Byers, T.J., Husain-Chishti, A., Dubreuil, R.R., Branton, D., Goldstein, L.S.B. (1989). Sequence similarity of the amino-terminal domain of Drosophila spectrin to actinin and dystrophin.  J. Cell Biol. 109(4(I)): 1633--1641.

FBrf0050174

Research paper

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.

PMC2115807 (PMC) (EuropePMC)