Cysteine oxidation and disulfide formation in the ribosomal exit tunnel.

Autor:	Schulte L; Institute of Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University of Frankfurt, Frankfurt, Germany., Mao J; Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University Frankfurt, Frankfurt, Germany., Reitz J; Institute for Biophysics, Buchmann Institute for Molecular Life Science, Goethe University Frankfurt, Frankfurt, Germany., Sreeramulu S; Institute of Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University of Frankfurt, Frankfurt, Germany., Kudlinzki D; Institute of Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University of Frankfurt, Frankfurt, Germany., Hodirnau VV; Institute for Biophysics, Buchmann Institute for Molecular Life Science, Goethe University Frankfurt, Frankfurt, Germany.; Institute of Science and Technology Austria, Klosterneuburg, Austria., Meier-Credo J; Max Planck Institute of Biophysics, Frankfurt, Germany., Saxena K; Institute of Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University of Frankfurt, Frankfurt, Germany., Buhr F; Institute of Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University of Frankfurt, Frankfurt, Germany.; Centre for Misfolding Diseases, University of Cambridge, Cambridge, UK., Langer JD; Max Planck Institute of Biophysics, Frankfurt, Germany., Blackledge M; Institute de Biologie Structurale, Grenoble, France. martin.blackledge@ibs.fr., Frangakis AS; Institute for Biophysics, Buchmann Institute for Molecular Life Science, Goethe University Frankfurt, Frankfurt, Germany. achilleas.frangakis@biophysik.org., Glaubitz C; Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University Frankfurt, Frankfurt, Germany. glaubitz@em.uni-frankfurt.de., Schwalbe H; Institute of Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University of Frankfurt, Frankfurt, Germany. schwalbe@nmr.uni-frankfurt.de.
Jazyk:	angličtina
Zdroj:	Nature communications [Nat Commun] 2020 Nov 04; Vol. 11 (1), pp. 5569. Date of Electronic Publication: 2020 Nov 04.
DOI:	10.1038/s41467-020-19372-x
Abstrakt:	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.
Databáze:	MEDLINE
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