ArticleThe Journal of biological chemistry2014
Direct evidence of an elongation factor-Tu/Ts·GTP·Aminoacyl-tRNA quaternary complex.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 22 citations in OpenAlex.
- Strategies for detecting aminoacylation and aminoacyl-tRNA editingIsrael journal of chemistry · 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
- Tuning tRNAs for improved translation.Frontiers in genetics · 2024Review
- Human Serum Mediated Bacteriophage Life Cycle Switch inLife (Basel, Switzerland) · 2023Article
- Mechanistic insights into tRNA cleavage by a contact-dependent growth inhibitor protein and translation factors.Nucleic acids research · 2022Article
- 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
- tRNA Translocation by the Eukaryotic 80S Ribosome and the Impact of GTP Hydrolysis.Cell reports · 2018Article
- Article
- Structure of a novel antibacterial toxin that exploits elongation factor Tu to cleave specific transfer RNAs.Nucleic acids research · 2017Article
- Fail-safe control of translation initiation by dissociation of eIF2α phosphorylated ternary complexes.eLife · 2017Article
- Activation of contact-dependent antibacterial tRNase toxins by translation elongation factors.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Functional Dynamics within the Human Ribosome Regulate the Rate of Active Protein Synthesis.Molecular cell · 2015Article
- Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
During protein synthesis, elongation factor-Tu (EF-Tu) bound to GTP chaperones the entry of aminoacyl-tRNA (aa-tRNA) into actively translating ribosomes. In so doing, EF-Tu increases the rate and fidelity of the translation mechanism. Recent evidence suggests that EF-Ts, the guanosine nucleotide exchange factor for EF-Tu, directly accelerates both the formation and dissociation of the EF-Tu-GTP-Phe-tRNA(Phe) ternary complex (Burnett, B. J., Altman, R. B., Ferrao, R., Alejo, J. L., Kaur, N., Kanji, J., and Blanchard, S. C. (2013) J. Biol. Chem. 288, 13917-13928). A central feature of this model is the existence of a quaternary complex of EF-Tu/Ts·GTP·aa-tRNA(aa). Here, through comparative investigations of phenylalanyl, methionyl, and arginyl ternary complexes, and the development of a strategy to monitor their formation and decay using fluorescence resonance energy transfer, we reveal the generality of this newly described EF-Ts function and the first direct evidence of the transient quaternary complex species. These findings suggest that EF-Ts may regulate ternary complex abundance in the cell through mechanisms that are distinct from its guanosine nucleotide exchange factor functions.
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