ArticleThe Journal of biological chemistry2015
Ancestral AlaX editing enzymes for control of genetic code fidelity are not tRNA-specific.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 19 citations in OpenAlex.
- Loss of AlaX, a trans-editing factor for several aminoacyl-tRNA synthetases, activates the unfolded protein response and arrests the cell cycle.Science China. Life sciences · 2026Article
- Human aminoacyl-tRNA synthetases as integrators of translation and cell signalling networks.Nature reviews. Molecular cell biology · 2026Review
- Eukaryotic AlaX provides multiple checkpoints for quality and quantity of aminoacyl-tRNAs in translation.Nucleic acids research · 2024Article
- The role of tRNA identity elements in aminoacyl-tRNA editing.Frontiers in microbiology · 2024Review
- Structural basis of tRNAPro acceptor stem recognition by a bacterial trans-editing domain.Nucleic acids research · 2023Article
- Impact of alanyl-tRNA synthetase editing deficiency in yeast.Nucleic acids research · 2021Article
- Indirect Routes to Aminoacyl-tRNA: The Diversity of Prokaryotic Cysteine Encoding Systems.Frontiers in genetics · 2021Article
- Stereospecificity control in aminoacyl-tRNA-synthetases: new evidence of d-amino acids activation and editing.Nucleic acids research · 2019Article
- The central role of tRNA in genetic code expansion.Biochimica et biophysica acta. General subjects · 2017Review
- Rewiring protein synthesis: From natural to synthetic amino acids.Biochimica et biophysica acta. General subjects · 2017Review
- Conformational and chemical selection by aProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- Naturally Occurring Isoleucyl-tRNA Synthetase without tRNA-dependent Pre-transfer Editing.The Journal of biological chemistry · 2016Article
- Trans-oligomerization of duplicated aminoacyl-tRNA synthetases maintains genetic code fidelity under stress.Nucleic acids research · 2015Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
Abstract
Accurate protein synthesis requires the hydrolytic editing of tRNAs incorrectly aminoacylated by aminoacyl-tRNA synthetases (ARSs). Recognition of cognate tRNAs by ARS is less error-prone than amino acid recognition, and, consequently, editing domains are generally believed to act only on the tRNAs cognate to their related ARSs. For example, the AlaX family of editing domains, including the editing domain of alanyl-tRNA synthetase and the related free-standing trans-editing AlaX enzymes, are thought to specifically act on tRNA(Ala), whereas the editing domains of threonyl-tRNA synthetases are specific for tRNA(Thr). Here we show that, contrary to this belief, AlaX-S, the smallest of the extant AlaX enzymes, deacylates Ser-tRNA(Thr) in addition to Ser-tRNA(Ala) and that a single residue is important to determine this behavior. Our data indicate that promiscuous forms of AlaX are ancestral to tRNA-specific AlaXs. We propose that former AlaX domains were used to maintain translational fidelity in earlier stages of genetic code evolution when mis-serylation of several tRNAs was possible.
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