ArticleRNA (New York, N.Y.)2011
Insights into the molecular determinants of EF-G catalyzed translocation.
Article in RNA (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
25 citing papers in PubMed, 36 citations in OpenAlex.
- 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
- Partial spontaneous intersubunit rotations in pretranslocation ribosomes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Insights into translocation mechanism and ribosome evolution from cryo-EM structures of translocation intermediates of Giardia intestinalis.Nucleic acids research · 2023Article
- Article
- tRNA Translocation by the Eukaryotic 80S Ribosome and the Impact of GTP Hydrolysis.Cell reports · 2018Article
- The ribosomal A-site finger is crucial for binding and activation of the stringent factor RelA.Nucleic acids research · 2018Article
- Variant ribosomal RNA alleles are conserved and exhibit tissue-specific expression.Science advances · 2018Article
- Aminoglycoside interactions and impacts on the eukaryotic ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The ribosome moves: RNA mechanics and translocation.Nature structural & molecular biology · 2017Article
- Miscoding-induced stalling of substrate translocation on the bacterial ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Multiperspective smFRET reveals rate-determining late intermediates of ribosomal translocation.Nature structural & molecular biology · 2016Article
- Steric interactions lead to collective tilting motion in the ribosome during mRNA-tRNA translocation.Nature communications · 2016Article
- Functional Dynamics within the Human Ribosome Regulate the Rate of Active Protein Synthesis.Molecular cell · 2015Article
- Chemically related 4,5-linked aminoglycoside antibiotics drive subunit rotation in opposite directions.Nature communications · 2015Article
- The bright future of single-molecule fluorescence imaging.Current opinion in chemical biology · 2014Review
- Visualization of two transfer RNAs trapped in transit during elongation factor G-mediated translocation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Frameshifting dynamics.Biopolymers · 2013Review
- Blasticidin S inhibits translation by trapping deformed tRNA on the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Translocation, the directional movement of transfer RNA (tRNA) and messenger RNA (mRNA) substrates on the ribosome during protein synthesis, is regulated by dynamic processes intrinsic to the translating particle. Using single-molecule fluorescence resonance energy transfer (smFRET) imaging, in combination with site-directed mutagenesis of the ribosome and tRNA substrates, we show that peptidyl-tRNA within the aminoacyl site of the bacterial pretranslocation complex can adopt distinct hybrid tRNA configurations resulting from uncoupled motions of the 3'-CCA terminus and the tRNA body. As expected for an on-path translocation intermediate, the hybrid configuration where both the 3'-CCA end and body of peptidyl-tRNA have moved in the direction of translocation exhibits dramatically enhanced puromycin reactivity, an increase in the rate at which EF-G engages the ribosome, and accelerated rates of translocation. These findings provide compelling evidence that the substrate for EF-G catalyzed translocation is an intermediate wherein the bodies of both tRNA substrates adopt hybrid positions within the translating 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.