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

Eleni Karinou, Emma L R Compton, Mélanie Morel, Arnaud Javelle

    Research output: Contribution to journalArticle

    25 Citations (Scopus)

    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.
    Original languageEnglish
    Pages (from-to)623-640
    Number of pages18
    JournalMolecular Microbiology
    Volume87
    Issue number3
    DOIs
    Publication statusPublished - Feb 2013

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    Dicarboxylic Acid Transporters
    Succinic Acid
    Sulpiride
    Escherichia coli
    Dicarboxylic Acids
    Sulfates
    Plant Proteins
    Protein Transport
    Substrate Specificity
    Anions
    Proteins
    Fungi
    Carbon
    Growth

    Keywords

    • c4-dicarboxylic acid transporter

    Cite this

    Karinou, Eleni ; Compton, Emma L R ; Morel, Mélanie ; Javelle, Arnaud. / The Escherichia coli SLC26 homologue YchM (DauA) is a C(4) -dicarboxylic acid transporter. In: Molecular Microbiology. 2013 ; Vol. 87, No. 3. pp. 623-640.
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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.",
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    The Escherichia coli SLC26 homologue YchM (DauA) is a C(4) -dicarboxylic acid transporter. / Karinou, Eleni; Compton, Emma L R; Morel, Mélanie; Javelle, Arnaud.

    In: Molecular Microbiology, Vol. 87, No. 3, 02.2013, p. 623-640.

    Research output: Contribution to journalArticle

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