Molecular cloning and expression analysis of a squalene synthase gene from a medicinal plant, Euphorbia pekinensis Rupr

Euphorbia pekinensis Rupr., which is also known as a medicinal plant, produces a large amount of alkaloids, phytosterols and triterpenes. In this study, we reported on the cDNA cloning and characterization of a novel squalene synthase (SQS) from E. pekinensis. Squalene synthase catalyzes the condens...

Full description

Saved in:
Bibliographic Details
Published in:Acta physiologiae plantarum 2013-10, Vol.35 (10), p.3007-3014
Main Authors: Zheng, Zhujun, Cao, Xiaoying, Li, Changgen, Chen, Yongqiang, Yuan, Bo, Xu, Yan, Jiang, Jihong
Format: Article
Language:English
Subjects:
Agriculture
alkaloids
amino acid sequences
amino acids
Biomedical and Life Sciences
complementary DNA
Escherichia coli
Euphorbia
gene expression
genes
high performance liquid chromatography
leaves
Life Sciences
medicinal plants
molecular cloning
open reading frames
Original Paper
phylogeny
Plant Anatomy/Development
Plant Biochemistry
Plant Genetics and Genomics
Plant Pathology
Plant Physiology
polyacrylamide gel electrophoresis
roots
squalene
stems
Western blotting
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Euphorbia pekinensis Rupr., which is also known as a medicinal plant, produces a large amount of alkaloids, phytosterols and triterpenes. In this study, we reported on the cDNA cloning and characterization of a novel squalene synthase (SQS) from E. pekinensis. Squalene synthase catalyzes the condensation of two molecules of farnesyl diphosphate (FPP) to produce squalene (SQ), the first committed precursor for sterol and triterpene biosynthesis. The full length cDNA named EpSQS (Genbank Accession Number JX509735) contained 1,614 bp with an open reading frame of 1,236 bp encoding a polypeptide of 411 amino acids. The deduced amino acid sequence of the EpSQS named EpSQS exhibited a high homology with other plant SQSs, and contained a single domain surrounded by helices. Phylogenetic analysis showed that EpSQS belonged to the plant SQS kingdom. Tissue expression analysis revealed that EpSQS expressed strongly in roots, weakly in stems and leaves, implying that EpSQS was a constitutive expression gene. The recombinant protein was expressed in Escherichia coli and detected by SDS-PAGE and western blot. The high performance liquid chromatography (HPLC) analysis showed that EpSQS could catalyze the reaction from farnesyl diphosphate (FPP) to squalene.
ISSN:0137-5881
1861-1664
DOI:10.1007/s11738-013-1333-7