ArticleProceedings of the National Academy of Sciences of the United States of America2004
A truncated aminoacyl-tRNA synthetase modifies RNA.
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 53 papers.
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53 citing papers in PubMed, 97 citations in OpenAlex.
- Compendium of RNA modifications for bacterial stress adaptation.Microbiology and molecular biology reviews : MMBR · 2026Review
- Human aminoacyl-tRNA synthetases as integrators of translation and cell signalling networks.Nature reviews. Molecular cell biology · 2026Review
- tRNA modifications: greasing the wheels of translation and beyond.RNA biology · 2025Review
- Architecture ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Engineering tRNAs for the Ribosomal Translation of Non-proteinogenic Monomers.Chemical reviews · 2024Review
- Impact of the chemical modification of tRNAs anticodon loop on the variability and evolution of codon usage in proteobacteria.Frontiers in microbiology · 2024Article
- Synthesis and Structure Elucidation of Glutamyl-Queuosine.Journal of the American Chemical Society · 2023Article
- A comprehensive analysis of translational misdecoding pattern and its implication on genetic code evolution.Nucleic acids research · 2023Article
- Impact of queuosine modification of endogenousFrontiers in molecular biosciences · 2022Article
- Diversification of aminoacyl-tRNA synthetase activitiesFrontiers in physiology · 2022Review
- Possible Ancestral Functions of the Genetic and RNA Operational Precodes and the Origin of the Genetic System.Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2021Article
- The expanding world of tRNA modifications and their disease relevance.Nature reviews. Molecular cell biology · 2021Review
- Article
- Comparative tRNA sequencing and RNA mass spectrometry for surveying tRNA modifications.Nature chemical biology · 2020Article
- Naturally occurring modified ribonucleosides.Wiley interdisciplinary reviews. RNA · 2020Review
- Modulation ofFrontiers in genetics · 2020Article
- The Ribosome as a Missing Link in Prebiotic Evolution III: Over-Representation of tRNA- and rRNA-Like Sequences and Plieofunctionality of Ribosome-Related Molecules Argues for the Evolution of Primitive Genomes from Ribosomal RNA Modules.International journal of molecular sciences · 2019Article
- Genomic characterization of three novel Basilisk-like phages infecting Bacillus anthracis.BMC genomics · 2018Article
- Functionality of tRNAs encoded in a mobile genetic element from an acidophilic bacterium.RNA biology · 2018Article
- The RNA chaperone La promotes pre-tRNA maturation via indiscriminate binding of both native and misfolded targets.Nucleic acids research · 2017Article
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5 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Aminoacyl-tRNA synthetases are modular enzymes composed of a central active site domain to which additional functional domains were appended in the course of evolution. Analysis of bacterial genome sequences revealed the presence of many shorter aminoacyl-tRNA synthetase paralogs. Here we report the characterization of a well conserved glutamyl-tRNA synthetase (GluRS) paralog (YadB in Escherichia coli) that is present in the genomes of >40 species of proteobacteria, cyanobacteria, and actinobacteria. The E. coli yadB gene encodes a truncated GluRS that lacks the C-terminal third of the protein and, consequently, the anticodon binding domain. Generation of a yadB disruption showed the gene to be dispensable for E. coli growth in rich and minimal media. Unlike GluRS, the YadB protein was able to activate glutamate in presence of ATP in a tRNA-independent fashion and to transfer glutamate onto tRNA(Asp). Neither tRNA(Glu) nor tRNA(Gln) were substrates. In contrast to canonical aminoacyl-tRNA, glutamate was not esterified to the 3'-terminal adenosine of tRNA(Asp). Instead, it was attached to the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of queuosine, the modified nucleoside occupying the first anticodon position of tRNA(Asp). Glutamyl-queuosine, like canonical Glu-tRNA, was hydrolyzed by mild alkaline treatment. Analysis of tRNA isolated under acidic conditions showed that this novel modification is present in normal E. coli tRNA; presumably it previously escaped detection as the standard conditions of tRNA isolation include an alkaline deacylation step that also causes hydrolysis of glutamyl-queuosine. Thus, this aminoacyl-tRNA synthetase fragment contributes to standard nucleotide modification of tRNA.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.