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Published on March 18, 2009; 10.1104/pp.109.135624

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Received January 13, 2009
Accepted March 16, 2009

Vitis vinifera MATE-type Proteins Act as Vacuolar H+-Dependent Acylated Anthocyanin Transporters

Camila Gomez , Nancy Terrier , Laurent Torregrosa , Sandrine Vialet , Alexandre Fournier-Level , Clotilde Verries , Jean-Marc Souquet , Jean-Paul Mazauric , Markus Klein , Veronique Cheynier , and Agnes Ageorges *

UMR Sciences pour l'OEnologie, INRA Campus SupAgro, 2 place Viala, F-34060 Montpellier, France; UMR DIAPC 1097 INRA Campus SupAgro, 2 place Viala, F-34060 Montpellier, France; Zurich Basel Plant Science Center, University of Zurich, Plant Biology, Zollikerstrasse 107, CH-8008 Zurich, Switzerland

* Corresponding author; email: ageorges{at}supagro.inra.fr.

In grapevine, anthocyanins are responsible for most of the red, blue and purple pigmentation found in the skin of berries. In cells, anthocyanins are synthesised in the cytoplasm and accumulated into the vacuole. However, little is known about the transport of these compounds through the tonoplast. Recently, the sequencing of Vitis vinifera genome allowed us to identify genes encoding proteins with high sequence similarity to the Multidrug and Toxic Extrusion (MATE) family. Among them, we selected two genes as anthocyanin transporter candidates and named them anthoMATE1 (AM1) and anthoMATE3 (AM3). The expression of both genes was mainly fruit-specific and concomitant with the accumulation of anthocyanin pigment. Subcellular localization assays in grapevine hairy roots stably transformed with AM1- or AM3::GFP fusion protein revealed that AM1 and AM3 are primarily localized to the tonoplast. Yeast vesicles expressing anthoMATEs transported acylated anthocyanins in the presence of MgATP. Inhibitor studies demonstrated that AM1 and AM3 proteins act in vitro as vacuolar H+-dependent acylated anthocyanin transporters. By contrast, under our experimental conditions, anthoMATEs could not transport malvidin 3-O-glucoside or cyanidin 3-O-glucoside, suggesting that the acyl conjugation was essential for the uptake. Taken together, these results provide evidence that in vitro the two grapevine AM1 and AM3 proteins mediate specifically acylated anthocyanin transport.




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