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. 2017 Aug 18;7:8808. doi: 10.1038/s41598-017-08818-w

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© The Author(s) 2017

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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Catalytic activity of mutant derivatives of E. coli TatA carrying single amino acid substitutions within TMH. (A) Amino acid sequence of the N-terminal regions of the chimeric TatA proteins analysed here. (B) In thylakoido complementation assays analysing the chimeric TatA proteins shown in (A). (C) Quantitation of catalytic activities of three (n = 3) independent experiments as shown in (B) given as percentage of the transport rate determined for the antibody-treated assays supplemented with pea TatA. For further details see the legends to Figs 1, 2, and 4.