Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS.
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Bonnefond L, Fender A, Rudinger-Thirion J, Giege R, Florentz C, Sissler M
Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS.
Biochemistry. 2005 Mar 29;44(12):4805-16.
- PubMed ID
- 15779907 [ View in PubMed]
- Abstract
The human mitochondrion possesses a translational machinery devoted to the synthesis of 13 proteins. While the required tRNAs and rRNAs are produced by transcription of the mitochondrial genome, all other factors needed for protein synthesis are synthesized in the cytosol and imported. This is the case for aminoacyl-tRNA synthetases, the enzymes which esterify their cognate tRNA with the specific amino acid. The genes for the full set of cytosolic aaRSs are well defined, but only nine genes for mitochondrial synthetases are known. Here we describe the genes for human mitochondrial aspartyl- and tyrosyl-tRNA synthetases and the initial characterization of the enzymes. Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs. Genes for the remaining missing synthetases were also found with the exception of glutaminyl-tRNA synthetase. Their sequence analysis confirms and further extends the view that, except for lysyl- and glycyl-tRNA synthetases, human mitochondrial and cytosolic enzymes are coded by two different sets of genes.
DrugBank Data that Cites this Article
- Polypeptides
Name UniProt ID Tyrosine--tRNA ligase, mitochondrial Q9Y2Z4 Details Aspartate--tRNA ligase, mitochondrial Q6PI48 Details Probable glutamate--tRNA ligase, mitochondrial Q5JPH6 Details Probable cysteine--tRNA ligase, mitochondrial Q9HA77 Details Threonine--tRNA ligase, mitochondrial Q9BW92 Details Alanine--tRNA ligase, mitochondrial Q5JTZ9 Details Probable asparagine--tRNA ligase, mitochondrial Q96I59 Details