Mechanism of tRNA Translocation on the Ribosome |
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Authors: | Rodnina M V Semenkov Yu P Savelsbergh A Katunin V I Peske F Wilden B Wintermeyer W |
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Institution: | (1) Institute of Physical Biochemistry, University of Witten/Herdecke, Witten, 58448, Germany;(2) Russian Academy of Sciences, St. Petersburg Nuclear Physics Institute, Gatchina, 188350, Russia;(3) Institute of Molecular Biology, University of Witten/Herdecke, Witten, 58448, Germany |
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Abstract: | During the translocation step of the elongation cycle of peptide synthesis two tRNAs together with the mRNA move synchronously and rapidly on the ribosome. Translocation is catalyzed by the elongation factor G (EF-G) and requires GTP hydrolysis. The fundamental biochemical features of the process were worked out in the 1970–80s, to a large part by A.S. Spirin and his colleagues. Recent results from pre-steady-state kinetic analysis and cryoelectron microscopy suggest that translocation is a multistep dynamic process that entails large-scale structural rearrangements of both ribosome and EF-G. Kinetic and thermodynamic data, together with the structural information on the conformational changes in the ribosome and EF-G, provide a detailed mechanistic model of translocation and suggest a mechanism of translocation catalysis by EF-G. |
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Keywords: | protein synthesis GTPase motor protein tRNA translocation hybrid states kinetics catalysis |
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