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Journal of Tea Science ›› 2016, Vol. 36 ›› Issue (4): 405-413.doi: 10.13305/j.cnki.jts.2016.04.009

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Cloning and Expression Analysis of Alanine Aminotransferase Gene in Camellia sinensis

BAI Peixian1,2, WANG Liyuan1,*, WEI Kang1, RUAN Li1, CHENG Hao1, ZHANG Fen1,2, ZHANG Chengcai1,2   

  1. 1. Tea Research Institute, Chinese Academy of Agricultural Sciences, National Center for Tea Improvement, Key Laboratory of Tea Biology and Resource Utilization, Ministry of Agriculture, Hangzhou 310008, China;
    2. Graduate School of Chinese Academy of Agricultural Sciences, Beijing 100081, China
  • Received:2016-03-24 Published:2019-08-26

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.

Key words: tea plant (Camellia sinensis), Alanine aminotransferase, cloning, expression, nitrogen induction

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