Mitochondrial type iron-sulfur cluster assembly in the amitochondriate eukaryotes Trichomonas vaginalis and Giardia intestinalis, as indicated by the phylogeny of IscS
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.
Grant support
AI11942
NIAID NIH HHS - United States
- MeSH
- Bacterial Proteins genetics MeSH
- Phylogeny * MeSH
- Giardia lamblia enzymology genetics MeSH
- Carbon-Sulfur Lyases genetics metabolism MeSH
- Mitochondria metabolism MeSH
- Molecular Sequence Data MeSH
- Iron-Sulfur Proteins biosynthesis MeSH
- DNA, Protozoan chemistry genetics MeSH
- Amino Acid Sequence MeSH
- Sequence Analysis, DNA MeSH
- Sequence Homology, Amino Acid MeSH
- Sequence Alignment MeSH
- Trichomonas vaginalis enzymology genetics MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Research Support, U.S. Gov't, P.H.S. MeSH
- Names of Substances
- Bacterial Proteins MeSH
- cysteine desulfurase MeSH Browser
- Carbon-Sulfur Lyases MeSH
- nifS protein, Bacteria MeSH Browser
- Iron-Sulfur Proteins MeSH
- DNA, Protozoan MeSH
Pyridoxal-5'-phosphate-dependent cysteine desulfurase (IscS) is an essential enzyme in the assembly of FeS clusters in bacteria as well as in the mitochondria of eukaryotes. Although FeS proteins are particularly important for the energy metabolism of amitochondrial anaerobic eukaryotes, there is no information about FeS cluster formation in these organisms. We identified and sequenced two IscS homologs of Trichomonas vaginalis (TviscS-1 and TviscS-2) and one of Giardia intestinalis (GiiscS). TviscS-1, TviscS-2, and GiiscS possess the typical conserved regions implicated in cysteine desulfurase activity. N-termini of TviscS-1 and TviscS-2 possess eight amino acid extensions, which resemble the N-terminal presequences that target proteins to hydrogenosomes in trichomonads. No presequence was evident in GiiscS from Giardia, an organism that apparently lacks hydrogenosmes or mitochondria. Phylogenetic analysis showed a close relationship among all eukaryotic IscS genes including those of amitochondriates. IscS of proteobacteria formed a sister group to the eukaryotic clade, suggesting that isc-related genes were present in the proteobacterial endosymbiotic ancestor of mitochondria and hydrogenosomes. NifS genes of nitrogen-fixing bacteria, which are IscS homologs required for specific formation of FeS clusters in nitrogenase, formed a more distant group. The phylogeny indicates the presence of a common mechanism for FeS cluster formation in mitochondriates as well as in amitochondriate eukaryotes. Furthermore, the analyses support a common origin of Trichomonas hydrogenosomes and mitochondria, as well as secondary loss of mitochondrion/hydrogenosome-like organelles in Giardia.
References provided by Crossref.org
Fe-S Cluster Assembly in Oxymonads and Related Protists
Fe-S cluster assembly in the supergroup Excavata
Probing the Biology of Giardia intestinalis Mitosomes Using In Vivo Enzymatic Tagging
Iron-induced changes in the proteome of Trichomonas vaginalis hydrogenosomes
The minimal proteome in the reduced mitochondrion of the parasitic protist Giardia intestinalis
Frataxin, a conserved mitochondrial protein, in the hydrogenosome of Trichomonas vaginalis
Giardia mitosomes and trichomonad hydrogenosomes share a common mode of protein targeting
GENBANK
AF311744, AF321005, AF321006
