Comparison of α-tropomyosin sequences from smooth and striated muscle

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Abstract
Tropomyosins are a closely related family of proteins with a dimeric alpha-coiled-coil structure. Skeletal isoforms are composed of two types of subunits, alpha and beta which, in turn, are assorted into two main molecular species alpha alpha and alpha beta. Both isoforms are present in different molar ratios in individual skeletal muscle types. In small mammals, however, only alpha-chain is expressed in cardiac muscle. 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 contraction. 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 tropomyosin. Here we report the nucleotide sequences of cloned complementary DNAs for rat striated and smooth muscle alpha-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 alpha-tropomyosin messenger RNA isoforms each encoding a different protein; these isoforms are tissue-specific, developmentally regulated and most probably encoded by the same gene.