English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Cysteine oxidation and disulfide formation in the ribosomal exit tunnel

MPS-Authors
/persons/resource/persons192975

Meier-Credo,  Jakob
Proteomics and Mass Spectrometry, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137770

Langer,  Julian David
Proteomics and Mass Spectrometry, Max Planck Institute of Biophysics, Max Planck Society;

External Ressource
No external resources are shared
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Schulte, L., Mao, J., Reitz, J., Sreeramulu, S., Kudlinzki, D., Hodirnau, V.-V., et al. (2020). Cysteine oxidation and disulfide formation in the ribosomal exit tunnel. Nature Communications, 11(1): 5569. doi:10.1038/s41467-020-19372-x.


Cite as: http://hdl.handle.net/21.11116/0000-0007-594E-F
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.