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 Nakada, Y.
Right arrow Articles by Lu, C.-D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nakada, Y.
Right arrow Articles by Lu, C.-D.

 Previous Article  |  Next Article 

Journal of Bacteriology, November 2001, p. 6517-6524, Vol. 183, No. 22
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.22.6517-6524.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Molecular Characterization and Regulation of the aguBA Operon, Responsible for Agmatine Utilization in Pseudomonas aeruginosa PAO1

Yuji Nakada,1 Ying Jiang,2 Takayuki Nishijyo,1 Yoshifumi Itoh,1 and Chung-Dar Lu2,*

National Food Research Institute, Tsukuba, Ibaraki 305-8642, Japan,1 and Department of Biology, Georgia State University, Atlanta, Georgia 303032

Received 30 May 2001/Accepted 22 August 2001

Pseudomonas aeruginosa PAO1 utilizes agmatine as the sole carbon and nitrogen source via two reactions catalyzed successively by agmatine deiminase (encoded by aguA; also called agmatine iminohydrolase) and N-carbamoylputrescine amidohydrolase (encoded by aguB). The aguBA and adjacent aguR genes were cloned and characterized. The predicted AguB protein (Mr 32,759; 292 amino acids) displayed sequence similarity (<= 60% identity) to enzymes of the beta -alanine synthase/nitrilase family. While the deduced AguA protein (Mr 41,190; 368 amino acids) showed no significant similarity to any protein of known function, assignment of agmatine deiminase to AguA in this report discovered a new family of carbon-nitrogen hydrolases widely distributed in organisms ranging from bacteria to Arabidopsis. The aguR gene encoded a putative regulatory protein (Mr 24,424; 221 amino acids) of the TetR protein family. Measurements of agmatine deiminase and N-carbamoylputrescine amidohydrolase activities indicated the induction effect of agmatine and N-carbamoylputrescine on expression of the aguBA operon. The presence of an inducible promoter for the aguBA operon in the aguR-aguB intergenic region was demonstrated by lacZ fusion experiments, and the transcription start of this promoter was localized 99 bp upstream from the initiation codon of aguB by S1 nuclease mapping. Experiments with knockout mutants of aguR established that expression of the aguBA operon became constitutive in the aguR background. Interaction of AguR overproduced in Escherichia coli with the aguBA regulatory region was demonstrated by gel retardation assays, supporting the hypothesis that AguR serves as the negative regulator of the aguBA operon, and binding of agmatine and N-carbamoylputrescine to AguR would antagonize its repressor function.

* Corresponding author. Mailing address: Department of Biology, Georgia State University, P.O. Box 4010, Atlanta, GA 30302-4010. Phone: (404) 651-2531. Fax: (404) 651-2509. E-mail: biocdl{at}panther.gsu.edu.

Journal of Bacteriology, November 2001, p. 6517-6524, Vol. 183, No. 22
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.22.6517-6524.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Chou, H. T., Kwon, D.-H., Hegazy, M., Lu, C.-D. (2008). Transcriptome Analysis of Agmatine and Putrescine Catabolism in Pseudomonas aeruginosa PAO1. J. Bacteriol. 190: 1966-1975 [Abstract] [Full Text]  
  • Lucas, P. M., Blancato, V. S., Claisse, O., Magni, C., Lolkema, J. S., Lonvaud-Funel, A. (2007). Agmatine deiminase pathway genes in Lactobacillus brevis are linked to the tyrosine decarboxylation operon in a putative acid resistance locus. Microbiology 153: 2221-2230 [Abstract] [Full Text]  
  • Yang, Z., Lu, C.-D. (2007). Functional Genomics Enables Identification of Genes of the Arginine Transaminase Pathway in Pseudomonas aeruginosa. J. Bacteriol. 189: 3945-3953 [Abstract] [Full Text]  
  • Llacer, J. L., Polo, L. M., Tavarez, S., Alarcon, B., Hilario, R., Rubio, V. (2007). The Gene Cluster for Agmatine Catabolism of Enterococcus faecalis: Study of Recombinant Putrescine Transcarbamylase and Agmatine Deiminase and a Snapshot of Agmatine Deiminase Catalyzing Its Reaction. J. Bacteriol. 189: 1254-1265 [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]  
  • Nakada, Y., Itoh, Y. (2005). Pseudomonas aeruginosa PAO1 genes for 3-guanidinopropionate and 4-guanidinobutyrate utilization may be derived from a common ancestor. Microbiology 151: 4055-4062 [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]  
  • Lu, C.-D., Yang, Z., Li, W. (2004). Transcriptome Analysis of the ArgR Regulon in Pseudomonas aeruginosa. J. Bacteriol. 186: 3855-3861 [Abstract] [Full Text]  
  • Griswold, A. R., Chen, Y.-Y. M., Burne, R. A. (2004). Analysis of an Agmatine Deiminase Gene Cluster in Streptococcus mutans UA159. J. Bacteriol. 186: 1902-1904 [Abstract] [Full Text]  
  • Minic, Z., Herve, G. (2003). Arginine Metabolism in the Deep Sea Tube Worm Riftia pachyptila and Its Bacterial Endosymbiont. J. Biol. Chem. 278: 40527-40533 [Abstract] [Full Text]  
  • Parschat, K., Hauer, B., Kappl, R., Kraft, R., Huttermann, J., Fetzner, S. (2003). Gene Cluster of Arthrobacter ilicis Ru61a Involved in the Degradation of Quinaldine to Anthranilate: CHARACTERIZATION AND FUNCTIONAL EXPRESSION OF THE QUINALDINE 4-OXIDASE qoxLMS GENES. J. Biol. Chem. 278: 27483-27494 [Abstract] [Full Text]  
  • Nakada, Y., Itoh, Y. (2003). Identification of the putrescine biosynthetic genes in Pseudomonas aeruginosa and characterization of agmatine deiminase and N-carbamoylputrescine amidohydrolase of the arginine decarboxylase pathway. Microbiology 149: 707-714 [Abstract] [Full Text]  
  • Piotrowski, M., Janowitz, T., Kneifel, H. (2003). Plant C-N Hydrolases and the Identification of a Plant N-Carbamoylputrescine Amidohydrolase Involved in Polyamine Biosynthesis. J. Biol. Chem. 278: 1708-1712 [Abstract] [Full Text]  
  • Nakada, Y., Nishijyo, T., Itoh, Y. (2002). Divergent Structure and Regulatory Mechanism of Proline Catabolic Systems: Characterization of the putAP Proline Catabolic Operon of Pseudomonas aeruginosa PAO1 and Its Regulation by PruR, an AraC/XylS Family Protein. J. Bacteriol. 184: 5633-5640 [Abstract] [Full Text]  
  • Lu, C.-D., Itoh, Y., Nakada, Y., Jiang, Y. (2002). Functional Analysis and Regulation of the Divergent spuABCDEFGH-spuI Operons for Polyamine Uptake and Utilization in Pseudomonas aeruginosa PAO1. J. Bacteriol. 184: 3765-3773 [Abstract] [Full Text]  
  • Nakada, Y., Itoh, Y. (2002). Characterization and Regulation of the gbuA Gene, Encoding Guanidinobutyrase in the Arginine Dehydrogenase Pathway of Pseudomonas aeruginosa PAO1. J. Bacteriol. 184: 3377-3384 [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»