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Research Paper |
Department of Biological and Chemical Sciences, The University of the West Indies, Cave Hill Campus, Barbados1
Author for correspondence: Sarah L. Sutrina. Tel: +1 246 417 4360. Fax: +1 246 417 4325. e-mail: ssutrina{at}uwichill.edu.bb
A strain of Salmonella typhimurium in which the genes encoding the general phosphoenolpyruvate:sugar phosphotransferase system (PTS) proteins HPr and Enzyme I have been deleted, the normally cryptic gene encoding the fructose-inducible Enzyme I (EI* or EIfructose) is expressed, and the fructose repressor protein is inactive (fruR or cra mutant) was studied. This strain lacks HPr and EI, but expresses FPr (DTP) and EIfructose constitutively. Since FPr and EIfructose can substitute for HPr and EI, the strain grew in minimal liquid medium supplemented with the PTS sugars glucose, fructose, N-acetylglucosamine, mannitol or mannose. However, it showed very poor to negligible growth on the PTS sugar glucitol. It also grew very poorly on the non-PTS sugars maltose, melibiose and especially glycerol. Adding cAMP to the medium allowed growth on glucitol, but did not affect growth on glycerol. We suggest that poor phosphorylation of the regulatory molecule Enzyme IIAglucose by FPr is responsible for these effects.
Keywords: phosphoenolpyruvate:sugar phosphotransferase system, carbon catabolite control, gene regulation, carbohydrate transport
Abbreviations: CAP, catabolite activator protein; DTP, diphosphoryltransfer protein; EI/EII, enzymes I/II; Fru, fructose; Glc, glucose; GlcNAc, N-acetylglucosamine; Gut, glucitol; Mtl, mannitol; PEP, phosphoenolpyruvate; PTS, phosphotransferase system
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B. Reichenbach, D. A. Breustedt, J. Stulke, B. Rak, and B. Gorke Genetic Dissection of Specificity Determinants in the Interaction of HPr with Enzymes II of the Bacterial Phosphoenolpyruvate:Sugar Phosphotransferase System in Escherichia coli J. Bacteriol., July 1, 2007; 189(13): 4603 - 4613. [Abstract] [Full Text] [PDF] |
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