Mitochondrial-type assembly of FeS centers in the hydrogenosomes of the amitochondriate eukaryote Trichomonas vaginalis
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem, Research Support, U.S. Gov't, P.H.S.
Grantová podpora
R01 DK053953
NIDDK NIH HHS - United States
GM65664
NIGMS NIH HHS - United States
DK53953
NIDDK NIH HHS - United States
R01 AI011942
NIAID NIH HHS - United States
R01 AI027857
NIAID NIH HHS - United States
F32 GM065664
NIGMS NIH HHS - United States
AI11942
NIAID NIH HHS - United States
AI27857
NIAID NIH HHS - United States
R37 DK053953
NIDDK NIH HHS - United States
R37 AI027857
NIAID NIH HHS - United States
PubMed
15226492
PubMed Central
PMC478578
DOI
10.1073/pnas.0401319101
PII: 0401319101
Knihovny.cz E-zdroje
- MeSH
- ferredoxiny genetika metabolismus MeSH
- genetická transkripce MeSH
- mitochondrie MeSH
- molekulární sekvence - údaje MeSH
- organely fyziologie MeSH
- protozoální proteiny genetika metabolismus MeSH
- Trichomonas vaginalis genetika ultrastruktura MeSH
- vodík metabolismus MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Research Support, U.S. Gov't, P.H.S. MeSH
- Názvy látek
- ferredoxiny MeSH
- protozoální proteiny MeSH
- vodík MeSH
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.
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