The Fe/S Cluster Assembly Protein Isd11 Is Essential for tRNA Thiolation in Trypanosoma brucei

0347296 - BC 2011 RIV US eng J - Journal Article
Paris, Zdeněk - Changmai, Piya - RUBIO, M. A. T. - Zíková, Alena - Stuart, K. D. - Alfonzo, J. D. - Lukeš, Julius
The Fe/S Cluster Assembly Protein Isd11 Is Essential for tRNA Thiolation in Trypanosoma brucei.
Journal of Biological Chemistry. Roč. 285, č. 29 (2010), s. 22394-22402. ISSN 0021-9258. E-ISSN 1083-351X
R&D Projects: GA ČR GA204/09/1667
Institutional research plan: CEZ:AV0Z60220518
Keywords : IRON-SULFUR PROTEINS * SACCHAROMYCES-CEREVISIAE * CYSTEINE DESULFURASE * THIO-MODIFICATION * FRATAXIN
Subject RIV: EB - Genetics ; Molecular Biology
Impact factor: 5.328, year: 2010

Fe/S clusters are part of the active site of many enzymes and are essential for cell viability. In eukaryotes the cysteine desulfurase Nfs (IscS) donates the sulfur during Fe/S cluster assembly and was thought sufficient for this reaction. Moreover, Nfs is indispensable for tRNA thiolation, a modification generally required for tRNA function and protein synthesis. Recently, Isd11 was discovered as an integral part of the Nfs activity at an early step of Fe/S cluster assembly. Here we show, using a combination of genetic, molecular, and biochemical approaches, that Isd11, in line with its strong association with Nfs, is localized in the mitochondrion of T. brucei. In addition to its involvement in Fe/S assembly, Isd11 also partakes in both cytoplasmic and mitochondrial tRNA thiolation, whereas Mtu1, another protein proposed to collaborate with Nfs in tRNA thiolation, is required for this process solely within the mitochondrion.
Permanent Link: http://hdl.handle.net/11104/0188102