title: Structure and DNA-binding traits of the transition state regulator AbrB.
abstract: 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.
authors.affiliation: Department of Molecular and Structural Biochemistry, North Carolina State University, 128 Polk Hall, Raleigh, NC 27659, USA.
authors.forename: Andrew L
authors.initials: AL
authors.lastname: Olson
authors.affiliation: Department of Molecular and Structural Biochemistry, North Carolina State University, 128 Polk Hall, Raleigh, NC 27659, USA.
authors.forename: Ashley T
authors.initials: AT
authors.lastname: Tucker
authors.affiliation: Department of Molecular and Structural Biochemistry, North Carolina State University, 128 Polk Hall, Raleigh, NC 27659, USA.
authors.forename: Benjamin G
authors.initials: BG
authors.lastname: Bobay
authors.affiliation: Duke Proteomics Core Facility, Institute for Genome Sciences and Policy, School of Medicine, B02 Levine Sciences Research Center, 450 Research Drive, Duke University, Durham, NC 27710, USA.
authors.forename: Erik J
authors.initials: EJ
authors.lastname: Soderblom
authors.affiliation: Duke Proteomics Core Facility, Institute for Genome Sciences and Policy, School of Medicine, B02 Levine Sciences Research Center, 450 Research Drive, Duke University, Durham, NC 27710, USA.
authors.forename: M Arthur
authors.initials: MA
authors.lastname: Moseley
authors.affiliation: Department of Molecular and Structural Biochemistry, North Carolina State University, 128 Polk Hall, Raleigh, NC 27659, USA.
authors.forename: Richele J
authors.initials: RJ
authors.lastname: Thompson
authors.affiliation: Department of Molecular and Structural Biochemistry, North Carolina State University, 128 Polk Hall, Raleigh, NC 27659, USA. Electronic address: jcavana@ncsu.edu.
authors.forename: John
authors.initials: J
authors.lastname: Cavanagh
mesh_terms: D001412:Bacillus subtilis / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D004269:DNA, Bacterial / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D062105:Molecular Docking Simulation; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D014157:Transcription Factors / Q000737:chemistry* / Q000378:metabolism*
chemical_list: C060762:AbrB protein, Bacillus subtilis; D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; D014157:Transcription Factors