Cysteine oxidation and disulfide formation in the ribosomal exit tunnel

  • 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.

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Author:Linda Schulte, Jiafei Mao, Julian Reitz, Sridhar SreeramuluORCiDGND, Denis KudlinzkiGND, Victor-Valentin Hodirnau, Jakob Meier-CredoORCiD, Krishna SaxenaORCiDGND, Florian Buhr, Julian David LangerORCiDGND, Martin Blackledge, Achilleas S. FrangakisORCiDGND, Clemens GlaubitzORCiDGND, Harald SchwalbeORCiDGND
Parent Title (German):Nature Communications
Publisher:Nature Publishing Group UK
Place of publication:[London]
Document Type:Article
Date of Publication (online):2020/11/01
Date of first Publication:2020/11/01
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2020/12/09
Issue:1, Article number: 5569
Page Number:11
Institutes:Biochemie, Chemie und Pharmazie / Biochemie und Chemie
Biowissenschaften / Biowissenschaften
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften
5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Licence (German):License LogoCreative Commons - Namensnennung 4.0