Localization of subunits in proteasomes from Thermoplasma acidophilum by immunoelectron microscopy.
The subunit topography of the Thermoplasma acidophilum proteasome was determined by immunoelectron microscopy using monospecific antibodies directed against the two constituent subunits (alpha,beta). Anti-alpha-subunit IgG was found to bind to the outer disks of the cylinder- or barrel-shaped molecule, while the binding sites of the anti-beta-subunit IgG were mapped on the two inner rings. Probably the homologues of the two subunits in the compositionally more complex but isomorphous eukaryotic proteasomes occupy equivalent positions.
Max-Planck-Institut für Biochemie, Martinsried, Germany.
A
A
Grziwa
W
W
Baumeister
B
B
Dahlmann
F
F
Kopp
D000907:Antibodies, Bacterial / Q000276:immunology; D003546:Cysteine Endopeptidases / Q000276:immunology / Q000648:ultrastructure*; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D015394:Molecular Structure; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000276:immunology / Q000648:ultrastructure*; D046988:Proteasome Endopeptidase Complex; D013822:Thermoplasma / Q000201:enzymology*
D000907:Antibodies, Bacterial; D046911:Macromolecular Substances; D009097:Multienzyme Complexes; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex