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Originally published In Press as doi:10.1074/jbc.M605010200 on July 20, 2006
J. Biol. Chem., Vol. 281, Issue 36, 26253-26259, September 8, 2006
Regulatory Protein Phosphorylation in Mycoplasma pneumoniae
A PP2C-TYPE PHOSPHATASE SERVES TO DEPHOSPHORYLATE HPr(Ser-P)*
Sven Halbedel1,
Julia Busse,
Sebastian R. Schmidl, and
Jörg Stülke2
From the
Department of General Microbiology, Institute of Microbiology and Genetics, Georg-August University, D-37077 Göttingen, Germany
Among the few regulatory events in the minimal bacterium Mycoplasma pneumoniae is the phosphorylation of the HPr phosphocarrier protein of the phosphotransferase system. In the presence of glycerol, HPr is phosphorylated in an ATP-dependent manner by the HPr kinase/phosphorylase. The role of the latter enzyme was studied by constructing a M. pneumoniae hprK mutant defective in HPr kinase/phosphorylase. This mutant strain no longer exhibited HPr kinase activity but, surprisingly, still had phosphatase activity toward serine-phosphorylated HPr (HPr(Ser-P)). An inspection of the genome sequence revealed the presence of a gene (prpC) encoding a presumptive protein serine/threonine phosphatase of the PP2C family. The phosphatase PrpC was purified and its biochemical activity in HPr(Ser-P) dephosphorylation demonstrated. Moreover, a prpC mutant strain was isolated and found to be impaired in HPr(Ser-P) dephosphorylation. Homologues of PrpC are present in many bacteria possessing HPr(Ser-P), suggesting that PrpC may play an important role in adjusting the cellular HPr phosphorylation state and thus controlling the diverse regulatory functions exerted by the different forms of HPr.
Received for publication, May 24, 2006
, and in revised form, July 19, 2006.
This work is dedicated to Michael Hecker on the occasion of his 60th birthday.
* This work was supported by Deutsche Forschungsgemeinschaft and the Fonds der Chemischen Industrie. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1 and S2.
1 Supported by a personal grant from the Fonds der Chemischen Industrie.
2 To whom correspondence should be addressed: Dept. of General Microbiology, Institute of Microbiology and Genetics, Georg-August University Göttingen, Grisebachstr. 8, D-37077 Göttingen, Germany. Tel.: 49-551-393781; Fax: 49-551-393808; E-mail: jstuelk{at}gwdg.de.

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Copyright © 2006 by the American Society for Biochemistry and Molecular Biology.
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