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. 2019 Aug 6;9:11381. doi: 10.1038/s41598-019-47916-9

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© The Author(s) 2019

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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Substrate stimulated AtABCG1 ATPase activity. (A) Relative ATPase activity of AtABCG1 in presence of 40 µM fatty acids and fatty alcohols (C₁₆–C₃₀). Significance analysis between basal activity and substrate stimulated ATPase activity was performed by t test. (two-tailed): ***P ≤ 0.0001, **P ≤ 0.01, *P ≤ 0.05. (B,C) Concentration dependent relative AtABCG1 activity in the presence of fatty acids (C₂₄–C₃₀) and fatty alcohols (C₂₆–C₃₀). The ATPase activity of the EQ/HA mutant was subtracted and data fitted according to Michaelis-Menten kinetics. Data represent mean and ±SD of at least three independent replicates. An ATPase activity of 100% corresponds to the basale activity of AtABCG1 in the absence of any substrate.