Import of proteins into mitochondria.
A mounting body of evidence suggests that cytoplasmically synthesized proteins destined to be imported into the mitochondrial interior must at least partly unfold to penetrate across the mitochondrial membranes. During post-translational import, this unfolding process appears to be a major rate-limiting step. It can be blocked by ligands that stabilize the protein's native conformation and appears to be accompanied by the cleavage of ATP outside the mitochondrial inner membrane.
D000818:Animals; D003576:Electron Transport Complex IV / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D051379:Mice; D008928:Mitochondria / Q000378:metabolism*; D008954:Models, Biological; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000235:genetics*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics; D013762:Tetrahydrofolate Dehydrogenase / Q000235:genetics
D011506:Proteins; D011993:Recombinant Fusion Proteins; D013762:Tetrahydrofolate Dehydrogenase; D003576:Electron Transport Complex IV