title: A DNA mimic: the structure and mechanism of action for the anti-repressor protein AbbA.
abstract: Bacteria respond to adverse environmental conditions by switching on the expression of large numbers of genes that enable them to adapt to unfavorable circumstances. In Bacillus subtilis, many adaptive genes are under the negative control of the global transition state regulator, the repressor protein AbrB. Stressful conditions lead to the de-repression of genes under AbrB control. Contributing to this de-repression is AbbA, an anti-repressor that binds to and blocks AbrB from binding to DNA. Here, we have determined the NMR structure of the functional AbbA dimer, confirmed that it binds to the N-terminal DNA-binding domain of AbrB, and have provided an initial description for the interaction using computational docking procedures. Interestingly, we show that AbbA has structural and surface characteristics that closely mimic the DNA phosphate backbone, enabling it to readily carry out its physiological function.
authors.affiliation: Department of Molecular and Structural Biochemistry, North Carolina State University, Campus Box 7622, 128 Polk Hall, Raleigh, NC 27695, USA.
authors.forename: Ashley T
authors.initials: AT
authors.lastname: Tucker
authors.affiliation: Department of Molecular and Structural Biochemistry, North Carolina State University, Campus Box 7622, 128 Polk Hall, Raleigh, NC 27695, USA.
authors.forename: Benjamin G
authors.initials: BG
authors.lastname: Bobay
authors.affiliation: Department of Molecular and Cellular Biology, Harvard University, 52 Oxford Street, Cambridge, MA 02138, USA.
authors.forename: Allison V
authors.initials: AV
authors.lastname: Banse
authors.affiliation: Department of Molecular and Structural Biochemistry, North Carolina State University, Campus Box 7622, 128 Polk Hall, Raleigh, NC 27695, USA.
authors.forename: Andrew L
authors.initials: AL
authors.lastname: Olson
authors.affiliation: Duke Proteomics Core Facility, Institute for Genome Sciences and Policy, Duke University School of Medicine, Duke University, B02 Levine Sciences Research Center, 450 Research Drive, Durham, NC 27708, USA.
authors.forename: Erik J
authors.initials: EJ
authors.lastname: Soderblom
authors.affiliation: Duke Proteomics Core Facility, Institute for Genome Sciences and Policy, Duke University School of Medicine, Duke University, B02 Levine Sciences Research Center, 450 Research Drive, Durham, NC 27708, USA.
authors.forename: M Arthur
authors.initials: MA
authors.lastname: Moseley
authors.affiliation: Department of Molecular and Structural Biochemistry, North Carolina State University, Campus Box 7622, 128 Polk Hall, Raleigh, NC 27695, USA.
authors.forename: Richele J
authors.initials: RJ
authors.lastname: Thompson
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 North Greene Street, Baltimore, MD 21201, USA.
authors.forename: Kristen M
authors.initials: KM
authors.lastname: Varney
authors.affiliation: Department of Molecular and Cellular Biology, Harvard University, 52 Oxford Street, Cambridge, MA 02138, USA.
authors.forename: Richard
authors.initials: R
authors.lastname: Losick
authors.affiliation: Department of Molecular and Structural Biochemistry, North Carolina State University, Campus Box 7622, 128 Polk Hall, Raleigh, NC 27695, USA. Electronic address: john_cavanagh@ncsu.edu.
authors.forename: John
authors.initials: J
authors.lastname: Cavanagh
mesh_terms: D001412:Bacillus subtilis / Q000737:chemistry* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D062105:Molecular Docking Simulation; D011487:Protein Conformation; D055503:Protein Multimerization
chemical_list: D001426:Bacterial Proteins
keywords: AbbA; DNA mimic; NMR; molecular docking; transition state regulator