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Eukaryotic Cell, August 2007, p. 1431-1438, Vol. 6, No. 8
1535-9778/07/$08.00+0     doi:10.1128/EC.00027-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Frataxin, a Conserved Mitochondrial Protein, in the Hydrogenosome of Trichomonas vaginalis{triangledown}

Pavel Dolezal,1 Andrew Dancis,2 Emmanuel Lesuisse,3 Róbert Sutak,1 Ivan Hrdy,1 T. Martin Embley,4 and Jan Tachezy1*

Department of Parasitology, Faculty of Science, Charles University in Prague, Vinicna 7, 128 44 Prague 2, Czech Republic,1 Department of Medicine, Division of Hematology-Oncology, University of Pennsylvania, Philadelphia, Pennsylvania 19104,2 Laboratoire d'Ingenierie des Proteines et Controle Metabolique, Departement de Biologie des Genomes, Institut Jacques Monod, Unite Mixte de Recherche 7592 CNRS-Universites Paris 6/7, 2 Place Jussieu, F-75251 Paris cedex 05, France,3 Division of Biology, The Devonshire Building, Newcastle University, Newcastle upon Tyne, NE1 7RU, UK4

Received 23 January 2007/ Accepted 5 June 2007

Recent data suggest that frataxin plays a key role in eukaryote cellular iron metabolism, particularly in mitochondrial heme and iron-sulfur (FeS) cluster biosynthesis. We have now identified a frataxin homologue (T. vaginalis frataxin) from the human parasite Trichomonas vaginalis. Instead of mitochondria, this unicellular eukaryote possesses hydrogenosomes, peculiar organelles that produce hydrogen but nevertheless share common ancestry with mitochondria. T. vaginalis frataxin contains conserved residues implicated in iron binding, and in silico, it is predicted to form a typical {alpha}-ß sandwich motif. The short N-terminal extension of T. vaginalis frataxin resembles presequences that target proteins to hydrogenosomes, a prediction confirmed by the results of overexpression of T. vaginalis frataxin in T. vaginalis. When expressed in the mitochondria of a frataxin-deficient Saccharomyces cerevisiae strain, T. vaginalis frataxin partially restored defects in heme and FeS cluster biosynthesis. Although components of heme synthesis or heme-containing proteins have not been found in T. vaginalis to date, T. vaginalis frataxin was also shown to interact with S. cerevisiae ferrochelatase by using a Biacore assay. The discovery of conserved iron-metabolizing pathways in mitochondria and hydrogenosomes provides additional evidence not only of their common evolutionary history, but also of the fundamental importance of this pathway for eukaryotes.

* Corresponding author. Mailing address: Department of Parasitology, Charles University, Faculty of Science, Vinicna 7, 128 44 Prague, Czech Republic. Phone: (420) 221951813. Fax: (420) 224919704. E-mail: tachezy{at}natur.cuni.cz

{triangledown} Published ahead of print on 15 June 2007.

Eukaryotic Cell, August 2007, p. 1431-1438, Vol. 6, No. 8
1535-9778/07/$08.00+0     doi:10.1128/EC.00027-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Long, S., Jirku, M., Ayala, F. J., Lukes, J. (2008). Mitochondrial localization of human frataxin is necessary but processing is not for rescuing frataxin deficiency in Trypanosoma brucei. Proc. Natl. Acad. Sci. USA 105: 13468-13473 [Abstract] [Full Text]  


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