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A novel mode of control of Mycoplasma pneumoniae HPr kinase/phosphatase activity reflects its parasitic lifestyle

Lehrstuhl für Mikrobiologie, Institut für Mikrobiologie, Biochemie und Genetik der Friedrich-Alexander-Universität Erlangen-Nürnberg, Staudtstr. 5,D-91058 Erlangen, Germany¹

Author for correspondence: Tel: +49 9131 8528818. Fax: +49 9131 8528082. e-mail: jstuelke{at}biologie.uni-erlangen.de

Among the few regulatory proteins encoded by Mycoplasma pneumoniae is HPr kinase/phosphatase (HPrK/P), the key regulator of carbon metabolism in low-GC Gram-positive bacteria. The corresponding gene, hprK, and the gene encoding the target protein HPr, ptsH, were overexpressed. In vitro analysis of the purified proteins confirmed ATP-dependent phosphorylation of HPr by HPrK/P. In contrast to HPrK/P of Bacillus subtilis, which is by default a phosphatase and needs high ATP concentrations for kinase activity, the M. pneumoniae enzyme exhibits kinase activity at very low ATP concentrations and depends on P_i for phosphatase activity. This inverted control of enzymic activity may result from the adaptation to very different ecological niches. While the standard activities of HPrK/P from M. pneumoniae and other Gram-positive bacteria differ, they are both modulated by the concentration of ATP, P_i and glycolytic intermediates. Site-directed mutagenesis of a potential ATP-binding site and of the HPrK/P signature sequence resulted in four different activity classes: (i) inactive proteins, (ii) enzymes with reduced kinase and phosphatase activities, (iii) enzymes that had lost phosphatase, but not kinase activity, and (iv) enzymes that exhibited increased phosphatase activity.

Keywords: phosphorylation, Walker A box, mutagenesis, catabolite repression

Abbreviations: PTS, phosphoenolpyruvate:sugar phosphotransferase system; HPr, histidine-containing phosphocarrier protein of the PTS; HPrK/P, HPr kinase/phosphatase; FBP, fructose 1,6-bisphosphate

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