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. 2018 Jan;24(1):56–66. doi: 10.1261/rna.062893.117

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© 2018 McKenney et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society

This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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FIGURE 3. — TbADAT2/3 catalytic residues do not contribute to increased affinity of TbTrm140 for tRNA. (A) EMSA of TbTrm140 to assess binding to tRNA^Thr_CGU in the presence of two TbADAT2/3 catalytic mutants (E92A) and (B) (C291A). (C) EMSA of TbTrm140 to tRNA^Thr_CGU in the presence of TbADAT2/3 C-terminal deletion binding mutant. In each panel, lanes 1 and 2 show a no-enzyme control reaction and a control reaction with no mutant TbADAT2/3 added, respectively. Lanes 3–7 show an increasing concentration of TbTrm140 (0.04, 0.08, 0.16, 0.32, and 0.56 µM, respectively). The bottom panels show the single-ligand binding isotherms used to calculate the individual K_dapp. Each graph represents at least five independent replicates.