Fig. 3: Acetylation of RutR at K52 and K62 abolishes DNA-binding shown by electrophoretic-mobility shift assays (EMSAs) and isothermal titration calorimetry (ITC).
a. The protein-dsDNA interactions between RutR variants and boxrutA and boxcarA promoter dsDNA fragments were studied in EMSAs. Acetylation of RutR at K52 and K62 strongly impairs dsDNA-binding. One exemplary result of at least three replicates is shown (n = 3). Source data are provided as Source Data file. b. K52- and K62-acetylation in RutR abolishes binding towards boxrutA. Interaction between non-acetylated RutR WT, and K52-/K62-acetylated RutR and promoter boxrutA DNA analyzed by ITC. Shown are exemplary ITC traces (DP: differential power). All interactions were determined at least in three biologically independent experiments and the values are given as means ± standard deviations (n ≥ 3; Supplementary Table 3). Source data are provided as Source Data file. c. K52- and K62-acetylation in RutR impairs binding towards boxcarA as shown by ITC. Shown are exemplary ITC traces (DP: differential power). All interactions were determined at least in three biologically independent experiments and the values are given as means ± standard deviations (n ≥ 3; Supplementary Table 3). Source data are provided as Source Data files.
