ArticleNature chemical biology2009
Natural amino acids do not require their native tRNAs for efficient selection by the ribosome.
Article in Nature chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Article
- Ribosomal RNA methylation by GidB modulates discrimination of mischarged tRNA.bioRxiv : the preprint server for biology · 2026Article
- Time-domain event detection using single-instruction, multiple-thread gpGPU architectures in single-molecule biophysical data.Computer physics communications · 2024Article
- β-Amino Acids Reduce Ternary Complex Stability and Alter the Translation Elongation Mechanism.ACS central science · 2024Article
- β-amino acids reduce ternary complex stability and alter the translation elongation mechanism.bioRxiv : the preprint server for biology · 2024Article
- Mechanistic studies of non-canonical amino acid mutagenesis.Methods in enzymology · 2021Article
- The chemistry and applications of RNA 2'-OH acylation.Nature reviews. Chemistry · 2020Article
- Function and origin of mistranslation in distinct cellular contexts.Critical reviews in biochemistry and molecular biology · 2017Review
- How EF-Tu can contribute to efficient proofreading of aa-tRNA by the ribosome.Nature communications · 2016Article
- Article
- Outwitting EF-Tu and the ribosome: translation with d-amino acids.Nucleic acids research · 2015Article
- Capturing transition paths and transition states for conformational rearrangements in the ribosome.Biophysical journal · 2014Article
- smFRET studies of the 'encounter' complexes and subsequent intermediate states that regulate the selectivity of ligand binding.FEBS letters · 2014Review
- Genetically encoded libraries of nonstandard peptides.Journal of nucleic acids · 2012Article
- In vitro and in vivo single-molecule fluorescence imaging of ribosome-catalyzed protein synthesis.Current opinion in chemical biology · 2011Review
- Biological mechanisms, one molecule at a time.Genes & development · 2011Review
- Cellular mechanisms that control mistranslation.Nature reviews. Microbiology · 2010Review
- Fluorescence anisotropy and resonance energy transfer: powerful tools for measuring real time protein dynamics in a physiological environment.Current opinion in pharmacology · 2010Review
- Do anticodons of misacylated tRNAs preferentially mismatch codons coding for the misloaded amino acid?BMC molecular biology · 2010Article
- Structure and dynamics of a processive Brownian motor: the translating ribosome.Annual review of biochemistry · 2010Review
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7 authors.
Funding
Abstract
The involvement of tRNA structural elements beyond the anticodon in aminoacyl-tRNA (aa-tRNA) selection by the ribosome has revealed that substrate recognition is considerably more complex than originally envisioned in the adaptor hypothesis. By combining recent breakthroughs in aa-tRNA synthesis and mechanistic and structural studies of protein synthesis, we have investigated whether aa-tRNA recognition further extends to the amino acid, which would explain various translation disorders exhibited by misacylated tRNAs. Contrary to expectation, we find that natural amino acids misacylated onto natural but non-native tRNAs are selected with efficiencies very similar to those of their correctly acylated counterparts. Despite this, small but reproducible differences in selection indeed demonstrate that the translational machinery is sensitive to the amino acid-tRNA pairing. These results suggest either that the ribosome is an exquisite sensor of natural versus unnatural amino acid-tRNA pairings and/or that aa-tRNA selection is not the primary step governing the amino acid specificity of the ribosome.
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