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Rapid Assembly of Multi-Gene Constructs using Modular Golden Gate Cloning
Published on: February 5, 2021
[Rapid cloning and functional characterization of hypericin synthase gene]
Yan-Wei Shi1, Xiao-Hui Zhi, Hai-Na Zheng
1State Key Laboratory of Bioactive Substance and Function of Natural Medicines & Key Laboratory of Biosynthesis of Natural Products, Ministry of Health of PRC, Institute of Materia Medica, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing 100050, China.
Yao Xue Xue Bao = Acta Pharmaceutica Sinica
|July 20, 2012
Summary
Researchers confirmed the function of the hyp-1 gene in synthesizing hypericin, a compound from St. John's wort. This discovery advances synthetic biotechnology for producing hypericin.
Area of Science:
- Biotechnology
- Natural Products Chemistry
- Molecular Biology
Background:
- Hypericin, a natural product from St. John's wort, shows therapeutic potential.
- The gene encoding the enzyme responsible for hypericin synthesis has been debated.
Purpose of the Study:
- To clone and express the hyp-1 gene.
- To confirm the function of the hyp-1 gene in catalyzing hypericin synthesis.
Main Methods:
- Synthesized primers for the hyp-1 gene.
- Cloned the hyp-1 gene using PCR and confirmed with DNA sequencing.
- Expressed the recombinant Hyp-1 protein in E. coli and verified expression via SDS-PAGE and Western blot.
Main Results:
- Successfully cloned and expressed the hyp-1 gene in E. coli.
- Confirmed the Hyp-1 protein's enzymatic activity in converting emodin to hypericin in vitro using LC-MS/MS.
- Validated the function of the hyp-1 gene in hypericin biosynthesis.
Conclusions:
- The hyp-1 gene encodes a functional enzyme catalyzing hypericin synthesis.
- This research provides a foundation for the biotechnological production of hypericin.
