线粒体内膜蛋白质插入机制的重构。
Reconstitution of the protein insertion machinery of the mitochondrial inner membrane.
作者信息
Haucke V, Schatz G
机构信息
Department of Biochemistry, Biozentrum, University of Basel, Switzerland.
出版信息
EMBO J. 1997 Aug 1;16(15):4560-7. doi: 10.1093/emboj/16.15.4560.
Abstract
We have reconstituted the protein insertion machinery of the yeast mitochondrial inner membrane into proteoliposomes. The reconstituted proteoliposomes have a distinct morphology and protein composition and correctly insert the ADP/ATP carrier (AAC) and Tim23p, two multi-spanning integral proteins of the mitochondrial inner membrane. The reconstituted system requires a membrane potential, but not Tim44p or mhsp70, both of which are required for the ATP-driven translocation of proteins into the matrix. The protein insertion machinery can thus operate independently of the energy-transducing Tim44p-mhsp70 complex.
摘要
我们已将酵母线粒体内膜的蛋白质插入机制重组到蛋白脂质体中。重组后的蛋白脂质体具有独特的形态和蛋白质组成，并能正确插入线粒体内膜的两种多次跨膜整合蛋白——ADP/ATP载体（AAC）和Tim23p。重组系统需要膜电位，但不需要Tim44p或mhsp70，而这两者是蛋白质ATP驱动转运到基质中所必需的。因此，蛋白质插入机制可以独立于能量转导的Tim44p-mhsp70复合体运行。
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