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  • Title: Sequence similarity of the amino-terminal domain of Drosophila beta spectrin to alpha actinin and dystrophin.
    Author: Byers TJ, Husain-Chishti A, Dubreuil RR, Branton D, Goldstein LS.
    Journal: J Cell Biol; 1989 Oct; 109(4 Pt 1):1633-41. PubMed ID: 2677025.
    Abstract:
    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.
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