Picture of industrial chimneys polluting horizon

Open Access research shaping international environmental governance...

Strathprints makes available scholarly Open Access content exploring environmental law and governance, in particular the work of the Strathclyde Centre for Environmental Law & Governance (SCELG) based within the School of Law.

SCELG aims to improve understanding of the trends, challenges and potential solutions across different interconnected areas of environmental law, including capacity-building for sustainable management of biodiversity, oceans, lands and freshwater, as well as for the fight against climate change. The intersection of international, regional, national and local levels of environmental governance, including the customary laws of indigenous peoples and local communities, and legal developments by private actors, is also a signifcant research specialism.

Explore Open Access research by SCELG or the School of Law. Or explore all of Strathclyde's Open Access research...

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

Full text not available in this repository. Request a copy from the Strathclyde author

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.