Structure and DNA-binding traits of the transition state regulator AbrB.

Journal Article (Journal Article)

The AbrB protein from Bacillus subtilis is a DNA-binding global regulator controlling the onset of a vast array of protective functions under stressful conditions. Such functions include biofilm formation, antibiotic production, competence development, extracellular enzyme production, motility, and sporulation. AbrB orthologs are known in a variety of prokaryotic organisms, most notably in all infectious strains of Clostridia, Listeria, and Bacilli. Despite its central role in bacterial response and defense, its structure has been elusive because of its highly dynamic character. Orienting its N- and C-terminal domains with respect to one another has been especially problematic. Here, we have generated a structure of full-length, tetrameric AbrB using nuclear magnetic resonance, chemical crosslinking, and mass spectrometry. We note that AbrB possesses a strip of positive electrostatic potential encompassing its DNA-binding region and that its C-terminal domain aids in DNA binding.

Full Text

Duke Authors

Cited Authors

  • Olson, AL; Tucker, AT; Bobay, BG; Soderblom, EJ; Moseley, MA; Thompson, RJ; Cavanagh, J

Published Date

  • November 4, 2014

Published In

Volume / Issue

  • 22 / 11

Start / End Page

  • 1650 - 1656

PubMed ID

  • 25308864

Pubmed Central ID

  • PMC4252516

Electronic International Standard Serial Number (EISSN)

  • 1878-4186

Digital Object Identifier (DOI)

  • 10.1016/j.str.2014.08.018


  • eng

Conference Location

  • United States