Characterization of the Brassica napus Flavonol Synthase Gene Family Reveals Bifunctional Flavonol Synthases

Flavonol synthase (FLS) is a key enzyme for the formation of flavonols, which are a subclass of the flavonoids. FLS catalyzes the conversion of dihydroflavonols to flavonols. The enzyme belongs to the 2-oxoglutarate-dependent dioxygenases (2-ODD) superfamily. We characterized the FLS gene family of...

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Main Authors: Hanna Marie Schilbert, Maximilian Schöne, Thomas Baier, Mareike Busche, Prisca Viehöver, Bernd Weisshaar, Daniela Holtgräwe
Format: Article
Language:English
Published: Frontiers Media S.A. 2021-10-01
Series:Frontiers in Plant Science
Subjects:
Online Access:https://www.frontiersin.org/articles/10.3389/fpls.2021.733762/full
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author Hanna Marie Schilbert
Maximilian Schöne
Thomas Baier
Mareike Busche
Prisca Viehöver
Bernd Weisshaar
Daniela Holtgräwe
author_facet Hanna Marie Schilbert
Maximilian Schöne
Thomas Baier
Mareike Busche
Prisca Viehöver
Bernd Weisshaar
Daniela Holtgräwe
author_sort Hanna Marie Schilbert
collection DOAJ
description Flavonol synthase (FLS) is a key enzyme for the formation of flavonols, which are a subclass of the flavonoids. FLS catalyzes the conversion of dihydroflavonols to flavonols. The enzyme belongs to the 2-oxoglutarate-dependent dioxygenases (2-ODD) superfamily. We characterized the FLS gene family of Brassica napus that covers 13 genes, based on the genome sequence of the B. napus cultivar Express 617. The goal was to unravel which BnaFLS genes are relevant for seed flavonol accumulation in the amphidiploid species B. napus. Two BnaFLS1 homeologs were identified and shown to encode bifunctional enzymes. Both exhibit FLS activity as well as flavanone 3-hydroxylase (F3H) activity, which was demonstrated in vivo and in planta. BnaFLS1-1 and -2 are capable of converting flavanones into dihydroflavonols and further into flavonols. Analysis of spatio-temporal transcription patterns revealed similar expression profiles of BnaFLS1 genes. Both are mainly expressed in reproductive organs and co-expressed with the genes encoding early steps of flavonoid biosynthesis. Our results provide novel insights into flavonol biosynthesis in B. napus and contribute information for breeding targets with the aim to modify the flavonol content in rapeseed.
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spelling doaj.art-c615703e05ba446ba4ef0fd0e61d08022022-12-21T21:29:52ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2021-10-011210.3389/fpls.2021.733762733762Characterization of the Brassica napus Flavonol Synthase Gene Family Reveals Bifunctional Flavonol SynthasesHanna Marie Schilbert0Maximilian Schöne1Thomas Baier2Mareike Busche3Prisca Viehöver4Bernd Weisshaar5Daniela Holtgräwe6Genetics and Genomics of Plants, CeBiTec and Faculty of Biology, Bielefeld University, Bielefeld, GermanyGenetics and Genomics of Plants, CeBiTec and Faculty of Biology, Bielefeld University, Bielefeld, GermanyAlgae Biotechnology and Bioenergy, CeBiTec and Faculty of Biology, Bielefeld University, Bielefeld, GermanyGenetics and Genomics of Plants, CeBiTec and Faculty of Biology, Bielefeld University, Bielefeld, GermanyGenetics and Genomics of Plants, CeBiTec and Faculty of Biology, Bielefeld University, Bielefeld, GermanyGenetics and Genomics of Plants, CeBiTec and Faculty of Biology, Bielefeld University, Bielefeld, GermanyGenetics and Genomics of Plants, CeBiTec and Faculty of Biology, Bielefeld University, Bielefeld, GermanyFlavonol synthase (FLS) is a key enzyme for the formation of flavonols, which are a subclass of the flavonoids. FLS catalyzes the conversion of dihydroflavonols to flavonols. The enzyme belongs to the 2-oxoglutarate-dependent dioxygenases (2-ODD) superfamily. We characterized the FLS gene family of Brassica napus that covers 13 genes, based on the genome sequence of the B. napus cultivar Express 617. The goal was to unravel which BnaFLS genes are relevant for seed flavonol accumulation in the amphidiploid species B. napus. Two BnaFLS1 homeologs were identified and shown to encode bifunctional enzymes. Both exhibit FLS activity as well as flavanone 3-hydroxylase (F3H) activity, which was demonstrated in vivo and in planta. BnaFLS1-1 and -2 are capable of converting flavanones into dihydroflavonols and further into flavonols. Analysis of spatio-temporal transcription patterns revealed similar expression profiles of BnaFLS1 genes. Both are mainly expressed in reproductive organs and co-expressed with the genes encoding early steps of flavonoid biosynthesis. Our results provide novel insights into flavonol biosynthesis in B. napus and contribute information for breeding targets with the aim to modify the flavonol content in rapeseed.https://www.frontiersin.org/articles/10.3389/fpls.2021.733762/fullflavonoid biosynthesisspecialized metabolismrapeseed2-oxoglutarate-dependent dioxygenasesflavanone 3-hydroxylasebifunctionality
spellingShingle Hanna Marie Schilbert
Maximilian Schöne
Thomas Baier
Mareike Busche
Prisca Viehöver
Bernd Weisshaar
Daniela Holtgräwe
Characterization of the Brassica napus Flavonol Synthase Gene Family Reveals Bifunctional Flavonol Synthases
Frontiers in Plant Science
flavonoid biosynthesis
specialized metabolism
rapeseed
2-oxoglutarate-dependent dioxygenases
flavanone 3-hydroxylase
bifunctionality
title Characterization of the Brassica napus Flavonol Synthase Gene Family Reveals Bifunctional Flavonol Synthases
title_full Characterization of the Brassica napus Flavonol Synthase Gene Family Reveals Bifunctional Flavonol Synthases
title_fullStr Characterization of the Brassica napus Flavonol Synthase Gene Family Reveals Bifunctional Flavonol Synthases
title_full_unstemmed Characterization of the Brassica napus Flavonol Synthase Gene Family Reveals Bifunctional Flavonol Synthases
title_short Characterization of the Brassica napus Flavonol Synthase Gene Family Reveals Bifunctional Flavonol Synthases
title_sort characterization of the brassica napus flavonol synthase gene family reveals bifunctional flavonol synthases
topic flavonoid biosynthesis
specialized metabolism
rapeseed
2-oxoglutarate-dependent dioxygenases
flavanone 3-hydroxylase
bifunctionality
url https://www.frontiersin.org/articles/10.3389/fpls.2021.733762/full
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