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Updated: May 10, 2026
06:58
Global Identification of Co-Translational Interaction Networks by Selective Ribosome Profiling
Published on: October 7, 2021
The twisted tale of cotranslational protein complex assembly
1School of Neurobiology, Biochemistry, and Biophysics, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel.
Current Opinion in Structural Biology
|May 8, 2026
Summary
Cotranslational assembly, where proteins assemble during synthesis, is a prevalent mechanism in cells. This process creates kinetically stable macromolecular complexes essential for cellular function, even under stress.
Area of Science:
- Molecular Biology
- Biophysics
- Cellular Biology
Background:
- Macromolecular complexes are vital cellular functional units.
- Classical models described assembly post-protein synthesis.
- Emerging evidence highlights cotranslational assembly during translation.
Purpose of the Study:
- To review advances in cotranslational assembly.
- To discuss thermodynamic and kinetic principles of assembly.
- To explore how complex features enable cotranslational assembly.
Main Methods:
- Literature review of cotranslational assembly studies.
- Analysis of thermodynamic and kinetic principles.
- Examination of structural and biophysical features of complexes.
Main Results:
- Cotranslational assembly is a prevalent mode of complex formation.
- Specific complex features facilitate cotranslational assembly.
- This assembly mode is governed by thermodynamic and kinetic factors.
Conclusions:
- Cotranslational assembly yields kinetically stable oligomeric states.
- Stable complexes resist dissociation and conformational changes.
- This stability ensures functionality in crowded or stressful cellular environments.
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