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.
Type
Journal articleSubject
Bacillus subtilisBacterial Proteins
Magnetic Resonance Spectroscopy
Protein Conformation
Models, Molecular
Protein Multimerization
Molecular Docking Simulation
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https://hdl.handle.net/10161/28902Published Version (Please cite this version)
10.1016/j.jmb.2014.02.010Publication Info
Tucker, Ashley T; Bobay, Benjamin G; Banse, Allison V; Olson, Andrew L; Soderblom,
Erik J; Moseley, M Arthur; ... Cavanagh, John (2014). A DNA mimic: the structure and mechanism of action for the anti-repressor protein
AbbA. Journal of molecular biology, 426(9). pp. 1911-1924. 10.1016/j.jmb.2014.02.010. Retrieved from https://hdl.handle.net/10161/28902.This is constructed from limited available data and may be imprecise. To cite this
article, please review & use the official citation provided by the journal.
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Show full item recordScholars@Duke
Benjamin Bobay
Assistant Professor in Radiology
I am the Assistant Director of the Duke University NMR Center and an Assistant Professor
in the Duke Radiology Department. I was originally trained as a structural biochemist
with an emphasis on utilizing NMR and continue to use this technique daily helping
collaborators characterize protein structures and small molecules through a diverse
set of NMR experiments. Through the structural characterization of various proteins,
from both planta and eukaryotes, I have developed a robust protocol of ut
Martin Arthur Moseley III
Adjunct Professor in the Department of Cell Biology
Erik James Soderblom
Associate Research Professor of Cell Biology
Director, Proteomics and Metabolomics Core Facility
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