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.
Sequence similarity of the amino-terminal domain of Drosophila beta spectrin to alpha actinin and dystrophin.
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T J Byers, A Husain-Chishti, R R Dubreuil, D Branton, L S Goldstein; Sequence similarity of the amino-terminal domain of Drosophila beta spectrin to alpha actinin and dystrophin.. J Cell Biol 1 October 1989; 109 (4): 1633–1641. doi: https://doi.org/10.1083/jcb.109.4.1633
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