齿肋赤藓热激蛋白60基因的电子克隆和生物信息学分析  

Electronic cloning and characterization of HSP60 gene from Syntrichia caninervis using bioinformatics tool

作　　者：蔡明[1,2] 高贝[1,2] 张道远[1] 

机构地区：[1]中国科学院干旱区生物地理与生物资源重点实验室,中国科学院新疆生态与地理研究所,新疆乌鲁木齐830011 [2]中国科学院大学,北京100049

出　　处：《生物信息学》2013年第3期216-223,共8页Chinese Journal of Bioinformatics

基　　金：国家自然科学基金资助项目(U1170304)

摘　　要：用电子克隆方法获得耐旱苔藓齿肋赤藓的热激蛋白60基因,采用生物信息学方法,对该基因编码蛋白从氨基酸组成、结构保守域、理化性质、信号肽、疏水性/亲水性、亚细胞定位、跨膜结构域、二级结构、功能域、活性位点、及同源性等方面进行了预测和分析。结果表明:齿肋赤藓热激蛋白60基因全长1 841bp,开放阅读框1 581bp,编码526个氨基酸残基;编码蛋白含有GroEL保守域,是chaperon-like superfamily家族;亚细胞定位分析显示,编码蛋白位于内质网中;活性化位点分析表明,编码蛋白存在6类活性位点;同源性分析表明,齿肋赤藓热激蛋白60与小立碗藓预测的HSP60同源性最高,达到92%,与卷柏的HSP60次之,同源性达88.83%。研究结果为该基因的实验克隆奠定基础。A novel heat shock protein 60 from Syntrichia caninervis was cloned in silico based on the transcriptome database of Syntrichia caninervis. Some characters of amino acids encoded by ScHSP60 gene, include the composi- tion of amino acid sequence, conserved domain, physical and chemical properties, Signal P-NN, hydrophobicity/ hydrophilicity, subcellular localization, transmembrane domain, secondary structure of protein, the functional do- main, signatures plus the homologies were analyzed by bioinformatics tool. Bioinformatic analysis showed that the full-length HSP60 gene from S. caninervis was 1 841bp, and it contained a complete ORF which encoded 526 ami- no acids. In addition, ScHSP60 contained a GroEL domain and belonged to chaperon-like superfamily. Further- more, the encoded protein located in endoplasmic reticulum and there were six signatures in the encoded protein. Homology comparison and phylogenetic analysis showed that the amino acid encode by ScHSP60 was highly homolo- gous with the predicted HSP60 in Physcomitrella patens and that in Selaginella tamariscina, with homologies of 92% and 88.83% ,respectivelly. The above results will provide basis for molecular cloning of HSP60 gene in S. caninervis.

关 键 词：齿肋赤藓 热激蛋白60 电子克隆 生物信息学分析 

分 类 号：Q785[生物学—分子生物学]