文献类型：期刊文献

中文题名：不同植物中推定蓖麻烯合酶基因的生物信息学分析

英文题名：Bioinformatics Analysis of Casbene Synthase Genes in Different Plants

作者：刘洪伟[1] 杨艳芳[1] 熊王丹[2] 吴平治[2] 吴国江[2] 邱德有[1]

第一作者：刘洪伟

机构：[1]林木遗传育种国家重点实验室,中国林业科学研究院林业研究所,北京100091;[2]中国科学院华南植物园植物资源保护与可持续利用重点实验室,广州510650

年份：2016

卷号：36

期号：4

起止页码：605-612

中文期刊名：植物研究

外文期刊名：Bulletin of Botanical Research

收录：CSTPCD;;北大核心:【北大核心2014】；CSCD:【CSCD2015_2016】；

基金：国家自然科学基金(31270705);中国林业科学研究院林业研究所中央级公益性科研院所基本科研业务费专项(RIF2014-01)~~

语种：中文

中文关键词：巴豆烷;蓖麻烯合酶;生物信息学

外文关键词：tigliane ; casbene synthase ： bioinformatics

分类号：S565.6

摘要：利用GenBank中已登录的完整的麻风树、乳浆大戟、蓖麻和乌桕中的13个蓖麻烯合酶（Casbenesyn．thase，CS；EC4．6．1．7）基因序列，通过生物信息学方法对其核酸及氨基酸序列、组成成分、导肽、信号肽、跨膜结构域、疏水性／亲水性、蛋白质的二级结构、三级结构及功能域等进行了分析预测。结果表明，13个CS基因的ORF长度均在1647—1845bp，蛋白分子量均在63．0～70．8kD，终止密码子为TGA或TAA，理论等电点均小于7．0，表明CS蛋白呈酸性。氨基酸含量最高的均为亮氨酸。核苷酸同源性比较分析表明，CS基因主要分为两类。导肽预测发现其中6个CS具有导肽，均为叶绿体导肽。信号肽和扩模结构域预测发现这些CS不存在信号肽和跨膜结构域，肽链整体呈现为亲水性。这些CS的主要二级结构元件为α-螺旋，并且都包含两个萜类合酶功能域。以上研究为进一步探索嬲基因的功能提供一定理论依据。
We used bioinformatics to study registered in the GenBank from Euphorbia 13 casbene synthase （ CS ; EC 4.6. esula, Jatropha curcas L. , Ricinus 1.7） full-length gene sequences communis and Triadica sebifera, and predicted the composition of nucleic acid and amino acid sequences, leader peptides, signal peptide, trans- membrane topological structure, hydrophobicity or hydropbilicity, the secondary and tertiary structure as well as the function domains. The 13 genes encoding ORFs were 1 647 - 1 845 bp, the molecular weight of the 13 predicted proteins were 63.0 - 70. 8 kD, and the term/nation codons were TGA or TAA. The theoretical isoelectric points of the 13 proteins were lower than 7.0, which suggested the most contented amino acid. By the homologous alignment of nucleic that CS proteins were acidic. Leu was acid, CS genes were divided into two groups. The prediction of leading peptides showed that at least 6 CSs had leader peptide （chloroplast leader peptide mainly） in common. All 13 CSs had no signal peptide and trans-membrane topological structure in and the peptide chains were hydrophilicity, a-helix was the dominant secondary structure constructional element of the 13 proteins which contained two terpenoid synthases function domains.