Nature Communications · 2015 · 72 citations · 66 references
Life SciencesBiochemistryMolecular BiologyMolecular BiophysicsPost-translational ModificationStructural BiologyRibosome StructureTranslation In EukaryotesElongation Factor G FunctionFluorescence Resonance Energy TransferRibosomal Conformational ChangesRibosomal TranslocationRibosome Conformational DynamicsSingle-molecule Fluorescence ImagingTransfer Rna DynamicsTranslation Elongation Factors
The coupled translocation of transfer RNA and messenger RNA through the ribosome entails large-scale structural rearrangements, including step-wise movements of the tRNAs. Recent structural work has visualized intermediates of translocation induced by elongation factor G (EF-G) with tRNAs trapped in chimeric states with respect to 30S and 50S ribosomal subunits. The functional role of the chimeric states is not known. Here we follow the formation of translocation intermediates by single-molecule fluorescence resonance energy transfer. Using EF-G mutants, a non-hydrolysable GTP analogue, and fusidic acid, we interfere with either translocation or EF-G release from the ribosome and identify several rapidly interconverting chimeric tRNA states on the reaction pathway. EF-G engagement prevents backward transitions early in translocation and increases the fraction of ribosomes that rapidly fluctuate between hybrid, chimeric and posttranslocation states. Thus, the engagement of EF-G alters the energetics of translocation towards a flat energy landscape, thereby promoting forward tRNA movement.
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Pattern Recognition and Machine Learning
Journal of Electronic Imaging · 2007 · 22.1K citations
Structures of the Bacterial Ribosome at 3.5 A Resolution
B.S. Schuwirth, M.A. Borovinskaya, C.W. Hau et al. · Science · 2005 · 1.4K citations · Full text
Intermediate states in the movement of transfer RNA in the ribosome
Danesh Moazed, Harry F. Noller · Nature · 1989 · 739 citations
Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
Marina V. Rodnina, Andreas Savelsbergh, Vladimir I. Katunin et al. · Nature · 1997 · 523 citations