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M605010200v1
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Papers In Press, published online ahead of print July 20, 2006
J. Biol. Chem, 10.1074/jbc.M605010200
Submitted on May 24, 2006
Revised on July 19, 2006
Accepted on July 20, 2006

Regulatory protein phosphorylation in mycoplasma pneumoniae: A PP2C-type phosphatase serves to dephosphorylate HPR(Ser-P)

Sven Halbedel, Julia Busse, Sebastian R. Schmidl, and Jörg Stülke

Dept. of General Microbiology, University of Göttingen, Göttingen 37077

Corresponding Author: jstuelk{at}gwdg.de

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 (HPrK/P). The role of the latter enzyme was studied by constructing a M. pneumoniae hprK mutant defective in HPrK/P. This mutant strain did no longer exhibit HPr kinase activity, but had surprisingly still HPr(Ser-P) phosphatase activity. 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.


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