This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hall, J. A. Articles by Pajor, A. M. Search for Related Content PubMed PubMed Citation Articles by Hall, J. A. Articles by Pajor, A. M.

Functional Characterization of a Na⁺-Coupled Dicarboxylate Carrier Protein from Staphylococcus aureus

Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston, Texas 77555

Received 2 March 2005/ Accepted 11 May 2005

We have cloned and functionally characterized a Na⁺-coupled dicarboxylate transporter, SdcS, from Staphylococcus aureus. This carrier protein is a member of the divalent anion/Na⁺ symporter (DASS) family and shares significant sequence homology with the mammalian Na⁺/dicarboxylate cotransporters NaDC-1 and NaDC-3. Analysis of SdcS function indicates transport properties consistent with those of its eukaryotic counterparts. Thus, SdcS facilitates the transport of the dicarboxylates fumarate, malate, and succinate across the cytoplasmic membrane in a Na⁺-dependent manner. Furthermore, kinetic work predicts an ordered reaction sequence with Na⁺ (K_0.5 of 2.7 mM) binding before dicarboxylate (K_m of 4.5 µM). Because this transporter and its mammalian homologs are functionally similar, we suggest that SdcS may serve as a useful model for DASS family structural analysis.

This article has been cited by other articles:

• Hall, J. A., Pajor, A. M. (2007). Functional Reconstitution of SdcS, a Na+-Coupled Dicarboxylate Carrier Protein from Staphylococcus aureus. J. Bacteriol. 189: 880-885 [Abstract] [Full Text]