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Hallmarks and evolutionary drivers of cotranslational protein complex assembly
Mihaly Badonyi1, Joseph A Marsh1
1MRC Human Genetics Unit, Institute of Genetics and Cancer, University of Edinburgh, UK.
The FEBS Journal
|May 19, 2023
Summary
Cotranslational assembly, where protein subunits join on the ribosome, is common. This review explores its mechanisms, evolution, and detection, highlighting ongoing research and challenges.
Area of Science:
- Molecular Biology
- Biochemistry
- Evolutionary Biology
Background:
- Recent discoveries show cotranslational assembly is prevalent in proteomes.
- Mechanisms enabling protein complex subunit assembly on the ribosome are increasingly understood.
- Emergent properties influencing cotranslational assembly have been identified through structural analyses.
Purpose of the Study:
- To review historical experiments and breakthroughs in detecting cotranslational assembly.
- To discuss the mechanistic, structural, and evolutionary factors driving cotranslational assembly.
- To introduce a framework for understanding cotranslational assembly hallmarks.
Main Methods:
- Review of historical experiments and literature.
- Analysis of structural data.
- Proteome-wide detection methodologies.
Main Results:
- Cotranslational assembly involves diverse mechanisms on the ribosome.
- Structural properties inherently influence subunit cotranslational assembly.
- Proteome-wide detection methods have advanced the field.
Conclusions:
- The evolutionary paths of cotranslational complexes are still unclear.
- Technical challenges remain in studying cotranslational assembly.
- New experimental results are refining our understanding of cotranslational assembly drivers.
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