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PXD021574 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleCysteine oxidation and disulfide formation in the ribosomal exit tunnel
DescriptionUnderstanding the conformational sampling of translation-arrested ribosome nascent chain complexes is key to understand co-translational folding. Up to now, coupling of cysteine oxidation, disulfide bond formation and structure formation in nascent chains has remained elusive. Here, we investigate the eye-lens protein γB-crystallin in the ribosomal exit tunnel. Using mass spectrometry, theoretical simulations, dynamic nuclear polarization-enhanced solid-state nuclear magnetic resonance and cryo-electron microscopy, we show that thiol groups of cysteine residues undergo S-glutathionylation and S-nitrosylation and form non-native disulfide bonds. Thus, covalent modification chemistry occurs already prior to nascent chain release as the ribosome exit tunnel provides sufficient space even for disulfide bond formation which can guide protein folding.
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterJulian Langer
SpeciesList scientific name: Escherichia coli; NCBI TaxID: 562; scientific name: Bos taurus (Bovine); NCBI TaxID: 9913;
ModificationListmonohydroxylated residue; nitrosylation; iodoacetamide derivatized residue; L-cysteine glutathione disulfide
InstrumentOrbitrap Fusion Lumos; impact II
Dataset History
RevisionDatetimeStatusChangeLog Entry
02020-09-20 23:38:16ID requested
12020-11-09 04:48:24announced
Publication List
Schulte L, Mao J, Reitz J, Sreeramulu S, Kudlinzki D, Hodirnau VV, Meier-Credo J, Saxena K, Buhr F, Langer JD, Blackledge M, Frangakis AS, Glaubitz C, Schwalbe H, Cysteine oxidation and disulfide formation in the ribosomal exit tunnel. Nat Commun, 11(1):5569(2020) [pubmed]
Keyword List
submitter keyword: Disulfide formation, ribosomal exit tunnel, cysterine oxidation, glutathione
Contact List
Julian Langer
contact affiliationMPI of Biophysics MPI for Brain Research Max von Laue Strasse 3/4 60438 Frankfurt am Main
contact emailjulian.langer@biophys.mpg.de
lab head
Julian Langer
contact affiliationMPIs for Biophysics and Brain Research
contact emailjulian.langer@biophys.mpg.de
dataset submitter
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Dataset FTP location
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