Excision of the Candystripe1 transposon from a hyper-mutable Y1-cs allele shows that the sorghumY1 gene controls the biosynthesis of both 3-deoxyanthocyanidin phytoalexins and phlobaphene pigments

Chopra, Surinder; Gevens, A. J.; Svabek, Catherine; Wood, Karl V.; Peterson, T.; Nicholson, Ralph L.

doi:10.1006/pmpp.2002.0411

Cited by 26 publications

(26 citation statements)

References 41 publications

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“…Several lines of evidence showed that flavan 4-ols are the precursors of 3-deoxyanthocyanidins [16,17,33-35]. Since, Zmf3 ’ h1 plays a role in the differential accumulation of p1 regulated flavan 4-ols, we tested if Zmf3 ’ h1 also influences the accumulation of 3-deoxyanthocyanidins.…”

Section: Resultsmentioning

confidence: 99%

“…In sorghum, attempted penetration of Cochliobolus heterostrophus leads to up regulation of a f3 ’ h gene and sequential accumulation of luteolinidin [27]. The 3-deoxyanthocyanidin pathway in sorghum requires a MYB protein encoded by yellow seed1 ( y1 ), an ortholog of maize p1 [33,45,46]. Similar to the regulation of Zmf3 ’ h1 by p1 , sorghum f3 ’ h is regulated by y1 [46].…”

Section: Discussionmentioning

confidence: 99%

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Expression of flavonoid 3’-hydroxylase is controlled by P1, the regulator of 3-deoxyflavonoid biosynthesis in maize

et al. 2012

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BackgroundThe maize (Zea mays) red aleurone1 (pr1) encodes a CYP450-dependent flavonoid 3’-hydroxylase (ZmF3’H1) required for the biosynthesis of purple and red anthocyanin pigments. We previously showed that Zmf3’h1 is regulated by C1 (Colorless1) and R1 (Red1) transcription factors. The current study demonstrates that, in addition to its role in anthocyanin biosynthesis, the Zmf3’h1 gene also participates in the biosynthesis of 3-deoxyflavonoids and phlobaphenes that accumulate in maize pericarps, cob glumes, and silks. Biosynthesis of 3-deoxyflavonoids is regulated by P1 (Pericarp color1) and is independent from the action of C1 and R1 transcription factors.ResultsIn maize, apiforol and luteoforol are the precursors of condensed phlobaphenes. Maize lines with functional alleles of pr1 and p1 (Pr1;P1) accumulate luteoforol, while null pr1 lines with a functional or non-functional p1 allele (pr1;P1 or pr1;p1) accumulate apiforol. Apiforol lacks a hydroxyl group at the 3’-position of the flavylium B-ring, while luteoforol has this hydroxyl group. Our biochemical analysis of accumulated compounds in different pr1 genotypes showed that the pr1 encoded ZmF3’H1 has a role in the conversion of mono-hydroxylated to bi-hydroxylated compounds in the B-ring. Steady state RNA analyses demonstrated that Zmf3’h1 mRNA accumulation requires a functional p1 allele. Using a combination of EMSA and ChIP experiments, we established that the Zmf3’h1 gene is a direct target of P1. Highlighting the significance of the Zmf3’h1 gene for resistance against biotic stress, we also show here that the p1 controlled 3-deoxyanthocyanidin and C-glycosyl flavone (maysin) defence compounds accumulate at significantly higher levels in Pr1 silks as compared to pr1 silks. By virtue of increased maysin synthesis in Pr1 plants, corn ear worm larvae fed on Pr1; P1 silks showed slower growth as compared to pr1; P1 silks.ConclusionsOur results show that the Zmf3’h1 gene participates in the biosynthesis of phlobaphenes and agronomically important 3-deoxyflavonoid compounds under the regulatory control of P1.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Expression of flavonoid 3’-hydroxylase is controlled by P1, the regulator of 3-deoxyflavonoid biosynthesis in maize

et al. 2012

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“…[15]). Furthermore, in some plants a bypass may exist avoiding the 3β‐hydroxylation of (2 S )‐flavanones and leading to (2 R ,4 R )‐flavan‐4‐ols (phlobaphenes) [16] and 3‐deoxyanthocyanidins.…”

Section: Introductionmentioning

confidence: 99%

Anthocyanidin synthase from Gerbera hybrida catalyzes the conversion of (+)‐catechin to cyanidin and a novel procyanidin

Wellmann¹,

Grießer²,

Schwab³

et al. 2006

FEBS Letters

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Anthocyanidins were proposed to derive from (+)-naringenin via (2R,3R)-dihydroflavonol(s) and (2R,3S,4S)-leucocyanidin(s) which are eventually oxidized by anthocyanidin synthase (ANS). Recently, the role of ANS has been put into question, because the recombinant enzyme from Arabidopsis exhibited primarily flavonol synthase (FLS) activity with negligible ANS activity. This and other studies led to the proposal that ANS as well as FLS may select for dihydroflavonoid substrates carrying a ''b-face'' C-3 hydroxyl group and initially form the 3-geminal diol by ''a-face'' hydroxylation. Assays with recombinant ANS from Gerbera hybrida fully supported the proposal and were extended to catechin and epicatechin isomers as potential substrates to delineate the enzyme specificity. Gerbera ANS converted (+)-catechin to two major and one minor product, whereas ent(À)-catechin (2S,3R-trans-catechin), (À)-epicatechin, ent(+)-epicatechin (2S,3S-cis-epicatechin) and (À)-gallocatechin were not accepted. The K m value for (+)-catechin was determined at 175 lM, and the products were identified by LC-MS n and NMR as the 4,4-dimer of oxidized (+)-catechin (93%), cyanidin (7%) and quercetin (trace). When these incubations were repeated in the presence of UDP-glucose:flavonoid 3-O-glucosyltransferase from Fragaria · ananassa (FaGT1), the product ratio shifted to cyanidin 3-O-glucoside (60%), cyanidin (14%) and dimeric oxidized (+)-catechin (26%) at an overall equivalent rate of conversion. The data appear to identify (+)-catechin as another substrate of ANS in vivo and shed new light on the mechanism of its catalysis. Moreover, the enzymatic dimerization of catechin monomers is reported for the first time suggesting a role for ANS beyond the oxidation of leucocyanidins.

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“…In maize, 3‐deoxyanthocyanins can occur in various tissues, most obviously in the flower silks, and the related tannin‐like 3‐deoxyflavonoid phlobaphenes are also produced (Styles and Ceska 1975, 1977). The production by sorghum and sugarcane of 3‐deoxyanthocyanidins and 3‐deoxyanthocyanins as phytoalexins in response to fungal pathogens has received much interest (Chopra et al 1999, 2002, Godshall and Lonergan 1987, Hipskind et al 1990, 1996, Lo and Nicholson 1998, Lo et al 1999, 2002, Viswanathan et al 1996a, b). In the Gesneriaceae, the 3‐deoxyanthocyanins provide bright red or orange‐red colours to flowers of some of the Gesnerioideae subfamily, which occurs principally in the New World (Bohm 1998, Harborne 1966, 1967).…”

Section: Introductionmentioning

confidence: 99%

Investigation of the biosynthesis of 3‐deoxyanthocyanins in Sinningia cardinalis

Winefield

Lewis

Swinny

et al. 2005

Physiologia Plantarum

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3‐Deoxyanthocyanins provide bright orange‐red colours to flowers of some members of the Gesneriaceae, including sinningia (Sinningia cardinalis). We examined 3‐deoxyanthocyanin biosynthesis in sinningia, in particular, the expression of key flavonoid biosynthetic genes and the activities of the encoded proteins. Two abundant 3‐deoxyanthocyanins, luteolinidin 5‐O‐glucoside and apigeninidin 5‐O‐glucoside, three flavone glycosides, luteolin 7‐O‐glucoside, luteolin 7‐O‐glucuronide and apigenin 7‐O‐glucuronide, and the cinnamic acid verbascoside were identified in sinningia petal tissue. Small amounts of a 3‐hydroxyanthocyanin were also detected in a limited region of the petal. cDNA clones for three flavonoid enzymes, flavanone 3‐hydroxylase (F3H), dihydroflavonol 4‐reductase/flavanone 4‐reductase (DFR/FNR) and anthocyanidin synthase (ANS), were isolated from a sinningia cDNA library made from petal RNA and used to measure transcript abundance during petal development. Only very low levels of F3H transcript were detected, while DFR/FNR transcript was highly abundant. ANS transcript levels were intermediate between these two. The F3H cDNA was shown to encode a functional F3H protein by complementation of the phenotype of an Antirrhinum majus F3H mutant. The recombinant DFR/FNR had activity against both flavanone and dihydroflavonol substrates to a comparable extent. The results suggest a mechanism of 3‐deoxyflavonoid biosynthesis in sinningia similar to that reported for Zea mays, in which lack of F3H activity allows action of the DFR/FNR on flavanone substrates and production of flavan‐4‐ols. These are then likely converted to 3‐deoxyanthocyanins through the action of the ANS and subsequent glucosylation.

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Excision of the Candystripe1 transposon from a hyper-mutable Y1-cs allele shows that the sorghumY1 gene controls the biosynthesis of both 3-deoxyanthocyanidin phytoalexins and phlobaphene pigments

Cited by 26 publications

References 41 publications

Expression of flavonoid 3’-hydroxylase is controlled by P1, the regulator of 3-deoxyflavonoid biosynthesis in maize

Expression of flavonoid 3’-hydroxylase is controlled by P1, the regulator of 3-deoxyflavonoid biosynthesis in maize

Anthocyanidin synthase from Gerbera hybrida catalyzes the conversion of (+)‐catechin to cyanidin and a novel procyanidin

Investigation of the biosynthesis of 3‐deoxyanthocyanins in Sinningia cardinalis

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