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Journal of Bacteriology, April 2000, p. 2033-2036, Vol. 182, No. 7
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Dephosphorylation of the Escherichia coli Transcriptional Antiterminator BglG by the Sugar Sensor BglF Is the Reversal of Its Phosphorylation

Qing Chen,1 Pieter W. Postma,2 and Orna Amster-Choder1,*

Department of Molecular Biology, The Hebrew University-Hadassah Medical School, Jerusalem 91120, Israel,1 and E. C. Slater Institute, BioCentrum, University of Amsterdam, 1018 TV Amsterdam, The Netherlands2

Received 8 June 1998/Accepted 8 December 1999

The Escherichia coli BglF protein catalyzes transport and phosphorylation of beta -glucosides. In addition, BglF is a membrane sensor which reversibly phosphorylates the transcriptional regulator BglG, depending on beta -glucoside availability. Therefore, BglF has three enzymatic activities: beta -glucoside phosphotransferase, BglG phosphorylase, and phospho-BglG (BglG-P) dephosphorylase. Cys-24 of BglF is the active site which delivers the phosphoryl group either to the sugar or to BglG. To characterize the dephosphorylase activity, we asked whether BglG-P can give the phosphoryl group back to Cys-24 of BglF. Here we provide evidence which is consistent with the interpretation that Cys-24-P is an intermediate in the BglG-P dephosphorylation reaction. Hence, the dephosphorylation reaction catalyzed by BglF proceeds via reversal of the phosphorylation reaction.

* Corresponding author. Mailing address: Department of Molecular Biology, The Hebrew University-Hadassah Medical School, POB 12272, Jerusalem 91120, Israel. Phone: 972 2 675 8460. Fax: 972 2 6784010. E-mail: amster{at}cc.huji.ac.il.

Journal of Bacteriology, April 2000, p. 2033-2036, Vol. 182, No. 7
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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