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 Griswold, A.
Right arrow Articles by Burne, R. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Griswold, A.
Right arrow Articles by Burne, R. A.
Agricola
Right arrow Articles by Griswold, A.
Right arrow Articles by Burne, R. A.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, March 2004, p. 1321-1327, Vol. 70, No. 3
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.3.1321-1327.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Characterization of the Arginine Deiminase Operon of Streptococcus rattus FA-1

Ann Griswold, Yi-Ywan M. Chen,{dagger} Jennifer A. Snyder,{dagger} and Robert A. Burne{dagger}*

Department of Oral Biology, University of Florida, Gainesville, Florida

Received 22 September 2003/ Accepted 2 December 2003

The arginine deiminase system (ADS) is of critical importance in oral biofilm pH homeostasis and microbial ecology. The ADS consists of three enzymes. Arginine is hydrolyzed by AD (ArcA) to generate citrulline and ammonia. Citrulline is then converted to ornithine and carbamoylphosphate via ornithine carbamoyltransferase (ArcB). Finally, carbamate kinase (ArcC) transfers a phosphate from carbamoylphosphate to ADP, yielding ATP. Ammonia production from this pathway protects bacteria from lethal acidification, and ATP production provides a source of energy for the cells. The purpose of this study was to initiate a characterization of the arc operon of Streptococcus rattus, the least cariogenic and sole ADS-positive member of the mutans streptococci. Using an arcB gene fragment obtained by degenerate PCRs, the FA-1 arc operon was identified in subgenomic DNA libraries and sequence analysis was performed. Results showed that the genes encoding the AD pathway in S. rattus FA-1 are organized as an arcABCDT-adiR operon gene cluster, including the enzymes of the pathway, an arginine-ornithine antiporter (ArcD) and a putative regulatory protein (AdiR). The arcA transcriptional start site was identified by primer extension, and a {sigma}70-like promoter was mapped 5' to arcA. Reverse transcriptase PCR was used to establish that arcABCDT could be cotranscribed. Reporter gene fusions and AD assays demonstrated that the operon is regulated by substrate induction and catabolite repression, the latter apparently through a CcpA-dependent pathway.

* Corresponding author. Mailing address: Department of Oral Biology, University of Florida, 1600 S.W. Archer Rd., Gainesville, FL 32610-0424. Phone: (352) 392-0011. Fax: (352) 392-7357. E-mail: rburne{at}dental.ufl.edu.

{dagger} Present address: Department of Microbiology and Immunology, University of Maryland School of Medicine, Baltimore, MD 21201.

Applied and Environmental Microbiology, March 2004, p. 1321-1327, Vol. 70, No. 3
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.3.1321-1327.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Makhlin, J., Kofman, T., Borovok, I., Kohler, C., Engelmann, S., Cohen, G., Aharonowitz, Y. (2007). Staphylococcus aureus ArcR Controls Expression of the Arginine Deiminase Operon. J. Bacteriol. 189: 5976-5986 [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]  
  • Griswold, A. R., Jameson-Lee, M., Burne, R. A. (2006). Regulation and Physiologic Significance of the Agmatine Deiminase System of Streptococcus mutans UA159. J. Bacteriol. 188: 834-841 [Abstract] [Full Text]  
  • Zeng, L., Dong, Y., Burne, R. A. (2006). Characterization of cis-Acting Sites Controlling Arginine Deiminase Gene Expression in Streptococcus gordonii. J. Bacteriol. 188: 941-949 [Abstract] [Full Text]  
  • Gruening, P., Fulde, M., Valentin-Weigand, P., Goethe, R. (2006). Structure, Regulation, and Putative Function of the Arginine Deiminase System of Streptococcus suis. J. Bacteriol. 188: 361-369 [Abstract] [Full Text]  
  • Dalton, T. L., Collins, J. T., Barnett, T. C., Scott, J. R. (2006). RscA, a Member of the MDR1 Family of Transporters, Is Repressed by CovR and Required for Growth of Streptococcus pyogenes under Heat Stress. J. Bacteriol. 188: 77-85 [Abstract] [Full Text]  
  • Naumoff, D. G., Xu, Y., Stalon, V., Glansdorff, N., Labedan, B. (2004). The difficulty of annotating genes: the case of putrescine carbamoyltransferase. Microbiology 150: 3908-3911 [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»