Abstract
We use Drosophila melanogaster to investigate the mechanisms by which myosin heavy chain isoforms contribute to muscle-specific cyto-architectures and contractile properties. We expressed various myosin isoforms in transgenic indirect flight muscles. Along with our collaborators, we examined 1) ATPase, in vitro actin sliding, step size and structure of the isolated myosin, 2) ultrastructure and mechanical properties of muscle fibers, and 3) locomotory abilities of the transgenic organisms. We found that isoform-specific differences in myosin cause relatively small structural variations in muscle assembly, but are critical to myofibril stability and function.
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