SEQUENCE SIMILARITY OF THE AMINO-TERMINAL DOMAIN OF DROSOPHILA BETA-SPECTRIN TO ALPHA-ACTININ AND DYSTROPHIN
SEQUENCE SIMILARITY OF THE AMINO-TERMINAL DOMAIN OF DROSOPHILA BETA-SPECTRIN TO ALPHA-ACTININ AND DYSTROPHIN
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DOI：
10.1083/jcb.109.4.1633
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发表时间：
1989-10-01
影响因子：
7.8
通讯作者：
GOLDSTEIN, LSB
中科院分区：
文献类型：
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作者：
BYERS, TJ;HUSAINCHISHTI, A;GOLDSTEIN, LSB
我们使用鸡α血影蛋白作为配体探针，从λ gt11表达文库中分离果蝇β血影蛋白cDNA序列。对氨基末端的800个氨基酸残基的推导氨基酸序列的分析揭示了一个约230个残基的显著保守的结构域，该结构域显示出与α辅肌动蛋白和肌营养不良蛋白的氨基末端结构域高度的序列相似性。这个保守的结构域构成了血影蛋白相关蛋白质的一个新的诊断标准，并允许这些蛋白质之一的已知特性来预测其他蛋白质的功能特性。在血影蛋白、α辅肌动蛋白和肌养蛋白中的氨基末端结构域和其他区域的保守性表明，通过进化以不同的组合连接一组共同的结构域，以产生血影蛋白超家族的独特成员。
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 .apprx.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.