Cloning and characterization of phenylalanine ammonia-lyase in medicinal Epimedium species

Phenylalanine ammonia-lyase (PAL) plays an important role in the phenylpropanoid pathway and in accumulation of major secondary metabolites in medicinal Epimedium species, including icariin, epimedin A, epimedin B, and epimedin C (hereafter designated as active components). In this study, three Epim...

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Published inPlant cell, tissue and organ culture Vol. 113; no. 2; pp. 257 - 267
Main Authors Zeng, Shaohua, Liu, Yilan, Zou, Caiyun, Huang, Wenjun, Wang, Ying
Format Journal Article
LanguageEnglish
Published Dordrecht Springer Netherlands 01.05.2013
Springer Nature B.V
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Summary:Phenylalanine ammonia-lyase (PAL) plays an important role in the phenylpropanoid pathway and in accumulation of major secondary metabolites in medicinal Epimedium species, including icariin, epimedin A, epimedin B, and epimedin C (hereafter designated as active components). In this study, three Epimedium sagittatum PALs ( EsPALs ) mRNA sequences, designated respectively as EsPAL1 , EsPAL2 and EsPAL3 deduced to encode 708, 716, and 739 amino acids, were isolated and characterized. Based on sequence and phylogenetic analyses, EsPAL1 was found to be closer to EsPAL2 than to EsPAL3 . Spatio-temporal expression profiles and metabolic accumulation profiles revealed that EsPAL3 was highly expressed in flavonoid-enriched tissues and leaves at certain developmental stages along with high levels of active components, while EsPAL1 was highly expressed in leathery leaves along with high lignin content. Under light stress, the total flavonoid content was enhanced by 100 μM phytohormones tested or 5 % sucrose through upregulating different EsPAL isoform(s). Our findings have laid a solid foundation for improving the content of bioactive components in Epimedium via metabolically engineering EsPAL .
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ISSN:0167-6857
1573-5044
DOI:10.1007/s11240-012-0265-z