Sequence similarity of the amino-terminal domain of Drosophila beta spectrin to alpha actinin and dystrophin.
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.
Byers
T J
TJ
Department of Cellular and Developmental Biology, Harvard University, Cambridge, Massachusetts 02138.
Husain-Chishti
A
A
Dubreuil
R R
RR
Branton
D
D
Goldstein
L S
LS
D000185:Actinin / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002645:Chickens; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics / Q000302:isolation & purification; D004330:Drosophila / Q000235:genetics*; D016189:Dystrophin; D004910:Erythrocyte Membrane / Q000378:metabolism; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D009124:Muscle Proteins / Q000235:genetics*; D009693:Nucleic Acid Hybridization; D011487:Protein Conformation; D012333:RNA, Messenger / Q000235:genetics; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid; D013049:Spectrin / Q000235:genetics*
D016189:Dystrophin; D046911:Macromolecular Substances; D009124:Muscle Proteins; D012333:RNA, Messenger; D000185:Actinin; D013049:Spectrin; D004247:DNA