Isolation and characterization of cDNA clones encoding a low molecular weight nonmuscle tropomyosin isoform

• Published in: The Journal of biological chemistry 1987-08, Vol.262 (22), p.10791-10800
• Main Authors: Yamawaki-Kataoka, Y, Helfman, D M
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Base Sequence; Biological and medical sciences; Blood Platelets - analysis; Cell Transformation, Viral; Contractile proteins; DNA - genetics; DNA - isolation & purification; DNA, Recombinant; fibroblasts; Fibroblasts - analysis; Fundamental and applied biological sciences. Psychology; Holoproteins; Horses; Humans; man; Molecular Weight; Nucleic Acid Hybridization; nucleotide sequence; Proteins; Rats; RNA, Messenger - genetics; RNA, Messenger - metabolism; Tropomyosin - genetics; tropomyosin 4
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(18)61033-6

cDNA clones encoding rat fibroblast tropomyosin 4 (TM-4) were isolated and characterized. DNA sequence analysis was carried out to determine the sequence of the protein. The derived amino acid sequence revealed that rat fibroblast TM-4 was found to contain 248 amino acids. The amino acid sequence of rat fibroblast TM-4 was compared with two other low molecular weight TM isoforms, equine platelet beta-TM and a human fibroblast TM. Rat TM-4 exhibited 98% sequence identity with the equine platelet TM but only 75% identity with the human fibroblast TM isoform. The high degree of conservation between the rat and equine proteins indicates that they belong to the same isotype of TM. Comparison of the amino acid sequences of the three low molecular TM isoforms along the length of the proteins reveals regions that are strongly conserved and regions that have considerably diverged. In the regions from amino acid residues 1 to 148 and 176 to 221, amino acid substitutes are moderate. The most variant regions in the sequence are in the middle part of the proteins from amino acids 149 to 175 and at the carboxyl-terminal region of the proteins from amino acids 222 to 248. The differences in the sequence of the rat and platelet TMs compared to the human TM may define distinct functional domains among the low molecular weight TMs. In addition, expression of tropomyosin was studied in a variety of tissues and transformed cells. We also demonstrate that at least three separate genes encode tropomyosins expressed in rat fibroblasts.