PXD019564-2

PXD019564 is an original dataset announced via ProteomeXchange.

Title	S-glutathionylation proteome profiling of Streptococcus mutans
Description	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
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:08:57.255.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Xian Peng
SpeciesList	scientific name: Streptococcus mutans UA159; NCBI TaxID: 210007;
ModificationList	monohydroxylated residue; acetylated residue
Instrument	Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2020-06-04 04:12:25	ID requested
1	2020-07-14 02:41:10	announced
⏵ 2	2024-10-22 05:08:57	announced	2024-10-22: Updated project metadata.

Dataset with its publication pending

submitter keyword: S-glutathionylation

Streptococcus mutans

post-translational modification

Peng Xian
contact affiliation	State Key Laboratory of Oral Diseases, National Clinical Research Center for Oral Diseases, West China Hospital of Stomatology, Sichuan University, Chengdu, China
contact email	pengx@scu.edu.cn
lab head
Xian Peng
contact affiliation	State Key Laboratory of Oral Diseases, Sichuan University
contact email	pengx@scu.edu.cn
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2020/07/PXD019564

PRIDE project URI

• PRIDE
  1. PXD019564
     1. Label: PRIDE project
     2. Name: S-glutathionylation proteome profiling of Streptococcus mutans