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首页> 外文期刊>The Journal of biological chemistry >The Mitochondrial ADP/ATP Carrier Associates with the Inner Membrane Presequence Translocase in a Stoichiometric Manner
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The Mitochondrial ADP/ATP Carrier Associates with the Inner Membrane Presequence Translocase in a Stoichiometric Manner

机译：线粒体ADP / ATP载体以化学计量的方式与内膜前译，内膜前译

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The majority of mitochondrial proteins are synthesized with amino-terminal signal sequences. The presequence translocase of the inner membrane (TIM23 complex) mediates the import of these preproteins. The essential TIM23 core complex closely cooperates with partner protein complexes like the presequence translocase-associated import motor and the respiratory chain. The inner mitochondrial membrane also contains a large number of metabolite carriers, but their association with preprotein translocases has been controversial. We performed a comprehensive analysis of the TIM23 interactome based on stable isotope labeling with amino acids in cell culture. Subsequent biochemical studies on identified partner proteins showed that the mitochondrial ADP/ATP carrier associates with the membrane-embedded core of the TIM23 complex in a stoichiometric manner, revealing an unexpected connection of mitochondrial protein biogenesis to metabolite transport. Our data indicate that direct TIM23-AAC coupling may support preprotein import into mitochondria when respiratory activity is low.
机译：大多数线粒体蛋白质由氨基末端信号序列合成。内膜（TIM23复合物）的前译团介质介导这些预蛋白质的进口。基本的TIM23核心复合体与伴侣蛋白复合物密切合作，如Presequence译团相关的进口电机和呼吸链。内部线粒体膜还含有大量代谢物载体，但它们与预蛋白翻译的关联具有争议性。基于稳定同位素标记与细胞培养中氨基酸的稳定同位素标记进行了全面分析。对鉴定的合作蛋白的后续生化研究表明，线粒体ADP / ATP载体以化学计量的方式与TIM23复合物的膜嵌入核心相关联，揭示了线粒体蛋白生物发生的意外连接到代谢物运输。我们的数据表明，当呼吸活动低时，直接TIM23-AAC耦合可以支持预蛋白质进口到线粒体中。

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