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J. Biol. Chem., Vol. 280, Issue 16, 15976-15983, April 22, 2005

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Structural and Functional Analysis of the C-terminal STAS (Sulfate Transporter and Anti-sigma Antagonist) Domain of the Arabidopsis thaliana Sulfate Transporter SULTR1.2^*

Hatem Rouached, Pierre Berthomieu, Elie El Kassis, Nicole Cathala, Vincent Catherinot, Gilles Labesse, Jean-Claude Davidian, and Pierre Fourcroy¶

From the Biochimie et Physiologie Moléculaire des Plantes, CNRS (UMR 5004), Université Montpellier 2, Institut National de la Recherche Agronomique, Ecole Nationale Supérieure Agronomique, Montpellier, 34060 France and Centre de Biochimie Structurale, INSERM U554, Centre National de la Recherche Scientifique (UMR 5048), Université Montpellier I, Montpellier, 34060 France

The C-terminal region of sulfate transporters from plants and animals belonging to the SLC26 family members shares a weak but significant similarity with the Bacillus sp. anti-anti-sigma protein SpoIIAA, thus defining the STAS domain (sulfate transporter and anti-sigma antagonist). The present study is a structure/function analysis of the STAS domain of SULTR1.2, an Arabidopsis thaliana sulfate transporter. A three-dimensional model of the SULTR1.2 STAS domain was built which indicated that it shares the SpoIIAA folds. Moreover, the phosphorylation site, which is necessary for SpoIIAA activity, is conserved in the SULTR1.2 STAS domain. The model was used to direct mutagenesis studies using a yeast mutant defective for sulfate transport. Truncation of the whole SULTR1.2 STAS domain resulted in the loss of sulfate transport function. Analyses of small deletions and mutations showed that the C-terminal tail of the SULTR1.2 STAS domain and particularly two cysteine residues plays an important role in sulfate transport by SULTR1.2. All the substitutions made at the putative phosphorylation site Thr-587 led to a complete loss of the sulfate transport function of SULTR1.2. The reduction or suppression of sulfate transport of the SULTR1.2 mutants in yeast was not due to an incorrect targeting to the plasma membrane. Both our three-dimensional modeling and mutational analyses strengthen the hypothesis that the SULTR1.2 STAS domain is involved in protein-protein interactions that could control sulfate transport.

Received for publication, February 11, 2005

^* This work was supported by grants from the French research organizations Institut National de la Recherche Agronomique and CNRS and fellowships from the French Ministère de l'Enseignement Supérieur et de la Recherche (to E. E. K.) and from the Tunisian government (to H. R.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed. Tel.: 33-499-612-612; Fax: 33-467-525-737; E-mail: fourcroy{at}ensam.inra.fr.

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