Cysteine oxidation and disulfide formation in the ribosomal exit tunnel
Copyright policy )Cysteine oxidation and disulfide formation in the ribosomal exit tunnel
AbstractUnderstanding 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.
- Chinese Academy of Sciences China (People's Republic of)
- Grenoble Alpes University France
- French National Centre for Scientific Research France
- University of Cambridge United Kingdom
- Institut de Biologie Structurale France
MESH: Oxidation-Reduction, Models, Molecular, 570, Protein Folding, MESH: Mutation, Magnetic Resonance Spectroscopy, [SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Protein Conformation, ddc:540, MESH: Protein Folding, Science, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Article, Mass Spectrometry, MESH: Protein Conformation, MESH: Models, MESH: S-Nitrosothiols, MESH: Disulfides, Cysteine, Disulfides, gamma-Crystallins, MESH: Glutathione, MESH: Mass Spectrometry, S-Nitrosothiols, MESH: gamma-Crystallins, MESH: Magnetic Resonance Spectroscopy, Molecular Biology/Structural Biology [q-bio.BM], Q, Cryoelectron Microscopy, Molecular, MESH: Cysteine, 540, Glutathione, MESH: Protein Biosynthesis, Protein Biosynthesis, Mutation, ddc:570, MESH: Cryoelectron Microscopy, MESH: Ribosomes, Oxidation-Reduction, Ribosomes, ddc: ddc:570, ddc: ddc:540
MESH: Oxidation-Reduction, Models, Molecular, 570, Protein Folding, MESH: Mutation, Magnetic Resonance Spectroscopy, [SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Protein Conformation, ddc:540, MESH: Protein Folding, Science, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Article, Mass Spectrometry, MESH: Protein Conformation, MESH: Models, MESH: S-Nitrosothiols, MESH: Disulfides, Cysteine, Disulfides, gamma-Crystallins, MESH: Glutathione, MESH: Mass Spectrometry, S-Nitrosothiols, MESH: gamma-Crystallins, MESH: Magnetic Resonance Spectroscopy, Molecular Biology/Structural Biology [q-bio.BM], Q, Cryoelectron Microscopy, Molecular, MESH: Cysteine, 540, Glutathione, MESH: Protein Biosynthesis, Protein Biosynthesis, Mutation, ddc:570, MESH: Cryoelectron Microscopy, MESH: Ribosomes, Oxidation-Reduction, Ribosomes, ddc: ddc:570, ddc: ddc:540
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