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. 2018 Jan 12;8:578. doi: 10.1038/s41598-017-19019-w

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© The Author(s) 2018

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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The presence of SecYEG prevents binding of FtsY to the C1 loop of YidC. In vivo photo cross-linking was performed with BL21 cells expressing either just YidC or together with SecYEG. In both cases pBpa was present at position 399 of YidC. YidC was purified via its His-tag and analysed using antibodies against Ffh (a) or FtsY (b). Note that the YidC amounts which are present in (a) and (b) are displayed in Fig. 1c (α-YidC -bottom). (c) In vivo p-formaldehyde cross-linking was performed with BL21 cells expressing YidC only or together with SecYEG. The cross-linked material was analysed with α-FtsY (top) and α-YidC (bottom) antibodies. Uncropped images are displayed in Supplementary Figure S4.