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. 2021 Feb 9;49(5):2684–2699. doi: 10.1093/nar/gkab033

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© The Author(s) 2021. 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 (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 2. — How m⁶A modification affects the impact of [Mg²⁺] variation and aminoglycoside addition on the efficiency of codon reading by T₃. Fractions of GTPs hydrolyzed on T₃ (y-axis) at different free [Mg²⁺] values and reaction times (x-axis, log₁₀ display) for T₃ reading of unmodified (A) GAA (closed black squares), GAA + paromomycin (Par) (open black squares), GAU (closed red circles), GAU + Par (open red circles) and modified. (B) Gm⁶AA (closed black squares), Gm⁶AA + Par (open black squares), Gm⁶AU (closed red circles), Gm⁶AU+Par (open red circles). k_cat/K_m-values for GTP hydrolysis on T₃ (y-axis) at different free [Mg²⁺] values for T₃ of unmodified. (C) GAA (closed black squares), GAA+Par (open black squares), GAU (closed red circles), GAU+Par (open red circles), GAU+Neo (open green circle) and modified. (D) Gm⁶AA (closed black squares), Gm⁶AA+Par (open black squares), Gm⁶AU (closed red circles), Gm⁶AU+Par (open red circles). All k_cat/K_m-data are summarized in Table 1. (A) and (B) were performed at 2.3 mM Free Mg^2+.