Identification of 3-hydroxy-3-methylglutaryl monoacyl-coenzyme A reductase (HMGR) associated with the synthesis of terpenoids in Santalum album L

文献类型： 外文期刊

第一作者： Niu, Meiyun

作者： Niu, Meiyun;Zhang, Xinhua;Zhang, Yueya;Li, Jianrong;Xiong, Yuping;Li, Yuan;Bian, Zhan;Ma, Guohua;Niu, Meiyun;Yan, Haifeng;Zhang, Yueya;Yan, Haifeng;da Silva, Jaime A. Teixeira

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关键词： MVA pathway; Prokaryotic protein expression; qRT-PCR; Sandalwood; SaHMGRs; Sesquiterpenes

期刊名称：GENE （ 影响因子：2.4； 五年影响因子：2.8 ）

ISSN： 0378-1119

年卷期： 2025 年 939 卷

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收录情况： SCI

摘要： Santalum album is an economically important plant in the craft, spices and medicine industries. The main chemical constituents found in sandalwood essential oils are sesquiterpenes. 3-Hydroxy-3-methylglutaryl monoacyl-coenzyme A reductase (HMGR) is one of the rate-limiting enzymes required for the synthesis of sandal sesquiterpenes, but there are no studies on the HMGR gene in S. album. In this study, the full-length ORFs of the upper rate-limiting enzyme genes SaHMGR1 and SaHMGR2, which lie upstream of the MVA metabolic pathway of sandal sesquiterpenes, were cloned for the first time. Bioinformatics and phylogenetic analyses were conducted. The results showed that Sa HMGR1 and Sa HMGR2 had typical domains of HMGR class I enzymes in the HMGR superfamily, including four catalytic sites, six NADPH-binding sites, five substrate binding regions, four inhibitor binding sites, and several dimer interface regions. A phylogenetic analysis showed that SaHMGR1 and SaHMGR2 were highly conserved relative to corresponding genes in other plants. An analysis of subcellular localization showed that these SaHMGR genes were located in the endoplasmic reticulum. SaHMGR1 and SaHMGR2 were detected by real-time PCR in roots, sapwood, heartwood, young leaves, mature leaves and twigs. Highest expression was in roots. SaHMGR1 expression was higher in mature leaves than in heartwood while SaHMGR2 expression was lower in mature leaves than in heartwood. Expression in Escherichia coli strain DH5 alpha with plasmid pET-32a (+) was also used to verify the functionality of both HMGR proteins, which catalyzed the formation of MVA from HMG-CoA. In E. coli, the enzymatic activity of Sa HMGR1 was higher than that of Sa HMGR2. These findings provide a basis for further studies on the function of SaHMGR genes and the regulation of sesquiterpene biosynthesis in S. album.

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