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. 2020 Mar 31;66(4):823–833. doi: 10.1007/s00294-020-01070-2

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© The Author(s) 2020

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — Biochemical properties of Kti12 mutants. a Thermostability profiles of CtKti12 K14 point mutants. Thermal shift assay, curves represent an average of three independent experiments. b Fluorescent polarization study of MANT-ATP bound by Kti12 mutants. CtKti12 WT Kd = 1.5 μM ± 0.2 μM, K14L Kd = 25.0 μM ± 2.4 μM. In case of CtKti12 K14A and K14V we were unable to determine K_d in a measured concentration range. c Relative tRNA^Sec-induced ATPase activity of CtKti12 and AnKti12 mutants, compared to the respective WT versions. Free phosphate concentration was measured using malachite green assay. Bars represent an average of three independent experiments ± standard deviation. Proteins carrying different amino acids at position 14 are color coded (K14 grey, A14 orange, L14 purple and V14 green)