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Volume 271, Number 32, Issue of August 9, 1996 pp. 19042-19052
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Tissue-specific Isoforms of Chicken Myomesin Are Generated by Alternative Splicing

(Received for publication, December 20, 1995, and in revised form, April 22, 1996)

From the Institute for Cell Biology, Swiss Federal Institute of Technology, 8093 Zurich, Switzerland

Myomesin is a high molecular weight protein that is present in the M-band of all fiber types of cross-striated skeletal muscle and heart. We have isolated two cDNAs encoding tissue-specific isoforms of chicken myomesin with calculated molecular masses of 174 kDa in skeletal muscle and 182 kDa in heart. Distinct sequences are found at the 3-end of the two cDNAs, giving rise to different C-terminal domains. Partial analysis of the gene structure has shown that in chicken, both isoforms are generated by alternative splicing of a composite exon. Amino acid sequences show that the main body of myomesin consists of five fibronectin type III (class I motifs) and seven immunoglobulin-like domains (class II motifs). An identical structure was found in M-protein and human 190K protein (the human counterpart of chicken myomesin), and a comparable domain arrangement occurs in the M-band-associated protein skelemin. We postulate that myomesin, M-protein, and skelemin belong to the same subfamily of high molecular weight M-band-associated proteins of the immunoglobulin superfamily and that they probably have the same ancestor in evolution.

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