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Volume 148, Issue 10

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

Abstract

Among the few regulatory proteins encoded by is HPr kinase/phosphatase (HPrK/P), the key regulator of carbon metabolism in low-GC Gram-positive bacteria. The corresponding gene, , and the gene encoding the target protein HPr, , were overexpressed. analysis of the purified proteins confirmed ATP-dependent phosphorylation of HPr by HPrK/P. In contrast to HPrK/P of , which is by default a phosphatase and needs high ATP concentrations for kinase activity, the enzyme exhibits kinase activity at very low ATP concentrations and depends on P 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 and other Gram-positive bacteria differ, they are both modulated by the concentration of ATP, P 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.

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Keyword(s): catabolite repression , FBP, fructose 1,6-bisphosphate , HPr, histidine-containing phosphocarrier protein of the PTS , HPrK/P, HPr kinase/phosphatase , mutagenesis , phosphorylation , PTS, phosphoenolpyruvate:sugar phosphotransferase system and Walker A box
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2002-10-01
2024-04-26
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A novel mode of control of Mycoplasma pneumoniae HPr kinase/phosphatase activity reflects its parasitic lifestyle
Microbiology 148, 3277 (2002); https://doi.org/10.1099/00221287-148-10-3277
/content/journal/micro/10.1099/00221287-148-10-3277
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