Adaptation of aminoacylation identity rules to mammalian mitochondria - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Biochimie Année : 2012

Adaptation of aminoacylation identity rules to mammalian mitochondria

Aurélie Fender
  • Fonction : Auteur
Agnès Gaudry
  • Fonction : Auteur
Frank Jühling
  • Fonction : Auteur
Marie Sissler
Catherine Florentz
  • Fonction : Auteur

Résumé

Many mammalian mitochondrial aminoacyl-tRNA synthetases are of bacterial-type and share structural domains with homologous bacterial enzymes of the same specificity. Despite this high similarity, synthetases from bacteria are known for their inability to aminoacylate mitochondrial tRNAs, while mitochondrial enzymes do aminoacylate bacterial tRNAs. Here, the reasons for non-aminoacylation by a bacterial enzyme of a mitochondrial tRNA have been explored. A mutagenic analysis performed on in vitro transcribed human mitochondrial tRNA(Asp) variants tested for their ability to become aspartylated by Escherichia coli aspartyl-tRNA synthetase, reveals that full conversion cannot be achieved on the basis of the currently established tRNA/synthetase recognition rules. Integration of the full set of aspartylation identity elements and stabilization of the structural tRNA scaffold by restoration of D- and T-loop interactions, enable only a partial gain in aspartylation efficiency. The sequence context and high structural instability of the mitochondrial tRNA are additional features hindering optimal adaptation of the tRNA to the bacterial enzyme. Our data support the hypothesis that non-aminoacylation of mitochondrial tRNAs by bacterial synthetases is linked to the large sequence and structural relaxation of the organelle encoded tRNAs, itself a consequence of the high rate of mitochondrial genome divergence.

Dates et versions

hal-03365931 , version 1 (05-10-2021)

Identifiants

Citer

Aurélie Fender, Agnès Gaudry, Frank Jühling, Marie Sissler, Catherine Florentz. Adaptation of aminoacylation identity rules to mammalian mitochondria. Biochimie, 2012, 94 (5), pp.1090-1097. ⟨10.1016/j.biochi.2012.02.030⟩. ⟨hal-03365931⟩

Collections

CNRS
1 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More