Molecular Cloning, Characterization, and Differential Expression of a Farnesyl-Diphosphate Synthase Gene from the Basidiomycetous FungusGanoderma lucidum
| Autor: | Liang Shi, Yu-Xiang Li, Xiang Ou-Yang, Mingwen Zhao, Yi-Xin Ding, Ang Ren, Chang-Hua Shang |
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| Rok vydání: | 2008 |
| Předmět: |
DNA
Complementary Reishi Molecular Sequence Data Gene Expression Saccharomyces cerevisiae Biology Molecular cloning Applied Microbiology and Biotechnology Biochemistry Homology (biology) Analytical Chemistry Complementary DNA Gene expression Amino Acid Sequence Cloning Molecular Molecular Biology Gene Peptide sequence Phylogeny Base Sequence Organic Chemistry Geranyltranstransferase General Medicine Molecular biology Complementation Open reading frame Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 72:1571-1579 |
| ISSN: | 1347-6947 0916-8451 |
| DOI: | 10.1271/bbb.80067 |
| Popis: | A farnesyl-diphosphate synthase gene, designated GlFPS, was isolated from a triterpene-producing basidiomycetous fungus, Ganoderma lucidum. The GlFPS cDNA was found to contain an open reading frame of 1,083 bp, encoding a protein of 360 amino acids with a calculated molecular mass of 41.27 kDa. The deduced amino acid sequence of the GlFPS cDNA exhibited a high homology with other fungal FPS genes, and contained four conserved domains. Phylogenetic analysis showed that GlFPS belonged to the basidiomycete FPS group. Competitive PCR revealed that GlFPS was constitutively expressed in the mycelium growth stage, whereas the transcripts of GlFPS accumulated to high levels rapidly during the process of mushroom primordia. Treatment of mycelia with exogenous methyl jasmonate also caused a large accumulation of GlFPS mRNA. Subsequently, promoter analysis indicated that the 5' upstream region of GlFPS possessed various potential regulatory elements associated with physiological and environmental factors. Functional complementation of GlFPS in an ERG20-disrupted yeast strain indicated that the cloned cDNA encoded a farnesyl-diphosphate synthase. |
| Databáze: | OpenAIRE |
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