| 红鳍东方鲀组织蛋白酶L基因的电子克隆及序列分析 |
| |
| 引用本文： | 梁静真,饶颖竹,陈蓉,邓富琳.红鳍东方鲀组织蛋白酶L基因的电子克隆及序列分析[J].南方农业学报,2012,43(10):1569-1574. |
| |
| 作者姓名： | 梁静真 饶颖竹 陈蓉 邓富琳 |
| |
| 作者单位： | 湛江师范学院生命科学与技术学院/湛江师范学院经济动物资源利用与保护研究所,广东湛江524048中山大学生命科学学院寄生生物研究中心暨有害生物控制与生物资源利用国家重点实验室,广州510275湛江师范学院生命科学与技术学院/湛江师范学院经济动物资源利用与保护研究所,广东湛江,524048 |
| |
| 基金项目： | 国家星火计划引导项目(2011GA780033,2008GA780049);广东省科技攻关项目(2011B020307008);湛江师范学院博士专项项目(ZL0703,ZL0704);南海水产经济动物增养殖广东普通高校重点实验室开放项目(2011GDU026) |
| |
| 摘 要： | 目的]采用电子克隆技术克隆红鳍东方鲀组织蛋白酶L基因,并应用生物信息学技术分析其推导氨基酸的序列特征,为进一步探索其在免疫功能中的作用奠定基础.方法]以斑马鱼的组织蛋白酶L核苷酸序列(Y08321.1)为探针,对红鳍东方鲀基因组数据库进行BLASTn分析,将检索到的匹配结果进行碱基3′端及5′端的适当延长,用DNAssist预测其编码信息;然后从GenBank获取若干物种组织蛋白酶L序列,用DNASTAR软件进行比对.结果]红鳍东方鲀组织蛋白酶L基因全长2005 bp,含7个外显子和6个内含子;包含编码336个氨基酸的开放阅读框(1011 bp);其推导的氨基酸序列具有组织蛋白酶L所特有的氨基酸保守结构域(ERWNIN和GNFD)及由Cys25、His159和Ash175残基组成的保守活性位点,与青鳉、鲤鱼的组织蛋白酶L基因具有较高的序列一致性.结论]红鳍东方鲀组织蛋白酶L的一些结构域和催化活性位点在进化过程中比较保守,与鱼类物种来源的组织蛋白酶L在氨基酸水平上一致性较高,在进化上亲缘关系较近.
|
| 关 键 词： | 红鳍东方鲀 组织蛋白酶L 生物信息学 电子克隆 序列分析 |
In silico cloning and sequence analysis of cathepsin L gene in Takifugu rubripes |
| |
| LIANG Jing-zhen,RAO Ying-zhu,CHEN Rong,DENG Fu-lin.In silico cloning and sequence analysis of cathepsin L gene in Takifugu rubripes[J].Journal of Southern Agriculture,2012,43(10):1569-1574. |
| |
| Authors: | LIANG Jing-zhen RAO Ying-zhu CHEN Rong DENG Fu-lin |
| |
| Institution: | 1 (1 Life Science and Technology School, Zhanjiang Normal University/Institute of Economic Animals Resource Utilization and Conservation, Zhanjiang, Guangdong 524048, China; 2 State Key Laboratory of Biocontrol and Center for Parasitic Organisms, School of Life Sciences, Sun Yat-sen University, Guangzhou 510275, China) |
| |
| Abstract: | 【Objective】This research aimed to clone the cathepsin L gene from Takifugu rubripes through in Silico cloning and to analyze the characteristics of the predicted amino acid sequence by the bioinformatics methods in order to provide bases for further studies related to the function of cathepsin L in the immunity system. 【Method】BLASTn was processed in the database of T. rubripes using the cathepsin L nucleotide sequence of Zebrafish （Y08321.1） as a probe； the matching sequences were subsequentially extended in the 3' and 5' direction， respectively. The coding information was estimated by DNAssist. An alignment with other cathepsin L sequences from GenBank was performed by DNASTAR. 【Result】 The predicted cathepsin L gene was 2005 bp in length， which contained 7 exons and 6 introns. It also contained an open reading frame （ORF） of 1011 bp encoding a polypeptide of 336 amino acids. The predicted amino acid sequence contained a catalytic triad formed by Cys25， His159， Asn175， and the conserved ERWNIN， GNFD motifs， which were all characteristics of cathepsin L. Homology analysis revealed that the deduced amino acid sequence of T. rubripes cathepsin L shared high percentage of identity compared to other species viz.， Oryzias latipes and carp. 【Conclusion】The motifs and catalytic active sites of T. rubripes cathepsin L were rather conserved. The T. rubripes cathepsin L shared high percentage of identity with other fish cathepsin L in the amino acid level， which was also close to other fish cathepsin L in respect to evolutionary developments. |
| |
| Keywords: | |
| 本文献已被 CNKI 等数据库收录！ |
| 点击此处可从《南方农业学报》浏览原始摘要信息 |
| 点击此处可从《南方农业学报》下载免费的PDF全文 |
|
