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. 2019 Nov 28;48(1):e3. doi: 10.1093/nar/gkz954

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© The Author(s) 2019. 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 Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 3. — Sequence-function characterization of WT BenM and evolved archetypical variants. (A) Amino-acid substitution profiles for the four phenotypic categories (left) of evolved BenM variants, with heat-mapping to indicate the BenM variant fold-induction for the lowest inducer concentration with a significant (P < 0.05) response compared to control medium. The displayed score (right) for the archetypical variants of improved dynamic and operational range, as well as for change of specificity, is indicative of fold-change between inducer and control medium for the lowest inducer concentration significantly improving ON state compared to OFF state according to the equation given in Methods. For the inversion-of-function variants, the score represents the correlation coefficient between dose-response curves for WT BenM and evolved variants calculated according to equation given Methods. (B) Depictions of BenM monomeric structures (PDB 3k1n), with domains color-coded for mutational spaces for each of the four phenotypic categories. (C–G) Dose-response curves for BenM variants, WT BenM, and reporter-only control (No BenM). Data represents mean fold-induction for dynamic range (C), operational range (D), and specificity (F–G) variants, whereas for inversion-of-function variants (E), mean fluorescence intensities are displayed. For all plots data represents means ± one standard deviation from three biological replicates. a.u. = arbitrary units.