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. 2020 Apr 29;20:104. doi: 10.1186/s12866-020-01796-6

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© The Author(s) 2020

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 7 — LiaR-DNase I footprint analysis of P_liaI. The DNA fragment was labeled on the top strand at the 5′-end with [γ-³²P]-ATP. The position of the protection site in the gel was determined from the running of the A, T, G and C standard reactions (Additional file 8: Figure S8). Protection of P_liaI by LiaR and LiaRD54A was investigated in the absence and presence of acetyl phosphate and at different protein concentrations. The primary binding site is indicated by a solid line, and the secondary binding site is indicated by a dashed line. The hypersensitive site at − 79 is indicated by an arrow