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Bacillus subtilis is a soil-dwelling Gram-positive bacterial species that has been extensively studied as a model of biofilm formation and stress-induced cellular differentiation. The tetrameric protein, SinR, has been identified as a master regulator for biofilm formation and linked to the regulation of the early transition states during cellular stress response, such as motility and biofilm-linked biosynthetic genes. SinR is a 111-residue protein that is active as a dimer of dimers, composed of two distinct domains, a DNA-binding helix-turn-helix N-terminus domain and a C-terminal multimerization domain. In order for biofilm formation to proceed, the antagonist, SinI, must inactivate SinR. This interaction results in a dramatic structural rearrangement of both proteins. Here we report the full-length backbone and side chain chemical shift values in addition to the experimentally derived secondary structure predictions as the first step towards directly studying the complex interaction dynamics between SinR and SinI.

Chemical shift assignments and secondary structure prediction of the master biofilm regulator, SinR, from Bacillus subtilis