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1 Department of Biomedical Sciences, Dental School, University of Maryland, Baltimore, 666 W. Baltimore Street, Baltimore, MD 21201, USA
2 Molecular and Cell Biology Program, University of Maryland, Baltimore, 108 N. Greene St, Baltimore, MD 21201, USA
Correspondence
Mark A. Strauch
mas002{at}dental.umaryland.edu
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 (AbrBBA) and purified B. subtilis AbrB (AbrBBS) 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 AbrBBS, and the B. subtilis promoter from the yxbB operon was regulated by AbrBBA.
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