THE ACTIN GENES OF DROSOPHILA - PROTEIN CODING REGIONS ARE HIGHLY CONSERVED BUT INTRON POSITIONS ARE NOT
THE ACTIN GENES OF DROSOPHILA - PROTEIN CODING REGIONS ARE HIGHLY CONSERVED BUT INTRON POSITIONS ARE NOT
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DOI:
10.1016/0092-8674(81)90506-7
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发表时间:
1981-01-01
期刊:
影响因子:
64.5
通讯作者:
DAVIDSON, N
中科院分区:
文献类型:
--
作者:
FYRBERG, EA;BOND, BJ;DAVIDSON, N
The entire set of 6 closely related Drosophila actin genes was isolated using recombinant DNA methodology, and the structures of the respective coding regions were characterized by gene mapping techniques and by nucleotide sequencing of selected portions. Structural comparisons of these genes have resulted in several unexpected findings. Most striking is the nonconservation of the positions of intervening sequences within the protein-encoding regions of these genes. One of the Drosophila actin genes, DmA4, is split within a glycine codon at position 13; none of the remaining 5 genes is interrupted in the analogous position. Another gene, DmA6, is split within a glycine codon at position 307; at least 2 of the Drosophila actin genes are not split in the analogous position. None of the Drosophila actin genes is split within codon 4, where the yeast actin gene is interrupted. The 6 Drosophila actin genes encode several different proteins, but the amino acid sequence of each is similar to that of vertebrate cytoplasmic actins. None of the genes encodes a protein comparable in primary sequence to vertebrate skeletal muscle actin. In each of these derived actin amino acid sequences the initiator methionine is directly followed by a cysteine residue, which in turn precedes the string of 3 acidic amino acids characteristic of the amino termini of mature vertebrate cytoplasmic actins. These findings are discussed in the context of actin gene evolution and function.