Mitochondrial and Nucleolar Localization of Cysteine Desulfurase Nfs and the Scaffold Protein Isu in Trypanosoma brucei

0429400 - BC 2015 RIV US eng J - Journal Article
Kovářová, Julie - Horáková, Eva - Changmai, Piya - Vancová, Marie - Lukeš, Julius
Mitochondrial and Nucleolar Localization of Cysteine Desulfurase Nfs and the Scaffold Protein Isu in Trypanosoma brucei.
Eukaryotic Cell. Roč. 13, č. 3 (2014), s. 353-362. ISSN 1535-9778
R&D Projects: GA ČR(CZ) GAP305/11/2179; GA MŠMT LH12104; GA MŠMT(CZ) EE2.3.30.0032
Institutional support: RVO:60077344
Keywords : transfer RNA * iron sulfur protein * blood stream forms
Subject RIV: EB - Genetics ; Molecular Biology
Impact factor: 2.820, year: 2014

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.
Permanent Link: http://hdl.handle.net/11104/0234520