A present-day aminoacyl-tRNA synthetase with ancestral editing properties.

Article Details

Citation
Copy to clipboard

Zhu B, Zhao MW, Eriani G, Wang ED

A present-day aminoacyl-tRNA synthetase with ancestral editing properties.

RNA. 2007 Jan;13(1):15-21. Epub 2006 Nov 9.

PubMed ID
17095543 [ View in PubMed
]
Abstract

Leucyl-, isoleucyl-, and valyl-tRNA synthetases form a subgroup of related aminoacyl-tRNA synthetases that attach similar amino acids to their cognate tRNAs. To prevent amino acid misincorporation during translation, these enzymes also hydrolyze mischarged tRNAs through a post-transfer editing mechanism. Here we show that LeuRS from the deep-branching bacterium Aquifex aeolicus edits the complete set of aminoacylated tRNAs generated by the three enzymes: Ile-tRNA(Ile), Val-tRNA(Ile), Val-tRNA(Val), Thr-tRNA(Val), and Ile-tRNA(Leu). This unusual enlarged editing property was studied in a model of a primitive editing system containing a composite minihelix carrying the triple leucine, isoleucine, and valine identity mimicking the primitive tRNA precursor. We found that the freestanding LeuRS editing domain can edit this precursor in contrast to IleRS and ValRS editing domains. These results suggest that A. aeolicus LeuRS carries editing properties that seem more primitive than those of IleRS and ValRS. They suggest that the A. aeolicus editing domain has preserved the ambiguous editing property from the ancestral common editing domain or, alternatively, that this plasticity results from a specific metabolic adaptation.

DrugBank Data that Cites this Article

Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
IsoleucineIsoleucine--tRNA ligase, mitochondrialProteinHumans
Unknown
Not AvailableDetails
LeucineProbable leucine--tRNA ligase, mitochondrialProteinHumans
Unknown
Not AvailableDetails
ValineValine--tRNA ligaseProteinHumans
Unknown
Not AvailableDetails
Drug Enzymes
DrugEnzymeKindOrganismPharmacological ActionActions
ValineValine--tRNA ligaseProteinHumans
Unknown
Substrate
Details