Unfolding and refolding of a purified precursor protein during import into isolated mitochondria.
A purified mitochondrial precursor protein unfolds to a protease-sensitive conformation at the surface of isolated mitochondria before being imported into the organelles. This unfolding is stimulated by a potential across the mitochondrial inner membrane, but does not require ATP. In contrast, import of the surface-bound unfolded precursor requires ATP, but no potential; it is accompanied by a refolding inside the mitochondria.
Eilers
M
M
University of Basel, Department of Biochemistry, Switzerland.
Hwang
S
S
Schatz
G
G
D000818:Animals; D003576:Electron Transport Complex IV / Q000235:genetics* / Q000378:metabolism; D004792:Enzyme Precursors / Q000235:genetics*; D046911:Macromolecular Substances; D051379:Mice; D008928:Mitochondria / Q000201:enzymology*; D011487:Protein Conformation; D011489:Protein Denaturation; D011993:Recombinant Fusion Proteins / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics*; D013762:Tetrahydrofolate Dehydrogenase / Q000235:genetics* / Q000378:metabolism; D014508:Urea / Q000494:pharmacology
D004792:Enzyme Precursors; D046911:Macromolecular Substances; D011993:Recombinant Fusion Proteins; D011994:Recombinant Proteins; D014508:Urea; D013762:Tetrahydrofolate Dehydrogenase; D003576:Electron Transport Complex IV