title: Cross-linking analysis of yeast mitochondrial outer membrane.
abstract: By enrichment of contact sites between the two mitochondrial boundary membranes it has been shown that this fraction contained a high activity of glutathione transferase and hexokinase which was bound to the outer membrane pore protein (Ohlendieck, K. et al. (1986) Biochim. Biophys. Acta 860, 672-689). Therefore, an interaction between the three proteins in the contact sites has been suggested. Cross-linking experiments with isolated outer membrane of yeast mitochondria show that glutathione transferase and the pore protein are already associated in the free outer membrane. Porin appeared to adopt four different oligomeric complexes in the membrane, including interactions with a 14 kDa polypeptide, which has glutathione transferase activity. The latter polypeptide could be phosphorylated by intrinsic or extrinsic protein kinases, while the porin itself was not phosphorylated. Yeast hexokinase, when bound to the outer membrane, was able to cross-link to the pore protein.
mesh_terms: D002462:Cell Membrane / Q000187:drug effects / Q000648:ultrastructure*; D003432:Cross-Linking Reagents / Q000494:pharmacology; D005982:Glutathione Transferase / Q000032:analysis; D006593:Hexokinase / Q000378:metabolism; D008565:Membrane Proteins / Q000032:analysis; D008928:Mitochondria / Q000648:ultrastructure*; D010750:Phosphoproteins / Q000032:analysis; D012441:Saccharomyces cerevisiae / Q000648:ultrastructure*; D013388:Succinimides / Q000494:pharmacology
chemical_list: D003432:Cross-Linking Reagents; D008565:Membrane Proteins; D010750:Phosphoproteins; D013388:Succinimides; D005982:Glutathione Transferase; D006593:Hexokinase; C011240:dithiobis(succinimidylpropionate)