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. 2019 Aug 9;47(18):9609–9618. doi: 10.1093/nar/gkz698

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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 License (http://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 3. — The apparent K_d of LacI is enhanced by using a stabilized version of LacI. (A) Analysis of a simple binding reaction with or without active degradation shows that a high degradation rate can significantly increase the effective K_d. k_on: binding rate, k_off: dissociation rate, k_deg: degradation rate. (B) Generating low concentration of stable GFP-LacI using a promoter of low activity (REV1pr). (C) Fluorescent images of the FROS on the original 256× LacO array with the constructs in B. (D) Quantification of the normalized dot intensity (left panel) and the free protein concentration (right panel) in these two strains (N = 137 and 57, respectively). The dot intensity increases by 15-fold (P-value < 0.0001) with the stable GFP-LacI, while the background concentration is about the same.