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Transport of F 1 ‐ATPase subunit β into mitochondria depends on both a membrane potential and nucleoside triphosphates
Author(s) -
Pfanner Nikolaus,
Neupert Walter
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81101-2
Subject(s) - oligomycin , mitochondrion , biochemistry , atpase , nucleoside , apyrase , lysis , gtp' , atp synthase , chemiosmosis , inner mitochondrial membrane , valinomycin , membrane potential , reticulocyte , f atpase , electron transport chain , atp–adp translocase , chemistry , biology , enzyme , rna , thylakoid , chloroplast , gene
Transport of cytoplasmically synthesized precursor proteins into or across the inner mitochondrial membrane requires a mitochondrial membrane potential. We have studied whether additional energy sources are also necessary for protein translocation. Reticulocyte lysate (containing radiolabelled precursor proteins) and mitochondria were depleted of ATP by pre‐incubation with apyrase. A membrane potential was then established by the addition of substrates of the electron transport chain. Oligomycin was included to prevent dissipation of Δψ by the action of the F 0 F 1 ‐ATPase. Under these conditions, import of subunit β of F 1 ‐ATPase (F 1 β) was inhibited. Addition of ATP or GTP restored import. When the membrane potential was destroyed, however, the import of F 1 β was completely inhibited even in the presence of ATP. We therefore conclude that the import of F 1 β depends on both nucleoside triphosphates and a membrane potential.