Identifies and characterizes the mp20 gene in Drosophila, which encodes a muscle-specific protein with putative calcium-binding sites expressed in synchronous but not asynchronous muscles.
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Hypothesis-generating for Drosophila muscle subtypes; leaves open relevance of homologs to vertebrate cardiac physiology.
A Drosophila melanogaster gene encoding a muscle specific protein was isolated by differential screening with RNA from primary cultures of myotubes. The gene encodes a 20-kD protein, muscle protein 20 (mp20), that is not detected in the asynchronous oscillatory flight muscles, but is found in most, if not all, other muscles (the synchronous muscles). The sequence of the protein, deduced from the DNA, contains two regions of 12 amino acids with significant similarity to high-affinity calcium-binding sites of other proteins. This protein is easily extracted from the contractile apparatus and thus does not seem to be a tightly bound structural component. The gene (located in polytene region 49F 9-13) is unique in the D. melanogaster genome and yields two transcripts, 1.0 and 0.9 kb long. The levels of the two transcripts are regulated differently during development, yet the coding regions of the two transcripts are identical.
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Ayme-Southgate et al. (1989) studied this question.
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