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Idiosyncrasies in decoding mitochondrial genomes

Authors :
Cyrille Megel
Anne-Marie Duchêne
Daphné Laporte
Marie Sissler
Jonathan L. Huot
Loukmane Karim
Hubert Dominique Becker
Laurence Maréchal-Drouard
Ludovic Enkler
Génétique moléculaire, génomique, microbiologie (GMGM)
Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS)
Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)
Architecture et réactivité de l'ARN (ARN)
Architecture et Réactivité de l'ARN (ARN)
Institut de biologie moléculaire et cellulaire (IBMC)
Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)
Institut de biologie moléculaire des plantes (IBMP)
Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)
Source :
Biochimie, Biochimie, Elsevier, 2014, 100, pp.95-106. ⟨10.1016/j.biochi.2014.01.004⟩, Biochimie, Elsevier, 2014, 100, pp.95-106
Publication Year :
2013

Abstract

Mitochondria originate from the α-proteobacterial domain of life. Since this unique event occurred, mitochondrial genomes of protozoans, fungi, plants and metazoans have highly derived and diverged away from the common ancestral DNA. These resulting genomes highly differ from one another, but all present-day mitochondrial DNAs have a very reduced coding capacity. Strikingly however, ATP production coupled to electron transport and translation of mitochondrial proteins are the two common functions retained in all mitochondrial DNAs. Paradoxically, most components essential for these two functions are now expressed from nuclear genes. Understanding how mitochondrial translation evolved in various eukaryotic models is essential to acquire new knowledge of mitochondrial genome expression. In this review, we provide a thorough analysis of the idiosyncrasies of mitochondrial translation as they occur between organisms. We address this by looking at mitochondrial codon usage and tRNA content. Then, we look at the aminoacyl-tRNA-forming enzymes in terms of peculiarities, dual origin, and alternate function(s). Finally we give examples of the atypical structural properties of mitochondrial tRNAs found in some organisms and the resulting adaptive tRNA-protein partnership.

Details

ISSN :
16386183 and 03009084
Volume :
100
Database :
OpenAIRE
Journal :
Biochimie
Accession number :
edsair.doi.dedup.....8d4b420df00a17856ac6b9ba77d373e0
Full Text :
https://doi.org/10.1016/j.biochi.2014.01.004⟩