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MBE Advance Access published online on September 28, 2007
Molecular Biology and Evolution, doi:10.1093/molbev/msm211
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© The Author 2007. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Research Article

The Tetratricopeptide Repeats of Receptors Involved in Protein Translocation Across Membranes

Thomas Schlegel1,*, Oliver Mirus2,*, Arndt von Haeseler1 and Enrico Schleiff2,3

1 Center for Integrative Bioinformatics Vienna, Max F. Perutz Laboratories, University of Vienna, Medical University of Vienna, Veterinary University of Vienna, Austria
2 Botanik, LMU München, Menzinger Str. 67, D-80638 München Germany

3 corresponding author, Enrico Schleiff, Botanik, LMU München, Menzinger Str. 67, Room 223, 80638 München, Germany, Tel.: +49-89-17861-182, Fax: +49-89-17861-185, E-mail: schleiff{at}lrz.uni-muenchen.de

Received for publication July 20, 2007. Revision received September 17, 2007. Accepted for publication September 24, 2007.

Transport of polypeptides across membranes is a general and essential process in every cell. This process is utilized by molecular machines composed of soluble and membrane inserted proteins. At least one component of the molecular transport machines present in different membranes contains a subunit with a domain composed of three tetratricopeptide repeat (TPR) motifs. These domains are important for protein-protein interaction, e.g. recognition of chaperones. To understand the evolution of these TPR domain-containing receptors involved in protein translocation, we inferred their phylogenetic relationships. We show that the evolutionary rate of these TPR domains is reduced when compared to the remaining sequence. The reduction is explained by the interaction of the TPR domains with their substrates. Based on the TPR tree, we propose that Sec72 recognizes Hsp70 and that Tom34 recognizes Hsp90. The phylogeny can further be used to assign the localization of the Toc64 isoforms to mitochondria or chloroplasts. Our findings are discussed in the context of the evolutionary development of translocation systems with focus on the occurrence of Hsp70/Hsp90-recognizing TPR domains in these machineries.

Key Words: Tom70 • Tom34 • Sec72 • Pex5 • Toc64 • Hop • mitochondria • peroxisomes • chloroplasts • endoplasmic reticulum

* both authors contributed to the same extent


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