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

• Published in: Journal of microbiology and biotechnology Vol. 23; no. 8; pp. 1055 - 1059
• Main Authors: Yoon, H.J., Kyungpook National University, Daegu, Republic of Korea, You, Y.H., Kyungpook National University, Daegu, Republic of Korea, Kim, Y.E., Kyungpook National University, Daegu, Republic of Korea, Kim, Y.J., Korea Environmental Industry and Technology Institute, Seoul, Republic of Korea, Kong, W.S., RDA, Suwon, Republic of Korea, kim, J.G., Kyungpook National University, Daegu, Republic of Korea
• Format: Journal Article
• Language: English
• Published: Seoul Korean Society for Applied Microbiology 01.08.2013; 한국미생물·생명공학회
• Subjects: Biological and medical sciences; Biotechnology; Catalytic Domain; CHAMPIGNON COMESTIBLE; Cloning, Molecular; Conserved Sequence; EDIBLE FUNGI; Fundamental and applied biological sciences. Psychology; Gene Expression Profiling; Open Reading Frames; Phenylalanine Ammonia-Lyase - biosynthesis; Phenylalanine Ammonia-Lyase - genetics; RNA, Messenger - biosynthesis; RNA, Messenger - genetics; Sequence Homology, Amino Acid; SETAS COMESTIBLES; Tricholoma - enzymology; Tricholoma - genetics; Tricholoma matsutake,phenylalanine ammonia-lyase; 생물학; Phenylalanine ammonia-lyase; Enzyme; Lyases; Tricholoma; Basidiomycota; Carbon-nitrogen lyases; Fungi; Ammonia-lyases; Messenger RNA; Tricholoma matsutake; Gene; Mycorrhiza; Ectomycorrhiza; mushroom
• ISSN: 1017-7825; 1738-8872
• DOI: 10.4014/jmb.1303.03064

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 function