Cyclic AMP receptor protein-dependent repression of heat-labile enterotoxin.

ABSTRACT: Enterotoxigenic Escherichia coli is a major cause of acute diarrheal illness worldwide and is responsible for high infant and child mortality rates in developing nations. Two types of enterotoxins, one heat labile and the other heat stable, are known to cause diarrhea. The expression of soluble heat-labile toxin is subject to catabolite (glucose) activation, and three binding sites for cAMP receptor protein (CRP or CAP) were identified upstream and within the toxin promoter by DNase I footprinting. One CRP operator is centered at -31.5, thus encompassing the promoter's -35 hexamer. Potassium permanganate footprinting revealed that the occupancy of this operator prevents RNA polymerase from forming an open complex in vitro. However, the operator centered at -31.5 is not sufficient for full

SUBMITTER: Bodero MD 

PROVIDER: S-EPMC2632052 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature