果蝇β-血影蛋白氨基末端结构域与α-辅肌动蛋白和肌营养不良蛋白的序列相似性。
Sequence similarity of the amino-terminal domain of Drosophila beta spectrin to alpha actinin and dystrophin.
作者信息
Byers T J, Husain-Chishti A, Dubreuil R R, Branton D, Goldstein L S
机构信息
Department of Cellular and Developmental Biology, Harvard University, Cambridge, Massachusetts 02138.
出版信息
J Cell Biol. 1989 Oct;109(4 Pt 1):1633-41. doi: 10.1083/jcb.109.4.1633.
We used chicken alpha spectrin as a ligand probe to isolate Drosophila beta spectrin cDNA sequences from a lambda gt11 expression library. Analysis of 800 residues of deduced amino acid sequence at the amino-terminal end revealed a strikingly conserved domain of integral of 230 residues that shows a high degree of sequence similarity to the amino-terminal domains of alpha actinin and dystrophin. This conserved domain constitutes a new diagnostic criterion for spectrin-related proteins and allows the known properties of one of these proteins to predict functional properties of the others. The conservation of the amino-terminal domain, and other regions in spectrin, alpha actinin, and dystrophin, demonstrates that a common set of domains were linked in different combinations through evolution to generate the distinctive members of the spectrin superfamily.
我们使用鸡α-血影蛋白作为配体探针，从λgt11表达文库中分离果蝇β-血影蛋白cDNA序列。对推导的氨基酸序列氨基末端800个残基的分析揭示了一个由230个残基组成的显著保守的完整结构域，该结构域与α-辅肌动蛋白和肌营养不良蛋白的氨基末端结构域具有高度的序列相似性。这个保守结构域构成了血影蛋白相关蛋白的一个新的诊断标准，并使得这些蛋白中的一种蛋白的已知特性能够预测其他蛋白的功能特性。血影蛋白、α-辅肌动蛋白和肌营养不良蛋白中氨基末端结构域以及其他区域的保守性表明，一组共同的结构域在进化过程中以不同的组合方式连接在一起，从而产生了血影蛋白超家族的不同成员。
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