Functional Characterization of Cinnamyl Alcohol Dehydrogenase during Developmental Stages and under Various Stress Conditions in Kenaf (Hibiscus cannabinus L.)

BioResources

Hyeun-Jong Bae¹  Seonjoo Park²  Jun Young Chung³  Inhwan Bae⁴  Hanhong Bae⁵  Bosung Choi⁶ 

[1] Ajou University, School of Medicine;Department of Bioenergy Science and Technology, Chonnam National University;Korea, Republic Of;Korea, Republic Of;College of Pharmacy, Chungang University;School of Biotechnology, Yeungnam University;

关键词: Cinnamyl alcohol dehydrogenase (CAD);    Abiotic stress;    Lignin;    Enzyme assay;    Real-time PCR;   

DOI  :  10.15376/biores.11.1.105-125

来源: DOAJ

【 摘 要 】

In this study, the entire gene encoding cinnamyl alcohol dehydrogenase in kenaf (HcCAD2) was cloned and characterized. CAD is a key enzyme in the last step of lignin biosynthesis. The full-length HcCAD ortholog is composed of a 1,074-bp open reading frame (ORF) encoding 357 amino acids (KM044582). BlastP and a phylogenetic study revealed that the deduced amino acid sequences share the highest similarity with Gossypium hirsutum (ABZ01817) (89%). Upon real-time PCR analysis, HcCAD1 (HM151380) and HcCAD2 were highly up-regulated in 4-week-old stem and mature flower tissues, which was matched with histochemical staining and lignin component analysis. The expression patterns of the two genes differed in response to wound, cold, NaCl, SA, H2O2, ABA, MeJA, and drought. CAD enzyme activity was measured with various aldehydes as substrates to form corresponding alcohols. The results indicated that the preferred substrates were coniferyl and sinapyl aldehydes with high catalytic efficiency.

【 授权许可】

Unknown