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The escherichia coli SLC26 homologue YchM (DauA) is a C(4)-dicarboxylic acid transporter

Karinou, Eleni and Compton-Daw, Emma and Morel, Mélanie and Javelle, Arnaud (2013) The escherichia coli SLC26 homologue YchM (DauA) is a C(4)-dicarboxylic acid transporter. Molecular Microbiology, 87 (3). pp. 623-640. ISSN 0950-382X

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Abstract

The SLC26/SulP (solute carrier/sulphate transporter) proteins are a ubiquitous superfamily of secondary anion transporters. Prior studies have focused almost exclusively on eukaryotic members and bacterial members are frequently classified as sulphate transporters based on their homology with SulP proteins from plants and fungi. In this study we have examined the function and physiological role of the Escherichia coli Slc26 homologue, YchM. We show that there is a clear YchM-dependent growth defect when succinate is used as the sole carbon source. Using an in vivo succinate transport assay, we show that YchM is the sole aerobic succinate transporter active at acidic pH. We demonstrate that YchM can also transport other C(4) -dicarboxylic acids and that its substrate specificity differs from the well-characterized succinate transporter, DctA. Accordingly ychM was re-designated dauA (dicarboxylic acid uptake system A). Finally, our data suggest that DauA is a protein with transport and regulation activities. This is the first report that a SLC26/SulP protein acts as a C(4) -dicarboxylic acid transporter and an unexpected new function for a prokaryotic member of this transporter family.

Item type: Article
ID code: 52112
Keywords: anion transport proteins, carbon, dicarboxylic acid transporters, escherichia coli, escherichia coli proteins, models, biological, phylogeny, sequence homology, amino acid, substrate specificity, succinic acid, Pharmacy and materia medica, Pharmacology, Toxicology and Pharmaceutics(all)
Subjects: Medicine > Pharmacy and materia medica
Department: Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences
Professional Services > Human Resources Directorate
Depositing user: Pure Administrator
Date deposited: 05 Mar 2015 14:49
Last modified: 16 Nov 2018 03:28
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URI: https://strathprints.strath.ac.uk/id/eprint/52112
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