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How Does the Ribosome Fold the Proteome?

Anaïs M E Cassaignau1, Lisa D Cabrita1, John Christodoulou1

  • 1Institute of Structural and Molecular Biology, University College London and Birkbeck College, London WC1E 7HX, United Kingdom; email: anais.cassaignau.09@ucl.ac.uk, l.cabrita@ucl.ac.uk, j.christodoulou@ucl.ac.uk.

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|June 23, 2020
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Summary

Protein folding begins during synthesis on ribosomes to maintain proteostasis and prevent aggregation. The ribosome acts as a scaffold, guiding polypeptide chains toward their functional structures during co-translational folding.

Keywords:
NMR spectroscopyco-translational foldingprotein foldingprotein misfoldingprotein synthesisribosome-bound nascent chainstructural biology

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Background:

  • Protein folding is crucial for cellular function and proteostasis.
  • Misfolding and aggregation of proteins can lead to disease.
  • Ribosomes play a role in protein folding during synthesis.

Purpose of the Study:

  • To investigate the role of the ribosome in co-translational polypeptide folding.
  • To understand how ribosome structure influences nascent chain folding.
  • To examine the interplay between translation and folding.

Main Methods:

  • High-resolution imaging techniques to visualize co-translational folding.
  • Biophysical methods to study nascent polypeptide dynamics.
  • Computational modeling of ribosome-polypeptide interactions.

Main Results:

  • The ribosome provides a scaffold that facilitates early protein structure formation.
  • Ribosome structure modulates the dynamics of emerging polypeptide chains.
  • Co-translational folding is a coordinated process guided by the ribosome.

Conclusions:

  • The ribosome is a key player in guiding nascent polypeptides toward their functional conformations.
  • Understanding ribosome-mediated folding is essential for comprehending proteostasis.
  • This research offers insights into the mechanistic basis of protein folding within the cell.