小鼠骨骼肌肌球蛋白重链生物信息学特性比较  

Comparison of MyHCs of Mus musculus based on bioinformatics methods

作　　者：史银斌[1,2] 孙丽君[2] 奚耕思[1] SHI Yinbin SUN Lijun XI Gengsi(School of Life Sciences School of Physical Education, Shaanxi Normal University, Xi＇an 710119, Shaanxi, China)

机构地区：[1]陕西师范大学生命科学学院 [2]陕西师范大学体育学院,陕西西安710119

出　　处：《陕西师范大学学报（自然科学版）》2017年第4期71-78,共8页Journal of Shaanxi Normal University：Natural Science Edition

基　　金：国家自然科学基金(11502134);中央高校基本科研业务费专项资金(GK201504012);陕西师范大学体育学院青年教师科研基金(20151604)

摘　　要：应用生物信息学软件对MyHCs蛋白不同亚型的基因序列进行比较分析,并根据比对结果建构系统进化树,对其蛋白进行结构与功能分析。结果表明:MyHC在体内以多种蛋白形式存在,其理化性质基本一致;可能的翻译后糖基化修饰多为N-糖基化,且都存在较多个位点,具有明显的Motor-domain Superfamily、MYSc、Myosin tail 1等多重保守结构域,并且N末端具有多个ATP结合位点等特异性功能区域。MyHCs蛋白二级结构均以α螺旋为主,辅以折叠和无规则卷曲等形式,其三级结构模式相似;系统进化树显示,MyHCⅡb、MyHCⅠ蛋白与其他蛋白有着较大的序列差异及较远的进化关系。MyHC蛋白不同亚型结构之间的细微差异为MyHC的重塑提供可能,进而在结构上与其功能相适应。The isoforms of Myosin heavy chain（MyHC）expressed in adult skeletal muscle fibers were analyzed by using of bioinformatics tools, and then the evolutionary tree was built according to the result of correlative sequence alignments, the purpose of the work is to analyze structure and function of the proteins. The results show that there are various forms of MyHC in skeletal muscle of adult mice, and few differences in the physicochemical characteristics. Relatively more glycosylation sites are found and the main glycosylation sites are N-giycosylation sites. Moreo- ver, mouse MyHCs contain multiple conservative domains such as motor-domain superfamily, MYSc, Myosin tail 1, etc.. Three states exist in their secondary structures： helix, coil and strand, their tertiary structures are similar. The phylogenetic tree results show that MyHC 1I b and MyHC I might be more original compared with other MyHCs because of its larger difference of sequences and farther branch length. The plasticity of muscles becomes possible as a result of various forms of MyHC and few differences in the structure.

关 键 词：肌球蛋白重链 序列比对 结构与功能分析 生物信息学 

分 类 号：Q811.4[生物学—生物工程]