草鱼CNBP的分子特征及其进化分析  被引量:1

Molecular Characterization and Evolution of Ctenopharyngodon idella CNBP

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作  者:陈琼[1] 林刚[1] 王娜[1] 胡成钰[1] 

机构地区:[1]南昌大学生命科学学院,南昌330031

出  处:《动物学杂志》2008年第6期97-102,共6页Chinese Journal of Zoology

基  金:江西省重点科技攻关项目(No.20061B0260301)

摘  要:从草鱼(Ctenopharyngodon idella)肝肾cDNA文库中克隆到细胞核酸结合蛋白基因CNBP的完整开放阅读框序列。分析表明草鱼CNBP由163个氨基酸残基组成,含有7个保守CCHC型锌指结构、核定位信号区和RGG框,与其他鱼类的同源性很高。与人及其他脊椎动物的相比,草鱼细胞核酸结合蛋白在第3个锌指中的第5个氨基酸残基由Gly变成His,另外在第1锌指和第2锌指结构间,缺失6~14个氨基酸残基。虽然如此,适应性进化分析显示细胞核酸结合蛋白没有经历正达尔文选择(ω≤1),即这种结构的差异还不足以产生新的功能。这表明CNBP处于中性进化中。The open reading frame of cellular nucleic acid-binding protein ( CNBP ) was cloned from Grass Carp (Ctertopharyngodon idella) cDNA library. The coding region encodes a 163-amino acid polypeptide with the highly conserved general structural organization of seven CCHC zinc finger domains, nuclear located signal and a RGG box which was highly conserved in fish. Compared with human and other vertebrates, the fifth glycine residue at the third zinc finger domain was substituted with histidine and 6 - 14 amino acid residues were absent between the first and the second zinc finger in the Grass Carp CNBP. Nevertheless, the grass carp CNBP was not in the positive Darwin selection (ω ≤1 ) by adaptive evolution analysis. Therefore, new function was not generated by structural difference of CNBP. These indicated that CNBP was in the neutral selection.

关 键 词:细胞核酸结合蛋白(CNBP) 进化 草鱼 

分 类 号:Q953[生物学—动物学]

 

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