SEQUENCE OF CDNAS ENCODING ACTIN DEPOLYMERIZING FACTOR AND COFILIN OF EMBRYONIC CHICKEN SKELETAL-MUSCLE - 2 FUNCTIONALLY DISTINCT ACTIN-REGULATORY PROTEINS EXHIBIT HIGH STRUCTURAL HOMOLOGY

被引:83
作者
ABE, H
ENDO, T
YAMAMOTO, K
OBINATA, T
机构
[1] CHIBA UNIV,DEPT BIOL,YAYOI CHO,CHIBA 260,JAPAN
[2] UNIV AIR,FAC LIBERAL ARTS,CHIBA 260,JAPAN
关键词
D O I
10.1021/bi00484a010
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Two actin-regulatory proteins of 19 and 20 kDa are involved in the regulation of actin assembly in developing chicken skeletal muscle. They are homologous with actin depolymerizing factor (ADF) and cofilin, a pH-dependent actin-modulating protein, which were originally discovered in chicken and mammalian brain, respectively. In this study, full-length cDNA clones were isolated by screening a λgt11 cDNA library constructed from poly(A+) RNA of embryonic chicken skeletal muscle with the antibodies specific for each protein, and their complete sequences were determined. The chicken cofilin cDNA encoded a protein of 166 amino acids, the sequence of which had over 80% identity with that of porcine brain cofilin. The amino acid sequence of the ADF was 165 amino acids and showed about 70% identity with either chicken or mammalian cofilin, in spite of the fact that ADF and cofilin are functionally distinct. Like chicken and mammalian cofilin, ADF contained a sequence similar to the nuclear transport signal sequence of SV40 large T antigen. ADF and cofilin shared a hexapeptide identical with the amino-terminal sequence of tropomyosin as well as the regions homologous to other actin-regulatory proteins, including depactin, gelsolin, and profîlin. The overall nucleotide sequences and Southern blot analysis of genomic DNA, however, indicated that the two proteins were derived from different genes. © 1990, American Chemical Society. All rights reserved.
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页码:7420 / 7425
页数:6
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