Cloning and analysis of mevalonate kinase (PnMVK1) gene in Panax notoginseng.
- Author:
Xu GUO
1
;
Hong-mei LUO
;
Shi-lin CHEN
Author Information
1. National Engineering Laboratory for Breeding of Endangered Medicinal Materials, Institute of Medicinal Plant Development, Chinese Academy of Medical Sciences & Peking Union Medical, Beijing 100193, China.
- Publication Type:Journal Article
- MeSH:
Amino Acid Sequence;
Cloning, Molecular;
Cluster Analysis;
Conserved Sequence;
DNA, Complementary;
genetics;
Gene Expression Regulation, Plant;
Molecular Sequence Data;
Molecular Weight;
Open Reading Frames;
Panax notoginseng;
enzymology;
genetics;
Phosphotransferases (Alcohol Group Acceptor);
genetics;
metabolism;
Phylogeny;
Plant Roots;
enzymology;
genetics;
Plants, Medicinal;
enzymology;
genetics;
Protein Structure, Secondary
- From:
Acta Pharmaceutica Sinica
2012;47(8):1092-1097
- CountryChina
- Language:Chinese
-
Abstract:
Mevalonate kinase (MVK) is a key enzyme in plant terpenoid biosynthetic pathway. This study focused on cloning and analysis of Panax notoginseng (Burk.) F. H. Chen MVK (PnMVK1) gene. After searching the transcriptome dataset of P. notoginseng, one unique sequence encoding MVK was discovered. The primers were designed according to the transcript sequence of PnMVK1 from the P. notoginseng transcriptome dataset. And then, the open reading frame of PnMVK1 was cloned from P. notoginseng by using RT-PCR strategy. The physical and chemical properties, secondary structure and three-dimensional structure of the PnMVK1 protein were forecasted and analyzed, and its structure and function were predicted. The cDNA (named as PnMVK1) contains a 1164 bp open reading frame and encodes a predicted protein of 387 amino acids. The GenBank accession number for this gene is JQ957844. No transmembrane region and signal peptide were present in PnMVK1. The conserved domain of mevalonate kinase was present in PnMVK1. PnMVK1 was more abundant in P. notoginseng root than other organisms. This study cloned and analyzed PnMVK1 gene from P. notoginseng for the first time. The result will provide a foundation for exploring the mechanism of terpenoid biosynthesis in P. notoginseng plants.