Structure and function of Pet100p, a molecular chaperone required for the assembly of cytochrome c oxidase in Saccharomyces cerevisiae
Structure and function of Pet100p, a molecular chaperone required for the assembly of cytochrome c oxidase in Saccharomyces cerevisiae
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DOI：
10.1042/bst0290436
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发表时间：
2001-08-01
影响因子：
3.9
通讯作者：
Poyton, RO
中科院分区：
文献类型：
--
作者：
Forsha, D;Church, C;Poyton, RO
细胞色素c氧化酶在真核细胞线粒体内膜的组装需要大量核基因的蛋白产物。在酵母中，其中一些作用于全球，并影响几个连锁蛋白质复合物的组装，而其他人则以细胞色素c氧化酶特异性的方式发挥作用。这些酵母蛋白中的许多都有人类的对应物，当突变时会导致与能量有关的疾病。这些蛋白质之一，Pet 100 p，是一种新的分子伴侣，其功能是将含有细胞色素c氧化酶亚基VII，VIIa和VIII的亚复合物纳入holo-（细胞色素c氧化酶）。在这里，我们报告的拓扑结构的Pet 100 p在线粒体内膜的处置，并表明其C-末端结构域是必不可少的，其功能作为一个cvtochrome c氧化酶特异性的“装配促进剂”。
The assembly of cytochrome c oxidase in the inner mitochondrial membranes of eukaryotic cells requires the protein products of a large number of nuclear genes. In yeast, some of these act globally and affect the assembly of several respiratory-chain protein complexes, whereas others act in a cytochrome c oxidase-specific fashion. Many of these yeast proteins have human counterparts, which when mutated lead to energy-related diseases. One of these proteins, Pet100p, is a novel molecular chaperone that functions to incorporate a subcomplex containing cytochrome c oxidase subunits VII, VIIa and VIII into holo-(cytochrome c oxidase). Here we report the topological disposition of Pet100p in the inner mitochondrial membrane and show that its C-terminal domain is essential for its function as a cvtochrome c oxidase-specific 'assembly facilitator'.