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线粒体热休克蛋白70/线粒体导入调节因子44复合物促进蛋白质导入。

Mitochondrial Hsp70/MIM44 complex facilitates protein import.

作者信息

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

机构信息

Institut für Physiologische Chemie der Universität München, Germany.

出版信息

Nature. 1994 Oct 27;371(6500):768-74. doi: 10.1038/371768a0.

DOI:10.1038/371768a0
PMID:7935837
Abstract

Protein translocation into mitochondria requires the mitochondrial protein Hsp70. This molecular chaperone of the mitochondrial matrix is recruited to the protein import machinery by MIM44, a component associated with the inner membrane of the mitochondria. Formation of the mt-Hsp70/MIM44 complex is regulated by ATP. MIM44 and mt-Hsp 70 interact in a sequential manner with incoming segments of unfolded preproteins and thereby facilitate stepwise vectorial translocation of proteins across the mitochondrial membranes. The complex appears to act as a molecular ratchet which is energetically driven by the hydrolysis of ATP.

摘要

蛋白质转运到线粒体中需要线粒体蛋白Hsp70。线粒体基质的这种分子伴侣由MIM44招募到蛋白质导入机制中,MIM44是一种与线粒体内膜相关的成分。mt-Hsp70/MIM44复合物的形成受ATP调节。MIM44和mt-Hsp 70与未折叠前体蛋白的进入片段依次相互作用,从而促进蛋白质在线粒体内膜上的逐步向量转运。该复合物似乎起着分子棘轮的作用,由ATP水解提供能量驱动。

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Mitochondrial Hsp70/MIM44 complex facilitates protein import.线粒体热休克蛋白70/线粒体导入调节因子44复合物促进蛋白质导入。
Nature. 1994 Oct 27;371(6500):768-74. doi: 10.1038/371768a0.
2
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Mitochondrial protein import: biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44.线粒体蛋白导入:基质热休克蛋白70与内膜蛋白MIM44相互作用的生化及遗传学证据
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Translocation arrest of an intramitochondrial sorting signal next to Tim11 at the inner-membrane import site.线粒体内膜导入位点处Tim11旁的线粒体内分选信号的易位阻滞。
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