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Int. J. Mol. Sci. 2009, 10(5), 2041-2053; doi: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
Keywords: Tim14 (also known as Pam18); Tim16 (also known as Pam16); mtHsp70; translocation motor Tim14 (also known as Pam18); Tim16 (also known as Pam16); mtHsp70; translocation motor
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

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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