Browse > Article

Cloning and Sequence Analysis of a Glyceraldehyde-3-phosphate Dehydrogenase Gene from Ganoderma lucidum  

Fei Xu (College of Life Sciences, Nanjing Agricultural University)
Zhao Ming Wen (College of Life Sciences, Nanjing Agricultural University)
Li Yu Xiang (College of Life Sciences, Nanjing Agricultural University)
Publication Information
Journal of Microbiology / v.44, no.5, 2006 , pp. 515-522 More about this Journal
Abstract
A cDNA library of Ganoderma lucidum has been constructed using a Zap Express cloning vector. A glyceraldehyde-3-phosphate dehydrogenase gene (gpd) was isolated from this library by hybridization of the recombinant phage clones with a gpd-specific gene probe generated by PCR. By comparison of the cDNA and the genomic DNA sequences, it was found that the complete nucleotide sequence encodes a putative polypeptide chain of 338 amino acids interrupted by 6 introns. The predicted amino acid sequence of this gene shows a high degree of sequence similarity to the GPD proteins from yeast and filamentous fungi. The promoter region contains a CT-rich stretch, two CAAT boxes, and a consensus TATA box. The possibility of using the gpd promoter in the construction of new transformation vectors is discussed.
Keywords
gyceraldehyde-3-phosphate dehydrogenase gene; Ganoderma lucidum; medicinal mushroom; strain improvement; promoter; transformation vector;
Citations & Related Records

Times Cited By Web Of Science : 8  (Related Records In Web of Science)
Times Cited By SCOPUS : 14
연도 인용수 순위
1 Hsu, H.Y., S.L. Lian, and C.C. Lin. 1990. Radioprotective effect of Ganoderma lucidum (Leyss. ex. Fr.) Karst after X-ray irradiation in mice. Am. J. Chin. Med. 18, 61-69   DOI   ScienceOn
2 Kim, D.H., S.B. Shim, N.J. Kim, and I.S. Jang. 1999. Beta-glucuronidase-inhibitory activity and hepatoprotective effect of Ganoderma lucidum. Biol. Pharm. Bull. 22, 162-164   DOI
3 Russo, P., J.T. Juutii, and M. Raudaskoski. 1992. Cloning, sequence and expression of a beta-tubulin-encoding gene in the homobasidiomycete Schizophyllum commune. Gene 119, 175-182   DOI   ScienceOn
4 Thompson, J.D., D.G. Higgings, and T.J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680   DOI
5 Van de Rhee, M.D., P.M. Graca, H.J. Huizing, and H. Mooibroek. 1996. Transformation of the cultivated mushroom, Agaricus bisporus, to hygromycin B resistance. Mol. Gen. Genet. 250, 252-258
6 Wang, S.Y, M.L. Hsu, H.C. Hsu, C.H. Tzeng, S.S. Lee, M.S. Shiao. and C.K. Ho. 1997. The anti-tumor effect of Ganoderma lucidum is mediated by cytokines released from activated macrophages and T lymphocytes. Int. J. Cancer 70, 699-705   DOI   ScienceOn
7 Su, C.Y., M.S. Shiao, and C.T. Wang. 1999. Differential effects of ganodermic acid S on the thromboxane A2-signaling pathways in human platelets. Biochem. Pharmacol. 58, 587-595   DOI   ScienceOn
8 Yoon, S.Y, S.K. Eo, Y.S. Kim, C.K. Lee, and S.S. Han. 1994. Antimicrobial activity of Ganoderma lucidum extract alone and in combination with some antibiotics. Arch. Pharm. Res. 17. 438-442   DOI
9 Lin, J.M., C.C. Lin, H.F. Chiu, J.J. Yang, and S.G. Lee. 1993. Evaluation of the anti-inflammatory and liver-protective effects of Anoectochilus formosanus, Ganoderma lucidum, and Gynostemma pentaphyllum in rats. Am. J. Chin. Med. 21, 59-69   DOI   ScienceOn
10 Smith, T.L. 1989. Disparate evolution of yeasts and filamentous fungi indicated by phylogenetic analysis of glyceraldehyde-3-phosphate dehydrogenase genes. Proc. Natl. Acad. Sci. USA 86, 7063-7066
11 Hirano, T., T. Sato, K. Okawa, K, Kanda, K. Yaegashi, and H. Enei. 1999. Isolation and characterization of the glyceraldehyde-3-phosphate dehydrogenase gene of Lentinus edodes. Biosci. Biotechnol. Biochem. 63, 1223-1227   DOI   ScienceOn
12 Hirano, T., T. Sato, K. Yaegashi, and H. Enei. 2000. Efficient transformation of the edible basidiomycete Lentinus edodes with a vector using a glyceraldehyde-3-phosphate dehydrogenase promoter to hygromycin B resistance. Mol. Gen. Genet. 263, 1047-1052   DOI
13 Piechaczyk, M., J.M. Blanchard, L. Marty, C. Dani, F. Panabieres, S. El Sabouty, P. Fort, and P. Jeanteur. 1984. Post-transcriptional regulation of glyceraldehyde-3-phosphate-dehydrogenase gene expression in rat tissues. Nucleic Acids Res. 12, 6951-6963   DOI
14 Chen, X., M. Stone, C. Schlagnhaufer, and C.P. Romaine. 2000. A fruiting body tissue method for efficient Agrobacteriummediated transformation of Agaricus bisporus. Appl. Environ. Microbiol. 66, 4510-4513   DOI
15 Punt, P.J, M.A. Dingemanse, A. Kuyvenhoven, R.D. Soede, P.H. Pouwels, and C.A. van den Hondel. 1990. Functional elements in the promoter region of the Aspergillus nidulans gpdA gene encoding glyceraldehyde-3-phosphate dehydrogenase. Gene 93, 101-109   DOI   ScienceOn
16 Herzog, R.W., N.K. Singh, C. Schmidt, and P.A. Lemke. 1995. Presence of a P1 bacteriophage sequence in transforming plasmids of Pleurotus ostreatus. Curr. Genet. 27, 460-465   DOI
17 Tasaka, K., M. Mio, K. Izushi, M. Akagi, and T. Makino. 1998. Anti-allergic constituents in the culture medium of Ganoderma lucidum. (II). The inhibitory effect of cyclooctasulfur on histamine release. Agents Actions 23, 157-160   DOI
18 Balance, D.J. 1990. Transformation systems for filamentous fungi and an overview of fungal gene structure. Molecular Industrial Mycology, p. 1-29. In S.A. Leong and R.M. Berka (eds.), Dekker, New York, USA
19 Verdoes, J.C., J. Wery, T. Boekhout, and A.J. Van Ooyen. 1997. Molecular characterization of the glyceraldehyde-3-phosphate dehydrogenase gene of Phaffia rhodozyma. Yeast 13, 1231-1242   DOI   ScienceOn
20 Waterham, H.R., M.E. Digan, P.J. Koutz, S.Y. Lair, and J.M. Cregg. 1997. Isolation of the Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase gene and regulation and use of its promoter. Gene 186, 37-44   DOI   ScienceOn
21 Holland, M.J. and J.P. Holland. 1978. Isolation and identification of yeast messenger ribonucleic acids coding for enolase, glyceraldehyde-3-phosphate dehydrogenase, and phosphoglycerate kinase. Biochemistry 17, 4900-4907   DOI   ScienceOn
22 EI-Mekkawy, S., M.R. Meselhy, N. Nakamura, Y. Tezuka, M. Hattori, N. Kakiuchi, K. Shimotohno, T. Kawahata, and T. Otake. 1998. Anti- HIV-1 and anti- HIV-1-protease substances from Ganoderma lucidum. Phytochemistry 49, 1651-1657   DOI   ScienceOn
23 Sun, L., H. Cai, W. Xu, Y. Hu, and Z. Lin. 2002. CaMV 35S promoter directs beta-glucuronidase expression in Ganoderma lucidum and Pleurotus citrinopileatus. Mol. Biotechnol. 20, 239-244   DOI   ScienceOn
24 Kim, S., J. Song, and H.T. Choi. 2004. Genetic transformation and mutant isolation in Ganoderma lucidum by restriction enzyme-mediated integration. FEMS Microbiol. Lett. 233, 201-204   DOI
25 Wolff, A.M. and J. Arnau. 2002. Cloning of glyceraldehyde-3-phosphate dehydrogenase-encoding genes in Mucor circinelloides (Syn. racemosus) and use of the GPDI promoter for recombinant protein production. Fungal Genet. Biol. 35, 21-29   DOI   ScienceOn
26 Harmsen, M.C., F.H. Schuren, S.M. Moukha, C.M. van Zuilen, P.J. Punt, and J.G. Wessels. 1992. Sequence analysis of the glyceraldehyde-3-phosphate dehydrogenase genes from the basidiomycetes Schizophyllum commune, Phanerochaete chrysosporium and Agaricus bisporus. Curr. Genet. 22, 447-454   DOI
27 Maruyama, H., K. Yamazaki, S. Murofushi, C. Konda, and T. Ikekawa. 1989. Antitumor activity of Sarcodon aspratus (Berk.) S. Ito and Ganoderma lucidum (Fr.) Karst. J. Pharmacobiodyn 12, 118-123   DOI
28 Kuo, C.Y., S.Y. Chou, and C.T. Huang. 2004. Cloning of glyceraldehyde-3-phosphate dehydrogenase gene and use of the gpd promoter for transformation in Flammulina velutipes. Appl. Microbiol. Biotechnol. 65, 593-599
29 Bitter, G.A. and K.M. Egan. 1984. Expression of heterologous genes in Saccharomyces cerevisiae from vectors utilizing the glyceraldehyde-3-phosphate dehydrogenase gene promoter. Gene 32, 263-274   DOI   ScienceOn
30 Sambrook, J., E.F. Fritsch, and T. Maniatis. 1989. Molecular Cloning: A Laboratory Manual, (2nd ed). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, USA