New insights into the operative network of FaEO, an enone oxidoreductase from Fragaria x ananassa Duch.
Plant Mol Biol
; 94(1-2): 125-136, 2017 May.
Article
em En
| MEDLINE
| ID: mdl-28283921
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.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oxirredutases
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Proteínas de Plantas
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Regulação Enzimológica da Expressão Gênica
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Regulação da Expressão Gênica de Plantas
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Fragaria
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Plant Mol Biol
Assunto da revista:
BIOLOGIA MOLECULAR
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BOTANICA
Ano de publicação:
2017
Tipo de documento:
Article
País de afiliação:
Itália