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Microbiology. 2005 Jun;151(Pt 6):1751-9.

The DNA-binding specificity of the Bacillus anthracis AbrB protein.

Author information

1
Department of Biomedical Sciences, Dental School, University of Maryland, Baltimore, MD 21201, USA. mas002@dental.umaryland.edu

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).

PMID:
15941984
DOI:
10.1099/mic.0.27803-0
[Indexed for MEDLINE]

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