Functional characterization of the β-amyrin synthase gene involved in platycoside biosynthesis in Platycodon grandiflorum
Autor: | Yurry Um, Yi Lee, Chang Pyo Hong, Mei Lan Jin, Dae Young Lee, Ok Tae Kim, Chang Kug Kim |
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Rok vydání: | 2017 |
Předmět: |
0301 basic medicine
chemistry.chemical_classification Amyrin ATP synthase biology Plant Science Horticulture Yeast 03 medical and health sciences chemistry.chemical_compound 030104 developmental biology Enzyme Triterpene chemistry Biochemistry Biosynthesis Complementary DNA biology.protein Gene Biotechnology |
Zdroj: | Horticulture, Environment, and Biotechnology. 58:613-619 |
ISSN: | 2211-3460 2211-3452 |
DOI: | 10.1007/s13580-017-0054-z |
Popis: | Platycodon grandiflorum A. DC. contains a variety of triterpene saponins induced from the base structure of oleanane-type in roots. The β-amyrin synthase (bAS) plays an important role in controlling the biosynthesis of triterpene saponins and we obtained the full-length cDNA of the gene, which is named PlgOSC1 in P. grandiflorum. To identify the PlgOSC1 products, we expressed it in heterologous yeast cells. Results of GC-MS analysis showed a unique peak that was consistent with that of the authentic β-amyrin standard with exactly the same retention time. Furthermore, the pattern of MS fragments of the peak was also exactly the same as that of the β-amyrin. In qRT-PCR analysis of four organs of P. grandiflorum, no difference in PlgOSC1 expression level was observed; therefore, platycosides derived from β-amyrin might be present in all P. grandiflorum tissues. In conclusion, PlgOSC1 encodes a bAS enzyme that catalyzes the first committed step of platycosides biosynthesis in P. grandiflorum. |
Databáze: | OpenAIRE |
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