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Updated: May 26, 2026
06:58
Global Identification of Co-Translational Interaction Networks by Selective Ribosome Profiling
Published on: October 7, 2021
Widespread cotranslational formation of protein complexes
1Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom.
Plos Genetics
|December 7, 2011
Summary
Protein complexes assemble during translation. This study reveals that many proteins associate with mRNAs encoding their interaction partners, indicating widespread cotranslational assembly of protein complexes.
Area of Science:
- Molecular Biology
- Cell Biology
- Genomics
Background:
- Cellular processes rely on multi-protein complexes.
- Mechanisms of protein complex assembly, particularly cotranslational assembly, remain largely unknown.
Purpose of the Study:
- To investigate whether protein complexes form during the translation of their constituent proteins (cotranslational assembly).
- To systematically identify mRNA-protein associations to understand complex formation dynamics.
Main Methods:
- Genomic approach to identify mRNAs associated with specific proteins in Schizosaccharomyces pombe.
- Copurification of 31 proteins lacking RNA-binding domains with associated mRNAs.
- Validation of mRNA-protein associations based on the presence of encoded proteins and polysomal integrity.
Main Results:
- Approximately 38% of tested proteins copurified with mRNAs encoding interacting partners.
- Observed associations were dependent on the presence of the interacting proteins and polysomal integrity.
- Demonstrated cotranslational interactions between bait proteins and nascent polypeptides.
Conclusions:
- The cotranslational formation of protein-protein interactions is a widespread phenomenon.
- This finding provides a novel mechanism for the assembly of multi-protein complexes.
- Highlights the dynamic interplay between translation and protein complex formation.
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