ArticleNucleic acids research2015
EF-Tu dynamics during pre-translocation complex formation: EF-Tu·GDP exits the ribosome via two different pathways.
Article in Nucleic acids research, 2015. 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, 28 citations in OpenAlex.
- Human protein synthesis requires aminoacyl-tRNA pivoting during proofreading.Nature communications · 2025Article
- Connecting tRNA Charging and Decoding through the Axis of Nucleotide Modifications at Position 37.Journal of molecular biology · 2025Review
- 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
- Geometric alignment of aminoacyl-tRNA relative to catalytic centers of the ribosome underpins accurate mRNA decoding.Nature communications · 2023Article
- The Structural Dynamics of Translation.Annual review of biochemistry · 2022Review
- Ataluren and aminoglycosides stimulate read-through of nonsense codons by orthogonal mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- 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
- Insights into the base-pairing preferences of 8-oxoguanosine on the ribosome.Nucleic acids research · 2019Article
- E. coli elongation factor Tu bound to a GTP analogue displays an open conformation equivalent to the GDP-bound form.Nucleic acids research · 2018Article
- Structural dynamics of translation elongation factor Tu during aa-tRNA delivery to the ribosome.Nucleic acids research · 2018Article
- Stringent Nucleotide Recognition by the Ribosome at the Middle Codon Position.Molecules (Basel, Switzerland) · 2017Article
- Ribosome dynamics during decoding.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Two proofreading steps amplify the accuracy of genetic code translation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- How EF-Tu can contribute to efficient proofreading of aa-tRNA by the ribosome.Nature communications · 2016Article
- Review: Translational GTPases.Biopolymers · 2016Review
- MEMLET: An Easy-to-Use Tool for Data Fitting and Model Comparison Using Maximum-Likelihood Estimation.Biophysical journal · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The G-protein EF-Tu, which undergoes a major conformational change when EF-Tu·GTP is converted to EF-Tu·GDP, forms part of an aminoacyl(aa)-tRNA·EF-Tu·GTP ternary complex (TC) that accelerates the binding of aa-tRNA to the ribosome during peptide elongation. Such binding, placing a portion of EF-Tu in contact with the GTPase Associated Center (GAC), is followed by GTP hydrolysis and Pi release, and results in formation of a pretranslocation (PRE) complex. Although tRNA movement through the ribosome during PRE complex formation has been extensively studied, comparatively little is known about the dynamics of EF-Tu interaction with either the ribosome or aa-tRNA. Here we examine these dynamics, utilizing ensemble and single molecule assays employing fluorescent labeled derivatives of EF-Tu, tRNA, and the ribosome to measure changes in either FRET efficiency or fluorescence intensity during PRE complex formation. Our results indicate that ribosome-bound EF-Tu separates from the GAC prior to its full separation from aa-tRNA, and suggest that EF-Tu·GDP dissociates from the ribosome by two different pathways. These pathways correspond to either reversible EF-Tu·GDP dissociation from the ribosome prior to the major conformational change in EF-Tu that follows GTP hydrolysis, or irreversible dissociation after or concomitant with this conformational change.
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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.