The Journal of Cell Biology, Vol 109, 1633-1641, Copyright © 1989 by The Rockefeller University Press

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Sequence similarity of the amino-terminal domain of Drosophila beta spectrin to alpha actinin and dystrophin

TJ Byers, A Husain-Chishti, RR Dubreuil, D Branton and LS Goldstein
Department of Cellular and Developmental Biology, Harvard University, Cambridge, Massachusetts 02138.

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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