Mitochondrial-type iron-sulfur cluster biosynthesis genes (IscS and IscU) in the apicomplexan Cryptosporidium parvum
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, U.S. Gov't, P.H.S.
Grant support
1D43 TWO 0091
FIC NIH HHS - United States
5R03-TWO 1507-02
FIC NIH HHS - United States
5R03-TWO 5536-02
FIC NIH HHS - United States
PubMed
14663084
DOI
10.1099/mic.0.26365-0
Knihovny.cz E-resources
- MeSH
- Cryptosporidium parvum genetics metabolism MeSH
- Gene Expression MeSH
- Phylogeny MeSH
- Cloning, Molecular MeSH
- Luminescent Proteins genetics metabolism MeSH
- Mitochondria metabolism MeSH
- Molecular Sequence Data MeSH
- Protein Sorting Signals genetics MeSH
- Iron-Sulfur Proteins biosynthesis genetics MeSH
- DNA, Protozoan genetics MeSH
- Genes, Protozoan * MeSH
- Protozoan Proteins biosynthesis genetics MeSH
- Recombinant Fusion Proteins genetics metabolism MeSH
- Amino Acid Sequence MeSH
- Base Sequence MeSH
- Sequence Homology, Amino Acid MeSH
- Green Fluorescent Proteins MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, U.S. Gov't, P.H.S. MeSH
- Names of Substances
- Luminescent Proteins MeSH
- Protein Sorting Signals MeSH
- Iron-Sulfur Proteins MeSH
- DNA, Protozoan MeSH
- Protozoan Proteins MeSH
- Recombinant Fusion Proteins MeSH
- Green Fluorescent Proteins MeSH
Several reports have indicated that the iron-sulfur cluster [Fe-S] assembly machinery in most eukaryotes is confined to the mitochondria and chloroplasts. The best-characterized and most highly conserved [Fe-S] assembly proteins are a pyridoxal-5'-phosphate-dependent cysteine desulfurase (IscS), and IscU, a protein functioning as a scaffold for the assembly of [Fe-S] prior to their incorporation into apoproteins. In this work, genes encoding IscS and IscU homologues have been isolated and characterized from the apicomplexan parasite Cryptosporidium parvum, an opportunistic pathogen in AIDS patients, for which no effective treatment is available. Primary sequence analysis (CpIscS and CpIscU) and phylogenetic studies (CpIscS) indicate that both genes are most closely related to mitochondrial homologues from other organisms. Moreover, the N-terminal signal sequences of CpIscS and CpIscU predicted in silico specifically target green fluorescent protein to the mitochondrial network of the yeast Saccharomyces cerevisiae. Overall, these findings suggest that the previously identified mitochondrial relict of C. parvum may have been retained by the parasite as an intracellular site for [Fe-S] assembly.
1st Faculty of Medicine Charles University Prague Czech Republic
Department of Parasitology Faculty of Science Charles University Prague Czech Republic
Wadsworth Center New York State Department of Health PO Box 22002 Albany NY 12201 2002 USA
References provided by Crossref.org
Frataxin, a conserved mitochondrial protein, in the hydrogenosome of Trichomonas vaginalis
GENBANK
AY029212, AY078500
