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Molecules 2016, 21(3), 316; doi:10.3390/molecules21030316

Cloning, Expression Profiling and Functional Analysis of CnHMGS, a Gene Encoding 3-hydroxy-3-Methylglutaryl Coenzyme A Synthase from Chamaemelum nobile

1
School of Biology and Pharmaceutical Engineering, Wuhan Polytechnic University, Wuhan 430023, China
2
College of Horticulture and Gardening, Yangtze University, Jingzhou 434025, Hubei, China
3
Hubei Collaborative Innovation Center of Targeted Antitumor Drug, Jingchu University of Technology, Jingmen 448000, Hubei, China
4
Medical School, Yangtze University, Jingzhou 434025, Hubei, China
*
Authors to whom correspondence should be addressed.
Academic Editor: Tobias A. M. Gulder
Received: 24 January 2016 / Revised: 28 February 2016 / Accepted: 2 March 2016 / Published: 8 March 2016
(This article belongs to the Special Issue Biosynthesis of Natural Products)
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Abstract

Roman chamomile (Chamaemelum nobile L.) is renowned for its production of essential oils, which major components are sesquiterpenoids. As the important enzyme in the sesquiterpenoid biosynthesis pathway, 3-hydroxy-3-methylglutaryl coenzyme A synthase (HMGS) catalyze the crucial step in the mevalonate pathway in plants. To isolate and identify the functional genes involved in the sesquiterpene biosynthesis of C. nobile L., a HMGS gene designated as CnHMGS (GenBank Accession No. KU529969) was cloned from C. nobile. The cDNA sequence of CnHMGS contained a 1377 bp open reading frame encoding a 458-amino-acid protein. The sequence of the CnHMGS protein was highly homologous to those of HMGS proteins from other plant species. Phylogenetic tree analysis revealed that CnHMGS clustered with the HMGS of Asteraceae in the dicotyledon clade. Further functional complementation of CnHMGS in the mutant yeast strain YSC6274 lacking HMGS activity demonstrated that the cloned CnHMGS cDNA encodes a functional HMGS. Transcript profile analysis indicated that CnHMGS was preferentially expressed in flowers and roots of C. nobile. The expression of CnHMGS could be upregulated by exogenous elicitors, including methyl jasmonate and salicylic acid, suggesting that CnHMGS was elicitor-responsive. The characterization and expression analysis of CnHMGS is helpful to understand the biosynthesis of sesquiterpenoid in C. nobile at the molecular level and also provides molecular wealth for the biotechnological improvement of this important medicinal plant. View Full-Text
Keywords: Chamaemelum nobile; sesquiterpenoid biosynthesis; 3-hydroxy-3-methylglutaryl coenzyme A synthase; cloning; expression profile; functional complementation analysis Chamaemelum nobile; sesquiterpenoid biosynthesis; 3-hydroxy-3-methylglutaryl coenzyme A synthase; cloning; expression profile; functional complementation analysis
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MDPI and ACS Style

Cheng, S.; Wang, X.; Xu, F.; Chen, Q.; Tao, T.; Lei, J.; Zhang, W.; Liao, Y.; Chang, J.; Li, X. Cloning, Expression Profiling and Functional Analysis of CnHMGS, a Gene Encoding 3-hydroxy-3-Methylglutaryl Coenzyme A Synthase from Chamaemelum nobile. Molecules 2016, 21, 316.

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