This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Nádvorník, R.
Right arrow Articles by Branny, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nádvorník, R.
Right arrow Articles by Branny, P.

 Previous Article  |  Next Article 

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.



This article has been cited by other articles:

  • Saskova, L., Novakova, L., Basler, M., Branny, P. (2007). Eukaryotic-Type Serine/Threonine Protein Kinase StkP Is a Global Regulator of Gene Expression in Streptococcus pneumoniae. J. Bacteriol. 189: 4168-4179 [Abstract] [Full Text]  
  • Zhang, W., Shi, L. (2004). Evolution of the PPM-family protein phosphatases in Streptomyces: duplication of catalytic domain and lateral recruitment of additional sensory domains. Microbiology 150: 4189-4197 [Abstract] [Full Text]  
  • Shi, L., Zhang, W. (2004). Comparative analysis of eukaryotic-type protein phosphatases in two streptomycete genomes. Microbiology 150: 2247-2256 [Abstract] [Full Text]  
  • Verma, A., Maurelli, A. T. (2003). Identification of Two Eukaryote-Like Serine/Threonine Kinases Encoded by Chlamydia trachomatis Serovar L2 and Characterization of Interacting Partners of Pkn1. Infect. Immun. 71: 5772-5784 [Abstract] [Full Text]  
  • Petrickova, K., Petricek, M. (2003). Eukaryotic-type protein kinases in Streptomyces coelicolor: variations on a common theme. Microbiology 149: 1609-1621 [Abstract] [Full Text]  
  • Umeyama, T., Horinouchi, S. (2001). Autophosphorylation of a Bacterial Serine/Threonine Kinase, AfsK, Is Inhibited by KbpA, an AfsK-Binding Protein. J. Bacteriol. 183: 5506-5512 [Abstract] [Full Text]  
  • Koul, A., Choidas, A., Tyagi, A. K., Drlica, K., Singh, Y., Ullrich, A. (2001). Serine/threonine protein kinases PknF and PknG of Mycobacterium tuberculosis: characterization and localization. Microbiology 147: 2307-2314 [Abstract] [Full Text]  
  • Joshi, B., Janda, L., Stoytcheva, Z., Tichy, P. (2000). PkwA, a WD-repeat protein, is expressed in spore-derived mycelium of Thermomonospora curvata and phosphorylation of its WD domain could act as a molecular switch. Microbiology 146: 3259-3267 [Abstract] [Full Text]  
  • Av-Gay, Y., Jamil, S., Drews, S. J. (1999). Expression and Characterization of the Mycobacterium tuberculosis Serine/Threonine Protein Kinase PknB. Infect. Immun. 67: 5676-5682 [Abstract] [Full Text]