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 Wang, Q. M.
Right arrow Articles by Skatrud, P. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wang, Q. M.
Right arrow Articles by Skatrud, P. L.
Right arrowPubmed/NCBI databases
*Gene*GEO Profiles
*Protein
*Compound via MeSH
*Substance via MeSH

 Previous Article  |  Next Article 

Journal of Bacteriology, August 2001, p. 4779-4785, Vol. 183, No. 16
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.16.4779-4785.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Identification and Characterization of a Monofunctional Glycosyltransferase from Staphylococcus aureus

Q. May Wang,* Robert B. Peery, Robert B. Johnson, William E. Alborn, Wu-Kuang Yeh, and Paul L. Skatrud*

Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285

Received 3 April 2001/Accepted 28 May 2001

A gene (mgt) encoding a monofunctional glycosyltransferase (MGT) from Staphylococcus aureus has been identified. This first reported gram-positive MGT shared significant homology with several MGTs from gram-negative bacteria and the N-terminal glycosyltransferase domain of class A high-molecular-mass penicillin-binding proteins from different species. S. aureus MGT contained an N-terminal hydrophobic domain perhaps involved with membrane association. It was expressed in Escherichia coli cells as a truncated protein lacking the hydrophobic domain and purified to homogeneity. Analysis by circular dichroism revealed that secondary structural elements of purified truncated S. aureus MGT were consistent with predicted structural elements, indicating that the protein might exhibit the expected folding. In addition, purified S. aureus MGT catalyzed incorporation of UDP-N-acetylglucosamine into peptidoglycan, proving that it was enzymatically active. MGT activity was inhibited by moenomycin A, and the reaction product was sensitive to lysozyme treatment. Moreover, a protein matching the calculated molecular weight of S. aureus MGT was identified from an S. aureus cell lysate using antibodies developed against purified MGT. Taken together, our results suggest that this enzyme is natively present in S. aureus cells and that it may play a role in bacterial cell wall biosynthesis.

* Corresponding author. Mailing address for Q. May Wang: Infectious Diseases Research, Eli Lilly and Company, Lilly Corp. Center D.C. 0438, Indianapolis, IN 46285. Phone: (317) 277-6975. Fax: (317) 276-1743. E-mail: qmwang{at}lilly.com. Mailing address for Paul L. Skatrud: Elanco Animal Health, Eli Lilly and Company, 2001 West Main St., D.C. GL52, Greenfield, IN 46140. Phone: (317) 276-7081. Fax: (317) 277-4288. E-mail: Skatrud_Paul_L{at}Lilly.com.

Journal of Bacteriology, August 2001, p. 4779-4785, Vol. 183, No. 16
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.16.4779-4785.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Rice, L. B., Carias, L. L., Rudin, S., Hutton, R., Marshall, S., Hassan, M., Josseaume, N., Dubost, L., Marie, A., Arthur, M. (2009). Role of Class A Penicillin-Binding Proteins in the Expression of {beta}-Lactam Resistance in Enterococcus faecium. J. Bacteriol. 191: 3649-3656 [Abstract] [Full Text]  
  • Steidl, R., Pearson, S., Stephenson, R. E., Ledala, N., Sitthisak, S., Wilkinson, B. J., Jayaswal, R. K. (2008). Staphylococcus aureus Cell Wall Stress Stimulon Gene-lacZ Fusion Strains: Potential for Use in Screening for Cell Wall-Active Antimicrobials. Antimicrob. Agents Chemother. 52: 2923-2925 [Abstract] [Full Text]  
  • van Heijenoort, J. (2007). Lipid Intermediates in the Biosynthesis of Bacterial Peptidoglycan. Microbiol. Mol. Biol. Rev. 71: 620-635 [Abstract] [Full Text]  
  • Terrak, M., Nguyen-Disteche, M. (2006). Kinetic Characterization of the Monofunctional Glycosyltransferase from Staphylococcus aureus.. J. Bacteriol. 188: 2528-2532 [Abstract] [Full Text]  
  • Sobral, R. G., Ludovice, A. M., de Lencastre, H., Tomasz, A. (2006). Role of murF in Cell Wall Biosynthesis: Isolation and Characterization of a murF Conditional Mutant of Staphylococcus aureus.. J. Bacteriol. 188: 2543-2553 [Abstract] [Full Text]  
  • Arbeloa, A., Segal, H., Hugonnet, J.-E., Josseaume, N., Dubost, L., Brouard, J.-P., Gutmann, L., Mengin-Lecreulx, D., Arthur, M. (2004). Role of Class A Penicillin-Binding Proteins in PBP5-Mediated {beta}-Lactam Resistance in Enterococcus faecalis. J. Bacteriol. 186: 1221-1228 [Abstract] [Full Text]  
  • Di Guilmi, A. M., Dessen, A., Dideberg, O., Vernet, T. (2003). Functional Characterization of Penicillin-Binding Protein 1b from Streptococcus pneumoniae. J. Bacteriol. 185: 1650-1658 [Abstract] [Full Text]  
  • McPherson, D. C., Popham, D. L. (2003). Peptidoglycan Synthesis in the Absence of Class A Penicillin-Binding Proteins in Bacillus subtilis. J. Bacteriol. 185: 1423-1431 [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»