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 Hilbert, F.
Right arrow Articles by Groisman, E. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hilbert, F.
Right arrow Articles by Groisman, E. A.

 Previous Article  |  Next Article 

Journal of Bacteriology, April 1999, p. 2158-2165, Vol. 181, No. 7
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

A Periplasmic D-Alanyl-D-Alanine Dipeptidase in the Gram-Negative Bacterium Salmonella enterica

Friederike Hilbert,1 Francisco García del Portillo,2 and Eduardo A. Groisman1,3,*

Department of Molecular Microbiology1 and Howard Hughes Medical Institute,3 Washington University School of Medicine, St. Louis, Missouri 63110, and Centro de Biología Molecular "Severo Ochoa," Universidad Autónoma de Madrid, 28049 Madrid, Spain2

Received 23 November 1998/Accepted 25 January 1999

The VanX protein is a D-alanyl-D-alanine (D-Ala-D-Ala) dipeptidase essential for resistance to the glycopeptide antibiotic vancomycin. While this enzymatic activity has been typically associated with vancomycin- and teicoplainin-resistant enterococci, we now report the identification of a D-Ala-D-Ala dipeptidase in the gram-negative species Salmonella enterica. The Salmonella enzyme is only 36% identical to VanX but exhibits a similar substrate specificity: it hydrolyzes D-Ala-D-Ala, DL-Ala-DL-Phe, and D-Ala-Gly but not the tripeptides D-Ala-D-Ala-D-Ala and DL-Ala-DL-Lys-Gly or the dipeptides L-Ala-L-Ala, N-acetyl-D-Ala-D-Ala, and L-Leu-Pro. The Salmonella dipeptidase gene, designated pcgL, appears to have been acquired by horizontal gene transfer because pcgL-hybridizing sequences were not detected in related bacterial species and the G+C content of the pcgL-containing region (41%) is much lower than the overall G+C content of the Salmonella chromosome (52%). In contrast to wild-type Salmonella, a pcgL mutant was unable to use D-Ala-D-Ala as a sole carbon source. The pcgL gene conferred D-Ala-D-Ala dipeptidase activity upon Escherichia coli K-12 but did not allow growth on D-Ala-D-Ala. The PcgL protein localizes to the periplasmic space of Salmonella, suggesting that this dipeptidase participates in peptidoglycan metabolism.

* Corresponding author. Mailing address: Department of Molecular Microbiology, Washington University School of Medicine, Campus Box 8230, 660 S. Euclid Ave., St. Louis, MO 63110. Phone: (314) 362-3692. Fax: (314) 362-1232.

Journal of Bacteriology, April 1999, p. 2158-2165, Vol. 181, No. 7
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Zhao, G., Weatherspoon, N., Kong, W., Curtiss, R. III, Shi, Y. (2008). A dual-signal regulatory circuit activates transcription of a set of divergent operons in Salmonella typhimurium. Proc. Natl. Acad. Sci. USA 105: 20924-20929 [Abstract] [Full Text]  
  • Kong, W., Weatherspoon, N., Shi, Y. (2008). Molecular Mechanism for Establishment of Signal-dependent Regulation in the PhoP/PhoQ System. J. Biol. Chem. 283: 16612-16621 [Abstract] [Full Text]  
  • Deghorain, M., Goffin, P., Fontaine, L., Mainardi, J.-L., Daniel, R., Errington, J., Hallet, B., Hols, P. (2007). Selectivity for D-Lactate Incorporation into the Peptidoglycan Precursors of Lactobacillus plantarum: Role of Aad, a VanX-Like D-Alanyl-D-Alanine Dipeptidase. J. Bacteriol. 189: 4332-4337 [Abstract] [Full Text]  
  • Shi, Y., Latifi, T., Cromie, M. J., Groisman, E. A. (2004). Transcriptional Control of the Antimicrobial Peptide Resistance ugtL Gene by the Salmonella PhoP and SlyA Regulatory Proteins. J. Biol. Chem. 279: 38618-38625 [Abstract] [Full Text]  
  • Lejona, S., Aguirre, A., Cabeza, M. L., Vescovi, E. G., Soncini, F. C. (2003). Molecular Characterization of the Mg2+-Responsive PhoP-PhoQ Regulon in Salmonella enterica. J. Bacteriol. 185: 6287-6294 [Abstract] [Full Text]  
  • Winfield, M. D., Groisman, E. A. (2003). Role of Nonhost Environments in the Lifestyles of Salmonella and Escherichia coli. Appl. Environ. Microbiol. 69: 3687-3694 [Full Text]  
  • Pucciarelli, M. G., Prieto, A. I., Casadesus, J., Garcia-del Portillo, F. (2002). Envelope instability in DNA adenine methylase mutants of Salmonella enterica. Microbiology 148: 1171-1182 [Abstract] [Full Text]  
  • Rao, P. S. S., Lim, T. M., Leung, K. Y. (2001). Opsonized Virulent Edwardsiella tarda Strains Are Able To Adhere to and Survive and Replicate within Fish Phagocytes but Fail To Stimulate Reactive Oxygen Intermediates. Infect. Immun. 69: 5689-5697 [Abstract] [Full Text]  
  • Groisman, E. A. (2001). The Pleiotropic Two-Component Regulatory System PhoP-PhoQ. J. Bacteriol. 183: 1835-1842 [Full Text]  
  • Miao, E. A., Miller, S. I. (2000). A conserved amino acid sequence directing intracellular type III secretion by Salmonella typhimurium. Proc. Natl. Acad. Sci. USA 97: 7539-7544 [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»