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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
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Diverging co-translational protein complex assembly pathways are governed by interface energy distribution.

Johannes Venezian1, Hagit Bar-Yosef1, Hila Ben-Arie Zilberman1

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Cellular protein assembly is orchestrated by ribosomes. This study identifies "hotspots" on nascent proteins that initiate interactions, preventing misfolding and disease.

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Area of Science:

  • Molecular Biology
  • Biophysics
  • Structural Biology

Background:

  • Protein-protein interactions are fundamental to cellular function.
  • The ribosome acts as a central platform for orchestrating these interactions during protein synthesis.
  • Understanding co-translational folding and complex assembly is crucial for cellular processes.

Purpose of the Study:

  • To investigate the characteristics governing co-translational protein folding and complex assembly.
  • To identify key residues and mechanisms initiating these interactions.
  • To explore the link between these mechanisms and human diseases.

Main Methods:

  • Selective ribosome profiling
  • Imaging techniques
  • N-terminomics
  • All-atom molecular dynamics simulations
  • AlphaFold-Multimer modeling
  • Conservation analysis

Main Results:

  • Identified specific "hotspot" residues that initiate co-translational assembly upon exposure from the ribosome exit tunnel.
  • Demonstrated that these hotspots possess high binding energy and are crucial for interface assembly.
  • Revealed that alpha-helices containing hotspots are thermolabile and require partner subunits for stability.
  • Showed that mutations in hotspots disrupt co-translational complexation, leading to protein aggregation.
  • Found that disease-associated variants in N-terminal acetyltransferases (NATs) disrupt these hotspot clusters.
  • Extended findings to other protein complexes, confirming the predictive power of interface energy profiles.

Conclusions:

  • Co-translational assembly is initiated by specific, high-affinity "hotspot" residues.
  • The stability of these interactions is dynamic and dependent on partner subunits.
  • Disruption of these hotspots is linked to protein aggregation and human diseases.
  • Interface energy distribution serves as a predictive model for co-translational assembly.