A muscle-type tropomyosin in human fibroblasts: evidence for expression by an alternative RNA splicing mechanism. | Zendy

Alexander R. MacLeod | Zendy; C. Houlker | Zendy; Fernando C. Reinach | Zendy; Lawrence B. Smillie | Zendy; K Talbot | Zendy; Girish Modi | Zendy; F S Walsh | Zendy

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A muscle-type tropomyosin in human fibroblasts: evidence for expression by an alternative RNA splicing mechanism.

Author(s) -

Alexander R. MacLeod,

C. Houlker,

Fernando C. Reinach,

Lawrence B. Smillie,

K Talbot,

Girish Modi,

F S Walsh

Publication year - 1985

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.82.23.7835

Subject(s) - tropomyosin , biology , alternative splicing , rna splicing , microbiology and biotechnology , complementary dna , skeletal muscle , rna , gene expression , amino acid , cdna library , gene , messenger rna , protein primary structure , actin , biochemistry , peptide sequence , anatomy

We have isolated a cDNA clone from a human fibroblast cDNA library that contains the entire protein-coding region of a 1.1-kilobase mRNA. This mRNA encodes a 284-amino acid tropomyosin, the primary structure of which most closely resembles smooth muscle tropomyosin. Thus, the expression of both 284-amino acid muscle-type and 247-amino acid non-muscle-type tropomyosins appears to be a normal feature of human non-muscle cells. We also present evidence to suggest that this cytoskeletal tropomyosin and a human skeletal muscle beta-tropomyosin are derived from a common structural gene by an alternative RNA splicing mechanism.

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