Comparison of α-tropomyosin sequences from smooth and striated muscle View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1985-05

AUTHORS

Nelson Ruiz-Opazo, Judah Weinberger, Bernardo Nadal-Ginard

ABSTRACT

Tropomyosins are a closely related family of proteins with a dimeric α-coiled-coil structure1. Skeletal isoforms are composed of two types of subunits, α and β2–4 which, in turn, are assorted into two main molecular species αα and αβ5–7. Both isoforms are present in different molar ratios in individual skeletal muscle types8,9. In small mammals, however, onlyα-chain is expressed in cardiac muscle8. Tropomyosin, in association with the troponin complex (troponin-I, -T and -C) plays a central role in the Ca2+dependent regulation of vertebrate striated muscle contraction10–12. On the other hand, despite structural similarities with the striated isoforms, the function of this protein in smooth muscle and non-muscle cells remains unknown, because in these cells contraction is thought to be regulated by myosin-linked processes independently of tropomyosin13–15. Here we report the nucleotide sequences of cloned complementary DNAs for rat striated and smooth muscle α-tropomyosin. Comparison of the derived amino-acid sequences reveals the existence of tissue-specific peptides that delimit the putative troponin-I and troponin-T binding domains of tropomyosin. S1-nuclease mapping studies reveal the existence of three distinct α-tropomyosin messenger RNA isoforms each encoding a different protein; these isoforms are tissue-specific, developmentally regulated and most probably encoded by the same gene. More... »

PAGES

67-70

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/315067a0

DOI

http://dx.doi.org/10.1038/315067a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1032332746

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/3838802


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