割手密谷胱甘肽硫转移酶基因SsGST的克隆与生物信息学分析  

Cloning and bioinformatics analysis of glutathione S-transferase gene SsGST in Saccharum spontaneum L.

作　　者：徐磊[1] 胡小文[1] 姚艳丽[1] 邢淑莲[1] 刘洋[1] 

机构地区：[1]中国热带农业科学院湛江实验站,广东湛江524013

出　　处：《广东农业科学》2015年第18期14-19,共6页Guangdong Agricultural Sciences

基　　金：中央级公益性科研院所基本科研业务费专项(ITBB120504);中国热带农业科学院湛江实验站科研启动专项(zjky201504)

摘　　要：为克隆割手密谷胱甘肽硫转移酶基因,采用电子克隆和RT-PCR技术获得了1个割手密GST基因,命名为Ss GST,并对其进行生物信息学分析。序列分析表明,割手密Ss GST基因c DNA全长702 bp,编码224个氨基酸,蛋白分子式为C1119H1756N300O327S5,预测蛋白质分子量为24.8 ku,等电点为6.21。蛋白疏水性分析表明Ss GST蛋白为亲水性蛋白。保守结构域预测表明Ss GST蛋白具有GST-N和GST-C结构域。Ss GST蛋白序列与玉米、高粱、谷子和甘蔗等植物的GST蛋白序列相似性较高,系统进化树分析表明,Ss GST蛋白与玉米GST蛋白亲缘关系最近。To clone glutathione S-transferase gene（GST）of Saccharum spontaneum L. In this study,a GST gene from S. spontaneum L. was cloned by in silico cloning and RT-PCR,named as SsGST,characteristics of SsGST gene were analyzed using bioinformatics tools. Sequence analysis showed that the full length c DNA of SsGST was 702 bp,which encoded 224 amino acids. The predicted protein molecular formula was C1119H1756N300O327S5,whose molecular mass was 24.8 ku and isoelectric point was 6.21. Hydrophobic analysis showed that SsGST protein was a hydrophilic protein. Conserved domain prediction indicated that SsGST protein had GST-N domain and GST-C domain. SsGST protein sequence had higher similarities with the GST protein sequence of maize,sorghum,foxtail millet and sugarcane and so on. Phylogenetic analysis showed that SsGST protein was close to GST protein of maize.

关 键 词：割手密 GST基因 电子克隆 RT-PCR 生物信息学 

分 类 号：S566.1[农业科学—作物学]