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

 Previous Article  |  Next Article 

Journal of Bacteriology, June 2004, p. 3855-3861, Vol. 186, No. 12
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.12.3855-3861.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Transcriptome Analysis of the ArgR Regulon in Pseudomonas aeruginosa

Chung-Dar Lu,* Zhe Yang, and Wei Li

Department of Biology, Georgia State University, Atlanta, Georgia 30303

Received 10 December 2003/ Accepted 5 March 2004

Arginine metabolism in pseudomonads with multiple catabolic pathways for its utilization as carbon and nitrogen sources is of particular interest as the model system to study control of metabolic integration. We performed transcriptome analyses to identify genes controlled by the arginine regulatory protein ArgR and to better understand arginine metabolic pathways of P. aeruginosa. We compared gene expression in wild-type strain PAO1 with that in argR mutant strain PAO501 grown in glutamate minimal medium in the presence and absence of arginine. Ten putative transcriptional units of 28 genes were inducible by ArgR and arginine, including all known ArgR-regulated operons under aerobic conditions. The newly identified genes include the putative adcAB operon, which encodes a catabolic arginine decarboxylase and an antiporter protein, and PA0328, which encodes a hypothetical fusion protein of a peptidase and a type IV autotransporter. Also identified as members of the arginine network are the following solute transport systems: PA1971 (braZ) for branched-chain amino acids permease; PA2042 for a putative sodium:serine symporter; PA3934, which belongs to the family of small oligopeptide transporters; and PA5152-5155, which encodes components of an ABC transporter for a putative opine uptake system. The effect of arginine on the expression of these genes was confirmed by lacZ fusion studies and by DNA binding studies with purified ArgR. Only five transcriptional units of nine genes were qualified as repressible by ArgR and arginine, with three operons (argF, carAB, and argG) in arginine biosynthesis and two operons (gltBD and gdhA) in glutamate biosynthesis. These results indicate that ArgR is important in control of arginine and glutamate metabolism and that arginine and ArgR may have a redundant effect in inducing the uptake systems of certain compounds.

* Corresponding author. Mailing address: Department of Biology, Georgia State University, 24 Peachtree Center Ave., Atlanta, GA 30303. Phone: (404) 651-2531. Fax: (404) 651-2509. E-mail: biocdl{at}panther.gsu.edu.

Journal of Bacteriology, June 2004, p. 3855-3861, Vol. 186, No. 12
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.12.3855-3861.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Behrends, V., Ebbels, T. M. D., Williams, H. D., Bundy, J. G. (2009). Time-Resolved Metabolic Footprinting for Nonlinear Modeling of Bacterial Substrate Utilization. Appl. Environ. Microbiol. 75: 2453-2463 [Abstract] [Full Text]  
  • Hovel-Miner, G., Pampou, S., Faucher, S. P., Clarke, M., Morozova, I., Morozov, P., Russo, J. J., Shuman, H. A., Kalachikov, S. (2009). {sigma}S Controls Multiple Pathways Associated with Intracellular Multiplication of Legionella pneumophila. J. Bacteriol. 191: 2461-2473 [Abstract] [Full Text]  
  • Li, C., Lu, C.-D. (2009). Arginine racemization by coupled catabolic and anabolic dehydrogenases. Proc. Natl. Acad. Sci. USA 106: 906-911 [Abstract] [Full Text]  
  • Benkert, B., Quack, N., Schreiber, K., Jaensch, L., Jahn, D., Schobert, M. (2008). Nitrate-responsive NarX-NarL represses arginine-mediated induction of the Pseudomonas aeruginosa arginine fermentation arcDABC operon. Microbiology 154: 3053-3060 [Abstract] [Full Text]  
  • Klein, J., Leupold, S., Munch, R., Pommerenke, C., Johl, T., Karst, U., Jansch, L., Jahn, D., Retter, I. (2008). ProdoNet: identification and visualization of prokaryotic gene regulatory and metabolic networks. Nucleic Acids Res 36: W460-W464 [Abstract] [Full Text]  
  • Anderson, G. G., Moreau-Marquis, S., Stanton, B. A., O'Toole, G. A. (2008). In Vitro Analysis of Tobramycin-Treated Pseudomonas aeruginosa Biofilms on Cystic Fibrosis-Derived Airway Epithelial Cells. Infect. Immun. 76: 1423-1433 [Abstract] [Full Text]  
  • Hartenbach, S., Daoud-El Baba, M., Weber, W., Fussenegger, M. (2007). An engineered L-arginine sensor of Chlamydia pneumoniae enables arginine-adjustable transcription control in mammalian cells and mice. Nucleic Acids Res 35: e136-e136 [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]  
  • Kwon, D. H., Lu, C.-D. (2006). Polyamines Induce Resistance to Cationic Peptide, Aminoglycoside, and Quinolone Antibiotics in Pseudomonas aeruginosa PAO1.. Antimicrob. Agents Chemother. 50: 1615-1622 [Abstract] [Full Text]  
  • Elbahloul, Y., Steinbuchel, A. (2006). Engineering the Genotype of Acinetobacter sp. Strain ADP1 To Enhance Biosynthesis of Cyanophycin. Appl. Environ. Microbiol. 72: 1410-1419 [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»