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. 2022 Sep 1;12:14862. doi: 10.1038/s41598-022-18958-3

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© The Author(s) 2022

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 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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Influence of membrane-extrinsic domain of TatB on thermal inactivation of CS. (a) CS (0.15 μM) was incubated at 43 °C either alone or in the presence of 1 mM oxaloacetate (OAA) or equimolar yeast Hsp90 (0.15 μM). (b) Same as in (a) but in the presence of TatB^22–171 (1x: 0.15 μM; 4x: 0.6 μM, 8x: 1.2 μM), TatB^22–91 (4x: 0.6 μM), or TatB^{22–171[H109/112/123A]} (4x: 0.6 μM). (c) Same as in (b) but with YpTatB^22–220 and YpTatB^22–91. BSA at a concentration of 0.6 μM (4x) or 1.2 μM (8x) served as negative controls. At the times indicated, aliquots were withdrawn and the activity was determined as described. The solid lines represent single exponential functions fit to the experimental data using Prism 8 software. Data are the average of biological replicates and the error bars represent the standard deviation.