Mitochondrial and nucleolar localization of cysteine desulfurase Nfs and the scaffold protein Isu in Trypanosoma brucei
Autor: | Julius Lukeš, Julie Kovářová, Eva Horáková, Piya Changmai, Marie Vancová |
---|---|
Rok vydání: | 2013 |
Předmět: |
Scaffold protein
Nucleolus Molecular Sequence Data Nuclear Localization Signals Trypanosoma brucei brucei Active Transport Cell Nucleus Protozoan Proteins Biology Trypanosoma brucei Mitochondrion Microbiology environment and public health Mitochondrial Proteins Nuclear Matrix-Associated Proteins Iron-Binding Proteins parasitic diseases medicine Amino Acid Sequence Molecular Biology Cell Nucleus Cysteine desulfurase fungi General Medicine Articles biology.organism_classification Cell biology Mitochondria Cell nucleus Cytosol Carbon-Sulfur Lyases medicine.anatomical_structure Biochemistry Frataxin biology.protein Ferredoxins Protein Multimerization Protein Binding |
Zdroj: | Eukaryotic cell. 13(3) |
ISSN: | 1535-9786 |
Popis: | Trypanosoma brucei has a complex life cycle during which its single mitochondrion is subjected to major metabolic and morphological changes. While the procyclic stage (PS) of the insect vector contains a large and reticulated mitochondrion, its counterpart in the bloodstream stage (BS) parasitizing mammals is highly reduced and seems to be devoid of most functions. We show here that key Fe-S cluster assembly proteins are still present and active in this organelle and that produced clusters are incorporated into overexpressed enzymes. Importantly, the cysteine desulfurase Nfs, equipped with the nuclear localization signal, was detected in the nucleolus of both T. brucei life stages. The scaffold protein Isu, an interacting partner of Nfs, was also found to have a dual localization in the mitochondrion and the nucleolus, while frataxin and both ferredoxins are confined to the mitochondrion. Moreover, upon depletion of Isu, cytosolic tRNA thiolation dropped in the PS but not BS parasites. |
Databáze: | OpenAIRE |
Externí odkaz: |