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Research Paper |
Lehrstuhl für Mikrobiologie, Institut für Mikrobiologie, Biochemie und Genetik der Friedrich-Alexander-Universität Erlangen-Nürnberg, Staudtstr. 5, D-91058 Erlangen, Germany1
Birla Institute of Scientific Research, Statue Circle, Jaipur 302001, Rajasthan, India2
Author for correspondence: Jörg Stülke. Tel: +49 9131 8528818. Fax: +49 9131 8528082. e-mail: jstuelke{at}biologie.uni-erlangen.de
HPr kinase/phosphatase (HPrK/P) is the key protein in regulation of carbon metabolism in Bacillus subtilis and many other Gram-positive bacteria. Whether this enzyme acts as a kinase or phosphatase is determined by the nutrient status of the cell. Mutational analysis of residues in a Walker A box nucleotide-binding motif revealed that it is not only important for kinase but is also involved in phosphatase activity. In addition, a signature sequence specifically conserved among HPrK/P orthologues is required for phosphatase activity and may be involved in interaction with HPr/HPr-(Ser46)-P. Carbon catabolite repression was abolished in a B. subtilis strain expressing a mutant form of HPrK/P deficient in kinase and phosphatase activities. The growth characteristics of this strain were similar to those of the wild-type. In contrast, B. subtilis strains expressing HPrK/P with partial kinase and no phosphatase activities showed growth impairment but exhibited catabolite repression.
Keywords: phosphorylation, glycolysis, Walker A box, mutagenesis
Abbreviations: CCR, carbon catabolite repression; FBP, fructose 1,6-bisphosphate; HPrK/P, HPr kinase/phosphatase; PTS, phosphotransferase system
J.R. deceased on 31 December 1999; he was formerly at the Department of Biology, University of California at San Diego, La Jolla, CA 92093-0116, USA.
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