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Nucleic Acids Research Advance Access published online on June 29, 2007
Nucleic Acids Research, doi:10.1093/nar/gkm441
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© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Computational Biology

Reconstructing the evolution of the mitochondrial ribosomal proteome

Paulien Smits1, Jan A. M. Smeitink1, Lambert P. van den Heuvel1, Martijn A. Huynen2 and Thijs J. G. Ettema2,*

1Nijmegen Center for Mitochondrial Disorders, Nijmegen Center for Molecular Life Sciences, Radboud University Nijmegen Medical Center, Geert–Grooteplein-Zuid 10 and 2Center for Molecular and Biomolecular Informatics, Nijmegen Center for Molecular Life Sciences, Radboud University Nijmegen Medical Center, Geert-Grooteplein 28, 6525 GA Nijmegen, The Netherlands

*To whom correspondence should be addressed. Email: thijs.ettema{at}ebc.uu.se

Received March 20, 2007. Revised May 16, 2007. Accepted May 17, 2007.

For production of proteins that are encoded by the mitochondrial genome, mitochondria rely on their own mitochondrial translation system, with the mitoribosome as its central component. Using extensive homology searches, we have reconstructed the evolutionary history of the mitoribosomal proteome that is encoded by a diverse subset of eukaryotic genomes, revealing an ancestral ribosome of alpha-proteobacterial descent that more than doubled its protein content in most eukaryotic lineages. We observe large variations in the protein content of mitoribosomes between different eukaryotes, with mammalian mitoribosomes sharing only 74 and 43% of its proteins with yeast and Leishmania mitoribosomes, respectively. We detected many previously unidentified mitochondrial ribosomal proteins (MRPs) and found that several have increased in size compared to their bacterial ancestral counterparts by addition of functional domains. Several new MRPs have originated via duplication of existing MRPs as well as by recruitment from outside of the mitoribosomal proteome. Using sensitive profile–profile homology searches, we found hitherto undetected homology between bacterial and eukaryotic ribosomal proteins, as well as between fungal and mammalian ribosomal proteins, detecting two novel human MRPs. These newly detected MRPs constitute, along with evolutionary conserved MRPs, excellent new screening targets for human patients with unresolved mitochondrial oxidative phosphorylation disorders.

Present address: Thijs J. G. Ettema, Department of Molecular Evolution, Evolutionary Biology Centre, Uppsala University, Norbyvägen 18C, 752 36 Uppsala, Sweden.


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