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酵母线粒体内膜导入机制(MIM)各组分的功能和物理相互作用。

Functional and physical interactions of components of the yeast mitochondrial inner-membrane import machinery (MIM).

作者信息

Blom J, Dekker P J, Meijer M

机构信息

Department of Molecular Cell Biology, BioCentrum Amsterdam, The Netherlands.

出版信息

Eur J Biochem. 1995 Aug 15;232(1):309-14. doi: 10.1111/j.1432-1033.1995.tb20813.x.

Abstract

The essential mitochondrial inner-membrane protein, Mim44, is involved in the translocation of preproteins across the mitochondrial inner membrane. Two other putative components of this protein-translocation system are the integral inner-membrane proteins, Mim23 and Mim17. Here, we present genetic evidence for functional co-operation of all three proteins. Furthermore, we show that Mim23 and Mim17 are associated in a protein complex that also contains two proteins of 55 kDa and 20 kDa. We speculate that this subcomplex forms the proteinaceous import channel of the inner-membrane which transiently interacts with a less abundant peripheral complex of Mim44 and mitochondrial heat-shock protein Hsp70.

摘要

线粒体内膜必需蛋白Mim44参与前体蛋白在线粒体内膜的转运。该蛋白转运系统的另外两个假定组分是内膜整合蛋白Mim23和Mim17。在此,我们提供了这三种蛋白功能协同的遗传学证据。此外,我们表明Mim23和Mim17存在于一个蛋白复合物中,该复合物还包含55 kDa和20 kDa的两种蛋白。我们推测,这个亚复合物形成内膜的蛋白质转运通道,它与含量较少的Mim44外周复合物和线粒体热休克蛋白Hsp70发生短暂相互作用。

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