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 Communjournal_title
Nature communicationsauthors
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 Hdoi
10.1038/s41467-020-19372-xsubject
Has Abstractpub_date
2020-11-04 00:00:00pages
5569issue
1issn
2041-1723pii
10.1038/s41467-020-19372-xjournal_volume
11pub_type
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