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

0347296 - BC 2011 RIV US eng J - Článek v odborném periodiku
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
Grant CEP: GA ČR GA204/09/1667
Výzkumný záměr: CEZ:AV0Z60220518
Klíčová slova: IRON-SULFUR PROTEINS * SACCHAROMYCES-CEREVISIAE * CYSTEINE DESULFURASE * THIO-MODIFICATION * FRATAXIN
Kód oboru RIV: EB - Genetika a molekulární biologie
Impakt faktor: 5.328, rok: 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.
Trvalý link: http://hdl.handle.net/11104/0188102