New insights into the operative network of FaEO,an enone oxidoreductase from <Emphasis Type="Italic">Fragaria x ananassa</Emphasis> Duch. |
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Authors: | Gabriella Collu Domenica Farci Francesca Esposito Francesca Pintus Joanna Kirkpatrick Dario Piano |
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Institution: | 1.Laboratory of Plant Physiology and Photobiology, Department of Life and Environmental Sciences,University of Cagliari,Cagliari,Italy;2.Department of Molecular Sensory Systems,Center of Advanced European Studies and Research (caesar),Bonn,Germany;3.Department of Life and Environmental Sciences,University of Cagliari, Cittadella Universitaria,Monserrato,Italy;4.Leibniz Institute on Aging – Fritz Lipmann Institute,Jena,Germany |
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Abstract: | The 2-methylene-furan-3-one reductase or Fragaria x ananassa Enone Oxidoreductase (FaEO) catalyses the last reductive step in the biosynthesis of 4-hydroxy-2,5-dimethyl-3(2H)-furanone, a major component in the characteristic flavour of strawberries. In the present work, we describe the association between FaEO and the vacuolar membrane of strawberry fruits. Even if FaEO lacks epitopes for stable or transient membrane-interactions, it contains a calmodulin-binding region, suggesting that in vivo FaEO may be associated with the membrane via a peripheral protein complex with calmodulin. Moreover, we also found that FaEO occurs in dimeric form in vivo and, as frequently observed for calmodulin-regulated proteins, it may be expressed in different isoforms by alternative gene splicing. Further mass spectrometry analysis confirmed that the isolated FaEO consists in the already known isoform and that it is the most characteristic during ripening. Finally, a characterization by absorption spectroscopy showed that FaEO has specific flavoprotein features. The relevance of these findings and their possible physiological implications are discussed. |
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