Localization of subunits in proteasomes from Thermoplasma acidophilum by immunoelectron microscopy

FEBS Lett. 1991 Sep 23;290(1-2):186-90. doi: 10.1016/0014-5793(91)81256-8.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Bacterial / immunology
  • Cysteine Endopeptidases / immunology
  • Cysteine Endopeptidases / ultrastructure*
  • Macromolecular Substances
  • Microscopy, Electron
  • Molecular Structure
  • Molecular Weight
  • Multienzyme Complexes / immunology
  • Multienzyme Complexes / ultrastructure*
  • Proteasome Endopeptidase Complex
  • Thermoplasma / enzymology*

Substances

  • Antibodies, Bacterial
  • Macromolecular Substances
  • Multienzyme Complexes
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex