Selective Accumulation of Delphinidin Derivatives in Tobacco Using a Putative Flavonoid 3′,5′-Hydroxylase cDNA from<i>Campanula medium</i>

Okinaka, Yasushi; Shimada, Yukihisa; Nakano-Shimada, Ritsuko; Ohbayashi, Masaya; Kiyokawa, Shigeto; Kikuchi, Yasuhiro

doi:10.1271/bbb.67.161

Cited by 58 publications

(41 citation statements)

References 17 publications

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“…The trees obtained confirmed the above result, indicating that the F3¢5¢Hs of Asteraceae arose within the Asteraceae (Figure 4). By contrast, the functionally verified F3¢5¢H sequence of Campanula medium (Okinaka et al, 2003) from the closely related Campanulaceae clustered with typical F3¢5¢Hs (Figure 3). …”

Section: Phylogenetic Analysismentioning

confidence: 92%

Cloning, Functional Identification and Sequence Analysis of Flavonoid 3′-hydroxylase and Flavonoid 3′,5′-hydroxylase cDNAs Reveals Independent Evolution of Flavonoid 3′,5′-hydroxylase in the Asteraceae Family

Seitz¹,

Eder²,

Deiml³

et al. 2006

Plant Mol Biol

143

133

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Flavonoids are ubiquitous secondary plant metabolites which function as protectants against UV light and pathogens and are involved in the attraction of pollinators as well as seed and fruit dispersers. The hydroxylation pattern of the B-ring of flavonoids is determined by the activity of two members of the vast and versatile cytochrome P450 protein (P450) family, the flavonoid 3'-hydroxylase (F3'H) and flavonoid 3',5'-hydroxylase (F3'5'H). Phylogenetic analysis of known sequences of F3'H and F3'5'H indicated that F3'5'H was recruited from F3'H before the divergence of angiosperms and gymnosperms. Seven cDNAs were isolated from species of the Asteraceae family, all of which were predicted to code for F3'Hs based on their sequences. The recombinant proteins of four of the heterologously in yeast expressed cDNAs exhibited the expected F3'H activity but surprisingly, three recombinant proteins showed F3'5'H activity. Phylogenetic analyses indicated the independent evolution of an Asteraceae-specific F3'5'H. Furthermore, sequence analysis of these unusual F3'5'H cDNAs revealed an elevated rate of nonsynonymous substitutions as typically found for duplicated genes acquiring new functions. Since F3'5'H is necessary for the synthesis of 3',4',5'-hydroxylated delphinidin-derivatives, which normally provide the basis for purple to blue flower colours, the evolution of an Asteraceae-specific F3'5'H probably reflects the adaptive value of efficient attraction of insect pollinators.

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Section: Phylogenetic Analysismentioning

confidence: 92%

Cloning, Functional Identification and Sequence Analysis of Flavonoid 3′-hydroxylase and Flavonoid 3′,5′-hydroxylase cDNAs Reveals Independent Evolution of Flavonoid 3′,5′-hydroxylase in the Asteraceae Family

Seitz¹,

Eder²,

Deiml³

et al. 2006

Plant Mol Biol

143

133

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“…delphinidin), which are usually a prerequisite for the expression of blue or purple flower color. F35H genes have already been cloned from Campanula medium (Okinaka et al 2003), Solanaceae (De Jong et al 2004), Catharanthus roseus (Kaltenbach et al 1999), and Eustoma grandiflorum (Nielsen & Podiwinsky 1997). In addition, flavonoid-3¢,5¢-hydroxylases have been well studied in Petunia hybrida (Holton et al 1993), which has two genetic loci Hf1 and Hf2.…”

Section: Introductionmentioning

confidence: 99%

Flavonoid-3′,5′-hydroxylase from Phalaenopsis: A Novel Member of Cytochrome P450s, its cDNA Cloning, Endogenous Expression and Molecular Modeling

et al. 2006

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A novel cDNA for the flavonoid-3',5'-hydroxylase (F35H) gene was cloned from petals of Phalaenopsis, and designated as Phf35h (accession number DQ148458 in GenBank/EMBL/DDBJ). The genomic clone of Phf35h was isolated by a PCR-based strategy. Nucleotide sequence analysis revealed that its genomic clone contains one intron and an open reading frame encoding a polypeptide of 507 amino acid residues. Southern hybridization analysis indicated the presence of a single gene coding for Phf35h. RT-PCR analysis showed that the Phf35h mRNA is transcribed in late phase of petal development, which is concomitant with the appearance of anthocyanins in petal tissue. The transcript is abundant in the purple petals but not in leaves or roots. The three-dimensional model of PhF3'5'H protein is classified into an alpha-domain which contains most of the alpha-helices with three small beta-sheets, a beta-domain that contains the larger beta-sheets with three small alpha-helices by homology modeling. The substrate-binding site for dihydrokaempferol on PhF3'5'H protein was determined by molecular docking algorithm. A highly conserved HPPTPLSLPH sequence was predicted to contact the aromatic ring of dihydrokaempferol.

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“…After the first isolation and functional characterization of the genes encoding F3#H and F3#5#H in petunia (Petunia hybrida; Holton et al, 1993;Brugliera et al, 1999), the genes were subsequently isolated from various plant species. F3#H was characterized in Arabidopsis (Arabidopsis thaliana; Schoenbohm et al, 2000), and F3#5#H cDNAs were isolated from a number of plants, including Solanum melongena (Toguri et al, 1993), Gentiana triflora (Tanaka et al, 1996), Eustoma grandiflorum (Nielsen and Podivinsky, 1997), Eustoma rusellianum (Shimada et al, 1999), Catharanthus roseus (Kaltenbach et al, 1999), Campanula medium (Okinaka et al, 2003), and Vinca major (Mori et al, 2004). Some plants, including Arabidopsis and important members of the Rosaceae such as apples (Malus spp.)…”

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confidence: 99%

Identification of the Flavonoid Hydroxylases from Grapevine and Their Regulation during Fruit Development

et al. 2005

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(J.B., D.M., S.P.R.)Flavonoids are important secondary metabolites in many fruits, and their hydroxylation pattern determines their color, stability, and antioxidant capacity. Hydroxylation of the B-ring of flavonoids is catalyzed by flavonoid 3#-hydroxylase (F3#H) and flavonoid 3#,5#-hydroxylase (F3#5#H), and may also require cytochrome b 5 . We report the identification of genes encoding F3#H, F3#5#H, and a putative cytochrome b 5 from grapevine (Vitis vinifera L. cv Shiraz) and their transcriptional regulation in fruit. Functionality of the genes VvF3#H and VvF3#5#H1 was demonstrated by ectopic expression in petunia (Petunia hybrida), which altered flower color and flavonoid composition as expected. VvF3#H was expressed in grapes before flowering, when 3#-hydroxylated flavonols are made, and all three genes were expressed after flowering, when proanthocyanidins (PAs) are synthesized. In berry skin, expression of all three genes was low at the onset of ripening (véraison) but increased after véraison concomitant with the accumulation of 3#-and 3#,5#-hydroxylated anthocyanins. VvF3#H and VvCytoB5 were expressed in seeds but not VvF3#5#H1, consistent with the accumulation of 3#-hydroxylated PAs in this tissue. VvCytoB5 expression was correlated with expression of both VvF3#H and VvF3#5#H1 in the different grape tissues. In contrast to red grapes, where VvF3#H, VvF3#5#H1, and VvCytoB5 were highly expressed during ripening, the expression of VvF3#5#H1 and VvCytoB5 in white grapes during ripening was extremely low, suggesting a difference in transcriptional regulation. Our results show that temporal and tissue-specific expression of VvF3#H, VvF3#5#H1, and VvCytoB5 in grapes is coordinated with the accumulation of the respective hydroxylated flavonols and PAs, as well as anthocyanins. Understanding the regulation of flavonoid hydroxylases could be used to modify flavonoid composition of fruits.

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Selective Accumulation of Delphinidin Derivatives in Tobacco Using a Putative Flavonoid 3′,5′-Hydroxylase cDNA fromCampanula medium

Cited by 58 publications

References 17 publications

Cloning, Functional Identification and Sequence Analysis of Flavonoid 3′-hydroxylase and Flavonoid 3′,5′-hydroxylase cDNAs Reveals Independent Evolution of Flavonoid 3′,5′-hydroxylase in the Asteraceae Family

Cloning, Functional Identification and Sequence Analysis of Flavonoid 3′-hydroxylase and Flavonoid 3′,5′-hydroxylase cDNAs Reveals Independent Evolution of Flavonoid 3′,5′-hydroxylase in the Asteraceae Family

Flavonoid-3′,5′-hydroxylase from Phalaenopsis: A Novel Member of Cytochrome P450s, its cDNA Cloning, Endogenous Expression and Molecular Modeling

Identification of the Flavonoid Hydroxylases from Grapevine and Their Regulation during Fruit Development

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