ArticleNature communications2016
How EF-Tu can contribute to efficient proofreading of aa-tRNA by the ribosome.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- RNAViruses · 2026Review
- Transient ion-mediated interactions regulate subunit rotation in a eukaryotic ribosome.bioRxiv : the preprint server for biology · 2025Article
- Simulating biomolecules for physiological timescales.Current opinion in structural biology · 2025Review
- Native ESI-MS and Collision-Induced Unfolding (CIU) of the Complex between Bacterial Elongation Factor-Tu and the Antibiotic Enacyloxin IIa.Journal of the American Society for Mass Spectrometry · 2024Article
- The Structural and Molecular Mechanisms ofMolecules (Basel, Switzerland) · 2024Review
- Geometric alignment of aminoacyl-tRNA relative to catalytic centers of the ribosome underpins accurate mRNA decoding.Nature communications · 2023Article
- Extensive breaking of genetic code degeneracy with non-canonical amino acids.Nature communications · 2023Article
- Structural insights of the elongation factor EF-Tu complexes in protein translation of Mycobacterium tuberculosis.Communications biology · 2022Article
- The Structural Dynamics of Translation.Annual review of biochemistry · 2022Review
- Interactions between nascent proteins and the ribosome surface inhibit co-translational folding.Nature chemistry · 2021Article
- Nascent polypeptide within the exit tunnel stabilizes the ribosome to counteract risky translation.The EMBO journal · 2021Article
- Article
- The dynamics of subunit rotation in a eukaryotic ribosome.Biophysica · 2021Article
- In silico analysis of bacterial translation factors reveal distinct translation event specific pI values.BMC genomics · 2021Article
- A steric gate controls P/E hybrid-state formation of tRNA on the ribosome.Nature communications · 2020Article
- Article
- Elongation Factor Tu Switch I Element is a Gate for Aminoacyl-tRNA Selection.Journal of molecular biology · 2020Article
- Elongation factor-Tu can repetitively engage aminoacyl-tRNA within the ribosome during the proofreading stage of tRNA selection.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- tRNA Dissociation from EF-Tu after GTP Hydrolysis: Primary Steps and Antibiotic Inhibition.Biophysical journal · 2020Article
- Unraveling 1,4-Butanediol Metabolism inFrontiers in microbiology · 2020Article
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2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It has long been recognized that the thermodynamics of mRNA-tRNA base pairing is insufficient to explain the high fidelity and efficiency of aminoacyl-tRNA (aa-tRNA) selection by the ribosome. To rationalize this apparent inconsistency, Hopfield proposed that the ribosome may improve accuracy by utilizing a multi-step kinetic proofreading mechanism. While biochemical, structural and single-molecule studies have provided a detailed characterization of aa-tRNA selection, there is a limited understanding of how the physical-chemical properties of the ribosome enable proofreading. To this end, we probe the role of EF-Tu during aa-tRNA accommodation (the proofreading step) through the use of energy landscape principles, molecular dynamics simulations and kinetic models. We find that the steric composition of EF-Tu can reduce the free-energy barrier associated with the first step of accommodation: elbow accommodation. We interpret this effect within an extended kinetic model of accommodation and show how EF-Tu can contribute to efficient and accurate proofreading.
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