Frataxin, a Conserved Mitochondrial Protein, in the Hydrogenosome of Trichomonas vaginalis
- 1 August 2007
- journal article
- Published by American Society for Microbiology in Eukaryotic Cell
- Vol. 6 (8), 1431-1438
- https://doi.org/10.1128/ec.00027-07
Abstract
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 α-β 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.Keywords
This publication has 48 references indexed in Scilit:
- Draft Genome Sequence of the Sexually Transmitted Pathogen Trichomonas vaginalisScience, 2007
- The role of iron regulatory proteins in mammalian iron homeostasis and diseaseNature Chemical Biology, 2006
- Assembly of Human Frataxin Is a Mechanism for Detoxifying Redox-Active IronBiochemistry, 2004
- Zinc suppresses the iron-accumulation phenotype of Saccharomyces cerevisiae lacking the yeast frataxin homologue (Yfh1)Biochemical Journal, 2003
- SWISS-MODEL: an automated protein homology-modeling serverNucleic Acids Research, 2003
- Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculiNature, 2001
- Unusual diversity in α-amanitin sensitivity of RNA polymerases in trichomonadsMolecular and Biochemical Parasitology, 2001
- Respiratory deficiency due to loss of mitochondrial DNA in yeast lacking the frataxin homologueNature Genetics, 1997
- Probing the Active-site Residues in Saccharomyces cerevisiae Ferrochelatase by Directed MutagenesisPublished by Elsevier BV ,1996
- Iron storage in Saccharomyces cerevisiaeFEBS Letters, 1988