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. 2021 Jun 23;12:680553. doi: 10.3389/fmicb.2021.680553

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Copyright © 2021 Merchel Piovesan Pereira, Adil Salim, Rai and Tagkopoulos.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Glutaraldehyde-evolved and tolerant E. coli MG1655 strains independently selected for mutations in yqhC. (A) Position information within the yqhC gene of the mutations observed for the evolved strains Glu1, Glu2, Glu3. The bases and amino acids (aa) mutated are indicated. (B) Fitness of glutaraldehyde-evolved strains over the parent or media-only evolved strains as measured in competition assays. Fitness above one denotes a fitness advantage. The experiment was performed in duplicate. (C) A representative gel-shift (EMSA) assay for each of the YqhC variants. The 100 bp DNA ladder (NEB) was applied to the gel for reference. The bottom arrow points to the free probe, and the top arrow indicates the YqhC protein bound to the DNA probe (promoter region of yqhD-dkgA operon). (D) A gel-shift (EMSA) assay with a negative-control DNA probe (non-binding DNA sequence) for reference. The concentration of protein for the parent YqhC was varied between 5 and 115 ng/μL. (E) Growth curves in M9 media with the presence of glutaraldehyde (concentrations indicated in the graph’s legend) for the evolved strains Glu1, Glu2 and Glu3 and their respective “repair” strains, in which the mutant yqhC was replaced with the wild-type version of the gene in the respective background strain.