The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria
The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria
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DOI：
10.1016/s0092-8674(00)81271-4
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发表时间：
1996-06-14
期刊：
影响因子：
64.5
通讯作者：
Langer, T
中科院分区：
文献类型：
--
作者：
Arlt, H;Tauer, R;Langer, T
高度保守的AAA家族的线粒体成员Yta10p和Yta12p构成了一个约850 kDa的膜嵌入复合物。作为ATP依赖性金属肽酶（AAA蛋白酶），YTA10-12复合物介导非组装内膜蛋白的降解。与核苷酸依赖复合物的形成和底物结合相反，结合多肽的蛋白质水解取决于ATP的水解和这两个亚基的金属肽酶活性。独立于其蛋白水解功能，YTA10-12复合物的伴侣样活性是膜相关ATP合成酶组装所必需的。我们认为，YTA10-12复合物中的蛋白水解和伴侣样活性介导了膜蛋白复合物的组装和降解过程，从而在维持膜完整性方面发挥了关键作用。
The mitochondrial members of the highly conserved AAA family, Yta10p and Yta12p, constitute a membrane-embedded complex of about 850 kDa. As an ATP dependent metallopeptidase (AAA protease), the YTA10-12 complex mediates the degradation of nonassembled inner membrane proteins. In contrast to nucleotide-dependent complex formation and substrate binding, proteolysis of bound polypeptides depends on the hydrolysis of ATP and the metallopeptidase activity of both subunits. Independent of its proteolytic function, the chaperone-like activity of the YTA10-12 complex is required for assembly of the membrane-associated ATP synthase. We propose that proteolytic and chaperone-like activities in the YTA10-12 complex mediate assembly and degradation processes of membrane protein complexes and thereby exert key functions in the maintenance of membrane integrity.