Abstract
The protein composition of Escherichia coli W3110 grown in the presence and absence of 5% sodium dodecyl sulfate (SDS) was examined by two-dimensional gel electrophoresis. In SDS-grown cells, at least 4 proteins were turned on, 13 were turned off, 15 were elevated, and 15 were depressed. The 19 unique and elevated SDS-induced spots constituted 7.91% of the total 35S-labeled protein. There was no apparent overlap between these 19 detergent (SDS) stress proteins and those of other known bacterial stress responses. The detergent stress stimulon is a distinct and independent stimulon. Its physiological relevance probably derives from the presence of bile salts in animal gastrointestinal tracts.