Baron M D, Davison M D, Jones P, Patel B, Critchley D R
J Biol Chem. 1987 Feb 25;262(6):2558-61.
We have isolated and sequenced a 2.1-kilobase cDNA encoding 86% of the sequence of alpha-actinin. The cDNA clone was isolated from a chick embryo fibroblast cDNA library constructed in the expression vector lambda gt11. Identification of this sequence as alpha-actinin was confirmed by immunological methods and by comparing the deduced protein sequence with the sequence of several CNBr fragments obtained from adult chicken smooth muscle (gizzard) alpha-actinin. The deduced protein sequence shows two distinct domains, one of which consists of four repeats of approximately 120 amino acids. This region corresponds to a previously identified 50-kDa tryptic peptide involved in formation of the alpha-actinin dimer. The last 19 residues of C-terminal sequence display an homology with the so-called E-F hand of Ca2+-binding proteins. Hybridization analysis reveals only one size of mRNA (approximately 3.5 kilobases) in fibroblasts, but multiple bands in genomic cDNA.
我们已经分离并测序了一个2.1千碱基的cDNA，它编码α - 辅肌动蛋白序列的86%。该cDNA克隆是从构建于表达载体λ gt11中的鸡胚成纤维细胞cDNA文库中分离得到的。通过免疫学方法以及将推导的蛋白质序列与从成年鸡平滑肌（砂囊）α - 辅肌动蛋白获得的几个溴化氰片段的序列进行比较，证实了该序列为α - 辅肌动蛋白。推导的蛋白质序列显示出两个不同的结构域，其中一个由大约120个氨基酸的四个重复序列组成。该区域对应于先前鉴定的参与α - 辅肌动蛋白二聚体形成的50 kDa胰蛋白酶肽。C末端序列的最后19个残基与所谓的Ca2 +结合蛋白的E - F手显示出同源性。杂交分析表明，成纤维细胞中只有一种大小的mRNA（约3.5千碱基），但基因组cDNA中有多条带。
