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Título

Glutamyl-tRNAGln amidotransferase is essential for mammalian mitochondrial translation in vivo

AutorEchevarría, Lucía; Clemente, Paula; Hernández-Sierra, Rosana ; Gallardo, M. Esther ; Fernández-Moreno, Miguel Ángel ; Garesse, Rafael
Fecha de publicación2014
EditorBiochemical Society
CitaciónBiochemical Journal 460(1): 91-101 (2014)
ResumenTranslational accuracy depends on the correct formation of aminoacyl-tRNAs, which, in the majority of cases, are produced by specific aminoacyl-tRNA synthetases that ligate each amino acid to its cognate isoaceptor tRNA. Aminoacylation of tRNAGln, however, is performed by various mechanisms in different systems. Since no mitochondrial glutaminyl-tRNA synthetase has been identified to date in mammalian mitochondria, GlntRNAGln has to be formed by an indirect mechanism in the organelle. It has been demonstrated that human mitochondria contain a non-discriminating glutamyl-tRNA synthetase and the heterotrimeric enzyme GatCAB (where Gat is glutamyltRNAGln amidotransferase), which are able to catalyse the formation of Gln-tRNAGln in vitro. In the present paper we demonstrate that mgatA (mouse GatA) interference inmouse cells produces a strong defect in mitochondrial translation without affecting the stability of the newly synthesized proteins. As a result, interfered cells present an impairment of the oxidative phosphorylation system and a significant increase in ROS (reactive oxygen species) levels. MS analysis of mitochondrial proteins revealed no glutamic acid found in the position of glutamines, strongly suggesting that misaminoacylated GlutRNAGln is rejected from the translational apparatus to maintain the fidelity of mitochondrial protein synthesis in mammals.
URIhttp://hdl.handle.net/10261/124498
DOI10.1042/BJ20131107
Identificadoresdoi: 10.1042/BJ20131107
issn: 0264-6021
e-issn: 1470-8728
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