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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 chimeric TatA proteins in in thylakoido complementation experiments. (A) Amino acid sequence of the N-terminal regions of the chimeric TatA proteins ecoTatA[N22pea], ecoTatA[N19pea], and ecoTatA[N17pea]. The residues derived from pea are depicted in bold. Please note that due to the use of E. coli TatA as reference the number of pea residues in each chimera is actually two residues higher than depicted in the name (see also Fig. 1). (B) I n thylakoido complementation of 16/23 transport by the RTS-generated chimeric TatA proteins shown in (A). For further details see the legends to Figs 1 and 2. (C) Quantitation of catalytic activities as shown in (B) given as percentage of the transport rate determined for the antibody-treated assays supplemented with pea TatA. Both mean values and standard deviations from three (n = 3) independently repeated experiments are shown.