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Updated: Aug 17, 2026

Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
The DNA-binding specificity of the Bacillus anthracis AbrB protein
Mark A Strauch1, Petek Ballar2, Austin J Rowshan1
1Department of Biomedical Sciences, Dental School, University of Maryland, Baltimore, 666 W. Baltimore Street, Baltimore, MD 21201, USA.
Abstract:
The Bacillus subtilis AbrB protein is a DNA-binding global regulator of a plethora of functions that are expressed during the transition from exponential growth to stationary phase and under suboptimal growth conditions. AbrB orthologues have been identified in a variety of prokaryotic organisms, notably in all species of Bacillus, Clostridium and Listeria that have been examined. Based on amino acid sequence identity in the N-terminal domains of the orthologues from B. subtilis and Bacillus anthracis, it was predicted that the proteins might display identical DNA-binding specificities. The binding of purified B. anthracis AbrB (AbrB(BA)) and purified B. subtilis AbrB (AbrB(BS)) at DNA targets of B. subtilis, B. anthracis and a synthetic origin was compared. In all cases examined, DNA-binding specificity was identical as judged by DNase I footprinting. In B. subtilis cells, the B. anthracis promoters from the atxA and abrB genes were regulated by AbrB(BS), and the B. subtilis promoter from the yxbB operon was regulated by AbrB(BA).
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