Protein unfolding by mitochondria - The Hsp70 import motor

被引:125
作者
Matouschek, A
Pfanner, N
Voos, W
机构
[1] Northwestern Univ, Dept Biochem Mol Biol & Cell Biol, Evanston, IL 60208 USA
[2] Univ Freiburg, Inst Biochem & Mol Biol, D-79104 Freiburg, Germany
关键词
D O I
10.1093/embo-reports/kvd093
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
Protein unfolding is a key step in the import of some proteins into mitochondria and chloroplasts and in the degradation of regulatory proteins by ATP-dependent proteases. In contrast to protein folding, the reverse process has remained largely uninvestigated until now. This review discusses recent discoveries on the mechanism of protein unfolding during translocation into mitochondria. The mitochondria can actively unfold preproteins by unraveling them from the N-terminus. The central component of the mitochondrial import motor, the matrix heat shock protein 70, functions by bath pulling and holding the preproteins.
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页码:404 / 410
页数:7
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