Cysteine oxidation and disulfide formation in the ribosomal exit tunnel.

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.

journal_name

Nat Commun

journal_title

Nature communications

authors

Schulte L,Mao J,Reitz J,Sreeramulu S,Kudlinzki D,Hodirnau VV,Meier-Credo J,Saxena K,Buhr F,Langer JD,Blackledge M,Frangakis AS,Glaubitz C,Schwalbe H

doi

10.1038/s41467-020-19372-x

subject

Has Abstract

pub_date

2020-11-04 00:00:00

pages

5569

issue

1

issn

2041-1723

pii

10.1038/s41467-020-19372-x

journal_volume

11

pub_type

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