Role of protein kinase G in growth and glutamine metabolism of Mycobacterium bovis BCG.
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.
Nguyen
Liem
L
Biozentrum, University of Basel, Klingelbergstrasse 50, CH 4056 Basel, Switzerland.
Walburger
Anne
A
Houben
Edith
E
Koul
Anil
A
Muller
Stefan
S
Morbitzer
Monika
M
Klebl
Bert
B
Ferrari
Giorgio
G
Pieters
Jean
J
D017869:Cyclic GMP-Dependent Protein Kinases / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D015971:Gene Expression Regulation, Enzymologic; D005973:Glutamine / Q000493:pharmacokinetics*; D009163:Mycobacterium bovis / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D014158:Transcription, Genetic / Q000502:physiology; D014316:Tritium
D005973:Glutamine; D014316:Tritium; D017869:Cyclic GMP-Dependent Protein Kinases