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.
Dates
Type | When |
---|---|
Created | 21 years, 3 months ago (May 14, 2004, 8:18 p.m.) |
Deposited | 2 years, 1 month ago (July 21, 2023, 8:48 p.m.) |
Indexed | 4 months, 2 weeks ago (April 10, 2025, 11:07 a.m.) |
Issued | 35 years, 10 months ago (Oct. 1, 1989) |
Published | 35 years, 10 months ago (Oct. 1, 1989) |
Published Online | 35 years, 10 months ago (Oct. 1, 1989) |
Published Print | 35 years, 10 months ago (Oct. 1, 1989) |
@article{Byers_1989, title={Sequence similarity of the amino-terminal domain of Drosophila beta spectrin to alpha actinin and dystrophin.}, volume={109}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.109.4.1633}, DOI={10.1083/jcb.109.4.1633}, number={4}, journal={The Journal of cell biology}, publisher={Rockefeller University Press}, author={Byers, T J and Husain-Chishti, A and Dubreuil, R R and Branton, D and Goldstein, L S}, year={1989}, month=oct, pages={1633–1641} }