ArticleProceedings of the National Academy of Sciences of the United States of America2014
Ribosome-induced tuning of GTP hydrolysis by a translational GTPase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 50 citations in OpenAlex.
- An apicoplast-localized GTPase is essential formSphere · 2026Article
- D-stem mutation in an essential tRNA increases translation speed at the cost of fidelity.PLoS genetics · 2025Article
- The ribosome termination complex remodels release factor RF3 and ejects GDP.Nature structural & molecular biology · 2024Article
- Salmonella antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of EF-Tu P-loop.Nucleic acids research · 2022Article
- Structural insights of the elongation factor EF-Tu complexes in protein translation of Mycobacterium tuberculosis.Communications biology · 2022Article
- Common Mechanism of Activated Catalysis in P-loop Fold Nucleoside Triphosphatases-United in Diversity.Biomolecules · 2022Article
- Kinetic Analysis Suggests Evolution of Ribosome Specificity in Modern Elongation Factor-Tus from "Generalist" Ancestors.Molecular biology and evolution · 2021Article
- Essentiality of c-di-AMP in Bacillus subtilis: Bypassing mutations converge in potassium and glutamate homeostasis.PLoS genetics · 2021Article
- Article
- 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
- How Ricin Damages the Ribosome.Toxins · 2019Review
- Translation in Prokaryotes.Cold Spring Harbor perspectives in biology · 2018Review
- EF-Tu and EF-G are activated by allosteric effects.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Transcription-translation coupling: direct interactions of RNA polymerase with ribosomes and ribosomal subunits.Nucleic acids research · 2017Article
- Ribosome dynamics during decoding.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Tetracycline does not directly inhibit the function of bacterial elongation factor Tu.PloS one · 2017Article
- Article
- Review: Translational GTPases.Biopolymers · 2016Review
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- Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
GTP hydrolysis by elongation factor Tu (EF-Tu), a translational GTPase that delivers aminoacyl-tRNAs to the ribosome, plays a crucial role in decoding and translational fidelity. The basic reaction mechanism and the way the ribosome contributes to catalysis are a matter of debate. Here we use mutational analysis in combination with measurements of rate/pH profiles, kinetic solvent isotope effects, and ion dependence of GTP hydrolysis by EF-Tu off and on the ribosome to dissect the reaction mechanism. Our data suggest that--contrary to current models--the reaction in free EF-Tu follows a pathway that does not involve the critical residue H84 in the switch II region. Binding to the ribosome without a cognate codon in the A site has little effect on the GTPase mechanism. In contrast, upon cognate codon recognition, the ribosome induces a rearrangement of EF-Tu that renders GTP hydrolysis sensitive to mutations of Asp21 and His84 and insensitive to K(+) ions. We suggest that Asp21 and His84 provide a network of interactions that stabilize the positions of the γ-phosphate and the nucleophilic water, respectively, and thus play an indirect catalytic role in the GTPase mechanism on the ribosome.
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Registered trials
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.