The Slc26 proteins are a ubiquitous superfamily of anion transporters conserved from bacteria to humans, among which four have been identified as human disease genes. Our functional knowledge of this protein family has increased but limited structural information is available. These proteins contain a transmembrane (TM) domain and a C-terminal cytoplasmic sulfate transporter and anti-sigma factor (STAS) domain. In a fundamental step towards understanding the structure/function relationships within the family we have used small-angle neutron scattering (SANS) on two distantly related bacterial homologues to show that there is a common, dimeric and structural architecture among Slc26A transporters. Pulsed electron–electron double resonance (PELDOR) spectroscopy supports the dimeric SANS-derived model. Using chimaeric/truncated proteins we have determined the domain organization: the STAS domains project away from the TM core and are essential for protein stability. We use the SANS-generated envelopes to assess a homology model of the TM core.
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October 2014
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Research Article|
September 22 2014
Conserved structure and domain organization among bacterial Slc26 transporters
Emma L. R. Compton;
Emma L. R. Compton
*College of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.
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Kimberly Page;
Kimberly Page
*College of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.
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Heather E. Findlay;
Heather E. Findlay
†School of Biochemistry, University of Bristol, Bristol BS8 1TD, U.K.
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Michael Haertlein;
Michael Haertlein
‡The Deuteration Laboratory, Institut Laue-Langevin, CIBB, 6 rue Jules Horowitz, 38042 Grenoble cedex 9, France
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Martine Moulin;
Martine Moulin
‡The Deuteration Laboratory, Institut Laue-Langevin, CIBB, 6 rue Jules Horowitz, 38042 Grenoble cedex 9, France
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Ulrich Zachariae;
Ulrich Zachariae
*College of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.
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David G. Norman;
David G. Norman
*College of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.
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Frank Gabel;
Frank Gabel
§Institut de Biologie Structurale CEA, CNRS, UJF, 41 rue Jules Horowitz, 38027 Grenoble, France
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Arnaud Javelle
Arnaud Javelle
1
*College of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.
∥Strathclyde Institute of Pharmacy and Biomedical Sciences, 161 Cathedral Street, Glasgow G4 0RE, U.K.
1To whom correspondence should be addressed (email arnaud.javelle@strath.ac.uk).
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Publisher: Portland Press Ltd
Received:
May 03 2013
Revision Received:
June 26 2014
Accepted:
July 17 2014
Accepted Manuscript online:
July 17 2014
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2014 Biochemical Society
2014
Biochem J (2014) 463 (2): 297–307.
Article history
Received:
May 03 2013
Revision Received:
June 26 2014
Accepted:
July 17 2014
Accepted Manuscript online:
July 17 2014
Citation
Emma L. R. Compton, Kimberly Page, Heather E. Findlay, Michael Haertlein, Martine Moulin, Ulrich Zachariae, David G. Norman, Frank Gabel, Arnaud Javelle; Conserved structure and domain organization among bacterial Slc26 transporters. Biochem J 15 October 2014; 463 (2): 297–307. doi: https://doi.org/10.1042/BJ20130619
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