Mitochondrial-type assembly of FeS centers in the hydrogenosomes of the amitochondriate eukaryote Trichomonas vaginalis.
Mitochondria are the site of assembly of FeS centers of mitochondrial and cytosolic FeS proteins. Various microaerophilic or anaerobic unicellular eukaryotes lack typical mitochondria ("amitochondriate" protists). In some of these organisms, a metabolically different organelle, the hydrogenosome, is found, which is thought to derive from the same proteobacterial ancestor as mitochondria. Here, we show that hydrogenosomes of Trichomonas vaginalis, a human genitourinary parasite, contain a key enzyme of FeS center biosynthesis, cysteine desulfurase (TviscS-2), which is phylogenetically related to its mitochondrial homologs. Hydrogenosomes catalyze the enzymatic assembly and insertion of FeS centers into apoproteins, as shown by the reconstruction of the apoform of [2Fe-2S]ferredoxin and the incorporation of 35S from labeled cysteine. Our results indicate that the biosynthesis of FeS proteins is performed by a homologous system in mitochondriate and amitochondriate eukaryotes and that this process is inherited from the proteobacterial ancestor of mitochondria.
Sutak
Robert
R
Department of Parasitology, Faculty of Science, Charles University, Vinicna 7, 128 44 Prague 2, Czech Republic.
Dolezal
Pavel
P
Fiumera
Heather L
HL
Hrdy
Ivan
I
Dancis
Andrew
A
Delgadillo-Correa
Maria
M
Johnson
Patricia J
PJ
Müller
Miklós
M
Tachezy
Jan
J
D000818:Animals; D005288:Ferredoxins / Q000235:genetics* / Q000378:metabolism*; D006859:Hydrogen / Q000378:metabolism; D008928:Mitochondria; D008969:Molecular Sequence Data; D015388:Organelles / Q000502:physiology*; D015800:Protozoan Proteins / Q000235:genetics / Q000378:metabolism; D014158:Transcription, Genetic; D014246:Trichomonas vaginalis / Q000235:genetics* / Q000648:ultrastructure
D005288:Ferredoxins; D015800:Protozoan Proteins; D006859:Hydrogen