ArticleProceedings of the National Academy of Sciences of the United States of America2004
A domain for editing by an archaebacterial tRNA synthetase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 57 citations in OpenAlex.
- Evaluating the evolutionary relationship of TATA binding protein (TBP) with various folding patterns of protein domains using support vector machine (SVM).Scientific reports · 2026Article
- A metal ion mediated functional dichotomy encodes plasticity during translation quality control.Nature communications · 2025Article
- The role of tRNA identity elements in aminoacyl-tRNA editing.Frontiers in microbiology · 2024Review
- A standalone editing protein deacylates mischarged canavanyl-tRNAArg to prevent canavanine incorporation into proteins.Nucleic acids research · 2023Article
- Amino Acid Specificity of Ancestral Aminoacyl-tRNA Synthetase Prior to the Last Universal Common Ancestor Commonote commonote.Journal of molecular evolution · 2022Article
- Oxidation alters the architecture of the phenylalanyl-tRNA synthetase editing domain to confer hyperaccuracy.Nucleic acids research · 2021Article
- Aminoacyl-tRNA synthetases.RNA (New York, N.Y.) · 2020Review
- Cross-editing by a tRNA synthetase allows vertebrates to abundantly express mischargeable tRNA without causing mistranslation.Nucleic acids research · 2020Article
- Evolutionary Gain of Alanine Mischarging to Noncognate tRNAs with a G4:U69 Base Pair.Journal of the American Chemical Society · 2016Article
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- Ancestral AlaX editing enzymes for control of genetic code fidelity are not tRNA-specific.The Journal of biological chemistry · 2015Article
- Identification of lethal mutations in yeast threonyl-tRNA synthetase revealing critical residues in its human homolog.The Journal of biological chemistry · 2015Article
- Emergence and evolution.Topics in current chemistry · 2014Review
- Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analyses of threonyl-tRNA synthetase editing domain from Aeropyrum pernix.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Yeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignment.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Mistranslation and its control by tRNA synthetases.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2011Article
- Naturally occurring aminoacyl-tRNA synthetases editing-domain mutations that cause mistranslation in Mycoplasma parasites.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Mechanistic insights into cognate substrate discrimination during proofreading in translation.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Revisiting the operational RNA code for amino acids: Ensemble attributes and their implications.RNA (New York, N.Y.) · 2010Article
- Genome-wide analysis of tRNA charging and activation of the eIF2 kinase Gcn2p.The Journal of biological chemistry · 2009Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The rules of the genetic code are established by aminoacylations of transfer RNAs by aminoacyl tRNA synthetases. New codon assignments, and the introduction of new kinds of amino acids, are blocked by vigorous tRNA-dependent editing reactions occurring at hydrolytic sites embedded within specialized domains in the synthetases. For some synthetases, these domains were present at the time of the last common ancestor and were fixed in evolution through all three of the kingdoms of life. Significantly, a well characterized domain for editing found in bacterial and eukaryotic threonyl- and all alanyl-tRNA synthetases is missing from archaebacterial threonine enzymes. Here we show that the archaebacterial Methanosarcina mazei ThrRS efficiently misactivates serine, but does not fuse serine to tRNA. Consistent with this observation, the enzyme cleared serine that was linked to threonine-specific tRNAs. M. mazei and most other archaebacterial ThrRSs have a domain, N2(A), fused to the N terminus and not found in bacterial or eukaryotic orthologs. Mutations at conserved residues in this domain led to an inability to clear threonine-specific tRNA mischarged with serine. Thus, these results demonstrate a domain for editing that is distinct from all others, is restricted to just one branch of the tree of life, and was most likely added to archaebacterial ThrRSs after the eukaryote/archaebacteria split.
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