ArticleProceedings of the National Academy of Sciences of the United States of America2017
Three tRNAs on the ribosome slow translation elongation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Article
- Genetic Code Expansion: Recent Developments and Emerging Applications.Chemical reviews · 2025Review
- Deep learning based local feature classification to automatically identify single molecule fluorescence events.Communications biology · 2024Article
- Decomposing bulk signals to reveal hidden information in processive enzyme reactions: A case study in mRNA translation.PLoS computational biology · 2024Article
- Transient disome complex formation in native polysomes during ongoing protein synthesis captured by cryo-EM.Nature communications · 2024Article
- Partial spontaneous intersubunit rotations in pretranslocation ribosomes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Membrane-dependent relief of translation elongation arrest on pseudouridine- and N1-methyl-pseudouridine-modified mRNAs.Nucleic acids research · 2022Article
- HDLBP binds ER-targeted mRNAs by multivalent interactions to promote protein synthesis of transmembrane and secreted proteins.Nature communications · 2022Article
- Zero-mode waveguides and nanopore-based sequencing technologies accelerate single-molecule studies.Biophysics and physicobiology · 2022Article
- Mechanisms that ensure speed and fidelity in eukaryotic translation termination.Science (New York, N.Y.) · 2021Article
- Yeast translation elongation factor eEF3 promotes late stages of tRNA translocation.The EMBO journal · 2021Article
- A Genetic Code Expansion-Derived Molecular Beacon for the Detection of Intracellular Amyloid-β Peptide Generation.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021Article
- A Genetic Code Expansion-Derived Molecular Beacon for the Detection of Intracellular Amyloid-β Peptide Generation.Angewandte Chemie (International ed. in English) · 2021Article
- Heterogeneous Dynamics of Protein-RNA Interactions across Transcriptome-Derived Messenger RNA Populations.Journal of the American Chemical Society · 2020Article
- Pairs of amino acids at the P- and A-sites of the ribosome predictably and causally modulate translation-elongation rates.Journal of molecular biology · 2020Article
- Fabrication of Zero Mode Waveguides for High Concentration Single Molecule Microscopy.Journal of visualized experiments : JoVE · 2020Article
- Elongation Factor Tu Switch I Element is a Gate for Aminoacyl-tRNA Selection.Journal of molecular biology · 2020Article
- The transcription factor Sp1 modulates RNA polymerase III gene transcription by controllingThe Journal of biological chemistry · 2020Article
- Dynamics of the context-specific translation arrest by chloramphenicol and linezolid.Nature chemical 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
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2 authors.
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Abstract
During protein synthesis, the ribosome simultaneously binds up to three different transfer RNA (tRNA) molecules. Among the three tRNA binding sites, the regulatory role of the exit (E) site, where deacylated tRNA spontaneously dissociates from the translational complex, has remained elusive. Here we use two donor-quencher pairs to observe and correlate both the conformation of ribosomes and tRNAs as well as tRNA occupancy. Our results reveal a partially rotated state of the ribosome wherein all three tRNA sites are occupied during translation elongation. The appearance and lifetime of this state depend on the E-site tRNA dissociation kinetics, which may vary among tRNA species and depends on temperature and ionic strength. The 3-tRNA partially rotated state is not a proper substrate for elongation factor G (EF-G), thus inhibiting translocation until the E-site tRNA dissociates. Our result presents two parallel kinetic pathways during translation elongation, underscoring the ability of E-site codons to modulate the dynamics of protein synthesis.
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