Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Antibodies, Bacterial / immunology
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Cysteine Endopeptidases / immunology
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Cysteine Endopeptidases / ultrastructure*
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Macromolecular Substances
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Microscopy, Electron
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Molecular Structure
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Molecular Weight
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Multienzyme Complexes / immunology
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Multienzyme Complexes / ultrastructure*
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Proteasome Endopeptidase Complex
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Thermoplasma / enzymology*
Substances
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Antibodies, Bacterial
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Macromolecular Substances
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Multienzyme Complexes
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex