Int. J. Mol. Sci. 2009, 10(5), 2041-2053; https://doi.org/10.3390/ijms10052041
The Mitochondrial Protein Translocation Motor: Structural Conservation between the Human and Yeast Tim14/Pam18-Tim16/Pam16 co-Chaperones
Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel
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Received: 14 March 2009 / Revised: 11 April 2009 / Accepted: 14 April 2009 / Published: 6 May 2009
(This article belongs to the Special Issue Protein Folding 2009)
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Abstract
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. View Full-Text
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Elsner, S.; Simian, D.; Iosefson, O.; Marom, M.; Azem, A. The Mitochondrial Protein Translocation Motor: Structural Conservation between the Human and Yeast Tim14/Pam18-Tim16/Pam16 co-Chaperones. Int. J. Mol. Sci. 2009, 10, 2041-2053.
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