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Journal of Bacteriology, September 2009, p. 5480-5488, Vol. 191, No. 17
0021-9193/09/$08.00+0 doi:10.1128/JB.00640-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Elena Jolkver,2,
Reinhard Krämer,2
Kay Marin,2* and
Volker F. Wendisch1*
Institute of Molecular Microbiology and Biotechnology, Westfalian Wilhelms University Muenster, Muenster, Germany,1 Institute of Biochemistry, Cologne University, Cologne, Germany2
Received 14 May 2009/ Accepted 24 June 2009
Transporters of the dicarboxylate amino acid-cation symporter family often mediate uptake of C4-dicarboxylates, such as succinate or L-malate, in bacteria. A member of this family, dicarboxylate transporter A (DctA) from Corynebacterium glutamicum, was characterized to catalyze uptake of the C4-dicarboxylates succinate, fumarate, and L-malate, which was inhibited by oxaloacetate, 2-oxoglutarate, and glyoxylate. DctA activity was not affected by sodium availability but was dependent on the electrochemical proton potential. Efficient growth of C. glutamicum in minimal medium with succinate, fumarate, or L-malate as the sole carbon source required high dctA expression levels due either to a promoter-up mutation identified in a spontaneous mutant or to ectopic overexpression. Mutant analysis indicated that DctA and DccT, a C4-dicarboxylate divalent anion/sodium symporter-type transporter, are the only transporters for succinate, fumarate, and L-malate in C. glutamicum.
Published ahead of print on 6 July 2009.
J.-W.Y. and E.J. contributed equally to this work.
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