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. 2019 Mar 6;9:3681. doi: 10.1038/s41598-018-38386-6

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© The Author(s) 2019

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 α3-helix of KhpA is critical for self-dimerization and for EloR/KhpA complex formation. (A) Measurements of β-galactosidase production in BACTH assays testing the interaction between EloR and KhpA, KhpA^I61F or KhpA^I61Y in addition to EloR^L239Y against KhpA (green bars). β-galactosidase production resulting from homodimerization of KhpA, KhpA^I61F and KhpA^I61Y is represented by orange bars, while negative and positive controls are shown in grey. (B) Immunoblot detection of 3xflag-EloR in strain RH425, SPH448, AW334 and AW336. A Crosslinked EloR/KhpA complex was observed in strain AW336 under non-reducing conditions, but not after reduction with β-mercaptoethanol (+BME). The image is cropped from the full-length immunoblot, which is shown in Fig. S3.