关键词: 茶树, 鸟氨酸转氨酶, Csδ-OAT, 克隆, 表达分析

Abstract: Degenerate primers were designed according to the known conserved regions of Ornithine- δ-aminotransferase gene（δ-OAT），and the complete cDNA sequence of δ-OAT was firstly cloned from Camellia sinensis using RT-PCR and RACE technologies. The cDNA was termed Csδ-OAT（GenBank accession KJ641844）and its full-length was 1 865 bp encoding a protein of 473 amino acids. The molecular weight of Csδ-OAT was 52.3 kD and theoretical isoelectric point was 7.19. The BLAST results showed that the functional domain of Csδ-OAT is highly conserved with a typical PLP binding site. Phylogenetic analysis of plant δ-OAT reveals that the evolution of Csδ-OAT corresponds with traditional biological classification. QRT-PCR analysis results showed that the expression of Csδ-OAT has obvious tissue specificity，and it was higher in flower，followed by leaves，but lower in other tissues. Moreover，we found that the expression of Csδ-OAT is induced by different abiotic stresses，including low- temperature，high salinity，ABA，drought and oxidative stresses，implying that Csδ-OAT is involved in responding to abiotic stress in plants.

Key words: tea plant, ornithine-δ-aminotransferase, Csδ-OAT, cloning, expression analysis