Toward an integrated structural model of the 26S proteasome.
The 26S proteasome is the end point of the ubiquitin-proteasome pathway and degrades ubiquitylated substrates. It is composed of the 20S core particle (CP), where degradation occurs, and the 19S regulatory particle (RP), which ensures substrate specificity of degradation. Whereas the CP is resolved to atomic resolution, the architecture of the RP is largely unknown. We provide a comprehensive analysis of the current structural knowledge on the RP, including structures of the RP subunits, physical protein-protein interactions, and cryoelectron microscopy data. These data allowed us to compute an atomic model for the CP-AAA-ATPase subcomplex. In addition to this atomic model, further subunits can be mapped approximately, which lets us hypothesize on the substrate path during its degradation.
Förster
Friedrich
F
Department of Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany. foerster@biochem.mpg.de
Lasker
Keren
K
Nickell
Stephan
S
Sali
Andrej
A
Baumeister
Wolfgang
W
D000818:Animals; D020285:Cryoelectron Microscopy; D008958:Models, Molecular; D046988:Proteasome Endopeptidase Complex / Q000737:chemistry* / Q000648:ultrastructure; D011485:Protein Binding; D021122:Protein Subunits / Q000737:chemistry
D021122:Protein Subunits; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease
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