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PXD019564-1

PXD019564 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleS-glutathionylation proteome profiling of Streptococcus mutans
DescriptionS-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
HostingRepositoryPRIDE
AnnounceDate2020-07-14
AnnouncementXMLSubmission_2020-07-14_02:41:09.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterXian Peng
SpeciesList scientific name: Streptococcus mutans UA159; NCBI TaxID: 210007;
ModificationListmonohydroxylated residue; acetylated residue
InstrumentQ Exactive Plus
Dataset History
RevisionDatetimeStatusChangeLog Entry
02020-06-04 04:12:25ID requested
12020-07-14 02:41:10announced
22024-10-22 05:08:57announced2024-10-22: Updated project metadata.
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: S-glutathionylation
Streptococcus mutans
post-translational modification
Contact List
Peng Xian
contact affiliationState Key Laboratory of Oral Diseases, National Clinical Research Center for Oral Diseases, West China Hospital of Stomatology, Sichuan University, Chengdu, China
contact emailpengx@scu.edu.cn
lab head
Xian Peng
contact affiliationState Key Laboratory of Oral Diseases, Sichuan University
contact emailpengx@scu.edu.cn
dataset submitter
Full Dataset Link List
Dataset FTP location
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PRIDE project URI
Repository Record List
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