CYP98A6 from Lithospermum erythrorhizon encodes 4‐coumaroyl‐4′‐hydroxyphenyllactic acid 3‐hydroxylase involved in rosmarinic acid biosynthesis1

Matsuno, Michiyo; Nagatsu, Akito; Ogihara, Yukio; Ellis, Brian E.; Mizukami, Hajime

doi:10.1016/s0014-5793(02)02368-2

Cited by 56 publications

(49 citation statements)

References 25 publications

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“…These enzymes catalyze the meta-hydroxylation of p-coumaric derivatives esterified to shikimate, quinate, or phenyllactate (Schoch et al, 2001;Matsuno et al, 2002). In Arabidopsis, CYP98A3 is required for the synthesis of lignin monomers and soluble sinapoyl esters (Franke et al, 2002a).…”

Section: Analysis Of Cyp98a3 Mutants Reveals the Existence Of An Altementioning

confidence: 99%

A coumaroyl-ester-3-hydroxylase Insertion Mutant Reveals the Existence of Nonredundant meta-Hydroxylation Pathways and Essential Roles for Phenolic Precursors in Cell Expansion and Plant Growth

et al. 2005

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Cytochromes P450 monooxygenases from the CYP98 family catalyze the meta-hydroxylation step in the phenylpropanoid biosynthetic pathway. The ref8 Arabidopsis (Arabidopsis thaliana) mutant, with a point mutation in the CYP98A3 gene, was previously described to show developmental defects, changes in lignin composition, and lack of soluble sinapoyl esters. We isolated a T-DNA insertion mutant in CYP98A3 and show that this mutation leads to a more drastic inhibition of plant development and inhibition of cell growth. Similar to the ref8 mutant, the insertion mutant has reduced lignin content, with stem lignin essentially made of p-hydroxyphenyl units and trace amounts of guaiacyl and syringyl units. However, its roots display an ectopic lignification and a substantial proportion of guaiacyl and syringyl units, suggesting the occurrence of an alternative CYP98A3-independent meta-hydroxylation mechanism active mainly in the roots. Relative to the control, mutant plantlets produce very low amounts of sinapoyl esters, but accumulate flavonol glycosides. Reduced cell growth seems correlated with alterations in the abundance of cell wall polysaccharides, in particular decrease in crystalline cellulose, and profound modifications in gene expression and homeostasis reminiscent of a stress response. CYP98A3 thus constitutes a critical bottleneck in the phenylpropanoid pathway and in the synthesis of compounds controlling plant development. CYP98A3 cosuppressed lines show a gradation of developmental defects and changes in lignin content (40% reduction) and structure (prominent frequency of p-hydroxyphenyl units), but content in foliar sinapoyl esters is similar to the control. The purple coloration of their leaves is correlated to the accumulation of sinapoylated anthocyanins.

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Section: Analysis Of Cyp98a3 Mutants Reveals the Existence Of An Altementioning

confidence: 99%

A coumaroyl-ester-3-hydroxylase Insertion Mutant Reveals the Existence of Nonredundant meta-Hydroxylation Pathways and Essential Roles for Phenolic Precursors in Cell Expansion and Plant Growth

et al. 2005

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“…In Lithospermum erythrorhizon a gene encoding a C3ЈH capable of hydroxylating p-coumaroyl-4-hydroxyphenyllactic acid has been isolated, although it has not been determined if shikimate or quinate p-coumaroyl esters are substrates for the enzyme (Matsuno et al 2002). In coVee, two C3ЈH enzymes have been identiWed, one of which utilizes both p-coumaroyl-shikimate and -quinate with similar eYciency and one of which can utilize p-coumaroylshikimate only (Mahesh et al 2007).…”

Section: Introductionmentioning

confidence: 99%

Red clover coumarate 3′-hydroxylase (CYP98A44) is capable of hydroxylating p-coumaroyl-shikimate but not p-coumaroyl-malate: implications for the biosynthesis of phaselic acid

Sullivan

Żarnowski

2009

Planta

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Red clover (Trifolium pratense) leaves accumulate several mumol of phaselic acid [2-O-caffeoyl-L-malate] per gram fresh weight. Post-harvest oxidation of such o-diphenols to o-quinones by endogenous polyphenol oxidases (PPO) prevents breakdown of forage protein during storage. Forages like alfalfa (Medicago sativa) lack both foliar PPO activity and o-diphenols. Consequently, breakdown of their protein upon harvest and storage results in economic losses and release of excess nitrogen into the environment. Understanding how red clover synthesizes o-diphenols such as phaselic acid will help in the development of forages utilizing this natural system of protein protection. We have proposed biosynthetic pathways in red clover for phaselic acid that involve a specific hydroxycinnamoyl-CoA:malate hydroxycinnamoyl transferase. It is unclear whether the transfer reaction to malate to form phaselic acid involves caffeic acid or p-coumaric acid and subsequent hydroxylation of the resulting p-coumaroyl-malate. The latter would require a coumarate 3'-hydroxylase (C3'H) capable of hydroxylating p-coumaroyl-malate, an activity not previously described. Here, a cytochrome P450 C3'H (CYP98A44) was identified and its gene cloned from red clover. CYP98A44 shares 96 and 79% amino acid identity with Medicago truncatula and Arabidopsis thaliana C3'H proteins that are capable of hydroxylating p-coumaroyl-shikimate and have been implicated in monolignol biosynthesis. CYP98A44 mRNA is expressed in stems and flowers and to a lesser extent in leaves. Immune serum raised against CYP98A44 recognizes a membrane-associated protein in red clover stems and leaves and cross-reacts with C3'H proteins from other species. CYP98A44 expressed in Saccharomyces cerevisiae is capable of hydroxylating p-coumaroyl-shikimate, but not p-coumaroyl-malate. This finding indicates that in red clover, phaselic acid is likely formed by transfer of a caffeoyl moiety to malic acid, although the existence of a second C3'H capable of hydroxylating p-coumaroyl-malate cannot be definitively ruled out.

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“…A cytochrome P450 (CYP98A6) cDNA clone coding for 3H was subsequently isolated from L. erythrorhizon and expression of the corresponding gene was shown to be drastically up-regulated by addition of YE or MJ to L. erythrorhizon cells (Matsuno et al 2002). In the present study we estimated these hydroxylation activities by measuring the rate of RA production from CHPL by microsome preparations in the presence of NADPH, an approach that reports the total activity of 3H and 3ЈH.…”

mentioning

confidence: 98%

Elicitor-induced rosmarinic acid biosynthesis in Lithospermum erythrorhizon cell suspension cultures: Activities of rosmarinic acid synthase and the final two cytochrome P450-catalyzed hydroxylations

Ogata

Tsuruga

Matsuno

et al. 2004

Plant Biotechnology

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A drastic increase in rosmarinic acid (RA) accumulation is induced in cultured cells of Lithospermum erythrorhizon after their exposure to yeast extract or methyl jasmonate. Addition of the elicitors to the cell cultures only slightly enhanced the activity of rosmarinic acid synthase, which catalyzes formation of 4-coumaroyl-4Ј-hydroxyphenyllactic acid (CHPL), the first reaction specific to RA biosynthesis. In contrast, the two-step cytochrome P450-catalyzed hydroxylations of CHPL to form RA were dramatically up-regulated by the elicitor treatments, indicating that these hydroxylation activities are likely to play a key regulatory role in elicitation of RA biosynthesis.

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CYP98A6 from Lithospermum erythrorhizon encodes 4‐coumaroyl‐4′‐hydroxyphenyllactic acid 3‐hydroxylase involved in rosmarinic acid biosynthesis¹

Cited by 56 publications

References 25 publications

A coumaroyl-ester-3-hydroxylase Insertion Mutant Reveals the Existence of Nonredundant meta-Hydroxylation Pathways and Essential Roles for Phenolic Precursors in Cell Expansion and Plant Growth

A coumaroyl-ester-3-hydroxylase Insertion Mutant Reveals the Existence of Nonredundant meta-Hydroxylation Pathways and Essential Roles for Phenolic Precursors in Cell Expansion and Plant Growth

Red clover coumarate 3′-hydroxylase (CYP98A44) is capable of hydroxylating p-coumaroyl-shikimate but not p-coumaroyl-malate: implications for the biosynthesis of phaselic acid

Elicitor-induced rosmarinic acid biosynthesis in Lithospermum erythrorhizon cell suspension cultures: Activities of rosmarinic acid synthase and the final two cytochrome P450-catalyzed hydroxylations

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