Protein insertion into the mitochondrial inner membrane by a twin-pore translocase

被引:238
作者
Rehling, P
Model, K
Brandner, K
Kovermann, P
Sickmann, A
Meyer, HE
Kühlbrandt, W
Wagner, R
Truscott, KN
Pfanner, N
机构
[1] Univ Freiburg, Inst Biochem & Mol Biol, D-79104 Freiburg, Germany
[2] Max Planck Inst Biophys, Abt Strukturbiol, D-60528 Frankfurt, Germany
[3] Univ Freiburg, Fak Biol, D-79104 Freiburg, Germany
[4] Univ Osnabruck, Fachbereich Biol Chem, D-49034 Osnabruck, Germany
[5] Ruhr Univ Bochum, Med Proteom Ctr, D-44780 Bochum, Germany
关键词
D O I
10.1126/science.1080945
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The mitochondrial inner membrane imports numerous proteins that span it multiple times using the membrane potential Deltapsi as the only external energy source. We purified the protein insertion complex (TIM22 complex), a twin-pore translocase that mediated the insertion of precursor proteins in a three-step process. After the precursor is tethered to the translocase without losing energy from the Deltapsi, two energy-requiring steps were needed. First, Deltapsi acted on the precursor protein and promoted its docking in the translocase complex. Then, Deltapsi and an internal signal peptide together induced rapid gating transitions in one pore and closing of the other pore and drove membrane insertion to completion. Thus, protein insertion was driven by the coordinated action of a twin-pore complex in two voltage-dependent steps.
引用
收藏
页码:1747 / 1751
页数:5
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