期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 101, 期 28, 页码 10368-10373出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0401319101
关键词
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资金
- NIAID NIH HHS [R01 AI011942, R37 AI027857, AI11942, AI27857, R01 AI027857] Funding Source: Medline
- NIDDK NIH HHS [R37 DK053953, R01 DK053953, DK53953] Funding Source: Medline
- NIGMS NIH HHS [F32 GM065664, GM65664] Funding Source: Medline
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 proteolbacterial 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-25]ferredoxin and the incorporation of S-35 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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