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Reticulocyte lysate (containing radiolabelled precursor proteins) and mitochondria were depleted of ATP by pre\u2010incubation 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 \u0394\u03c8 by the action of the F<jats:sub>0<\/jats:sub>F<jats:sub>1<\/jats:sub>\u2010ATPase. Under these conditions, import of subunit \u03b2 of F<jats:sub>1<\/jats:sub>\u2010ATPase (F<jats:sub>1<\/jats:sub>\u03b2) was inhibited. Addition of ATP or GTP restored import. When the membrane potential was destroyed, however, the import of F<jats:sub>1<\/jats:sub>\u03b2 was completely inhibited even in the presence of ATP. We therefore conclude that the import of F<jats:sub>1<\/jats:sub>\u03b2 depends on both nucleoside triphosphates and a membrane potential.<\/jats:p>","DOI":"10.1016\/0014-5793(86)81101-2","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T07:57:40Z","timestamp":1027583860000},"page":"152-156","source":"Crossref","is-referenced-by-count":123,"title":["Transport of F<sub>1<\/sub>\u2010ATPase subunit \u03b2 into mitochondria depends on both a membrane potential and nucleoside triphosphates"],"prefix":"10.1002","volume":"209","author":[{"given":"Nikolaus","family":"Pfanner","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Walter","family":"Neupert","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2001,11]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0304-4157(84)90004-2"},{"key":"e_1_2_1_3_1","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1007\/978-1-4684-4604-3_13","volume-title":"The Enzymes of Biological Membranes","author":"Harmey M.A.","year":"1985"},{"key":"e_1_2_1_4_1","volume":"15","author":"Pfanner N.","year":"1986","journal-title":"Curr. 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