Characterization and Expression of Caffeoyl-Coenzyme A 3-O-Methyltransferase Proposed for the Induced Resistance Response of Vitis vinifera L

Busam, G.; Junghanns, Kay T; Kneusel, Richard E.; Kassemeyer, Hanns-Heinz; Matern, Ulrich

doi:10.1104/pp.115.3.1039

Cited by 73 publications

(36 citation statements)

References 46 publications

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“…This strongly suggests that the PFOMT may indeed be involved in the methylation of these compounds. Similar responses to biotic or abiotic stresses have been observed on the transcript level for several other CCoAOMT-like genes (36,44,46,47).…”

Section: Substrate Specificities Of Other Ccoaomt-like Proteins-supporting

confidence: 50%

A Novel Mg2+-dependent O-Methyltransferase in the Phenylpropanoid Metabolism of Mesembryanthemum crystallinum

Ibdah

Zhang

Schmidt

et al. 2003

Journal of Biological Chemistry

114

149

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Upon irradiation with elevated light intensities, the ice plant (Mesembryanthemum crystallinum) accumulates a complex pattern of methylated and glycosylated flavonol conjugates in the upper epidermal layer. Identification of a flavonol methylating activity, partial purification of the enzyme, and sequencing of the corresponding peptide fragments revealed a novel S-adenosyl-L-methionine-dependent O-methyltransferase that was specific for flavonoids and caffeoyl-CoA. Cloning and functional expression of the corresponding cDNA verified that the new methyltransferase is a multifunctional 26.6-kDa Mg 2؉ -dependent enzyme, which shows a significant sequence similarity to the cluster of caffeoyl coenzyme A-methylating enzymes. Functional analysis of highly homologous members from chickweed (Stellaria longipes), Arabidopsis thaliana, and tobacco (Nicotiana tabacum) demonstrated that the enzymes from the ice plant, chickweed, and A. thaliana possess a broader substrate specificity toward o-hydroquinone-like structures than previously anticipated for Mg 2؉ -dependent O-methyltransferases, and are distinctly different from the tobacco enzyme. Besides caffeoyl-CoA and flavonols, a high specificity was also observed for caffeoylglucose, a compound never before reported to be methylated by any plant O-methyltransferase. Based on phylogenetic analysis of the amino acid sequence and differences in acceptor specificities among both animal and plant Omethyltransferases, we propose that the enzymes from the Centrospermae, along with the predicted gene product from A. thaliana, form a novel subclass within the caffeoyl coenzyme A-dependent O-methyltransferases, with potential divergent functions not restricted to lignin monomer biosynthesis.Methylation by S-adenosyl-L-methionine (AdoMet) 1 dependent O-methyltransferases (OMTs) (EC 2.1.1) is a common modification in natural product biosynthesis. Site-specific O-methylation modulates the physiological properties of such compounds and reduces the chemical reactivity of phenolic hydroxyl groups (1). In plants, O-methylation is also required for monolignol biosynthesis and accounts for the structural differences and properties of lignin, which next to cellulose is the most prominent polymer on earth (2).Plant OMTs can be categorized into two major classes (3). Class I includes a group of low molecular weight (23,000 to 27,000) and Mg 2ϩ -dependent OMTs, whereas class II consists of higher molecular weight OMTs of about 38,000 to 43,000 that do not require Mg 2ϩ for catalytic activity. Prominent class II members include caffeic acid, flavonoid, coumarin, and alkaloid OMTs (4 -6). Within the class I OMTs, a group of small caffeoyl coenzyme A OMTs (CCoAOMTs) have been suggested to be key enzymes in the biosynthesis of monolignols, the precursors of gymnosperm and angiosperm lignins (7,8). In angiosperms, this task may also be performed by class II OMTs that are specific for caffeic acid, caffeyl aldehyde, or caffeyl alcohol (COMT) (9 -11). This apparent redundancy results in a cell-and tis...

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Section: Substrate Specificities Of Other Ccoaomt-like Proteins-supporting

confidence: 50%

A Novel Mg2+-dependent O-Methyltransferase in the Phenylpropanoid Metabolism of Mesembryanthemum crystallinum

Ibdah

Zhang

Schmidt

et al. 2003

Journal of Biological Chemistry

114

149

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“…However, some type 2 OMTs are also active with flavonoids and/or phenylpropanoid conjugates (Ibdah et al, 2003;Kim et al, 2006;Lee et al, 2008). The candidate AOMT presented 56% and 54% identity with PFOMT from M. crystallinum (Ibdah et al, 2003) and caffeoylCoA-OMT (CCoA-OMT) from grapevine (Busam et al, 1997), respectively (Fig. 1A).…”

Section: Isolation Of a Candidate Aomt Cdna From Grapevinementioning

confidence: 99%

A Novel Cation-DependentO-Methyltransferase Involved in Anthocyanin Methylation in Grapevine

et al. 2009

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(C.V., E.M., V.C., A.A.)Anthocyanins are major pigments in colored grape (Vitis vinifera) berries, and most of them are monomethoxylated or dimethoxylated. We report here the functional characterization of an anthocyanin O-methyltransferase (AOMT) from grapevine. The expression pattern in two cultivars with different anthocyanin methylation profiles (Syrah and Nebbiolo) showed a peak at start ripening (véraison), when the concentrations of all methylated anthocyanins begin to increase. The purified recombinant AOMT protein was active on both anthocyanins and flavonols in vitro, with K m in the micromolar range, and was dependent on divalent cations for activity. AOMT showed a preference for 3#,5# methylation when a 3#,4#,5# hydroxylated anthocyanin substrate was tested. In order to assess its in planta activity, we performed transient expression of AOMT in tobacco (Nicotiana benthamiana) leaves expressing the Production of Anthocyanin Pigment1 (PAP1) transcription factor from Arabidopsis (Arabidopsis thaliana). PAP1 expression in leaves induced the accumulation of the nonmethylated anthocyanin delphinidin 3-rutinoside. The coexpression of PAP1 and AOMT resulted in an accumulation of malvidin 3-rutinoside. We also showed that AOMT localized exclusively in the cytoplasm of tobacco leaf cells. These results demonstrate the ability of this enzyme to methylate anthocyanins both in vitro and in vivo, indicating that AOMT plays a major role in anthocyanin biosynthesis in grape berries.

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“…Substrate affinity analysis has revealed that CCoAOMT shows higher methylation rate with caffeoyl-CoA than 5-hydroxyferuloyl-CoA (Ye et al, 1994;Busam et al, 1997;Martz et al, 1998;Zhong et al, 2000). CCoAOMT is reported to exist in a multigene family that can be grouped into class I and II (Raes et al, 2003).…”

Section: Sl Pang Et Almentioning

confidence: 99%

“…It has been reported that this gene is encoded by one to two members in parsley (Grimmig and Matern, 1997), grapevine (Busam et al, 1997), alfalfa (Inoue et al, 1998) and aspen (Meng and Campbell, 1998), five to ten members in zinnia (Ye et al, 1994), and seven members in Arabidopsis (Raes et al, 2003). There are three classes of CCoAOMT in tobacco, and it was suggested that each class plays a role at different stages of lignification (Maury et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Isolation and characterization of CCoAOMT in interspecific hybrid of Acacia auriculiformis x Acacia mangium - a key gene in lignin biosynthesis

Pang¹,

Ong²,

Lee³

et al. 2014

Genet. Mol. Res.

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ABSTRACT. This study was directed at the understanding of the function of CCoAOMT isolated from Acacia auriculiformis x Acacia mangium. Full length cDNA of the Acacia hybrid CCoAOMT (AhCCoAOMT) was 1024-bp long, containing 750-bp coding regions, with one major open reading frame of 249 amino acids. On the other hand, full length genomic sequence of the CCoAOMT (AhgflCCoAOMT) was 2548 bp long, containing three introns and four exons with a 5' untranslated region (5'UTR) of 391 bp in length. The 5'UTR of the characterized CCoAOMT gene contains various regulatory elements. Southern analysis revealed that the Acacia hybrid has more than three copies of the CCoAOMT gene. Real-time PCR showed that this gene was expressed in root, inner bark, leaf, flower and seed pod of the Acacia hybrid. Downregulation of the homologous CCoAOMT gene in tobacco by antisense (AS) and intron-containing hairpin (IHP) constructs containing partial AhCCoAOMT led to reduction in lignin content. Expression of the CCoAOMT in AS line (pART-HAS78-03) and IHP line (pART-HIHP78-06) was reduced respectively by 37 and 75% compared to the control, resulting in a decrease in the estimated lignin content by 24 and 56%, respectively. AhCCoAOMT was found to have altered not only S and G units but also total lignin content, which is of economic value to the pulp industry. Subsequent polymorphism analysis of this gene across eight different genetic backgrounds each of A. mangium and A. auriculiformis revealed 47 single nucleotide polymorphisms (SNPs) in A. auriculiformis CCoAOMT and 30 SNPs in A. mangium CCoAOMT.

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Characterization and Expression of Caffeoyl-Coenzyme A 3-O-Methyltransferase Proposed for the Induced Resistance Response of Vitis vinifera L

Cited by 73 publications

References 46 publications

A Novel Mg2+-dependent O-Methyltransferase in the Phenylpropanoid Metabolism of Mesembryanthemum crystallinum

A Novel Mg2+-dependent O-Methyltransferase in the Phenylpropanoid Metabolism of Mesembryanthemum crystallinum

A Novel Cation-DependentO-Methyltransferase Involved in Anthocyanin Methylation in Grapevine

Isolation and characterization of CCoAOMT in interspecific hybrid of Acacia auriculiformis x Acacia mangium - a key gene in lignin biosynthesis

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