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First published online August 8, 2003; 10.1105/tpc.013854

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The Plant Cell, Vol. 15, 2165-2180, September 2003, Copyright © 2003,
American Society of Plant Biologists

A Grape ASR Protein Involved in Sugar and Abscisic Acid Signaling

Birsen Çakir, Alice Agasse, Cécile Gaillard, Amélie Saumonneau, Serge Delrot and Rossitza Atanassova1

Unité Mixte de Recherche Centre National de la Recherche Scientifique 6161, Transport des Assimilats, Laboratoire de Physiologie, Biochimie et Biologie Moléculaire Végétales, Bâtiment Botanique, Unité de Formation et de Recherches Sciences, 86022 Poitiers Cédex, France

1 To whom correspondence should be addressed. E-mail rossitza.atanassova{at}univ-poitiers.fr; fax 33-[0]5-49-45-41-86

The function of ASR (ABA [abscisic acid]-, stress-, and ripening-induced) proteins remains unknown. A grape ASR, VvMSA, was isolated by means of a yeast one-hybrid approach using as a target the proximal promoter of a grape putative monosaccharide transporter (VvHT1). This promoter contains two sugar boxes, and its activity is induced by sucrose and glucose. VvMSA and VvHT1 share similar patterns of expression during the ripening of grape. Both genes are inducible by sucrose in grape berry cell culture, and sugar induction of VvMSA is enhanced strongly by ABA. These data suggest that VvMSA is involved in a common transduction pathway of sugar and ABA signaling. Gel-shift assays demonstrate a specific binding of VvMSA to the 160-bp fragment of the VvHT1 promoter and more precisely to two sugar-responsive elements present in this target. The positive regulation of VvHT1 promoter activity by VvMSA also is shown in planta by coexpression experiments. The nuclear localization of the yellow fluorescent protein–VvMSA fusion protein and the functionality of the VvMSA nuclear localization signal are demonstrated. Thus, a biological function is ascribed to an ASR protein. VvMSA acts as part of a transcription-regulating complex involved in sugar and ABA signaling.




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