The biosynthesis of phytoalexins in Dianthus caryophyllus L. Cell cultures: Induction of benzoyl-CoA:Anthranilate N-benzoyltransferase activity

Reinhard, Klaus; Matern, Ulrich

doi:10.1016/0003-9861(89)90376-7

Cited by 39 publications

(13 citation statements)

References 23 publications

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“…It is interesting that the conversion of cinnamoyl-CoA to benzoyl-CoA has already been shown to occur in mammals (Mao et al, 1994). In addition, benzoyl-CoA is an intermediate in the synthesis of dianthramide phytoalexins in elicited cells of Dianthus caryophillus (Reinhard and Matern, 1989). This benzoyl-CoA thioester could represent in tobacco the immediate precursor of salicyloyl-CoA, which in turn could be converted to SA by thioesterases (Fig.…”

Section: Discussionmentioning

confidence: 99%

Free and Conjugated Benzoic Acid in Tobacco Plants and Cell Cultures. Induced Accumulation upon Elicitation of Defense Responses and Role as Salicylic Acid Precursors

et al. 2001

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Salicylic acid (SA) is a key endogenous component of local and systemic disease resistance in plants. In this study, we investigated the role of benzoic acid (BA) as precursor of SA biosynthesis in tobacco (Nicotiana tabacum cv Samsun NN) plants undergoing a hypersensitive response following infection with tobacco mosaic virus or in tobacco cell suspensions elicited with β-megaspermin, an elicitor from Phytophthora megasperma. We found a small pool of conjugated BA in healthy leaves and untreated cell suspensions of tobacco, whereas free BA levels were barely detectable. Infection of plants with tobacco mosaic virus or elicitation of cells led to a rapid de novo synthesis and accumulation of conjugated BA, whereas free BA was weakly induced. In presence of diphenylene iodonium, an inhibitor of superoxide anion formation, SA accumulation was abolished in elicited cells and much higher BA levels were concomitantly induced, mainly as a conjugated form. Furthermore, piperonylic acid, an inhibitor of cinnamate-4-hydroxylase was used as a powerful tool to redirect the metabolic flow from the main phenylpropanoid pathway into the SA biosynthetic branch. Under these conditions, in vivo labeling and radioisotope dilution experiments with [14C]trans-cinnamic acid as precursor clearly indicated that the free form of BA produced in elicited tobacco cells is not the major precursor of SA biosynthesis. The main conjugated form of BA accumulating after elicitation of tobacco cells was identified for the first time as benzoyl-glucose. Our data point to the likely role of conjugated forms of BA in SA biosynthesis.

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Section: Discussionmentioning

confidence: 99%

Free and Conjugated Benzoic Acid in Tobacco Plants and Cell Cultures. Induced Accumulation upon Elicitation of Defense Responses and Role as Salicylic Acid Precursors

et al. 2001

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Section: Atmyb15mentioning

confidence: 99%

“…It has been reported that genes encoding the key enzymes of lignin synthesis, such as phenylalanine ammonia lyase (PAL), are induced by wounding at the transcriptional level (Ohl et al 1990). It has also been observed that genes involved in the biosynthesis of phytoalexins are activated by fungal elicitor in carnation (Reinhard and Matern 1989).The shikimate pathway, especially the first (3-deoxy-Darabino-heptulosonate 7-phosphase synthase (DAHPS)) and penultimate (5-enopyruvylshikimate-3-phosphase synthase (EPSPS)) enzymes, has been studied extensively in plants. Some genes encoding enzymes involved in the shikimate pathway have been isolated from various plant species, many of which exhibited tissue-specific and environmental stimuli-induced expression patterns (Gorlach et al 1994;Bischoff et al 1996).…”

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Overexpression of the Wounding‐Responsive Gene AtMYB15 Activates the Shikimate Pathway in Arabidopsis

Chen

Zhang

et al. 2006

JIPB

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The MYB transcription factor genes play important roles in many developmental processes and various defense responses of plants. The shikimate pathway is a major biosynthetic pathway for the production of three aromatic amino acids and other aromatic compounds that are involved in multiple responses of plants, including protection against UV and defense. Herein, we describe the characterization of the R2R3-MYB gene AtMYB15 as an activator of the shikimate pathway in Arabidopsis. The AtMYB15 protein is nuclear localized and a transcriptional activation domain is found in its C-terminal portion. Northern blots showed that AtMYB15 is an early wounding-inducible gene. Resutls of microarray analysis, confirmed using quantitative real-time polymerase chain reaction, showed that overexpression of AtMYB15 in transgenic plants resulted in elevated expression of almost all the genes involved in the shikimate pathway. Bioinformatics analysis showed that one or more AtMYB15-binding AC elements were detected in the promoters of these upregulated genes. Furthermore, these genes in the shikimate pathway were also found to be induced by wounding. These data suggest an important role of AtMYB15 as a possible direct regulator of the Arabidopsis shikimate pathway in response to wounding. www.blackwell-synergy.com; www.jipb.netThe shikimate pathway, which is present only in bacteria, fungi, yeasts, plants, and some apicomplexan parasites and not in animals, is a common route for the biosynthesis of the three aromatic amino acids phenylalanine, tyrosine, and tryptophan (Herrmann 1995;Roberts et al. 1998;Herrmann and Weaver 1999). This pathway occurs in the cytosol in bacteria and fungi, whereas in plants it operates in plastids (Herrmann and Weaver 1999). The pathway starts with phosphoenolpyruvate and erythrose 4-phosphate, which are eventually converted to chorismate over a series of seven enzymatic steps (Herrmann and Weaver 1999). In bacteria, almost all the aromatic amino acids for protein biosynthesis are synthesized through the shikimate pathway. However, in plants, the products of the shikimate pathway have dual functions not only as building blocks of protein synthesis, but also as the precursors of a variety of secondary metabolites, such as lignins (Ehlting et al. 2005), indolic acetic acid (Ljung et al. 2002), alkaloids (van der Fits and Memelink 2000), and phytoalexins (Kuc and Rush 1985). These compounds, the biosynthesis of which is regulated developmentally and environmentally (Gasser et al. 1988;Keith et al. 1991;Gorlach et al. 1995aGorlach et al. , 1995b, play important roles in growth control, physical support, electron transport, and defense responses.Plants respond to wounding by increasing the production of compounds involved in the healing of wound damage and defense against microbial invasion. It has been reported that, AtMYB15Regulates Shikimate Pathway 1085 when mechanically wounded or attacked by insects, plants require more chorismates to synthesize aromatic secondary metabolites (Dyer et al. 198...

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“…An unspecific OMT activity has been reported in carnation tissues [4], but the results of these previous investigations only concerned a ‘crude’ enzymatic activity. As we have here reported the isolation of a new strictly specific F 4′‐OMT from carnation tissues, it is likely that this enzyme could represent only one of the many different OMTs present in the tissues of this ornamental.…”

Section: Discussionmentioning

confidence: 99%

“…As far as we know, OMT activity in carnation ( Dianthus caryophyllus L) has not been investigated thoroughly yet. Reinhard and Matern [4] found in carnation an OMT activity related to the tissue defensive response towards Phytophthora megasperma. This enzymatic activity plays a fundamental role in the biosynthesis of methylated dianthramide‐derivatives, the carnation phytoalexins.…”

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confidence: 99%

Purification and properties of a new S‐adenosyl‐l‐ methionine:flavonoid 4′‐O‐methyltransferase from carnation (Dianthus caryophyllus L.)

Curir

Lanzotti

Dolci

et al. 2003

European Journal of Biochemistry

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A new enzyme, S-adenosyl-L-methionine:flavonoid 4¢-Omethyltransferase (EC 2.1.1.-) (F 4¢-OMT), has been purified 1 399-fold from the tissues of carnation (Dianthus caryophyllus L). The enzyme, with a molecular mass of 43-45 kDa and a pI of 4.15, specifically methylates the hydroxy substituent in 4¢-position of the flavones, flavanones and isoflavones in the presence of S-adenosyl-L-methionine. A high affinity for the flavone kaempferol was observed), while other 4¢-hydroxylated flavonoids proved likewise to be suitable substrates. Enzyme activity had no apparent Mg + + requirement but was inhibited by SH-group reagents. The optimum pH value for F 4¢-OMT activity was found to be around neutrality. Kinetic analysis of the enzyme bi-substrate reaction indicates a Ping-Pong mechanism and excludes the formation of a ternary complex. The F 4¢-OMT activity was increased, in both in vitro and in vivo carnation tissues, by the inoculation with Fusarium oxysporum f. sp. dianthi. The enzyme did not display activity towards hydroxycinnamic acid derivatives, some of which are involved, as methylated monolignols, in lignin biosynthesis; the role of this enzyme could be therefore mainly defensive, rather than structural, although its precise function still needs to be ascertained.

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The biosynthesis of phytoalexins in Dianthus caryophyllus L. Cell cultures: Induction of benzoyl-CoA:Anthranilate N-benzoyltransferase activity

Cited by 39 publications

References 23 publications

Free and Conjugated Benzoic Acid in Tobacco Plants and Cell Cultures. Induced Accumulation upon Elicitation of Defense Responses and Role as Salicylic Acid Precursors

Free and Conjugated Benzoic Acid in Tobacco Plants and Cell Cultures. Induced Accumulation upon Elicitation of Defense Responses and Role as Salicylic Acid Precursors

Overexpression of the Wounding‐Responsive Gene AtMYB15 Activates the Shikimate Pathway in Arabidopsis

Purification and properties of a new S‐adenosyl‐l‐ methionine:flavonoid 4′‐O‐methyltransferase from carnation (Dianthus caryophyllus L.)

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