Metabolomic and genetic analyses of flavonol synthesis in Arabidopsis thaliana support the in vivo involvement of leucoanthocyanidin dioxygenase

R. Stracke, R.C.H. de Vos, L. Bartelniewoehner, H. Ishihara, M. Sagasser, S. Martens, B. Weisshaar

    Research output: Contribution to journalArticleAcademicpeer-review

    69 Citations (Scopus)

    Abstract

    Flavonol synthase (FLS) (EC-number 1.14.11.23), the enzyme that catalyses the conversion of flavonols into dihydroflavonols, is part of the flavonoid biosynthesis pathway. In Arabidopsis thaliana, this activity is thought to be encoded by several loci. In addition to the FLAVONOL SYNTHASE1 (FLS1) locus that has been confirmed by enzyme activity assays, loci displaying similarity of the deduced amino acid sequences to FLS1 have been identified. We studied the putative A. thaliana FLS gene family using a combination of genetic and metabolite analysis approaches. Although several of the FLS gene family members are expressed, only FLS1 appeared to influence flavonoid biosynthesis. Seedlings of an A. thaliana fls1 null mutant (fls1-2) show enhanced anthocyanin levels, drastic reduction in flavonol glycoside content and concomitant accumulation of glycosylated forms of dihydroflavonols, the substrate of the FLS reaction. By using a leucoanthocyanidin dioxygenase (ldox) fls1-2 double mutant, we present evidence that the remaining flavonol glycosides found in the fls1-2 mutant are synthesized in planta by the FLS-like side activity of the LDOX enzyme
    Original languageEnglish
    Pages (from-to)427-445
    JournalPlanta
    Volume229
    Issue number2
    DOIs
    Publication statusPublished - 2009

      Fingerprint

    Keywords

    • phenylpropanoid biosynthesis
    • anthocyanidin synthase
    • functional expression
    • transcription factor
    • petunia-hybrida
    • flavanone 3-beta-hydroxylase
    • differential regulation
    • conserved histidine
    • mass-spectrometry
    • escherichia-coli

    Cite this