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Článek

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PubMed

Záznam pochází z PubMed

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

Eukaryotic cell. 2007 Aug ; 6 (8) : 1431-8. [epub] 20070615

Eukaryot Cell
ISSN 1535-9778 | 1535-9786
Zdroj

Jazyk angličtina Země Spojené státy americké Médium print-electronic

Typ dokumentu časopisecké články, Research Support, N.I.H., Extramural, práce podpořená grantem

Perzistentní odkaz https://www.medvik.cz/link/pmid17573543

Grantová podpora
R01 DK053953 NIDDK NIH HHS - United States
R37 DK053953 NIDDK NIH HHS - United States
060068 Wellcome Trust - United Kingdom
DK53953 NIDDK NIH HHS - United States

Online Plný text

PubMed 17573543
PubMed Central PMC1951141
DOI 10.1128/ec.00027-07
PII: EC.00027-07
Knihovny.cz E-zdroje

MeSH
frataxin MeSH
genetická transkripce MeSH
konzervovaná sekvence MeSH
mitochondriální proteiny genetika metabolismus MeSH
molekulární modely MeSH
molekulární sekvence - údaje MeSH
organely metabolismus MeSH
proteiny vázající železo genetika metabolismus MeSH
sekvence aminokyselin MeSH
sekvenční seřazení MeSH
Trichomonas vaginalis genetika metabolismus MeSH
zvířata MeSH
Check Tag
zvířata MeSH
Publikační typ
časopisecké články MeSH
práce podpořená grantem MeSH
Research Support, N.I.H., Extramural MeSH
Názvy látek
frataxin MeSH
mitochondriální proteiny MeSH
proteiny vázající železo MeSH

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-beta 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.

Department of Parasitology Charles University Faculty of Science Vinicna 7 128 44 Prague Czech Republic

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