Phenylalanine ammonia-lyase genes

Xiang L, BS Moore (2002) Inactivation, complementation, and heterologous expression of encP, a novel bacterial phenylalanine ammonia-lyase gene. J Biol Chem 277 32505-32509. 

Cramer CL, Edwards K, Dron M, Liang X, Dildine SL, Bolwell GP, Dixon R, Lamb CJ, Schuch W (1989) Phenylalanine ammonia lyase gene organization and structure. Plant Mol Biol 12 367-383... 

Cochrane FC, Davin LB, Lewis NG (2004) The arabidopsis phenylalanine ammonia lyase gene family kinetic characterization of the four PAL isoforms. Phytochemistry 65(11) 1557-1564... 

Cramer, C.L., Edwards, K., Dron, M., Liang, X., Dildine, S.L., Bolwell, G.P., Dixon, R.A., Lamb, C.J. Schuch, W. (1989). Phenylalanine ammonia-lyase gene organisation and structure. Plant Molecular Biology 12, 367-84. 

Lois, R., Dietrich, A., Hahlbrock, K. Schulz, W. (1989). A phenylalanine ammonia-lyase gene from parsley structure, regulation and identification of elicitor and light-responsive ds-acting elements. The EMBO Journal 8, 1641-8. 

Wanner, L.A., Li, G., Ware, D., Somssich, l.E. and Davis, K.R. (1995) The phenylalanine ammonia-lyase gene familiy in Arabidopsis thaliana. Plant Mol. Biol., 27, 327-38. 

Modes of expression and common structural features of the complete phenylalanine ammonia-lyase gene family in parsley. Proc. Natl. Acad. Sci. USA 92, 5905-5909. 

KAO, Y.Y., HARDING, S.A., TSAI, C.J., Differential expression of two distinct phenylalanine ammonia-lyase genes in condensed tannin-accumulating and lignifying cells of quaking aspen. Plant Physiol, 2002,130, 796-807. 

Jiang, Y., et al., Molecular and analysis of a phenylalanine ammonia -lyase gene (LrPAL2) from Lycoris radiata. Mol Biol Rep., 2013. 40(3) p. 2293-300. 

Takeda, J., Ozeki, Y, and Yoshida, K., Action spectrum for induction of promoter activity of phenylalanine ammonia-lyase gene by UV in carrot suspension cells, Photochem. Photohiol, 66, 464-470, 1999. 

Minami, E.I., Ozeki, Y., Matsuoka, M., Koizuka, N. Tanaka, Y. (1989) Structure and some characterisation of the gene for phenylalanine ammonia-lyase from rice plants. European Journal of Biochemistry 185, 19-25. 

The enc cluster contains four genes (encH, encl, encJ, encP) involved in the biosynthesis of the unusual benzoyl-CoA (185) starter from phenylalanine (186) via a plant-like p-oxidation mechanism (Fig. 32) [208-210]. This pathway is initiated by the unique phenylalanine ammonia-lyase EncP [211], which catalyzes the generation of cinnamic acid (187) from 186. The cinnamate-CoA ligase EncH... 

Fig. 1. Simplified diagram of the phenylpropanoid and flavonoid biosynthetic pathways. Enzymes that catalyze the reactions are placed on the left-hand side, and transcription factors on the right-hand side of the arrows. Both transcription factors for which their control over the enzymatic steps has been genetically proven, as well as transcription factors that have been shown to interact with promoters of the structural genes, are shown. PAL Phenylalanine ammonia lyase C4H cinnamate 4-hydroxylase 4CL 4-coumaroyl-coenzyme A ligase CHS chalcone synthase CHI chalcone-flavanone isomerase F3H flavanone 3(3-hydroxylase DFR dihydroflavonol 4-reductase AS anthocyanin synthase UFGT UDP glucose-flavonol glucosyl transferase RT anthocyanin rhamnosyl transferase...

Ellcitors have been widely used in studies of defense gene activation (for reviews see 3,58). Since It Is simpler to treat plant cells with ellcitors, as opposed to Intact pathogens, results are not compromised by other components of the pathogen. There has been the tendency, however, to assume that If a substance causes induction of early defense genes such as phenylalanine ammonia lyase, then It Is necessarily a phytoalexin ellcitor. Ebel et a1. (M) showed, however, that some substances which activate early defense genes do not lead to phytoalexin accumulation. Therefore, ellcitors should be carefully checked to ensure that they In fact activate phytoalexin pathways. 

Keywords chemotaxonomy patchy distribution biosynthesis genes horizontal gene transfer endophytes evolution tryptophan decarboxylase tyrosine decarboxylase phenylalanine ammonia-lyase chalcone synthase strictosidine synthase berberine bridge enzyme codeine reductase... 

In the phenylpropanoid pathway, the first biosynthetic step leading to SA is a deamination of phenylalanine to CA which is catalyzed by phenylalanine ammonia lyase (PAL). This enzyme is induced by a range of biotic and abiotic stress conditions and is a key regulator in the phenylpropanoid pathway, which yields a variety of phenolics among others involved in structural and defense-related functions [42]. In recent years, PAL and its corresponding genes have been subject of numerous studies in various plant species [43 7]. 

The importance of SA in the activation of resistance was further underscored by the demonstration that otherwise resistant Arabidopsis plants become susceptible to Peronospora parasitica when phenylalanine ammonia lyase (PAL) activity is specifically inhibited by 2-aminoindan-2-phosphonic acid [77]. Since PAL catalyzes the first step in the SA biosynthetic pathway and resistance was restored in these PAL-suppressed plants by exogenous application of SA, increased susceptibility is presumably caused by a block in SA synthesis. Likewise, tobacco plants exhibiting epigenetic suppression of PAL gene expression due to cosuppression do not develop SAR in response to TMV infection [78]. In addition, these plants fail to systemically express the PR-la gene after TMV infection. 

The phenolic compound content of the Cucurbitaceae is very low. Only trace amounts (3mg/ kg f w.) of neochlorogenic acid (3 -caffeoylquinic acid) were detected in one out of three zucchini (summer-squash) cultivars [40]. In an extensive study on the phenolic content of melons, watermelon, etc., only traces (ferulic acid were detected after hydrolysis. Very small antioxidant activity was reported for cucumber extracts [61], consistent with the very small phenolic compound content. However, the phenolic metabolism of melons is activated under environmental stress and wounding induces the phenylalanine ammonia lyase (PAL) gene [62]. 

ZHU, Q., DABI, T., BEECHE, A., YAMAMOTO, R., LAWTON, M.A., LAMB, C., Cloning and projrerties of a rice gene encoding phenylalanine ammonia-lyase, Plant Mol. Biol., 1995, 29,535-550. 

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