Translocation of proteins into mitochondria

被引:1100
|
作者
Neupert, Walter
Herrmann, Johannes M.
机构
[1] Univ Munich, Inst Physiol Chem, D-81377 Munich, Germany
[2] Univ Kaiserslautern, Inst Zellbiol, D-67663 Kaiserslautern, Germany
关键词
chaperones; membranes; protein folding; protein import; TIM; TOM; translocases;
D O I
10.1146/annurev.biochem.76.052705.163409
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
About 10% to 15% of the nuclear genes of eukaryotic organisms encode mitochondrial proteins. These proteins are synthesized in the cytosol and recognized by receptors on the surface of mitochondria. Translocases in the outer and inner membrane of mitochondria mediate the import and intramitochondrial sorting of these proteins; ATP and the membrane potential are used as energy sources. Chaperones and auxilliary factors assist in the folding and assembly of mitochondrial proteins into their native, three-dimensional structures. This review summarizes the present knowledge on the import and sorting of mitochondrial precursor proteins, with a special emphasis on unresolved questions and topics of current research.
引用
收藏
页码:723 / 749
页数:27
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