Abstract
The 26S proteasome is the most downstream element of the ubiquitin-proteasome pathway of protein degradation. It is composed of the 20S core particle (CP) and the 19S regulatory particle (RP). The RP consists of 6 AAA-ATPases and at least 13 non-ATPase subunits. Based on a cryo-EM map of the 26S proteasome, structures of homologs, and physical protein-protein interactions we derive an atomic model of the AAA-ATPase-CP sub-complex. The ATPase order in our model (Rpt1/Rpt2/Rpt6/Rpt3/Rpt4/Rpt5) is in excellent agreement with the recently identified base-precursor complexes formed during the assembly of the RP. Furthermore, the atomic CP-AAA-ATPase model suggests that the assembly chaperone Nas6 facilitates CP-RP association by enhancing the shape complementarity between Rpt3 and its binding CP alpha subunits partners.
Original language | English |
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Pages (from-to) | 228-33 |
Number of pages | 6 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 388 |
Issue number | 2 |
DOIs | |
Publication status | Published - 2009 |
Externally published | Yes |
Keywords
- Adenosine Triphosphatases
- Animals
- Cryoelectron Microscopy
- Crystallography, X-Ray
- Drosophila melanogaster
- Proteasome Endopeptidase Complex
- Protein Structure, Quaternary