绵羊及相关物种去乙酰化酶1的理化性质和蛋白结构预测  

Bioinformatics Analysis on the Physiochemical Property and Protein Structure of Ovine and Related Species Sirtuin 1

作　　者：景炅婕[1] 张静[1] 贾夏丽[1] 梁琛[1] 刘建华[1] 潘洋洋[1] 张方[1] 胡子乔 任端阳 刘文忠[1] 

机构地区：[1]山西农业大学动物科技学院,山西太谷030801

出　　处：《山西农业大学学报（自然科学版）》2015年第2期124-132,共9页Journal of Shanxi Agricultural University(Natural Science Edition)

基　　金：国家自然科学基金项目(31372292)

摘　　要：为深入研究SIRT1基因及其编码蛋白的结构和功能,特别是在各信号通路中的作用,本文基于NCBI发布的包括绵羊在内的9个物种的SIRT1基因的核苷酸和蛋白质序列,采用生物信息学方法分析SIRT1蛋白的理化性质和蛋白结构,预测了绵羊SIRT1蛋白的结构和翻译后修饰位点。结果表明,不同物种SIRT1蛋白的理化性质基本一致。绵羊SIRT1是一种接近于中性的亲水性脂溶蛋白,预测其有40个潜在的O-糖基化位点、2个N-糖基化位点、33个磷酸化位点、18个乙酰化修饰位点、11个泛素化修饰位点和3个类泛素化修饰位点。这些结果为进一步研究SIRT1的功能和表达调控奠定了科学依据。For further research on the structure and function of SIRT1 gene and its encoding protein, especially in the role of each signal pathway, we analyzed the physiochemical property of SIRT1 based on the nucleotide and amino acid sequences in nine species in NCBI GenBank databases. Structure and post-translational modification sites of ovine S1RT1 were predicted by bioinformatics methods. The results showed that the physiochemical properties of SIRT1 in all the nine species were similar. Ovine SIRT1 was nearly a neutral hydrophilic liposoluble protein. The post-transla tional modification sites predicted in ovine SIRT1 included 40 O-glycosylation, two N-glycosylation, 33 phosphoryla- tion, 18 acetylation, 11 ubiquitinoylation and three SUMO sites. These results lay a scientific foundation for further study on the function and expression regulation of ovine SIRT1.

关 键 词：绵羊 去乙酰化酶1 生物信息学分析 蛋白结构 

分 类 号：Q7[生物学—分子生物学] Q55