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. 2021 Aug 20;49(17):10120–10135. doi: 10.1093/nar/gkab711

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© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 6. — EMSA analysis of the effect of different mutations in the IdeR recognition helix on DNA binding by IdeR. Binding of the (A) IdeR^Q43A and (B) IdeR^P39G variants to the consensus DNA sequence. The IdeR variants were added in increasing concentrations (15 nM–2.25 μM dimer) to 30 nM fluorescence-labeled double-stranded DNA probe in the presence of 30 μM Co²⁺ and competitor DNA. Protein–DNA complexes were resolved on a 4% Tris-acetate polyacrylamide gel. The left-most lane is a control reaction without protein. ds, unbound double-stranded DNA probe; ss, non-hybridized single-stranded DNA; C, protein–dsDNA complex.