AEM
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
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 Espinosa-Urgel, M.
Right arrow Articles by Ramos, J.-L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Espinosa-Urgel, M.
Right arrow Articles by Ramos, J.-L.
Agricola
Right arrow Articles by Espinosa-Urgel, M.
Right arrow Articles by Ramos, J.-L.

Applied and Environmental Microbiology, November 2001, p. 5219-5224, Vol. 67, No. 11
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.11.5219-5224.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Expression of a Pseudomonas putida Aminotransferase Involved in Lysine Catabolism Is Induced in the Rhizosphere

Manuel Espinosa-Urgel and Juan-Luis Ramos*

Department of Plant Biochemistry and Molecular and Cellular Biology, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Científicas, E-18008 Granada, Spain

Received 1 June 2001/Accepted 13 September 2001

Using a transposon carrying a promoterless lux operon to generate transcriptional fusions by insertional mutagenesis, we have identified a Pseudomonas putida gene with increased expression in the presence of corn root exudates. Expression of the transcriptional fusion, induced by the amino acid lysine, was detected in P. putida in the rhizosphere of plants as well as in response to seed exudates. The mutant was unable to grow on lysine or delta -aminovalerate as carbon sources, which indicates that the affected function is involved in the pathway for lysine catabolism. However, the mutant strain grew with glutaric acid, the product of delta -aminovalerate metabolism via glutaric acid semialdehyde, as a C source. The translated sequence of the interrupted gene showed high levels of similarity with aminotransferases. These sets of data suggest that the product of this gene has delta -aminovalerate aminotransferase activity. This is the first direct genetic evidence correlating a DNA sequence with such activity in Pseudomonadaceae.


* Corresponding author. Mailing address: CSIC-EEZ, C/Profesor Albareda 1, E-18008 Granada, Spain. Phone: 34-958-121011. Fax: 34-958-129600. E-mail: jlramos{at}eez.csic.es.


Applied and Environmental Microbiology, November 2001, p. 5219-5224, Vol. 67, No. 11
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.11.5219-5224.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Microbiol. Mol. Biol. Rev. Eukaryot. Cell All ASM Journals

Copyright © 2001 by the American Society for Microbiology. All rights reserved.