Cloning and characterization of 3-hydroxy-3-methylglutary CoA reductase cDNA of Glycyrrhiza uralensis.
- Author:
Qixians RONG
1
;
Qiaoxian XU
;
Chunsheng LIU
;
Luqi HUANG
Author Information
- Publication Type:Journal Article
- MeSH: Amino Acid Sequence; Cloning, Molecular; DNA, Complementary; genetics; Glycyrrhiza uralensis; chemistry; classification; enzymology; genetics; Hydroxymethylglutaryl CoA Reductases; chemistry; genetics; metabolism; Molecular Sequence Data; Phylogeny; Plant Proteins; chemistry; genetics; metabolism; Sequence Alignment
- From: China Journal of Chinese Materia Medica 2011;36(10):1275-1279
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo clone and analysis the sequence of 3-hydroxy-3-methylglutary CoA reductase (HMGR) cDNA from Glycyrrhiza uralensis.
METHODThe primers were designed based on the conservative region of HMGR nucleic acids sequence from public database. The target gene was obtained from root of G. uralensis by use of homologous cDNA amplificati on and RACE technologies. The sequence alignment was performed using BLAST. The open reading frame was identified by use of the ORF Finder. The protein domains were defined by use of Prosite software. Clustal was used to conduct multiple amino acid sequence alignment and MEGA 5.0 was used to conduct the phylogenetic tree.
RESULTThe GuHMGR cDNA sequence was obtained contains 1 842 bp contains a 1 722 bp ORF, encoding 573 amino acids with 3-hydroxy-3-methylglutary CoA reductases family profile. Deduced amino acid sequence had 84% and 76% homology to the amino acid sequence of Pisum sativum, Medicago truncatula.
CONCLUSIONThe cloning of 3-hydroxy-3-methylglutary CoA reductase (HMGR) cDNA will provide a foundation for exploring the function of HMGR in glycyrrhizin biosynthesis.
