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Journal of Bacteriology, January 1999, p. 15-23, Vol. 181, No. 1
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Pkg2, a Novel Transmembrane Protein Ser/Thr Kinase of Streptomyces granaticolor

Richard Nádvorník, Tomás Vomastek, Jirí Janecek, Zuzana Techniková, and Pavel Branny*

Cell and Molecular Microbiology Division, Institute of Microbiology, Czech Academy of Sciences, 142 20 Prague 4, Czech Republic

Received 19 October 1998/Accepted 21 October 1998

A 4.2-kb SphI-BamHI fragment of chromosomal DNA from Streptomyces granaticolor was cloned and shown to encode a protein with significant sequence similarity to the eukaryotic protein serine/threonine kinases. It consists of 701 amino acids and in the N-terminal part contains all conserved catalytic domains of protein kinases. The C-terminal domain of Pkg2 contains seven tandem repeats of 11 or 12 amino acids with similarity to the tryptophan-docking motif known to stabilize a symmetrical three-dimensional structure called a propeller structure. The pkg2 gene was overexpressed in Escherichia coli, and the gene product (Pkg2) has been found to be autophosphorylated at serine and threonine residues. The N- and C-terminal parts of Pkg2 are separated with a hydrophobic stretch of 21 amino acids which translocated a PhoA fusion protein into the periplasm. Thus, Pkg2 is the first transmembrane protein serine/threonine kinase described for streptomycetes. Replacement of the pkg2 gene by the spectinomycin resistance gene resulted in changes in the morphology of aerial hyphae.

* Corresponding author. Cell and Molecular Microbiology Division, Institute of Microbiology, Czech Academy of Sciences, Vídenská 1083, 142 20 Prague 4, Czech Republic. Phone: (42 2) 475 26 58. Fax: (42 2) 472 22 57. E-mail: branny{at}biomed.cas.cz.

Journal of Bacteriology, January 1999, p. 15-23, Vol. 181, No. 1
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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