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ENVIRONMENTAL STRESS AND ADAPTATION TO STRESS

AtHMA3, a P_1B-ATPase Allowing Cd/Zn/Co/Pb Vacuolar Storage in Arabidopsis^1,[W]

Commissariat à l'Energie Atomique, DSV, IBEB, Lab Echanges Membran and Signalisation, Saint-Paul-lez-Durance F–13108, France; CNRS, UMR Biol Veget and Microbiol Environ, Saint-Paul-lez-Durance F–13108, France; and Aix-Marseille Université, Saint-Paul-lez-Durance F–13108, France

The Arabidopsis (Arabidopsis thaliana) Heavy Metal Associated3 (AtHMA3) protein belongs to the P_1B-2 subgroup of the P-type ATPase family, which is involved in heavy metal transport. In a previous study, we have shown, using heterologous expression in the yeast Saccharomyces cerevisiae, that in the presence of toxic metals, AtHMA3 was able to phenotypically complement the cadmium/lead (Cd/Pb)-hypersensitive strain ycf1 but not the zinc (Zn)-hypersensitive strain zrc1. In this study, we demonstrate that AtHMA3 in planta is located in the vacuolar membrane, with a high expression level in guard cells, hydathodes, vascular tissues, and the root apex. Confocal imaging in the presence of the Zn/Cd fluorescent probe BTC-5N revealed that AtHMA3 participates in the vacuolar storage of Cd. A T-DNA insertional mutant was found more sensitive to Zn and Cd. Conversely, ectopic overexpression of AtHMA3 improved plant tolerance to Cd, cobalt, Pb, and Zn; Cd accumulation increased by about 2- to 3-fold in plants overexpressing AtHMA3 compared with wild-type plants. Thus, AtHMA3 likely plays a role in the detoxification of biological (Zn) and nonbiological (Cd, cobalt, and Pb) heavy metals by participating in their vacuolar sequestration, an original function for a P_1B-2 ATPase in a multicellular eukaryote.

² Present address: IFR 110 Génomique, Ecophysiologie et Ecologie Fonctionnelles, UMR1136 UHP Nancy1/INRA Interaction Arbres Microorganismes, Faculté des Sciences et Techniques, BP239, Vandoeuvre-les-Nancy F–54506, France.

³ Present address: URVVC EA 2069, Université de Reims Champagne Ardenne, UFR Sciences Exactes et Naturelles, Moulin de la Housse, Bâtiment 18, BP 1039, Reims cedex 02 F–51687, France.

⁴ Present address: UMR6026-ICM CNRS-Université de Rennes 1, Campus de Beaulieu, CS 74205, Rennes F–35042, France.

⁵ Present address: CEA, DSV, IBEB, Lab Bioenerget Biotechnol Bacteries and Microalgues, Saint-Paul-lez-Durance F–13108, France.

The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Pierre Richaud (pierre.richaud{at}cea.fr).

^[W] The online version of this article contains Web-only data.

www.plantphysiol.org/cgi/doi/10.1104/pp.108.130294

^* Corresponding author; e-mail pierre.richaud{at}cea.fr.

Received September 24, 2008; accepted November 21, 2008; published November 26, 2008.

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