Identification of Tam41 maintaining integrity of the TIM23 protein translocator complex in mitochondria.
Identification of Tam41 maintaining integrity of the TIM23 protein translocator complex in mitochondria.
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DOI：
10.1083/jcb.200603087
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发表时间：
2006-08-28
期刊：
影响因子：
--
通讯作者：
Endo T
中科院分区：
文献类型：
--
作者：
Tamura Y;Harada Y;Yamano K;Watanabe K;Ishikawa D;Ohshima C;Nishikawa S;Yamamoto H;Endo T
新合成的线粒体蛋白质借助于线粒体外膜和内膜中的蛋白质转运体复合物输入到线粒体中。我们报告的鉴定酵母Tam 41，线粒体蛋白转运系统的新成员。Tam 41是面向基质的外周线粒体内膜蛋白。TAM 41基因的破坏导致酵母细胞的温度敏感性生长，并导致在体内和体外升高的温度下通过TIM 23转运蛋白复合物的蛋白质输入缺陷。虽然Tam 41不是TIM 23复合物的组成部分，但Tam 41的缺失导致TIM 23复合物的分子大小减小以及Pam 18和Pam-16的部分聚集。Pam 16在没有Tam 41的线粒体中的输入被延迟，并且输入的Pam 16在体外形成聚集体。这些结果表明，Tam 41通过维持来自内膜基质侧的TIM 23蛋白转运复合物的功能完整性来促进线粒体蛋白的输入。
Newly synthesized mitochondrial proteins are imported into mitochondria with the aid of protein translocator complexes in the outer and inner mitochondrial membranes. We report the identification of yeast Tam41, a new member of mitochondrial protein translocator systems. Tam41 is a peripheral inner mitochondrial membrane protein facing the matrix. Disruption of the TAM41 gene led to temperature-sensitive growth of yeast cells and resulted in defects in protein import via the TIM23 translocator complex at elevated temperature both in vivo and in vitro. Although Tam41 is not a constituent of the TIM23 complex, depletion of Tam41 led to a decreased molecular size of the TIM23 complex and partial aggregation of Pam18 and -16. Import of Pam16 into mitochondria without Tam41 was retarded, and the imported Pam16 formed aggregates in vitro. These results suggest that Tam41 facilitates mitochondrial protein import by maintaining the functional integrity of the TIM23 protein translocator complex from the matrix side of the inner membrane.
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