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PXD034411

PXD034411 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitlePeroxiredoxins act as a post-translational modification in cytoplasmic protein quality control
DescriptionThe redox state of proteins is essential for their function and to guarantee cell fitness. In the endoplasmic reticulum, cells recognize and resolve undesirable cysteine oxidations by protein quality control machinery that involves protein disulfide isomerases. While disulfide bonds are uncommon in the reducing environment of the cytoplasm, they play a key role in redox signaling during oxidative stress and disease states. Using global proteomic analyses, here we show that the cytoplasmic peroxiredoxin Tsa1 covalently binds cysteine residues of hundreds of proteins, including metabolic enzymes, and acts as a protective chaperone to maintain protein function. Thioredoxins maintain the balance of this peroxiredoxin post-translational mark. Our study unveils a mechanism involving the peroxiredoxin-thioredoxin cycle in cytoplasmic protein quality control in eukaryotes
HostingRepositoryPRIDE
AnnounceDate2025-01-27
AnnouncementXMLSubmission_2025-01-27_00:28:47.088.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterEva Borràs
SpeciesList scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationListL-cysteine methyl disulfide; N-ethylmaleimide derivatized cysteine; monohydroxylated residue; iodoacetamide derivatized residue
InstrumentLTQ Orbitrap Velos; LTQ Orbitrap Elite
Dataset History
RevisionDatetimeStatusChangeLog Entry
02022-06-09 08:17:27ID requested
12025-01-27 00:28:47announced
Publication List
10.1016/J.CELREP.2024.115224;
Keyword List
submitter keyword: peroxiredoxin, mass spectrometry
Contact List
Eduard Sabido
contact affiliationCRG, UPF
contact emaileduard.sabido@crg.eu
lab head
Eva Borràs
contact affiliationUPF
contact emaileva.borras@upf.edu
dataset submitter
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Dataset FTP location
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