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. 2016 Jun 20;44(13):6377–6390. doi: 10.1093/nar/gkw561

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© The Author(s) 2016. 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 License (http://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. — Putative tRNA-binding sites. (A) Methyl transfer activity of the alanine-substituted mutant proteins. The mutant name indicates the site of alanine substitution. The initial velocity of WT _TkoTrm11 is expressed as 100%. Error-bar indicates the standard deviation (SD) that was calculated between three independent experiments. (B) The binding-affinity values of the WT _TkoTrm11 and K151A mutant for Tko tRNA^Trp were analyzed by a gel mobility shift assay. (C) The binding-affinity values of WT _TkoTrm11 and R152A mutant for Tko tRNA^Trp were also analyzed by a gel mobility shift assay. (D) The binding-affinity values of WT _TkoTrm11 and R152A mutant for Tko tRNA^Trp were analyzed by a gel mobility shift assay. The formations of a complex by WT _TkoTrm11 or each of the three mutants with Tko tRNA^Trp and unbound free tRNA were indicated by two black lines labeled on the right side of the gel.