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Updated: Jul 18, 2025
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Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
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Wiggle and Shake: Managing and Exploiting Conformational Dynamics during Proteasome Biogenesis
Daniel Betancourt1, Tomiwa Lawal1, Robert J Tomko1
1Department of Biomedical Sciences, Florida State University College of Medicine, Tallahassee, FL 32306, USA.
Biomolecules
|August 26, 2023
Summary
The 26S proteasome
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- The 26S proteasome is a large protease complex crucial for cellular protein homeostasis.
- Dysfunctional proteasome assembly or activity is linked to various human diseases.
- Proteasome assembly involves numerous subunits and dedicated chaperone proteins.
Purpose of the Study:
- To review current knowledge on 26S proteasome assembly.
- To emphasize the role of conformational dynamics in proteasome biogenesis.
- To identify emerging questions in the field of proteasome assembly.
Main Methods:
- Review of existing literature.
- Analysis of cryo-electron microscopy data.
- Integration of structural and functional insights.
Main Results:
- The 26S proteasome is a dynamic machine with conformational changes occurring during assembly and function.
- Conformational dynamics play a critical role in guiding specific proteasome biogenesis events.
- Near-atomic resolution cryo-electron microscopy has advanced our understanding of proteasome structure and dynamics.
Conclusions:
- Understanding proteasome assembly dynamics is essential for comprehending its role in human health and disease.
- Further research into proteasome biogenesis dynamics is warranted.
- This review highlights key areas for future investigation in proteasome assembly.
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