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Motor-free mitochondrial presequence translocase drives membrane integration of preproteins.

Abstract：

: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. However, the major preprotein transport machinery of the inner membrane, termed the presequence translocase, translocates polypeptide chains into or across the membrane. Different views exist of the molecular mechanism of the translocase, in particular of the coupling with the import motor of the matrix. We have 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.

journal_name

Nat Cell Biol

journal_title

Nature cell biology

authors

van der Laan M,Meinecke M,Dudek J,Hutu DP,Lind M,Perschil I,Guiard B,Wagner R,Pfanner N,Rehling P

doi

10.1038/ncb1635

subject

Has Abstract

pub_date

2007-10-01 00:00:00

pages

1152-9

issue

10

eissn

1465-7392

issn

1476-4679

pii

ncb1635

journal_volume

9

pub_type

杂志文章

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