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Journal of Bacteriology, June 2002, p. 3044-3052, Vol. 184, No. 11
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.11.3044-3052.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

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

Tanja Eppler,1 Pieter Postma,2 Alexandra Schütz,3 Uwe Völker,3 and Winfried Boos1*

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 EIIAGlc, as well as the adenylate cyclase and the cyclic AMP-catabolite activator protein system, have to be present. We followed the level of EIIAGlc 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 EIIAGlc. Isopropyl-ß-D-thiogalactopyranoside-induced overexpression of EIIAGlc did not prevent repression by G3P, excluding the possibility that G3P-mediated catabolite repression is due to the formation of unphosphorylated EIIAGlc. 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 EIIAGlc 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.

* Corresponding author. Mailing address: Department of Biology, University of Konstanz, 78457 Konstanz, Germany. Phone: 49 7531 88 2658. Fax: 49 7531 88 3356. E-mail: Winfried.Boos{at}uni-konstanz.de.

Journal of Bacteriology, June 2002, p. 3044-3052, Vol. 184, No. 11
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.11.3044-3052.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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