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Abstract：
The translocases of the mitochondrial outer and inner membranes, the TOM and TIMs, import hundreds of nucleus-encoded proteins into mitochondria. TOM and TIMs are multi-subunit protein complexes that work in cooperation with other complexes to import proteins in different sub-mitochondrial destinations. The overall architecture of these protein complexes is conserved among yeast/fungi, animals, and plants. Recent studies have revealed unique characteristics of this machinery, particularly in the eukaryotic supergroup Excavata. Despite multiple differences, homologues of Tim17, an essential component of one of the TIM complexes and a member of the Tim17/Tim22/Tim23 family, have been found in all eukaryotes. Here, we review the structure and function of Tim17 and Tim17-containing protein complexes in different eukaryotes, and then compare them to the single homologue of this protein found in Trypanosoma brucei, a unicellular parasitic protozoan.
摘要：
线粒体外膜和内膜的移位酶，TOM和TIM,将数百种细胞核编码的蛋白质导入线粒体。TOM和TIM是多亚基蛋白质复合物，可与其他复合物协同工作，以在不同的亚线粒体目的地导入蛋白质。这些蛋白质复合物的整体结构在酵母/真菌中是保守的，动物,和植物。最近的研究揭示了这种机器的独特特征，特别是在真核超群Excavata中。尽管存在多重差异,Tim17的同系物，是TIM复合物之一的重要组成部分，也是Tim17/Tim22/Tim23家族的成员，在所有的真核生物中都有发现.这里,我们回顾了Tim17和含Tim17的蛋白质复合物在不同真核生物中的结构和功能，然后将它们与在布鲁氏锥虫中发现的这种蛋白质的单一同源物进行比较，单细胞寄生原生动物。
