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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. 5 — Oligomerization studies on LiaR. The oligomerization state of LiaR was analyzed by a 10% native-PAGE. Samples with or without acetyl phosphate (AcP) were incubated for 1 h in PB, at room temperature, and were resolved by gel electrophoresis. VraR was used as a control of the effect of phosphorylation in the oligomerization state of the protein. LiaS at 10 μM was added to investigate its phosphatase activity and its effect on the oligomerization of LiaR