The DNA-binding specificity of the Bacillus anthracis AbrB protein
Strauch, Mark A. and Ballar, Petek and Rowshan, Austin J. and Zoller, Katherine L.,, 151, 1751-1759 (2005),
doi = https://doi.org/10.1099/mic.0.27803-0,
publicationName = Microbiology Society,
issn = 1350-0872,
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 (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.,
language=,
type=