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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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Cotranslational protein folding through non-native structural intermediates.

Siyu Wang1, Amir Bitran2, Ekaterina Samatova1

  • 1Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Göttingen 37077, Germany.

Science Advances
|September 5, 2025
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Summary
This summary is machine-generated.

This study reveals how proteins fold as they are made, identifying key interactions that guide the process. Understanding this cotranslational folding is crucial for predicting protein misfolding and designing new proteins.

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Area of Science:

  • Molecular Biology
  • Biophysics
  • Computational Biology

Background:

  • Protein folding is essential for cellular function, but occurs during translation (cotranslational folding) within the ribosome.
  • Misfolding, linked to diseases, arises from disruptions in cotranslational folding pathways.
  • Predicting these pathways at an atomistic level remains a significant challenge.

Purpose of the Study:

  • To computationally predict and experimentally validate the atomistic details of cotranslational folding pathways.
  • To investigate the role of non-native hydrophobic interactions in stabilizing early folding intermediates.
  • To understand how the ribosome's environment and molecular chaperones influence cotranslational folding.

Main Methods:

  • Atomistic molecular dynamics simulations to predict folding pathways.
  • Experimental validation using biophysical techniques.
  • Analysis of interactions between nascent peptides and the ribosome exit tunnel.

Main Results:

  • A vectorial hierarchy of folding was computationally predicted and experimentally validated.
  • Early folding intermediates are stabilized by transient, non-native hydrophobic interactions.
  • Disruption of these interactions impairs cotranslational folding.
  • The chaperone trigger factor modulates the folding pathway by maintaining peptide dynamics.

Conclusions:

  • Surface-exposed residues play a critical, previously unrecognized role in cotranslational folding.
  • The findings provide new tools for improving protein folding prediction and protein design.
  • This work deepens our understanding of the fundamental mechanisms governing protein biogenesis.