MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization.
MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization.
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DOI：
10.1091/mbc.e11-09-0774
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发表时间：
2012-01
影响因子：
3.3
通讯作者：
Deckers M
中科院分区：
文献类型：
--
作者：
Alkhaja AK;Jans DC;Nikolov M;Vukotic M;Lytovchenko O;Ludewig F;Schliebs W;Riedel D;Urlaub H;Jakobs S;Deckers M
MINOS 1/Mio 10是一种保守的线粒体蛋白，是线粒体内膜组织和嵴形态所必需的。MINOS 1/Mio 10是一种新的组成部分的线粒体膜蛋白/Fcj 1复合物的内膜，连接的形态表型的突变体的活性的线粒体内膜组织复合物。线粒体的内膜特别富含蛋白质，并显示出独特的形态学，其特征在于大的内陷、线粒体嵴和靠近外膜的内界膜。线粒体内膜蛋白似乎并不均匀地分布在内膜中，而是组织成功能不同的亚室。目前还不清楚内膜的组织是如何实现的。我们鉴定了一个保守的线粒体内膜蛋白MINOS 1/MIO 10（C1 orf 151/YCL 057 C-A）。MIO 10突变酵母细胞在不可发酵碳源上的生长受到影响，并表现出改变的线粒体形态。在超微结构水平，突变线粒体显示内膜组织的损失。蛋白质组学分析揭示MINOS 1/Mio 10是人类和酵母线粒体中Mitofilin/Fcj 1复合物的新成分。因此，我们的分析揭示了新的见解组成的线粒体内膜组织机构。
MINOS1/Mio10, a conserved mitochondrial protein, is required for mitochondrial inner membrane organization and cristae morphology. MINOS1/Mio10 is a novel constituent of the mitofilin/Fcj1 complex of the inner membrane, linking the morphology phenotype of the mutant to the activity of the mitochondrial inner membrane organizing complex. The inner membrane of mitochondria is especially protein rich and displays a unique morphology characterized by large invaginations, the mitochondrial cristae, and the inner boundary membrane, which is in proximity to the outer membrane. Mitochondrial inner membrane proteins appear to be not evenly distributed in the inner membrane, but instead organize into functionally distinct subcompartments. It is unknown how the organization of the inner membrane is achieved. We identified MINOS1/MIO10 (C1orf151/YCL057C-A), a conserved mitochondrial inner membrane protein. mio10-mutant yeast cells are affected in growth on nonfermentable carbon sources and exhibit altered mitochondrial morphology. At the ultrastructural level, mutant mitochondria display loss of inner membrane organization. Proteomic analyses reveal MINOS1/Mio10 as a novel constituent of Mitofilin/Fcj1 complexes in human and yeast mitochondria. Thus our analyses reveal new insight into the composition of the mitochondrial inner membrane organizing machinery.