Isolation and characterization of a cDNA encoding a chick alpha-actinin.
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.
D000185:Actinin / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D002642:Chick Embryo; D004247:DNA / Q000032:analysis / Q000302:isolation & purification*; D005347:Fibroblasts / Q000032:analysis; D008970:Molecular Weight; D009693:Nucleic Acid Hybridization
D000185:Actinin; D004247:DNA