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中国农学通报 ›› 2015, Vol. 31 ›› Issue (32): 54-61.doi: 10.11924/j.issn.1000-6850.casb15070064

所属专题: 生物技术

• 生物技术科学 • 上一篇    下一篇

野巴旦杏AlsCBF基因的克隆及生物信息学分析

李 宁1,2,李 疆1,刘立强1,罗淑萍1   

  1. (1新疆农业大学,乌鲁木齐 830052;2新疆农业科学院,乌鲁木齐 830091)
  • 收稿日期:2015-07-10 修回日期:2015-07-24 接受日期:2015-07-28 出版日期:2015-11-16 发布日期:2015-11-16
  • 通讯作者: 李 疆
  • 基金资助:
    国家自然科学基金项目“新疆野扁桃不同逆境梯度下的繁殖对策与生态适应性研究”(31260186);新疆维吾尔自治区“十二五”重大科技专项项目“新疆特色果树种质资源利用技术研究与示范”(201130102-1);新疆维吾尔自治区果树学重点学科基金。

Cloning and Bioinformatic Analysis of AlsCBF Gene from Amygdalus ledebouriana Schleche

Li Ning1,2, Li Jiang1, Liu Liqiang1, Luo Shuping1   

  1. (1Xinjiang Agricultural University, Urumqi 830052;2Xinjiang Academy of Agricultural Science, Urumqi 830091)
  • Received:2015-07-10 Revised:2015-07-24 Accepted:2015-07-28 Online:2015-11-16 Published:2015-11-16

摘要: 对克隆获得的野巴旦杏基因AlsCBF进行生物信息学分析,从而为该基因的功能鉴定提供理论基础,以期为新疆巴旦杏的抗寒育种提供基因来源。通过采用RT-PCR和RACE方法从野巴旦杏中克隆到植物抗逆途径关键转录因子CBF基因全长并命名为AlsCBF,GenBank登录号为HQ908653。生物信息学分析表明:该基因全长1171 bp,其中编码区长714 bp,编码237个氨基酸,其蛋白的分子式为C1156H1832N332O356S15,相对分子质量为26.5581 kDa,理论等电点为6.76,该蛋白为亲水性蛋白,无信号肽存在;其蛋白质二级结构以α-螺旋、β-折叠和无规卷曲为主。肽链可能含有8处丝氨酸磷酸化位点,1处苏氨酸磷酸化位点。三维结构预测表明其符合AP2结构域模型特点。本研究通过对AlsCBF基因的生物信息学分析,获得了该基因的相关信息,并与已有研究结果进行比对分析,推测该基因在植物抗寒过程中有重要的作用。

关键词: 水稻条纹叶枯病, 水稻条纹叶枯病, 20%寡聚酸碘, 田间防效

Abstract: AlsCBF gene from the Amygdalus ledebouriana Schleche was cloned and the gene related information was analyzed. Thus the study could provide a theoretical basis for the identification of gene function, and provide a source of gene for plant cold-resistance breeding. The full-length of cDNA of plant defense pathway transcription factor was isolated from Amygdalus ledebouriana Schleche by RT-PCR and RACE, which was named AlsCBF and submitted to GenBank (Accession number: HQ908653). According to the bioinformatics analysis, the cloned AlsCBF gene was 1171 bp including code segment 714 bp, encoding 237 amino acids, the predicted AlsCBF protein’s molecular formula was C1156H1832N332O356S15, whose relative molecular mass was 26.5581 kDa and isoelectric point was 6.76. It was predicted that this protein was hydrophilic protein, and there was no signal peptide. Characteristic prediction results indicated that the secondary structure of AlsCBF protein mainly included α-helix, β-sheet and random coil. And there were eight serine sites, one threonine sites. Three-dimensional structure predicted that AlsCBF protein confirmed the characteristics of AP2 domain model. In this study, related information was obtained by means of bioinformatics analysis of AlsCBF gene, and through comparing with previous studies, the gene played an important role in the plant cold-resistance.