Tetratricopeptide repeat proteins Tom70 and Tom71 mediate yeast mitochondrial morphogenesis
Tetratricopeptide repeat proteins Tom70 and Tom71 mediate yeast mitochondrial morphogenesis
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DOI：
10.1038/sj.embor.7401113
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发表时间：
2008-01-01
期刊：
影响因子：
7.7
通讯作者：
Okamoto, Koji
中科院分区：
文献类型：
--
作者：
Kondo-Okamoto, Noriko;Shaw, Janet M.;Okamoto, Koji
维持正确的线粒体形状需要大量的蛋白质作用于细胞器的表面或内部。虽然可溶性F-box蛋白Mfb1最近被发现与线粒体外周相关，并调节出芽酵母的细胞器连接，但它如何定位于线粒体尚不清楚。本研究表明，Mfb1线粒体定位需要两种四肽重复蛋白——一般蛋白前输入受体Tom70（外膜转位酶的一个组成部分）及其旁联体tom71。在缺乏Tom70和Tom71的细胞中，线粒体形成短管和聚集体，与mfb1缺失突变体中观察到的异常形态相似。此外，Mfb1在体内与Tom71相互作用，并在体外通过Tom70与线粒体结合。我们的数据表明，Tom70在可溶性蛋白募集到线粒体表面的过程中发挥了意想不到的作用，并表明Tom71在mfb1介导的线粒体形态发生中具有特殊作用。
The maintenance of correct mitochondrial shape requires numerous proteins that act on the surface or inside of the organelle. Although the soluble F-box protein Mfb1 was recently found to associate peripherally with mitochondria and to regulate organelle connectivity in budding yeast, how it localizes to mitochondria is unknown. Here, we show that two tetratricopeptide repeat proteins-the general preprotein import receptor Tom70 (a component of translocase of the outer membrane) and its paralogue Tom71-are required for Mfb1 mitochondrial localization. Mitochondria in cells lacking Tom70 and Tom71 form short tubules and aggregates, aberrant morphologies similar to those observed in the mfb1-null mutant. In addition, Mfb1 interacts with Tom71 in vivo, and binds to mitochondria through Tom70 in vitro. Our data indicate an unexpected role for Tom70 in recruitment of soluble proteins to the mitochondrial surface, and indicate that Tom71 has a specialized role in Mfb1-mediated mitochondrial morphogenesis.