Primary structure of the brain alpha-spectrin

Veli-Matti Wasenius, Matti Saraste, Petri Salven, Marja Erämaa, Liisa Holm, Veli-Pekka Lehto

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

We have determined the nucleotide sequence coding for the chicken brain alpha-spectrin. It is derived both from the cDNA and genomic sequences, comprises the entire coding frame, 5' and 3' untranslated sequences, and terminates in the poly(A)-tail.
The deduced amino acid sequence was used to map the domain structure of the protein. The alpha-chain of brain spectrin contains 22 segments of which 20 correspond to the repeat of the human erythrocyte spectrin (Speicher, D. W., and V. T. Marchesi. 1984. Nature (Lond.). 311:177-180.), typically made of 106 residues. These homologous segments probably account for the flexible, rod-like structure of spectrin. Secondary structure prediction suggests predominantly alpha-helical structure for the entire chain. Parts of the primary structure are excluded from the repetitive pattern and they reside in the middle part of the sequence and in its COOH terminus.
Search for homology in other proteins showed the presence of the following distinct structures in these nonrepetitive regions: (a) the COOH-terminal part of the molecule that shows homology with alpha-actinin, (b) two typical EF-hand (i.e., Ca2+-binding) structures in this region, (c) a sequence close to the EF-hand that fulfills the criteria for a calmodulin-binding site, and (d) a domain in the middle of the sequence that is homologous to a NH2-terminal segment of several src-tyrosine kinases and to a domain of phospholipase C. These regions are good candidates to carry some established as well as some yet unestablished functions of spectrin.
Comparative analysis showed that alpha-spectrin is well conserved across the species boundaries from Xenopus to man, and that the human erythrocyte alpha-spectrin is divergent from the other spectrins.
Original languageEnglish
Pages (from-to)79-93
JournalJournal of Cell Biology
Volume108
Issue number1
DOIs
Publication statusPublished - 1989
MoE publication typeA1 Journal article-refereed

Fingerprint

Spectrin
Brain
EF Hand Motifs
Erythrocytes
Actinin
src-Family Kinases
Type C Phospholipases
Calmodulin
Sequence Homology
Xenopus
Amino Acid Sequence
Chickens
Complementary DNA
Binding Sites
Messenger RNA

Cite this

Wasenius, V-M., Saraste, M., Salven, P., Erämaa, M., Holm, L., & Lehto, V-P. (1989). Primary structure of the brain alpha-spectrin. Journal of Cell Biology, 108(1), 79-93. https://doi.org/10.1083/jcb.108.1.79
Wasenius, Veli-Matti ; Saraste, Matti ; Salven, Petri ; Erämaa, Marja ; Holm, Liisa ; Lehto, Veli-Pekka. / Primary structure of the brain alpha-spectrin. In: Journal of Cell Biology. 1989 ; Vol. 108, No. 1. pp. 79-93.
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abstract = "We have determined the nucleotide sequence coding for the chicken brain alpha-spectrin. It is derived both from the cDNA and genomic sequences, comprises the entire coding frame, 5' and 3' untranslated sequences, and terminates in the poly(A)-tail. The deduced amino acid sequence was used to map the domain structure of the protein. The alpha-chain of brain spectrin contains 22 segments of which 20 correspond to the repeat of the human erythrocyte spectrin (Speicher, D. W., and V. T. Marchesi. 1984. Nature (Lond.). 311:177-180.), typically made of 106 residues. These homologous segments probably account for the flexible, rod-like structure of spectrin. Secondary structure prediction suggests predominantly alpha-helical structure for the entire chain. Parts of the primary structure are excluded from the repetitive pattern and they reside in the middle part of the sequence and in its COOH terminus. Search for homology in other proteins showed the presence of the following distinct structures in these nonrepetitive regions: (a) the COOH-terminal part of the molecule that shows homology with alpha-actinin, (b) two typical EF-hand (i.e., Ca2+-binding) structures in this region, (c) a sequence close to the EF-hand that fulfills the criteria for a calmodulin-binding site, and (d) a domain in the middle of the sequence that is homologous to a NH2-terminal segment of several src-tyrosine kinases and to a domain of phospholipase C. These regions are good candidates to carry some established as well as some yet unestablished functions of spectrin. Comparative analysis showed that alpha-spectrin is well conserved across the species boundaries from Xenopus to man, and that the human erythrocyte alpha-spectrin is divergent from the other spectrins.",
author = "Veli-Matti Wasenius and Matti Saraste and Petri Salven and Marja Er{\"a}maa and Liisa Holm and Veli-Pekka Lehto",
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Wasenius, V-M, Saraste, M, Salven, P, Erämaa, M, Holm, L & Lehto, V-P 1989, 'Primary structure of the brain alpha-spectrin', Journal of Cell Biology, vol. 108, no. 1, pp. 79-93. https://doi.org/10.1083/jcb.108.1.79

Primary structure of the brain alpha-spectrin. / Wasenius, Veli-Matti; Saraste, Matti; Salven, Petri; Erämaa, Marja; Holm, Liisa; Lehto, Veli-Pekka.

In: Journal of Cell Biology, Vol. 108, No. 1, 1989, p. 79-93.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Primary structure of the brain alpha-spectrin

AU - Wasenius, Veli-Matti

AU - Saraste, Matti

AU - Salven, Petri

AU - Erämaa, Marja

AU - Holm, Liisa

AU - Lehto, Veli-Pekka

PY - 1989

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N2 - We have determined the nucleotide sequence coding for the chicken brain alpha-spectrin. It is derived both from the cDNA and genomic sequences, comprises the entire coding frame, 5' and 3' untranslated sequences, and terminates in the poly(A)-tail. The deduced amino acid sequence was used to map the domain structure of the protein. The alpha-chain of brain spectrin contains 22 segments of which 20 correspond to the repeat of the human erythrocyte spectrin (Speicher, D. W., and V. T. Marchesi. 1984. Nature (Lond.). 311:177-180.), typically made of 106 residues. These homologous segments probably account for the flexible, rod-like structure of spectrin. Secondary structure prediction suggests predominantly alpha-helical structure for the entire chain. Parts of the primary structure are excluded from the repetitive pattern and they reside in the middle part of the sequence and in its COOH terminus. Search for homology in other proteins showed the presence of the following distinct structures in these nonrepetitive regions: (a) the COOH-terminal part of the molecule that shows homology with alpha-actinin, (b) two typical EF-hand (i.e., Ca2+-binding) structures in this region, (c) a sequence close to the EF-hand that fulfills the criteria for a calmodulin-binding site, and (d) a domain in the middle of the sequence that is homologous to a NH2-terminal segment of several src-tyrosine kinases and to a domain of phospholipase C. These regions are good candidates to carry some established as well as some yet unestablished functions of spectrin. Comparative analysis showed that alpha-spectrin is well conserved across the species boundaries from Xenopus to man, and that the human erythrocyte alpha-spectrin is divergent from the other spectrins.

AB - We have determined the nucleotide sequence coding for the chicken brain alpha-spectrin. It is derived both from the cDNA and genomic sequences, comprises the entire coding frame, 5' and 3' untranslated sequences, and terminates in the poly(A)-tail. The deduced amino acid sequence was used to map the domain structure of the protein. The alpha-chain of brain spectrin contains 22 segments of which 20 correspond to the repeat of the human erythrocyte spectrin (Speicher, D. W., and V. T. Marchesi. 1984. Nature (Lond.). 311:177-180.), typically made of 106 residues. These homologous segments probably account for the flexible, rod-like structure of spectrin. Secondary structure prediction suggests predominantly alpha-helical structure for the entire chain. Parts of the primary structure are excluded from the repetitive pattern and they reside in the middle part of the sequence and in its COOH terminus. Search for homology in other proteins showed the presence of the following distinct structures in these nonrepetitive regions: (a) the COOH-terminal part of the molecule that shows homology with alpha-actinin, (b) two typical EF-hand (i.e., Ca2+-binding) structures in this region, (c) a sequence close to the EF-hand that fulfills the criteria for a calmodulin-binding site, and (d) a domain in the middle of the sequence that is homologous to a NH2-terminal segment of several src-tyrosine kinases and to a domain of phospholipase C. These regions are good candidates to carry some established as well as some yet unestablished functions of spectrin. Comparative analysis showed that alpha-spectrin is well conserved across the species boundaries from Xenopus to man, and that the human erythrocyte alpha-spectrin is divergent from the other spectrins.

U2 - 10.1083/jcb.108.1.79

DO - 10.1083/jcb.108.1.79

M3 - Article

VL - 108

SP - 79

EP - 93

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 1

ER -

Wasenius V-M, Saraste M, Salven P, Erämaa M, Holm L, Lehto V-P. Primary structure of the brain alpha-spectrin. Journal of Cell Biology. 1989;108(1):79-93. https://doi.org/10.1083/jcb.108.1.79