Molecular cloning and expression of Hedychium coronarium farnesyl pyrophosphate synthase gene and its possible involvement in the biosynthesis of floral and wounding/herbivory induced leaf volatile sesquiterpenoids |
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Authors: | Jian-bin Lan Rang-cai YuYun-yi Yu Yan-ping Fan |
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Affiliation: | Center of Flower Research, College of Horticulture, South China Agricultural University, Guangzhou 510642, China |
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Abstract: | Farnesyl pyrophosphate synthase (FPPS EC 2.5.1.10) catalyzes the production of farnesyl pyrophosphate (FPP), which is a key precursor for many sesquiterpenoids such as floral scent and defense volatiles against herbivore attack. Here we report a new full-length cDNA encoding farnesyl diphosphate synthase from Hedychium coronarium. The open reading frame for full-length HcFPPS encodes a protein of 356 amino acids, which is 1068 nucleotides long with calculated molecular mass of 40.7 kDa. Phylogenetic tree analysis indicates that HcFPPS belongs to the plant FPPS super-family and has strong relationship with FPPS from Musa acuminata. Expression of the HcFPPS gene in Escherichia coli yielded FPPS activity. Tissue-specific and developmental analyses of the HcFPPS mRNA and corresponding volatile sesquiterpenoid levels in H. coronarium flowers revealed that the HcFPPS might play a regulatory role in floral volatile sesquiterpenoid biosynthesis. The emission of the FPP-derived volatile terpenoid correlates with strong expression of HcFPPS induced by mechanical wounding and Udaspes folus-damage in leaves, which suggests that HcFPPS may have an important ecological function in H. coronarium vegetative organ. |
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Keywords: | FPPS, farnesyl pyrophosphate synthase DMAPP, dimethylallyl pyrophosphate FPP, farnesyl pyrophosphate GC&ndash MS, gas chromatography&ndash mass spectrometry GPP, geranyl pyrophosphate IPP, isopentenyl pyrophosphate DXP, 1-deoxyxylulose-5-phosphate |
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