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A DNA mimic: the structure and mechanism of action for the anti-repressor protein AbbA.

Publication ,  Journal Article
Tucker, AT; Bobay, BG; Banse, AV; Olson, AL; Soderblom, EJ; Moseley, MA; Thompson, RJ; Varney, KM; Losick, R; Cavanagh, J
Published in: J Mol Biol
May 1, 2014
Published version (DOI) Open Access Copy (Duke) Link to item

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.

Duke Scholars

Benjamin Bobay
Author Benjamin Bobay Radiology
Erik James Soderblom
Author Erik James Soderblom Cell Biology
Martin Arthur Moseley III
Author Martin Arthur Moseley III Cell Biology

Published In

J Mol Biol

DOI

10.1016/j.jmb.2014.02.010

EISSN

1089-8638

Publication Date

May 1, 2014

Volume

426

Issue

9

Start / End Page

1911 / 1924

Location

Netherlands

Related Subject Headings

  • Protein Multimerization
  • Protein Conformation
  • Molecular Docking Simulation
  • Models, Molecular
  • Magnetic Resonance Spectroscopy
  • Biochemistry & Molecular Biology
  • Bacterial Proteins
  • Bacillus subtilis
  • 3107 Microbiology
  • 3101 Biochemistry and cell biology
 

Citation

APA
Chicago
ICMJE
MLA
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Tucker, A. T., Bobay, B. G., Banse, A. V., Olson, A. L., Soderblom, E. J., Moseley, M. A., … Cavanagh, J. (2014). A DNA mimic: the structure and mechanism of action for the anti-repressor protein AbbA. J Mol Biol, 426(9), 1911–1924. https://doi.org/10.1016/j.jmb.2014.02.010
Tucker, Ashley T., Benjamin G. Bobay, Allison V. Banse, Andrew L. Olson, Erik J. Soderblom, M Arthur Moseley, Richele J. Thompson, Kristen M. Varney, Richard Losick, and John Cavanagh. “A DNA mimic: the structure and mechanism of action for the anti-repressor protein AbbA.” J Mol Biol 426, no. 9 (May 1, 2014): 1911–24. https://doi.org/10.1016/j.jmb.2014.02.010.
Tucker AT, Bobay BG, Banse AV, Olson AL, Soderblom EJ, Moseley MA, et al. A DNA mimic: the structure and mechanism of action for the anti-repressor protein AbbA. J Mol Biol. 2014 May 1;426(9):1911–24.
Tucker, Ashley T., et al. “A DNA mimic: the structure and mechanism of action for the anti-repressor protein AbbA.” J Mol Biol, vol. 426, no. 9, May 2014, pp. 1911–24. Pubmed, doi:10.1016/j.jmb.2014.02.010.
Tucker AT, Bobay BG, Banse AV, Olson AL, Soderblom EJ, Moseley MA, Thompson RJ, Varney KM, Losick R, Cavanagh J. A DNA mimic: the structure and mechanism of action for the anti-repressor protein AbbA. J Mol Biol. 2014 May 1;426(9):1911–1924.
Journal cover image

Published In

J Mol Biol

DOI

10.1016/j.jmb.2014.02.010

EISSN

1089-8638

Publication Date

May 1, 2014

Volume

426

Issue

9

Start / End Page

1911 / 1924

Location

Netherlands

Related Subject Headings

  • Protein Multimerization
  • Protein Conformation
  • Molecular Docking Simulation
  • Models, Molecular
  • Magnetic Resonance Spectroscopy
  • Biochemistry & Molecular Biology
  • Bacterial Proteins
  • Bacillus subtilis
  • 3107 Microbiology
  • 3101 Biochemistry and cell biology