Molecular cloning and characterization of the cinnamate 4-hydroxylase gene from Eupatorium adenophorum

文献类型： 外文期刊

第一作者： Chen, Lijuan

作者： Chen, Lijuan;Lin, Yi;Chen, Lijuan;Guo, Huiming;Wu, Yulun;Cheng, Hongmei

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关键词： cinnamate-4-hydroxylase;enzymatic genes;Eupatorium adenophorum;phenylpropanoid metabolism

期刊名称：WEED BIOLOGY AND MANAGEMENT （ 影响因子：1.059； 五年影响因子：1.276 ）

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收录情况： SCI

摘要： Cinnamate-4-hydroxylase (CA4H), a cytochrome P450-dependent monooxygenase, plays crucial roles in phenylpropanoid metabolism and plant defense. Previously, the authors showed that the expression of CA4H was induced in response to an allelopathic substance in Eupatorium adenophorum. Here, the full-length cDNA of EaCA4H was cloned by using rapid amplification of cDNA ends. The 1518 bp open reading frame of EaCA4H was deduced to encode a protein of 505 amino acid residues. Like other CA4H proteins, the predicted EaCA4H polypeptides contained conserved domains of cytochrome P450. A Southern blot analysis indicated that at least five copies of EaCA4H exists in the genome of E. adenophorum. Subcellular localization revealed nuclear-localized EaCA4H-green fluorescent protein fusion protein in onion epidermal cells. Heterologous silencing of endogenous CA4H in tobacco by a conserved EaCA4H fragment resulted in reduced expressions of key enzymatic genes and the production of downstream flavonoids in the phenylpropanoid pathway. Intriguingly, similar effects were observed in transgenic tobacco plants overexpressing EaCA4H. Altogether, the results indicate that the disturbed expression of CA4H in plants leads to relatively low expression levels of key enzymatic genes and the accumulation of the flavonoids that are involved in phenylpropanoid metabolism.

分类号： S4

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