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Cloning and mRNA Expression Analysis of the Gene Encoding Phenylalanine Ammonia-Lyase of the Ectomycorrhizal Fungus Tricholoma matsutake

  • Yoon, Hyeokjun (Department of Life Sciences and Biotechnology, Kyungpook National University) ;
  • You, Young-Hyun (Department of Life Sciences and Biotechnology, Kyungpook National University) ;
  • Kim, Ye-Eun (Department of Life Sciences and Biotechnology, Kyungpook National University) ;
  • Kim, Young Ja (Korea Environmental Industry & Technology Institute) ;
  • Kong, Won-Sik (National Institute of Horticultural & Herbal Science, RDA) ;
  • Kim, Jong-Guk (Department of Life Sciences and Biotechnology, Kyungpook National University)
  • Received : 2013.03.19
  • Accepted : 2013.06.21
  • Published : 2013.08.28

Abstract

The ectomycorrhizal fungus Tricholoma matsutake grows symbiotically with Pinus densiflora. Phenylalanine ammonia-lyase (E.C. 4.3.1.24) catalyzes the conversion of L-phenylalanine to trans-cinnamic acid. The role of fungal phenylalanine ammonia-lyase, however, has not been clear until now. In this study, the gene encoding phenylalanine ammonia-lyase (PAL), which was isolated from T. matsutake, was cloned and characterized. The PAL gene (tmpal) consists of 2,160 nucleotides, coding for a polypeptide containing 719 amino acid residues. The deduced amino acid sequence of tmpal from T. matsutake shows high identity (70%) with that from Laccaria bicolor. Comparative analysis of the PAL genes among T. matsutake and other species of the class Agaricomycetes showed that both active sites and binding sites were significantly conserved among these genes. The transcriptional analysis of the PAL gene revealed a differential gene expression pattern depending on the developmental stages (mycelium, primordium, stipe, pileus, and gills) of T. matsutake. These results suggest that the PAL gene in T. matsutake plays an important role in multiple physiological functions.

Keywords

References

  1. Dobson MJ, Tuite MF, Roberts NA, Kingsman AJ, Kingsman SM, Perkins RE, et al. 1982. Conservation of high efficiency promoter sequences in Saccharomyces cerevisiae. Nucleic Acids Res. 10: 2625-2637. https://doi.org/10.1093/nar/10.8.2625
  2. Ewing B, Hillier L, Wendl MC, Green P. 1998. Base-calling of automated sequencer traces using phred. I. Accuracy assessment. Genome Res. 8: 175-185. https://doi.org/10.1101/gr.8.3.175
  3. Fritz RR, Hodgins DS, Abell CW. 1976. Phenylalanine ammonia-lyase. Induction and purification from yeast and clearance in mammals. J. Biol. Chem. 251: 4646-4650.
  4. Huang X, Madan A. 1999. CAP3: a DNA sequence assembly program. Genome Res. 9: 868-877. https://doi.org/10.1101/gr.9.9.868
  5. Hyun MW, Y un YH, Kim JY, K im S H. 2 011. F ungal and plant phenylalanine ammonia-lyase. Mycobiology 39: 257-265. https://doi.org/10.5941/MYCO.2011.39.4.257
  6. Kim NS, Hahn Y, Oh JH, Lee JY, Oh KJ, Kim JM, et al. 2004. Gene cataloging and expression profiling in human gastric cancer cells by expressed sequence tags. Genomics 83: 1024- 1045. https://doi.org/10.1016/j.ygeno.2003.12.002
  7. Kim SH, Virmani D, Wake K, MacDonald K, Kronstad JW, Ellis BE. 2001. Cloning and disruption of a phenylalanine ammonia-lyase gene from Ustilago maydis. Curr. Genet. 40: 40-48. https://doi.org/10.1007/s002940100230
  8. Kim WK, Mauthe W, Hausner G, Klassen GR. 1990. Isolation of high molecular weight DNA and doublestranded RNAs from fungi. Can. J. Bot. 68: 1898-1902. https://doi.org/10.1139/b90-249
  9. Leal GA, Gomes LH, Albuquerque PS, Tavares FC, Figueira A. 2 010. S earching f or Moniliophthora perniciosa pathogenicity genes. Fungal Biol. 114: 842-854. https://doi.org/10.1016/j.funbio.2010.07.009
  10. MacDonald MJ, D 'Cunha GB. 2007. A m odern view o f phenylalanine ammonia lyase. Biochem. Cell Biol. 85: 273-282. https://doi.org/10.1139/O07-018
  11. Marchler-Bauer A, Lu S, Anderson JB, Chitsaz F, Derbyshire MK, DeWeese-Scott C, et al. 2011. CDD: a conserved domain database for the functional annotation of proteins. Nucleic Acids Res. 39: 225-229. https://doi.org/10.1093/nar/gkq769
  12. Mauch-Mani B, Slusarenko AJ. 1996. Production of salicylic acid precursors is a major function of phenylalanine ammonia-lyase in the Resistance of Arabidopsis to Peronospora parasitica. Plant Cell 8: 203-212. https://doi.org/10.1105/tpc.8.2.203
  13. Solovyev V, Salamov A. 1997. The Gene-Finder computer tools for analysis of human and model organisms genome sequences. Proc. Int. Conf. Intell. Syst. Mol. Biol. 5: 294-302.
  14. Tamura K, Dudley J, Nei M , Kumar S. 2007. M EGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24: 1596-1599. https://doi.org/10.1093/molbev/msm092
  15. Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG. 1997. The CLUSTAL_X Windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 24: 4876-4882.

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