The effect of removing the N-terminal extension of the Drosophila myosin regulatory light chain upon flight ability and the contractile dynamics of the indirect flight muscle

The Drosophila myosin regulatory light chain (DMLC2) is homologous to MLC2s of vertebrate organisms, except for the presence of a unique 46-amino acid N-terminal extension. TO study the role of the DMLC2 N-terminal extension in Drosophila flight muscle, we constructed a truncated form of the Dmlc2 g ene lacking amino acids 2-46 (Dmlc2(Delta 2-46)). The mutant gene was expre ssed in vivo, with no wild-type Dmlc2 gene expression, via P-element-mediat ed germline transformation. Expression of the truncated DMLC2 rescues the r ecessive lethality and dominant flightless phenotype of the Dmlc2 null, wit h no discernible effect on indirect flight muscle (IFM) sacromere assembly. Homozygous Dmlc2(Delta 2-46) flies have reduced IFM dynamic stiffness and elastic modulus at the frequency of maximum power output. The viscous modul us, a measure of the fly's ability to perform oscillatory work, was not sig nificantly affected in Dmlc2(Delta 2-46) IFM. In vivo flight performance me asurements of DmlC2(Delta 2-46) flies using a visual dosed-loop flight aren a show deficits in maximum metabolic power (P-CO2*), mechanical power (P-me ch*), and flight force. However, mutant flies were capable of generating fl ight force levels comparable to body weight, thus enabling them to fly, alb eit with diminished performance. The reduction in elastic modulus in Dmlc2( Delta 2-46) skinned fibers is consistent with the N-terminal extension bein g a link between the thick and thin filaments that is parallel to the cross -bridges. Removal of this parallel link causes an unfavorable shift in the resonant properties of the flight system, thus leading to attenuated flight performance.