Understanding the DNA recognition and binding by the AbrB-like family of transcriptional regulators is of significant interest since these proteins enable bacteria to elicit the appropriate response to diverse environmental stimuli. Although these "transition-state regulator" proteins have been well characterized at the genetic level, the general and specific mechanisms of DNA binding remain elusive. We present RDC-refined NMR solution structures and dynamic properties of the DNA-binding domains of three Bacillus subtilis transition-state regulators: AbrB, Abh, and SpoVT. We combined previously investigated DNase I footprinting, DNA methylation, gel-shift assays, and mutagenic and NMR studies to generate a structural model of the complex between AbrBN5s and its cognate promoter, abrB8. These investigations have enabled us to generate a model for the specific nature of the transition-state regulator-DNA interaction, a structure that has remained elusive thus far.
Insights into the Nature of DNA Binding of AbrB-like Transcription Factors
Sullivan, D. M., Bobay, B. G., Kojetin, D. J., Thompson, R. J., Rance, M., Strauch, M. A., & Cavanagh, J. (2008). Insights into the Nature of DNA Binding of AbrB-like Transcription Factors. Structure, 16(11), 1702-1713. https://doi.org/10.1016/j.str.2008.08.014