PXD038309 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | 3-Mercaptopyruvate sulfur transferase is a protein persulfidase |
Description | Protein S-persulfidation (P-SSH) is recognized as a common post-translational modification across all domains of life. It occurs under basal conditions and is often observed to be elevated under stress conditions. However, the mechanism(s) by which proteins are persulfidated inside cells have remained unclear. Here we report that 3-mercaptopyruvate sulfur transferase (MPST) engages in direct protein-to-protein transpersulfidation reactions beyond its previously known protein substrates thioredoxin and MOCS3/Uba4, associated with H2S generation and tRNA thiolation, respectively. We observe that depletion of MPST in human cells lowers overall intracellular protein persulfidation levels and identify a subset of proteins whose persulfidation depends on MPST. The predicted involvement of these proteins in the adaptation to stress responses supports the notion that MPST-dependent protein persulfidation promotes cytoprotective functions. The observation of MPST-independent protein persulfidation suggests that other protein persulfidases remain to be identified. |
HostingRepository | PRIDE |
AnnounceDate | 2023-11-14 |
AnnouncementXML | Submission_2023-11-14_08:46:58.197.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Marcin Luzarowski |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive HF |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2022-11-23 04:25:13 | ID requested | |
1 | 2023-05-10 13:43:15 | announced | |
⏵ 2 | 2023-11-14 08:47:06 | announced | 2023-11-14: Updated project metadata. |
Publication List
Pedre B, Talwar D, Barayeu U, Schilling D, Luzarowski M, Sokolowski M, Glatt S, Dick TP, 3-Mercaptopyruvate sulfur transferase is a protein persulfidase. Nat Chem Biol, 19(4):507-517(2023) [pubmed] |
Keyword List
submitter keyword: cytoprotection, post-translational modification, MPST,S-persulfidation, protein persulfidation |
Contact List
Tobias P. Dick |
contact affiliation | Division of Redox Regulation, DKFZ-ZMBH Alliance, German Cancer Research Center (DKFZ), Heidelberg, Germany Faculty of Biosciences, Heidelberg University, Heidelberg, Germany |
contact email | T.Dick@dkfz-heidelberg.de |
lab head | |
Marcin Luzarowski |
contact affiliation | University of Heidelberg |
contact email | m.luzarowski@zmbh.uni-heidelberg.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD038309
- Label: PRIDE project
- Name: 3-Mercaptopyruvate sulfur transferase is a protein persulfidase