Roles of the Nfu Fe-S targeting factors in the trypanosome mitochondrion
Jazyk angličtina Země Anglie, Velká Británie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
27181928
DOI
10.1016/j.ijpara.2016.04.006
PII: S0020-7519(16)30067-4
Knihovny.cz E-zdroje
- Klíčová slova
- Fe–S, Iron–sulphur cluster, Mitochondrion, Nfu1, Trypanosoma brucei,
- MeSH
- chemická frakcionace MeSH
- down regulace MeSH
- elektroporace MeSH
- fylogeneze MeSH
- kultivované buňky MeSH
- mitochondriální proteiny fyziologie MeSH
- mitochondrie chemie fyziologie MeSH
- plazmidy MeSH
- proteiny obsahující železo a síru genetika imunologie fyziologie MeSH
- proteiny tepelného šoku HSP70 metabolismus MeSH
- protilátky protozoální biosyntéza MeSH
- protozoální proteiny genetika imunologie fyziologie MeSH
- RNA interference MeSH
- Trypanosoma brucei brucei chemie klasifikace genetika fyziologie MeSH
- výpočetní biologie MeSH
- western blotting MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- mitochondriální proteiny MeSH
- proteiny obsahující železo a síru MeSH
- proteiny tepelného šoku HSP70 MeSH
- protilátky protozoální MeSH
- protozoální proteiny MeSH
Iron-sulphur clusters (ISCs) are protein co-factors essential for a wide range of cellular functions. The core iron-sulphur cluster assembly machinery resides in the mitochondrion, yet due to export of an essential precursor from the organelle, it is also needed for cytosolic and nuclear iron-sulphur cluster assembly. In mitochondria all [4Fe-4S] iron-sulphur clusters are synthesised and transferred to specific apoproteins by so-called iron-sulphur cluster targeting factors. One of these factors is the universally present mitochondrial Nfu1, which in humans is required for the proper assembly of a subset of mitochondrial [4Fe-4S] proteins. Although most eukaryotes harbour a single Nfu1, the genomes of Trypanosoma brucei and related flagellates encode three Nfu genes. All three Nfu proteins localise to the mitochondrion in the procyclic form of T. brucei, and TbNfu2 and TbNfu3 are both individually essential for growth in bloodstream and procyclic forms, suggesting highly specific functions for each of these proteins in the trypanosome cell. Moreover, these two proteins are functional in the iron-sulphur cluster assembly in a heterologous system and rescue the growth defect of a yeast deletion mutant.
Faculty of Chemistry Biochemistry University of Kaiserslautern 67663 Kaiserslautern Germany
Faculty of Sciences University of South Bohemia 370 05 České Budějovice Czech Republic
Citace poskytuje Crossref.org
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