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. 2020 Jul 23;10:12295. doi: 10.1038/s41598-020-69225-2

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© The Author(s) 2020

Open Access This 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Dependence of NisT ATPase rate on different substrates. The ATPase rate of purified 10HNisT was analyzed in the presence of different substrates. (a) The leader peptide of NisA (NisA_LP, black dots), (b) uNisA (grey dots), (c) dNisA (blue dots) and (d) mNisA (red dots) was used in various concentrations (µM) and the ATPase rate is shown as normalized ATPase rate (%). The basal ATPase rate (from 10HNisT without any substrate; compare Fig. 3) was set as 100% (dashed line) and further values were normalized accordingly. The assays were performed in at least four independent experiments and are represented as means ± s.d. (n = 4). The means were analyzed by a one-way ANOVA and the differences were not significant (p-value: ≥ 0.05). ns: not significant.