Electron microscopy of 26 S complex containing 20 S proteasome.
A high molecular weight protease complex (26 S complex) involved in the intracellular protein degradation of ubiquitinated proteins was purified from rat liver and studied by electron microscopy. The most prevalent molecular species with best preserved symmetrical morphology had two large rectangular terminal structures attached to a thinner central one having four protein layers. We concluded that they were the closest representation of the 26 S complex so far reported. The central structure was identified as 20 S proteasome and the terminal one as recognition units for ubiquitinated proteins.
Ikai
A
A
Laboratory of Biodynamics, Tokyo Institute of Technology, Yokohama, Japan.
Nishigai
M
M
Tanaka
K
K
Ichihara
A
A
D000818:Animals; D003546:Cysteine Endopeptidases / Q000648:ultrastructure*; D010450:Endopeptidases / Q000648:ultrastructure*; D008099:Liver / Q000737:chemistry; D008854:Microscopy, Electron; D009097:Multienzyme Complexes / Q000648:ultrastructure*; D046988:Proteasome Endopeptidase Complex; D051381:Rats; D014452:Ubiquitins / Q000737:chemistry
D009097:Multienzyme Complexes; D014452:Ubiquitins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex