Role of mitochondrial inner membrane organizing system in protein biogenesis of the mitochondrial outer membrane.
Role of mitochondrial inner membrane organizing system in protein biogenesis of the mitochondrial outer membrane.
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DOI：
10.1091/mbc.e12-04-0295
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发表时间：
2012-10
影响因子：
3.3
通讯作者：
van der Laan M
中科院分区：
文献类型：
--
作者：
Bohnert M;Wenz LS;Zerbes RM;Horvath SE;Stroud DA;von der Malsburg K;Müller JM;Oeljeklaus S;Perschil I;Warscheid B;Chacinska A;Veenhuis M;van der Klei IJ;Daum G;Wiedemann N;Becker T;Pfanner N;van der Laan M
线粒体内膜组织系统 (MINOS) 是维持内膜结构所需的大型蛋白质复合物。我们报告说，MINOS 独立地与线粒体外膜的两个前蛋白转位酶相互作用，并在外膜 β-桶蛋白的生物发生中发挥作用。线粒体包含两层膜，外膜和具有折叠嵴的内膜。线粒体内膜组织系统 (MINOS) 是维持内膜结构所需的大型蛋白质复合物。 MINOS 与外膜前蛋白转运机制、外膜转位酶 (TOM) 以及分选和组装机制 (SAM) 相互作用。然而，MINOS 是否在外膜蛋白的生物合成中发挥作用尚不清楚。我们剖析了 MINOS 与 TOM 和 SAM 的相互作用，并报告 MINOS 独立地与两种易位酶结合。 MINOS 通过 Sam50 的保守多肽转运相关结构域与 SAM 复合物结合。缺乏 MINOS 大核心亚基 mitofilin 的线粒体在外膜 β-桶蛋白的生物合成中受到损害，而缺乏其他五个 MINOS 亚基中任何一个的突变线粒体以与野生型线粒体类似的方式导入 β-桶蛋白。我们表明，丝裂蛋白在 β-桶生物发生的早期阶段是必需的，包括通过 TOM 复合体的初始易位。我们得出结论，MINOS 独立地与 TOM 和 SAM 相互作用，并且核心亚基 mitofilin 参与外膜 β-桶蛋白的生物发生。
The mitochondrial inner membrane organizing system (MINOS) is a large protein complex required for maintaining inner membrane architecture. We report that MINOS independently interacts with both preprotein translocases of the outer mitochondrial membrane and plays a role in the biogenesis of β-barrel proteins of the outer membrane. Mitochondria contain two membranes, the outer membrane and the inner membrane with folded cristae. The mitochondrial inner membrane organizing system (MINOS) is a large protein complex required for maintaining inner membrane architecture. MINOS interacts with both preprotein transport machineries of the outer membrane, the translocase of the outer membrane (TOM) and the sorting and assembly machinery (SAM). It is unknown, however, whether MINOS plays a role in the biogenesis of outer membrane proteins. We have dissected the interaction of MINOS with TOM and SAM and report that MINOS binds to both translocases independently. MINOS binds to the SAM complex via the conserved polypeptide transport–associated domain of Sam50. Mitochondria lacking mitofilin, the large core subunit of MINOS, are impaired in the biogenesis of β-barrel proteins of the outer membrane, whereas mutant mitochondria lacking any of the other five MINOS subunits import β-barrel proteins in a manner similar to wild-type mitochondria. We show that mitofilin is required at an early stage of β-barrel biogenesis that includes the initial translocation through the TOM complex. We conclude that MINOS interacts with TOM and SAM independently and that the core subunit mitofilin is involved in biogenesis of outer membrane β-barrel proteins.