Format

Send to

Choose Destination
Biochimie. 2014 May;100:95-106. doi: 10.1016/j.biochi.2014.01.004. Epub 2014 Jan 16.

Idiosyncrasies in decoding mitochondrial genomes.

Author information

1
Unité Mixte de Recherche 7156, Génétique Moléculaire, Génomique, Microbiologie, CNRS, Université de Strasbourg, 21, rue René Descartes, 67084 Strasbourg, France.
2
Institut de Biologie Moléculaire des Plantes, IBMP, CNRS, conventionné avec l'Université de Strasbourg, 12 rue du Général Zimmer, 67084 Strasbourg, France.
3
Architecture et Réactivité de l'ARN, IBMC, CNRS, conventionné avec l'Université de Strasbourg, 15 rue René Descartes, 67084 Strasbourg, France.
4
Institut de Biologie Moléculaire des Plantes, IBMP, CNRS, conventionné avec l'Université de Strasbourg, 12 rue du Général Zimmer, 67084 Strasbourg, France. Electronic address: laurence.drouard@ibmp-cnrs.unistra.fr.

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.

KEYWORDS:

Aminoacyl-tRNA synthetase; Codon usage; Mitochondria; Transfer RNA

PMID:
24440477
DOI:
10.1016/j.biochi.2014.01.004
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center