Mitochondrial-type assembly of FeS centers in the hydrogenosomes of the amitochondriate eukaryote Trichomonas vaginalis

. 2004 Jul 13 ; 101 (28) : 10368-73. [epub] 20040629

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.

Perzistentní odkaz   https://www.medvik.cz/link/pmid15226492

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

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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