Signal recognition initiates reorganization of the presequence translocase during protein import
Signal recognition initiates reorganization of the presequence translocase during protein import
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DOI：
10.1038/emboj.2013.23
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发表时间：
2013-03-20
期刊：
影响因子：
11.4
通讯作者：
Rehling, Peter
中科院分区：
文献类型：
--
作者：
Lytovchenko, Oleksandr;Melin, Jonathan;Rehling, Peter
线粒体前序列转位酶与内膜膜间隙 (IMS) 侧含有前序列的前体相互作用，介导它们转位到基质中。人们对这些基质靶向信号如何激活易位酶以启动前体转运也知之甚少。因此，我们分析了前序列易位酶的信号识别如何在导入过程中启动 Tim 蛋白之间的重组。我们的分析表明，前序受体 Tim50 在涉及 Tim23 通道 IMS 域的过程中以信号敏感的方式与 Tim21 相互作用。 Tim50 的信号驱动释放 Tim21 促进 Pam17 的募集，从而触发基质运输所需的 TIM23 复合物的运动相关形式的形成。 EMBO 杂志 (2013) 32, 886-898。 doi：10.1038/emboj.2013.23； 2013 年 2 月 12 日在线发布
The mitochondrial presequence translocase interacts with presequence-containing precursors at the intermembrane space (IMS) side of the inner membrane to mediate their translocation into the matrix. Little is known as too how these matrix-targeting signals activate the translocase in order to initiate precursor transport. Therefore, we analysed how signal recognition by the presequence translocase initiates reorganization among Tim-proteins during import. Our analyses revealed that the presequence receptor Tim50 interacts with Tim21 in a signal-sensitive manner in a process that involves the IMS-domain of the Tim23 channel. The signal-driven release of Tim21 from Tim50 promotes recruitment of Pam17 and thus triggers formation of the motor-associated form of the TIM23 complex required for matrix transport. The EMBO Journal (2013) 32, 886-898. doi:10.1038/emboj.2013.23; Published online 12 February 2013