Cysteine oxidation and disulfide formation in the ribosomal exit tunnel

Linda Schulte, Jiafei Mao, Julian Reitz, Sridhar Sreeramulu, Denis Kudlinzki, Victor-Valentin Hodirnau, Jakob Meier-Credo, Krishna Saxena, Florian Buhr, Julian D. Langer, Martin Blackledge (), Achilleas S. Frangakis (), Clemens Glaubitz () and Harald Schwalbe ()
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Linda Schulte: Goethe University of Frankfurt
Jiafei Mao: Goethe University Frankfurt
Julian Reitz: Goethe University Frankfurt
Sridhar Sreeramulu: Goethe University of Frankfurt
Denis Kudlinzki: Goethe University of Frankfurt
Victor-Valentin Hodirnau: Goethe University Frankfurt
Jakob Meier-Credo: Max Planck Institute of Biophysics
Krishna Saxena: Goethe University of Frankfurt
Florian Buhr: Goethe University of Frankfurt
Julian D. Langer: Max Planck Institute of Biophysics
Martin Blackledge: Institute de Biologie Structurale
Achilleas S. Frangakis: Goethe University Frankfurt
Clemens Glaubitz: Goethe University Frankfurt
Harald Schwalbe: Goethe University of Frankfurt

Nature Communications, 2020, vol. 11, issue 1, 1-11

Abstract: Abstract 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.

Date: 2020
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DOI: 10.1038/s41467-020-19372-x

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