Differential induction of chalcone synthase mRNA activity at the onset of phytoalexin accumulation in compatible and incompatible plant-pathogen interactions

Bell, John; Dixon, Richard A.; Bailey, J. A.; Rowell, P.M.; Lamb, Chris

doi:10.1073/pnas.81.11.3384

Cited by 81 publications

(43 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…DNA was isolated from tobacco leaves by the cetyltrimethylammonium bromide procedure (13). RNA was extracted by phenol extraction and isolated as described (14). Blot hybridizations and other standard manipulations were as described by Sambrook et al (15).…”

Section: Materials and Methods Pal2 Expressionmentioning

confidence: 99%

Abnormal plant development and down-regulation of phenylpropanoid biosynthesis in transgenic tobacco containing a heterologous phenylalanine ammonia-lyase gene.

Elkind

Edwards

Mavandad

et al. 1990

Proc. Natl. Acad. Sci. U.S.A.

296

187

View full text Add to dashboard Cite

Biosynthesis of phenylpropanoid natural products in tobacco was perturbed by introduction of a heterologous (bean) phenylalanine ammonia-lyase (PAL; L-phenylalanine ammonia-lyase, EC 4.3.1.5) gene, modified by inclusion of cauliflower mosaic virus 35S enhancer sequences in its promoter. These transgenic plants can exhibit a series of unusual phenotypes including localized fluorescent lesions, altered leaf shape and texture, reduced lignification in xylem, stunted growth, reduced pollen viability, and altered flower morphology and pigmentation. Genetic analysis of a transformant with severe symptoms showed that symptom development was inherited as a single, partially dominant trait and cosegregated with reduced levels of PAL activity and soluble phenylpropanoid products. Accumulation of transcripts encoded by the endogenous tobacco PAL genes was suppressed. We conclude that the transgene disrupts PAL regulation and that some of the phenotypes reflect interference with putative signals dependent on phenylpropanoid biosynthesis.Phenylalanine ammonia-lyase (PAL; L-phenylalanine ammonia-lyase, EC 4.3.1.5) catalyzes the first step in the synthesis of a diverse array of plant natural products based on the phenylpropane skeleton (1). PAL activity is highly regulated during development associated with the synthesis of flavonoid pigments and during xylogenesis with the cell wall polymer lignin and by environmental cues for the synthesis of these and other protective compounds (2). Distinct isoforms of the PAL enzyme subunit are encoded by a small family of differentially regulated genes (3-6). Transgenic plants containing the reporter gene p-glucuronidase under the control of the bean PAL2 promoter show tissue-and cell-type-specific expression associated with xylem differentiation during vascular development, in pigmented regions of petals, in root hairs, and in root and shoot meristems (7,8). Moreover, in stems the PAL2 promoter is activated in epidermal and subepidermal layers by illumination of dark-adapted plants and in the epidermis and perivascular parenchyma in response to wounding (7). Nuclear run-off transcription experiments have shown that the activation of PAL transcription by environmental stimuli is characteristically rapid but transient (9).These data indicate that PAL transcription is a major control site regulating the induction of PAL activity and initiation of phenylpropanoid biosynthesis in response to developmental and environmental cues. In the present paper, we have used a gene transfer approach to perturb this key step of phenylpropanoid biosynthesis. MATERIALS AND METHODS PAL2 ExpressionVectors. An expression cassette pYE1, consisting of a cauliflower mosaic virus 35S enhancer element and nopaline synthase 3' flanking sequences was constructed from pBI221 (10) cut with EcoRV and Sac I and ligated to the Sal I (filled-in with Klenow)/Sac I fragment of the pUC19 polylinker. The 5.3-kilobase (kb) PAL2 gene (4) including 1170 base pairs (bp) of 5' flanking sequence was used to generate two exo...

show abstract

Section: Materials and Methods Pal2 Expressionmentioning

confidence: 99%

Abnormal plant development and down-regulation of phenylpropanoid biosynthesis in transgenic tobacco containing a heterologous phenylalanine ammonia-lyase gene.

Elkind

Edwards

Mavandad

et al. 1990

Proc. Natl. Acad. Sci. U.S.A.

296

187

View full text Add to dashboard Cite

show abstract

“…7A). Flavonoid phytoalexins have frequently been proposed to participate in plant response to pathogen attack and the corresponding enzymes involved are induced by pathogens (Bell et al, 1984;Lawton and Lamb, 1987;García-Ponce and Rocha-Sosa, 2000). We infected PvACCaseTGUS plants with P. syringae pv tomato/AvrRpm1 (Pst), a pathogen known to establish an incompatible interaction with Arabidopsis.…”

Section: Stress Activationmentioning

confidence: 99%

Hormonal and Stress Induction of the Gene Encoding Common Bean Acetyl-Coenzyme A Carboxylase

2006

View full text Add to dashboard Cite

Regulation of the cytosolic acetyl-coenzyme A carboxylase (ACCase) gene promoter from common bean (Phaseolus vulgaris) was studied in transgenic Arabidopsis (Arabidopsis thaliana) plants using a β-glucuronidase (GUS) reporter gene fusion (PvACCase∷GUS). Under normal growth conditions, GUS was expressed in hydathodes, stipules, trichome bases, flowers, pollen, and embryos. In roots, expression was observed in the tip, elongation zone, hypocotyl-root transition zone, and lateral root primordia. The PvACCase promoter was induced by wounding, Pseudomonas syringae infection, hydrogen peroxide, jasmonic acid (JA), ethylene, or auxin treatment. Analysis of PvACCase∷GUS expression in JA and ethylene mutants (coronatine insensitive1-1 [coi1-1], ethylene resistant1-1 [etr1-1], coi1-1/etr1-1) suggests that neither JA nor ethylene perception participates in the activation of this gene in response to wounding, although each of these independent signaling pathways is sufficient for pathogen or hydrogen peroxide-induced PvACCase gene expression. We propose a model involving different pathways of PvACCase gene activation in response to stress.

show abstract

“…For this reason, many of the enzymes screened in Table1 were also assayed in control and infected bean hypocotyls ( Table 2). The infected hypocotyls were harvested at a time previously determined as giving elevated levels of chalcone synthase activity during phytoalexin accumulation and mature lesion formation in a compatible interaction [17]. A comparison of the basal enzyme activities in control cell cultures and hypocotyls indicates that most activities were within the same order of magnitude in the two systems.…”

Section: Time Lhlmentioning

confidence: 99%

“…Kievitsboon koekok were germinated and hypocotyls excised and infected with spore suspensions of C. lindemuthianum race y as described [17]. Parallel control hypocotyls were incubated with droplets of sterile distilled H 2 0 in place of the spore suspensions.…”

Section: Injected Bean Hypocotylsmentioning

confidence: 99%

“…Acetyl-CoA carboxylase (EC 6.4.1.2); ATP citrate (pro-3S)-lyase (EC 4.1.3.8); caffeic acid 0-methyltransferase or luteolin methyltransferase (EC 2.1.3.42); chalcone isomerase (EC 5.5.1.6); chalcone synthase (previous name flavanone synthase); cinnamic acid 4-hydroxylase or trans-cinnamate 4-monooxygenase (EC 1.14.1 3.1 1); endo-I,3-~-~-glucanase (EC 3.2.1.39); glucose-6-phosphate dehydrogenase (EC 1.1.1.49); P-D-glucosidase (EC 3.2.1.21); glutamate dehydrogenase (NADP') (EC 1.4.1.4); glutamate synthase (NADH) (EC 1.4.1.14); glutamine synthetase (EC 6.3.1.2); 4-hydroxycinnamic acid -CoA ligase or 4-coumaryl-CoA synthetase (EC 6.2.1.1 2); 4-hydroxycinnamic acid 3-monooxygenase (EC 1.14. 17.2); a-D-mannosidase (EC 3.2.1.24); peroxidase (EC 1.11.1.7); L-phenylalanine ammonia-lyase (EC 4.3.1.5); phospho-2-keto-3-deoxy-heptonate aldolase (EC 4.1.2.1 5); proline 2-oxoglutarate 5-dioxygenase (EC 1.14.1 1.2); shikimate dehydrogenase (EC 1 .I. 1.25).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Metabolic changes in elicitor-treated bean cells. Selectivity of enzyme induction in relation to phytoalexin accumulation

1985

Self Cite

View full text Add to dashboard Cite

1. Treatment of cell suspension cultures of Phaseolus vulgaris C.V. Immuna with an elicitor preparation heatreleased from the cell walls of the phytopathogenic fungus Colletotrichum lindemuthianum resulted in rapid accumulation of the prenylated 5-hydroxyisoflavanone phytoalexin kievitone followed by later accumulation of the pterocarpan-derived phytoalexin phaseollin. Kievitone formation was preceded by rapid transient increases in the extractable activities of the enzymes L-phenylalanine ammonia-lyase and chalcone synthase.2. The extractable activites of 15 enzymes were measured in the cell cultures during the period of kievitone accumulation. The results suggest a highly selective induction of enzymes associated directly with the phytoalexin pathway. No induction of enzymes of pathways diverging from or providing Substrates for the phenylpropanoid + isoflavonoid pathway was observed. The increase in glutamate dehydrogenase activity in control cultures was prevented by elicitor application.3. A comparison of enzyme activities in control and Colletotrichum-infected bean hypocotyls provided further evidence of the selective induction of enzymes of phytoalexin synthesis, although peroxidase, glutamate dehydrogenase and glutamate synthase activities were higher in infected than in healthy hypocotyls.4. It is concluded that the major enzymic changes occurring in elicitor-treated bean cells are probably those directly associated with defence mechanisms such as the formation of isoflavonoid phytoalexins (this paper) or accumulation of phenolic compounds and hydroxyproline-protein in the cell walls [Bolwell, G. P. et al. (1985) Eur. J. Biochem. 148, 571 -5781.Previous studies have shown that the accumulation of isoflavonoid phytoalexins (host synthesised, antimicrobial compounds) in bean cell suspension cultures treated with elicitor from the cell walls of the phytopathogenic fungus Colletotrichum lindemuthianum is preceded by increased extractable activities and rates of synthesis of key biosynthetic enzymes of the phenylpropanoid pathway and flavonoid branch pathway leading to phytoalexins [l -31. Similar enzyme changes are associated with the phytoalexin response in soybean [4]. However, with the exceptions of the characterisation of a 3-9,dihydroxypterocarpan 6a-hydroxylase and the penultimate enzyme in the biosynthesis of the glyceollins in Correspondence to R. A. Dixon,

show abstract

Differential induction of chalcone synthase mRNA activity at the onset of phytoalexin accumulation in compatible and incompatible plant-pathogen interactions

Cited by 81 publications

References 26 publications

Abnormal plant development and down-regulation of phenylpropanoid biosynthesis in transgenic tobacco containing a heterologous phenylalanine ammonia-lyase gene.

Abnormal plant development and down-regulation of phenylpropanoid biosynthesis in transgenic tobacco containing a heterologous phenylalanine ammonia-lyase gene.

Hormonal and Stress Induction of the Gene Encoding Common Bean Acetyl-Coenzyme A Carboxylase

Metabolic changes in elicitor-treated bean cells. Selectivity of enzyme induction in relation to phytoalexin accumulation

Contact Info

Product

Resources

About