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Infection and Immunity, November 1999, p. 5676-5682, Vol. 67, No. 11
Department of Medicine, Division of
Infectious Diseases, University of British Columbia, Vancouver,
British Columbia, Canada V5Z 3J5
Received 24 June 1999/Returned for modification 29 July
1999/Accepted 26 August 1999
PknB is a member of the newly discovered eukaryotic-like protein
serine/threonine kinase (PSTK) family of proteins. The pknB gene was cloned and expressed in Escherichia coli. The
active recombinant protein was purified and shown to be reactive with antiphosphoserine antibodies, as well as with antibodies to the phosphorylated eukaryotic Ser/Thr kinases mitogen-activated protein kinase kinase 3 and 6, P38, and Creb. In vitro kinase assays
demonstrated that PknB is a functional kinase that is
autophosphorylated on serine/threonine residues and is also able to
phosphorylate the peptide substrate myelin basic protein. Analysis of
pknB expression in Mycobacterium tuberculosis
indicates the presence of pknB mRNA in (i) organisms grown
in vitro in bacteriological media, (ii) a murine macrophage in vitro
infection model, and (iii) in vivo alveolar macrophages from a patient
with tuberculosis.
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Expression and Characterization of the Mycobacterium
tuberculosis Serine/Threonine Protein Kinase PknB
*
Corresponding author. Mailing address: Department of
Medicine, Division of Infectious Diseases, University of British
Columbia, 2733 Heather St., Vancouver, British Columbia, Canada V5Z
3J5. Phone: (604) 875-4588. Fax: (604) 875-4013. E-mail:
yossi{at}interchange.ubc.ca.
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