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
Right arrow Citation Map
Services
Right arrow E-mail this article to a friend
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 Jones, G.
Right arrow Articles by Dyson, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jones, G.
Right arrow Articles by Dyson, P.

 Previous Article  |  Next Article 

Journal of Bacteriology, November 2006, p. 7470-7476, Vol. 188, No. 21
0021-9193/06/$08.00+0     doi:10.1128/JB.00800-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Evolution of Transmembrane Protein Kinases Implicated in Coordinating Remodeling of Gram-Positive Peptidoglycan: Inside versus Outside{triangledown}

Greg Jones and Paul Dyson*

School of Medicine, University of Wales Swansea, Singleton Park, Swansea SA2 8PP, United Kingdom

Received 5 June 2006/ Accepted 16 August 2006

Members of a family of serine/threonine protein kinases (STPKs), unique to gram-positive bacteria, comprise an intracellular kinase domain and reiterated extracellular PASTA (for "penicillin-binding protein and serine/threonine kinase associated") domains. PASTA domains exhibit low affinity for ß-lactam antibiotics that are structurally similar to their likely normal ligands: stem peptides of unlinked peptidoglycan. The PASTA-domain STPKs are found in the actinobacteria and firmicutes and, as exemplified by PknB of Mycobacterium tuberculosis, they are functionally implicated in aspects of growth, cell division, and development. Whereas the kinase domains are well conserved, there is a wide divergence in the sequences of the multiple PASTA domains. Closer inspection reveals position-dependent evolution of individual PASTA domains: a domain at one position within a gene has a close phylogenetic relationship with a domain at a similar position in an orthologous gene, whereas neighboring domains have clearly diverged one from one another. A similar position-dependent relationship is demonstrated in the second family of proteins with multiple PASTA domains: the high-molecular-weight type II penicillin-binding protein (PBP2x) family. These transpeptidases are recruited to the division site by a localized pool of unlinked peptidoglycan. We infer that protein localization is guided by low-affinity interactions between structurally different unlinked peptidoglycan stem peptides and individual PASTA domains. The STPKs possess a greater multiplicity and diversity of PASTA domains, allowing interactions with a wider range of stem-peptide ligands. These interactions are believed to activate the intracellular kinase domain, allowing an STPK to coordinate peptidoglycan remodeling and reproduction of a complex cell wall structure.

* Corresponding author. Mailing address: School of Medicine, University of Wales Swansea, Singleton Park, Swansea SA2 8PP, United Kingdom. Phone: 44 1792 295667. Fax: 44 1792 295447. E-mail: p.j.dyson{at}swansea.ac.uk.

{triangledown} Published ahead of print on 25 August 2006.

Journal of Bacteriology, November 2006, p. 7470-7476, Vol. 188, No. 21
0021-9193/06/$08.00+0     doi:10.1128/JB.00800-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Osaki, M., Arcondeguy, T., Bastide, A., Touriol, C., Prats, H., Trombe, M.-C. (2009). The StkP/PhpP Signaling Couple in Streptococcus pneumoniae: Cellular Organization and Physiological Characterization. J. Bacteriol. 191: 4943-4950 [Abstract] [Full Text]  
  • Debarbouille, M., Dramsi, S., Dussurget, O., Nahori, M.-A., Vaganay, E., Jouvion, G., Cozzone, A., Msadek, T., Duclos, B. (2009). Characterization of a Serine/Threonine Kinase Involved in Virulence of Staphylococcus aureus. J. Bacteriol. 191: 4070-4081 [Abstract] [Full Text]  
  • Absalon, C., Obuchowski, M., Madec, E., Delattre, D., Holland, I. B., Seror, S. J. (2009). CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis. Microbiology 155: 932-943 [Abstract] [Full Text]  
  • Hett, E. C., Rubin, E. J. (2008). Bacterial Growth and Cell Division: a Mycobacterial Perspective. Microbiol. Mol. Biol. Rev. 72: 126-156 [Abstract] [Full Text]  
  • Narayan, A., Sachdeva, P., Sharma, K., Saini, A. K., Tyagi, A. K., Singh, Y. (2007). Serine threonine protein kinases of mycobacterial genus: phylogeny to function. Physiol. Genomics 29: 66-75 [Abstract] [Full Text]  


Copyright © 2010 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»