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Updated: Jun 20, 2026

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Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
Published on: December 17, 2016
The 20S proteasome as an assembly platform for the 19S regulatory complex
Klavs B Hendil1, Franziska Kriegenburg, Keiji Tanaka
1Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK-2200 Copenhagen N, Denmark.
Journal of Molecular Biology
|September 29, 2009
Summary
The 26S proteasome
Area of Science:
- Cellular Biology
- Molecular Biology
- Biochemistry
Background:
- The 26S proteasome is a crucial cellular machine for protein degradation.
- It comprises a 20S core particle and two 19S regulatory complexes.
- The 19S regulatory complex consists of a base and a lid sub-complex.
Purpose of the Study:
- To investigate the assembly pathway of the human 19S regulatory complex.
- To identify early assembly intermediates of the 19S regulatory complex.
Main Methods:
- Biochemical analysis of proteasome assembly intermediates.
- Characterization of protein complexes using biochemical techniques.
Main Results:
- Two distinct assembly intermediates of the human 19S regulatory complex were identified.
- One intermediate is a dimer of Rpt3 and Rpt6 ATPase subunits.
- The other is a complex of nascent lid subunits (Rpn2, Rpn10, Rpn11, Rpn13, Txnl1) attached to the 20S proteasome, preceding base subunit incorporation.
Conclusions:
- 19S regulatory complex assembly initiates on preexisting 20S proteasomes.
- Assembly of the lid sub-complex partially precedes the assembly of the base sub-complex.
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