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油桐种子FADX基因的克隆和序列分析     被引量:11

Study on the Cloning and Sequence Analysis of FADX Gene from Vernicia fordii

文献类型:期刊文献

中文题名:油桐种子FADX基因的克隆和序列分析

英文题名:Study on the Cloning and Sequence Analysis of FADX Gene from Vernicia fordii

作者:李元[1] 汪阳东[2] 李鹏[2] 魏建民[1]

第一作者:李元

机构:[1]内蒙古农业大学生物工程学院;[2]中国林业科学研究院亚热带林业研究所

年份:2008

卷号:36

期号:11

起止页码:4753-4755

中文期刊名:安徽农业科学

外文期刊名:Journal of Anhui Agricultural Sciences

收录:北大核心:【北大核心2004】;

基金:浙江省重大科技项目"能源植物种质资源与高能植物品种选育及中试"(2006#2009)(2005C12003);中国林科院科技发展基金项目"生物柴油原料植物油桐脂肪酸合成酶相关基因克隆和功能分析"(2006-2007)

语种:中文

中文关键词:油桐;FADX基因;克隆;生物信息学分析

外文关键词:Verniciafordii; FA DX gene; Clone; Bioinformatic analysis

分类号:S794.3

摘要:[目的]克隆油桐种子FADX基因全长cDNA。对该基因作生物信息学分析,为进一步研究该基因的功能提供参考。[方法]以未成熟的油桐种子为材料,利用改良TRIzoL法提取总RNA,并根据GenBank中已经登录的α桐酸合成酶基因FADX的序列,设计特异性引物;采用RTPCR方法,克隆得到FADX基因全长cDNA,应用Antheprot软件和InterProScan对该基因进行了生物信息学分析。[结果]该序列5'端和3'端非编码区序列长度分别为13、47 bp,含有1个开放阅读框(14~1 174 bp),编码386个氨基酸,含有典型的脂肪酸脱氢酶结构域;相对分子量是44 343.0,理论等电点为8.33。二级结构预测表明,该蛋白α螺旋含量占29%,β折叠占32%,转角占6%。[结论]该蛋白属于脂肪酸脱氢酶。
[Objective] The research aimed to clone full-length cDNA of FADX of Verniciafordii seeds. The bioinformatic analysis of this gene was done, and provided reference for the further research of the function of gene. [Method] Total RNA were successfully extracted by developing Verniciafordii seeds with improved TRIzoL method. Primer was designed according to the FADX sequences recorded in Genbank. Full-length cDNA of FADX was obtained by cloning it with RT -PCR method. Bioinformatic analysis were done by using the software of Antheprot and Interproscan. [Result] The length of 5' side and 3' side unencoded area's sequences were 13 bp and 47 bp, contained an opening reading frame from 14 bp to 1 174 bp which encoded a polypeptide of 386 amino acids, and contained a specific fattic acid dehydrogenase structural domain. Relative molecular weight was 44 343.0, pI was 8.33, and the calculation of secondary structure showed that the protein contained 29% in α - helix, 32% in β-pleated sheet, and 6% inβ-returu.[Conclusion] This protein had the property of fattic acid dehydrogenase.

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