TY  - JOUR
A1  - Schulte, Linda
A1  - Mao, Jiafei
A1  - Reitz, Julian
A1  - Sreeramulu, Sridhar
A1  - Kudlinzki, Denis
A1  - Hodirnau, Victor-Valentin
A1  - Meier-Credo, Jakob
A1  - Saxena, Krishna
A1  - Buhr, Florian
A1  - Langer, Julian David
A1  - Blackledge, Martin
A1  - Frangakis, Achilleas S.
A1  - Glaubitz, Clemens
A1  - Schwalbe, Harald
T1  - Cysteine oxidation and disulfide formation in the ribosomal exit tunnel
T2  - Nature Communications
N2  - 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.
Y1  - 2020
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/57021
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-570218
SN  - 2041-1723
VL  - 11
IS  - 1, Article number: 5569
PB  - Nature Publishing Group UK
CY  - [London]
ER  -