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. 2022 Dec 22;51(1):449–462. doi: 10.1093/nar/gkac1189

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© The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 5. — Ribosome-bound THR impairs the elongation cycle. (A) Pre-steady state kinetics of A-site tRNA binding upon interaction of the ternary complex EF-Tu•GTP•Phe-tRNA^Phe(Prf16/17) (0.1 μM) with the 70S initiated ribosomes (0.4 μM) containing fMet-tRNA_i^fMet in the P site. Shown are time courses in the absence (blue) and presence (red) of THR. (B) Pre-steady state kinetics of translocation upon interaction of the 70S pre-translocation ribosome complexes (60 nM) containing deacylated-tRNA_i^fMet in the P site and fMet-Phe-tRNA^Phe(Prf16/17) in the A site with EF-G (2 μM). Color scheme is the same as in panel A. Each time course represents the average of five to seven experimental replicates. Standard deviations associated with the kinetics were calculated using GraphPad Prism software. (C) Time courses of dissociation of peptidyl-tRNA from the A site of the 70S pre-translocation ribosome complexes in the absence (blue) or presence (red) of THR.