Affiliation:
1. Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston, Texas 77555
Abstract
ABSTRACT
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.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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