The preprotein translocation channel of the outer membrane of mitochondria
The preprotein translocation channel of the outer membrane of mitochondria
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DOI：
10.1016/s0092-8674(00)81206-4
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发表时间：
1998-06-12
期刊：
影响因子：
64.5
通讯作者：
Neupert, W
中科院分区：
文献类型：
--
作者：
Künkele, KP;Heins, S;Neupert, W
线粒体外膜的前蛋白转位酶（TOM复合物）促进核编码的线粒体前蛋白的识别、插入和转位。我们从粗糙脉孢菌中纯化了TOM复合物，并对其组成和功能性质进行了分析。TOM复合物含有阳离子选择性高电导通道。在重构为脂质体后，其介导蛋白质整合到脂质双层中并跨脂质双层移位。TOM复合物颗粒具有约138埃的直径，如通过电子显微镜和图像分析所揭示的;它们包含两个或三个染色填充的开口的中心，我们将其解释为具有约20埃的表观直径的孔。我们的结论是，这里报道的结构代表线粒体外膜的蛋白质传导通道。
The preprotein translocase of the outer membrane of mitochondria (TOM complex) facilitates the recognition, insertion, and translocation of nuclear-encoded mitochondrial preproteins. We have purified the TOM complex from Neurospora crassa and analyzed its composition and functional properties. The TOM complex contains a cation-selective high-conductance channel. Upon reconstitution into liposomes, it mediates integration of proteins into and translocation across the lipid bilayer. TOM complex particles have a diameter of about 138 Angstrom, as revealed by electron microscopy and image analysis; they contain two or three centers of stain-filled openings, which we interpret as pores with an apparent diameter of about 20 Angstrom. We conclude that the structure reported here represents the protein-conducting channel of the mitochondrial outer membrane.