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Journal of Bacteriology, September 2008, p. 5898-5906, Vol. 190, No. 17
0021-9193/08/$08.00+0     doi:10.1128/JB.00643-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

The Plant-Associated Bacterium Stenotrophomonas rhizophila Expresses a New Enzyme for the Synthesis of the Compatible Solute Glucosylglycerol{triangledown}

Martin Hagemann,1* Kathrin Ribbeck-Busch,1,2 Stephan Klähn,1 Dirk Hasse,1 Robert Steinbruch,1 and Gabriele Berg2,{dagger}

University of Rostock, Institute Biosciences, Plant Physiology,1 Microbiology, Albert-Einstein-Str. 3, D-18051 Rostock, Germany2

Received 8 May 2008/ Accepted 20 June 2008

The rhizobacterium Stenotrophomonas rhizophila accumulates the compatible solutes glucosylglycerol (GG) and trehalose under salt stress conditions. The complete gene for the GG synthesis enzyme was cloned and sequenced. This enzyme from S. rhizophila represented a novel fusion protein composed of a putative C-terminal GG-phosphate synthase domain and an N-terminal putative GG-phosphate phosphatase domain, which was named GgpPS. A similar gene was cloned from Pseudomonas sp. strain OA146. The ggpPS gene was induced after a salt shock in S. rhizophila cells. After the salt-loaded cells reached stationary phase, the ggpPS mRNA content returned to the low level characteristic of the control cells, and GG was released into the medium. The complete ggpPS gene and a truncated version devoid of the phosphatase part were obtained as recombinant proteins. Enzyme activity tests revealed the expected abilities of the full-length protein to synthesize GG and the truncated GgpPS to synthesize GG-phosphate. However, dephosphorylation of GG-phosphate was detected only with the complete GgpPS protein. These enzyme activities were confirmed by complementation experiments using defined GG-defective mutants of the cyanobacterium Synechocystis sp. strain PCC 6803. Genes coding for proteins very similar to the newly identified fusion protein GgpPS for GG synthesis in S. rhizophila were found in genome sequences of related bacteria, where these genes are often linked to a gene coding for a transporter of the Mfs superfamily.

* Corresponding author. Mailing address: Universität Rostock, Institut Biowissenschaften/Pflanzenphysiologie, Albert-Einstein-Str. 3, D-18051 Rostock, Germany. Phone: 49-381-4986113. Fax: 49-381-4986112. E-mail: martin.hagemann{at}uni-rostock.de

{triangledown} Published ahead of print on 27 June 2008.

{dagger} Present address: Graz University of Technology, Department Environmental Biotechnology, Petersgasse 12, A-8010 Graz, Austria.

Journal of Bacteriology, September 2008, p. 5898-5906, Vol. 190, No. 17
0021-9193/08/$08.00+0     doi:10.1128/JB.00643-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Klahn, S., Marquardt, D. M., Rollwitz, I., Hagemann, M. (2009). Expression of the ggpPS gene for glucosylglycerol biosynthesis from Azotobacter vinelandii improves the salt tolerance of Arabidopsis thaliana. J Exp Bot 0: erp030v1-erp030 [Abstract] [Full Text]  


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