茶叶科学2016，Vol.36Issue(4)：405-413,9.
茶树丙氨酸氨基转移酶基因的克隆与表达分析
Cloning and Expression Analysis of Alanine Aminotransferase Gene in Camellia sinensis
摘要
Abstract
Alanine Aminotransferase (AlaAT) is a critical enzyme involved in carbohydrate and nitrogen metabolisms. In this study, a cDNA (1 747 bp) with a complete ORF (1 626 bp) of AlaAT1 was isolated from tea plant (Camellia sinensis). The cDNA encodes a protein with 541 amino acids, which has a molecular mass of 59.4 kD and a theoretical isoelectric point (pI) of 5.82. The deduced sequence of protein CsAlaAT1 shared 84% similarity with AlaAT1 in Arabidopsis thaliana, which contains a highly-conserved pyridoxal 5′-phosphate binding site. Secondary structure prediction showed that the CsAlaAT1 was comprised of alpha helix (40.67%), random coil (29.57%), beta turn (13.68%) and extended strand (16.08%), localized in mitochondrion and had no signal peptide or transmembrane structure. The expression levels of CsAlaAT1 in various tissues and its responses to different N concentration were investigated by real-time fluorescent quantitative RT-PCR. The results of RT-PCR showed that CsAlaAT1 expressed in all tissues of tea plant and the highest transcript level was observed in roots. The transcript abundance of CsAlaAT1 was up-regulated by N in both shoots and mature leaves, especially under high N condition. Interestingly, the expression of CsAlaAT1 in roots was highly induced high N condition, but showed an opposite trend under low N treatment for 24 h.关键词
茶树/丙氨酸氨基转移酶/克隆/表达/氮素诱导Key words
tea plant (Camellia sinensis)/Alanine aminotransferase/cloning/expression/nitrogen induction分类
农业科技引用本文复制引用
白培贤,王丽鸳,韦康,阮丽,成浩,张芬,张成才..茶树丙氨酸氨基转移酶基因的克隆与表达分析[J].茶叶科学,2016,36(4):405-413,9.基金项目
国家自然科学基金（31570695）、国家现代农业产业技术体系（nycytx-23）、浙江省农业新品种选育重点专项（2012C2905-4）。 （）
