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Journal of Bacteriology, April 2000, p. 1935-1941, Vol. 182, No. 7
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Sinorhizobium meliloti putA Gene Regulation: a New Model within the Family Rhizobiaceae

María José Soto, José Ignacio Jiménez-Zurdo, Pieter van Dillewijn, and Nicolás Toro*

Departamento de Microbiología del Suelo y Sistemas Simbióticos, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Científicas, 18008 Granada, Spain

Received 21 October 1999/Accepted 22 December 1999

Proline dehydrogenase (PutA) is a bifunctional enzyme that catalyzes the oxidation of proline to glutamate. In Sinorhizobium meliloti, as in other microorganisms, the putA gene is transcriptionally activated in response to proline. In Rhodobacter capsulatus, Agrobacterium, and most probably in Bradyrhizobium, this activation is dependent on an Lrp-like protein encoded by the putR gene, located immediately upstream of putA. Interestingly, sequence and genetic analysis of the region upstream of the S. meliloti putA gene did not reveal such a putR locus or any other encoded transcriptional activator of putA. Furthermore, results obtained with an S. meliloti putA null mutation indicate the absence of any proline-responsive transcriptional activator and that PutA serves as an autogenous repressor. Therefore, the model of S. meliloti putA regulation completely diverges from that of its Rhizobiaceae relatives and resembles more that of enteric bacteria. However, some differences have been found with the latter model: (i) S. meliloti putA gene is not catabolite repressed, and (ii) the gene encoding for the major proline permease (putP) does not form part of an operon with the putA gene.

* Corresponding author. Mailing address: Departamento de Microbiología del Suelo y Sistemas Simbióticos, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Científicas, Profesor Albareda 1, 18008 Granada, Spain. Phone: 34-958-121011. Fax: 34-958-129600. E-mail: ntoro{at}eez.csic.es.

Journal of Bacteriology, April 2000, p. 1935-1941, Vol. 182, No. 7
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Gu, D., Zhou, Y., Kallhoff, V., Baban, B., Tanner, J. J., Becker, D. F. (2004). Identification and Characterization of the DNA-binding Domain of the Multifunctional PutA Flavoenzyme. J. Biol. Chem. 279: 31171-31176 [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]  
  • van Dillewijn, P., Soto, M. J., Villadas, P. J., Toro, N. (2001). Construction and Environmental Release of a Sinorhizobium meliloti Strain Genetically Modified To Be More Competitive for Alfalfa Nodulation. Appl. Environ. Microbiol. 67: 3860-3865 [Abstract] [Full Text]  
  • Vílchez, S., Manzanera, M., Ramos, J. L. (2000). Control of Expression of Divergent Pseudomonas putida put Promoters for Proline Catabolism. Appl. Environ. Microbiol. 66: 5221-5225 [Abstract] [Full Text]  


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