Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

S-glutathionylation proteome profiling of Streptococcus mutans

ABSTRACT: S-glutathionylation is an important post-translational modification (PTM) process that targets the protein cysteine thiol by the addition of glutathione (GSH). This modification can prevent proteolysis from over-oxidation of protein cysteine residue during the condition of oxidative or nitrosative stress. Recent studies suggest that protein S-glutathionylation plays an essential role in control of cell-signaling pathways by affecting the protein function in bacteria and even humans. In this study, we investigated the impacts of S-glutathionylation on physiological regulation within Streptococcus mutans, the primary etiological agent of human dental caries. To determine S-glutathionylated proteins in bacteria, the Cys-reactive isobaric reagents iodoTMT (iodoacetyl Tandem Mass Tag) were used to label the S-glutathionylated Cys sites and anti-TMT antibody conjugated resins were used to enrich the modified peptides. Proteome profiling identified a total of 357 glutathionylated cysteines sites on 239 proteins. Functional enrichment analysis indicated that these S-glutathionylated proteins were involved in diverse important biological processes, such as pyruvate metabolism and glycolysis

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Streptococcus Mutans Ua159

TISSUE(S): Whole Body

SUBMITTER: Xian Peng

LAB HEAD: Peng Xian

PROVIDER: PXD019564 | Pride | 2020-07-14

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	W8094TPRo_IP.raw	Raw
	txt.zip	Other

Items per page:

1 - 2 of 2

Similar Datasets

Alterations of protein S-glutathionylation modification in macrophages under oxidative conditions

Project description:S-glutathionylation is an important regulatory posttranslational modification of protein cysteine (Cys) thiols, yet the role of specific cysteine residues as targets of modification is poorly understood. To identify the specific molecular targets and pathways of Grx1 that are susceptible to redox-dependent regulation, we applied a quantitative redox proteomics approach that permits site-specific profiling of S-glutathionylation at a proteome-wide scale in macrophages.

2021-11-01 | PXD027965 | Pride

Protein S-glutathionylation in HeLa cells identified by nanoLC-LTQ-Orbitrap XL MS/MS

Project description:Cysteine modifications have been widely detected among different protein in different species. Here, we examined protein glutathionylation in HeLa cells under both untreated and diamide-treated conditions. A strategy using resin-assisted enrichment of glutathionylated proteins or peptides after biotin-switch is commonly used for detection of glutathionylation and other reversible cysteine modifications, and was also applied in this study. Using these strategies we identified a large number of glutathionylated protein with modification sites under both untreated and diamide-treated conditions.

2020-04-29 | PXD017717 | Pride

In-vitro glutathionylation of SMYD2

Project description:Glutathionylation is an important post-translational modification and developing tools to identify which cysteine residues on proteins are glutathionylated in response to different physiological conditions is necessary. This project utilizes an approach consisting of azido-glutathione, a single purified protein, and an oxidant to form disulfide bonds between the azide modified glutathione and the cysteine residues of the protein. After this the reaction is quenched with iodoacetamide, subjected to a click reaction with a chemically cleavable alkyne conjugated biotin, and digested with trypsin. These peptide fragments are eluted from streptavidin beads and subjected to LC-MS/MS to determine which cysteine residues are glutathionylated in-vitro.

2019-04-03 | PXD011123 | Pride

Transcription profiling of human liver cell line after cysteine deprivation

Project description:First experiment: Cells were cultured in sulfur amino acid-free DMEM supplemented with 0.1 mM methionine + 0.1 mM cysteine (complete) or supplemented only with 0.1 mM methionine (cysteine-free). Cells were cultured in either medium for 42 h (Long + Cys; Long -Cys) or in cysteine-free medium for 36 h followed by 6 h in complete medium (Short +Cys); Second experiment: C3A/HepG2 cells were cultured in sulfur amino acid-free DMEM supplemented with 0.1 mM Met and 0.1 mM Cys (complete) or supplemented only with 0.1 mM Met (cysteine-devoid). Cells were cultured in complete medium for 42 h (Long +Cys) or in complete medium for 36 h followed by cysteine-devoid medium for 6 h (Short -Cys). Experiment Overall Design: First experiment: Three plates of cells were cultured under each condition. Cells were cultured in sulfur amino acid-free DMEM supplemented with 0.1 mM methionine + 0.1 mM cysteine (complete) or supplemented only with 0.1 mM methionine (cysteine-free). Cells were cultured in either medium for 42 h (Long + Cys; Long -Cys) or in cysteine-free medium for 36 h followed by 6 h in complete medium (Short +Cys). Experiment Overall Design: Second experiment: C3A/HepG2 cells were cultured in sulfur amino acid-free DMEM supplemented with 0.1 mM Met and 0.1 mM Cys (complete) or supplemented only with 0.1 mM Met (cysteine-devoid). Cells were cultured in complete medium for 42 h (Long +Cys) or in complete medium for 36 h followed by cysteine-devoid medium for 6 h (Short -Cys).

2008-06-16 | E-GEOD-9517 | biostudies-arrayexpress

Cysteine deprivation in liver cell line

2007-12-13 | GSE9517 | GEO

Comparative proteomics using iodoTMT to identify changes in protein expression and cysteine oxidation in Leishmania mexicana

Project description:Two cell-lines of Leishmania mexicana were investigated using a TMT-based approach; wild-type and an attenuated H-line. Half of each sample was fully reduced and all cysteine residues were labelled with the cysteine-reactive iodoTMT reagent, while the other half was reacted with N-ethylmaleimide to block all free cysteines before the remaining reversibly modified cysteines were reduced and labelled with iodoTMT. This allowed direct comparisons to be made between the level of modified cysteines and the total cysteine count.

2018-11-23 | PXD010938 | Pride

Glutathionylation decreases methyltransferase activity of PRMT5 and inhibits cell proliferation

Project description:Glutathionylation is an important posttranslational modification that protects proteins from further oxidative damage as well as influencing protein structure and activity. In the present study, we demonstrate that the cysteine-42 residue in protein arginine N-methyltransferase 5 (PRMT5) is glutathionylated in aged mice or in cells that have been exposed to oxidative stress. Deglutathionylation of this protein is catalyzed by glutaredoxin-1 (Grx1). Using mutagenesis and subsequent biochemical analyses, we show that glutathionylation decreased the binding affinity of PRMT5 with methylosome protein-50 (MEP50) and reduced the methyltransferase activity of PRMT5. Furthermore, overexpression of PRMT5-C42A mutant caused a significant increase in histone methylation in HEK293T and A549 cells and promoted cell growth, whereas overexpression of the PRMT5-C42D mutant, a mimic of glutathionylated PRMT5, inhibited cell proliferation. Taken together, our results demonstrate a new mechanism of regulation of PRMT5 methyltransferases activity and suggest that PRMT5 glutathionylation is partly responsible for reactive oxygen species-mediated cell growth inhibition

2020-09-02 | PXD020428 | Pride

Clickable glutathione-based Isotope Coded Affinity Label to quantify glutathionylation

Project description:Identification of cysteines with high oxidation susceptibility is important for understanding redox-mediated biological processes associated with health and disease. We developed a chemical proteomic strategy that helps find cysteines with high susceptibility to S-glutathionylation. Our strategy is based on the isotopically labelled clickable glutathione derivatives that can quantify relative levels of glutathionylated and reduced forms (SSG vs. SH) of cysteines in mass spectrometry, which is named 'Clickable Glutathione-based Isotope-coded Affinity-Tag (G-ICAT).' The G-ICAT approach was applied to the mouse C2C12 cell line upon addition of hydrogen peroxide, finding 1,518 glutathionylated cysteines and their relative levels of SSG over SH upon adding hydron peroxide. This chemical proteomic strategy will significantly contribute to identifying functional cysteines regulated by glutathionylation in redox signaling.

2024-03-07 | PXD034976 | Pride

Site-specific Identification of Glutathionylation

Project description:Cardiomyocytes proteins were investigated for their glutathionylation in response to hydrogen peroxide generated from glucose oxidase and using a clickable glutathione derivative. After exposure, or not, to hydrogen peroxide the glutathionylated proteins were enriched and LC-MS/MS analyses was performed.

2019-03-06 | PXD012171 | Pride

Isotopic-labelled Clickable Glutathione to Quantify Protein S-Glutathionylation

Project description:Investigated protein glutathionylation in HL-1 cardiomyocyte cells in response to hydrogen peroxide using a clickable glutathione approach. After exposure, or not, to hydrogen peroxide the glutathionylated proteins with heavy or light azido glutathione were enriched and subjected to LC-MS/MS analysis followed by quantification.

2021-09-08 | PXD014937 | Pride