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Journal of Bacteriology, August 2000, p. 4216-4221, Vol. 182, No. 15
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

New Substrates for the Dicarboxylate Transport System of Sinorhizobium meliloti

Svetlana Yurgel,1 Michael W. Mortimer,1 Kimberly N. Rogers,1 and Michael L. Kahn1,2,*

Institute of Biological Chemistry1 and Department of Microbiology,2 Washington State University, Pullman, Washington 99164-6340

Received 10 December 1999/Accepted 5 May 2000

The dicarboxylate transport (Dct) system of Sinorhizobium meliloti, which is essential for a functional nitrogen-fixing symbiosis, has been thought to transport only dicarboxylic acids. We show here that the permease component of the Dct system, DctA, can transport orotate, a monocarboxylic acid, with an apparent Km of 1.7 mM and a Vmax of 163 nmol min-1 per mg of protein in induced cells. DctA was not induced by the presence of orotate. The transport of orotate was inhibited by several compounds, including succinamic acid and succinamide, which are not dicarboxylic acids. The dicarboxylic acid maleate (cis-butenedioic acid) was not an inhibitor of orotate transport, which suggests that it was not recognized by DctA. However, maleate was an excellent inducer of DctA expression. Our evaluation of 17 compounds as inducers and inhibitors of transport suggests that substrates recognized by S. meliloti DctA must have appropriately spaced carbonyl groups and an extended conformation, while good inducers are more likely to have a curved conformation.

* Corresponding author. Mailing address: Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340. Phone: (509) 335-8327. Fax: (509) 335-7643. E-mail: kahn{at}wsu.edu.

Journal of Bacteriology, August 2000, p. 4216-4221, Vol. 182, No. 15
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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