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园艺学报 ›› 2009, Vol. 36 ›› Issue (12): 1799-1804.

• 观赏植物 • 上一篇    下一篇

蝴蝶兰多酚氧化酶基因克隆及序列分析

许传俊1, 2 ;周文灵1 ; 陈冬茵1;赖艳艳1 ;李玲1*   

  1. (1 华南师范大学生命科学学院, 广东省植物发育生物工程重点实验室, 广州510631; 2福建省亚热带植物研究所, 福建厦门 361006)
  • 收稿日期:2009-05-18 修回日期:2009-11-04 出版日期:2009-12-25 发布日期:2009-12-25
  • 通讯作者: 李玲

Molecular Cloning and Ana lysis of Homological Gene PPO from Phalaenopsis

XU Chuan-jun1, 2 ; ZHOU Wen-ling1;CHEN Dong-yin1; LA I Yan-yan1; LI Ling1*   

  1. 1Guangdong Key Lab of Biotechnology for Plant Development, College of Life Science, South China Normal University, Guangzhou 510631, China; 2 Fujian Institute of Subtropical Botany, Xiamen, Fujian 361006, China
  • Received:2009-05-18 Revised:2009-11-04 Online:2009-12-25 Published:2009-12-25
  • Contact: LI Ling

摘要: 利用RT-PCR和RACE技术从蝴蝶兰中克隆的多酚氧化酶同源基因, 命名为PhPPO, 其cDNA
全长1 851 bp, 完整的编码框长1 647 bp, 编码549个氨基酸, 生物信息学分析表明其具有酪氨酸酶家族的特征, 具有保守的CuA 和CuB 结合区, 以及向叶绿体运输的导肽结构。将其亚克隆到表达载体pPRoEXHTa上, 在BL21 (DE3) 进行表达, 经ITPG诱导, 获得蝴蝶兰PPO原核表达蛋白。

关键词: 蝴蝶兰, 多酚氧化酶, 基因, 克隆, 褐变, 原核表达

Abstract: The PPO homolog, designated as PhPPO, was cloned from Phalaenopsis by RT-PCR and RACE. The full length cDNA of PhPPO was 1 851 bp, has an open read frame of 1 647 bp, encoding a protein of 549 amino acids. Bioinformatic analysis showed that PhPPO protein shared the characters of tryosinase family, bearing the conserved CuA and CuB binding domains and a chloroplast-targeting leading peptide.Prokaryotic expression vectors based on pPRoEXHTa had been constructed and then exp ressed in the BL21 (DE3) induced with ITPG.

Key words: Phalaenopsis, PPO, gene, clone, browning, prokaryotic expression

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