Molecular cloning, characterization and expression analysis of a new gene encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase from Salvia miltiorrhiza

P Liao, W Zhou, L Zhang, J Wang, X Yan… - Acta Physiologiae …, 2009 - Springer
P Liao, W Zhou, L Zhang, J Wang, X Yan, Y Zhang, R Zhang, L Li, G Zhou, G Kai
Acta Physiologiae Plantarum, 2009Springer
Abstract The 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) catalyzes the conversion of
HMG-CoA to mevalonate (MVA), which is the first committed step in MVA pathway for
isoprenoid biosynthesis in plants. In this study, a full-length cDNA encoding HMGR was
isolated from Salvia miltiorrhiza by rapid amplification of cDNA ends (RACE) for the first time,
which was designated as SmHMGR (GenBank Accession No. EU680958). The full-length
cDNA of SmHMGR was 2,115 bp containing a 1,695 bp open reading frame (ORF) encoding …
Abstract
The 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) catalyzes the conversion of HMG-CoA to mevalonate (MVA), which is the first committed step in MVA pathway for isoprenoid biosynthesis in plants. In this study, a full-length cDNA encoding HMGR was isolated from Salvia miltiorrhiza by rapid amplification of cDNA ends (RACE) for the first time, which was designated as SmHMGR (GenBank Accession No.EU680958). The full-length cDNA of SmHMGR was 2,115 bp containing a 1,695 bp open reading frame (ORF) encoding a polypeptide of 565 amino acids. Bioinformatic analyzes revealed that the deduced SmHMGR had extensive homology with other plant HMGRs contained two transmembrane domains and a catalytic domain. Molecular modeling showed that SmHMGR is a new HMGR with a spatial structure similar to other plant HMGRs. Phylogenetic tree analysis indicated that SmHMGR belongs to the plant HMGR super-family and has the closest relationship with HMGR from Picrorhiza kurrooa. Expression pattern analysis implied that SmHMGR expressed highest in root, followed by stem and leaf. The expression of SmHMGR could be up-regulated by salicylic acid (SA) and methyl jasmonate (MeJA), suggesting that SmHMGR was elicitor-responsive. This work will be helpful to understand more about the role of HMGR involved in the tanshinones biosynthesis at the molecular level.
Springer
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