresponding site within the protein as it changes the charge of the residue. In eukaryotes it predominantly affects mitochondrial proteins because the donor of succinate, succinyl-coenzyme A, is primarily generated in the tricarboxylic acid (TCA) cycle. Although numerous succinylated mitochondrial proteins were identified in Saccharomyces cerevisiae, a detailed characterization of yeast mitochondrial succinylome is lacking. Here we performed a proteomic mass spectrometry analysis of purified yeast mitochondria and detected 313 succinylated mitochondrial proteins with 1762 novel succinylation sites.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Peter Barath

LAB HEAD: Peter Barath

PROVIDER: PXD023604 | Pride | 2021-10-26

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	190904_WT_01_z_300ug_01.raw	Raw
	190904_WT_01_z_300ug_02.raw	Raw
	190904_WT_01_z_300ug_03.raw	Raw
	190904_dLsc_00_z_300ug_01.raw	Raw
	190904_dLsc_00_z_300ug_02.raw	Raw

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Publications

The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids.

Frankovsky Jan J Keresztesová Barbora B Bellová Jana J Kunová Nina N Čanigová Nikola N Hanakova Katerina K Bauer Jacob A JA Ondrovičová Gabriela G Lukáčová Veronika V Siváková Barbara B Zdrahal Zbynek Z Pevala Vladimír V Procházková Katarína K Nosek Jozef J Baráth Peter P Kutejova Eva E Tomaska Lubomir L

The Journal of biological chemistry 20210901 4

Acylation modifications, such as the succinylation of lysine, are post-translational modifications and a powerful means of regulating protein activity. Some acylations occur nonenzymatically, driven by an increase in the concentration of acyl group donors. Lysine succinylation has a profound effect on the corresponding site within the protein, as it dramatically changes the charge of the residue. In eukaryotes, it predominantly affects mitochondrial proteins because the donor of succinate, succi ...[more]

PMID: 34480900

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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.