How mitochondria import hydrophilic and hydrophobic proteins

被引：47
作者：
Chacinska, A [1 ]
Pfanner, N [1 ]
Meisinger, C [1 ]
机构：
[1] Univ Freiburg, Inst Biochem & Mol Biol, D-79104 Freiburg, Germany
来源：
TRENDS IN CELL BIOLOGY | 2002年 / 12卷 / 07期
关键词：
D O I：
10.1016/S0962-8924(02)02310-3
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
Most mitochondrial proteins are nuclear encoded and have to be transported into the organelle after synthesis on cytosolic ribosomes. Three multimeric protein complexes have been identified that import precursor proteins destined for the mitochondria: the TOM complex in the outer membrane and two TIM complexes in the inner membrane. Recent work has provided a detailed view of the different mechanisms operating during the import of the two major classes of mitochondrial proteins - hydrophilic proteins with cleavable presequences and hydrophobic proteins with multiple internal signals.
引用
收藏
页码：299 / 303
页数：5
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