ArticleBiophysical journal2017
tRNA Fluctuations Observed on Stalled Ribosomes Are Suppressed during Ongoing Protein Synthesis.
Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
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- Sexually dimorphic RNA helicases DDX3X and DDX3Y differentially regulate RNA metabolism through phase separation.Molecular cell · 2022Article
- Can DyeCycling break the photobleaching limit in single-molecule FRET?Nano research · 2022Article
- Optimization of a fluorescent-mRNA based real-time assay for precise kinetic measurements of ribosomal translocation.RNA biology · 2021Article
- Site-Specific Fluorescent Labeling of RNA Interior Positions.Molecules (Basel, Switzerland) · 2021Review
- Fabrication of Zero Mode Waveguides for High Concentration Single Molecule Microscopy.Journal of visualized experiments : JoVE · 2020Article
- Dynamics of the context-specific translation arrest by chloramphenicol and linezolid.Nature chemical biology · 2020Article
- Nanoaperture fabrication via colloidal lithography for single molecule fluorescence analysis.PloS one · 2019Article
- Translocation kinetics and structural dynamics of ribosomes are modulated by the conformational plasticity of downstream pseudoknots.Nucleic acids research · 2018Article
- The Antiparallel Dimerization of Myosin X Imparts Bundle Selectivity for Processive Motility.Biophysical journal · 2018Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The pretranslocation complex of the ribosome can undergo spontaneous fluctuations of messenger RNA and transfer RNAs (tRNAs) between classical and hybrid states, and occupation of the hybrid tRNA positions has been proposed to precede translocation. The classical and hybrid state tRNA positions have been extensively characterized when the ribosome is stalled along the messenger RNA by either the absence or delayed addition of elongation factor G (EF-G), or by the presence of antibiotics or GTP analogs that block translocation. However, during multiple ongoing elongation cycles when both EF-G and ternary complexes are present, EF-G can bind to the pretranslocation complex much faster than the timescale of the classic-hybrid transitions. Using single-molecule fluorescence resonance energy transfer between adjacent tRNAs and between A-site tRNA and ribosomal protein L11, we found that the tRNAs do not fluctuate between the hybrid and classical states, but instead adopt a position with fluorescence resonance energy transfer efficiencies between those of the stalled classical and hybrid states.
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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.