Frataxin, a conserved mitochondrial protein in hydrogenosome of Trichomonas vaginalis. - Université Paris Cité Accéder directement au contenu
Article Dans Une Revue Eukaryotic Cell Année : 2007

Frataxin, a conserved mitochondrial protein in hydrogenosome of Trichomonas vaginalis.

Résumé

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 (Tvfrataxin) from the human parasite Trichomonas vaginalis. Instead of mitochondria, this unicellular eukaryote possesses hydrogenosomes, peculiar organelles that make hydrogen but nevertheless share common ancestry with mitochondria. Tvfrataxin contains conserved residues implicated in iron binding, and in silico it is predicted to form a typical alpha-beta-sandwich motif. The short N-terminal extension of Tvfrataxin resembles presequences that target proteins to hydrogenosomes, a prediction confirmed by overexpression of Tvfrataxin in T. vaginalis. When expressed in the mitochondria of a frataxin deficient Saccharomyces cerevisiae strain, Tvfrataxin 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, Tvfrataxin was also shown to interact with S. cerevisiae ferrochelatase 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.

Dates et versions

hal-00159114 , version 1 (02-07-2007)

Identifiants

Citer

Pavel Dolezal, Andrew Dancis, Emmanuel Lesuisse, Róbert Sutak, Ivan Hrdý, et al.. Frataxin, a conserved mitochondrial protein in hydrogenosome of Trichomonas vaginalis.. Eukaryotic Cell, 2007, Sous presse (?), ⟨10.1128/EC.00027-07⟩. ⟨hal-00159114⟩
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