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 Caballero, A.
Right arrow Articles by Ramos, J. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Caballero, A.
Right arrow Articles by Ramos, J. L.

 Previous Article  |  Next Article 

Journal of Bacteriology, January 2005, p. 396-399, Vol. 187, No. 1
0021-9193/05/$08.00+0     doi:10.1128/JB.187.1.396-399.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Assimilation of Nitrogen from Nitrite and Trinitrotoluene in Pseudomonas putida JLR11

Antonio Caballero,1 Abraham Esteve-Núñez,1,{dagger} Gerben J. Zylstra,2 and Juan L. Ramos1*

Consejo Superior de Investigaciones Cientificas, Estación Experimental del Zaidin, Department of Biochemistry and Molecular and Cellular Biology of Plants, Granada, Spain,1 Biotechnology Center for Agriculture and the Environment, Cook College, Rutgers University, New Brunswick, New Jersey2

Received 4 June 2004/ Accepted 28 September 2004

Pseudomonas putida JLR11 releases nitrogen from the 2,4,6-trinitrotoluene (TNT) ring as nitrite or ammonium. These processes can occur simultaneously, as shown by the observation that a nasB mutant impaired in the reduction of nitrite to ammonium grew at a slower rate than the parental strain. Nitrogen from TNT is assimilated via the glutamine syntethase-glutamate synthase (GS-GOGAT) pathway, as evidenced by the inability of GOGAT mutants to use TNT. This pathway is also used to assimilate ammonium from reduced nitrate and nitrite. Three mutants that had insertions in ntrC, nasT, and cnmA, which encode regulatory proteins, failed to grow on nitrite but grew on TNT, although slower than the wild type.


* Corresponding author. Mailing address: EEZ-CSIC, C/ Prof. Albareda, 1 E-18008 Granada, Spain. Phone: 34 958 181608. Fax: 34 958 135740. E-mail: jlramos{at}eez.csic.es.

{dagger} Present address: Department of Microbiology, University of Massachusetts, Amherst, MA 01003.


Journal of Bacteriology, January 2005, p. 396-399, Vol. 187, No. 1
0021-9193/05/$08.00+0     doi:10.1128/JB.187.1.396-399.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • van Dillewijn, P., Wittich, R.-M., Caballero, A., Ramos, J.-L. (2008). Subfunctionality of Hydride Transferases of the Old Yellow Enzyme Family of Flavoproteins of Pseudomonas putida. Appl. Environ. Microbiol. 74: 6703-6708 [Abstract] [Full Text]  
  • Stenuit, B., Eyers, L., Rozenberg, R., Habib-Jiwan, J.-L., Agathos, S. N. (2006). Aerobic Growth of Escherichia coli with 2,4,6-Trinitrotoluene (TNT) as the Sole Nitrogen Source and Evidence of TNT Denitration by Whole Cells and Cell-Free Extracts. Appl. Environ. Microbiol. 72: 7945-7948 [Abstract] [Full Text]  
  • Revelles, O., Espinosa-Urgel, M., Fuhrer, T., Sauer, U., Ramos, J. L. (2005). Multiple and Interconnected Pathways for L-Lysine Catabolism in Pseudomonas putida KT2440. J. Bacteriol. 187: 7500-7510 [Abstract] [Full Text]