Cysteine oxidation and disulfide formation in the ribosomal exit tunnel.
Cryoelectron Microscopy
Cysteine
/ chemistry
Disulfides
/ chemistry
Glutathione
/ analogs & derivatives
Magnetic Resonance Spectroscopy
Mass Spectrometry
Models, Molecular
Mutation
Oxidation-Reduction
Protein Biosynthesis
Protein Conformation
Protein Folding
Ribosomes
/ chemistry
S-Nitrosothiols
/ chemistry
gamma-Crystallins
/ chemistry
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
04 11 2020
04 11 2020
Historique:
received:
04
09
2020
accepted:
08
10
2020
entrez:
5
11
2020
pubmed:
6
11
2020
medline:
15
12
2020
Statut:
epublish
Résumé
Understanding 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.
Identifiants
pubmed: 33149120
doi: 10.1038/s41467-020-19372-x
pii: 10.1038/s41467-020-19372-x
pmc: PMC7642426
doi:
Substances chimiques
Disulfides
0
S-Nitrosothiols
0
gamma-Crystallins
0
S-glycolylglutathione
50409-85-3
Glutathione
GAN16C9B8O
Cysteine
K848JZ4886
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
5569Références
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