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Nucleotide sequence of the rat skeletal muscle actin gene
Year:
1982
Source of publication :
Nature
Authors :
Shani, Moshe
;
.
Volume :
298
Co-Authors:
Zakut, R., Department of Cell Biology, Weizmann Institute of Science, Rehovot 76100, Israel
Shani, M., Chemical Immunology, Weizmann Institute of Science, Rehovot 76100, Israel
Givol, D., Department of Cell Biology, Weizmann Institute of Science, Rehovot 76100, Israel
Neuman, S., Department of Cell Biology, Weizmann Institute of Science, Rehovot 76100, Israel
Yaffe, D., Department of Cell Biology, Weizmann Institute of Science, Rehovot 76100, Israel
Nudel, U., Department of Cell Biology, Weizmann Institute of Science, Rehovot 76100, Israel
Facilitators :
From page:
857
To page:
859
(
Total pages:
3
)
Abstract:
The actins constitute a family of highly conserved proteins found in all eukaryotic cells. Their conservation through a very wide range of taxonomic groups and the existence of tissue-specific isoforms make the actin genes very interesting for the study of the evolution of genes and their controlling elements. On the basis of amino acid sequence data, at least six different mammalian actins have been identified (skeletal muscle, cardiac muscle, two smooth muscle actins and the cytoplasmic β- and γ-actins) 1-5. Rat spleen DNA digested by the EcoRI restriction enzyme contains at least 12 different fragments with actin-like sequences but only one which hybridized, in very stringent conditions, with the skeletal muscle cloned cDNA probe6. Here we describe the sequence of the actin gene in that fragment. The nucleotide sequence codes for two amino acids, Met-Cys, preceding the known N-terminal Asp of the mature protein. There are five small introns in the coding region and a large intron in the 5′-untranslated region. Comparison of the structure of the rat skeletal muscle actin gene with the available data on actin genes from other organisms shows that while the sequenced actin genes from Drosophila and yeast have introns at different locations, introns located at codons specifying amino acids 41, 121, 204 and 267 have been preserved at least from the echinoderm to the vertebrates. A similar analysis has been done by Davidson7. An intron at codon 150 is common to a plant actin gene and the skeletal muscle acting gene. © 1982 Nature Publishing Group.
Note:
Related Files :
animal experiment
Animals
DNA
Echinodermata
Evolution
Genes
gene structure
Heredity
Mammalia
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More details
DOI :
10.1038/298857a0
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
23140
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:57
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Scientific Publication
Nucleotide sequence of the rat skeletal muscle actin gene
298
Zakut, R., Department of Cell Biology, Weizmann Institute of Science, Rehovot 76100, Israel
Shani, M., Chemical Immunology, Weizmann Institute of Science, Rehovot 76100, Israel
Givol, D., Department of Cell Biology, Weizmann Institute of Science, Rehovot 76100, Israel
Neuman, S., Department of Cell Biology, Weizmann Institute of Science, Rehovot 76100, Israel
Yaffe, D., Department of Cell Biology, Weizmann Institute of Science, Rehovot 76100, Israel
Nudel, U., Department of Cell Biology, Weizmann Institute of Science, Rehovot 76100, Israel
Nucleotide sequence of the rat skeletal muscle actin gene
The actins constitute a family of highly conserved proteins found in all eukaryotic cells. Their conservation through a very wide range of taxonomic groups and the existence of tissue-specific isoforms make the actin genes very interesting for the study of the evolution of genes and their controlling elements. On the basis of amino acid sequence data, at least six different mammalian actins have been identified (skeletal muscle, cardiac muscle, two smooth muscle actins and the cytoplasmic β- and γ-actins) 1-5. Rat spleen DNA digested by the EcoRI restriction enzyme contains at least 12 different fragments with actin-like sequences but only one which hybridized, in very stringent conditions, with the skeletal muscle cloned cDNA probe6. Here we describe the sequence of the actin gene in that fragment. The nucleotide sequence codes for two amino acids, Met-Cys, preceding the known N-terminal Asp of the mature protein. There are five small introns in the coding region and a large intron in the 5′-untranslated region. Comparison of the structure of the rat skeletal muscle actin gene with the available data on actin genes from other organisms shows that while the sequenced actin genes from Drosophila and yeast have introns at different locations, introns located at codons specifying amino acids 41, 121, 204 and 267 have been preserved at least from the echinoderm to the vertebrates. A similar analysis has been done by Davidson7. An intron at codon 150 is common to a plant actin gene and the skeletal muscle acting gene. © 1982 Nature Publishing Group.
Scientific Publication
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