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. 2018 Aug 1;8:11552. doi: 10.1038/s41598-018-29884-8

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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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FliW is not a prerequisite for flagellin recognition by FlhA-C. (a) Coomassie-stained SDS-PAGE of a pulldown assay employing GST-tagged FlhA-C. Flagellin alone does not interacts with FlhA-C (lane 2). FliS alone is able to recruit flagellin to FlhA-C (lane 3), while FliW alone is not (lane 4). Lanes 1, 5, 6 and 7 represent the input of purified GST-FlhA-C, Flagellin, FliS and FliW, respectively. (b) Reconstitution of the FliS/flagellin/FliW/FlhA-C complex on size exclusion chromatography shows an apparent heterotetramer. Arrows indicate the protein size standard in kDa. The inset shows a Coomassie-stained SDS-PAGE of the peak fraction.