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

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Sullivan, DM; Bobay, BG; Kojetin, DJ; Thompson, RJ; Rance, M; Strauch, MA; Cavanagh, J

Published Date

  • November 2008

Published In

Volume / Issue

  • 16 / 11

Start / End Page

  • 1702 - 1713

PubMed ID

  • 19000822

Pubmed Central ID

  • PMC2606041

Electronic International Standard Serial Number (EISSN)

  • 1878-4186

International Standard Serial Number (ISSN)

  • 0969-2126

Digital Object Identifier (DOI)

  • 10.1016/j.str.2008.08.014


  • eng