The preprotein translocation channel of the outer membrane of mitochondria

被引:314
作者
Künkele, KP
Heins, S
Dembowski, M
Nargang, FE
Benz, R
Thieffry, M
Walz, J
Lill, R
Nussberger, S
Neupert, W
机构
[1] Univ Munich, Inst Physiol Chem Phys Biochem & Zellbiol, D-80336 Munich, Germany
[2] Univ Alberta, Dept Biol Sci, Edmonton, AB T6G 2E9, Canada
[3] CNRS, Neurobiol Cellulaire & Mol Lab, F-91198 Gif Sur Yvette, France
[4] Univ Wurzburg, Theodor Boveri Inst, Lehrstuhl Biotechnol, D-97074 Wurzburg, Germany
[5] Max Planck Inst Biochem, Abt Mol Strukturbiol, D-82152 Martinsried, Germany
[6] Philipps Univ Marburg, Inst Zytobiol, D-35033 Marburg, Germany
基金
英国医学研究理事会;
关键词
D O I
10.1016/S0092-8674(00)81206-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:1009 / 1019
页数:11
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