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How EF-Tu can contribute to efficient proofreading of aa-tRNA by the ribosome

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Official URL:https://doi.org/10.1038/ncomms13314
PubMed:View item in PubMed
Creators Name:Noel, J.K. and Whitford, P.C.
Journal Title:Nature Communications
Journal Abbreviation:Nat Commun
Volume:7
Page Range:13314
Date:31 October 2016
Abstract:It has long been recognized that the thermodynamics of mRNA–tRNA base pairing is insufficient to explain the high fidelity and efficiency of aminoacyl-tRNA (aa-tRNA) selection by the ribosome. To rationalize this apparent inconsistency, Hopfield proposed that the ribosome may improve accuracy by utilizing a multi-step kinetic proofreading mechanism. While biochemical, structural and single-molecule studies have provided a detailed characterization of aa-tRNA selection, there is a limited understanding of how the physical–chemical properties of the ribosome enable proofreading. To this end, we probe the role of EF-Tu during aa-tRNA accommodation (the proofreading step) through the use of energy landscape principles, molecular dynamics simulations and kinetic models. We find that the steric composition of EF-Tu can reduce the free-energy barrier associated with the first step of accommodation: elbow accommodation. We interpret this effect within an extended kinetic model of accommodation and show how EF-Tu can contribute to efficient and accurate proofreading.
ISSN:2041-1723
Publisher:Nature Publishing Group (U.K.)
Item Type:Article

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