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Journal of Bacteriology, August 2005, p. 5852-5856, Vol. 187, No. 16
0021-9193/05/$08.00+0 doi:10.1128/JB.187.16.5852-5856.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Role of Protein Kinase G in Growth and Glutamine Metabolism of Mycobacterium bovis BCG
Liem Nguyen,1,
Anne Walburger,1,
Edith Houben,1
Anil Koul,2,
Stefan Muller,2
Monika Morbitzer,2
Bert Klebl,2
Giorgio Ferrari,1,¶ and
Jean Pieters1*
Biozentrum, University of Basel, Basel, Switzerland,1
Axxima Pharmaceuticals, Munich, Germany2
Received 19 May 2005/
Accepted 31 May 2005
The survival of pathogenic mycobacteria in macrophages requires the eukaryotic enzyme-like serine/threonine protein kinase G. This kinase with unknown specificity is secreted into the cytosol of infected macrophages and inhibits phagosome-lysosome fusion. The pknG gene is the terminal gene in a putative operon containing glnH, encoding a protein potentially involved in glutamine uptake. Here, we report that the deletion of pknG did not affect either glutamine uptake or intracellular glutamine concentrations. In vitro growth of Mycobacterium bovis BCG lacking pknG was identical to that of the wild type. We conclude that in M. bovis BCG, glutamine metabolism is not regulated by protein kinase G.
* Corresponding author. Mailing address: Biozentrum, University of Basel, Klingelbergstrasse 50, CH 4056 Basel, Switzerland. Phone: 00 41 61 267 14 94. E-mail:
jean.pieters{at}unibas.ch.
Present address: University of British Columbia, Vancouver, Canada.
Present address: Centre d'Immunologie de Marseille-Luminy, Marseille, France.
Present address: Janssens Pharmaceuticals, Beersel, Belgium.
¶ Present address: Actelion, Basel, Switzerland.
Journal of Bacteriology, August 2005, p. 5852-5856, Vol. 187, No. 16
0021-9193/05/$08.00+0 doi:10.1128/JB.187.16.5852-5856.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
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