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MIM复合体介导前体蛋白穿过线粒体内膜,并将其与线粒体热休克蛋白70/ATP驱动系统偶联。

The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP driving system.

作者信息

Berthold J, Bauer M F, Schneider H C, Klaus C, Dietmeier K, Neupert W, Brunner M

机构信息

Institut für Physiologische Chemie, Universität München, Federal Republic of Germany.

出版信息

Cell. 1995 Jun 30;81(7):1085-93. doi: 10.1016/s0092-8674(05)80013-3.

Abstract

We have identified a complex in mitochondria that functions as a part of the preprotein import machinery of the inner membrane (MIM complex). Two known components, MIM23 and MIM17, and two novel components, MIM33 and MIM14, were found as constituents of this complex. In the presence of a translocating chain, the outer membrane import machinery (MOM complex) and the MIM complex form translocation contact sites. On the matrix side, the MIM complex is associated with the mt-Hsp70-MIM44 system. We propose a structure of the import machinery in which the MIM complex constitutes a proteinaceous channel that accepts preproteins from the MOM complex, facilitates their reversible transmembrane movement, and mediates unidirectional transport by linkage to the ATP-dependent mt-Hsp70-MIM44 system.

摘要

我们在 mitochondria 中鉴定出一种复合物,它作为内膜前体蛋白导入机制(MIM 复合物)的一部分发挥作用。发现两个已知成分 MIM23 和 MIM17 以及两个新成分 MIM33 和 MIM14 是该复合物的组成部分。在存在转运链的情况下,外膜导入机制(MOM 复合物)和 MIM 复合物形成转运接触位点。在基质侧,MIM 复合物与 mt-Hsp70-MIM44 系统相关联。我们提出了一种导入机制的结构,其中 MIM 复合物构成一个蛋白质通道,该通道接受来自 MOM 复合物的前体蛋白,促进它们可逆的跨膜移动,并通过与依赖 ATP 的 mt-Hsp70-MIM44 系统相连介导单向运输。

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