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 Huynh, P. L.
Right arrow Articles by Brückner, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Huynh, P. L.
Right arrow Articles by Brückner, R.

 Previous Article  |  Next Article 

Journal of Bacteriology, April 2000, p. 1895-1902, Vol. 182, No. 7
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Characterization of an HPr Kinase Mutant of Staphylococcus xylosus

Phuong Lan Huynh,1 Ivana Jankovic,1 Norbert F. Schnell,2 and Reinhold Brückner1,*

Mikrobielle Genetik, Universität Tübingen, D-72076 Tübingen, Germany,1 and Zeneca Pharmaceuticals, Macclesfield, Cheshire SK10 4 TG, United Kingdom2

Received 4 October 1999/Accepted 29 December 1999

The Staphylococcus xylosus gene hprK, encoding HPr kinase (HPrK), has been isolated from a genomic library. The HPrK enzyme, purified as a His6 fusion protein, phosphorylated HPr, the phosphocarrier protein of the bacterial phosphotransferase system, at a serine residue in an ATP-dependent manner, and it also catalyzed the reverse reaction. Therefore, the enzyme constitutes a bifunctional HPr kinase/phosphatase. Insertional inactivation of the gene in the genome of S. xylosus resulted in the concomitant loss of both HPr kinase and His serine-phosphorylated-HPr phosphatase activities in cell extracts, strongly indicating that the HPrK enzyme is also responsible for both reactions in vivo. HPrK deficiency had a profound pleiotropic effect on the physiology of S. xylosus. The hprK mutant strain showed a severe growth defect in complex medium upon addition of glucose. Glucose uptake in glucose-grown cells was strongly enhanced compared with the wild type. Carbon catabolite repression of three tested enzyme activities by glucose, sucrose, and fructose was abolished. These results clearly demonstrate the prominent role of HPr kinase in global control to adjust catabolic capacities of S. xylosus according to the availability of preferred carbon sources.

* Corresponding author. Mailing address: Mikrobielle Genetik, Universität Tübingen, Auf der Morgenstelle 28, D-72076 Tübingen, Germany. Phone: 49-7071-2974635. Fax: 49-7071-294634. E-mail: reinhold.brueckner{at}uni-tuebingen.de.

Journal of Bacteriology, April 2000, p. 1895-1902, Vol. 182, No. 7
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Somerville, G. A., Proctor, R. A. (2009). At the Crossroads of Bacterial Metabolism and Virulence Factor Synthesis in Staphylococci. Microbiol. Mol. Biol. Rev. 73: 233-248 [Abstract] [Full Text]  
  • Deutscher, J., Francke, C., Postma, P. W. (2006). How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria. Microbiol. Mol. Biol. Rev. 70: 939-1031 [Abstract] [Full Text]  
  • Hamilton, A., Robinson, C., Sutcliffe, I. C., Slater, J., Maskell, D. J., Davis-Poynter, N., Smith, K., Waller, A., Harrington, D. J. (2006). Mutation of the Maturase Lipoprotein Attenuates the Virulence of Streptococcus equi to a Greater Extent than Does Loss of General Lipoprotein Lipidation. Infect. Immun. 74: 6907-6919 [Abstract] [Full Text]  
  • Ryan, S. M., Fitzgerald, G. F., van Sinderen, D. (2005). Transcriptional Regulation and Characterization of a Novel {beta}-Fructofuranosidase-Encoding Gene from Bifidobacterium breve UCC2003. Appl. Environ. Microbiol. 71: 3475-3482 [Abstract] [Full Text]  
  • Stoll, H., Dengjel, J., Nerz, C., Gotz, F. (2005). Staphylococcus aureus Deficient in Lipidation of Prelipoproteins Is Attenuated in Growth and Immune Activation. Infect. Immun. 73: 2411-2423 [Abstract] [Full Text]  
  • Caescu, C. I., Vidal, O., Krzewinski, F., Artenie, V., Bouquelet, S. (2004). Bifidobacterium longum Requires a Fructokinase (Frk; ATP:D-Fructose 6-Phosphotransferase, EC 2.7.1.4) for Fructose Catabolism. J. Bacteriol. 186: 6515-6525 [Abstract] [Full Text]  
  • Uziel, O., Borovok, I., Schreiber, R., Cohen, G., Aharonowitz, Y. (2004). Transcriptional Regulation of the Staphylococcus aureus Thioredoxin and Thioredoxin Reductase Genes in Response to Oxygen and Disulfide Stress. J. Bacteriol. 186: 326-334 [Abstract] [Full Text]  
  • Ramstrom, H., Sanglier, S., Leize-Wagner, E., Philippe, C., Van Dorsselaer, A., Haiech, J. (2003). Properties and Regulation of the Bifunctional Enzyme HPr Kinase/Phosphatase in Bacillus subtilis. J. Biol. Chem. 278: 1174-1185 [Abstract] [Full Text]  
  • Steinhauer, K., Jepp, T., Hillen, W., Stulke, J. (2002). A novel mode of control of Mycoplasma pneumoniae HPr kinase/phosphatase activity reflects its parasitic lifestyle. Microbiology 148: 3277-3284 [Abstract] [Full Text]  
  • Hanson, K. G., Steinhauer, K., Reizer, J., Hillen, W., Stulke, J. (2002). HPr kinase/phosphatase of Bacillus subtilis: expression of the gene and effects of mutations on enzyme activity, growth and carbon catabolite repression. Microbiology 148: 1805-1811 [Abstract] [Full Text]  
  • Galinier, A., Lavergne, J.-P., Geourjon, C., Fieulaine, S., Nessler, S., Jault, J.-M. (2002). A New Family of Phosphotransferases with a P-loop Motif. J. Biol. Chem. 277: 11362-11367 [Abstract] [Full Text]  
  • Marquez, J. A., Hasenbein, S., Koch, B., Fieulaine, S., Nessler, S., Russell, R. B., Hengstenberg, W., Scheffzek, K. (2002). Structure of the full-length HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 A resolution: Mimicking the product/substrate of the phospho transfer reactions. Proc. Natl. Acad. Sci. USA 99: 3458-3463 [Abstract] [Full Text]  
  • Monedero, V., Kuipers, O. P., Jamet, E., Deutscher, J. (2001). Regulatory Functions of Serine-46-Phosphorylated HPr in Lactococcus lactis. J. Bacteriol. 183: 3391-3398 [Abstract] [Full Text]  
  • Djordjevic, G. M., Tchieu, J. H., Saier, M. H. Jr. (2001). Genes Involved in Control of Galactose Uptake in Lactobacillus brevis and Reconstitution of the Regulatory System in Bacillus subtilis. J. Bacteriol. 183: 3224-3236 [Abstract] [Full Text]  
  • Jankovic, I., Egeter, O., Brückner, R. (2001). Analysis of Catabolite Control Protein A-Dependent Repression in Staphylococcus xylosus by a Genomic Reporter Gene System. J. Bacteriol. 183: 580-586 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»