Membrane topography of the subunits of ubiquinol-cytochrome-c oxidoreductase of Saccharomyces cerevisiae. The 14-kDa and the 11-kDa subunits face opposite sides of the mitochondrial inner membrane

Eur J Biochem. 1990 Sep 24;192(3):761-5. doi: 10.1111/j.1432-1033.1990.tb19287.x.

Abstract

The topology of the subunits of ubiquinol-cytochrome-c oxidoreductase of the yeast Saccharomyces cerevisiae has been determined using a digitonin/proteinase K assay. With this assay we were able selectively to disrupt the mitochondrial membranes and to identify the subunits which became proteinase-K sensitive after disruption of either the outer or both outer and inner membranes. This approach confirmed previous indications for the localization of the core I protein, cytochrome c1, cytochrome b, the FeS protein and the 17-kDa subunit, while it also provided direct evidence for the site of accessibility to proteinase K of the 14-kDa and 11-kDa subunits. The 14-kDa subunit faces the mitochondrial matrix and the 11-kDa subunit faces the intermembrane space.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Membrane / enzymology
  • Cytochrome b Group / analysis
  • Cytochrome c Group / analysis
  • Digitonin
  • Electron Transport Complex III / analysis
  • Electron Transport Complex III / chemistry*
  • Electron Transport Complex III / genetics
  • Endopeptidase K
  • Fumarate Hydratase / analysis
  • Intracellular Membranes / enzymology
  • Saccharomyces cerevisiae / enzymology*
  • Serine Endopeptidases

Substances

  • Cytochrome b Group
  • Cytochrome c Group
  • Serine Endopeptidases
  • Endopeptidase K
  • Fumarate Hydratase
  • Electron Transport Complex III
  • Digitonin