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Motor-free mitochondrial presequence translocase drives membrane integration of preproteins
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2007 (English)In: Nature Cell Biology, ISSN 1465-7392, Vol. 9, no 10, 1152-1159 p.Article in journal (Refereed) Published
Abstract [en]

The mitochondrial inner membrane is the central energy-converting membrane of eukaryotic cells. the electrochemical proton gradient generated by the respiratory chain drives the ATP synthase. to maintain this proton-motive force, the inner membrane forms a tight barrier and strictly controls the translocation of ions(1). However, the major preprotein transport machinery of the inner membrane, termed the presequence translocase, translocates polypeptide chains into or across the membrane(2-9). Different views exist of the molecular mechanism of the translocase, in particular of the coupling with the import motor of the matrix(8,10,11). Wehave reconstituted preprotein transport into the mitochondrial inner membrane by incorporating the purified presequence translocase into cardiolipin-containing liposomes. We show that the motor-free form of the presequence translocase integrates preproteins into the membrane. the reconstituted presequence translocase responds to targeting peptides and mediates voltage-driven preprotein translocation, lateral release and insertion into the lipid phase. thus, the minimal system for preprotein integration into the mitochondrial inner membrane is the presequence translocase, a cardiolipin-rich membrane and a membrane potential.

Place, publisher, year, edition, pages
2007. Vol. 9, no 10, 1152-1159 p.
National Category
Biological Sciences Chemical Sciences
URN: urn:nbn:se:uu:diva-143308DOI: 10.1038/ncb1635ISI: 000249882300010OAI: oai:DiVA.org:uu-143308DiVA: diva2:390509
Available from: 2011-01-21 Created: 2011-01-20 Last updated: 2011-01-21Bibliographically approved

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