Dataset Information

Proteom-wide analysis of lysine N-homocysteinylation and Hcy-induced proteom changes in Saccharomyces cerevisiae

ABSTRACT: Hyperhomocysteinemia (HHcy) inhibits growth and is cytotoxic to bacterial, yeast, and mammalian cells. The aim of this study was to determine the changes in proteome of the yeast induced by HHcy and map N-homocysteinylated sites. We identified 38 up- and 32-down-regulated proteins as well as 244 N-homocysteinylation sites in 98 proteins in Saccharomyces cerevisiae; with 57 sites in 34 proteins occurring in vivo. The bioinformatics analysis indicated that the N-homocysteinylated proteins were involved in a wide range of cellular functions with mostly cytosolic and ribosomal localizations. Furthermore, we discovered that lysine N-homocysteinylation sites are surrounded by neutral, hydrophobic and buried amino acid residues, and 60% of them occur within helix. The KEGG enrichment pathway analysis of these N-Hcy-proteins suggested that N-homocysteinylation disrupts metabolism of amino acids, ribosome biogenesis and glycolysis/gluconeogenesis. These findings suggest that protein N-homocysteinylation and dysregulation of cellular proteostasis affecting ribosomal proteins, biosynthesis of amino acids and changes in basic cellular pathways signaling are involved in the toxicity of HHcy in yeast. Homologous proteins are likely to be involved in HHcy toxicity in human and animal cells. We believe that the collection of N-homocysteinylation sites presented here is an important resource for future functional studies of N-homocysteinylation in yeast.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Equus Caballus (horse) Bos Taurus (bovine) Saccharomyces Cerevisiae (baker's Yeast) Mus Musculus (mouse)

SUBMITTER: Agata Malinowska

LAB HEAD: Michal Dadlez

PROVIDER: PXD020821 | Pride | 2021-04-08

REPOSITORIES: Pride

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			Action	DRS
	709091804perl_AJ_hpH_01.raw	Raw
	709091804perl_AJ_hpH_02.raw	Raw
	709091804perl_AJ_hpH_03.raw	Raw
	709091804perl_AJ_hpH_04.raw	Raw
	709091804perl_AJ_hpH_05.raw	Raw

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Publications

Proteome-Wide Analysis of Protein Lysine N-Homocysteinylation in Saccharomyces cerevisiae.

Perl A-Kaján Joanna J Malinowska Agata A Zimny Jarosl Aw JA Cysewski Dominik D Suszyńska-Zajczyk Joanna J Jakubowski Hieronim H

Journal of proteome research 20210402 5

Protein N-homocysteinylation by a homocysteine (Hcy) metabolite, Hcy-thiolactone, is an emerging post-translational modification (PTM) that occurs in all tested organisms and has been linked to human diseases. The yeast Saccharomyces cerevisiae is widely used as a model eukaryotic organism in biomedical research, including studies of protein PTMs. However, patterns of global protein N-homocysteinylation in yeast are not known. Here, we identified 68 in vivo and 197 <i ...[more]

PMID: 33797904

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Project description:The biology and physiology of Siberian sturgeon reproduction differ substantially from teleost fish. Seminal plasma support and protect the viability, motility and fertilizing capacity of spermatozoa by creating the optimal environment for the storage. The present study for the first time described in-depth proteomic characterization of Siberian sturgeon seminal plasma using gel based and gel-free proteomic approaches: LC-MS/MS, 2DE and 2D blue native (BN)/SDS-PAGE. LC-MS/MS allowed to identify 657 proteins, which were classified according to their functions and pathways. 2DE visualized 339 spots corresponding to 76 unique proteins (almost 60% were present in various proteoforms). For the first time we demonstrated interactions between seminal proteins; four (C1-C4) multiprotein complexes were identified after 2D BN/SDS-PAGE; composed of (C1) serotransferrin-2 (TF) and fish-egg lectin (FEL); (C2) serum albumin 2 (ALB) and retinol-binding protein 4 (RBP4); (C3) ALB and TF (C3) and (C4) apolipoprotein A-I (APOA1), riboflavin-binding protein (RfBP) and myoglobin (MB). BN-SDS-PAGE also revealed that immunoglobulin and TF formed homomultimeric (dimer, trimer, tetramer and pentamer) complexes in seminal plasma. ALB, TF, Beta-Ala-His dipeptidase, glyceraldehyde-3-phosphate dehydrogenase, IGH, APOA1, hemopexin, type-4 ice-structuring protein, FEL, RfBP and glycogen phosphorylase, liver form-like were selected as major seminal plasma proteins. The functional analysis of identified proteins indicated their involvement mainly in immune system process and response to stimulus, metabolism, vesicle-mediated transport, proteolysis, and catherin binding involved in cell-cell adhesion. Moreover, 67 proteins were associated with reproductive processes, including spermatogenesis, fertilization, acrosomal reaction and sperm motility. Comparative proteomic analysis of sturgeon seminal plasma showed common proteins with fish and human and 150 proteins specific for sturgeon which may reflect the specificity of sturgeon reproduction. To conclude, this integrative proteomic view lead to deeper insight into physiological function of seminal plasma and processes occurred in sturgeon reproductive tract.

Dataset Information

Proteom-wide analysis of lysine N-homocysteinylation and Hcy-induced proteom changes in Saccharomyces cerevisiae

Dataset's files

Publications

Proteome-Wide Analysis of Protein Lysine <i>N</i>-Homocysteinylation in <i>Saccharomyces cerevisiae</i>.

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