Molecular Cloning of a HMG-CoA Reductase Gene from <i>Eucommia ulmoides</i> Oliver

Jiang, Jihong; Kai, Guoyin; Cao, Xiaoying; Chen, Fengmei; He, Dongning; Liu, Qun

doi:10.1007/s10540-006-9010-3

Cited by 33 publications

(36 citation statements)

References 24 publications

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“…The tissue expression pattern showed that HMGR had strongly expressed differences, which suggested that HMGR might be a constitutively expressing gene. The similar results were reported by Jiang et al (2006). In addition, the expression pattern in different tissues suggested that this gene is expressed in a tissue-dependent manner in pigs.…”

Section: Discussionsupporting

confidence: 88%

“…The HMGR gene has been widely cloned in many species, i.e. the human HMG-CoA reductase gene has been localized to human chromosome 5q12 by in situ hybridization and contains 20 exons and 19 introns (Humphries et al, 1985;Luskey and Stevens, 1985), chicken (Sato et al, 2003), rat (Simonet and Ness, 1988;Sundaresan et al, 1989;Duckworth et al, 1991) and some plants (Ha et al, 2003;Jiang et al, 2006). Information regarding this gene in pigs, however, is limiting.…”

Section: Discussionmentioning

confidence: 99%

“…3-Hydroxy-3-methylglutaryl-CoA reductase (HMGR) catalyzes the conversion of HMG-CoA to mevalonate and is considered as the rate-limiting enzyme in the overall pathway of cholesterol biosynthesis (Istvan and Deisenhofer, 2000;Jiang et al, 2006). Leveille et al (1975) showed that liver is an important site of cholesterol synthesis and is controlled by gene of HMGR.…”

Section: Introductionmentioning

confidence: 99%

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Expression of HMGR and corresponding cholesterol content in tissues of two pig breeds

Liu

Fang

Lin

et al. 2009

Animal

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The 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) is an essential enzyme in cholesterol biosynthesis. To study the expression of HMGR and corresponding cholesterol content in liver, adipose and muscle, six Chinese local breed (Huai pig) and Landrace pigs were selected. The results indicated that significant differences of cholesterol content in adipose ( P , 0.01), liver ( P , 0.05) and muscle ( P , 0.01) tissues were detected between pigs of differing genetic backgrounds. HMGR mRNA expression were noted for adipose, liver and muscle of the two vastly differing genetics. Moreover cholesterol content differed ( P , 0.01) among tissues across breed. Likewise, HMGR mRNA expression was different between adipose and liver tissues, muscle and liver tissues in both breeds; however, no difference was noted between adipose and muscle tissues. Results from this study indicate that cholesterol content and HMGR mRNA expression are higher in Huai pig tissues suggesting this gene is expressed in a breed-and tissue-dependent manner in pigs. Understanding the causes of variation in HMGR gene expression may provide crucial information about cholesterol biosynthesis.

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Section: Discussionsupporting

confidence: 88%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Expression of HMGR and corresponding cholesterol content in tissues of two pig breeds

Liu

Fang

Lin

et al. 2009

Animal

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“…Although PgHMGR1 was expressed in different levels among the tested organs, the PgHMGR1 gene seems to be expressed constitutively throughout ginseng development, which was similar to the characterized homologs from Salvia miltiorrhiza (Liao et al, 2009) and Eucommia ulmoides (Jiang et al, 2006). Indeed, the heterologous expression of the two fulllength ginseng HMGRs in the Arabidopsis hmgr1-1 mutant background showed that only PgHMGR1 could complement the dwarf and sterile phenotypes of hmgr1-1 (Suzuki et al, 2004), which suggests that PgHMGR1 is a functional ortholog of AtHMGR1.…”

Section: Pghmgr1 Localized Into the Cytoplasmic Organelles And Its Gementioning

confidence: 74%

Functional Analysis of 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase Encoding Genes in Triterpene Saponin-Producing Ginseng

et al. 2014

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Ginsenosides are glycosylated triterpenes that are considered to be important pharmaceutically active components of the ginseng (Panax ginseng 'Meyer') plant, which is known as an adaptogenic herb. However, the regulatory mechanism underlying the biosynthesis of triterpene saponin through the mevalonate pathway in ginseng remains unclear. In this study, we characterized the role of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGR) concerning ginsenoside biosynthesis. Through analysis of full-length complementary DNA, two forms of ginseng HMGR (PgHMGR1 and PgHMGR2) were identified as showing high sequence identity. The steady-state mRNA expression patterns of PgHMGR1 and PgHMGR2 are relatively low in seed, leaf, stem, and flower, but stronger in the petiole of seedling and root. The transcripts of PgHMGR1 were relatively constant in 3-and 6-year-old ginseng roots. However, PgHMGR2 was increased five times in the 6-year-old ginseng roots compared with the 3-year-old ginseng roots, which indicates that HMGRs have constant and specific roles in the accumulation of ginsenosides in roots. Competitive inhibition of HMGR by mevinolin caused a significant reduction of total ginsenoside in ginseng adventitious roots. Moreover, continuous dark exposure for 2 to 3 d increased the total ginsenosides content in 3-year-old ginseng after the dark-induced activity of PgHMGR1. These results suggest that PgHMGR1 is associated with the dark-dependent promotion of ginsenoside biosynthesis. We also observed that the PgHMGR1 can complement Arabidopsis (Arabidopsis thaliana) hmgr1-1 and that the overexpression of PgHMGR1 enhanced the production of sterols and triterpenes in Arabidopsis and ginseng. Overall, this finding suggests that ginseng HMGRs play a regulatory role in triterpene ginsenoside biosynthesis.

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“…HMGR catalyzes the conversion of HMG-CoA into mevalonate (MVA) to yield a biologically active isoprenoid precursor, isopentenyl pyrophosphate (IPP) unit (Friesen & Rodwell, 2004;Jiang et al, 2006;Wang et al, 2007), which serves as the basis for the biosynthesis of molecules used in many metabolic processes such as steroid biosynthesis (Pitera, Paddon, Newman, & Keasling, 2007), terpenoid biosynthesis (Cheng et al, 2007) and carotenoid biosynthesis (Tada et al, 1990). The isolation and molecular characterization of plant HMGRs have been performed in both monocots and dicots such as Arabidopsis thaliana (Dudareva et al, 2005), rice (Ha, Lee, Kim, & Hwang, 2001), Camptotheca acuminate (Maldonado-Mendoza, Vincent, & Nessler, 1997), Ganoderma lucidum (Shang et al, 2008), and hazel .…”

Section: Introductionmentioning

confidence: 99%

Cloning of 3-Hydroxy-3-methylglutaryl-coenzyme A Reductase Gene from Vanda Mimi Palmer and Its Heterologous Expression in Escherichia coli

Teh¹,

Abdullah²,

Namasivayam³

et al. 2012

JPS

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Plant 3-hydroxy-3-methylglutaryl-CoA-reductase (HMGR) is involved in the conversion of HMG-CoA into mevalonate (MVA), which yields a biologically active isoprenoid precursor, isopentenyl pyrophosphate (IPP) unit. To date, heterologous expression of HMGR isolated from orchidaceae family has not been reported. The aims of this study were to isolate, clone, over-express and functionally characterize the cDNA encoding a 3-hydroxy-3-methylglutaryl-CoA-reductase of Vanda Mimi Palmer (VMPHMGR) in Escherichia coli strain BL21 (DE3) pLysS. The deduced VMPHMGR contains an open reading frame (ORF) of 1689 bp and generates a protein of 562 amino acids with a calculated molecular mass of 59780 Da and a predicted pI value of 6.63, which is 76% identical to other plant HMGRs. Expression analysis of VMPHMGR transcript by real-time RT-PCR showed that it was differentially regulated. Primers with appropriate restriction sites were used to amplify and facilitate in-frame cloning of the VMPHMGR into pET32(a). The expression of VMPHMGR, in E. coli, fused to N-terminal thioredoxin (Trx·Tag), S·Tag and His·Tag fusion proteins in pET32(a) yielded a partially soluble recombinant protein. This expressed VMPHMGR was subjected to functional enzymatic assay and GCMS analysis of the end products detected dehydromevalonic lactone and pantolactone, which were derivatives of mevalonate lactone.

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Molecular Cloning of a HMG-CoA Reductase Gene from Eucommia ulmoides Oliver

Cited by 33 publications

References 24 publications

Expression of HMGR and corresponding cholesterol content in tissues of two pig breeds

Expression of HMGR and corresponding cholesterol content in tissues of two pig breeds

Functional Analysis of 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase Encoding Genes in Triterpene Saponin-Producing Ginseng

Cloning of 3-Hydroxy-3-methylglutaryl-coenzyme A Reductase Gene from Vanda Mimi Palmer and Its Heterologous Expression in Escherichia coli

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