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J. Biol. Chem., Vol. 282, Issue 32, 23541-23552, August 10, 2007

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Regulation of Root Nitrate Uptake at the NRT2.1 Protein Level in Arabidopsis thaliana^*

Judith Wirth¹, Franck Chopin¹, Véronique Santoni, Gaëlle Viennois, Pascal Tillard, Anne Krapp, Laurence Lejay², Franoise Daniel-Vedele, and Alain Gojon

From the Institut de Biologie Intégrative des Plantes, UMR 5004, Biochimie et Physiologie Moléculaire des Plantes, CNRS/INRA/SupAgro/UM2, Place Viala, F-34060 Montpellier, France and the Unité de Nutrition Azotée des Plantes, INRA, route de St. Cyr, F-78026 Versailles, France

In Arabidopsis the NRT2.1 gene encodes a main component of the root high-affinity nitrate uptake system (HATS). Its regulation has been thoroughly studied showing a strong correlation between NRT2.1 expression and HATS activity. Despite its central role in plant nutrition, nothing is known concerning localization and regulation of NRT2.1 at the protein level. By combining a green fluorescent protein fusion strategy and an immunological approach, we show that NRT2.1 is mainly localized in the plasma membrane of root cortical and epidermal cells, and that several forms of the protein seems to co-exist in cell membranes (the monomer and at least one higher molecular weight complex). The monomer is the most abundant form of NRT2.1, and seems to be the one involved in transport. It strictly requires the NAR2.1 protein to be expressed and addressed at the plasma membrane. No rapid changes in NRT2.1 abundance were observed in response to light, sucrose, or nitrogen treatments that strongly affect both NRT2.1 mRNA level and HATS activity. This suggests the occurrence of post-translational regulatory mechanisms. One such mechanism could correspond to the cleavage of NRT2.1 C terminus, which results in the presence of both intact and truncated proteins in the plasma membrane.

Received for publication, January 31, 2007 , and in revised form, June 14, 2007.

^* This work was supported by European Union program PLUSN Grant HPRN-CT-2002-00247. 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1-S4.

¹ Both authors contributed equally to this work.

² To whom correspondence should be addressed. Tel.: 33-499-612-602; Fax: 33-467-525-737; E-mail: lejay{at}supagro.inra.fr.

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