Structure, evolution, and regulation of a fast skeletal muscle troponin I gene.

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Abstract
The complete structure of a quail fast skeletal muscle troponin I gene was determined by nucleotide sequence comparison of troponin I genomic and cDNA sequences. This 4.5-kilobase troponin I gene has eight exons. The actin-binding domain of troponin I is encoded by a single exon, whereas the troponin C-binding domain is split into at least two exons. The exon organization of the fast troponin I gene suggests that gene conversion directs the nonrandom conservation of the carboxyl-terminal halves of troponin I isoforms and that the amino-terminal extension of the cardiac isoform originated by splice-junction sliding. Comparison of the structure of the troponin I gene with the structures of other contractile protein genes reveals homologous sequences in their 5' flanking regions and similar large introns that separate protein-coding exons from 5' nontranslated exons. These common structural features may function to coordinate the activation of contractile-protein genes during myogenesis.