@article{mbs:/content/journal/micro/10.1099/mic.0.27803-0, author = "Strauch, Mark A. and Ballar, Petek and Rowshan, Austin J. and Zoller, Katherine L.", title = "The DNA-binding specificity of the Bacillus anthracis AbrB protein", journal= "Microbiology", year = "2005", volume = "151", number = "6", pages = "1751-1759", doi = "https://doi.org/10.1099/mic.0.27803-0", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.27803-0", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", 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.", }