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Title: Insights into the nature of DNA binding of AbrB-like transcription factors.

Authors: Sullivan, Daniel M; Bobay, Benjamin G; Kojetin, Douglas J; Thompson, Richele J; Rance, Mark; Strauch, Mark A; Cavanagh, John

Published In Structure, (2008 Nov 12)

Abstract: 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 AbrBN(55) 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.

PubMed ID: 19000822 Exiting the NIEHS site

MeSH Terms: No MeSH terms associated with this publication

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