The Mitochondrial Protein Translocation Motor: Structural Conservation between the Human and Yeast Tim14/Pam18-Tim16/Pam16 co-Chaperones
The Mitochondrial Protein Translocation Motor: Structural Conservation between the Human and Yeast Tim14/Pam18-Tim16/Pam16 co-Chaperones
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DOI：
10.3390/ijms10052041
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发表时间：
2009-05-01
影响因子：
5.6
通讯作者：
Azem, Abdussalam
中科院分区：
文献类型：
--
作者：
Elsner, Shira;Simian, Dana;Azem, Abdussalam
我们关于蛋白质输入线粒体过程的大部分知识来自于以酿酒酵母为模型系统的研究。最近，一些哺乳动物线粒体运动蛋白的同源物被鉴定出来。我们特别感兴趣的是人类Tim14/Pam18-Tim16/Pam16复合物。我们选择了一种结构方法来研究酵母Tim14/Pam18-Tim16/Pam16蛋白与其人类同源物之间的进化保守性。为此，我们在体外研究了纯化的人蛋白的结构特性及其与酵母同源物的相互作用。我们的研究结果表明，人类Tim14/Pam18和Tim16/Pam16蛋白的可溶结构域与它们的酵母对应物相互作用，形成异二聚体复合物，这些复合物与酵母mtHsp70相互作用。
Most of our knowledge regarding the process of protein import into mitochondria has come from research employing Saccharomyces cerevisiae as a model system. Recently, several mammalian homologues of the mitochondrial motor proteins were identified. Of particular interest for us is the human Tim14/Pam18-Tim16/Pam16 complex. We chose a structural approach in order to examine the evolutionary conservation between yeast Tim14/Pam18-Tim16/Pam16 proteins and their human homologues. For this purpose, we examined the structural properties of the purified human proteins and their interaction with their yeast homologues, in vitro. Our results show that the soluble domains of the human Tim14/Pam18 and Tim16/Pam16 proteins interact with their yeast counterparts, forming heterodimeric complexes and that these complexes interact with yeast mtHsp70.