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. 2020 Jul 30;11:3796. doi: 10.1038/s41467-020-17606-6

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© The Author(s) 2020

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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Fig. 7 — EMSA experiment showing the interaction between a 41 bp DNA fragment containing matS (MW_theo = 27 kDa) and 3 μM of MatP (MW_theo = 21 kDa), his-tagged MatPΔ20 (MW_theo = 32 kDa), or untagged MatPΔ20 (MW_theo = 18 kDa). Based on the theoretical molecular weight (MW_theo) of the DNA molecule and of the different proteins used, we have estimated the theoretical molecular weight of the different protein-DNA complexes following three different hypotheses. Hypothesis 1 (Hyp1) proposes that MatP and MatPΔ20 bind DNA as a dimer; hypothesis 2 (Hyp2) proposes that MatP and MatPΔ20 bind DNA as a tetramer; hypothesis 3 (Hyp3) proposes that MatP binds DNA as a tetramer, whereas MatPΔ20 binds DNA as a dimer. Note that only hypothesis 3 proposes theoretical molecular weights that are in accordance with EMSA results.