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 ∼230 residues that shows a high degre...

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Bibliographic Details
Published in:The Journal of cell biology 1989-10, Vol.109 (4), p.1633-1641
Main Authors: Byers, T.J. (Harvard University, Cambridge, MA), Husain-Chishti, A, Dubreuil, R.R, Branton, D, Goldstein, L.S.B
Format: Article
Language:English
Subjects:
Actinin - genetics
Actins
ADN
Amino Acid Sequence
Amino acids
Analytical, structural and metabolic biochemistry
Animals
Antiserum
Base Sequence
beta -spectrin
Biological and medical sciences
cDNA
Chickens
Cloning, Molecular
Complementary DNA
Diptera
DNA
DNA - genetics
DNA - isolation & purification
DROSOPHILA
Drosophila - genetics
Drosophilidae
Dystrophin
Erythrocyte Membrane - metabolism
Erythrocytes
Fundamental and applied biological sciences. Psychology
Glycoproteins
ligand probe
Macromolecular Substances
Molecular Sequence Data
Molecular spectra
Muscle Proteins - genetics
Nucleic Acid Hybridization
NUCLEOTIDE
NUCLEOTIDES
NUCLEOTIDOS
Protein Conformation
PROTEINAS
PROTEINE
PROTEINS
Restriction Mapping
RNA, Messenger - genetics
sequence conservation
Sequence Homology, Nucleic Acid
Spectrin - genetics
Spectroscopic analysis
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Description
Summary: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 ∼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.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.109.4.1633