Translational 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, Gln-tRNAGln 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 glutamyl-tRNAGln amidotransferase), which are able to catalyse the formation of Gln-tRNAGlnin vitro. In the present paper we demonstrate that mgatA (mouse GatA) interference in mouse 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 Glu-tRNAGln is rejected from the translational apparatus to maintain the fidelity of mitochondrial protein synthesis in mammals.
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Research Article|
April 25 2014
Glutamyl-tRNAGln amidotransferase is essential for mammalian mitochondrial translation in vivo
Lucía Echevarría;
Lucía Echevarría
1
*Departamento de Bioquímica, Instituto de Investigaciones Biomédicas “Alberto Sols” UAM-CSIC, Centro de Investigación Biomédica en Red en Enfermedades Raras (CIBERER), Facultad de Medicina, Universidad Autónoma de Madrid, Madrid, Spain
†Instituto de Investigación Sanitaria 12 de Octubre (i+12), Madrid, Spain
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Paula Clemente;
Paula Clemente
2
*Departamento de Bioquímica, Instituto de Investigaciones Biomédicas “Alberto Sols” UAM-CSIC, Centro de Investigación Biomédica en Red en Enfermedades Raras (CIBERER), Facultad de Medicina, Universidad Autónoma de Madrid, Madrid, Spain
†Instituto de Investigación Sanitaria 12 de Octubre (i+12), Madrid, Spain
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Rosana Hernández-Sierra;
Rosana Hernández-Sierra
*Departamento de Bioquímica, Instituto de Investigaciones Biomédicas “Alberto Sols” UAM-CSIC, Centro de Investigación Biomédica en Red en Enfermedades Raras (CIBERER), Facultad de Medicina, Universidad Autónoma de Madrid, Madrid, Spain
†Instituto de Investigación Sanitaria 12 de Octubre (i+12), Madrid, Spain
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María Esther Gallardo;
María Esther Gallardo
*Departamento de Bioquímica, Instituto de Investigaciones Biomédicas “Alberto Sols” UAM-CSIC, Centro de Investigación Biomédica en Red en Enfermedades Raras (CIBERER), Facultad de Medicina, Universidad Autónoma de Madrid, Madrid, Spain
†Instituto de Investigación Sanitaria 12 de Octubre (i+12), Madrid, Spain
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Miguel A. Fernández-Moreno;
Miguel A. Fernández-Moreno
3
*Departamento de Bioquímica, Instituto de Investigaciones Biomédicas “Alberto Sols” UAM-CSIC, Centro de Investigación Biomédica en Red en Enfermedades Raras (CIBERER), Facultad de Medicina, Universidad Autónoma de Madrid, Madrid, Spain
†Instituto de Investigación Sanitaria 12 de Octubre (i+12), Madrid, Spain
3Correspondence may be addressed to either of these authors (email miguel.fernandez@uam.es or rafael.garesse@uam.es).
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Rafael Garesse
Rafael Garesse
3
*Departamento de Bioquímica, Instituto de Investigaciones Biomédicas “Alberto Sols” UAM-CSIC, Centro de Investigación Biomédica en Red en Enfermedades Raras (CIBERER), Facultad de Medicina, Universidad Autónoma de Madrid, Madrid, Spain
†Instituto de Investigación Sanitaria 12 de Octubre (i+12), Madrid, Spain
3Correspondence may be addressed to either of these authors (email miguel.fernandez@uam.es or rafael.garesse@uam.es).
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Publisher: Portland Press Ltd
Received:
August 20 2013
Revision Received:
February 14 2014
Accepted:
March 03 2014
Accepted Manuscript online:
March 03 2014
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2014 Biochemical Society
2014
Biochem J (2014) 460 (1): 91–101.
Article history
Received:
August 20 2013
Revision Received:
February 14 2014
Accepted:
March 03 2014
Accepted Manuscript online:
March 03 2014
Citation
Lucía Echevarría, Paula Clemente, Rosana Hernández-Sierra, María Esther Gallardo, Miguel A. Fernández-Moreno, Rafael Garesse; Glutamyl-tRNAGln amidotransferase is essential for mammalian mitochondrial translation in vivo. Biochem J 15 May 2014; 460 (1): 91–101. doi: https://doi.org/10.1042/BJ20131107
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