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First published online January 27, 2006; 10.1104/pp.105.074955 Plant Physiology 140:1047-1058 (2006) © 2006 American Society of Plant Biologists Cinnamate Metabolism in Ripening Fruit. Characterization of a UDP-Glucose:Cinnamate Glucosyltransferase from Strawberry1Biomolecular Food Technology, Technical University Munich, 85354 Freising, Germany (S.L., H.A.C., W.S.); Departamento de Bioquímica y Biología Molecular Edificio Severo Ochoa (C-6), Campus Universitario de Rabanales, Universidad de Córdoba, 14071 Cordoba, Spain (M.B., J.M.-B.); Plant Research International, Business Units Cell Cybernetics and Genetics and Breeding, 6700 AA Wageningen, The Netherlands (A.A., E.M.J.S.); and Section of Biology and Membrane Physics, Technical University Darmstadt, 64287 Darmstadt, Germany (R.K.)
Strawberry (Fragaria x ananassa) fruit accumulate (hydroxy)cinnamoyl glucose (Glc) esters, which may serve as the biogenetic precursors of diverse secondary metabolites, such as the flavor constituents methyl cinnamate and ethyl cinnamate. Here, we report on the isolation of a cDNA encoding a UDP-Glc:cinnamate glucosyltransferase (Fragaria x ananassa glucosyltransferase 2 [FaGT2]) from ripe strawberry cv Elsanta that catalyzes the formation of 1-O-acyl-Glc esters of cinnamic acid, benzoic acid, and their derivatives in vitro. Quantitative real-time PCR analysis indicated that FaGT2 transcripts accumulate to high levels during strawberry fruit ripening and to lower levels in flowers. The levels in fruits positively correlated with the in planta concentration of cinnamoyl, p-coumaroyl, and caffeoyl Glc. In the leaf, high amounts of Glc esters were detected, but FaGT2 mRNA was not observed. The expression of FaGT2 is negatively regulated by auxin, induced by oxidative stress, and by hydroxycinnamic acids. Although FaGT2 glucosylates a number of aromatic acids in vitro, quantitative analysis in transgenic lines containing an antisense construct of FaGT2 under the control of the constitutive 35S cauliflower mosaic virus promoter demonstrated that the enzyme is only involved in the formation of cinnamoyl Glc and p-coumaroyl Glc during ripening.
1 This work was supported by Degussa AG. 2 These authors contributed equally to the paper. 3 Present address: Department of Plant Sciences, Weizmann Institute of Science, 76100 Rehovot, Israel. 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: Wilfried Schwab (schwab{at}wzw.tum.de). Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.105.074955. * Corresponding author; e-mail schwab{at}wzw.tum.de; fax 498161548595. Received November 30, 2005; returned for revision November 30, 2005; accepted December 14, 2005. This article has been cited by other articles:
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