The complete exon-intron organization of the murine gene encoding sarcomeric myomesin has been determined. The gene is composed of 38 exons and 37 introns, spanning approximately 105 kb of DNA. Intron positions and phases are essentially identical to those identified in M-protein. They are related to the modular structure of myomesin, which is composed almost entirely of immunoglobulin and fibronectin type III domains. Nearly all repeats follow a two exon-one domain structure. The start and end of each domain are defined by introns in phase I, while internal introns are more divergent in position and very rarely use phase I. Genomic Southern blotting and reverse transcription-polymerase chain reaction revealed that differential splicing of a single exon gives rise to two polypeptides, described in the literature as myomesin and skelemin, respectively. A single transcriptional start point was detected in both skeletal and cardiac muscle. Analysis of the presumptive promoter region revealed several potential regulatory elements. CAT expression assays using promoter deletion constructs identified three regions that seem to be important for the muscle-specific transcriptional activation of the myomesin gene. These results provide the basis for a comparative analysis of the regulation of myomesin and M-protein genes in vivo.
Copyright 1999 Academic Press.