Characterization of the phenylalanine ammonia lyase gene from the rubber tree (Hevea brasiliensis Müll. Arg.) and differential response during Rigidoporus microporus infection
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Department of Plant Science, Faculty of Natural Resources, Prince of Songkla University, Hat Yai, Songkhla, 90112, Thailand
Center of Excellence on Agricultural Biotechnology (AG-BIO/PERDO-CHE), Bangkok, 10900, Thailand
Submission date: 2016-06-17
Acceptance date: 2016-10-28
Corresponding author
Korakot Nakkanong
Department of Plant Science, Faculty of Natural Resources, Prince of Songkla University, Hat Yai, Songkhla, 90112, Thailand
Journal of Plant Protection Research 2016;56(4):380-388
Phenylalanine ammonia lyase (PAL) is a specific branch point enzyme of primary and secondary metabolism. It plays a key role in plant development and defense mechanisms. Phenylalanine ammonia lyase from Hevea brasiliensis (HbPAL) presented a complete open reading frame (ORF) of 2,145 bp with 721 encoded amino acids. The sequence alignment indicated that the amino acid sequence of HbPAL shared a high identity with PA L genes found in other plants. Phylogenetic tree analysis indicated that HbPAL was more closely related to PALs in Manihot esculenta and Jatropha curcas than to those from other plants. Transcription pattern analysis indicated that HbPAL was constitutively expressed in all tissues examined, most highly in young leaves. The HbPAL gene was evaluated by quantitative real-time PCR (qRT-PCR) after infection with Rigidoporus microporus at 0, 12, 24, 48, 72 and 96 hours post inoculation. The expression patterns of the PA L gene differed among the three rubber clones used in the study. The transcription level of the white root rot disease tolerant clone, PB5/51 increased sharply during the latter stages of infection, while it was relatively subdued in the white root rot disease susceptible clones, RRIM600 and BPM24. These results suggest that the HbPAL gene may play a role in the molecular defense response of H. brasiliensis to pathogen attack and could be used as a selection criterion for disease tolerance.
The authors have declared that no conflict of interests exist.
Allwood E.G., Davies D.R., Gerrish C., Ellis B.E., Bolwell G.P. 1999. Phosphorylation of phenylalanine ammonia-lyase: evidence for a novel protein kinase and identification of the phosphorylated residue. FEBS Letters 457 (1): 47–52.
Appert C., Logemann E., Hahlbrock K., Schmid J., Amrhein N. 1994. Structural and catalytic properties of the four phenylalanine ammonia-lyase isoenzymes from parsley (Petroselinum crispum Nym.). European Journal of Biochemistry 225 (1): 491–499.
Araujo L., Bispo W.M.S., Rios V.S., Fernandes S.A., Rodrigues F.A. 2015. Induction of the phenylpropanoid pathway by acibenzolar-s-methyl and potassium phosphite increases mango resistance to Ceratocystis fimbriata infection. Plant Disease 99 (4): 447–459.
Bowles D.J. 1990. Defense-related proteins in higher plants. Annual Review of Biochemistry 59 (1): 873–907.
Cass C.L., Peraldi A., Dowd P.F., Mottiar Y., Santoro N., Karlen S.D., Bukhman Y.V., Foster C.E., Thrower N., Bruno L.C., Moskvin O.V., Johnson E.T., Willhoit M.E., Phutane M., Ralph J., Mansfield S.D., Nicholson P., Sedbrook J.C. 2015. Effects of phenylalanine ammonia lyase (PAL) knockdown on cell wall composition, biomass digestibility, and biotic and abiotic stress responses in Brachypodium. Journal of Experimental Botany 66 (14): 4317–4335.
Clarke J.D., Volko S.M., Ledford H., Ausubel F.M., Dong X. 2000. Roles of salicylic acid, jasmonic acid, and ethylene in cpr-induced resistance in Arabidopsis. The Plant Cell 12 (11): 2175–2190.
Fondevilla S., Kuster H., Krajinski F., Cubero J.I., Rubiales D. 2011. Identification of genes differentially expressed in a resistant reaction to Mycosphaerella pinodes in pea using microarray technology. BMC Genomics 12 (1): 28.
Frohman M.A., Dush M.K., Martin G.R. 1988. Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer. Proceeding of the National Academy of Sciences of the United States of America 85 (23): 8998–9002.
Gao J., Zhang S., Cai F., Zheng X.J., Lin N., Qin X., Ou Y., Gu X., Zhu X., Xu Y., Chen F. 2012. Characterization, and expression profile of a phenylalanine ammonia lyase gene from Jatropha curcas L. Molecular Biology Reports 39 (4): 3443–3452.
Jin Q., Yao Y., Cai Y.P., Lin Y. 2013. Molecular cloning and sequence analysis of a phenylalanine ammonialyase gene from Dendrobium. PLoS One 8 (4): e62352.
Joos H.J., Hahlbrock K. 1992. Phenylalanine ammonia-lyase in potato (Solanum tuberosum L.). Genomic complexity, structural comparison of two selected genes and modes of expression. European Journal of Biochemistry 204 (2): 621–629.
Kavousi H.R., Marashi H., Mozafari J., Bagheri A.R. 2009. Expression of phenylpropanoid pathway genes in chickpea defense against race 3 of Ascochyta rabiei. Plant Pathology Journal 8 (3): 127–132.
Kim D.S., Hwang B.K. 2014. An important role of the pepper phenylalanine ammonia-lyase gene (PAL1) in salicylic acid-dependent signalling of the defence response to microbial pathogens. Journal of Experimental Botany 65 (9): 2295–2306.
Kumar A., Ellis B.E. 2001. The phenylalanine ammonia-lyase gene family in raspberry. Structure, expression, and evolution. Plant Physiology 127 (1): 230–239.
Lee B.K., Park M.R., Srinivas B., Chun J.C., Kwon I.S., Chung I.M., Yoo N.H., Choi K.G., Yun S.J. 2003. Induction of phenylalanine ammonia-lyase gene expression by paraquat and stress-related hormones in rehmannia glutinosa. Molecules and Cells 16 (1): 34–39.
Liu R., Xu S., Li J., Hu Y., Lin Z. 2006. Expression profile of a PAL gene from Astragalus membranaceus var. Mongholicus and its crucial role in flux into flavonoid biosynthesis. Plant Cell Reports 25 (7): 705–710.
Ma W.L., Wu M., Wu Y., Ren Z.M., Zhong Y. 2013. Cloning and characterisation of a phenylalanine ammonia-lyase gene from Rhus chinensis. Plant Cell Reports 32 (8): 1179–1190.
MacDonald M.J., D’Cunha G.B. 2007. A modern view of phenylalanine ammonia lyase. Biochemistry and Cell Biology 85 (3): 273–282.
Maher E.A., Bate N.J., Ni W., Elbind Y., Dixon R.A., Lamb C.J. 1994. Increase disease susceptibility of transgenic tobacco plants with suppressed levels of preformed phenylpropanoid products. Proceedings of the National Academy of Sciences of the United States of America 91 (16): 7802–7806.
Mohammed C.L., Rimbawanto A., Page D.E. 2014. Management of basidiomycete root- and stem-rot diseases in oil palm, rubber and tropical hardwood plantation crops. Forest Pathology 44 (6): 428– 446.
Mur L.A.J., Naylor G., Warner S.A.J., Sugars J.M., White R.F., Draper J. 1996. Salicylic acid potentiates defence gene expression in tissue exhibiting acquired resistance to pathogen attack. The Plant Journal 9 (4): 559–571.
Nandris D., Nicole M., Geiger J.P. 1987. Root rot disease of rubber trees. Plant Disease 71 (4): 298–306.
Ogbebor N.O., Adekunle A.T., Eghafona O.N., Ogboghodo A.I. 2013. Incidence of Rigidoporus lignosus (Klotzsch) imaz of para rubber in Nigeria. Researcher 5 (12): 181–184.
Oghenekaro A.O., Omorusi V.I., Asiegbu F.O. 2016. Defencerelated gene expression of Hevea brasiliensis clones in response to the white rot pathogen, Rigidoporus microporus. Forest Pathology 46 (4): 318–326. DOI:10.1111/efp.12260.
Pallas J.A., Paiva N.L., Lamb C., Dixon R.A. 1996. Tobacco plants epigenetically suppressed in phenylalanine ammonia-lyase expression do not develop systemic acquired resistance in response to infection by tobacco mosaic virus. The Plant Journal 10 (2): 281–293.
Pellegrini L., Rohfritsch O., Fritig B., Legrand M. 1994. Phenylalanine ammonia-lyase in tobacco. Molecular cloning and gene expression during the hypersensitive reaction to tobacco mosaic virus and the response to a fungal elicitor. Plant Physiology 106 (3): 877–886.
Pereira L.F., Goodwin P.H., Erickson L. 1999. The role of a phenylalanine ammonia lyase gene during cassava bacterial bright and cassava bacterial necrosis. Journal of Plant Research 112 (1): 51–60.
Pfaffl M.W. 2001. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Research 29 (9): e45.
Rasmussen R. 2000. Quantification on the light cycler. p. 21–34. In: “Rapid Cycle Real-Time PCR, Methods and Applications” (S. Meuer, C. Wittwer, K.I. Nakagawara, eds.). Springer Press, Heidelberg, Germany, 408 pp.
Sambrook J., Fritsch E.F., Maniatist T. 1989. Molecular Cloning: a Laboratory Manual. Vol. 1. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, USA, 626 pp.
Sayari M., Babaeizad V., Ghanbari M.A.T., Rahimian H. 2014. Expression of the pathogenesis related proteins, NH-1, PAL, and lipoxygenase in the iranian Tarom and Khazar rice cultivars, in reaction to Rhizoctonia solani – the causal agent of rice sheath blight. Journal of Plant Protection Research 54 (1): 35–43.
Shadle G.L., Wesley S.V., Korth K.L., Chen F., Lamb C., Dixon R.A. 2003. Phenylpropanoid compounds and disease resistance in transgenic tobacco with altered expression of l-phenylalanine ammonia-lyase. Phytochemistry 64 (1): 153–161.
Sherif S.M., Shukla M.R., Murch S.J., Bernier L., Saxena P.K. 2016. Simultaneous induction of jasmonic acid and disease-responsive genes signifies tolerance of American elm to Dutch elm disease. Scientific Reports 6: 21934.
Shirasu K., Nakajima H., Rajasekhar V.K., Dixon R.A., Lamb C. 1997. Salicylic acid potentiates an agonist-dependent gain control that amplifies pathogen signals in the activation of defense mechanisms. The Plant Cell 9 (2): 261–270.
Song J., Wang Z. 2009. Molecular cloning, expression and characterization of a phenylalanine ammonia-lyase gene (SmPAL1) from Salvia miltiorrhiza. Molecular Biology Reports 36 (5): 939–952.
Suzuki H., Xia Y., Cameron R., Shadle G., Blount J., Lamb C., Dixon R.A. 2004. Signals for local and systemic responses of plants to pathogen attack. Journal of Experimental Botany 55 (395): 169–179.
Thompson J.D., Higgins D.G, Gibson T.J. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Research 22 (22): 4673–4680.
Wang L., Wang Y., Cao H., Hao X., Zeng J., Yang Y., Wang X. 2016. Transcriptome analysis of an anthracnose-resistant tea plant cultivar reveals genes associated with resistance to Colletotrichum camelliae. PLoS One 11 (2): e0148535.
Yang H.R., Tang K., Liu H.T., Huang W.D. 2011. Effect of salicylic acid on jasmonic acid-related defense response of pea seed-lings to wounding. Scientia Horticulturae 128 (3): 166–173.
Zhu Q., Dabi T., Beeche A., Yamamoto R., Lawton M.A., Lamb C. 1995. Cloning and properties of a rice gene encoding phenylalanine ammonia-lyase. Plant Molecular Biology 29 (3): 535–550.
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