ArticleNucleic acids research2011
Is the sequence-specific binding of aminoacyl-tRNAs by EF-Tu universal among bacteria?
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 25 citations in OpenAlex.
- Serine tRNAs compete to regulate the mRNA translation of serine-sensitive codons.Science advances · 2025Article
- Contribution of tRNA sequence and modifications to the decoding preferences of E. coli and M. mycoides tRNAGlyUCC for synonymous glycine codons.Nucleic acids research · 2024Article
- Tuning tRNAs for improved translation.Frontiers in genetics · 2024Review
- Eukaryotic tRNA sequences present conserved and amino acid-specific structural signatures.Nucleic acids research · 2022Article
- Uniform affinity-tuning of N-methyl-aminoacyl-tRNAs to EF-Tu enhances their multiple incorporation.Nucleic acids research · 2021Article
- Partition of tRNAGly isoacceptors between protein and cell-wall peptidoglycan synthesis in Staphylococcus aureus.Nucleic acids research · 2021Article
- Unusual tertiary pairs in eukaryotic tRNARNA (New York, N.Y.) · 2020Article
- Characterization of glutamyl-tRNA-dependent dehydratases using nonreactive substrate mimics.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- SynMyco transposon: engineering transposon vectors for efficient transformation of minimal genomes.DNA research : an international journal for rapid publication of reports on genes and genomes · 2019Article
- Evolutionary tuning impacts the design of bacterial tRNAs for the incorporation of unnatural amino acids by ribosomes.Current opinion in chemical biology · 2018Review
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- Electrophoretic Deformation of Individual Transfer RNA Molecules Reveals Their Identity.Nano letters · 2016Article
- Methionine Mistranslation Bypasses the Restraint of the Genetic Code to Generate Mutant Proteins with Distinct Activities.PLoS genetics · 2015Article
- Non-Conserved Residues in Clostridium acetobutylicum tRNA(Ala) Contribute to tRNA Tuning for Efficient Antitermination of the alaS T Box Riboswitch.Life (Basel, Switzerland) · 2015Article
- Evolving tRNA(Sec) for efficient canonical incorporation of selenocysteine.Journal of the American Chemical Society · 2015Article
- Article
- The determination of tRNALeu recognition nucleotides for Escherichia coli L/F transferase.RNA (New York, N.Y.) · 2014Article
- tRNA residues evolved to promote translational accuracy.RNA (New York, N.Y.) · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Three base pairs in the T-stem are primarily responsible for the sequence-specific interaction of tRNA with Escherichia coli and Thermus thermophilus EF-Tu. While the amino acids on the surface of EF-Tu that contact aminoacyl-tRNA (aa-tRNA) are highly conserved among bacteria, the T-stem sequences of individual tRNA are variable, making it unclear whether or not this protein-nucleic acid interaction is also sequence specific in other bacteria. We propose and validate a thermodynamic model that predicts the ΔG° of any tRNA to EF-Tu using the sequence of its three T-stem base pairs. Despite dramatic differences in T-stem sequences, the predicted ΔG° values for the majority of tRNA classes are similar in all bacteria and closely match the ΔG° values determined for E. coli tRNAs. Each individual tRNA class has evolved to have a characteristic ΔG° value to EF-Tu, but different T-stem sequences are used to achieve this ΔG° value in different bacteria. Thus, the compensatory relationship between the affinity of the tRNA body and the affinity of the esterified amino acid is universal among bacteria. Additionally, we predict and validate a small number of aa-tRNAs that bind more weakly to EF-Tu than expected and thus are candidates for acting as activated amino acid donors in processes outside of translation.
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