title: The carboxyl-terminal two-thirds of the ADP/ATP carrier polypeptide contains sufficient information to direct translocation into mitochondria.
abstract: The precursor of the mitochondrial inner membrane protein ADP/ATP carrier is cytoplasmically synthesized without an amino-terminal peptide extension. We constructed a truncated precursor lacking the 103 amino acids from the amino terminus (about a third of the protein). Import of the truncated precursor into mitochondria showed the import characteristics of the authentic precursor, including nucleoside triphosphate dependence, requirement for a protease-sensitive component on the mitochondrial surface, two-step specific binding to the outer membrane, and membrane potential-dependent translocation into the inner membrane. We conclude that, in contrast to all other mitochondrial precursor proteins studied so far, domains of the ADP/ATP carrier distant from the amino terminus can carry specific targeting information for transport into mitochondria.
authors.affiliation: Institut für Physiologische Chemie, Universität München, Federal Republic of Germany.
authors.forename: N
authors.initials: N
authors.lastname: Pfanner
authors.forename: P
authors.initials: P
authors.lastname: Hoeben
authors.forename: M
authors.initials: M
authors.lastname: Tropschug
authors.forename: W
authors.initials: W
authors.lastname: Neupert
mesh_terms: D000818:Animals; D003001:Cloning, Molecular; D007425:Intracellular Membranes / Q000201:enzymology; D008928:Mitochondria / Q000201:enzymology*; D000226:Mitochondrial ADP, ATP Translocases / Q000235:genetics* / Q000378:metabolism; D009491:Neurospora / Q000201:enzymology*; D009492:Neurospora crassa / Q000201:enzymology* / Q000235:genetics; D009713:Nucleotidyltransferases / Q000235:genetics*; D014176:Protein Biosynthesis; D011499:Protein Processing, Post-Translational; D012156:Reticulocytes / Q000378:metabolism
chemical_list: D000226:Mitochondrial ADP, ATP Translocases; D009713:Nucleotidyltransferases