Fig. 2: DNA-binding by RemA.
From: Structural and functional characterization of the bacterial biofilm activator RemA
a Electrostatic surface of the RemA 8-mer (side and back view, PDB-ID: “7BM2”). ‘S’ indicates sulfates found at the surface of the crystal structure. A detailed view on the coordination of the sulfates S1, S2, and S3 is given in figure panels (b) and (c), respectively. d Structure of a RemA dimer of (RemA)8 (left side; PDB-ID: “7BM2”), AgrA-C bound to DNA (middle; PDB-ID: “3BS1”), and the superimposition of both (right side). e EMSAs of wild type RemA, RemA-R50A, and RemA-R51A with a DNA fragment containing the regulatory epsA region. Results were confirmed with three independent preparations of recombinant proteins. f β-galactosidase activity in strains carrying PepsA-lacZ fusions. Activity assays of a remA mutant strain (n = 5) and of complementation strains encoding inducible (+ IPTG), ectopic copies of wild type RemA (n = 9), RemA-R50A (n = 3), and RemA-R51A (n = 3). Each point reflects the LacZ activity measured in a biological replicate. Data are presented as mean from independent experiments. Source data are provided as a source data file. g Biofilm assays of wildtype B. subtilis 3610, a remA deletion strain (ΔremA) and its complementation with wildtype RemA (ΔremA + remA), remA-R50A (R50A), and remA-R51A (R51A). The length of the scale bars corresponds to 0.5 cm. Biofilm formation was analyzed in at least two independent experiments for each strain with several independently grown colonies per experiment. The colonies shown represent typical examples.
