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J. Biol. Chem., Vol. 260, Issue 27, 14440-14445, Nov, 1985
Y Yamawaki-Kataoka and DM Helfman
A cDNA expression library of approximately 80,000 members was prepared from
rat embryonic fibroblast mRNA using the plasmid expression vectors pUC8 and
pUC9. Using an immunological screening procedure and 32P- labeled cDNA
probes, clones encoding rat embryonic fibroblast tropomyosin 1 (TM-1) were
identified and isolated. DNA sequence analysis was carried out to determine
the amino acid sequence of the protein. Rat embryonic fibroblast TM-1 was
found to contain 284 amino acids and is most homologous to smooth muscle
alpha-tropomyosin compared with skeletal muscle alpha- and
beta-tropomyosins and platelet beta-tropomyosin. Among the various
tropomyosins, two regions where the greatest sequence divergence is evident
are between amino acids 185 and 216 and amino acids 258 and 284. Rat
embryonic fibroblast TM-1 and chicken smooth muscle alpha-tropomyosin are
most closely related from amino acids 185 and 216 compared with skeletal
muscle and platelet tropomyosins. In contrast, rat embryonic fibroblast
TM-1, smooth muscle alpha-tropomyosin, and platelet tropomyosin are most
homologous from amino acids 258 and 284 compared with skeletal muscle
tropomyosins. These differences in sequences at the carboxyl-terminal
region of the various tropomyosins are discussed in relation to differences
in their binding to skeletal muscle troponin and its T1 fragment.
Rat embryonic fibroblast tropomyosin 1. cDNA and complete primary amino acid sequence
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