Insights into the molecular architecture of the 26S proteasome.
Cryo-electron microscopy in conjunction with advanced image analysis was used to analyze the structure of the 26S proteasome and to elucidate its variable features. We have been able to outline the boundaries of the ATPase module in the "base" part of the regulatory complex that can vary in its position and orientation relative to the 20S core particle. This variation is consistent with the "wobbling" model that was previously proposed to explain the role of the regulatory complex in opening the gate in the alpha-rings of the core particle. In addition, a variable mass near the mouth of the ATPase ring has been identified as Rpn10, a multiubiquitin receptor, by correlating the electron microscopy data with quantitative mass spectrometry.
Nickell
Stephan
S
Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany.
Beck
Florian
F
Scheres
Sjors H W
SH
Korinek
Andreas
A
Förster
Friedrich
F
Lasker
Keren
K
Mihalache
Oana
O
Sun
Na
N
Nagy
István
I
Sali
Andrej
A
Plitzko
Jürgen M
JM
Carazo
Jose-Maria
JM
Mann
Matthias
M
Baumeister
Wolfgang
W
D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000648:ultrastructure; D000818:Animals; D020285:Cryoelectron Microscopy; D004331:Drosophila melanogaster / Q000201:enzymology; D013058:Mass Spectrometry; D008958:Models, Molecular; D046988:Proteasome Endopeptidase Complex / Q000737:chemistry* / Q000648:ultrastructure; D021122:Protein Subunits / Q000737:chemistry; D021381:Protein Transport
D021122:Protein Subunits; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease; D000251:Adenosine Triphosphatases