Chinese Bulletin of Botany ›› 2024, Vol. 59 ›› Issue (2): 204-216.DOI: 10.11983/CBB23109  cstr: 32102.14.CBB23109

• EXPERIMENTAL COMMUNICATIONS • Previous Articles     Next Articles

Sequence Identification and Functional Analysis of Cinnamyl Alcohol Dehydrogenase Gene from Agropyron mongolicum

Heping Wang1,2, Zhen Sun2, Yuchen Liu2, Yanlong Su2, Jinyu Du2,5, Yan Zhao5, Hongbo Zhao1, Zhaoming Wang6, Feng Yuan6, Yaling Liu6, Zhenying Wu2,3,4, Feng He2,3,4,*(), Chunxiang Fu2,3,4,*()   

  1. 1College of Horticulture, South China Agricultural University, Guangzhou 510642, China
    2Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao 266101, China
    3Shandong Energy Institute, Qingdao 266101, China
    4Qingdao New Energy Shandong Laboratory, Qingdao 266101, China
    5Key Laboratory of Grassland Resources, Ministry of Education/Key Laboratory of Forage Cultivation, Processing and Efficient Utilization of Ministry of Agriculture and Rural Affairs/College of Grassland, Resource and Environmental Science, Inner Mongolia Agricultural University, Hohhot 010018, China
    6Key Laboratory of Forage Breeding and Seed Production in Inner Mongolia Autonomous Region, Hohhot 010018, China
  • Received:2023-08-09 Accepted:2023-12-19 Online:2024-03-10 Published:2024-03-10
  • Contact: * E-mail: hefeng@qibebt.ac.cn; fucx@qibebt.ac.cn

Abstract: As an essential enzyme in plant secondary metabolism, cinnamyl alcohol dehydrogenase (CAD) plays a key role in regulating plant growth and development, as well as biological/abiotic stress resistance. Agropyron mongolicum is a traditional forage grass widely distributed in the desert grassland areas of northern China, which exhibited high tolerance to drought and cold stresses. To explore the role of cinnamyl alcohol dehydrogenase in A. mongolicum, in this study, a CAD gene was identified from the full-length transcriptome data of A. mongolicum and subsequentially analyzed in vitro. The 1 083 bp coding sequence of AmCAD encodes 361 amino acids, which has typical conserved CAD region containing two Zn2+ binding motifs and NADP(H) cofactor binding motifs, belongs to the typical CAD protein, and its three-dimensional structure is similar to AtCAD5. AmCAD is highly expressed in the stem. The AmCAD recombinant protein showed a robust catalytic ability to different cinnamaldehyde substrates, with the highest substrate affinity of coniferyl aldehyde and sinapaldehyde. Under drought stress condition, the expression level of AmCAD was significantly induced, indicating a potential function of this gene in stress tolerance. The experimental results indicate that AmCAD may play an important role in lignin biosynthesis and drought stress tolerance in A. mongolicum. Our research provided potentially valuable genetic resources for molecular breeding of A. mongolicum to improve biomass quality and stress resistance.

Key words: Agropyron mongolicum, cinnamyl alcohol dehydrogenase, lignin, drought resistance