This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Eppler, T. Articles by Boos, W. Search for Related Content PubMed PubMed Citation Articles by Eppler, T. Articles by Boos, W.

Glycerol-3-Phosphate-Induced Catabolite Repression in Escherichia coli

Department of Biology, University of Konstanz, 78457 Konstanz,¹ Department of Microbiology, University of Marburg, 35032 Marburg, Germany,³ Swammerdam Institute for Life Sciences, University of Amsterdam, 1018 WS Amsterdam, The Netherlands²

Received 12 December 2001/ Accepted 11 March 2002

The formation of glycerol-3-phosphate (G3P) in cells growing on TB causes catabolite repression, as shown by the reduction in malT expression. For this repression to occur, the general proteins of the phosphoenolpyruvate-dependent phosphotransferase system (PTS), in particular EIIA^Glc, as well as the adenylate cyclase and the cyclic AMP-catabolite activator protein system, have to be present. We followed the level of EIIA^Glc phosphorylation after the addition of glycerol or G3P. In contrast to glucose, which causes a dramatic shift to the dephosphorylated form, glycerol or G3P only slightly increased the amount of dephosphorylated EIIA^Glc. Isopropyl-ß-D-thiogalactopyranoside-induced overexpression of EIIA^Glc did not prevent repression by G3P, excluding the possibility that G3P-mediated catabolite repression is due to the formation of unphosphorylated EIIA^Glc. A mutant carrying a C-terminally truncated adenylate cyclase was no longer subject to G3P-mediated repression. We conclude that the stimulation of adenylate cyclase by phosphorylated EIIA^Glc is controlled by G3P and other phosphorylated sugars such as D-glucose-6-phosphate and is the basis for catabolite repression by non-PTS compounds. Further metabolism of these compounds is not necessary for repression. Two-dimensional polyacrylamide gel electrophoresis was used to obtain an overview of proteins that are subject to catabolite repression by glycerol. Some of the prominently repressed proteins were identified by peptide mass fingerprinting. Among these were periplasmic binding proteins (glutamine and oligopeptide binding protein, for example), enzymes of the tricarboxylic acid cycle, aldehyde dehydrogenase, Dps (a stress-induced DNA binding protein), and D-tagatose-1,6-bisphosphate aldolase.

This article has been cited by other articles:

• Deutscher, J., Francke, C., Postma, P. W. (2006). How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria. Microbiol. Mol. Biol. Rev. 70: 939-1031 [Abstract] [Full Text]  
• Dippel, R., Boos, W. (2005). The Maltodextrin System of Escherichia coli: Metabolism and Transport. J. Bacteriol. 187: 8322-8331 [Abstract] [Full Text]  
• Dippel, R., Bergmiller, T., Bohm, A., Boos, W. (2005). The Maltodextrin System of Escherichia coli: Glycogen-Derived Endogenous Induction and Osmoregulation. J. Bacteriol. 187: 8332-8339 [Abstract] [Full Text]  
• Lee, S. K., Newman, J. D., Keasling, J. D. (2005). Catabolite Repression of the Propionate Catabolic Genes in Escherichia coli and Salmonella enterica: Evidence for Involvement of the Cyclic AMP Receptor Protein. J. Bacteriol. 187: 2793-2800 [Abstract] [Full Text]  
• Xavier, K. B., Bassler, B. L. (2005). Regulation of Uptake and Processing of the Quorum-Sensing Autoinducer AI-2 in Escherichia coli. J. Bacteriol. 187: 238-248 [Abstract] [Full Text]  
• Polen, T., Rittmann, D., Wendisch, V. F., Sahm, H. (2003). DNA Microarray Analyses of the Long-Term Adaptive Response of Escherichia coli to Acetate and Propionate. Appl. Environ. Microbiol. 69: 1759-1774 [Abstract] [Full Text]