Localization of subunits in proteasomes from Thermoplasma acidophilum by immunoelectron microscopy

The subunit topography of the Thermoplasma acidophilum proteasome was determined by iminunoelectron microscopy using monospecific antibodies directed against the two constituent subunits (,β). Anti--subunit IgG was found to bind to the outer disks of the cylinder- or barrel-shaped molecule, while the binding sites of the anti-β-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.