Publications
2012
Fender A, Gaudry A, Jühling F, Sissler M, Florentz C
Adaptation of aminoacylation identity rules to mammalian mitochondria. Journal Article
In: Biochimie, vol. 94, no. 5, pp. 1090-1097, 2012, ISBN: 22402012, (Available online 1 March 2012).
Abstract | Links | BibTeX | Tags: FLORENTZ, Identity elements Mitochondrial tRNA Cross-aminoacylation Structural plasticity, SISSLER, Unité ARN
@article{,
title = {Adaptation of aminoacylation identity rules to mammalian mitochondria.},
author = {A Fender and A Gaudry and F Jühling and M Sissler and C Florentz},
url = {http://www.ncbi.nlm.nih.gov/pubmed/22402012?dopt=Abstract},
doi = {10.1016/j.biochi.2012.02.030},
isbn = {22402012},
year = {2012},
date = {2012-01-01},
journal = {Biochimie},
volume = {94},
number = {5},
pages = {1090-1097},
abstract = {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.},
note = {Available online 1 March 2012},
keywords = {FLORENTZ, Identity elements Mitochondrial tRNA Cross-aminoacylation Structural plasticity, SISSLER, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
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.